data_7EDQ
# 
_entry.id   7EDQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7EDQ         pdb_00007edq 10.2210/pdb7edq/pdb 
WWPDB D_1300021235 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7EDQ 
_pdbx_database_status.recvd_initial_deposition_date   2021-03-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fan, C.P.' 1 ? 
'Guo, D.Y.' 2 ? 
'Yang, L.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            55 
_citation.language                  ? 
_citation.page_first                128445 
_citation.page_last                 128445 
_citation.title                     
'Repurposing old drugs as novel inhibitors of human MIF from structural and functional analysis.' 
_citation.year                      2022 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2021.128445 
_citation.pdbx_database_id_PubMed   34758374 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, L.' 1 ? 
primary 'Yang, C.' 2 ? 
primary 'Wang, L.' 3 ? 
primary 'Yang, Z.' 4 ? 
primary 'Guo, D.'  5 ? 
primary 'Fan, C.'  6 ? 
# 
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 'Macrophage migration inhibitory factor' 12355.056 3   5.3.2.1,5.3.3.12 ? ? ? 
2 non-polymer syn '6,7-bis(oxidanyl)chromen-2-one'         178.142   1   ?                ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                           35.453    8   ?                ? ? ? 
4 water       nat water                                    18.015    446 ?                ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'MIF,Glycosylation-inhibiting factor,GIF,L-dopachrome isomerase,L-dopachrome tautomerase,Phenylpyruvate tautomerase' 
# 
_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       
;PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLC
GLLAERLRISPDRVYINYYDMNAANVGWNNSTFA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLC
GLLAERLRISPDRVYINYYDMNAANVGWNNSTFA
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '6,7-bis(oxidanyl)chromen-2-one' HFC 
3 'CHLORIDE ION'                   CL  
4 water                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   MET n 
1 3   PHE n 
1 4   ILE n 
1 5   VAL n 
1 6   ASN n 
1 7   THR n 
1 8   ASN n 
1 9   VAL n 
1 10  PRO n 
1 11  ARG n 
1 12  ALA n 
1 13  SER n 
1 14  VAL n 
1 15  PRO n 
1 16  ASP n 
1 17  GLY n 
1 18  PHE n 
1 19  LEU n 
1 20  SER n 
1 21  GLU n 
1 22  LEU n 
1 23  THR n 
1 24  GLN n 
1 25  GLN n 
1 26  LEU n 
1 27  ALA n 
1 28  GLN n 
1 29  ALA n 
1 30  THR n 
1 31  GLY n 
1 32  LYS n 
1 33  PRO n 
1 34  PRO n 
1 35  GLN n 
1 36  TYR n 
1 37  ILE n 
1 38  ALA n 
1 39  VAL n 
1 40  HIS n 
1 41  VAL n 
1 42  VAL n 
1 43  PRO n 
1 44  ASP n 
1 45  GLN n 
1 46  LEU n 
1 47  MET n 
1 48  ALA n 
1 49  PHE n 
1 50  GLY n 
1 51  GLY n 
1 52  SER n 
1 53  SER n 
1 54  GLU n 
1 55  PRO n 
1 56  CYS n 
1 57  ALA n 
1 58  LEU n 
1 59  CYS n 
1 60  SER n 
1 61  LEU n 
1 62  HIS n 
1 63  SER n 
1 64  ILE n 
1 65  GLY n 
1 66  LYS n 
1 67  ILE n 
1 68  GLY n 
1 69  GLY n 
1 70  ALA n 
1 71  GLN n 
1 72  ASN n 
1 73  ARG n 
1 74  SER n 
1 75  TYR n 
1 76  SER n 
1 77  LYS n 
1 78  LEU n 
1 79  LEU n 
1 80  CYS n 
1 81  GLY n 
1 82  LEU n 
1 83  LEU n 
1 84  ALA n 
1 85  GLU n 
1 86  ARG n 
1 87  LEU n 
1 88  ARG n 
1 89  ILE n 
1 90  SER n 
1 91  PRO n 
1 92  ASP n 
1 93  ARG n 
1 94  VAL n 
1 95  TYR n 
1 96  ILE n 
1 97  ASN n 
1 98  TYR n 
1 99  TYR n 
1 100 ASP n 
1 101 MET n 
1 102 ASN n 
1 103 ALA n 
1 104 ALA n 
1 105 ASN n 
1 106 VAL n 
1 107 GLY n 
1 108 TRP n 
1 109 ASN n 
1 110 ASN n 
1 111 SER n 
1 112 THR n 
1 113 PHE n 
1 114 ALA 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                   114 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MIF, GLIF, MMIF' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
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 
CL  non-polymer         . 'CHLORIDE ION'                   ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                          ? 'C2 H5 N O2'     75.067  
HFC non-polymer         . '6,7-bis(oxidanyl)chromen-2-one' ? 'C9 H6 O4'       178.142 
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 
# 
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   PRO 1   1   1   PRO PRO A . n 
A 1 2   MET 2   2   2   MET MET A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  PHE 18  18  18  PHE PHE A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  SER 20  20  20  SER SER A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  MET 47  47  47  MET MET A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  CYS 56  56  56  CYS CYS A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  CYS 59  59  59  CYS CYS A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  CYS 80  80  80  CYS CYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 MET 101 101 101 MET MET A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
B 1 1   PRO 1   1   1   PRO PRO B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ASN 6   6   6   ASN ASN B . n 
B 1 7   THR 7   7   7   THR THR B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  PRO 10  10  10  PRO PRO B . n 
B 1 11  ARG 11  11  11  ARG ARG B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  PHE 18  18  18  PHE PHE B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  SER 20  20  20  SER SER B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  THR 23  23  23  THR THR B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  LYS 32  32  32  LYS LYS B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  TYR 36  36  36  TYR TYR B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  GLN 45  45  45  GLN GLN B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  MET 47  47  47  MET MET B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  PRO 55  55  55  PRO PRO B . n 
B 1 56  CYS 56  56  56  CYS CYS B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  CYS 59  59  59  CYS CYS B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  HIS 62  62  62  HIS HIS B . n 
B 1 63  SER 63  63  63  SER SER B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  LYS 66  66  66  LYS LYS B . n 
B 1 67  ILE 67  67  67  ILE ILE B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLN 71  71  71  GLN GLN B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  TYR 75  75  75  TYR TYR B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  CYS 80  80  80  CYS CYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  SER 90  90  90  SER SER B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  TYR 95  95  95  TYR TYR B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  ASN 97  97  97  ASN ASN B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  TYR 99  99  99  TYR TYR B . n 
B 1 100 ASP 100 100 100 ASP ASP B . n 
B 1 101 MET 101 101 101 MET MET B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 TRP 108 108 108 TRP TRP B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 PHE 113 113 113 PHE PHE B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
C 1 1   PRO 1   1   1   PRO PRO C . n 
C 1 2   MET 2   2   2   MET MET C . n 
C 1 3   PHE 3   3   3   PHE PHE C . n 
C 1 4   ILE 4   4   4   ILE ILE C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   ASN 6   6   6   ASN ASN C . n 
C 1 7   THR 7   7   7   THR THR C . n 
C 1 8   ASN 8   8   8   ASN ASN C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  PRO 10  10  10  PRO PRO C . n 
C 1 11  ARG 11  11  11  ARG ARG C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  SER 13  13  13  SER SER C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  PRO 15  15  15  PRO PRO C . n 
C 1 16  ASP 16  16  16  ASP ASP C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  PHE 18  18  18  PHE PHE C . n 
C 1 19  LEU 19  19  19  LEU LEU C . n 
C 1 20  SER 20  20  20  SER SER C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  THR 23  23  23  THR THR C . n 
C 1 24  GLN 24  24  24  GLN GLN C . n 
C 1 25  GLN 25  25  25  GLN GLN C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  ALA 27  27  27  ALA ALA C . n 
C 1 28  GLN 28  28  28  GLN GLN C . n 
C 1 29  ALA 29  29  29  ALA ALA C . n 
C 1 30  THR 30  30  30  THR THR C . n 
C 1 31  GLY 31  31  31  GLY GLY C . n 
C 1 32  LYS 32  32  32  LYS LYS C . n 
C 1 33  PRO 33  33  33  PRO PRO C . n 
C 1 34  PRO 34  34  34  PRO PRO C . n 
C 1 35  GLN 35  35  35  GLN GLN C . n 
C 1 36  TYR 36  36  36  TYR TYR C . n 
C 1 37  ILE 37  37  37  ILE ILE C . n 
C 1 38  ALA 38  38  38  ALA ALA C . n 
C 1 39  VAL 39  39  39  VAL VAL C . n 
C 1 40  HIS 40  40  40  HIS HIS C . n 
C 1 41  VAL 41  41  41  VAL VAL C . n 
C 1 42  VAL 42  42  42  VAL VAL C . n 
C 1 43  PRO 43  43  43  PRO PRO C . n 
C 1 44  ASP 44  44  44  ASP ASP C . n 
C 1 45  GLN 45  45  45  GLN GLN C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  MET 47  47  47  MET MET C . n 
C 1 48  ALA 48  48  48  ALA ALA C . n 
C 1 49  PHE 49  49  49  PHE PHE C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  SER 53  53  53  SER SER C . n 
C 1 54  GLU 54  54  54  GLU GLU C . n 
C 1 55  PRO 55  55  55  PRO PRO C . n 
C 1 56  CYS 56  56  56  CYS CYS C . n 
C 1 57  ALA 57  57  57  ALA ALA C . n 
C 1 58  LEU 58  58  58  LEU LEU C . n 
C 1 59  CYS 59  59  59  CYS CYS C . n 
C 1 60  SER 60  60  60  SER SER C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  HIS 62  62  62  HIS HIS C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  ILE 64  64  64  ILE ILE C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  LYS 66  66  66  LYS LYS C . n 
C 1 67  ILE 67  67  67  ILE ILE C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  GLY 69  69  69  GLY GLY C . n 
C 1 70  ALA 70  70  70  ALA ALA C . n 
C 1 71  GLN 71  71  71  GLN GLN C . n 
C 1 72  ASN 72  72  72  ASN ASN C . n 
C 1 73  ARG 73  73  73  ARG ARG C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  TYR 75  75  75  TYR TYR C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  LYS 77  77  77  LYS LYS C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  CYS 80  80  80  CYS CYS C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  LEU 82  82  82  LEU LEU C . n 
C 1 83  LEU 83  83  83  LEU LEU C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  GLU 85  85  85  GLU GLU C . n 
C 1 86  ARG 86  86  86  ARG ARG C . n 
C 1 87  LEU 87  87  87  LEU LEU C . n 
C 1 88  ARG 88  88  88  ARG ARG C . n 
C 1 89  ILE 89  89  89  ILE ILE C . n 
C 1 90  SER 90  90  90  SER SER C . n 
C 1 91  PRO 91  91  91  PRO PRO C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  ARG 93  93  93  ARG ARG C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  TYR 95  95  95  TYR TYR C . n 
C 1 96  ILE 96  96  96  ILE ILE C . n 
C 1 97  ASN 97  97  97  ASN ASN C . n 
C 1 98  TYR 98  98  98  TYR TYR C . n 
C 1 99  TYR 99  99  99  TYR TYR C . n 
C 1 100 ASP 100 100 100 ASP ASP C . n 
C 1 101 MET 101 101 101 MET MET C . n 
C 1 102 ASN 102 102 102 ASN ASN C . n 
C 1 103 ALA 103 103 103 ALA ALA C . n 
C 1 104 ALA 104 104 104 ALA ALA C . n 
C 1 105 ASN 105 105 105 ASN ASN C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 GLY 107 107 107 GLY GLY C . n 
C 1 108 TRP 108 108 108 TRP TRP C . n 
C 1 109 ASN 109 109 109 ASN ASN C . n 
C 1 110 ASN 110 110 110 ASN ASN C . n 
C 1 111 SER 111 111 111 SER SER C . n 
C 1 112 THR 112 112 112 THR THR C . n 
C 1 113 PHE 113 113 113 PHE PHE C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HFC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HFC 
_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 
D 2 HFC 1   201 1   HFC ELN A . 
E 3 CL  1   202 1   CL  CL  A . 
F 3 CL  1   203 4   CL  CL  A . 
G 3 CL  1   204 5   CL  CL  A . 
H 3 CL  1   201 2   CL  CL  B . 
I 3 CL  1   202 8   CL  CL  B . 
J 3 CL  1   201 3   CL  CL  C . 
K 3 CL  1   202 6   CL  CL  C . 
L 3 CL  1   203 7   CL  CL  C . 
M 4 HOH 1   301 124 HOH HOH A . 
M 4 HOH 2   302 422 HOH HOH A . 
M 4 HOH 3   303 366 HOH HOH A . 
M 4 HOH 4   304 203 HOH HOH A . 
M 4 HOH 5   305 251 HOH HOH A . 
M 4 HOH 6   306 350 HOH HOH A . 
M 4 HOH 7   307 270 HOH HOH A . 
M 4 HOH 8   308 222 HOH HOH A . 
M 4 HOH 9   309 29  HOH HOH A . 
M 4 HOH 10  310 17  HOH HOH A . 
M 4 HOH 11  311 198 HOH HOH A . 
M 4 HOH 12  312 243 HOH HOH A . 
M 4 HOH 13  313 333 HOH HOH A . 
M 4 HOH 14  314 317 HOH HOH A . 
M 4 HOH 15  315 278 HOH HOH A . 
M 4 HOH 16  316 297 HOH HOH A . 
M 4 HOH 17  317 305 HOH HOH A . 
M 4 HOH 18  318 25  HOH HOH A . 
M 4 HOH 19  319 242 HOH HOH A . 
M 4 HOH 20  320 38  HOH HOH A . 
M 4 HOH 21  321 172 HOH HOH A . 
M 4 HOH 22  322 56  HOH HOH A . 
M 4 HOH 23  323 347 HOH HOH A . 
M 4 HOH 24  324 240 HOH HOH A . 
M 4 HOH 25  325 8   HOH HOH A . 
M 4 HOH 26  326 411 HOH HOH A . 
M 4 HOH 27  327 98  HOH HOH A . 
M 4 HOH 28  328 210 HOH HOH A . 
M 4 HOH 29  329 180 HOH HOH A . 
M 4 HOH 30  330 153 HOH HOH A . 
M 4 HOH 31  331 41  HOH HOH A . 
M 4 HOH 32  332 281 HOH HOH A . 
M 4 HOH 33  333 16  HOH HOH A . 
M 4 HOH 34  334 33  HOH HOH A . 
M 4 HOH 35  335 284 HOH HOH A . 
M 4 HOH 36  336 92  HOH HOH A . 
M 4 HOH 37  337 31  HOH HOH A . 
M 4 HOH 38  338 48  HOH HOH A . 
M 4 HOH 39  339 301 HOH HOH A . 
M 4 HOH 40  340 52  HOH HOH A . 
M 4 HOH 41  341 4   HOH HOH A . 
M 4 HOH 42  342 67  HOH HOH A . 
M 4 HOH 43  343 43  HOH HOH A . 
M 4 HOH 44  344 50  HOH HOH A . 
M 4 HOH 45  345 280 HOH HOH A . 
M 4 HOH 46  346 108 HOH HOH A . 
M 4 HOH 47  347 261 HOH HOH A . 
M 4 HOH 48  348 316 HOH HOH A . 
M 4 HOH 49  349 168 HOH HOH A . 
M 4 HOH 50  350 70  HOH HOH A . 
M 4 HOH 51  351 89  HOH HOH A . 
M 4 HOH 52  352 79  HOH HOH A . 
M 4 HOH 53  353 263 HOH HOH A . 
M 4 HOH 54  354 99  HOH HOH A . 
M 4 HOH 55  355 104 HOH HOH A . 
M 4 HOH 56  356 283 HOH HOH A . 
M 4 HOH 57  357 319 HOH HOH A . 
M 4 HOH 58  358 231 HOH HOH A . 
M 4 HOH 59  359 212 HOH HOH A . 
M 4 HOH 60  360 134 HOH HOH A . 
M 4 HOH 61  361 218 HOH HOH A . 
M 4 HOH 62  362 150 HOH HOH A . 
M 4 HOH 63  363 328 HOH HOH A . 
M 4 HOH 64  364 179 HOH HOH A . 
M 4 HOH 65  365 410 HOH HOH A . 
M 4 HOH 66  366 388 HOH HOH A . 
M 4 HOH 67  367 300 HOH HOH A . 
M 4 HOH 68  368 315 HOH HOH A . 
M 4 HOH 69  369 209 HOH HOH A . 
M 4 HOH 70  370 102 HOH HOH A . 
M 4 HOH 71  371 109 HOH HOH A . 
M 4 HOH 72  372 382 HOH HOH A . 
M 4 HOH 73  373 73  HOH HOH A . 
M 4 HOH 74  374 165 HOH HOH A . 
M 4 HOH 75  375 192 HOH HOH A . 
M 4 HOH 76  376 55  HOH HOH A . 
M 4 HOH 77  377 340 HOH HOH A . 
M 4 HOH 78  378 156 HOH HOH A . 
M 4 HOH 79  379 71  HOH HOH A . 
M 4 HOH 80  380 103 HOH HOH A . 
M 4 HOH 81  381 96  HOH HOH A . 
M 4 HOH 82  382 309 HOH HOH A . 
M 4 HOH 83  383 416 HOH HOH A . 
M 4 HOH 84  384 271 HOH HOH A . 
M 4 HOH 85  385 120 HOH HOH A . 
M 4 HOH 86  386 2   HOH HOH A . 
M 4 HOH 87  387 63  HOH HOH A . 
M 4 HOH 88  388 169 HOH HOH A . 
M 4 HOH 89  389 15  HOH HOH A . 
M 4 HOH 90  390 237 HOH HOH A . 
M 4 HOH 91  391 123 HOH HOH A . 
M 4 HOH 92  392 155 HOH HOH A . 
M 4 HOH 93  393 183 HOH HOH A . 
M 4 HOH 94  394 392 HOH HOH A . 
M 4 HOH 95  395 129 HOH HOH A . 
M 4 HOH 96  396 232 HOH HOH A . 
M 4 HOH 97  397 35  HOH HOH A . 
M 4 HOH 98  398 36  HOH HOH A . 
M 4 HOH 99  399 443 HOH HOH A . 
M 4 HOH 100 400 51  HOH HOH A . 
M 4 HOH 101 401 138 HOH HOH A . 
M 4 HOH 102 402 28  HOH HOH A . 
M 4 HOH 103 403 352 HOH HOH A . 
M 4 HOH 104 404 142 HOH HOH A . 
M 4 HOH 105 405 266 HOH HOH A . 
M 4 HOH 106 406 368 HOH HOH A . 
M 4 HOH 107 407 396 HOH HOH A . 
M 4 HOH 108 408 132 HOH HOH A . 
M 4 HOH 109 409 404 HOH HOH A . 
M 4 HOH 110 410 385 HOH HOH A . 
M 4 HOH 111 411 97  HOH HOH A . 
M 4 HOH 112 412 34  HOH HOH A . 
M 4 HOH 113 413 107 HOH HOH A . 
M 4 HOH 114 414 365 HOH HOH A . 
M 4 HOH 115 415 197 HOH HOH A . 
M 4 HOH 116 416 336 HOH HOH A . 
M 4 HOH 117 417 286 HOH HOH A . 
M 4 HOH 118 418 187 HOH HOH A . 
M 4 HOH 119 419 376 HOH HOH A . 
M 4 HOH 120 420 23  HOH HOH A . 
M 4 HOH 121 421 394 HOH HOH A . 
M 4 HOH 122 422 267 HOH HOH A . 
M 4 HOH 123 423 401 HOH HOH A . 
M 4 HOH 124 424 220 HOH HOH A . 
M 4 HOH 125 425 195 HOH HOH A . 
M 4 HOH 126 426 178 HOH HOH A . 
M 4 HOH 127 427 302 HOH HOH A . 
M 4 HOH 128 428 269 HOH HOH A . 
M 4 HOH 129 429 423 HOH HOH A . 
M 4 HOH 130 430 101 HOH HOH A . 
M 4 HOH 131 431 258 HOH HOH A . 
M 4 HOH 132 432 351 HOH HOH A . 
M 4 HOH 133 433 268 HOH HOH A . 
M 4 HOH 134 434 330 HOH HOH A . 
M 4 HOH 135 435 69  HOH HOH A . 
M 4 HOH 136 436 446 HOH HOH A . 
M 4 HOH 137 437 364 HOH HOH A . 
M 4 HOH 138 438 427 HOH HOH A . 
M 4 HOH 139 439 369 HOH HOH A . 
M 4 HOH 140 440 246 HOH HOH A . 
M 4 HOH 141 441 395 HOH HOH A . 
M 4 HOH 142 442 437 HOH HOH A . 
M 4 HOH 143 443 375 HOH HOH A . 
M 4 HOH 144 444 314 HOH HOH A . 
M 4 HOH 145 445 419 HOH HOH A . 
M 4 HOH 146 446 344 HOH HOH A . 
M 4 HOH 147 447 298 HOH HOH A . 
M 4 HOH 148 448 221 HOH HOH A . 
M 4 HOH 149 449 140 HOH HOH A . 
M 4 HOH 150 450 386 HOH HOH A . 
M 4 HOH 151 451 349 HOH HOH A . 
M 4 HOH 152 452 40  HOH HOH A . 
M 4 HOH 153 453 405 HOH HOH A . 
M 4 HOH 154 454 191 HOH HOH A . 
N 4 HOH 1   301 147 HOH HOH B . 
N 4 HOH 2   302 391 HOH HOH B . 
N 4 HOH 3   303 358 HOH HOH B . 
N 4 HOH 4   304 335 HOH HOH B . 
N 4 HOH 5   305 447 HOH HOH B . 
N 4 HOH 6   306 241 HOH HOH B . 
N 4 HOH 7   307 277 HOH HOH B . 
N 4 HOH 8   308 182 HOH HOH B . 
N 4 HOH 9   309 273 HOH HOH B . 
N 4 HOH 10  310 95  HOH HOH B . 
N 4 HOH 11  311 400 HOH HOH B . 
N 4 HOH 12  312 208 HOH HOH B . 
N 4 HOH 13  313 86  HOH HOH B . 
N 4 HOH 14  314 141 HOH HOH B . 
N 4 HOH 15  315 21  HOH HOH B . 
N 4 HOH 16  316 194 HOH HOH B . 
N 4 HOH 17  317 159 HOH HOH B . 
N 4 HOH 18  318 262 HOH HOH B . 
N 4 HOH 19  319 216 HOH HOH B . 
N 4 HOH 20  320 81  HOH HOH B . 
N 4 HOH 21  321 205 HOH HOH B . 
N 4 HOH 22  322 88  HOH HOH B . 
N 4 HOH 23  323 27  HOH HOH B . 
N 4 HOH 24  324 304 HOH HOH B . 
N 4 HOH 25  325 415 HOH HOH B . 
N 4 HOH 26  326 84  HOH HOH B . 
N 4 HOH 27  327 117 HOH HOH B . 
N 4 HOH 28  328 135 HOH HOH B . 
N 4 HOH 29  329 295 HOH HOH B . 
N 4 HOH 30  330 6   HOH HOH B . 
N 4 HOH 31  331 118 HOH HOH B . 
N 4 HOH 32  332 238 HOH HOH B . 
N 4 HOH 33  333 160 HOH HOH B . 
N 4 HOH 34  334 154 HOH HOH B . 
N 4 HOH 35  335 12  HOH HOH B . 
N 4 HOH 36  336 289 HOH HOH B . 
N 4 HOH 37  337 11  HOH HOH B . 
N 4 HOH 38  338 327 HOH HOH B . 
N 4 HOH 39  339 408 HOH HOH B . 
N 4 HOH 40  340 72  HOH HOH B . 
N 4 HOH 41  341 57  HOH HOH B . 
N 4 HOH 42  342 74  HOH HOH B . 
N 4 HOH 43  343 235 HOH HOH B . 
N 4 HOH 44  344 248 HOH HOH B . 
N 4 HOH 45  345 229 HOH HOH B . 
N 4 HOH 46  346 236 HOH HOH B . 
N 4 HOH 47  347 247 HOH HOH B . 
N 4 HOH 48  348 255 HOH HOH B . 
N 4 HOH 49  349 176 HOH HOH B . 
N 4 HOH 50  350 121 HOH HOH B . 
N 4 HOH 51  351 136 HOH HOH B . 
N 4 HOH 52  352 87  HOH HOH B . 
N 4 HOH 53  353 438 HOH HOH B . 
N 4 HOH 54  354 276 HOH HOH B . 
N 4 HOH 55  355 190 HOH HOH B . 
N 4 HOH 56  356 348 HOH HOH B . 
N 4 HOH 57  357 37  HOH HOH B . 
N 4 HOH 58  358 384 HOH HOH B . 
N 4 HOH 59  359 383 HOH HOH B . 
N 4 HOH 60  360 420 HOH HOH B . 
N 4 HOH 61  361 45  HOH HOH B . 
N 4 HOH 62  362 265 HOH HOH B . 
N 4 HOH 63  363 75  HOH HOH B . 
N 4 HOH 64  364 414 HOH HOH B . 
N 4 HOH 65  365 130 HOH HOH B . 
N 4 HOH 66  366 225 HOH HOH B . 
N 4 HOH 67  367 193 HOH HOH B . 
N 4 HOH 68  368 398 HOH HOH B . 
N 4 HOH 69  369 174 HOH HOH B . 
N 4 HOH 70  370 219 HOH HOH B . 
N 4 HOH 71  371 46  HOH HOH B . 
N 4 HOH 72  372 114 HOH HOH B . 
N 4 HOH 73  373 3   HOH HOH B . 
N 4 HOH 74  374 244 HOH HOH B . 
N 4 HOH 75  375 233 HOH HOH B . 
N 4 HOH 76  376 380 HOH HOH B . 
N 4 HOH 77  377 441 HOH HOH B . 
N 4 HOH 78  378 421 HOH HOH B . 
N 4 HOH 79  379 296 HOH HOH B . 
N 4 HOH 80  380 326 HOH HOH B . 
N 4 HOH 81  381 47  HOH HOH B . 
N 4 HOH 82  382 10  HOH HOH B . 
N 4 HOH 83  383 200 HOH HOH B . 
N 4 HOH 84  384 360 HOH HOH B . 
N 4 HOH 85  385 448 HOH HOH B . 
N 4 HOH 86  386 373 HOH HOH B . 
N 4 HOH 87  387 44  HOH HOH B . 
N 4 HOH 88  388 105 HOH HOH B . 
N 4 HOH 89  389 122 HOH HOH B . 
N 4 HOH 90  390 381 HOH HOH B . 
N 4 HOH 91  391 22  HOH HOH B . 
N 4 HOH 92  392 353 HOH HOH B . 
N 4 HOH 93  393 226 HOH HOH B . 
N 4 HOH 94  394 367 HOH HOH B . 
N 4 HOH 95  395 214 HOH HOH B . 
N 4 HOH 96  396 80  HOH HOH B . 
N 4 HOH 97  397 399 HOH HOH B . 
N 4 HOH 98  398 426 HOH HOH B . 
N 4 HOH 99  399 32  HOH HOH B . 
N 4 HOH 100 400 164 HOH HOH B . 
N 4 HOH 101 401 387 HOH HOH B . 
N 4 HOH 102 402 339 HOH HOH B . 
N 4 HOH 103 403 355 HOH HOH B . 
N 4 HOH 104 404 173 HOH HOH B . 
N 4 HOH 105 405 224 HOH HOH B . 
N 4 HOH 106 406 337 HOH HOH B . 
N 4 HOH 107 407 144 HOH HOH B . 
N 4 HOH 108 408 306 HOH HOH B . 
N 4 HOH 109 409 196 HOH HOH B . 
N 4 HOH 110 410 149 HOH HOH B . 
N 4 HOH 111 411 417 HOH HOH B . 
N 4 HOH 112 412 204 HOH HOH B . 
N 4 HOH 113 413 332 HOH HOH B . 
N 4 HOH 114 414 442 HOH HOH B . 
N 4 HOH 115 415 213 HOH HOH B . 
N 4 HOH 116 416 260 HOH HOH B . 
N 4 HOH 117 417 62  HOH HOH B . 
N 4 HOH 118 418 312 HOH HOH B . 
N 4 HOH 119 419 307 HOH HOH B . 
N 4 HOH 120 420 403 HOH HOH B . 
N 4 HOH 121 421 425 HOH HOH B . 
N 4 HOH 122 422 175 HOH HOH B . 
N 4 HOH 123 423 245 HOH HOH B . 
N 4 HOH 124 424 264 HOH HOH B . 
N 4 HOH 125 425 83  HOH HOH B . 
N 4 HOH 126 426 343 HOH HOH B . 
N 4 HOH 127 427 324 HOH HOH B . 
N 4 HOH 128 428 234 HOH HOH B . 
N 4 HOH 129 429 82  HOH HOH B . 
N 4 HOH 130 430 436 HOH HOH B . 
N 4 HOH 131 431 434 HOH HOH B . 
N 4 HOH 132 432 293 HOH HOH B . 
N 4 HOH 133 433 430 HOH HOH B . 
N 4 HOH 134 434 439 HOH HOH B . 
N 4 HOH 135 435 361 HOH HOH B . 
N 4 HOH 136 436 424 HOH HOH B . 
N 4 HOH 137 437 311 HOH HOH B . 
N 4 HOH 138 438 54  HOH HOH B . 
N 4 HOH 139 439 9   HOH HOH B . 
O 4 HOH 1   301 77  HOH HOH C . 
O 4 HOH 2   302 429 HOH HOH C . 
O 4 HOH 3   303 359 HOH HOH C . 
O 4 HOH 4   304 202 HOH HOH C . 
O 4 HOH 5   305 127 HOH HOH C . 
O 4 HOH 6   306 254 HOH HOH C . 
O 4 HOH 7   307 372 HOH HOH C . 
O 4 HOH 8   308 256 HOH HOH C . 
O 4 HOH 9   309 377 HOH HOH C . 
O 4 HOH 10  310 320 HOH HOH C . 
O 4 HOH 11  311 431 HOH HOH C . 
O 4 HOH 12  312 24  HOH HOH C . 
O 4 HOH 13  313 252 HOH HOH C . 
O 4 HOH 14  314 282 HOH HOH C . 
O 4 HOH 15  315 177 HOH HOH C . 
O 4 HOH 16  316 59  HOH HOH C . 
O 4 HOH 17  317 230 HOH HOH C . 
O 4 HOH 18  318 146 HOH HOH C . 
O 4 HOH 19  319 345 HOH HOH C . 
O 4 HOH 20  320 30  HOH HOH C . 
O 4 HOH 21  321 310 HOH HOH C . 
O 4 HOH 22  322 291 HOH HOH C . 
O 4 HOH 23  323 137 HOH HOH C . 
O 4 HOH 24  324 418 HOH HOH C . 
O 4 HOH 25  325 93  HOH HOH C . 
O 4 HOH 26  326 201 HOH HOH C . 
O 4 HOH 27  327 294 HOH HOH C . 
O 4 HOH 28  328 211 HOH HOH C . 
O 4 HOH 29  329 308 HOH HOH C . 
O 4 HOH 30  330 157 HOH HOH C . 
O 4 HOH 31  331 181 HOH HOH C . 
O 4 HOH 32  332 288 HOH HOH C . 
O 4 HOH 33  333 100 HOH HOH C . 
O 4 HOH 34  334 322 HOH HOH C . 
O 4 HOH 35  335 143 HOH HOH C . 
O 4 HOH 36  336 53  HOH HOH C . 
O 4 HOH 37  337 14  HOH HOH C . 
O 4 HOH 38  338 378 HOH HOH C . 
O 4 HOH 39  339 215 HOH HOH C . 
O 4 HOH 40  340 91  HOH HOH C . 
O 4 HOH 41  341 413 HOH HOH C . 
O 4 HOH 42  342 13  HOH HOH C . 
O 4 HOH 43  343 227 HOH HOH C . 
O 4 HOH 44  344 61  HOH HOH C . 
O 4 HOH 45  345 20  HOH HOH C . 
O 4 HOH 46  346 363 HOH HOH C . 
O 4 HOH 47  347 151 HOH HOH C . 
O 4 HOH 48  348 440 HOH HOH C . 
O 4 HOH 49  349 275 HOH HOH C . 
O 4 HOH 50  350 189 HOH HOH C . 
O 4 HOH 51  351 64  HOH HOH C . 
O 4 HOH 52  352 65  HOH HOH C . 
O 4 HOH 53  353 223 HOH HOH C . 
O 4 HOH 54  354 7   HOH HOH C . 
O 4 HOH 55  355 184 HOH HOH C . 
O 4 HOH 56  356 85  HOH HOH C . 
O 4 HOH 57  357 116 HOH HOH C . 
O 4 HOH 58  358 112 HOH HOH C . 
O 4 HOH 59  359 166 HOH HOH C . 
O 4 HOH 60  360 60  HOH HOH C . 
O 4 HOH 61  361 49  HOH HOH C . 
O 4 HOH 62  362 313 HOH HOH C . 
O 4 HOH 63  363 5   HOH HOH C . 
O 4 HOH 64  364 113 HOH HOH C . 
O 4 HOH 65  365 272 HOH HOH C . 
O 4 HOH 66  366 152 HOH HOH C . 
O 4 HOH 67  367 131 HOH HOH C . 
O 4 HOH 68  368 257 HOH HOH C . 
O 4 HOH 69  369 239 HOH HOH C . 
O 4 HOH 70  370 158 HOH HOH C . 
O 4 HOH 71  371 374 HOH HOH C . 
O 4 HOH 72  372 279 HOH HOH C . 
O 4 HOH 73  373 162 HOH HOH C . 
O 4 HOH 74  374 167 HOH HOH C . 
O 4 HOH 75  375 39  HOH HOH C . 
O 4 HOH 76  376 290 HOH HOH C . 
O 4 HOH 77  377 66  HOH HOH C . 
O 4 HOH 78  378 186 HOH HOH C . 
O 4 HOH 79  379 342 HOH HOH C . 
O 4 HOH 80  380 68  HOH HOH C . 
O 4 HOH 81  381 94  HOH HOH C . 
O 4 HOH 82  382 357 HOH HOH C . 
O 4 HOH 83  383 126 HOH HOH C . 
O 4 HOH 84  384 1   HOH HOH C . 
O 4 HOH 85  385 325 HOH HOH C . 
O 4 HOH 86  386 287 HOH HOH C . 
O 4 HOH 87  387 128 HOH HOH C . 
O 4 HOH 88  388 389 HOH HOH C . 
O 4 HOH 89  389 119 HOH HOH C . 
O 4 HOH 90  390 76  HOH HOH C . 
O 4 HOH 91  391 148 HOH HOH C . 
O 4 HOH 92  392 171 HOH HOH C . 
O 4 HOH 93  393 206 HOH HOH C . 
O 4 HOH 94  394 139 HOH HOH C . 
O 4 HOH 95  395 90  HOH HOH C . 
O 4 HOH 96  396 435 HOH HOH C . 
O 4 HOH 97  397 111 HOH HOH C . 
O 4 HOH 98  398 133 HOH HOH C . 
O 4 HOH 99  399 331 HOH HOH C . 
O 4 HOH 100 400 58  HOH HOH C . 
O 4 HOH 101 401 18  HOH HOH C . 
O 4 HOH 102 402 199 HOH HOH C . 
O 4 HOH 103 403 259 HOH HOH C . 
O 4 HOH 104 404 341 HOH HOH C . 
O 4 HOH 105 405 42  HOH HOH C . 
O 4 HOH 106 406 338 HOH HOH C . 
O 4 HOH 107 407 163 HOH HOH C . 
O 4 HOH 108 408 393 HOH HOH C . 
O 4 HOH 109 409 161 HOH HOH C . 
O 4 HOH 110 410 285 HOH HOH C . 
O 4 HOH 111 411 356 HOH HOH C . 
O 4 HOH 112 412 334 HOH HOH C . 
O 4 HOH 113 413 217 HOH HOH C . 
O 4 HOH 114 414 170 HOH HOH C . 
O 4 HOH 115 415 185 HOH HOH C . 
O 4 HOH 116 416 432 HOH HOH C . 
O 4 HOH 117 417 370 HOH HOH C . 
O 4 HOH 118 418 329 HOH HOH C . 
O 4 HOH 119 419 115 HOH HOH C . 
O 4 HOH 120 420 19  HOH HOH C . 
O 4 HOH 121 421 106 HOH HOH C . 
O 4 HOH 122 422 292 HOH HOH C . 
O 4 HOH 123 423 253 HOH HOH C . 
O 4 HOH 124 424 371 HOH HOH C . 
O 4 HOH 125 425 110 HOH HOH C . 
O 4 HOH 126 426 407 HOH HOH C . 
O 4 HOH 127 427 445 HOH HOH C . 
O 4 HOH 128 428 228 HOH HOH C . 
O 4 HOH 129 429 354 HOH HOH C . 
O 4 HOH 130 430 26  HOH HOH C . 
O 4 HOH 131 431 318 HOH HOH C . 
O 4 HOH 132 432 428 HOH HOH C . 
O 4 HOH 133 433 249 HOH HOH C . 
O 4 HOH 134 434 409 HOH HOH C . 
O 4 HOH 135 435 250 HOH HOH C . 
O 4 HOH 136 436 321 HOH HOH C . 
O 4 HOH 137 437 274 HOH HOH C . 
O 4 HOH 138 438 346 HOH HOH C . 
O 4 HOH 139 439 323 HOH HOH C . 
O 4 HOH 140 440 207 HOH HOH C . 
O 4 HOH 141 441 444 HOH HOH C . 
O 4 HOH 142 442 379 HOH HOH C . 
O 4 HOH 143 443 303 HOH HOH C . 
O 4 HOH 144 444 412 HOH HOH C . 
O 4 HOH 145 445 188 HOH HOH C . 
O 4 HOH 146 446 406 HOH HOH C . 
O 4 HOH 147 447 299 HOH HOH C . 
O 4 HOH 148 448 145 HOH HOH C . 
O 4 HOH 149 449 390 HOH HOH C . 
O 4 HOH 150 450 397 HOH HOH C . 
O 4 HOH 151 451 125 HOH HOH C . 
O 4 HOH 152 452 78  HOH HOH C . 
O 4 HOH 153 453 362 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B GLN 28 ? CD  ? B GLN 28 CD  
2  1 Y 1 B GLN 28 ? OE1 ? B GLN 28 OE1 
3  1 Y 1 B GLN 28 ? NE2 ? B GLN 28 NE2 
4  1 Y 1 B LEU 46 ? CD1 ? B LEU 46 CD1 
5  1 Y 1 B LEU 46 ? CD2 ? B LEU 46 CD2 
6  1 Y 1 B GLU 85 ? CG  ? B GLU 85 CG  
7  1 Y 1 B GLU 85 ? CD  ? B GLU 85 CD  
8  1 Y 1 B GLU 85 ? OE1 ? B GLU 85 OE1 
9  1 Y 1 B GLU 85 ? OE2 ? B GLU 85 OE2 
10 1 Y 1 C LYS 77 ? CE  ? C LYS 77 CE  
11 1 Y 1 C LYS 77 ? NZ  ? C LYS 77 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.11.1_2575 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7EDQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.581 
_cell.length_a_esd                 ? 
_cell.length_b                     68.472 
_cell.length_b_esd                 ? 
_cell.length_c                     86.294 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7EDQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7EDQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.69 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         54.33 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.50 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            290 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2.0M Ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-06-26 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate            13.89 
_reflns.entry_id                         7EDQ 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.266 
_reflns.d_resolution_low                 43.147 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       107167 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  10.5 
_reflns.pdbx_Rmerge_I_obs                0.057 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.057 
_reflns.pdbx_netI_over_av_sigmaI         18.3 
_reflns.pdbx_netI_over_sigmaI            18.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.059 
_reflns.pdbx_Rpim_I_all                  0.018 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     1.000 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  1.27 
_reflns_shell.d_res_low                   1.29 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.2 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           5219 
_reflns_shell.percent_possible_all        99.9 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                1.435 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             8.1 
_reflns_shell.pdbx_Rsym_value             1.435 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             0.528 
_reflns_shell.pdbx_Rpim_I_all             0.553 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.553 
_reflns_shell.pdbx_CC_star                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                49.910 
_refine.B_iso_mean                               19.8013 
_refine.B_iso_min                                7.780 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7EDQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.2660 
_refine.ls_d_res_low                             43.1470 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     107082 
_refine.ls_number_reflns_R_free                  2009 
_refine.ls_number_reflns_R_work                  105073 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9900 
_refine.ls_percent_reflns_R_free                 1.8800 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1702 
_refine.ls_R_factor_R_free                       0.1898 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1698 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1MIF 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.2000 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1500 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.2660 
_refine_hist.d_res_low                        43.1470 
_refine_hist.number_atoms_solvent             446 
_refine_hist.number_atoms_total               3057 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       342 
_refine_hist.pdbx_B_iso_mean_ligand           33.06 
_refine_hist.pdbx_B_iso_mean_solvent          30.19 
_refine_hist.pdbx_number_atoms_protein        2590 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012 ? 2692 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.103 ? 3671 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.107 ? 405  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 484  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.626 ? 1558 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? ? ? ? 1 TORSIONAL ? A 1531 7.372 ? 1 
'X-RAY DIFFRACTION' 2 ? ? ? ? ? 2 TORSIONAL ? B 1531 7.372 ? 1 
'X-RAY DIFFRACTION' 3 ? ? ? ? ? 3 TORSIONAL ? C 1531 7.372 ? 1 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 1.266  1.2972 . . 139 7404 100.0000 . . . 0.3539 0.0000 0.3685 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.2972 1.3323 . . 147 7402 100.0000 . . . 0.4321 0.0000 0.2977 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.3323 1.3715 . . 142 7454 100.0000 . . . 0.3445 0.0000 0.2834 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.3715 1.4158 . . 142 7432 100.0000 . . . 0.2801 0.0000 0.2395 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.4158 1.4664 . . 140 7428 100.0000 . . . 0.2337 0.0000 0.2097 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.4664 1.5251 . . 141 7460 100.0000 . . . 0.2106 0.0000 0.1828 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.5251 1.5945 . . 147 7463 100.0000 . . . 0.1930 0.0000 0.1782 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.5945 1.6786 . . 138 7453 100.0000 . . . 0.1855 0.0000 0.1598 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.6786 1.7838 . . 143 7491 100.0000 . . . 0.2357 0.0000 0.1657 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.7838 1.9215 . . 140 7511 100.0000 . . . 0.1630 0.0000 0.1517 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.9215 2.1149 . . 144 7528 100.0000 . . . 0.1951 0.0000 0.1457 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.1149 2.4209 . . 142 7550 100.0000 . . . 0.1656 0.0000 0.1548 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4209 3.0499 . . 149 7606 100.0000 . . . 0.1697 0.0000 0.1721 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0499 43.147 . . 155 7891 100.0000 . . . 0.1663 0.0000 0.1537 . . . . . . . . . . . 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 2 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 3 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A PRO 1  . A ALA 12  . A PRO 1  A ALA 12  ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 2 A VAL 14 . A LEU 19  . A VAL 14 A LEU 19  ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 3 A GLU 21 . A ALA 27  . A GLU 21 A ALA 27  ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 4 A GLN 28 . A GLN 28  . A GLN 28 A GLN 28  ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 5 A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 6 A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 7 A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 8 A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 1 9 A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 2 1 B PRO 1  . B ALA 12  . B PRO 1  B ALA 12  ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 2 B VAL 14 . B LEU 19  . B VAL 14 B LEU 19  ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 3 B GLU 21 . B SER 52  . B GLU 21 B SER 52  ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 4 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 5 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 6 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 7 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 8 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 2 9 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 12 or resid 14 through 19 or resid 21 through 52 or resid 54 through 76 or (resid 77 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resid 78 through 114))
;
1 3 1 C PRO 1  . C ALA 12  . C PRO 1  C ALA 12  ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 2 C VAL 14 . C LEU 19  . C VAL 14 C LEU 19  ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 3 C GLU 21 . C ALA 27  . C GLU 21 C ALA 27  ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 4 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 5 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 6 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 7 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
1 3 8 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 12 or resid 14 through 19 or resid 21 through 27 or (resid 28 and (name N or name CA or name C or name O or name CB or name CG )) or resid 29 through 45 or (resid 46 and (name N or name CA or name C or name O or name CB or name CG )) or resid 47 through 52 or resid 54 through 84 or (resid 85 and (name N or name CA or name C or name O or name CB )) or resid 86 through 114))
;
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     7EDQ 
_struct.title                        'MIF complex to compound7' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7EDQ 
_struct_keywords.text            'tautomerase, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MIF_HUMAN 
_struct_ref.pdbx_db_accession          P14174 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLC
GLLAERLRISPDRVYINYYDMNAANVGWNNSTFA
;
_struct_ref.pdbx_align_begin           2 
# 
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 7EDQ A 1 ? 114 ? P14174 2 ? 115 ? 1 114 
2 1 7EDQ B 1 ? 114 ? P14174 2 ? 115 ? 1 114 
3 1 7EDQ C 1 ? 114 ? P14174 2 ? 115 ? 1 114 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7740  ? 
1 MORE         -123  ? 
1 'SSA (A^2)'  12990 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 PRO A 10  ? VAL A 14  ? PRO A 10  VAL A 14  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 17  ? GLY A 31  ? GLY A 17  GLY A 31  1 ? 15 
HELX_P HELX_P3  AA3 PRO A 33  ? TYR A 36  ? PRO A 33  TYR A 36  5 ? 4  
HELX_P HELX_P4  AA4 GLY A 68  ? ARG A 88  ? GLY A 68  ARG A 88  1 ? 21 
HELX_P HELX_P5  AA5 SER A 90  ? ASP A 92  ? SER A 90  ASP A 92  5 ? 3  
HELX_P HELX_P6  AA6 ASN A 102 ? ALA A 104 ? ASN A 102 ALA A 104 5 ? 3  
HELX_P HELX_P7  AA7 PRO B 10  ? VAL B 14  ? PRO B 10  VAL B 14  5 ? 5  
HELX_P HELX_P8  AA8 GLY B 17  ? GLY B 31  ? GLY B 17  GLY B 31  1 ? 15 
HELX_P HELX_P9  AA9 PRO B 33  ? TYR B 36  ? PRO B 33  TYR B 36  5 ? 4  
HELX_P HELX_P10 AB1 GLY B 68  ? ARG B 88  ? GLY B 68  ARG B 88  1 ? 21 
HELX_P HELX_P11 AB2 SER B 90  ? ASP B 92  ? SER B 90  ASP B 92  5 ? 3  
HELX_P HELX_P12 AB3 ASN B 102 ? ALA B 104 ? ASN B 102 ALA B 104 5 ? 3  
HELX_P HELX_P13 AB4 PRO C 10  ? VAL C 14  ? PRO C 10  VAL C 14  5 ? 5  
HELX_P HELX_P14 AB5 GLY C 17  ? GLY C 31  ? GLY C 17  GLY C 31  1 ? 15 
HELX_P HELX_P15 AB6 PRO C 33  ? TYR C 36  ? PRO C 33  TYR C 36  5 ? 4  
HELX_P HELX_P16 AB7 GLY C 68  ? ARG C 88  ? GLY C 68  ARG C 88  1 ? 21 
HELX_P HELX_P17 AB8 SER C 90  ? ASP C 92  ? SER C 90  ASP C 92  5 ? 3  
HELX_P HELX_P18 AB9 ASN C 102 ? ALA C 104 ? ASN C 102 ALA C 104 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 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 SER B 111 ? THR B 112 ? SER B 111 THR B 112 
AA1 2 VAL B 106 ? TRP B 108 ? VAL B 106 TRP B 108 
AA1 3 VAL A 94  ? ASP A 100 ? VAL A 94  ASP A 100 
AA1 4 ALA A 57  ? SER A 63  ? ALA A 57  SER A 63  
AA1 5 MET A 2   ? THR A 7   ? MET A 2   THR A 7   
AA1 6 ALA A 38  ? VAL A 42  ? ALA A 38  VAL A 42  
AA1 7 LEU C 46  ? PHE C 49  ? LEU C 46  PHE C 49  
AA2 1 LEU A 46  ? PHE A 49  ? LEU A 46  PHE A 49  
AA2 2 ALA B 38  ? VAL B 42  ? ALA B 38  VAL B 42  
AA2 3 MET B 2   ? THR B 7   ? MET B 2   THR B 7   
AA2 4 ALA B 57  ? SER B 63  ? ALA B 57  SER B 63  
AA2 5 VAL B 94  ? ASP B 100 ? VAL B 94  ASP B 100 
AA2 6 VAL C 106 ? TRP C 108 ? VAL C 106 TRP C 108 
AA2 7 SER C 111 ? THR C 112 ? SER C 111 THR C 112 
AA3 1 SER A 111 ? THR A 112 ? SER A 111 THR A 112 
AA3 2 VAL A 106 ? TRP A 108 ? VAL A 106 TRP A 108 
AA3 3 VAL C 94  ? ASP C 100 ? VAL C 94  ASP C 100 
AA3 4 ALA C 57  ? SER C 63  ? ALA C 57  SER C 63  
AA3 5 MET C 2   ? THR C 7   ? MET C 2   THR C 7   
AA3 6 ALA C 38  ? VAL C 42  ? ALA C 38  VAL C 42  
AA3 7 LEU B 46  ? PHE B 49  ? LEU B 46  PHE B 49  
# 
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 O SER B 111 ? O SER B 111 N TRP B 108 ? N TRP B 108 
AA1 2 3 O GLY B 107 ? O GLY B 107 N ILE A 96  ? N ILE A 96  
AA1 3 4 O ASN A 97  ? O ASN A 97  N CYS A 59  ? N CYS A 59  
AA1 4 5 O LEU A 58  ? O LEU A 58  N ASN A 6   ? N ASN A 6   
AA1 5 6 N VAL A 5   ? N VAL A 5   O VAL A 42  ? O VAL A 42  
AA1 6 7 N VAL A 39  ? N VAL A 39  O ALA C 48  ? O ALA C 48  
AA2 1 2 N ALA A 48  ? N ALA A 48  O VAL B 39  ? O VAL B 39  
AA2 2 3 O VAL B 42  ? O VAL B 42  N VAL B 5   ? N VAL B 5   
AA2 3 4 N ASN B 6   ? N ASN B 6   O LEU B 58  ? O LEU B 58  
AA2 4 5 N CYS B 59  ? N CYS B 59  O ASN B 97  ? O ASN B 97  
AA2 5 6 N ILE B 96  ? N ILE B 96  O GLY C 107 ? O GLY C 107 
AA2 6 7 N TRP C 108 ? N TRP C 108 O SER C 111 ? O SER C 111 
AA3 1 2 O SER A 111 ? O SER A 111 N TRP A 108 ? N TRP A 108 
AA3 2 3 N GLY A 107 ? N GLY A 107 O ILE C 96  ? O ILE C 96  
AA3 3 4 O ASN C 97  ? O ASN C 97  N CYS C 59  ? N CYS C 59  
AA3 4 5 O LEU C 58  ? O LEU C 58  N ASN C 6   ? N ASN C 6   
AA3 5 6 N VAL C 5   ? N VAL C 5   O VAL C 42  ? O VAL C 42  
AA3 6 7 O VAL C 39  ? O VAL C 39  N ALA B 48  ? N ALA B 48  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A HFC 201 ? 10 'binding site for residue HFC A 201' 
AC2 Software A CL  202 ? 4  'binding site for residue CL A 202'  
AC3 Software A CL  203 ? 4  'binding site for residue CL A 203'  
AC4 Software A CL  204 ? 3  'binding site for residue CL A 204'  
AC5 Software B CL  201 ? 3  'binding site for residue CL B 201'  
AC6 Software B CL  202 ? 3  'binding site for residue CL B 202'  
AC7 Software C CL  201 ? 3  'binding site for residue CL C 201'  
AC8 Software C CL  202 ? 5  'binding site for residue CL C 202'  
AC9 Software C CL  203 ? 3  'binding site for residue CL C 203'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 10 GLN A 35  ? GLN A 35  . ? 1_555 ? 
2  AC1 10 TYR A 36  ? TYR A 36  . ? 1_555 ? 
3  AC1 10 TRP A 108 ? TRP A 108 . ? 1_555 ? 
4  AC1 10 PHE A 113 ? PHE A 113 . ? 1_555 ? 
5  AC1 10 HOH M .   ? HOH A 366 . ? 1_555 ? 
6  AC1 10 HOH M .   ? HOH A 379 . ? 1_555 ? 
7  AC1 10 GLY B 50  ? GLY B 50  . ? 3_644 ? 
8  AC1 10 PRO C 34  ? PRO C 34  . ? 3_644 ? 
9  AC1 10 GLN C 35  ? GLN C 35  . ? 3_644 ? 
10 AC1 10 TYR C 95  ? TYR C 95  . ? 1_555 ? 
11 AC2 4  PRO A 1   ? PRO A 1   . ? 1_555 ? 
12 AC2 4  ILE A 64  ? ILE A 64  . ? 1_555 ? 
13 AC2 4  HOH O .   ? HOH C 319 . ? 1_555 ? 
14 AC2 4  HOH O .   ? HOH C 381 . ? 3_644 ? 
15 AC3 4  GLY A 68  ? GLY A 68  . ? 1_555 ? 
16 AC3 4  GLY A 69  ? GLY A 69  . ? 1_555 ? 
17 AC3 4  ALA A 70  ? ALA A 70  . ? 1_555 ? 
18 AC3 4  GLN A 71  ? GLN A 71  . ? 1_555 ? 
19 AC4 3  ASN A 102 ? ASN A 102 . ? 1_555 ? 
20 AC4 3  ASN A 105 ? ASN A 105 . ? 1_555 ? 
21 AC4 3  HOH O .   ? HOH C 337 . ? 1_555 ? 
22 AC5 3  HOH M .   ? HOH A 314 . ? 1_555 ? 
23 AC5 3  PRO B 1   ? PRO B 1   . ? 1_555 ? 
24 AC5 3  ILE B 64  ? ILE B 64  . ? 1_555 ? 
25 AC6 3  HOH M .   ? HOH A 325 . ? 1_555 ? 
26 AC6 3  ASN B 102 ? ASN B 102 . ? 1_555 ? 
27 AC6 3  ASN B 105 ? ASN B 105 . ? 1_555 ? 
28 AC7 3  HOH N .   ? HOH B 406 . ? 1_555 ? 
29 AC7 3  PRO C 1   ? PRO C 1   . ? 1_555 ? 
30 AC7 3  ILE C 64  ? ILE C 64  . ? 1_555 ? 
31 AC8 5  GLY C 68  ? GLY C 68  . ? 1_555 ? 
32 AC8 5  GLY C 69  ? GLY C 69  . ? 1_555 ? 
33 AC8 5  ALA C 70  ? ALA C 70  . ? 1_555 ? 
34 AC8 5  GLN C 71  ? GLN C 71  . ? 1_555 ? 
35 AC8 5  HOH O .   ? HOH C 444 . ? 1_555 ? 
36 AC9 3  HOH N .   ? HOH B 335 . ? 1_555 ? 
37 AC9 3  ASN C 102 ? ASN C 102 . ? 1_555 ? 
38 AC9 3  ASN C 105 ? ASN C 105 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   7EDQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 424 ? ? O A HOH 434 ? ? 2.13 
2 1 O A HOH 414 ? ? O A HOH 419 ? ? 2.15 
3 1 O C HOH 305 ? ? O C HOH 338 ? ? 2.18 
4 1 O B HOH 359 ? ? O B HOH 392 ? ? 2.19 
5 1 O C GLY 31  ? ? O C HOH 301 ? ? 2.19 
# 
_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     370 
_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     304 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            C 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_1             31 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            C 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             32 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.149 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            -0.187 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER B 111 ? ? -151.71 -157.29 
2 1 SER C 111 ? ? -149.70 -157.75 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   C 
_pdbx_validate_polymer_linkage.auth_comp_id_1   GLY 
_pdbx_validate_polymer_linkage.auth_seq_id_1    31 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   C 
_pdbx_validate_polymer_linkage.auth_comp_id_2   LYS 
_pdbx_validate_polymer_linkage.auth_seq_id_2    32 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             1.15 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       454 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.88 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HFC C1   C  Y N 138 
HFC C2   C  Y N 139 
HFC C3   C  Y N 140 
HFC C4   C  Y N 141 
HFC C5   C  Y N 142 
HFC C6   C  Y N 143 
HFC O7   O  N N 144 
HFC C8   C  N N 145 
HFC C9   C  N N 146 
HFC C10  C  N N 147 
HFC O11  O  N N 148 
HFC O12  O  N N 149 
HFC O13  O  N N 150 
HFC H1   H  N N 151 
HFC H2   H  N N 152 
HFC H3   H  N N 153 
HFC H4   H  N N 154 
HFC H5   H  N N 155 
HFC H6   H  N N 156 
HIS N    N  N N 157 
HIS CA   C  N S 158 
HIS C    C  N N 159 
HIS O    O  N N 160 
HIS CB   C  N N 161 
HIS CG   C  Y N 162 
HIS ND1  N  Y N 163 
HIS CD2  C  Y N 164 
HIS CE1  C  Y N 165 
HIS NE2  N  Y N 166 
HIS OXT  O  N N 167 
HIS H    H  N N 168 
HIS H2   H  N N 169 
HIS HA   H  N N 170 
HIS HB2  H  N N 171 
HIS HB3  H  N N 172 
HIS HD1  H  N N 173 
HIS HD2  H  N N 174 
HIS HE1  H  N N 175 
HIS HE2  H  N N 176 
HIS HXT  H  N N 177 
HOH O    O  N N 178 
HOH H1   H  N N 179 
HOH H2   H  N N 180 
ILE N    N  N N 181 
ILE CA   C  N S 182 
ILE C    C  N N 183 
ILE O    O  N N 184 
ILE CB   C  N S 185 
ILE CG1  C  N N 186 
ILE CG2  C  N N 187 
ILE CD1  C  N N 188 
ILE OXT  O  N N 189 
ILE H    H  N N 190 
ILE H2   H  N N 191 
ILE HA   H  N N 192 
ILE HB   H  N N 193 
ILE HG12 H  N N 194 
ILE HG13 H  N N 195 
ILE HG21 H  N N 196 
ILE HG22 H  N N 197 
ILE HG23 H  N N 198 
ILE HD11 H  N N 199 
ILE HD12 H  N N 200 
ILE HD13 H  N N 201 
ILE HXT  H  N N 202 
LEU N    N  N N 203 
LEU CA   C  N S 204 
LEU C    C  N N 205 
LEU O    O  N N 206 
LEU CB   C  N N 207 
LEU CG   C  N N 208 
LEU CD1  C  N N 209 
LEU CD2  C  N N 210 
LEU OXT  O  N N 211 
LEU H    H  N N 212 
LEU H2   H  N N 213 
LEU HA   H  N N 214 
LEU HB2  H  N N 215 
LEU HB3  H  N N 216 
LEU HG   H  N N 217 
LEU HD11 H  N N 218 
LEU HD12 H  N N 219 
LEU HD13 H  N N 220 
LEU HD21 H  N N 221 
LEU HD22 H  N N 222 
LEU HD23 H  N N 223 
LEU HXT  H  N N 224 
LYS N    N  N N 225 
LYS CA   C  N S 226 
LYS C    C  N N 227 
LYS O    O  N N 228 
LYS CB   C  N N 229 
LYS CG   C  N N 230 
LYS CD   C  N N 231 
LYS CE   C  N N 232 
LYS NZ   N  N N 233 
LYS OXT  O  N N 234 
LYS H    H  N N 235 
LYS H2   H  N N 236 
LYS HA   H  N N 237 
LYS HB2  H  N N 238 
LYS HB3  H  N N 239 
LYS HG2  H  N N 240 
LYS HG3  H  N N 241 
LYS HD2  H  N N 242 
LYS HD3  H  N N 243 
LYS HE2  H  N N 244 
LYS HE3  H  N N 245 
LYS HZ1  H  N N 246 
LYS HZ2  H  N N 247 
LYS HZ3  H  N N 248 
LYS HXT  H  N N 249 
MET N    N  N N 250 
MET CA   C  N S 251 
MET C    C  N N 252 
MET O    O  N N 253 
MET CB   C  N N 254 
MET CG   C  N N 255 
MET SD   S  N N 256 
MET CE   C  N N 257 
MET OXT  O  N N 258 
MET H    H  N N 259 
MET H2   H  N N 260 
MET HA   H  N N 261 
MET HB2  H  N N 262 
MET HB3  H  N N 263 
MET HG2  H  N N 264 
MET HG3  H  N N 265 
MET HE1  H  N N 266 
MET HE2  H  N N 267 
MET HE3  H  N N 268 
MET HXT  H  N N 269 
PHE N    N  N N 270 
PHE CA   C  N S 271 
PHE C    C  N N 272 
PHE O    O  N N 273 
PHE CB   C  N N 274 
PHE CG   C  Y N 275 
PHE CD1  C  Y N 276 
PHE CD2  C  Y N 277 
PHE CE1  C  Y N 278 
PHE CE2  C  Y N 279 
PHE CZ   C  Y N 280 
PHE OXT  O  N N 281 
PHE H    H  N N 282 
PHE H2   H  N N 283 
PHE HA   H  N N 284 
PHE HB2  H  N N 285 
PHE HB3  H  N N 286 
PHE HD1  H  N N 287 
PHE HD2  H  N N 288 
PHE HE1  H  N N 289 
PHE HE2  H  N N 290 
PHE HZ   H  N N 291 
PHE HXT  H  N N 292 
PRO N    N  N N 293 
PRO CA   C  N S 294 
PRO C    C  N N 295 
PRO O    O  N N 296 
PRO CB   C  N N 297 
PRO CG   C  N N 298 
PRO CD   C  N N 299 
PRO OXT  O  N N 300 
PRO H    H  N N 301 
PRO HA   H  N N 302 
PRO HB2  H  N N 303 
PRO HB3  H  N N 304 
PRO HG2  H  N N 305 
PRO HG3  H  N N 306 
PRO HD2  H  N N 307 
PRO HD3  H  N N 308 
PRO HXT  H  N N 309 
SER N    N  N N 310 
SER CA   C  N S 311 
SER C    C  N N 312 
SER O    O  N N 313 
SER CB   C  N N 314 
SER OG   O  N N 315 
SER OXT  O  N N 316 
SER H    H  N N 317 
SER H2   H  N N 318 
SER HA   H  N N 319 
SER HB2  H  N N 320 
SER HB3  H  N N 321 
SER HG   H  N N 322 
SER HXT  H  N N 323 
THR N    N  N N 324 
THR CA   C  N S 325 
THR C    C  N N 326 
THR O    O  N N 327 
THR CB   C  N R 328 
THR OG1  O  N N 329 
THR CG2  C  N N 330 
THR OXT  O  N N 331 
THR H    H  N N 332 
THR H2   H  N N 333 
THR HA   H  N N 334 
THR HB   H  N N 335 
THR HG1  H  N N 336 
THR HG21 H  N N 337 
THR HG22 H  N N 338 
THR HG23 H  N N 339 
THR HXT  H  N N 340 
TRP N    N  N N 341 
TRP CA   C  N S 342 
TRP C    C  N N 343 
TRP O    O  N N 344 
TRP CB   C  N N 345 
TRP CG   C  Y N 346 
TRP CD1  C  Y N 347 
TRP CD2  C  Y N 348 
TRP NE1  N  Y N 349 
TRP CE2  C  Y N 350 
TRP CE3  C  Y N 351 
TRP CZ2  C  Y N 352 
TRP CZ3  C  Y N 353 
TRP CH2  C  Y N 354 
TRP OXT  O  N N 355 
TRP H    H  N N 356 
TRP H2   H  N N 357 
TRP HA   H  N N 358 
TRP HB2  H  N N 359 
TRP HB3  H  N N 360 
TRP HD1  H  N N 361 
TRP HE1  H  N N 362 
TRP HE3  H  N N 363 
TRP HZ2  H  N N 364 
TRP HZ3  H  N N 365 
TRP HH2  H  N N 366 
TRP HXT  H  N N 367 
TYR N    N  N N 368 
TYR CA   C  N S 369 
TYR C    C  N N 370 
TYR O    O  N N 371 
TYR CB   C  N N 372 
TYR CG   C  Y N 373 
TYR CD1  C  Y N 374 
TYR CD2  C  Y N 375 
TYR CE1  C  Y N 376 
TYR CE2  C  Y N 377 
TYR CZ   C  Y N 378 
TYR OH   O  N N 379 
TYR OXT  O  N N 380 
TYR H    H  N N 381 
TYR H2   H  N N 382 
TYR HA   H  N N 383 
TYR HB2  H  N N 384 
TYR HB3  H  N N 385 
TYR HD1  H  N N 386 
TYR HD2  H  N N 387 
TYR HE1  H  N N 388 
TYR HE2  H  N N 389 
TYR HH   H  N N 390 
TYR HXT  H  N N 391 
VAL N    N  N N 392 
VAL CA   C  N S 393 
VAL C    C  N N 394 
VAL O    O  N N 395 
VAL CB   C  N N 396 
VAL CG1  C  N N 397 
VAL CG2  C  N N 398 
VAL OXT  O  N N 399 
VAL H    H  N N 400 
VAL H2   H  N N 401 
VAL HA   H  N N 402 
VAL HB   H  N N 403 
VAL HG11 H  N N 404 
VAL HG12 H  N N 405 
VAL HG13 H  N N 406 
VAL HG21 H  N N 407 
VAL HG22 H  N N 408 
VAL HG23 H  N N 409 
VAL HXT  H  N N 410 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HFC C10 C9   doub N N 129 
HFC C10 C2   sing N N 130 
HFC C9  C8   sing N N 131 
HFC C3  C2   doub Y N 132 
HFC C3  C4   sing Y N 133 
HFC C2  C1   sing Y N 134 
HFC O13 C4   sing N N 135 
HFC C8  O11  doub N N 136 
HFC C8  O7   sing N N 137 
HFC C4  C5   doub Y N 138 
HFC C1  O7   sing N N 139 
HFC C1  C6   doub Y N 140 
HFC C5  C6   sing Y N 141 
HFC C5  O12  sing N N 142 
HFC C3  H1   sing N N 143 
HFC C6  H2   sing N N 144 
HFC C9  H3   sing N N 145 
HFC C10 H4   sing N N 146 
HFC O12 H5   sing N N 147 
HFC O13 H6   sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           31570762 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    7EDQ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.014797 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014605 
_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]   0.011588 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
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   . PRO A 1 1   ? 31.164 -18.890 -12.052 1.00 14.30 ? 1   PRO A N   1 
ATOM   2    C  CA  . PRO A 1 1   ? 30.008 -18.216 -11.450 1.00 14.39 ? 1   PRO A CA  1 
ATOM   3    C  C   . PRO A 1 1   ? 30.454 -16.970 -10.732 1.00 14.09 ? 1   PRO A C   1 
ATOM   4    O  O   . PRO A 1 1   ? 31.659 -16.770 -10.496 1.00 14.46 ? 1   PRO A O   1 
ATOM   5    C  CB  . PRO A 1 1   ? 29.478 -19.239 -10.445 1.00 16.26 ? 1   PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 1   ? 29.863 -20.551 -11.034 1.00 16.96 ? 1   PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 1   ? 31.204 -20.315 -11.659 1.00 15.94 ? 1   PRO A CD  1 
ATOM   8    N  N   . MET A 1 2   ? 29.486 -16.168 -10.340 1.00 13.95 ? 2   MET A N   1 
ATOM   9    C  CA  . MET A 1 2   ? 29.740 -14.904 -9.672  1.00 15.19 ? 2   MET A CA  1 
ATOM   10   C  C   . MET A 1 2   ? 28.751 -14.751 -8.530  1.00 13.48 ? 2   MET A C   1 
ATOM   11   O  O   . MET A 1 2   ? 27.550 -14.962 -8.723  1.00 13.48 ? 2   MET A O   1 
ATOM   12   C  CB  . MET A 1 2   ? 29.497 -13.802 -10.719 1.00 20.50 ? 2   MET A CB  1 
ATOM   13   C  CG  . MET A 1 2   ? 29.501 -12.393 -10.323 1.00 24.97 ? 2   MET A CG  1 
ATOM   14   S  SD  . MET A 1 2   ? 28.998 -11.521 -11.844 1.00 25.62 ? 2   MET A SD  1 
ATOM   15   C  CE  . MET A 1 2   ? 29.969 -12.250 -13.124 1.00 23.45 ? 2   MET A CE  1 
ATOM   16   N  N   . PHE A 1 3   ? 29.245 -14.416 -7.341  1.00 12.16 ? 3   PHE A N   1 
ATOM   17   C  CA  . PHE A 1 3   ? 28.389 -14.153 -6.189  1.00 11.87 ? 3   PHE A CA  1 
ATOM   18   C  C   . PHE A 1 3   ? 28.678 -12.750 -5.686  1.00 11.79 ? 3   PHE A C   1 
ATOM   19   O  O   . PHE A 1 3   ? 29.838 -12.407 -5.440  1.00 12.48 ? 3   PHE A O   1 
ATOM   20   C  CB  . PHE A 1 3   ? 28.628 -15.183 -5.105  1.00 13.13 ? 3   PHE A CB  1 
ATOM   21   C  CG  . PHE A 1 3   ? 27.794 -14.954 -3.884  1.00 13.99 ? 3   PHE A CG  1 
ATOM   22   C  CD1 . PHE A 1 3   ? 26.405 -15.088 -3.942  1.00 14.39 ? 3   PHE A CD1 1 
ATOM   23   C  CD2 . PHE A 1 3   ? 28.384 -14.573 -2.686  1.00 16.51 ? 3   PHE A CD2 1 
ATOM   24   C  CE1 . PHE A 1 3   ? 25.646 -14.863 -2.834  1.00 15.68 ? 3   PHE A CE1 1 
ATOM   25   C  CE2 . PHE A 1 3   ? 27.586 -14.346 -1.577  1.00 17.72 ? 3   PHE A CE2 1 
ATOM   26   C  CZ  . PHE A 1 3   ? 26.213 -14.466 -1.674  1.00 17.36 ? 3   PHE A CZ  1 
ATOM   27   N  N   . ILE A 1 4   ? 27.622 -11.966 -5.507  1.00 11.79 ? 4   ILE A N   1 
ATOM   28   C  CA  . ILE A 1 4   ? 27.739 -10.598 -5.017  1.00 11.97 ? 4   ILE A CA  1 
ATOM   29   C  C   . ILE A 1 4   ? 26.887 -10.477 -3.768  1.00 11.60 ? 4   ILE A C   1 
ATOM   30   O  O   . ILE A 1 4   ? 25.741 -10.925 -3.763  1.00 12.35 ? 4   ILE A O   1 
ATOM   31   C  CB  . ILE A 1 4   ? 27.278 -9.585  -6.089  1.00 14.34 ? 4   ILE A CB  1 
ATOM   32   C  CG1 . ILE A 1 4   ? 28.011 -9.800  -7.436  1.00 16.52 ? 4   ILE A CG1 1 
ATOM   33   C  CG2 . ILE A 1 4   ? 27.471 -8.180  -5.607  1.00 15.49 ? 4   ILE A CG2 1 
ATOM   34   C  CD1 . ILE A 1 4   ? 27.286 -9.197  -8.649  1.00 18.57 ? 4   ILE A CD1 1 
ATOM   35   N  N   . VAL A 1 5   ? 27.415 -9.822  -2.739  1.00 11.99 ? 5   VAL A N   1 
ATOM   36   C  CA  . VAL A 1 5   ? 26.623 -9.497  -1.557  1.00 13.49 ? 5   VAL A CA  1 
ATOM   37   C  C   . VAL A 1 5   ? 26.744 -8.012  -1.281  1.00 12.97 ? 5   VAL A C   1 
ATOM   38   O  O   . VAL A 1 5   ? 27.859 -7.490  -1.170  1.00 13.30 ? 5   VAL A O   1 
ATOM   39   C  CB  . VAL A 1 5   ? 27.016 -10.321 -0.308  1.00 17.45 ? 5   VAL A CB  1 
ATOM   40   C  CG1 . VAL A 1 5   ? 28.438 -10.384 -0.079  1.00 20.44 ? 5   VAL A CG1 1 
ATOM   41   C  CG2 . VAL A 1 5   ? 26.392 -9.758  0.931   1.00 17.90 ? 5   VAL A CG2 1 
ATOM   42   N  N   . ASN A 1 6   ? 25.599 -7.338  -1.197  1.00 11.96 ? 6   ASN A N   1 
ATOM   43   C  CA  . ASN A 1 6   ? 25.514 -5.949  -0.770  1.00 12.46 ? 6   ASN A CA  1 
ATOM   44   C  C   . ASN A 1 6   ? 24.898 -5.921  0.618   1.00 12.46 ? 6   ASN A C   1 
ATOM   45   O  O   . ASN A 1 6   ? 23.871 -6.555  0.848   1.00 13.31 ? 6   ASN A O   1 
ATOM   46   C  CB  . ASN A 1 6   ? 24.659 -5.153  -1.749  1.00 15.02 ? 6   ASN A CB  1 
ATOM   47   C  CG  . ASN A 1 6   ? 25.460 -4.700  -2.948  1.00 19.60 ? 6   ASN A CG  1 
ATOM   48   O  OD1 . ASN A 1 6   ? 26.012 -3.603  -2.950  1.00 20.62 ? 6   ASN A OD1 1 
ATOM   49   N  ND2 . ASN A 1 6   ? 25.507 -5.519  -3.946  1.00 22.79 ? 6   ASN A ND2 1 
ATOM   50   N  N   . THR A 1 7   ? 25.530 -5.204  1.546   1.00 12.76 ? 7   THR A N   1 
ATOM   51   C  CA  . THR A 1 7   ? 25.052 -5.231  2.922   1.00 13.39 ? 7   THR A CA  1 
ATOM   52   C  C   . THR A 1 7   ? 25.308 -3.897  3.587   1.00 13.33 ? 7   THR A C   1 
ATOM   53   O  O   . THR A 1 7   ? 26.238 -3.168  3.222   1.00 13.09 ? 7   THR A O   1 
ATOM   54   C  CB  . THR A 1 7   ? 25.700 -6.398  3.701   1.00 13.54 ? 7   THR A CB  1 
ATOM   55   O  OG1 . THR A 1 7   ? 25.261 -6.393  5.054   1.00 13.92 ? 7   THR A OG1 1 
ATOM   56   C  CG2 . THR A 1 7   ? 27.209 -6.267  3.725   1.00 13.87 ? 7   THR A CG2 1 
ATOM   57   N  N   . ASN A 1 8   ? 24.475 -3.589  4.581   1.00 13.70 ? 8   ASN A N   1 
ATOM   58   C  CA  . ASN A 1 8   ? 24.718 -2.413  5.420   1.00 14.62 ? 8   ASN A CA  1 
ATOM   59   C  C   . ASN A 1 8   ? 25.693 -2.685  6.565   1.00 15.53 ? 8   ASN A C   1 
ATOM   60   O  O   . ASN A 1 8   ? 26.068 -1.747  7.271   1.00 16.93 ? 8   ASN A O   1 
ATOM   61   C  CB  . ASN A 1 8   ? 23.396 -1.858  5.974   1.00 15.26 ? 8   ASN A CB  1 
ATOM   62   C  CG  . ASN A 1 8   ? 22.572 -2.893  6.702   1.00 15.91 ? 8   ASN A CG  1 
ATOM   63   O  OD1 . ASN A 1 8   ? 22.795 -4.091  6.618   1.00 15.91 ? 8   ASN A OD1 1 
ATOM   64   N  ND2 . ASN A 1 8   ? 21.608 -2.405  7.463   1.00 18.00 ? 8   ASN A ND2 1 
ATOM   65   N  N   . VAL A 1 9   ? 26.122 -3.925  6.756   1.00 15.25 ? 9   VAL A N   1 
ATOM   66   C  CA  . VAL A 1 9   ? 27.110 -4.211  7.804   1.00 16.42 ? 9   VAL A CA  1 
ATOM   67   C  C   . VAL A 1 9   ? 28.406 -3.461  7.483   1.00 16.70 ? 9   VAL A C   1 
ATOM   68   O  O   . VAL A 1 9   ? 28.787 -3.346  6.295   1.00 16.84 ? 9   VAL A O   1 
ATOM   69   C  CB  . VAL A 1 9   ? 27.339 -5.739  7.874   1.00 18.69 ? 9   VAL A CB  1 
ATOM   70   C  CG1 . VAL A 1 9   ? 28.601 -6.092  8.701   1.00 20.98 ? 9   VAL A CG1 1 
ATOM   71   C  CG2 . VAL A 1 9   ? 26.070 -6.432  8.386   1.00 19.15 ? 9   VAL A CG2 1 
ATOM   72   N  N   . PRO A 1 10  ? 29.091 -2.879  8.461   1.00 17.96 ? 10  PRO A N   1 
ATOM   73   C  CA  . PRO A 1 10  ? 30.285 -2.088  8.149   1.00 18.71 ? 10  PRO A CA  1 
ATOM   74   C  C   . PRO A 1 10  ? 31.459 -2.969  7.762   1.00 17.82 ? 10  PRO A C   1 
ATOM   75   O  O   . PRO A 1 10  ? 31.530 -4.157  8.097   1.00 17.36 ? 10  PRO A O   1 
ATOM   76   C  CB  . PRO A 1 10  ? 30.573 -1.340  9.453   1.00 20.44 ? 10  PRO A CB  1 
ATOM   77   C  CG  . PRO A 1 10  ? 29.889 -2.111  10.500  1.00 21.11 ? 10  PRO A CG  1 
ATOM   78   C  CD  . PRO A 1 10  ? 28.728 -2.811  9.888   1.00 19.83 ? 10  PRO A CD  1 
ATOM   79   N  N   . ARG A 1 11  ? 32.393 -2.361  7.021   1.00 18.53 ? 11  ARG A N   1 
ATOM   80   C  CA  . ARG A 1 11  ? 33.525 -3.125  6.512   1.00 20.14 ? 11  ARG A CA  1 
ATOM   81   C  C   . ARG A 1 11  ? 34.308 -3.798  7.628   1.00 20.46 ? 11  ARG A C   1 
ATOM   82   O  O   . ARG A 1 11  ? 34.807 -4.923  7.459   1.00 21.11 ? 11  ARG A O   1 
ATOM   83   C  CB  . ARG A 1 11  ? 34.439 -2.223  5.687   1.00 22.46 ? 11  ARG A CB  1 
ATOM   84   C  CG  . ARG A 1 11  ? 35.805 -2.866  5.353   1.00 26.62 ? 11  ARG A CG  1 
ATOM   85   C  CD  . ARG A 1 11  ? 35.703 -4.028  4.353   1.00 30.26 ? 11  ARG A CD  1 
ATOM   86   N  NE  . ARG A 1 11  ? 36.982 -4.679  4.020   1.00 32.88 ? 11  ARG A NE  1 
ATOM   87   C  CZ  . ARG A 1 11  ? 37.465 -5.755  4.641   1.00 34.68 ? 11  ARG A CZ  1 
ATOM   88   N  NH1 . ARG A 1 11  ? 36.787 -6.304  5.645   1.00 35.51 ? 11  ARG A NH1 1 
ATOM   89   N  NH2 . ARG A 1 11  ? 38.616 -6.295  4.255   1.00 35.56 ? 11  ARG A NH2 1 
ATOM   90   N  N   . ALA A 1 12  ? 34.443 -3.126  8.770   1.00 20.86 ? 12  ALA A N   1 
ATOM   91   C  CA  . ALA A 1 12  ? 35.250 -3.685  9.842   1.00 22.74 ? 12  ALA A CA  1 
ATOM   92   C  C   . ALA A 1 12  ? 34.632 -4.938  10.433  1.00 22.63 ? 12  ALA A C   1 
ATOM   93   O  O   . ALA A 1 12  ? 35.324 -5.678  11.140  1.00 24.22 ? 12  ALA A O   1 
ATOM   94   C  CB  . ALA A 1 12  ? 35.461 -2.637  10.928  1.00 24.07 ? 12  ALA A CB  1 
ATOM   95   N  N   . SER A 1 13  ? 33.348 -5.175  10.183  1.00 21.43 ? 13  SER A N   1 
ATOM   96   C  CA  . SER A 1 13  ? 32.691 -6.373  10.652  1.00 22.15 ? 13  SER A CA  1 
ATOM   97   C  C   . SER A 1 13  ? 32.728 -7.509  9.632   1.00 21.54 ? 13  SER A C   1 
ATOM   98   O  O   . SER A 1 13  ? 32.175 -8.573  9.900   1.00 22.97 ? 13  SER A O   1 
ATOM   99   C  CB  . SER A 1 13  ? 31.253 -6.045  11.047  1.00 24.55 ? 13  SER A CB  1 
ATOM   100  O  OG  . SER A 1 13  ? 31.227 -5.141  12.166  1.00 26.69 ? 13  SER A OG  1 
ATOM   101  N  N   . VAL A 1 14  ? 33.353 -7.328  8.473   1.00 19.43 ? 14  VAL A N   1 
ATOM   102  C  CA  . VAL A 1 14  ? 33.562 -8.418  7.523   1.00 19.08 ? 14  VAL A CA  1 
ATOM   103  C  C   . VAL A 1 14  ? 34.872 -9.103  7.922   1.00 19.20 ? 14  VAL A C   1 
ATOM   104  O  O   . VAL A 1 14  ? 35.931 -8.462  7.841   1.00 20.99 ? 14  VAL A O   1 
ATOM   105  C  CB  . VAL A 1 14  ? 33.646 -7.894  6.086   1.00 19.31 ? 14  VAL A CB  1 
ATOM   106  C  CG1 . VAL A 1 14  ? 33.891 -9.040  5.115   1.00 19.71 ? 14  VAL A CG1 1 
ATOM   107  C  CG2 . VAL A 1 14  ? 32.363 -7.140  5.707   1.00 19.68 ? 14  VAL A CG2 1 
ATOM   108  N  N   . PRO A 1 15  ? 34.845 -10.360 8.357   1.00 18.45 ? 15  PRO A N   1 
ATOM   109  C  CA  . PRO A 1 15  ? 36.067 -10.967 8.919   1.00 19.32 ? 15  PRO A CA  1 
ATOM   110  C  C   . PRO A 1 15  ? 37.094 -11.266 7.846   1.00 18.56 ? 15  PRO A C   1 
ATOM   111  O  O   . PRO A 1 15  ? 36.780 -11.422 6.666   1.00 18.29 ? 15  PRO A O   1 
ATOM   112  C  CB  . PRO A 1 15  ? 35.562 -12.262 9.560   1.00 20.22 ? 15  PRO A CB  1 
ATOM   113  C  CG  . PRO A 1 15  ? 34.315 -12.574 8.832   1.00 20.61 ? 15  PRO A CG  1 
ATOM   114  C  CD  . PRO A 1 15  ? 33.690 -11.269 8.395   1.00 19.50 ? 15  PRO A CD  1 
ATOM   115  N  N   . ASP A 1 16  ? 38.350 -11.346 8.278   1.00 18.80 ? 16  ASP A N   1 
ATOM   116  C  CA  . ASP A 1 16  ? 39.407 -11.850 7.406   1.00 18.66 ? 16  ASP A CA  1 
ATOM   117  C  C   . ASP A 1 16  ? 39.011 -13.201 6.856   1.00 19.02 ? 16  ASP A C   1 
ATOM   118  O  O   . ASP A 1 16  ? 38.424 -14.027 7.559   1.00 20.67 ? 16  ASP A O   1 
ATOM   119  C  CB  . ASP A 1 16  ? 40.688 -12.115 8.201   1.00 19.51 ? 16  ASP A CB  1 
ATOM   120  C  CG  . ASP A 1 16  ? 41.425 -10.874 8.569   1.00 20.95 ? 16  ASP A CG  1 
ATOM   121  O  OD1 . ASP A 1 16  ? 41.002 -9.768  8.173   1.00 22.21 ? 16  ASP A OD1 1 
ATOM   122  O  OD2 . ASP A 1 16  ? 42.473 -11.015 9.246   1.00 20.77 ? 16  ASP A OD2 1 
ATOM   123  N  N   . GLY A 1 17  ? 39.322 -13.420 5.593   1.00 17.57 ? 17  GLY A N   1 
ATOM   124  C  CA  . GLY A 1 17  ? 39.071 -14.709 4.992   1.00 16.82 ? 17  GLY A CA  1 
ATOM   125  C  C   . GLY A 1 17  ? 37.693 -14.903 4.423   1.00 16.12 ? 17  GLY A C   1 
ATOM   126  O  O   . GLY A 1 17  ? 37.410 -15.984 3.892   1.00 16.78 ? 17  GLY A O   1 
ATOM   127  N  N   . PHE A 1 18  ? 36.845 -13.873 4.474   1.00 15.34 ? 18  PHE A N   1 
ATOM   128  C  CA  . PHE A 1 18  ? 35.459 -14.054 4.048   1.00 15.48 ? 18  PHE A CA  1 
ATOM   129  C  C   . PHE A 1 18  ? 35.346 -14.335 2.551   1.00 14.76 ? 18  PHE A C   1 
ATOM   130  O  O   . PHE A 1 18  ? 34.605 -15.228 2.146   1.00 14.85 ? 18  PHE A O   1 
ATOM   131  C  CB  . PHE A 1 18  ? 34.643 -12.832 4.457   1.00 17.04 ? 18  PHE A CB  1 
ATOM   132  C  CG  . PHE A 1 18  ? 33.164 -12.999 4.247   1.00 18.56 ? 18  PHE A CG  1 
ATOM   133  C  CD1 . PHE A 1 18  ? 32.478 -14.049 4.854   1.00 20.09 ? 18  PHE A CD1 1 
ATOM   134  C  CD2 . PHE A 1 18  ? 32.469 -12.099 3.470   1.00 18.97 ? 18  PHE A CD2 1 
ATOM   135  C  CE1 . PHE A 1 18  ? 31.105 -14.181 4.690   1.00 21.13 ? 18  PHE A CE1 1 
ATOM   136  C  CE2 . PHE A 1 18  ? 31.095 -12.226 3.311   1.00 19.73 ? 18  PHE A CE2 1 
ATOM   137  C  CZ  . PHE A 1 18  ? 30.435 -13.287 3.898   1.00 20.51 ? 18  PHE A CZ  1 
ATOM   138  N  N   . LEU A 1 19  ? 36.058 -13.577 1.711   1.00 14.31 ? 19  LEU A N   1 
ATOM   139  C  CA  . LEU A 1 19  ? 35.973 -13.835 0.271   1.00 14.92 ? 19  LEU A CA  1 
ATOM   140  C  C   . LEU A 1 19  ? 36.474 -15.234 -0.062  1.00 14.43 ? 19  LEU A C   1 
ATOM   141  O  O   . LEU A 1 19  ? 35.904 -15.917 -0.931  1.00 14.83 ? 19  LEU A O   1 
ATOM   142  C  CB  . LEU A 1 19  ? 36.809 -12.831 -0.519  1.00 17.09 ? 19  LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 19  ? 36.349 -11.395 -0.523  1.00 18.86 ? 19  LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 19  ? 37.307 -10.571 -1.371  1.00 19.92 ? 19  LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 19  ? 34.957 -11.293 -1.091  1.00 20.27 ? 19  LEU A CD2 1 
ATOM   146  N  N   . SER A 1 20  ? 37.536 -15.692 0.630   1.00 15.28 ? 20  SER A N   1 
ATOM   147  C  CA  . SER A 1 20  ? 38.039 -17.040 0.381   1.00 17.27 ? 20  SER A CA  1 
ATOM   148  C  C   . SER A 1 20  ? 37.040 -18.104 0.809   1.00 16.90 ? 20  SER A C   1 
ATOM   149  O  O   . SER A 1 20  ? 36.835 -19.098 0.096   1.00 17.43 ? 20  SER A O   1 
ATOM   150  C  CB  . SER A 1 20  ? 39.345 -17.256 1.125   1.00 19.48 ? 20  SER A CB  1 
ATOM   151  O  OG  . SER A 1 20  ? 39.754 -18.609 0.931   1.00 22.44 ? 20  SER A OG  1 
ATOM   152  N  N   . GLU A 1 21  ? 36.384 -17.902 1.952   1.00 17.30 ? 21  GLU A N   1 
ATOM   153  C  CA  . GLU A 1 21  ? 35.384 -18.865 2.384   1.00 17.95 ? 21  GLU A CA  1 
ATOM   154  C  C   . GLU A 1 21  ? 34.247 -18.944 1.385   1.00 16.43 ? 21  GLU A C   1 
ATOM   155  O  O   . GLU A 1 21  ? 33.808 -20.038 1.021   1.00 16.63 ? 21  GLU A O   1 
ATOM   156  C  CB  . GLU A 1 21  ? 34.862 -18.505 3.765   1.00 20.15 ? 21  GLU A CB  1 
ATOM   157  C  CG  . GLU A 1 21  ? 34.013 -19.577 4.356   1.00 23.24 ? 21  GLU A CG  1 
ATOM   158  C  CD  . GLU A 1 21  ? 33.598 -19.238 5.761   1.00 26.57 ? 21  GLU A CD  1 
ATOM   159  O  OE1 . GLU A 1 21  ? 33.625 -18.034 6.118   1.00 27.86 ? 21  GLU A OE1 1 
ATOM   160  O  OE2 . GLU A 1 21  ? 33.278 -20.184 6.511   1.00 28.22 ? 21  GLU A OE2 1 
ATOM   161  N  N   . LEU A 1 22  ? 33.773 -17.793 0.907   1.00 15.34 ? 22  LEU A N   1 
ATOM   162  C  CA  . LEU A 1 22  ? 32.722 -17.801 -0.104  1.00 15.02 ? 22  LEU A CA  1 
ATOM   163  C  C   . LEU A 1 22  ? 33.177 -18.525 -1.356  1.00 14.89 ? 22  LEU A C   1 
ATOM   164  O  O   . LEU A 1 22  ? 32.425 -19.315 -1.926  1.00 15.28 ? 22  LEU A O   1 
ATOM   165  C  CB  . LEU A 1 22  ? 32.330 -16.358 -0.450  1.00 15.77 ? 22  LEU A CB  1 
ATOM   166  C  CG  . LEU A 1 22  ? 31.489 -15.654 0.615   1.00 16.16 ? 22  LEU A CG  1 
ATOM   167  C  CD1 . LEU A 1 22  ? 31.363 -14.183 0.211   1.00 16.17 ? 22  LEU A CD1 1 
ATOM   168  C  CD2 . LEU A 1 22  ? 30.113 -16.313 0.727   1.00 17.34 ? 22  LEU A CD2 1 
ATOM   169  N  N   . THR A 1 23  ? 34.403 -18.243 -1.818  1.00 14.44 ? 23  THR A N   1 
ATOM   170  C  CA  . THR A 1 23  ? 34.913 -18.872 -3.037  1.00 14.52 ? 23  THR A CA  1 
ATOM   171  C  C   . THR A 1 23  ? 34.912 -20.382 -2.896  1.00 14.90 ? 23  THR A C   1 
ATOM   172  O  O   . THR A 1 23  ? 34.437 -21.107 -3.786  1.00 15.00 ? 23  THR A O   1 
ATOM   173  C  CB  . THR A 1 23  ? 36.332 -18.378 -3.307  1.00 14.62 ? 23  THR A CB  1 
ATOM   174  O  OG1 . THR A 1 23  ? 36.317 -16.963 -3.552  1.00 13.87 ? 23  THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 23  ? 36.954 -19.065 -4.527  1.00 15.33 ? 23  THR A CG2 1 
ATOM   176  N  N   . GLN A 1 24  ? 35.460 -20.875 -1.777  1.00 15.71 ? 24  GLN A N   1 
ATOM   177  C  CA  . GLN A 1 24  ? 35.591 -22.310 -1.614  1.00 18.08 ? 24  GLN A CA  1 
ATOM   178  C  C   . GLN A 1 24  ? 34.244 -22.959 -1.425  1.00 16.49 ? 24  GLN A C   1 
ATOM   179  O  O   . GLN A 1 24  ? 34.005 -24.036 -1.969  1.00 16.25 ? 24  GLN A O   1 
ATOM   180  C  CB  . GLN A 1 24  ? 36.479 -22.620 -0.415  1.00 25.95 ? 24  GLN A CB  1 
ATOM   181  C  CG  . GLN A 1 24  ? 37.840 -22.079 -0.606  1.00 29.02 ? 24  GLN A CG  1 
ATOM   182  C  CD  . GLN A 1 24  ? 38.769 -22.440 0.516   1.00 29.81 ? 24  GLN A CD  1 
ATOM   183  O  OE1 . GLN A 1 24  ? 38.353 -23.007 1.517   1.00 30.22 ? 24  GLN A OE1 1 
ATOM   184  N  NE2 . GLN A 1 24  ? 40.023 -22.018 0.393   1.00 30.19 ? 24  GLN A NE2 1 
ATOM   185  N  N   . GLN A 1 25  ? 33.374 -22.358 -0.615  1.00 16.51 ? 25  GLN A N   1 
ATOM   186  C  CA  . GLN A 1 25  ? 32.074 -22.971 -0.401  1.00 17.56 ? 25  GLN A CA  1 
ATOM   187  C  C   . GLN A 1 25  ? 31.222 -22.962 -1.665  1.00 16.37 ? 25  GLN A C   1 
ATOM   188  O  O   . GLN A 1 25  ? 30.496 -23.929 -1.923  1.00 16.36 ? 25  GLN A O   1 
ATOM   189  C  CB  . GLN A 1 25  ? 31.363 -22.298 0.766   1.00 19.78 ? 25  GLN A CB  1 
ATOM   190  C  CG  . GLN A 1 25  ? 32.075 -22.526 2.095   1.00 23.53 ? 25  GLN A CG  1 
ATOM   191  C  CD  . GLN A 1 25  ? 32.078 -23.987 2.466   1.00 28.32 ? 25  GLN A CD  1 
ATOM   192  O  OE1 . GLN A 1 25  ? 31.008 -24.575 2.627   1.00 31.06 ? 25  GLN A OE1 1 
ATOM   193  N  NE2 . GLN A 1 25  ? 33.284 -24.601 2.589   1.00 29.30 ? 25  GLN A NE2 1 
ATOM   194  N  N   . LEU A 1 26  ? 31.320 -21.902 -2.479  1.00 15.08 ? 26  LEU A N   1 
ATOM   195  C  CA  . LEU A 1 26  ? 30.567 -21.879 -3.737  1.00 15.37 ? 26  LEU A CA  1 
ATOM   196  C  C   . LEU A 1 26  ? 31.139 -22.860 -4.758  1.00 16.13 ? 26  LEU A C   1 
ATOM   197  O  O   . LEU A 1 26  ? 30.388 -23.434 -5.555  1.00 16.70 ? 26  LEU A O   1 
ATOM   198  C  CB  . LEU A 1 26  ? 30.541 -20.481 -4.325  1.00 15.98 ? 26  LEU A CB  1 
ATOM   199  C  CG  . LEU A 1 26  ? 29.565 -19.621 -3.556  1.00 17.40 ? 26  LEU A CG  1 
ATOM   200  C  CD1 . LEU A 1 26  ? 29.855 -18.162 -3.872  1.00 19.02 ? 26  LEU A CD1 1 
ATOM   201  C  CD2 . LEU A 1 26  ? 28.151 -20.028 -3.928  1.00 18.34 ? 26  LEU A CD2 1 
ATOM   202  N  N   . ALA A 1 27  ? 32.461 -23.049 -4.777  1.00 16.93 ? 27  ALA A N   1 
ATOM   203  C  CA  . ALA A 1 27  ? 33.027 -24.068 -5.657  1.00 18.26 ? 27  ALA A CA  1 
ATOM   204  C  C   . ALA A 1 27  ? 32.436 -25.427 -5.323  1.00 19.69 ? 27  ALA A C   1 
ATOM   205  O  O   . ALA A 1 27  ? 32.030 -26.196 -6.205  1.00 20.45 ? 27  ALA A O   1 
ATOM   206  C  CB  . ALA A 1 27  ? 34.548 -24.085 -5.484  1.00 18.11 ? 27  ALA A CB  1 
ATOM   207  N  N   . GLN A 1 28  ? 32.360 -25.731 -4.037  1.00 20.23 ? 28  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 28  ? 31.815 -27.021 -3.633  1.00 22.17 ? 28  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 28  ? 30.335 -27.138 -3.969  1.00 21.74 ? 28  GLN A C   1 
ATOM   210  O  O   . GLN A 1 28  ? 29.880 -28.186 -4.451  1.00 22.80 ? 28  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 28  ? 32.094 -27.245 -2.151  1.00 26.18 ? 28  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 28  ? 33.549 -27.572 -1.930  1.00 31.24 ? 28  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 28  ? 33.843 -29.009 -2.349  1.00 35.66 ? 28  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 28  ? 33.491 -29.929 -1.628  1.00 38.16 ? 28  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 28  ? 34.425 -29.206 -3.540  1.00 36.63 ? 28  GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 29  ? 29.572 -26.078 -3.694  1.00 19.83 ? 29  ALA A N   1 
ATOM   217  C  CA  . ALA A 1 29  ? 28.128 -26.116 -3.868  1.00 19.10 ? 29  ALA A CA  1 
ATOM   218  C  C   . ALA A 1 29  ? 27.741 -26.183 -5.339  1.00 19.08 ? 29  ALA A C   1 
ATOM   219  O  O   . ALA A 1 29  ? 26.851 -26.945 -5.705  1.00 20.00 ? 29  ALA A O   1 
ATOM   220  C  CB  . ALA A 1 29  ? 27.498 -24.894 -3.203  1.00 18.05 ? 29  ALA A CB  1 
ATOM   221  N  N   . THR A 1 30  ? 28.389 -25.394 -6.193  1.00 18.41 ? 30  THR A N   1 
ATOM   222  C  CA  . THR A 1 30  ? 28.040 -25.385 -7.607  1.00 18.92 ? 30  THR A CA  1 
ATOM   223  C  C   . THR A 1 30  ? 28.698 -26.514 -8.377  1.00 19.52 ? 30  THR A C   1 
ATOM   224  O  O   . THR A 1 30  ? 28.292 -26.787 -9.514  1.00 20.00 ? 30  THR A O   1 
ATOM   225  C  CB  . THR A 1 30  ? 28.454 -24.059 -8.266  1.00 18.84 ? 30  THR A CB  1 
ATOM   226  O  OG1 . THR A 1 30  ? 29.889 -23.937 -8.232  1.00 17.80 ? 30  THR A OG1 1 
ATOM   227  C  CG2 . THR A 1 30  ? 27.803 -22.878 -7.577  1.00 20.07 ? 30  THR A CG2 1 
ATOM   228  N  N   . GLY A 1 31  ? 29.704 -27.164 -7.807  1.00 18.82 ? 31  GLY A N   1 
ATOM   229  C  CA  . GLY A 1 31  ? 30.429 -28.157 -8.554  1.00 19.75 ? 31  GLY A CA  1 
ATOM   230  C  C   . GLY A 1 31  ? 31.426 -27.599 -9.539  1.00 20.85 ? 31  GLY A C   1 
ATOM   231  O  O   . GLY A 1 31  ? 32.072 -28.381 -10.248 1.00 22.34 ? 31  GLY A O   1 
ATOM   232  N  N   . LYS A 1 32  ? 31.562 -26.281 -9.622  1.00 21.14 ? 32  LYS A N   1 
ATOM   233  C  CA  . LYS A 1 32  ? 32.470 -25.652 -10.566 1.00 21.65 ? 32  LYS A CA  1 
ATOM   234  C  C   . LYS A 1 32  ? 33.833 -25.497 -9.911  1.00 20.40 ? 32  LYS A C   1 
ATOM   235  O  O   . LYS A 1 32  ? 33.938 -25.296 -8.697  1.00 19.73 ? 32  LYS A O   1 
ATOM   236  C  CB  . LYS A 1 32  ? 31.962 -24.262 -10.942 1.00 23.69 ? 32  LYS A CB  1 
ATOM   237  C  CG  . LYS A 1 32  ? 30.499 -24.163 -11.390 1.00 25.72 ? 32  LYS A CG  1 
ATOM   238  C  CD  . LYS A 1 32  ? 30.344 -24.286 -12.843 1.00 26.02 ? 32  LYS A CD  1 
ATOM   239  C  CE  . LYS A 1 32  ? 28.942 -23.902 -13.310 1.00 26.03 ? 32  LYS A CE  1 
ATOM   240  N  NZ  . LYS A 1 32  ? 28.864 -24.047 -14.774 1.00 26.49 ? 32  LYS A NZ  1 
ATOM   241  N  N   . PRO A 1 33  ? 34.908 -25.511 -10.669 1.00 20.43 ? 33  PRO A N   1 
ATOM   242  C  CA  . PRO A 1 33  ? 36.248 -25.336 -10.067 1.00 19.83 ? 33  PRO A CA  1 
ATOM   243  C  C   . PRO A 1 33  ? 36.377 -23.956 -9.432  1.00 16.93 ? 33  PRO A C   1 
ATOM   244  O  O   . PRO A 1 33  ? 35.856 -22.967 -9.969  1.00 16.40 ? 33  PRO A O   1 
ATOM   245  C  CB  . PRO A 1 33  ? 37.190 -25.468 -11.272 1.00 22.71 ? 33  PRO A CB  1 
ATOM   246  C  CG  . PRO A 1 33  ? 36.356 -26.151 -12.361 1.00 23.61 ? 33  PRO A CG  1 
ATOM   247  C  CD  . PRO A 1 33  ? 34.948 -25.705 -12.129 1.00 22.60 ? 33  PRO A CD  1 
ATOM   248  N  N   . PRO A 1 34  ? 37.079 -23.837 -8.301  1.00 16.07 ? 34  PRO A N   1 
ATOM   249  C  CA  . PRO A 1 34  ? 37.214 -22.510 -7.655  1.00 15.63 ? 34  PRO A CA  1 
ATOM   250  C  C   . PRO A 1 34  ? 37.857 -21.450 -8.539  1.00 14.33 ? 34  PRO A C   1 
ATOM   251  O  O   . PRO A 1 34  ? 37.595 -20.263 -8.352  1.00 13.88 ? 34  PRO A O   1 
ATOM   252  C  CB  . PRO A 1 34  ? 38.060 -22.781 -6.404  1.00 17.42 ? 34  PRO A CB  1 
ATOM   253  C  CG  . PRO A 1 34  ? 38.625 -24.195 -6.588  1.00 18.24 ? 34  PRO A CG  1 
ATOM   254  C  CD  . PRO A 1 34  ? 37.744 -24.930 -7.558  1.00 17.12 ? 34  PRO A CD  1 
ATOM   255  N  N   . GLN A 1 35  ? 38.728 -21.836 -9.470  1.00 14.30 ? 35  GLN A N   1 
ATOM   256  C  CA  . GLN A 1 35  ? 39.322 -20.902 -10.407 1.00 14.98 ? 35  GLN A CA  1 
ATOM   257  C  C   . GLN A 1 35  ? 38.263 -20.097 -11.145 1.00 13.97 ? 35  GLN A C   1 
ATOM   258  O  O   . GLN A 1 35  ? 38.540 -18.987 -11.616 1.00 14.54 ? 35  GLN A O   1 
ATOM   259  C  CB  . GLN A 1 35  ? 40.193 -21.692 -11.388 1.00 16.47 ? 35  GLN A CB  1 
ATOM   260  C  CG  . GLN A 1 35  ? 41.483 -22.321 -10.778 1.00 18.64 ? 35  GLN A CG  1 
ATOM   261  C  CD  . GLN A 1 35  ? 41.299 -23.769 -10.188 1.00 20.02 ? 35  GLN A CD  1 
ATOM   262  O  OE1 . GLN A 1 35  ? 40.175 -24.300 -9.957  1.00 19.59 ? 35  GLN A OE1 1 
ATOM   263  N  NE2 . GLN A 1 35  ? 42.429 -24.442 -10.019 1.00 20.74 ? 35  GLN A NE2 1 
ATOM   264  N  N   . TYR A 1 36  ? 37.058 -20.644 -11.277 1.00 13.36 ? 36  TYR A N   1 
ATOM   265  C  CA  . TYR A 1 36  ? 35.988 -20.003 -12.034 1.00 14.27 ? 36  TYR A CA  1 
ATOM   266  C  C   . TYR A 1 36  ? 35.022 -19.194 -11.177 1.00 14.09 ? 36  TYR A C   1 
ATOM   267  O  O   . TYR A 1 36  ? 34.091 -18.572 -11.725 1.00 14.64 ? 36  TYR A O   1 
ATOM   268  C  CB  . TYR A 1 36  ? 35.153 -21.074 -12.742 1.00 16.14 ? 36  TYR A CB  1 
ATOM   269  C  CG  . TYR A 1 36  ? 35.857 -21.783 -13.859 1.00 18.93 ? 36  TYR A CG  1 
ATOM   270  C  CD1 . TYR A 1 36  ? 36.737 -22.818 -13.609 1.00 21.14 ? 36  TYR A CD1 1 
ATOM   271  C  CD2 . TYR A 1 36  ? 35.623 -21.438 -15.169 1.00 21.13 ? 36  TYR A CD2 1 
ATOM   272  C  CE1 . TYR A 1 36  ? 37.376 -23.480 -14.632 1.00 22.41 ? 36  TYR A CE1 1 
ATOM   273  C  CE2 . TYR A 1 36  ? 36.252 -22.111 -16.208 1.00 22.41 ? 36  TYR A CE2 1 
ATOM   274  C  CZ  . TYR A 1 36  ? 37.144 -23.114 -15.919 1.00 22.78 ? 36  TYR A CZ  1 
ATOM   275  O  OH  . TYR A 1 36  ? 37.777 -23.805 -16.934 1.00 24.04 ? 36  TYR A OH  1 
ATOM   276  N  N   . ILE A 1 37  ? 35.224 -19.160 -9.865  1.00 12.95 ? 37  ILE A N   1 
ATOM   277  C  CA  . ILE A 1 37  ? 34.290 -18.495 -8.954  1.00 12.80 ? 37  ILE A CA  1 
ATOM   278  C  C   . ILE A 1 37  ? 34.792 -17.099 -8.669  1.00 12.24 ? 37  ILE A C   1 
ATOM   279  O  O   . ILE A 1 37  ? 35.940 -16.936 -8.241  1.00 12.69 ? 37  ILE A O   1 
ATOM   280  C  CB  . ILE A 1 37  ? 34.184 -19.268 -7.632  1.00 14.39 ? 37  ILE A CB  1 
ATOM   281  C  CG1 . ILE A 1 37  ? 33.696 -20.714 -7.870  1.00 16.22 ? 37  ILE A CG1 1 
ATOM   282  C  CG2 . ILE A 1 37  ? 33.290 -18.497 -6.658  1.00 15.41 ? 37  ILE A CG2 1 
ATOM   283  C  CD1 . ILE A 1 37  ? 32.240 -20.836 -8.190  1.00 18.24 ? 37  ILE A CD1 1 
ATOM   284  N  N   . ALA A 1 38  ? 33.953 -16.095 -8.898  1.00 11.46 ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 38  ? 34.271 -14.721 -8.551  1.00 11.16 ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 38  ? 33.315 -14.290 -7.453  1.00 11.56 ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 38  ? 32.132 -14.628 -7.482  1.00 12.51 ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 38  ? 34.151 -13.773 -9.745  1.00 12.41 ? 38  ALA A CB  1 
ATOM   289  N  N   . VAL A 1 39  ? 33.808 -13.488 -6.501  1.00 11.74 ? 39  VAL A N   1 
ATOM   290  C  CA  . VAL A 1 39  ? 33.015 -13.052 -5.359  1.00 12.20 ? 39  VAL A CA  1 
ATOM   291  C  C   . VAL A 1 39  ? 33.243 -11.568 -5.131  1.00 11.96 ? 39  VAL A C   1 
ATOM   292  O  O   . VAL A 1 39  ? 34.356 -11.055 -5.313  1.00 12.62 ? 39  VAL A O   1 
ATOM   293  C  CB  . VAL A 1 39  ? 33.327 -13.867 -4.083  1.00 13.78 ? 39  VAL A CB  1 
ATOM   294  C  CG1 . VAL A 1 39  ? 32.987 -15.335 -4.271  1.00 14.39 ? 39  VAL A CG1 1 
ATOM   295  C  CG2 . VAL A 1 39  ? 34.758 -13.735 -3.677  1.00 16.39 ? 39  VAL A CG2 1 
ATOM   296  N  N   . HIS A 1 40  ? 32.199 -10.889 -4.674  1.00 12.19 ? 40  HIS A N   1 
ATOM   297  C  CA  . HIS A 1 40  ? 32.270 -9.449  -4.472  1.00 11.93 ? 40  HIS A CA  1 
ATOM   298  C  C   . HIS A 1 40  ? 31.408 -9.128  -3.256  1.00 11.97 ? 40  HIS A C   1 
ATOM   299  O  O   . HIS A 1 40  ? 30.233 -9.493  -3.215  1.00 12.71 ? 40  HIS A O   1 
ATOM   300  C  CB  . HIS A 1 40  ? 31.711 -8.800  -5.734  1.00 12.78 ? 40  HIS A CB  1 
ATOM   301  C  CG  . HIS A 1 40  ? 31.664 -7.305  -5.729  1.00 13.20 ? 40  HIS A CG  1 
ATOM   302  N  ND1 . HIS A 1 40  ? 30.956 -6.603  -6.685  1.00 14.05 ? 40  HIS A ND1 1 
ATOM   303  C  CD2 . HIS A 1 40  ? 32.204 -6.373  -4.904  1.00 14.08 ? 40  HIS A CD2 1 
ATOM   304  C  CE1 . HIS A 1 40  ? 31.063 -5.305  -6.449  1.00 14.21 ? 40  HIS A CE1 1 
ATOM   305  N  NE2 . HIS A 1 40  ? 31.831 -5.140  -5.381  1.00 14.32 ? 40  HIS A NE2 1 
ATOM   306  N  N   . VAL A 1 41  ? 31.989 -8.482  -2.255  1.00 11.89 ? 41  VAL A N   1 
ATOM   307  C  CA  . VAL A 1 41  ? 31.280 -8.112  -1.032  1.00 13.05 ? 41  VAL A CA  1 
ATOM   308  C  C   . VAL A 1 41  ? 31.301 -6.597  -0.919  1.00 12.66 ? 41  VAL A C   1 
ATOM   309  O  O   . VAL A 1 41  ? 32.369 -5.992  -1.032  1.00 13.42 ? 41  VAL A O   1 
ATOM   310  C  CB  . VAL A 1 41  ? 31.924 -8.773  0.198   1.00 15.24 ? 41  VAL A CB  1 
ATOM   311  C  CG1 . VAL A 1 41  ? 31.261 -8.290  1.501   1.00 16.37 ? 41  VAL A CG1 1 
ATOM   312  C  CG2 . VAL A 1 41  ? 31.810 -10.276 0.037   1.00 16.82 ? 41  VAL A CG2 1 
ATOM   313  N  N   . VAL A 1 42  ? 30.140 -6.000  -0.689  1.00 12.58 ? 42  VAL A N   1 
ATOM   314  C  CA  . VAL A 1 42  ? 29.979 -4.551  -0.668  1.00 13.09 ? 42  VAL A CA  1 
ATOM   315  C  C   . VAL A 1 42  ? 29.382 -4.152  0.680   1.00 12.64 ? 42  VAL A C   1 
ATOM   316  O  O   . VAL A 1 42  ? 28.172 -4.235  0.880   1.00 13.25 ? 42  VAL A O   1 
ATOM   317  C  CB  . VAL A 1 42  ? 29.089 -4.053  -1.819  1.00 13.77 ? 42  VAL A CB  1 
ATOM   318  C  CG1 . VAL A 1 42  ? 29.229 -2.545  -1.907  1.00 15.40 ? 42  VAL A CG1 1 
ATOM   319  C  CG2 . VAL A 1 42  ? 29.502 -4.692  -3.133  1.00 14.76 ? 42  VAL A CG2 1 
ATOM   320  N  N   . PRO A 1 43  ? 30.221 -3.746  1.639   1.00 14.24 ? 43  PRO A N   1 
ATOM   321  C  CA  . PRO A 1 43  ? 29.726 -3.370  2.967   1.00 14.42 ? 43  PRO A CA  1 
ATOM   322  C  C   . PRO A 1 43  ? 29.336 -1.903  3.007   1.00 14.05 ? 43  PRO A C   1 
ATOM   323  O  O   . PRO A 1 43  ? 29.436 -1.160  2.017   1.00 13.95 ? 43  PRO A O   1 
ATOM   324  C  CB  . PRO A 1 43  ? 30.926 -3.655  3.874   1.00 16.18 ? 43  PRO A CB  1 
ATOM   325  C  CG  . PRO A 1 43  ? 32.106 -3.414  2.980   1.00 17.25 ? 43  PRO A CG  1 
ATOM   326  C  CD  . PRO A 1 43  ? 31.690 -3.814  1.574   1.00 15.60 ? 43  PRO A CD  1 
ATOM   327  N  N   . ASP A 1 44  ? 28.825 -1.483  4.165   1.00 14.60 ? 44  ASP A N   1 
ATOM   328  C  CA  . ASP A 1 44  ? 28.569 -0.073  4.453   1.00 15.54 ? 44  ASP A CA  1 
ATOM   329  C  C   . ASP A 1 44  ? 27.510 0.541   3.559   1.00 14.79 ? 44  ASP A C   1 
ATOM   330  O  O   . ASP A 1 44  ? 27.500 1.772   3.377   1.00 15.98 ? 44  ASP A O   1 
ATOM   331  C  CB  . ASP A 1 44  ? 29.840 0.774   4.385   1.00 18.86 ? 44  ASP A CB  1 
ATOM   332  C  CG  . ASP A 1 44  ? 30.793 0.450   5.480   1.00 24.00 ? 44  ASP A CG  1 
ATOM   333  O  OD1 . ASP A 1 44  ? 30.449 0.692   6.650   1.00 26.95 ? 44  ASP A OD1 1 
ATOM   334  O  OD2 . ASP A 1 44  ? 31.867 -0.081  5.170   1.00 26.85 ? 44  ASP A OD2 1 
ATOM   335  N  N   . GLN A 1 45  ? 26.577 -0.264  3.047   1.00 13.65 ? 45  GLN A N   1 
ATOM   336  C  CA  . GLN A 1 45  ? 25.589 0.267   2.129   1.00 13.59 ? 45  GLN A CA  1 
ATOM   337  C  C   . GLN A 1 45  ? 24.410 0.908   2.856   1.00 14.18 ? 45  GLN A C   1 
ATOM   338  O  O   . GLN A 1 45  ? 24.073 0.564   3.991   1.00 15.61 ? 45  GLN A O   1 
ATOM   339  C  CB  . GLN A 1 45  ? 25.098 -0.823  1.180   1.00 13.83 ? 45  GLN A CB  1 
ATOM   340  C  CG  . GLN A 1 45  ? 26.227 -1.346  0.295   1.00 13.78 ? 45  GLN A CG  1 
ATOM   341  C  CD  . GLN A 1 45  ? 26.802 -0.253  -0.557  1.00 14.25 ? 45  GLN A CD  1 
ATOM   342  O  OE1 . GLN A 1 45  ? 26.182 0.135   -1.552  1.00 15.35 ? 45  GLN A OE1 1 
ATOM   343  N  NE2 . GLN A 1 45  ? 27.989 0.247   -0.197  1.00 14.62 ? 45  GLN A NE2 1 
ATOM   344  N  N   . LEU A 1 46  ? 23.772 1.828   2.150   1.00 13.74 ? 46  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 46  ? 22.540 2.480   2.596   1.00 14.13 ? 46  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 46  ? 21.371 1.625   2.107   1.00 14.03 ? 46  LEU A C   1 
ATOM   347  O  O   . LEU A 1 46  ? 21.023 1.640   0.923   1.00 15.07 ? 46  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 46  ? 22.480 3.889   2.019   1.00 15.67 ? 46  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 46  ? 21.257 4.727   2.331   1.00 18.98 ? 46  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 46  ? 21.075 4.947   3.832   1.00 20.28 ? 46  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 46  ? 21.401 6.049   1.637   1.00 19.96 ? 46  LEU A CD2 1 
ATOM   352  N  N   . MET A 1 47  ? 20.806 0.826   3.011   1.00 15.09 ? 47  MET A N   1 
ATOM   353  C  CA  . MET A 1 47  ? 19.835 -0.189  2.653   1.00 16.45 ? 47  MET A CA  1 
ATOM   354  C  C   . MET A 1 47  ? 18.797 -0.341  3.740   1.00 16.51 ? 47  MET A C   1 
ATOM   355  O  O   . MET A 1 47  ? 19.056 -0.087  4.918   1.00 17.47 ? 47  MET A O   1 
ATOM   356  C  CB  . MET A 1 47  ? 20.482 -1.581  2.501   1.00 18.95 ? 47  MET A CB  1 
ATOM   357  C  CG  . MET A 1 47  ? 21.584 -1.626  1.528   1.00 20.78 ? 47  MET A CG  1 
ATOM   358  S  SD  . MET A 1 47  ? 22.446 -3.204  1.489   1.00 19.83 ? 47  MET A SD  1 
ATOM   359  C  CE  . MET A 1 47  ? 21.228 -4.196  1.906   1.00 18.85 ? 47  MET A CE  1 
ATOM   360  N  N   . ALA A 1 48  ? 17.623 -0.793  3.330   1.00 15.61 ? 48  ALA A N   1 
ATOM   361  C  CA  . ALA A 1 48  ? 16.601 -1.183  4.275   1.00 15.87 ? 48  ALA A CA  1 
ATOM   362  C  C   . ALA A 1 48  ? 15.967 -2.446  3.758   1.00 14.74 ? 48  ALA A C   1 
ATOM   363  O  O   . ALA A 1 48  ? 15.957 -2.711  2.548   1.00 14.61 ? 48  ALA A O   1 
ATOM   364  C  CB  . ALA A 1 48  ? 15.565 -0.082  4.422   1.00 16.57 ? 48  ALA A CB  1 
ATOM   365  N  N   . PHE A 1 49  ? 15.475 -3.251  4.687   1.00 14.02 ? 49  PHE A N   1 
ATOM   366  C  CA  . PHE A 1 49  ? 14.810 -4.507  4.367   1.00 13.96 ? 49  PHE A CA  1 
ATOM   367  C  C   . PHE A 1 49  ? 13.537 -4.502  5.207   1.00 14.16 ? 49  PHE A C   1 
ATOM   368  O  O   . PHE A 1 49  ? 13.605 -4.382  6.440   1.00 14.89 ? 49  PHE A O   1 
ATOM   369  C  CB  . PHE A 1 49  ? 15.701 -5.694  4.714   1.00 14.94 ? 49  PHE A CB  1 
ATOM   370  C  CG  . PHE A 1 49  ? 15.194 -7.012  4.188   1.00 15.76 ? 49  PHE A CG  1 
ATOM   371  C  CD1 . PHE A 1 49  ? 14.080 -7.605  4.752   1.00 16.32 ? 49  PHE A CD1 1 
ATOM   372  C  CD2 . PHE A 1 49  ? 15.863 -7.682  3.177   1.00 16.89 ? 49  PHE A CD2 1 
ATOM   373  C  CE1 . PHE A 1 49  ? 13.617 -8.819  4.309   1.00 16.76 ? 49  PHE A CE1 1 
ATOM   374  C  CE2 . PHE A 1 49  ? 15.413 -8.917  2.720   1.00 17.50 ? 49  PHE A CE2 1 
ATOM   375  C  CZ  . PHE A 1 49  ? 14.280 -9.479  3.278   1.00 17.40 ? 49  PHE A CZ  1 
ATOM   376  N  N   . GLY A 1 50  ? 12.375 -4.525  4.557   1.00 14.41 ? 50  GLY A N   1 
ATOM   377  C  CA  . GLY A 1 50  ? 11.121 -4.434  5.296   1.00 17.07 ? 50  GLY A CA  1 
ATOM   378  C  C   . GLY A 1 50  ? 10.948 -3.132  6.043   1.00 18.31 ? 50  GLY A C   1 
ATOM   379  O  O   . GLY A 1 50  ? 10.219 -3.083  7.045   1.00 20.86 ? 50  GLY A O   1 
ATOM   380  N  N   . GLY A 1 51  ? 11.578 -2.065  5.572   1.00 17.69 ? 51  GLY A N   1 
ATOM   381  C  CA  . GLY A 1 51  ? 11.497 -0.746  6.168   1.00 19.17 ? 51  GLY A CA  1 
ATOM   382  C  C   . GLY A 1 51  ? 12.507 -0.470  7.257   1.00 19.29 ? 51  GLY A C   1 
ATOM   383  O  O   . GLY A 1 51  ? 12.613 0.676   7.712   1.00 21.05 ? 51  GLY A O   1 
ATOM   384  N  N   . SER A 1 52  ? 13.242 -1.455  7.715   1.00 16.85 ? 52  SER A N   1 
ATOM   385  C  CA  . SER A 1 52  ? 14.174 -1.206  8.801   1.00 16.49 ? 52  SER A CA  1 
ATOM   386  C  C   . SER A 1 52  ? 15.593 -1.482  8.351   1.00 17.43 ? 52  SER A C   1 
ATOM   387  O  O   . SER A 1 52  ? 15.843 -2.135  7.334   1.00 16.44 ? 52  SER A O   1 
ATOM   388  C  CB  . SER A 1 52  ? 13.830 -1.998  10.061  1.00 17.19 ? 52  SER A CB  1 
ATOM   389  O  OG  . SER A 1 52  ? 13.890 -3.378  9.757   1.00 18.27 ? 52  SER A OG  1 
ATOM   390  N  N   A SER A 1 53  ? 16.544 -0.976  9.134   0.29 19.20 ? 53  SER A N   1 
ATOM   391  N  N   B SER A 1 53  ? 16.530 -1.038  9.165   0.71 18.87 ? 53  SER A N   1 
ATOM   392  C  CA  A SER A 1 53  ? 17.954 -1.039  8.770   0.29 20.48 ? 53  SER A CA  1 
ATOM   393  C  CA  B SER A 1 53  ? 17.921 -1.069  8.760   0.71 19.78 ? 53  SER A CA  1 
ATOM   394  C  C   A SER A 1 53  ? 18.799 -1.806  9.782   0.29 20.18 ? 53  SER A C   1 
ATOM   395  C  C   B SER A 1 53  ? 18.792 -1.818  9.752   0.71 19.53 ? 53  SER A C   1 
ATOM   396  O  O   A SER A 1 53  ? 19.981 -1.505  9.957   0.29 20.67 ? 53  SER A O   1 
ATOM   397  O  O   B SER A 1 53  ? 19.993 -1.556  9.836   0.71 19.74 ? 53  SER A O   1 
ATOM   398  C  CB  A SER A 1 53  ? 18.533 0.345   8.476   0.29 21.84 ? 53  SER A CB  1 
ATOM   399  C  CB  B SER A 1 53  ? 18.444 0.326   8.446   0.71 20.95 ? 53  SER A CB  1 
ATOM   400  O  OG  A SER A 1 53  ? 18.217 1.273   9.496   0.29 22.41 ? 53  SER A OG  1 
ATOM   401  O  OG  B SER A 1 53  ? 17.832 0.798   7.260   0.71 20.88 ? 53  SER A OG  1 
ATOM   402  N  N   . GLU A 1 54  ? 18.224 -2.828  10.425  1.00 19.40 ? 54  GLU A N   1 
ATOM   403  C  CA  . GLU A 1 54  ? 19.054 -3.828  11.057  1.00 20.16 ? 54  GLU A CA  1 
ATOM   404  C  C   . GLU A 1 54  ? 19.857 -4.523  9.951   1.00 18.53 ? 54  GLU A C   1 
ATOM   405  O  O   . GLU A 1 54  ? 19.570 -4.367  8.749   1.00 18.03 ? 54  GLU A O   1 
ATOM   406  C  CB  . GLU A 1 54  ? 18.205 -4.855  11.814  1.00 21.93 ? 54  GLU A CB  1 
ATOM   407  C  CG  . GLU A 1 54  ? 17.336 -4.260  12.898  1.00 22.92 ? 54  GLU A CG  1 
ATOM   408  C  CD  . GLU A 1 54  ? 16.006 -3.875  12.320  1.00 23.29 ? 54  GLU A CD  1 
ATOM   409  O  OE1 . GLU A 1 54  ? 15.270 -3.146  13.002  1.00 23.46 ? 54  GLU A OE1 1 
ATOM   410  O  OE2 . GLU A 1 54  ? 15.697 -4.295  11.172  1.00 22.85 ? 54  GLU A OE2 1 
ATOM   411  N  N   . PRO A 1 55  ? 20.904 -5.255  10.312  1.00 18.87 ? 55  PRO A N   1 
ATOM   412  C  CA  . PRO A 1 55  ? 21.719 -5.889  9.274   1.00 17.88 ? 55  PRO A CA  1 
ATOM   413  C  C   . PRO A 1 55  ? 20.878 -6.671  8.267   1.00 15.92 ? 55  PRO A C   1 
ATOM   414  O  O   . PRO A 1 55  ? 19.929 -7.380  8.622   1.00 15.70 ? 55  PRO A O   1 
ATOM   415  C  CB  . PRO A 1 55  ? 22.662 -6.781  10.075  1.00 19.17 ? 55  PRO A CB  1 
ATOM   416  C  CG  . PRO A 1 55  ? 22.848 -6.029  11.371  1.00 20.01 ? 55  PRO A CG  1 
ATOM   417  C  CD  . PRO A 1 55  ? 21.503 -5.423  11.645  1.00 19.79 ? 55  PRO A CD  1 
ATOM   418  N  N   . CYS A 1 56  ? 21.188 -6.481  6.990   1.00 15.05 ? 56  CYS A N   1 
ATOM   419  C  CA  . CYS A 1 56  ? 20.472 -7.161  5.919   1.00 14.46 ? 56  CYS A CA  1 
ATOM   420  C  C   . CYS A 1 56  ? 21.442 -7.348  4.760   1.00 14.30 ? 56  CYS A C   1 
ATOM   421  O  O   . CYS A 1 56  ? 22.540 -6.787  4.751   1.00 13.90 ? 56  CYS A O   1 
ATOM   422  C  CB  . CYS A 1 56  ? 19.222 -6.379  5.482   1.00 14.55 ? 56  CYS A CB  1 
ATOM   423  S  SG  . CYS A 1 56  ? 19.537 -4.732  4.857   1.00 16.33 ? 56  CYS A SG  1 
ATOM   424  N  N   . ALA A 1 57  ? 21.039 -8.148  3.772   1.00 13.48 ? 57  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 57  ? 21.879 -8.348  2.603   1.00 13.10 ? 57  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 57  ? 21.018 -8.569  1.379   1.00 12.62 ? 57  ALA A C   1 
ATOM   427  O  O   . ALA A 1 57  ? 19.992 -9.248  1.444   1.00 13.28 ? 57  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 57  ? 22.832 -9.533  2.773   1.00 13.92 ? 57  ALA A CB  1 
ATOM   429  N  N   . LEU A 1 58  ? 21.473 -8.030  0.258   1.00 12.27 ? 58  LEU A N   1 
ATOM   430  C  CA  . LEU A 1 58  ? 20.900 -8.301  -1.060  1.00 12.47 ? 58  LEU A CA  1 
ATOM   431  C  C   . LEU A 1 58  ? 22.010 -8.885  -1.905  1.00 12.10 ? 58  LEU A C   1 
ATOM   432  O  O   . LEU A 1 58  ? 23.068 -8.270  -2.030  1.00 12.55 ? 58  LEU A O   1 
ATOM   433  C  CB  . LEU A 1 58  ? 20.377 -7.022  -1.719  1.00 13.69 ? 58  LEU A CB  1 
ATOM   434  C  CG  . LEU A 1 58  ? 19.276 -6.317  -0.912  1.00 15.60 ? 58  LEU A CG  1 
ATOM   435  C  CD1 . LEU A 1 58  ? 18.855 -5.037  -1.610  1.00 17.65 ? 58  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A 1 58  ? 18.059 -7.259  -0.717  1.00 17.17 ? 58  LEU A CD2 1 
ATOM   437  N  N   . CYS A 1 59  ? 21.763 -10.056 -2.462  1.00 12.10 ? 59  CYS A N   1 
ATOM   438  C  CA  . CYS A 1 59  ? 22.813 -10.825 -3.096  1.00 12.24 ? 59  CYS A CA  1 
ATOM   439  C  C   . CYS A 1 59  ? 22.345 -11.358 -4.427  1.00 11.49 ? 59  CYS A C   1 
ATOM   440  O  O   . CYS A 1 59  ? 21.144 -11.443 -4.707  1.00 12.01 ? 59  CYS A O   1 
ATOM   441  C  CB  . CYS A 1 59  ? 23.180 -12.049 -2.244  1.00 12.78 ? 59  CYS A CB  1 
ATOM   442  S  SG  . CYS A 1 59  ? 23.436 -11.747 -0.504  1.00 14.17 ? 59  CYS A SG  1 
ATOM   443  N  N   . SER A 1 60  ? 23.299 -11.794 -5.220  1.00 11.90 ? 60  SER A N   1 
ATOM   444  C  CA  . SER A 1 60  ? 22.962 -12.526 -6.430  1.00 12.26 ? 60  SER A CA  1 
ATOM   445  C  C   . SER A 1 60  ? 23.991 -13.599 -6.709  1.00 11.44 ? 60  SER A C   1 
ATOM   446  O  O   . SER A 1 60  ? 25.167 -13.447 -6.375  1.00 11.85 ? 60  SER A O   1 
ATOM   447  C  CB  . SER A 1 60  ? 22.866 -11.623 -7.659  1.00 13.89 ? 60  SER A CB  1 
ATOM   448  O  OG  . SER A 1 60  ? 24.089 -11.002 -7.924  1.00 14.95 ? 60  SER A OG  1 
ATOM   449  N  N   . LEU A 1 61  ? 23.544 -14.677 -7.357  1.00 11.93 ? 61  LEU A N   1 
ATOM   450  C  CA  . LEU A 1 61  ? 24.432 -15.732 -7.838  1.00 11.99 ? 61  LEU A CA  1 
ATOM   451  C  C   . LEU A 1 61  ? 24.124 -15.926 -9.303  1.00 11.84 ? 61  LEU A C   1 
ATOM   452  O  O   . LEU A 1 61  ? 22.987 -16.243 -9.651  1.00 12.78 ? 61  LEU A O   1 
ATOM   453  C  CB  . LEU A 1 61  ? 24.190 -17.038 -7.075  1.00 13.49 ? 61  LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 61  ? 25.067 -18.217 -7.549  1.00 13.68 ? 61  LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 61  ? 26.553 -18.007 -7.260  1.00 14.80 ? 61  LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 61  ? 24.614 -19.525 -6.893  1.00 14.91 ? 61  LEU A CD2 1 
ATOM   457  N  N   . HIS A 1 62  ? 25.119 -15.712 -10.152 1.00 11.72 ? 62  HIS A N   1 
ATOM   458  C  CA  . HIS A 1 62  ? 25.008 -15.948 -11.589 1.00 12.00 ? 62  HIS A CA  1 
ATOM   459  C  C   . HIS A 1 62  ? 25.868 -17.169 -11.919 1.00 11.72 ? 62  HIS A C   1 
ATOM   460  O  O   . HIS A 1 62  ? 27.022 -17.236 -11.500 1.00 12.68 ? 62  HIS A O   1 
ATOM   461  C  CB  . HIS A 1 62  ? 25.538 -14.753 -12.388 1.00 13.09 ? 62  HIS A CB  1 
ATOM   462  C  CG  . HIS A 1 62  ? 24.743 -13.501 -12.231 1.00 13.23 ? 62  HIS A CG  1 
ATOM   463  N  ND1 . HIS A 1 62  ? 24.776 -12.728 -11.098 1.00 15.32 ? 62  HIS A ND1 1 
ATOM   464  C  CD2 . HIS A 1 62  ? 23.902 -12.879 -13.093 1.00 14.04 ? 62  HIS A CD2 1 
ATOM   465  C  CE1 . HIS A 1 62  ? 23.970 -11.687 -11.255 1.00 15.08 ? 62  HIS A CE1 1 
ATOM   466  N  NE2 . HIS A 1 62  ? 23.435 -11.755 -12.463 1.00 15.38 ? 62  HIS A NE2 1 
ATOM   467  N  N   . SER A 1 63  ? 25.314 -18.123 -12.657 1.00 12.25 ? 63  SER A N   1 
ATOM   468  C  CA  . SER A 1 63  ? 26.068 -19.320 -13.018 1.00 13.04 ? 63  SER A CA  1 
ATOM   469  C  C   . SER A 1 63  ? 25.563 -19.860 -14.338 1.00 12.51 ? 63  SER A C   1 
ATOM   470  O  O   . SER A 1 63  ? 24.370 -19.771 -14.626 1.00 12.62 ? 63  SER A O   1 
ATOM   471  C  CB  . SER A 1 63  ? 25.896 -20.403 -11.940 1.00 14.70 ? 63  SER A CB  1 
ATOM   472  O  OG  . SER A 1 63  ? 26.606 -21.594 -12.229 1.00 15.42 ? 63  SER A OG  1 
ATOM   473  N  N   . ILE A 1 64  ? 26.467 -20.419 -15.140 1.00 12.95 ? 64  ILE A N   1 
ATOM   474  C  CA  . ILE A 1 64  ? 26.078 -21.121 -16.366 1.00 13.70 ? 64  ILE A CA  1 
ATOM   475  C  C   . ILE A 1 64  ? 25.640 -22.516 -15.936 1.00 14.75 ? 64  ILE A C   1 
ATOM   476  O  O   . ILE A 1 64  ? 26.474 -23.381 -15.661 1.00 15.35 ? 64  ILE A O   1 
ATOM   477  C  CB  . ILE A 1 64  ? 27.219 -21.160 -17.384 1.00 13.98 ? 64  ILE A CB  1 
ATOM   478  C  CG1 . ILE A 1 64  ? 27.592 -19.736 -17.799 1.00 13.72 ? 64  ILE A CG1 1 
ATOM   479  C  CG2 . ILE A 1 64  ? 26.810 -22.016 -18.572 1.00 14.54 ? 64  ILE A CG2 1 
ATOM   480  C  CD1 . ILE A 1 64  ? 28.896 -19.695 -18.505 1.00 14.40 ? 64  ILE A CD1 1 
ATOM   481  N  N   . GLY A 1 65  ? 24.325 -22.703 -15.803 1.00 14.70 ? 65  GLY A N   1 
ATOM   482  C  CA  . GLY A 1 65  ? 23.802 -23.950 -15.278 1.00 15.37 ? 65  GLY A CA  1 
ATOM   483  C  C   . GLY A 1 65  ? 23.982 -24.029 -13.763 1.00 14.83 ? 65  GLY A C   1 
ATOM   484  O  O   . GLY A 1 65  ? 24.429 -23.086 -13.092 1.00 15.06 ? 65  GLY A O   1 
ATOM   485  N  N   . LYS A 1 66  ? 23.627 -25.198 -13.210 1.00 15.03 ? 66  LYS A N   1 
ATOM   486  C  CA  . LYS A 1 66  ? 23.685 -25.458 -11.775 1.00 15.06 ? 66  LYS A CA  1 
ATOM   487  C  C   . LYS A 1 66  ? 22.756 -24.516 -11.016 1.00 15.56 ? 66  LYS A C   1 
ATOM   488  O  O   . LYS A 1 66  ? 23.001 -24.174 -9.860  1.00 16.68 ? 66  LYS A O   1 
ATOM   489  C  CB  . LYS A 1 66  ? 25.110 -25.396 -11.221 1.00 16.72 ? 66  LYS A CB  1 
ATOM   490  C  CG  . LYS A 1 66  ? 26.103 -26.257 -12.012 1.00 19.04 ? 66  LYS A CG  1 
ATOM   491  C  CD  . LYS A 1 66  ? 25.625 -27.668 -12.110 1.00 22.19 ? 66  LYS A CD  1 
ATOM   492  C  CE  . LYS A 1 66  ? 25.702 -28.391 -10.807 1.00 25.00 ? 66  LYS A CE  1 
ATOM   493  N  NZ  . LYS A 1 66  ? 25.221 -29.808 -11.000 1.00 27.15 ? 66  LYS A NZ  1 
ATOM   494  N  N   . ILE A 1 67  ? 21.654 -24.129 -11.653 1.00 15.11 ? 67  ILE A N   1 
ATOM   495  C  CA  . ILE A 1 67  ? 20.622 -23.286 -11.056 1.00 15.37 ? 67  ILE A CA  1 
ATOM   496  C  C   . ILE A 1 67  ? 19.305 -24.034 -11.231 1.00 16.57 ? 67  ILE A C   1 
ATOM   497  O  O   . ILE A 1 67  ? 19.031 -24.561 -12.318 1.00 17.53 ? 67  ILE A O   1 
ATOM   498  C  CB  . ILE A 1 67  ? 20.577 -21.915 -11.765 1.00 15.63 ? 67  ILE A CB  1 
ATOM   499  C  CG1 . ILE A 1 67  ? 21.902 -21.127 -11.573 1.00 15.68 ? 67  ILE A CG1 1 
ATOM   500  C  CG2 . ILE A 1 67  ? 19.357 -21.125 -11.321 1.00 16.55 ? 67  ILE A CG2 1 
ATOM   501  C  CD1 . ILE A 1 67  ? 22.147 -20.623 -10.162 1.00 15.85 ? 67  ILE A CD1 1 
ATOM   502  N  N   . GLY A 1 68  ? 18.500 -24.096 -10.179 1.00 15.92 ? 68  GLY A N   1 
ATOM   503  C  CA  . GLY A 1 68  ? 17.215 -24.769 -10.301 1.00 16.59 ? 68  GLY A CA  1 
ATOM   504  C  C   . GLY A 1 68  ? 16.550 -24.817 -8.946  1.00 16.30 ? 68  GLY A C   1 
ATOM   505  O  O   . GLY A 1 68  ? 17.111 -24.384 -7.951  1.00 15.94 ? 68  GLY A O   1 
ATOM   506  N  N   . GLY A 1 69  ? 15.345 -25.368 -8.913  1.00 16.99 ? 69  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 69  ? 14.553 -25.342 -7.685  1.00 17.54 ? 69  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 69  ? 15.269 -25.866 -6.457  1.00 17.08 ? 69  GLY A C   1 
ATOM   509  O  O   . GLY A 1 69  ? 15.442 -25.148 -5.469  1.00 16.35 ? 69  GLY A O   1 
ATOM   510  N  N   . ALA A 1 70  ? 15.669 -27.131 -6.507  1.00 18.08 ? 70  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 70  ? 16.351 -27.749 -5.379  1.00 18.94 ? 70  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 70  ? 17.725 -27.138 -5.150  1.00 17.81 ? 70  ALA A C   1 
ATOM   513  O  O   . ALA A 1 70  ? 18.128 -26.906 -3.999  1.00 17.50 ? 70  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 70  ? 16.479 -29.264 -5.608  1.00 19.33 ? 70  ALA A CB  1 
ATOM   515  N  N   . GLN A 1 71  ? 18.476 -26.896 -6.232  1.00 16.82 ? 71  GLN A N   1 
ATOM   516  C  CA  . GLN A 1 71  ? 19.820 -26.364 -6.061  1.00 16.08 ? 71  GLN A CA  1 
ATOM   517  C  C   . GLN A 1 71  ? 19.766 -25.004 -5.392  1.00 15.06 ? 71  GLN A C   1 
ATOM   518  O  O   . GLN A 1 71  ? 20.590 -24.701 -4.516  1.00 15.34 ? 71  GLN A O   1 
ATOM   519  C  CB  . GLN A 1 71  ? 20.543 -26.270 -7.407  1.00 17.04 ? 71  GLN A CB  1 
ATOM   520  C  CG  . GLN A 1 71  ? 20.890 -27.647 -7.927  1.00 18.18 ? 71  GLN A CG  1 
ATOM   521  C  CD  . GLN A 1 71  ? 21.461 -27.569 -9.314  1.00 19.48 ? 71  GLN A CD  1 
ATOM   522  O  OE1 . GLN A 1 71  ? 22.670 -27.542 -9.488  1.00 20.76 ? 71  GLN A OE1 1 
ATOM   523  N  NE2 . GLN A 1 71  ? 20.597 -27.483 -10.313 1.00 20.11 ? 71  GLN A NE2 1 
ATOM   524  N  N   . ASN A 1 72  ? 18.793 -24.169 -5.780  1.00 14.68 ? 72  ASN A N   1 
ATOM   525  C  CA  . ASN A 1 72  ? 18.736 -22.821 -5.220  1.00 14.03 ? 72  ASN A CA  1 
ATOM   526  C  C   . ASN A 1 72  ? 18.326 -22.839 -3.757  1.00 14.16 ? 72  ASN A C   1 
ATOM   527  O  O   . ASN A 1 72  ? 18.798 -22.006 -2.973  1.00 14.79 ? 72  ASN A O   1 
ATOM   528  C  CB  . ASN A 1 72  ? 17.759 -21.943 -6.010  1.00 14.23 ? 72  ASN A CB  1 
ATOM   529  C  CG  . ASN A 1 72  ? 18.178 -21.738 -7.446  1.00 13.65 ? 72  ASN A CG  1 
ATOM   530  O  OD1 . ASN A 1 72  ? 19.268 -22.128 -7.886  1.00 13.74 ? 72  ASN A OD1 1 
ATOM   531  N  ND2 . ASN A 1 72  ? 17.300 -21.094 -8.196  1.00 13.74 ? 72  ASN A ND2 1 
ATOM   532  N  N   . ARG A 1 73  ? 17.464 -23.786 -3.360  1.00 14.93 ? 73  ARG A N   1 
ATOM   533  C  CA  . ARG A 1 73  ? 17.164 -23.931 -1.937  1.00 16.05 ? 73  ARG A CA  1 
ATOM   534  C  C   . ARG A 1 73  ? 18.432 -24.276 -1.173  1.00 16.03 ? 73  ARG A C   1 
ATOM   535  O  O   . ARG A 1 73  ? 18.691 -23.734 -0.089  1.00 16.61 ? 73  ARG A O   1 
ATOM   536  C  CB  . ARG A 1 73  ? 16.088 -24.998 -1.701  1.00 17.52 ? 73  ARG A CB  1 
ATOM   537  C  CG  . ARG A 1 73  ? 14.689 -24.484 -2.035  1.00 19.57 ? 73  ARG A CG  1 
ATOM   538  C  CD  . ARG A 1 73  ? 13.585 -25.491 -1.642  1.00 23.14 ? 73  ARG A CD  1 
ATOM   539  N  NE  . ARG A 1 73  ? 13.537 -26.624 -2.554  1.00 25.80 ? 73  ARG A NE  1 
ATOM   540  C  CZ  . ARG A 1 73  ? 12.931 -26.584 -3.744  1.00 27.42 ? 73  ARG A CZ  1 
ATOM   541  N  NH1 . ARG A 1 73  ? 12.348 -25.450 -4.145  1.00 27.75 ? 73  ARG A NH1 1 
ATOM   542  N  NH2 . ARG A 1 73  ? 12.926 -27.650 -4.548  1.00 27.84 ? 73  ARG A NH2 1 
ATOM   543  N  N   . SER A 1 74  ? 19.247 -25.165 -1.738  1.00 15.72 ? 74  SER A N   1 
ATOM   544  C  CA  . SER A 1 74  ? 20.487 -25.555 -1.089  1.00 16.45 ? 74  SER A CA  1 
ATOM   545  C  C   . SER A 1 74  ? 21.456 -24.383 -1.023  1.00 15.72 ? 74  SER A C   1 
ATOM   546  O  O   . SER A 1 74  ? 22.092 -24.144 0.011   1.00 15.87 ? 74  SER A O   1 
ATOM   547  C  CB  . SER A 1 74  ? 21.087 -26.736 -1.844  1.00 19.32 ? 74  SER A CB  1 
ATOM   548  O  OG  . SER A 1 74  ? 22.224 -27.194 -1.151  1.00 21.87 ? 74  SER A OG  1 
ATOM   549  N  N   . TYR A 1 75  ? 21.568 -23.626 -2.109  1.00 14.80 ? 75  TYR A N   1 
ATOM   550  C  CA  . TYR A 1 75  ? 22.454 -22.460 -2.090  1.00 14.48 ? 75  TYR A CA  1 
ATOM   551  C  C   . TYR A 1 75  ? 22.005 -21.467 -1.033  1.00 14.22 ? 75  TYR A C   1 
ATOM   552  O  O   . TYR A 1 75  ? 22.829 -20.857 -0.350  1.00 14.62 ? 75  TYR A O   1 
ATOM   553  C  CB  . TYR A 1 75  ? 22.476 -21.735 -3.447  1.00 14.70 ? 75  TYR A CB  1 
ATOM   554  C  CG  . TYR A 1 75  ? 23.058 -22.509 -4.612  1.00 15.39 ? 75  TYR A CG  1 
ATOM   555  C  CD1 . TYR A 1 75  ? 24.148 -23.360 -4.448  1.00 17.73 ? 75  TYR A CD1 1 
ATOM   556  C  CD2 . TYR A 1 75  ? 22.520 -22.382 -5.865  1.00 15.17 ? 75  TYR A CD2 1 
ATOM   557  C  CE1 . TYR A 1 75  ? 24.685 -24.060 -5.528  1.00 19.00 ? 75  TYR A CE1 1 
ATOM   558  C  CE2 . TYR A 1 75  ? 23.029 -23.081 -6.948  1.00 15.42 ? 75  TYR A CE2 1 
ATOM   559  C  CZ  . TYR A 1 75  ? 24.107 -23.919 -6.768  1.00 17.88 ? 75  TYR A CZ  1 
ATOM   560  O  OH  . TYR A 1 75  ? 24.617 -24.617 -7.832  1.00 19.67 ? 75  TYR A OH  1 
ATOM   561  N  N   . SER A 1 76  ? 20.693 -21.271 -0.898  1.00 14.44 ? 76  SER A N   1 
ATOM   562  C  CA  . SER A 1 76  ? 20.215 -20.279 0.053   1.00 14.28 ? 76  SER A CA  1 
ATOM   563  C  C   . SER A 1 76  ? 20.521 -20.703 1.479   1.00 14.16 ? 76  SER A C   1 
ATOM   564  O  O   . SER A 1 76  ? 20.873 -19.866 2.301   1.00 14.51 ? 76  SER A O   1 
ATOM   565  C  CB  . SER A 1 76  ? 18.716 -20.071 -0.110  1.00 15.07 ? 76  SER A CB  1 
ATOM   566  O  OG  . SER A 1 76  ? 18.488 -19.527 -1.385  1.00 16.13 ? 76  SER A OG  1 
ATOM   567  N  N   . LYS A 1 77  ? 20.371 -21.994 1.800   1.00 14.57 ? 77  LYS A N   1 
ATOM   568  C  CA  . LYS A 1 77  ? 20.733 -22.453 3.134   1.00 16.45 ? 77  LYS A CA  1 
ATOM   569  C  C   . LYS A 1 77  ? 22.224 -22.254 3.398   1.00 16.44 ? 77  LYS A C   1 
ATOM   570  O  O   . LYS A 1 77  ? 22.613 -21.765 4.461   1.00 16.99 ? 77  LYS A O   1 
ATOM   571  C  CB  . LYS A 1 77  ? 20.311 -23.917 3.294   1.00 18.09 ? 77  LYS A CB  1 
ATOM   572  C  CG  . LYS A 1 77  ? 20.564 -24.477 4.660   1.00 20.70 ? 77  LYS A CG  1 
ATOM   573  C  CD  . LYS A 1 77  ? 20.189 -25.929 4.737   1.00 23.80 ? 77  LYS A CD  1 
ATOM   574  C  CE  . LYS A 1 77  ? 20.504 -26.459 6.121   1.00 26.99 ? 77  LYS A CE  1 
ATOM   575  N  NZ  . LYS A 1 77  ? 20.261 -27.920 6.184   1.00 29.49 ? 77  LYS A NZ  1 
ATOM   576  N  N   . LEU A 1 78  ? 23.070 -22.582 2.422   1.00 15.42 ? 78  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 78  ? 24.503 -22.409 2.600   1.00 16.27 ? 78  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 78  ? 24.854 -20.939 2.778   1.00 15.46 ? 78  LEU A C   1 
ATOM   579  O  O   . LEU A 1 78  ? 25.596 -20.564 3.694   1.00 15.41 ? 78  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 78  ? 25.206 -22.973 1.355   1.00 17.52 ? 78  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 78  ? 26.697 -22.661 1.192   1.00 19.35 ? 78  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 78  ? 27.519 -23.469 2.192   1.00 21.01 ? 78  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 78  ? 27.143 -22.927 -0.251  1.00 20.00 ? 78  LEU A CD2 1 
ATOM   584  N  N   . LEU A 1 79  ? 24.345 -20.087 1.879   1.00 14.59 ? 79  LEU A N   1 
ATOM   585  C  CA  . LEU A 1 79  ? 24.773 -18.689 1.857   1.00 14.69 ? 79  LEU A CA  1 
ATOM   586  C  C   . LEU A 1 79  ? 24.184 -17.910 3.020   1.00 14.92 ? 79  LEU A C   1 
ATOM   587  O  O   . LEU A 1 79  ? 24.885 -17.108 3.642   1.00 14.83 ? 79  LEU A O   1 
ATOM   588  C  CB  . LEU A 1 79  ? 24.435 -18.059 0.504   1.00 15.54 ? 79  LEU A CB  1 
ATOM   589  C  CG  . LEU A 1 79  ? 25.243 -18.654 -0.658  1.00 16.43 ? 79  LEU A CG  1 
ATOM   590  C  CD1 . LEU A 1 79  ? 24.617 -18.278 -1.987  1.00 16.81 ? 79  LEU A CD1 1 
ATOM   591  C  CD2 . LEU A 1 79  ? 26.702 -18.184 -0.617  1.00 17.43 ? 79  LEU A CD2 1 
ATOM   592  N  N   . CYS A 1 80  ? 22.903 -18.134 3.341   1.00 14.77 ? 80  CYS A N   1 
ATOM   593  C  CA  . CYS A 1 80  ? 22.368 -17.511 4.542   1.00 15.13 ? 80  CYS A CA  1 
ATOM   594  C  C   . CYS A 1 80  ? 23.127 -17.971 5.776   1.00 15.03 ? 80  CYS A C   1 
ATOM   595  O  O   . CYS A 1 80  ? 23.342 -17.188 6.702   1.00 15.66 ? 80  CYS A O   1 
ATOM   596  C  CB  . CYS A 1 80  ? 20.892 -17.823 4.691   1.00 15.80 ? 80  CYS A CB  1 
ATOM   597  S  SG  . CYS A 1 80  ? 19.793 -17.025 3.487   1.00 15.86 ? 80  CYS A SG  1 
ATOM   598  N  N   . GLY A 1 81  ? 23.510 -19.247 5.826   1.00 15.82 ? 81  GLY A N   1 
ATOM   599  C  CA  . GLY A 1 81  ? 24.282 -19.722 6.965   1.00 16.65 ? 81  GLY A CA  1 
ATOM   600  C  C   . GLY A 1 81  ? 25.596 -18.983 7.125   1.00 16.29 ? 81  GLY A C   1 
ATOM   601  O  O   . GLY A 1 81  ? 25.965 -18.579 8.230   1.00 17.14 ? 81  GLY A O   1 
ATOM   602  N  N   . LEU A 1 82  ? 26.306 -18.768 6.013   1.00 15.95 ? 82  LEU A N   1 
ATOM   603  C  CA  . LEU A 1 82  ? 27.558 -18.017 6.053   1.00 16.43 ? 82  LEU A CA  1 
ATOM   604  C  C   . LEU A 1 82  ? 27.325 -16.554 6.438   1.00 15.62 ? 82  LEU A C   1 
ATOM   605  O  O   . LEU A 1 82  ? 28.110 -15.982 7.205   1.00 16.15 ? 82  LEU A O   1 
ATOM   606  C  CB  . LEU A 1 82  ? 28.230 -18.103 4.680   1.00 18.24 ? 82  LEU A CB  1 
ATOM   607  C  CG  . LEU A 1 82  ? 28.909 -19.423 4.346   1.00 20.71 ? 82  LEU A CG  1 
ATOM   608  C  CD1 . LEU A 1 82  ? 29.281 -19.465 2.881   1.00 21.52 ? 82  LEU A CD1 1 
ATOM   609  C  CD2 . LEU A 1 82  ? 30.141 -19.616 5.252   1.00 22.13 ? 82  LEU A CD2 1 
ATOM   610  N  N   . LEU A 1 83  ? 26.283 -15.917 5.881   1.00 15.00 ? 83  LEU A N   1 
ATOM   611  C  CA  . LEU A 1 83  ? 26.024 -14.526 6.236   1.00 14.99 ? 83  LEU A CA  1 
ATOM   612  C  C   . LEU A 1 83  ? 25.635 -14.394 7.707   1.00 15.53 ? 83  LEU A C   1 
ATOM   613  O  O   . LEU A 1 83  ? 26.008 -13.426 8.376   1.00 15.64 ? 83  LEU A O   1 
ATOM   614  C  CB  . LEU A 1 83  ? 24.937 -13.935 5.346   1.00 15.23 ? 83  LEU A CB  1 
ATOM   615  C  CG  . LEU A 1 83  ? 25.352 -13.819 3.869   1.00 16.20 ? 83  LEU A CG  1 
ATOM   616  C  CD1 . LEU A 1 83  ? 24.170 -13.503 2.993   1.00 16.87 ? 83  LEU A CD1 1 
ATOM   617  C  CD2 . LEU A 1 83  ? 26.369 -12.728 3.687   1.00 17.94 ? 83  LEU A CD2 1 
ATOM   618  N  N   . ALA A 1 84  ? 24.901 -15.369 8.247   1.00 15.44 ? 84  ALA A N   1 
ATOM   619  C  CA  . ALA A 1 84  ? 24.534 -15.313 9.658   1.00 16.59 ? 84  ALA A CA  1 
ATOM   620  C  C   . ALA A 1 84  ? 25.765 -15.506 10.540  1.00 17.77 ? 84  ALA A C   1 
ATOM   621  O  O   . ALA A 1 84  ? 25.991 -14.751 11.499  1.00 19.01 ? 84  ALA A O   1 
ATOM   622  C  CB  . ALA A 1 84  ? 23.461 -16.373 9.940   1.00 17.36 ? 84  ALA A CB  1 
ATOM   623  N  N   . GLU A 1 85  ? 26.596 -16.506 10.214  1.00 18.18 ? 85  GLU A N   1 
ATOM   624  C  CA  . GLU A 1 85  ? 27.730 -16.854 11.066  1.00 20.62 ? 85  GLU A CA  1 
ATOM   625  C  C   . GLU A 1 85  ? 28.813 -15.787 11.004  1.00 19.43 ? 85  GLU A C   1 
ATOM   626  O  O   . GLU A 1 85  ? 29.383 -15.411 12.030  1.00 20.34 ? 85  GLU A O   1 
ATOM   627  C  CB  . GLU A 1 85  ? 28.292 -18.194 10.594  1.00 24.47 ? 85  GLU A CB  1 
ATOM   628  C  CG  . GLU A 1 85  ? 29.635 -18.611 11.192  1.00 29.59 ? 85  GLU A CG  1 
ATOM   629  C  CD  . GLU A 1 85  ? 30.207 -19.847 10.476  1.00 34.34 ? 85  GLU A CD  1 
ATOM   630  O  OE1 . GLU A 1 85  ? 30.900 -20.640 11.150  1.00 36.41 ? 85  GLU A OE1 1 
ATOM   631  O  OE2 . GLU A 1 85  ? 29.959 -20.027 9.241   1.00 35.81 ? 85  GLU A OE2 1 
ATOM   632  N  N   . ARG A 1 86  ? 29.093 -15.267 9.810   1.00 18.03 ? 86  ARG A N   1 
ATOM   633  C  CA  . ARG A 1 86  ? 30.225 -14.369 9.629   1.00 18.16 ? 86  ARG A CA  1 
ATOM   634  C  C   . ARG A 1 86  ? 29.857 -12.902 9.709   1.00 18.31 ? 86  ARG A C   1 
ATOM   635  O  O   . ARG A 1 86  ? 30.668 -12.103 10.184  1.00 19.79 ? 86  ARG A O   1 
ATOM   636  C  CB  . ARG A 1 86  ? 30.912 -14.634 8.285   1.00 19.82 ? 86  ARG A CB  1 
ATOM   637  C  CG  . ARG A 1 86  ? 31.395 -16.021 8.112   1.00 21.99 ? 86  ARG A CG  1 
ATOM   638  C  CD  . ARG A 1 86  ? 32.319 -16.391 9.188   1.00 24.45 ? 86  ARG A CD  1 
ATOM   639  N  NE  . ARG A 1 86  ? 32.943 -17.643 8.855   1.00 26.53 ? 86  ARG A NE  1 
ATOM   640  C  CZ  . ARG A 1 86  ? 33.598 -18.390 9.723   1.00 29.18 ? 86  ARG A CZ  1 
ATOM   641  N  NH1 . ARG A 1 86  ? 33.705 -18.004 10.995  1.00 30.28 ? 86  ARG A NH1 1 
ATOM   642  N  NH2 . ARG A 1 86  ? 34.144 -19.522 9.297   1.00 30.01 ? 86  ARG A NH2 1 
ATOM   643  N  N   . LEU A 1 87  ? 28.677 -12.516 9.215   1.00 17.01 ? 87  LEU A N   1 
ATOM   644  C  CA  . LEU A 1 87  ? 28.273 -11.123 9.215   1.00 16.94 ? 87  LEU A CA  1 
ATOM   645  C  C   . LEU A 1 87  ? 27.174 -10.833 10.209  1.00 16.70 ? 87  LEU A C   1 
ATOM   646  O  O   . LEU A 1 87  ? 26.796 -9.660  10.352  1.00 17.28 ? 87  LEU A O   1 
ATOM   647  C  CB  . LEU A 1 87  ? 27.818 -10.675 7.807   1.00 17.30 ? 87  LEU A CB  1 
ATOM   648  C  CG  . LEU A 1 87  ? 28.869 -10.784 6.695   1.00 18.02 ? 87  LEU A CG  1 
ATOM   649  C  CD1 . LEU A 1 87  ? 28.402 -10.047 5.445   1.00 18.00 ? 87  LEU A CD1 1 
ATOM   650  C  CD2 . LEU A 1 87  ? 30.215 -10.246 7.118   1.00 19.66 ? 87  LEU A CD2 1 
ATOM   651  N  N   . ARG A 1 88  ? 26.646 -11.855 10.893  1.00 16.75 ? 88  ARG A N   1 
ATOM   652  C  CA  . ARG A 1 88  ? 25.584 -11.659 11.888  1.00 18.34 ? 88  ARG A CA  1 
ATOM   653  C  C   . ARG A 1 88  ? 24.311 -11.085 11.278  1.00 17.40 ? 88  ARG A C   1 
ATOM   654  O  O   . ARG A 1 88  ? 23.589 -10.335 11.928  1.00 19.19 ? 88  ARG A O   1 
ATOM   655  C  CB  . ARG A 1 88  ? 26.034 -10.837 13.105  1.00 22.06 ? 88  ARG A CB  1 
ATOM   656  C  CG  . ARG A 1 88  ? 27.449 -11.114 13.538  1.00 27.10 ? 88  ARG A CG  1 
ATOM   657  C  CD  . ARG A 1 88  ? 27.694 -12.588 13.858  1.00 32.28 ? 88  ARG A CD  1 
ATOM   658  N  NE  . ARG A 1 88  ? 26.910 -13.102 14.977  1.00 37.08 ? 88  ARG A NE  1 
ATOM   659  C  CZ  . ARG A 1 88  ? 26.801 -14.398 15.286  1.00 40.43 ? 88  ARG A CZ  1 
ATOM   660  N  NH1 . ARG A 1 88  ? 26.077 -14.780 16.339  1.00 41.72 ? 88  ARG A NH1 1 
ATOM   661  N  NH2 . ARG A 1 88  ? 27.415 -15.316 14.533  1.00 41.24 ? 88  ARG A NH2 1 
ATOM   662  N  N   . ILE A 1 89  ? 24.021 -11.473 10.041  1.00 15.93 ? 89  ILE A N   1 
ATOM   663  C  CA  . ILE A 1 89  ? 22.793 -11.077 9.364   1.00 15.81 ? 89  ILE A CA  1 
ATOM   664  C  C   . ILE A 1 89  ? 21.782 -12.209 9.509   1.00 16.06 ? 89  ILE A C   1 
ATOM   665  O  O   . ILE A 1 89  ? 22.063 -13.362 9.168   1.00 17.14 ? 89  ILE A O   1 
ATOM   666  C  CB  . ILE A 1 89  ? 23.060 -10.789 7.876   1.00 15.08 ? 89  ILE A CB  1 
ATOM   667  C  CG1 . ILE A 1 89  ? 24.079 -9.661  7.760   1.00 15.23 ? 89  ILE A CG1 1 
ATOM   668  C  CG2 . ILE A 1 89  ? 21.755 -10.409 7.201   1.00 15.16 ? 89  ILE A CG2 1 
ATOM   669  C  CD1 . ILE A 1 89  ? 24.606 -9.512  6.339   1.00 15.03 ? 89  ILE A CD1 1 
ATOM   670  N  N   . SER A 1 90  ? 20.580 -11.875 9.975   1.00 15.53 ? 90  SER A N   1 
ATOM   671  C  CA  . SER A 1 90  ? 19.522 -12.879 10.079  1.00 16.47 ? 90  SER A CA  1 
ATOM   672  C  C   . SER A 1 90  ? 19.128 -13.372 8.691   1.00 14.61 ? 90  SER A C   1 
ATOM   673  O  O   . SER A 1 90  ? 18.928 -12.558 7.791   1.00 14.16 ? 90  SER A O   1 
ATOM   674  C  CB  . SER A 1 90  ? 18.293 -12.221 10.691  1.00 19.79 ? 90  SER A CB  1 
ATOM   675  O  OG  . SER A 1 90  ? 18.496 -11.806 12.025  1.00 23.75 ? 90  SER A OG  1 
ATOM   676  N  N   . PRO A 1 91  ? 18.929 -14.688 8.514   1.00 14.82 ? 91  PRO A N   1 
ATOM   677  C  CA  . PRO A 1 91  ? 18.514 -15.200 7.201   1.00 14.54 ? 91  PRO A CA  1 
ATOM   678  C  C   . PRO A 1 91  ? 17.229 -14.590 6.683   1.00 14.15 ? 91  PRO A C   1 
ATOM   679  O  O   . PRO A 1 91  ? 17.068 -14.492 5.460   1.00 14.03 ? 91  PRO A O   1 
ATOM   680  C  CB  . PRO A 1 91  ? 18.374 -16.723 7.430   1.00 15.22 ? 91  PRO A CB  1 
ATOM   681  C  CG  . PRO A 1 91  ? 19.342 -17.003 8.519   1.00 16.51 ? 91  PRO A CG  1 
ATOM   682  C  CD  . PRO A 1 91  ? 19.291 -15.777 9.445   1.00 16.26 ? 91  PRO A CD  1 
ATOM   683  N  N   . ASP A 1 92  ? 16.318 -14.160 7.565   1.00 13.94 ? 92  ASP A N   1 
ATOM   684  C  CA  . ASP A 1 92  ? 15.077 -13.565 7.084   1.00 14.67 ? 92  ASP A CA  1 
ATOM   685  C  C   . ASP A 1 92  ? 15.255 -12.120 6.639   1.00 14.29 ? 92  ASP A C   1 
ATOM   686  O  O   . ASP A 1 92  ? 14.274 -11.495 6.234   1.00 14.42 ? 92  ASP A O   1 
ATOM   687  C  CB  . ASP A 1 92  ? 13.904 -13.741 8.076   1.00 16.86 ? 92  ASP A CB  1 
ATOM   688  C  CG  . ASP A 1 92  ? 14.084 -12.969 9.344   1.00 19.05 ? 92  ASP A CG  1 
ATOM   689  O  OD1 . ASP A 1 92  ? 15.091 -12.246 9.506   1.00 19.05 ? 92  ASP A OD1 1 
ATOM   690  O  OD2 . ASP A 1 92  ? 13.173 -13.090 10.189  1.00 22.09 ? 92  ASP A OD2 1 
ATOM   691  N  N   . ARG A 1 93  ? 16.491 -11.622 6.633   1.00 13.69 ? 93  ARG A N   1 
ATOM   692  C  CA  . ARG A 1 93  ? 16.813 -10.301 6.114   1.00 13.44 ? 93  ARG A CA  1 
ATOM   693  C  C   . ARG A 1 93  ? 17.806 -10.410 4.966   1.00 12.87 ? 93  ARG A C   1 
ATOM   694  O  O   . ARG A 1 93  ? 18.566 -9.470  4.700   1.00 13.81 ? 93  ARG A O   1 
ATOM   695  C  CB  . ARG A 1 93  ? 17.281 -9.351  7.221   1.00 13.53 ? 93  ARG A CB  1 
ATOM   696  C  CG  . ARG A 1 93  ? 16.163 -9.117  8.248   1.00 13.95 ? 93  ARG A CG  1 
ATOM   697  C  CD  . ARG A 1 93  ? 16.604 -8.183  9.387   1.00 14.27 ? 93  ARG A CD  1 
ATOM   698  N  NE  . ARG A 1 93  ? 17.071 -6.885  8.885   1.00 14.47 ? 93  ARG A NE  1 
ATOM   699  C  CZ  . ARG A 1 93  ? 16.293 -5.895  8.436   1.00 14.68 ? 93  ARG A CZ  1 
ATOM   700  N  NH1 . ARG A 1 93  ? 14.966 -5.997  8.427   1.00 14.95 ? 93  ARG A NH1 1 
ATOM   701  N  NH2 . ARG A 1 93  ? 16.838 -4.767  7.990   1.00 15.43 ? 93  ARG A NH2 1 
ATOM   702  N  N   . VAL A 1 94  ? 17.763 -11.536 4.246   1.00 12.97 ? 94  VAL A N   1 
ATOM   703  C  CA  . VAL A 1 94  ? 18.634 -11.779 3.107   1.00 12.82 ? 94  VAL A CA  1 
ATOM   704  C  C   . VAL A 1 94  ? 17.757 -12.135 1.914   1.00 12.47 ? 94  VAL A C   1 
ATOM   705  O  O   . VAL A 1 94  ? 16.893 -13.021 2.019   1.00 13.43 ? 94  VAL A O   1 
ATOM   706  C  CB  . VAL A 1 94  ? 19.608 -12.933 3.378   1.00 13.81 ? 94  VAL A CB  1 
ATOM   707  C  CG1 . VAL A 1 94  ? 20.403 -13.243 2.116   1.00 14.68 ? 94  VAL A CG1 1 
ATOM   708  C  CG2 . VAL A 1 94  ? 20.534 -12.623 4.545   1.00 14.53 ? 94  VAL A CG2 1 
ATOM   709  N  N   . TYR A 1 95  ? 17.994 -11.474 0.785   1.00 12.67 ? 95  TYR A N   1 
ATOM   710  C  CA  . TYR A 1 95  ? 17.498 -11.951 -0.501  1.00 12.57 ? 95  TYR A CA  1 
ATOM   711  C  C   . TYR A 1 95  ? 18.688 -12.342 -1.374  1.00 12.19 ? 95  TYR A C   1 
ATOM   712  O  O   . TYR A 1 95  ? 19.726 -11.662 -1.371  1.00 13.03 ? 95  TYR A O   1 
ATOM   713  C  CB  . TYR A 1 95  ? 16.747 -10.854 -1.238  1.00 12.79 ? 95  TYR A CB  1 
ATOM   714  C  CG  . TYR A 1 95  ? 15.343 -10.580 -0.749  1.00 13.07 ? 95  TYR A CG  1 
ATOM   715  C  CD1 . TYR A 1 95  ? 14.551 -11.585 -0.199  1.00 13.94 ? 95  TYR A CD1 1 
ATOM   716  C  CD2 . TYR A 1 95  ? 14.791 -9.308  -0.891  1.00 14.05 ? 95  TYR A CD2 1 
ATOM   717  C  CE1 . TYR A 1 95  ? 13.254 -11.322 0.196   1.00 14.15 ? 95  TYR A CE1 1 
ATOM   718  C  CE2 . TYR A 1 95  ? 13.487 -9.030  -0.488  1.00 14.12 ? 95  TYR A CE2 1 
ATOM   719  C  CZ  . TYR A 1 95  ? 12.739 -10.051 0.065   1.00 14.04 ? 95  TYR A CZ  1 
ATOM   720  O  OH  . TYR A 1 95  ? 11.435 -9.861  0.450   1.00 15.24 ? 95  TYR A OH  1 
ATOM   721  N  N   . ILE A 1 96  ? 18.537 -13.434 -2.126  1.00 12.14 ? 96  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 96  ? 19.541 -13.861 -3.106  1.00 12.00 ? 96  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 96  ? 18.814 -14.117 -4.416  1.00 12.27 ? 96  ILE A C   1 
ATOM   724  O  O   . ILE A 1 96  ? 18.008 -15.045 -4.491  1.00 12.96 ? 96  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 96  ? 20.236 -15.163 -2.658  1.00 12.69 ? 96  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 96  ? 20.832 -15.035 -1.259  1.00 13.81 ? 96  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 96  ? 21.301 -15.546 -3.672  1.00 13.03 ? 96  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 96  ? 21.086 -16.389 -0.584  1.00 15.56 ? 96  ILE A CD1 1 
ATOM   729  N  N   . ASN A 1 97  ? 19.107 -13.343 -5.448  1.00 11.67 ? 97  ASN A N   1 
ATOM   730  C  CA  . ASN A 1 97  ? 18.547 -13.625 -6.760  1.00 12.19 ? 97  ASN A CA  1 
ATOM   731  C  C   . ASN A 1 97  ? 19.470 -14.563 -7.527  1.00 11.92 ? 97  ASN A C   1 
ATOM   732  O  O   . ASN A 1 97  ? 20.693 -14.352 -7.572  1.00 12.45 ? 97  ASN A O   1 
ATOM   733  C  CB  . ASN A 1 97  ? 18.335 -12.326 -7.541  1.00 13.57 ? 97  ASN A CB  1 
ATOM   734  C  CG  . ASN A 1 97  ? 17.150 -11.543 -7.040  1.00 15.23 ? 97  ASN A CG  1 
ATOM   735  O  OD1 . ASN A 1 97  ? 16.200 -12.124 -6.551  1.00 16.20 ? 97  ASN A OD1 1 
ATOM   736  N  ND2 . ASN A 1 97  ? 17.215 -10.223 -7.140  1.00 16.51 ? 97  ASN A ND2 1 
ATOM   737  N  N   . TYR A 1 98  ? 18.889 -15.598 -8.124  1.00 11.76 ? 98  TYR A N   1 
ATOM   738  C  CA  . TYR A 1 98  ? 19.626 -16.600 -8.871  1.00 12.34 ? 98  TYR A CA  1 
ATOM   739  C  C   . TYR A 1 98  ? 19.400 -16.415 -10.366 1.00 12.06 ? 98  TYR A C   1 
ATOM   740  O  O   . TYR A 1 98  ? 18.259 -16.194 -10.818 1.00 12.22 ? 98  TYR A O   1 
ATOM   741  C  CB  . TYR A 1 98  ? 19.162 -18.010 -8.472  1.00 12.78 ? 98  TYR A CB  1 
ATOM   742  C  CG  . TYR A 1 98  ? 19.505 -18.303 -7.042  1.00 12.59 ? 98  TYR A CG  1 
ATOM   743  C  CD1 . TYR A 1 98  ? 20.791 -18.682 -6.679  1.00 12.58 ? 98  TYR A CD1 1 
ATOM   744  C  CD2 . TYR A 1 98  ? 18.541 -18.177 -6.036  1.00 12.69 ? 98  TYR A CD2 1 
ATOM   745  C  CE1 . TYR A 1 98  ? 21.113 -18.935 -5.366  1.00 12.28 ? 98  TYR A CE1 1 
ATOM   746  C  CE2 . TYR A 1 98  ? 18.868 -18.411 -4.710  1.00 12.45 ? 98  TYR A CE2 1 
ATOM   747  C  CZ  . TYR A 1 98  ? 20.162 -18.774 -4.380  1.00 12.61 ? 98  TYR A CZ  1 
ATOM   748  O  OH  . TYR A 1 98  ? 20.548 -19.016 -3.082  1.00 13.39 ? 98  TYR A OH  1 
ATOM   749  N  N   . TYR A 1 99  ? 20.477 -16.507 -11.138 1.00 11.76 ? 99  TYR A N   1 
ATOM   750  C  CA  . TYR A 1 99  ? 20.449 -16.329 -12.595 1.00 12.47 ? 99  TYR A CA  1 
ATOM   751  C  C   . TYR A 1 99  ? 21.169 -17.496 -13.250 1.00 12.37 ? 99  TYR A C   1 
ATOM   752  O  O   . TYR A 1 99  ? 22.371 -17.692 -13.024 1.00 12.63 ? 99  TYR A O   1 
ATOM   753  C  CB  . TYR A 1 99  ? 21.159 -15.024 -12.989 1.00 12.79 ? 99  TYR A CB  1 
ATOM   754  C  CG  . TYR A 1 99  ? 20.517 -13.821 -12.348 1.00 13.49 ? 99  TYR A CG  1 
ATOM   755  C  CD1 . TYR A 1 99  ? 20.902 -13.389 -11.100 1.00 13.68 ? 99  TYR A CD1 1 
ATOM   756  C  CD2 . TYR A 1 99  ? 19.454 -13.187 -12.976 1.00 16.22 ? 99  TYR A CD2 1 
ATOM   757  C  CE1 . TYR A 1 99  ? 20.282 -12.272 -10.502 1.00 14.77 ? 99  TYR A CE1 1 
ATOM   758  C  CE2 . TYR A 1 99  ? 18.835 -12.120 -12.415 1.00 17.66 ? 99  TYR A CE2 1 
ATOM   759  C  CZ  . TYR A 1 99  ? 19.218 -11.668 -11.170 1.00 17.23 ? 99  TYR A CZ  1 
ATOM   760  O  OH  . TYR A 1 99  ? 18.565 -10.581 -10.617 1.00 19.19 ? 99  TYR A OH  1 
ATOM   761  N  N   . ASP A 1 100 ? 20.444 -18.229 -14.084 1.00 13.05 ? 100 ASP A N   1 
ATOM   762  C  CA  . ASP A 1 100 ? 21.010 -19.295 -14.896 1.00 13.27 ? 100 ASP A CA  1 
ATOM   763  C  C   . ASP A 1 100 ? 21.377 -18.635 -16.216 1.00 12.69 ? 100 ASP A C   1 
ATOM   764  O  O   . ASP A 1 100 ? 20.499 -18.330 -17.033 1.00 14.81 ? 100 ASP A O   1 
ATOM   765  C  CB  . ASP A 1 100 ? 19.952 -20.375 -15.110 1.00 15.57 ? 100 ASP A CB  1 
ATOM   766  C  CG  . ASP A 1 100 ? 20.490 -21.577 -15.855 1.00 17.03 ? 100 ASP A CG  1 
ATOM   767  O  OD1 . ASP A 1 100 ? 21.691 -21.565 -16.265 1.00 16.50 ? 100 ASP A OD1 1 
ATOM   768  O  OD2 . ASP A 1 100 ? 19.720 -22.560 -15.981 1.00 20.24 ? 100 ASP A OD2 1 
ATOM   769  N  N   . MET A 1 101 ? 22.668 -18.387 -16.416 1.00 12.13 ? 101 MET A N   1 
ATOM   770  C  CA  . MET A 1 101 ? 23.140 -17.661 -17.587 1.00 12.38 ? 101 MET A CA  1 
ATOM   771  C  C   . MET A 1 101 ? 23.388 -18.612 -18.758 1.00 12.62 ? 101 MET A C   1 
ATOM   772  O  O   . MET A 1 101 ? 23.967 -19.696 -18.602 1.00 13.56 ? 101 MET A O   1 
ATOM   773  C  CB  . MET A 1 101 ? 24.457 -16.954 -17.259 1.00 13.34 ? 101 MET A CB  1 
ATOM   774  C  CG  . MET A 1 101 ? 24.368 -15.948 -16.155 1.00 14.84 ? 101 MET A CG  1 
ATOM   775  S  SD  . MET A 1 101 ? 23.231 -14.571 -16.460 1.00 16.49 ? 101 MET A SD  1 
ATOM   776  C  CE  . MET A 1 101 ? 23.989 -13.792 -17.891 1.00 16.73 ? 101 MET A CE  1 
ATOM   777  N  N   . ASN A 1 102 ? 22.967 -18.200 -19.939 1.00 12.61 ? 102 ASN A N   1 
ATOM   778  C  CA  . ASN A 1 102 ? 23.389 -18.878 -21.156 1.00 13.51 ? 102 ASN A CA  1 
ATOM   779  C  C   . ASN A 1 102 ? 24.870 -18.618 -21.395 1.00 13.13 ? 102 ASN A C   1 
ATOM   780  O  O   . ASN A 1 102 ? 25.352 -17.505 -21.189 1.00 13.08 ? 102 ASN A O   1 
ATOM   781  C  CB  . ASN A 1 102 ? 22.634 -18.308 -22.358 1.00 15.14 ? 102 ASN A CB  1 
ATOM   782  C  CG  . ASN A 1 102 ? 21.164 -18.633 -22.349 1.00 19.35 ? 102 ASN A CG  1 
ATOM   783  O  OD1 . ASN A 1 102 ? 20.673 -19.391 -21.519 1.00 20.82 ? 102 ASN A OD1 1 
ATOM   784  N  ND2 . ASN A 1 102 ? 20.453 -18.076 -23.320 1.00 21.70 ? 102 ASN A ND2 1 
ATOM   785  N  N   . ALA A 1 103 ? 25.589 -19.647 -21.856 1.00 12.32 ? 103 ALA A N   1 
ATOM   786  C  CA  . ALA A 1 103 ? 27.030 -19.510 -22.066 1.00 12.67 ? 103 ALA A CA  1 
ATOM   787  C  C   . ALA A 1 103 ? 27.352 -18.359 -23.015 1.00 12.91 ? 103 ALA A C   1 
ATOM   788  O  O   . ALA A 1 103 ? 28.379 -17.687 -22.855 1.00 13.21 ? 103 ALA A O   1 
ATOM   789  C  CB  . ALA A 1 103 ? 27.608 -20.830 -22.591 1.00 13.62 ? 103 ALA A CB  1 
ATOM   790  N  N   . ALA A 1 104 ? 26.515 -18.139 -24.033 1.00 12.93 ? 104 ALA A N   1 
ATOM   791  C  CA  . ALA A 1 104 ? 26.750 -17.057 -24.980 1.00 13.54 ? 104 ALA A CA  1 
ATOM   792  C  C   . ALA A 1 104 ? 26.644 -15.683 -24.337 1.00 12.72 ? 104 ALA A C   1 
ATOM   793  O  O   . ALA A 1 104 ? 27.068 -14.693 -24.945 1.00 13.44 ? 104 ALA A O   1 
ATOM   794  C  CB  . ALA A 1 104 ? 25.753 -17.129 -26.129 1.00 16.03 ? 104 ALA A CB  1 
ATOM   795  N  N   . ASN A 1 105 ? 26.059 -15.597 -23.149 1.00 12.49 ? 105 ASN A N   1 
ATOM   796  C  CA  . ASN A 1 105 ? 25.847 -14.328 -22.471 1.00 12.09 ? 105 ASN A CA  1 
ATOM   797  C  C   . ASN A 1 105 ? 26.815 -14.109 -21.329 1.00 11.86 ? 105 ASN A C   1 
ATOM   798  O  O   . ASN A 1 105 ? 26.577 -13.207 -20.513 1.00 12.41 ? 105 ASN A O   1 
ATOM   799  C  CB  . ASN A 1 105 ? 24.396 -14.216 -22.005 1.00 12.72 ? 105 ASN A CB  1 
ATOM   800  C  CG  . ASN A 1 105 ? 23.449 -14.081 -23.164 1.00 13.92 ? 105 ASN A CG  1 
ATOM   801  O  OD1 . ASN A 1 105 ? 23.831 -13.586 -24.208 1.00 15.27 ? 105 ASN A OD1 1 
ATOM   802  N  ND2 . ASN A 1 105 ? 22.198 -14.467 -22.979 1.00 14.96 ? 105 ASN A ND2 1 
ATOM   803  N  N   . VAL A 1 106 ? 27.909 -14.867 -21.290 1.00 11.61 ? 106 VAL A N   1 
ATOM   804  C  CA  . VAL A 1 106 ? 28.958 -14.649 -20.300 1.00 12.11 ? 106 VAL A CA  1 
ATOM   805  C  C   . VAL A 1 106 ? 30.274 -14.465 -21.014 1.00 12.85 ? 106 VAL A C   1 
ATOM   806  O  O   . VAL A 1 106 ? 30.772 -15.400 -21.648 1.00 13.19 ? 106 VAL A O   1 
ATOM   807  C  CB  . VAL A 1 106 ? 29.033 -15.761 -19.243 1.00 12.81 ? 106 VAL A CB  1 
ATOM   808  C  CG1 . VAL A 1 106 ? 30.080 -15.407 -18.204 1.00 13.65 ? 106 VAL A CG1 1 
ATOM   809  C  CG2 . VAL A 1 106 ? 27.632 -16.003 -18.579 1.00 13.20 ? 106 VAL A CG2 1 
ATOM   810  N  N   . GLY A 1 107 ? 30.794 -13.239 -20.952 1.00 12.54 ? 107 GLY A N   1 
ATOM   811  C  CA  . GLY A 1 107 ? 32.095 -12.921 -21.486 1.00 12.86 ? 107 GLY A CA  1 
ATOM   812  C  C   . GLY A 1 107 ? 33.216 -13.168 -20.495 1.00 11.96 ? 107 GLY A C   1 
ATOM   813  O  O   . GLY A 1 107 ? 33.044 -13.031 -19.288 1.00 12.43 ? 107 GLY A O   1 
ATOM   814  N  N   . TRP A 1 108 ? 34.365 -13.558 -21.043 1.00 12.65 ? 108 TRP A N   1 
ATOM   815  C  CA  . TRP A 1 108 ? 35.573 -13.822 -20.270 1.00 12.81 ? 108 TRP A CA  1 
ATOM   816  C  C   . TRP A 1 108 ? 36.718 -13.916 -21.272 1.00 12.95 ? 108 TRP A C   1 
ATOM   817  O  O   . TRP A 1 108 ? 36.542 -14.490 -22.351 1.00 13.08 ? 108 TRP A O   1 
ATOM   818  C  CB  . TRP A 1 108 ? 35.457 -15.174 -19.536 1.00 13.58 ? 108 TRP A CB  1 
ATOM   819  C  CG  . TRP A 1 108 ? 36.692 -15.608 -18.834 1.00 14.05 ? 108 TRP A CG  1 
ATOM   820  C  CD1 . TRP A 1 108 ? 37.222 -15.075 -17.718 1.00 13.74 ? 108 TRP A CD1 1 
ATOM   821  C  CD2 . TRP A 1 108 ? 37.587 -16.656 -19.239 1.00 15.61 ? 108 TRP A CD2 1 
ATOM   822  N  NE1 . TRP A 1 108 ? 38.369 -15.741 -17.366 1.00 14.51 ? 108 TRP A NE1 1 
ATOM   823  C  CE2 . TRP A 1 108 ? 38.626 -16.701 -18.300 1.00 15.84 ? 108 TRP A CE2 1 
ATOM   824  C  CE3 . TRP A 1 108 ? 37.618 -17.541 -20.323 1.00 17.14 ? 108 TRP A CE3 1 
ATOM   825  C  CZ2 . TRP A 1 108 ? 39.682 -17.607 -18.390 1.00 18.61 ? 108 TRP A CZ2 1 
ATOM   826  C  CZ3 . TRP A 1 108 ? 38.663 -18.454 -20.407 1.00 19.47 ? 108 TRP A CZ3 1 
ATOM   827  C  CH2 . TRP A 1 108 ? 39.681 -18.471 -19.455 1.00 20.15 ? 108 TRP A CH2 1 
ATOM   828  N  N   . ASN A 1 109 ? 37.876 -13.359 -20.941 1.00 13.19 ? 109 ASN A N   1 
ATOM   829  C  CA  . ASN A 1 109 ? 39.093 -13.610 -21.720 1.00 13.06 ? 109 ASN A CA  1 
ATOM   830  C  C   . ASN A 1 109 ? 38.888 -13.304 -23.202 1.00 13.56 ? 109 ASN A C   1 
ATOM   831  O  O   . ASN A 1 109 ? 39.284 -14.077 -24.073 1.00 14.99 ? 109 ASN A O   1 
ATOM   832  C  CB  . ASN A 1 109 ? 39.542 -15.068 -21.568 1.00 14.61 ? 109 ASN A CB  1 
ATOM   833  C  CG  . ASN A 1 109 ? 40.959 -15.293 -22.035 1.00 16.20 ? 109 ASN A CG  1 
ATOM   834  O  OD1 . ASN A 1 109 ? 41.811 -14.402 -21.944 1.00 15.98 ? 109 ASN A OD1 1 
ATOM   835  N  ND2 . ASN A 1 109 ? 41.195 -16.460 -22.624 1.00 17.22 ? 109 ASN A ND2 1 
ATOM   836  N  N   . ASN A 1 110 ? 38.306 -12.142 -23.499 1.00 12.70 ? 110 ASN A N   1 
ATOM   837  C  CA  . ASN A 1 110 ? 38.163 -11.669 -24.889 1.00 13.82 ? 110 ASN A CA  1 
ATOM   838  C  C   . ASN A 1 110 ? 37.129 -12.416 -25.720 1.00 14.44 ? 110 ASN A C   1 
ATOM   839  O  O   . ASN A 1 110 ? 37.012 -12.158 -26.928 1.00 15.46 ? 110 ASN A O   1 
ATOM   840  C  CB  . ASN A 1 110 ? 39.509 -11.552 -25.622 1.00 15.02 ? 110 ASN A CB  1 
ATOM   841  C  CG  . ASN A 1 110 ? 40.323 -10.401 -25.108 1.00 16.91 ? 110 ASN A CG  1 
ATOM   842  O  OD1 . ASN A 1 110 ? 39.848 -9.260  -25.092 1.00 18.03 ? 110 ASN A OD1 1 
ATOM   843  N  ND2 . ASN A 1 110 ? 41.551 -10.668 -24.688 1.00 18.38 ? 110 ASN A ND2 1 
ATOM   844  N  N   . SER A 1 111 ? 36.337 -13.288 -25.115 1.00 13.55 ? 111 SER A N   1 
ATOM   845  C  CA  . SER A 1 111 ? 35.366 -14.089 -25.856 1.00 14.57 ? 111 SER A CA  1 
ATOM   846  C  C   . SER A 1 111 ? 34.189 -14.360 -24.921 1.00 13.97 ? 111 SER A C   1 
ATOM   847  O  O   . SER A 1 111 ? 33.993 -13.673 -23.919 1.00 14.10 ? 111 SER A O   1 
ATOM   848  C  CB  . SER A 1 111 ? 36.034 -15.391 -26.356 1.00 17.16 ? 111 SER A CB  1 
ATOM   849  O  OG  . SER A 1 111 ? 35.164 -16.112 -27.213 1.00 19.70 ? 111 SER A OG  1 
ATOM   850  N  N   . THR A 1 112 ? 33.410 -15.371 -25.240 1.00 14.03 ? 112 THR A N   1 
ATOM   851  C  CA  . THR A 1 112 ? 32.369 -15.829 -24.323 1.00 13.98 ? 112 THR A CA  1 
ATOM   852  C  C   . THR A 1 112 ? 32.502 -17.332 -24.128 1.00 15.07 ? 112 THR A C   1 
ATOM   853  O  O   . THR A 1 112 ? 33.255 -18.005 -24.837 1.00 16.32 ? 112 THR A O   1 
ATOM   854  C  CB  . THR A 1 112 ? 30.967 -15.542 -24.846 1.00 13.73 ? 112 THR A CB  1 
ATOM   855  O  OG1 . THR A 1 112 ? 30.771 -16.363 -25.999 1.00 15.11 ? 112 THR A OG1 1 
ATOM   856  C  CG2 . THR A 1 112 ? 30.765 -14.031 -25.154 1.00 14.33 ? 112 THR A CG2 1 
ATOM   857  N  N   . PHE A 1 113 ? 31.724 -17.878 -23.200 1.00 14.17 ? 113 PHE A N   1 
ATOM   858  C  CA  . PHE A 1 113 ? 31.766 -19.307 -22.930 1.00 14.43 ? 113 PHE A CA  1 
ATOM   859  C  C   . PHE A 1 113 ? 31.031 -20.133 -23.978 1.00 14.44 ? 113 PHE A C   1 
ATOM   860  O  O   . PHE A 1 113 ? 31.125 -21.366 -23.929 1.00 15.96 ? 113 PHE A O   1 
ATOM   861  C  CB  . PHE A 1 113 ? 31.092 -19.585 -21.571 1.00 14.93 ? 113 PHE A CB  1 
ATOM   862  C  CG  . PHE A 1 113 ? 31.957 -19.318 -20.368 1.00 15.82 ? 113 PHE A CG  1 
ATOM   863  C  CD1 . PHE A 1 113 ? 32.067 -18.043 -19.841 1.00 15.36 ? 113 PHE A CD1 1 
ATOM   864  C  CD2 . PHE A 1 113 ? 32.554 -20.380 -19.696 1.00 18.76 ? 113 PHE A CD2 1 
ATOM   865  C  CE1 . PHE A 1 113 ? 32.865 -17.805 -18.733 1.00 16.18 ? 113 PHE A CE1 1 
ATOM   866  C  CE2 . PHE A 1 113 ? 33.320 -20.158 -18.568 1.00 20.14 ? 113 PHE A CE2 1 
ATOM   867  C  CZ  . PHE A 1 113 ? 33.486 -18.867 -18.097 1.00 19.02 ? 113 PHE A CZ  1 
ATOM   868  N  N   . ALA A 1 114 ? 30.313 -19.530 -24.922 1.00 14.83 ? 114 ALA A N   1 
ATOM   869  C  CA  . ALA A 1 114 ? 29.557 -20.358 -25.878 1.00 16.09 ? 114 ALA A CA  1 
ATOM   870  C  C   . ALA A 1 114 ? 30.451 -21.235 -26.729 1.00 17.84 ? 114 ALA A C   1 
ATOM   871  O  O   . ALA A 1 114 ? 31.514 -20.778 -27.182 1.00 19.79 ? 114 ALA A O   1 
ATOM   872  C  CB  . ALA A 1 114 ? 28.683 -19.507 -26.775 1.00 16.98 ? 114 ALA A CB  1 
ATOM   873  O  OXT . ALA A 1 114 ? 30.069 -22.404 -26.996 1.00 18.21 ? 114 ALA A OXT 1 
ATOM   874  N  N   . PRO B 1 1   ? 10.073 -7.764  -3.063  1.00 15.95 ? 1   PRO B N   1 
ATOM   875  C  CA  . PRO B 1 1   ? 10.755 -7.069  -4.165  1.00 16.00 ? 1   PRO B CA  1 
ATOM   876  C  C   . PRO B 1 1   ? 11.973 -6.338  -3.685  1.00 15.99 ? 1   PRO B C   1 
ATOM   877  O  O   . PRO B 1 1   ? 12.144 -6.125  -2.496  1.00 15.70 ? 1   PRO B O   1 
ATOM   878  C  CB  . PRO B 1 1   ? 9.704  -6.081  -4.644  1.00 17.07 ? 1   PRO B CB  1 
ATOM   879  C  CG  . PRO B 1 1   ? 8.392  -6.753  -4.325  1.00 18.30 ? 1   PRO B CG  1 
ATOM   880  C  CD  . PRO B 1 1   ? 8.644  -7.419  -2.996  1.00 17.65 ? 1   PRO B CD  1 
ATOM   881  N  N   . MET B 1 2   ? 12.803 -5.926  -4.632  1.00 15.80 ? 2   MET B N   1 
ATOM   882  C  CA  . MET B 1 2   ? 14.055 -5.242  -4.346  1.00 17.01 ? 2   MET B CA  1 
ATOM   883  C  C   . MET B 1 2   ? 14.165 -4.080  -5.320  1.00 15.34 ? 2   MET B C   1 
ATOM   884  O  O   . MET B 1 2   ? 13.943 -4.263  -6.523  1.00 14.97 ? 2   MET B O   1 
ATOM   885  C  CB  . MET B 1 2   ? 15.176 -6.259  -4.615  1.00 21.77 ? 2   MET B CB  1 
ATOM   886  C  CG  . MET B 1 2   ? 16.562 -5.836  -4.538  1.00 25.31 ? 2   MET B CG  1 
ATOM   887  S  SD  . MET B 1 2   ? 17.496 -7.301  -5.088  1.00 25.92 ? 2   MET B SD  1 
ATOM   888  C  CE  . MET B 1 2   ? 16.783 -8.663  -4.193  1.00 25.13 ? 2   MET B CE  1 
ATOM   889  N  N   . PHE B 1 3   ? 14.453 -2.887  -4.797  1.00 14.38 ? 3   PHE B N   1 
ATOM   890  C  CA  . PHE B 1 3   ? 14.689 -1.714  -5.627  1.00 13.72 ? 3   PHE B CA  1 
ATOM   891  C  C   . PHE B 1 3   ? 16.050 -1.155  -5.296  1.00 13.36 ? 3   PHE B C   1 
ATOM   892  O  O   . PHE B 1 3   ? 16.346 -0.869  -4.126  1.00 14.46 ? 3   PHE B O   1 
ATOM   893  C  CB  . PHE B 1 3   ? 13.592 -0.672  -5.410  1.00 15.14 ? 3   PHE B CB  1 
ATOM   894  C  CG  . PHE B 1 3   ? 13.781 0.548   -6.233  1.00 15.76 ? 3   PHE B CG  1 
ATOM   895  C  CD1 . PHE B 1 3   ? 13.629 0.494   -7.610  1.00 15.98 ? 3   PHE B CD1 1 
ATOM   896  C  CD2 . PHE B 1 3   ? 14.175 1.737   -5.643  1.00 18.19 ? 3   PHE B CD2 1 
ATOM   897  C  CE1 . PHE B 1 3   ? 13.824 1.607   -8.390  1.00 17.09 ? 3   PHE B CE1 1 
ATOM   898  C  CE2 . PHE B 1 3   ? 14.365 2.861   -6.406  1.00 19.58 ? 3   PHE B CE2 1 
ATOM   899  C  CZ  . PHE B 1 3   ? 14.205 2.797   -7.802  1.00 19.19 ? 3   PHE B CZ  1 
ATOM   900  N  N   . ILE B 1 4   ? 16.847 -0.966  -6.340  1.00 12.97 ? 4   ILE B N   1 
ATOM   901  C  CA  . ILE B 1 4   ? 18.200 -0.447  -6.213  1.00 13.34 ? 4   ILE B CA  1 
ATOM   902  C  C   . ILE B 1 4   ? 18.315 0.809   -7.065  1.00 13.90 ? 4   ILE B C   1 
ATOM   903  O  O   . ILE B 1 4   ? 17.915 0.803   -8.228  1.00 14.07 ? 4   ILE B O   1 
ATOM   904  C  CB  . ILE B 1 4   ? 19.236 -1.488  -6.686  1.00 14.50 ? 4   ILE B CB  1 
ATOM   905  C  CG1 . ILE B 1 4   ? 19.053 -2.840  -5.969  1.00 16.66 ? 4   ILE B CG1 1 
ATOM   906  C  CG2 . ILE B 1 4   ? 20.636 -0.957  -6.471  1.00 15.59 ? 4   ILE B CG2 1 
ATOM   907  C  CD1 . ILE B 1 4   ? 19.720 -3.986  -6.705  1.00 19.39 ? 4   ILE B CD1 1 
ATOM   908  N  N   . VAL B 1 5   ? 18.900 1.863   -6.508  1.00 13.91 ? 5   VAL B N   1 
ATOM   909  C  CA  . VAL B 1 5   ? 19.213 3.066   -7.280  1.00 15.17 ? 5   VAL B CA  1 
ATOM   910  C  C   . VAL B 1 5   ? 20.678 3.396   -7.111  1.00 14.29 ? 5   VAL B C   1 
ATOM   911  O  O   . VAL B 1 5   ? 21.155 3.534   -5.980  1.00 14.93 ? 5   VAL B O   1 
ATOM   912  C  CB  . VAL B 1 5   ? 18.327 4.270   -6.897  1.00 18.56 ? 5   VAL B CB  1 
ATOM   913  C  CG1 . VAL B 1 5   ? 18.215 4.456   -5.447  1.00 21.89 ? 5   VAL B CG1 1 
ATOM   914  C  CG2 . VAL B 1 5   ? 18.856 5.580   -7.516  1.00 18.68 ? 5   VAL B CG2 1 
ATOM   915  N  N   . ASN B 1 6   ? 21.388 3.496   -8.232  1.00 12.87 ? 6   ASN B N   1 
ATOM   916  C  CA  . ASN B 1 6   ? 22.765 3.961   -8.265  1.00 13.40 ? 6   ASN B CA  1 
ATOM   917  C  C   . ASN B 1 6   ? 22.769 5.341   -8.883  1.00 13.39 ? 6   ASN B C   1 
ATOM   918  O  O   . ASN B 1 6   ? 22.171 5.539   -9.938  1.00 14.04 ? 6   ASN B O   1 
ATOM   919  C  CB  . ASN B 1 6   ? 23.635 3.019   -9.098  1.00 14.57 ? 6   ASN B CB  1 
ATOM   920  C  CG  . ASN B 1 6   ? 24.179 1.853   -8.253  1.00 17.38 ? 6   ASN B CG  1 
ATOM   921  O  OD1 . ASN B 1 6   ? 25.273 1.952   -7.709  1.00 18.73 ? 6   ASN B OD1 1 
ATOM   922  N  ND2 . ASN B 1 6   ? 23.430 0.801   -8.125  1.00 18.76 ? 6   ASN B ND2 1 
ATOM   923  N  N   . THR B 1 7   ? 23.445 6.299   -8.246  1.00 13.25 ? 7   THR B N   1 
ATOM   924  C  CA  . THR B 1 7   ? 23.367 7.657   -8.739  1.00 13.72 ? 7   THR B CA  1 
ATOM   925  C  C   . THR B 1 7   ? 24.674 8.364   -8.425  1.00 14.20 ? 7   THR B C   1 
ATOM   926  O  O   . THR B 1 7   ? 25.401 7.990   -7.490  1.00 14.23 ? 7   THR B O   1 
ATOM   927  C  CB  . THR B 1 7   ? 22.166 8.401   -8.124  1.00 14.30 ? 7   THR B CB  1 
ATOM   928  O  OG1 . THR B 1 7   ? 22.163 9.749   -8.592  1.00 14.74 ? 7   THR B OG1 1 
ATOM   929  C  CG2 . THR B 1 7   ? 22.248 8.425   -6.604  1.00 15.50 ? 7   THR B CG2 1 
ATOM   930  N  N   . ASN B 1 8   ? 24.977 9.386   -9.239  1.00 14.79 ? 8   ASN B N   1 
ATOM   931  C  CA  . ASN B 1 8   ? 26.121 10.251  -9.005  1.00 15.81 ? 8   ASN B CA  1 
ATOM   932  C  C   . ASN B 1 8   ? 25.798 11.401  -8.061  1.00 17.66 ? 8   ASN B C   1 
ATOM   933  O  O   . ASN B 1 8   ? 26.714 12.124  -7.648  1.00 19.63 ? 8   ASN B O   1 
ATOM   934  C  CB  . ASN B 1 8   ? 26.720 10.760  -10.329 1.00 16.53 ? 8   ASN B CB  1 
ATOM   935  C  CG  . ASN B 1 8   ? 25.716 11.471  -11.225 1.00 16.53 ? 8   ASN B CG  1 
ATOM   936  O  OD1 . ASN B 1 8   ? 24.514 11.440  -11.004 1.00 16.16 ? 8   ASN B OD1 1 
ATOM   937  N  ND2 . ASN B 1 8   ? 26.225 12.095  -12.290 1.00 17.70 ? 8   ASN B ND2 1 
ATOM   938  N  N   . VAL B 1 9   ? 24.542 11.565  -7.668  1.00 17.22 ? 9   VAL B N   1 
ATOM   939  C  CA  . VAL B 1 9   ? 24.249 12.663  -6.743  1.00 18.51 ? 9   VAL B CA  1 
ATOM   940  C  C   . VAL B 1 9   ? 24.898 12.379  -5.393  1.00 18.77 ? 9   VAL B C   1 
ATOM   941  O  O   . VAL B 1 9   ? 25.011 11.213  -4.986  1.00 18.85 ? 9   VAL B O   1 
ATOM   942  C  CB  . VAL B 1 9   ? 22.745 12.961  -6.625  1.00 20.79 ? 9   VAL B CB  1 
ATOM   943  C  CG1 . VAL B 1 9   ? 22.100 13.216  -7.977  1.00 20.86 ? 9   VAL B CG1 1 
ATOM   944  C  CG2 . VAL B 1 9   ? 22.048 11.891  -5.901  1.00 22.04 ? 9   VAL B CG2 1 
ATOM   945  N  N   . PRO B 1 10  ? 25.352 13.395  -4.674  1.00 20.43 ? 10  PRO B N   1 
ATOM   946  C  CA  . PRO B 1 10  ? 26.070 13.138  -3.426  1.00 21.55 ? 10  PRO B CA  1 
ATOM   947  C  C   . PRO B 1 10  ? 25.155 12.652  -2.310  1.00 21.69 ? 10  PRO B C   1 
ATOM   948  O  O   . PRO B 1 10  ? 23.949 12.913  -2.286  1.00 21.36 ? 10  PRO B O   1 
ATOM   949  C  CB  . PRO B 1 10  ? 26.729 14.480  -3.101  1.00 23.41 ? 10  PRO B CB  1 
ATOM   950  C  CG  . PRO B 1 10  ? 25.963 15.473  -3.821  1.00 23.26 ? 10  PRO B CG  1 
ATOM   951  C  CD  . PRO B 1 10  ? 25.324 14.819  -5.024  1.00 21.96 ? 10  PRO B CD  1 
ATOM   952  N  N   . ARG B 1 11  ? 25.772 11.937  -1.360  1.00 22.01 ? 11  ARG B N   1 
ATOM   953  C  CA  . ARG B 1 11  ? 25.031 11.345  -0.249  1.00 24.36 ? 11  ARG B CA  1 
ATOM   954  C  C   . ARG B 1 11  ? 24.252 12.393  0.536   1.00 24.21 ? 11  ARG B C   1 
ATOM   955  O  O   . ARG B 1 11  ? 23.143 12.122  1.009   1.00 23.79 ? 11  ARG B O   1 
ATOM   956  C  CB  . ARG B 1 11  ? 25.982 10.576  0.679   1.00 27.21 ? 11  ARG B CB  1 
ATOM   957  C  CG  . ARG B 1 11  ? 25.393 10.174  2.035   1.00 31.67 ? 11  ARG B CG  1 
ATOM   958  C  CD  . ARG B 1 11  ? 24.377 9.049   1.909   1.00 35.74 ? 11  ARG B CD  1 
ATOM   959  N  NE  . ARG B 1 11  ? 23.777 8.684   3.199   1.00 38.95 ? 11  ARG B NE  1 
ATOM   960  C  CZ  . ARG B 1 11  ? 22.641 9.201   3.662   1.00 40.89 ? 11  ARG B CZ  1 
ATOM   961  N  NH1 . ARG B 1 11  ? 21.981 10.109  2.948   1.00 41.54 ? 11  ARG B NH1 1 
ATOM   962  N  NH2 . ARG B 1 11  ? 22.154 8.806   4.832   1.00 41.40 ? 11  ARG B NH2 1 
ATOM   963  N  N   . ALA B 1 12  ? 24.813 13.591  0.701   1.00 24.87 ? 12  ALA B N   1 
ATOM   964  C  CA  . ALA B 1 12  ? 24.136 14.607  1.495   1.00 25.73 ? 12  ALA B CA  1 
ATOM   965  C  C   . ALA B 1 12  ? 22.858 15.087  0.837   1.00 26.43 ? 12  ALA B C   1 
ATOM   966  O  O   . ALA B 1 12  ? 22.022 15.699  1.507   1.00 27.78 ? 12  ALA B O   1 
ATOM   967  C  CB  . ALA B 1 12  ? 25.070 15.795  1.728   1.00 26.26 ? 12  ALA B CB  1 
ATOM   968  N  N   A SER B 1 13  ? 22.688 14.863  -0.458  0.54 26.02 ? 13  SER B N   1 
ATOM   969  N  N   B SER B 1 13  ? 22.700 14.850  -0.460  0.46 26.36 ? 13  SER B N   1 
ATOM   970  C  CA  A SER B 1 13  ? 21.469 15.278  -1.134  0.54 26.03 ? 13  SER B CA  1 
ATOM   971  C  CA  B SER B 1 13  ? 21.511 15.249  -1.194  0.46 26.60 ? 13  SER B CA  1 
ATOM   972  C  C   A SER B 1 13  ? 20.357 14.240  -1.050  0.54 26.26 ? 13  SER B C   1 
ATOM   973  C  C   B SER B 1 13  ? 20.423 14.181  -1.197  0.46 26.47 ? 13  SER B C   1 
ATOM   974  O  O   A SER B 1 13  ? 19.220 14.534  -1.438  0.54 27.15 ? 13  SER B O   1 
ATOM   975  O  O   B SER B 1 13  ? 19.362 14.392  -1.799  0.46 27.22 ? 13  SER B O   1 
ATOM   976  C  CB  A SER B 1 13  ? 21.758 15.638  -2.596  0.54 25.94 ? 13  SER B CB  1 
ATOM   977  C  CB  B SER B 1 13  ? 21.885 15.648  -2.629  0.46 27.13 ? 13  SER B CB  1 
ATOM   978  O  OG  A SER B 1 13  ? 21.908 14.475  -3.383  0.54 25.28 ? 13  SER B OG  1 
ATOM   979  O  OG  B SER B 1 13  ? 22.764 16.765  -2.640  0.46 27.24 ? 13  SER B OG  1 
ATOM   980  N  N   . VAL B 1 14  ? 20.647 13.050  -0.542  1.00 25.74 ? 14  VAL B N   1 
ATOM   981  C  CA  . VAL B 1 14  ? 19.601 12.039  -0.359  1.00 25.57 ? 14  VAL B CA  1 
ATOM   982  C  C   . VAL B 1 14  ? 18.845 12.389  0.910   1.00 26.24 ? 14  VAL B C   1 
ATOM   983  O  O   . VAL B 1 14  ? 19.445 12.423  1.997   1.00 27.20 ? 14  VAL B O   1 
ATOM   984  C  CB  . VAL B 1 14  ? 20.191 10.625  -0.261  1.00 25.49 ? 14  VAL B CB  1 
ATOM   985  C  CG1 . VAL B 1 14  ? 19.053 9.586   -0.097  1.00 25.85 ? 14  VAL B CG1 1 
ATOM   986  C  CG2 . VAL B 1 14  ? 21.024 10.326  -1.484  1.00 24.62 ? 14  VAL B CG2 1 
ATOM   987  N  N   . PRO B 1 15  ? 17.559 12.712  0.834   1.00 26.18 ? 15  PRO B N   1 
ATOM   988  C  CA  . PRO B 1 15  ? 16.884 13.206  2.034   1.00 27.78 ? 15  PRO B CA  1 
ATOM   989  C  C   . PRO B 1 15  ? 16.701 12.133  3.095   1.00 28.76 ? 15  PRO B C   1 
ATOM   990  O  O   . PRO B 1 15  ? 16.584 10.939  2.805   1.00 28.15 ? 15  PRO B O   1 
ATOM   991  C  CB  . PRO B 1 15  ? 15.541 13.720  1.503   1.00 28.16 ? 15  PRO B CB  1 
ATOM   992  C  CG  . PRO B 1 15  ? 15.318 13.062  0.265   1.00 27.89 ? 15  PRO B CG  1 
ATOM   993  C  CD  . PRO B 1 15  ? 16.685 12.756  -0.349  1.00 26.70 ? 15  PRO B CD  1 
ATOM   994  N  N   . ASP B 1 16  ? 16.680 12.583  4.345   1.00 30.87 ? 16  ASP B N   1 
ATOM   995  C  CA  . ASP B 1 16  ? 16.322 11.695  5.437   1.00 33.18 ? 16  ASP B CA  1 
ATOM   996  C  C   . ASP B 1 16  ? 14.954 11.100  5.157   1.00 32.40 ? 16  ASP B C   1 
ATOM   997  O  O   . ASP B 1 16  ? 14.023 11.794  4.739   1.00 33.43 ? 16  ASP B O   1 
ATOM   998  C  CB  . ASP B 1 16  ? 16.271 12.462  6.760   1.00 35.96 ? 16  ASP B CB  1 
ATOM   999  C  CG  . ASP B 1 16  ? 17.652 12.868  7.273   1.00 39.30 ? 16  ASP B CG  1 
ATOM   1000 O  OD1 . ASP B 1 16  ? 17.698 13.592  8.287   1.00 40.49 ? 16  ASP B OD1 1 
ATOM   1001 O  OD2 . ASP B 1 16  ? 18.680 12.490  6.663   1.00 40.95 ? 16  ASP B OD2 1 
ATOM   1002 N  N   . GLY B 1 17  ? 14.820 9.815   5.415   1.00 29.94 ? 17  GLY B N   1 
ATOM   1003 C  CA  . GLY B 1 17  ? 13.555 9.174   5.172   1.00 27.68 ? 17  GLY B CA  1 
ATOM   1004 C  C   . GLY B 1 17  ? 13.346 8.689   3.752   1.00 25.55 ? 17  GLY B C   1 
ATOM   1005 O  O   . GLY B 1 17  ? 12.302 8.079   3.476   1.00 26.01 ? 17  GLY B O   1 
ATOM   1006 N  N   . PHE B 1 18  ? 14.329 8.862   2.860   1.00 23.78 ? 18  PHE B N   1 
ATOM   1007 C  CA  . PHE B 1 18  ? 14.146 8.430   1.474   1.00 22.19 ? 18  PHE B CA  1 
ATOM   1008 C  C   . PHE B 1 18  ? 13.959 6.913   1.372   1.00 21.46 ? 18  PHE B C   1 
ATOM   1009 O  O   . PHE B 1 18  ? 13.135 6.436   0.579   1.00 20.93 ? 18  PHE B O   1 
ATOM   1010 C  CB  . PHE B 1 18  ? 15.349 8.887   0.650   1.00 21.87 ? 18  PHE B CB  1 
ATOM   1011 C  CG  . PHE B 1 18  ? 15.213 8.691   -0.838  1.00 22.61 ? 18  PHE B CG  1 
ATOM   1012 C  CD1 . PHE B 1 18  ? 14.138 9.232   -1.526  1.00 24.09 ? 18  PHE B CD1 1 
ATOM   1013 C  CD2 . PHE B 1 18  ? 16.179 7.986   -1.550  1.00 22.93 ? 18  PHE B CD2 1 
ATOM   1014 C  CE1 . PHE B 1 18  ? 14.025 9.079   -2.897  1.00 24.70 ? 18  PHE B CE1 1 
ATOM   1015 C  CE2 . PHE B 1 18  ? 16.080 7.825   -2.922  1.00 23.98 ? 18  PHE B CE2 1 
ATOM   1016 C  CZ  . PHE B 1 18  ? 15.001 8.385   -3.598  1.00 24.18 ? 18  PHE B CZ  1 
ATOM   1017 N  N   . LEU B 1 19  ? 14.739 6.131   2.131   1.00 20.51 ? 19  LEU B N   1 
ATOM   1018 C  CA  . LEU B 1 19  ? 14.553 4.676   2.067   1.00 20.77 ? 19  LEU B CA  1 
ATOM   1019 C  C   . LEU B 1 19  ? 13.153 4.280   2.508   1.00 21.55 ? 19  LEU B C   1 
ATOM   1020 O  O   . LEU B 1 19  ? 12.545 3.374   1.929   1.00 21.46 ? 19  LEU B O   1 
ATOM   1021 C  CB  . LEU B 1 19  ? 15.576 3.935   2.934   1.00 21.70 ? 19  LEU B CB  1 
ATOM   1022 C  CG  . LEU B 1 19  ? 17.052 3.992   2.549   1.00 23.40 ? 19  LEU B CG  1 
ATOM   1023 C  CD1 . LEU B 1 19  ? 17.881 3.142   3.498   1.00 24.56 ? 19  LEU B CD1 1 
ATOM   1024 C  CD2 . LEU B 1 19  ? 17.244 3.522   1.132   1.00 24.44 ? 19  LEU B CD2 1 
ATOM   1025 N  N   A SER B 1 20  ? 12.641 4.925   3.553   0.56 22.45 ? 20  SER B N   1 
ATOM   1026 N  N   B SER B 1 20  ? 12.640 4.922   3.555   0.44 22.47 ? 20  SER B N   1 
ATOM   1027 C  CA  A SER B 1 20  ? 11.296 4.617   4.021   0.56 23.76 ? 20  SER B CA  1 
ATOM   1028 C  CA  B SER B 1 20  ? 11.291 4.612   4.014   0.44 23.77 ? 20  SER B CA  1 
ATOM   1029 C  C   A SER B 1 20  ? 10.251 5.023   2.993   0.56 22.71 ? 20  SER B C   1 
ATOM   1030 C  C   B SER B 1 20  ? 10.250 5.021   2.985   0.44 22.75 ? 20  SER B C   1 
ATOM   1031 O  O   A SER B 1 20  ? 9.270  4.300   2.783   0.56 22.84 ? 20  SER B O   1 
ATOM   1032 O  O   B SER B 1 20  ? 9.265  4.302   2.774   0.44 22.85 ? 20  SER B O   1 
ATOM   1033 C  CB  A SER B 1 20  ? 11.048 5.301   5.361   0.56 26.42 ? 20  SER B CB  1 
ATOM   1034 C  CB  B SER B 1 20  ? 11.026 5.279   5.359   0.44 26.45 ? 20  SER B CB  1 
ATOM   1035 O  OG  A SER B 1 20  ? 9.699  5.148   5.776   0.56 28.86 ? 20  SER B OG  1 
ATOM   1036 O  OG  B SER B 1 20  ? 11.734 4.623   6.392   0.44 28.94 ? 20  SER B OG  1 
ATOM   1037 N  N   . GLU B 1 21  ? 10.454 6.164   2.326   1.00 22.56 ? 21  GLU B N   1 
ATOM   1038 C  CA  . GLU B 1 21  ? 9.523  6.586   1.286   1.00 22.43 ? 21  GLU B CA  1 
ATOM   1039 C  C   . GLU B 1 21  ? 9.511  5.605   0.127   1.00 21.00 ? 21  GLU B C   1 
ATOM   1040 O  O   . GLU B 1 21  ? 8.447  5.236   -0.386  1.00 20.65 ? 21  GLU B O   1 
ATOM   1041 C  CB  . GLU B 1 21  ? 9.880  7.985   0.796   1.00 24.18 ? 21  GLU B CB  1 
ATOM   1042 C  CG  . GLU B 1 21  ? 8.794  8.540   -0.110  1.00 26.76 ? 21  GLU B CG  1 
ATOM   1043 C  CD  . GLU B 1 21  ? 9.045  9.969   -0.552  1.00 28.72 ? 21  GLU B CD  1 
ATOM   1044 O  OE1 . GLU B 1 21  ? 8.044  10.683  -0.838  1.00 30.11 ? 21  GLU B OE1 1 
ATOM   1045 O  OE2 . GLU B 1 21  ? 10.224 10.388  -0.571  1.00 28.59 ? 21  GLU B OE2 1 
ATOM   1046 N  N   . LEU B 1 22  ? 10.696 5.187   -0.317  1.00 19.58 ? 22  LEU B N   1 
ATOM   1047 C  CA  . LEU B 1 22  ? 10.746 4.186   -1.372  1.00 19.25 ? 22  LEU B CA  1 
ATOM   1048 C  C   . LEU B 1 22  ? 10.052 2.909   -0.932  1.00 19.02 ? 22  LEU B C   1 
ATOM   1049 O  O   . LEU B 1 22  ? 9.301  2.312   -1.708  1.00 18.95 ? 22  LEU B O   1 
ATOM   1050 C  CB  . LEU B 1 22  ? 12.192 3.867   -1.730  1.00 19.07 ? 22  LEU B CB  1 
ATOM   1051 C  CG  . LEU B 1 22  ? 12.941 4.969   -2.485  1.00 19.73 ? 22  LEU B CG  1 
ATOM   1052 C  CD1 . LEU B 1 22  ? 14.396 4.589   -2.629  1.00 20.06 ? 22  LEU B CD1 1 
ATOM   1053 C  CD2 . LEU B 1 22  ? 12.287 5.206   -3.813  1.00 21.04 ? 22  LEU B CD2 1 
ATOM   1054 N  N   . THR B 1 23  ? 10.281 2.476   0.318   1.00 19.00 ? 23  THR B N   1 
ATOM   1055 C  CA  . THR B 1 23  ? 9.661  1.244   0.810   1.00 19.71 ? 23  THR B CA  1 
ATOM   1056 C  C   . THR B 1 23  ? 8.150  1.338   0.745   1.00 20.33 ? 23  THR B C   1 
ATOM   1057 O  O   . THR B 1 23  ? 7.477  0.436   0.238   1.00 20.67 ? 23  THR B O   1 
ATOM   1058 C  CB  . THR B 1 23  ? 10.115 0.947   2.254   1.00 18.77 ? 23  THR B CB  1 
ATOM   1059 O  OG1 . THR B 1 23  ? 11.545 0.765   2.278   1.00 18.62 ? 23  THR B OG1 1 
ATOM   1060 C  CG2 . THR B 1 23  ? 9.440  -0.306  2.798   1.00 19.08 ? 23  THR B CG2 1 
ATOM   1061 N  N   . GLN B 1 24  ? 7.600  2.426   1.277   1.00 20.68 ? 24  GLN B N   1 
ATOM   1062 C  CA  . GLN B 1 24  ? 6.152  2.557   1.356   1.00 21.95 ? 24  GLN B CA  1 
ATOM   1063 C  C   . GLN B 1 24  ? 5.544  2.771   -0.022  1.00 20.80 ? 24  GLN B C   1 
ATOM   1064 O  O   . GLN B 1 24  ? 4.495  2.200   -0.337  1.00 20.88 ? 24  GLN B O   1 
ATOM   1065 C  CB  . GLN B 1 24  ? 5.776  3.639   2.366   1.00 25.36 ? 24  GLN B CB  1 
ATOM   1066 C  CG  . GLN B 1 24  ? 6.171  3.295   3.834   1.00 29.47 ? 24  GLN B CG  1 
ATOM   1067 C  CD  . GLN B 1 24  ? 5.733  1.892   4.340   1.00 32.58 ? 24  GLN B CD  1 
ATOM   1068 O  OE1 . GLN B 1 24  ? 4.630  1.413   4.066   1.00 34.68 ? 24  GLN B OE1 1 
ATOM   1069 N  NE2 . GLN B 1 24  ? 6.604  1.261   5.107   1.00 32.84 ? 24  GLN B NE2 1 
ATOM   1070 N  N   . GLN B 1 25  ? 6.184  3.589   -0.860  1.00 20.36 ? 25  GLN B N   1 
ATOM   1071 C  CA  . GLN B 1 25  ? 5.620  3.830   -2.182  1.00 21.29 ? 25  GLN B CA  1 
ATOM   1072 C  C   . GLN B 1 25  ? 5.663  2.572   -3.031  1.00 19.79 ? 25  GLN B C   1 
ATOM   1073 O  O   . GLN B 1 25  ? 4.742  2.314   -3.819  1.00 19.63 ? 25  GLN B O   1 
ATOM   1074 C  CB  . GLN B 1 25  ? 6.370  4.963   -2.885  1.00 24.21 ? 25  GLN B CB  1 
ATOM   1075 C  CG  . GLN B 1 25  ? 6.149  6.342   -2.275  1.00 27.95 ? 25  GLN B CG  1 
ATOM   1076 C  CD  . GLN B 1 25  ? 4.724  6.778   -2.444  1.00 31.17 ? 25  GLN B CD  1 
ATOM   1077 O  OE1 . GLN B 1 25  ? 4.230  6.885   -3.573  1.00 32.72 ? 25  GLN B OE1 1 
ATOM   1078 N  NE2 . GLN B 1 25  ? 4.055  7.068   -1.335  1.00 31.99 ? 25  GLN B NE2 1 
ATOM   1079 N  N   . LEU B 1 26  ? 6.724  1.775   -2.883  1.00 19.44 ? 26  LEU B N   1 
ATOM   1080 C  CA  . LEU B 1 26  ? 6.807  0.523   -3.629  1.00 19.33 ? 26  LEU B CA  1 
ATOM   1081 C  C   . LEU B 1 26  ? 5.846  -0.529  -3.095  1.00 20.09 ? 26  LEU B C   1 
ATOM   1082 O  O   . LEU B 1 26  ? 5.302  -1.320  -3.877  1.00 20.71 ? 26  LEU B O   1 
ATOM   1083 C  CB  . LEU B 1 26  ? 8.243  0.006   -3.637  1.00 18.80 ? 26  LEU B CB  1 
ATOM   1084 C  CG  . LEU B 1 26  ? 9.131  0.783   -4.608  1.00 20.26 ? 26  LEU B CG  1 
ATOM   1085 C  CD1 . LEU B 1 26  ? 10.592 0.499   -4.297  1.00 21.41 ? 26  LEU B CD1 1 
ATOM   1086 C  CD2 . LEU B 1 26  ? 8.782  0.462   -6.061  1.00 21.74 ? 26  LEU B CD2 1 
ATOM   1087 N  N   . ALA B 1 27  ? 5.645  -0.587  -1.768  1.00 19.47 ? 27  ALA B N   1 
ATOM   1088 C  CA  . ALA B 1 27  ? 4.651  -1.505  -1.216  1.00 19.94 ? 27  ALA B CA  1 
ATOM   1089 C  C   . ALA B 1 27  ? 3.288  -1.211  -1.812  1.00 21.18 ? 27  ALA B C   1 
ATOM   1090 O  O   . ALA B 1 27  ? 2.588  -2.115  -2.266  1.00 22.30 ? 27  ALA B O   1 
ATOM   1091 C  CB  . ALA B 1 27  ? 4.619  -1.401  0.307   1.00 20.25 ? 27  ALA B CB  1 
ATOM   1092 N  N   . GLN B 1 28  ? 2.922  0.068   -1.868  1.00 21.45 ? 28  GLN B N   1 
ATOM   1093 C  CA  . GLN B 1 28  ? 1.643  0.457   -2.443  1.00 22.90 ? 28  GLN B CA  1 
ATOM   1094 C  C   . GLN B 1 28  ? 1.580  0.161   -3.934  1.00 22.91 ? 28  GLN B C   1 
ATOM   1095 O  O   . GLN B 1 28  ? 0.562  -0.342  -4.431  1.00 24.07 ? 28  GLN B O   1 
ATOM   1096 C  CB  . GLN B 1 28  ? 1.375  1.937   -2.182  1.00 24.41 ? 28  GLN B CB  1 
ATOM   1097 C  CG  . GLN B 1 28  ? 1.244  2.284   -0.706  1.00 25.74 ? 28  GLN B CG  1 
ATOM   1098 N  N   . ALA B 1 29  ? 2.648  0.482   -4.666  1.00 21.67 ? 29  ALA B N   1 
ATOM   1099 C  CA  . ALA B 1 29  ? 2.627  0.333   -6.117  1.00 21.32 ? 29  ALA B CA  1 
ATOM   1100 C  C   . ALA B 1 29  ? 2.557  -1.133  -6.533  1.00 21.46 ? 29  ALA B C   1 
ATOM   1101 O  O   . ALA B 1 29  ? 1.839  -1.481  -7.482  1.00 21.25 ? 29  ALA B O   1 
ATOM   1102 C  CB  . ALA B 1 29  ? 3.865  1.014   -6.716  1.00 21.17 ? 29  ALA B CB  1 
ATOM   1103 N  N   . THR B 1 30  ? 3.316  -2.002  -5.857  1.00 21.78 ? 30  THR B N   1 
ATOM   1104 C  CA  . THR B 1 30  ? 3.354  -3.418  -6.184  1.00 22.39 ? 30  THR B CA  1 
ATOM   1105 C  C   . THR B 1 30  ? 2.244  -4.213  -5.522  1.00 23.06 ? 30  THR B C   1 
ATOM   1106 O  O   . THR B 1 30  ? 2.027  -5.359  -5.921  1.00 24.50 ? 30  THR B O   1 
ATOM   1107 C  CB  . THR B 1 30  ? 4.695  -4.044  -5.774  1.00 22.64 ? 30  THR B CB  1 
ATOM   1108 O  OG1 . THR B 1 30  ? 4.842  -3.992  -4.349  1.00 22.71 ? 30  THR B OG1 1 
ATOM   1109 C  CG2 . THR B 1 30  ? 5.892  -3.362  -6.483  1.00 23.56 ? 30  THR B CG2 1 
ATOM   1110 N  N   . GLY B 1 31  ? 1.568  -3.663  -4.515  1.00 22.48 ? 31  GLY B N   1 
ATOM   1111 C  CA  . GLY B 1 31  ? 0.599  -4.423  -3.746  1.00 22.80 ? 31  GLY B CA  1 
ATOM   1112 C  C   . GLY B 1 31  ? 1.180  -5.381  -2.720  1.00 24.08 ? 31  GLY B C   1 
ATOM   1113 O  O   . GLY B 1 31  ? 0.412  -6.072  -2.032  1.00 26.74 ? 31  GLY B O   1 
ATOM   1114 N  N   . LYS B 1 32  ? 2.481  -5.438  -2.581  1.00 23.22 ? 32  LYS B N   1 
ATOM   1115 C  CA  . LYS B 1 32  ? 3.180  -6.363  -1.694  1.00 22.80 ? 32  LYS B CA  1 
ATOM   1116 C  C   . LYS B 1 32  ? 3.336  -5.738  -0.308  1.00 20.34 ? 32  LYS B C   1 
ATOM   1117 O  O   . LYS B 1 32  ? 3.421  -4.506  -0.181  1.00 19.29 ? 32  LYS B O   1 
ATOM   1118 C  CB  . LYS B 1 32  ? 4.578  -6.630  -2.251  1.00 25.96 ? 32  LYS B CB  1 
ATOM   1119 C  CG  . LYS B 1 32  ? 4.630  -7.036  -3.726  1.00 28.71 ? 32  LYS B CG  1 
ATOM   1120 C  CD  . LYS B 1 32  ? 4.606  -8.502  -3.882  1.00 29.52 ? 32  LYS B CD  1 
ATOM   1121 C  CE  . LYS B 1 32  ? 4.933  -8.903  -5.316  1.00 29.12 ? 32  LYS B CE  1 
ATOM   1122 N  NZ  . LYS B 1 32  ? 4.894  -10.362 -5.390  1.00 29.05 ? 32  LYS B NZ  1 
ATOM   1123 N  N   . PRO B 1 33  ? 3.423  -6.542  0.750   1.00 20.26 ? 33  PRO B N   1 
ATOM   1124 C  CA  . PRO B 1 33  ? 3.620  -5.985  2.092   1.00 19.89 ? 33  PRO B CA  1 
ATOM   1125 C  C   . PRO B 1 33  ? 4.965  -5.285  2.183   1.00 17.83 ? 33  PRO B C   1 
ATOM   1126 O  O   . PRO B 1 33  ? 5.982  -5.757  1.638   1.00 17.55 ? 33  PRO B O   1 
ATOM   1127 C  CB  . PRO B 1 33  ? 3.639  -7.226  2.995   1.00 21.57 ? 33  PRO B CB  1 
ATOM   1128 C  CG  . PRO B 1 33  ? 3.129  -8.352  2.148   1.00 22.34 ? 33  PRO B CG  1 
ATOM   1129 C  CD  . PRO B 1 33  ? 3.484  -8.014  0.744   1.00 21.79 ? 33  PRO B CD  1 
ATOM   1130 N  N   . PRO B 1 34  ? 5.032  -4.188  2.927   1.00 17.25 ? 34  PRO B N   1 
ATOM   1131 C  CA  . PRO B 1 34  ? 6.326  -3.501  3.095   1.00 16.71 ? 34  PRO B CA  1 
ATOM   1132 C  C   . PRO B 1 34  ? 7.404  -4.402  3.684   1.00 15.54 ? 34  PRO B C   1 
ATOM   1133 O  O   . PRO B 1 34  ? 8.594  -4.197  3.394   1.00 15.32 ? 34  PRO B O   1 
ATOM   1134 C  CB  . PRO B 1 34  ? 5.990  -2.298  3.994   1.00 18.75 ? 34  PRO B CB  1 
ATOM   1135 C  CG  . PRO B 1 34  ? 4.626  -2.503  4.458   1.00 19.78 ? 34  PRO B CG  1 
ATOM   1136 C  CD  . PRO B 1 34  ? 3.918  -3.474  3.574   1.00 18.49 ? 34  PRO B CD  1 
ATOM   1137 N  N   . GLN B 1 35  ? 7.028  -5.400  4.497   1.00 15.73 ? 35  GLN B N   1 
ATOM   1138 C  CA  . GLN B 1 35  ? 7.982  -6.331  5.080   1.00 15.51 ? 35  GLN B CA  1 
ATOM   1139 C  C   . GLN B 1 35  ? 8.815  -7.041  4.027   1.00 14.90 ? 35  GLN B C   1 
ATOM   1140 O  O   . GLN B 1 35  ? 9.907  -7.524  4.333   1.00 16.00 ? 35  GLN B O   1 
ATOM   1141 C  CB  . GLN B 1 35  ? 7.260  -7.353  5.964   1.00 16.38 ? 35  GLN B CB  1 
ATOM   1142 C  CG  . GLN B 1 35  ? 6.715  -6.749  7.265   1.00 18.28 ? 35  GLN B CG  1 
ATOM   1143 C  CD  . GLN B 1 35  ? 5.327  -6.175  7.126   1.00 19.65 ? 35  GLN B CD  1 
ATOM   1144 O  OE1 . GLN B 1 35  ? 4.768  -6.073  6.032   1.00 18.77 ? 35  GLN B OE1 1 
ATOM   1145 N  NE2 . GLN B 1 35  ? 4.774  -5.750  8.253   1.00 21.15 ? 35  GLN B NE2 1 
ATOM   1146 N  N   . TYR B 1 36  ? 8.307  -7.160  2.806   1.00 13.88 ? 36  TYR B N   1 
ATOM   1147 C  CA  . TYR B 1 36  ? 8.978  -7.862  1.729   1.00 14.41 ? 36  TYR B CA  1 
ATOM   1148 C  C   . TYR B 1 36  ? 9.720  -6.933  0.786   1.00 14.57 ? 36  TYR B C   1 
ATOM   1149 O  O   . TYR B 1 36  ? 10.349 -7.416  -0.162  1.00 15.64 ? 36  TYR B O   1 
ATOM   1150 C  CB  . TYR B 1 36  ? 7.982  -8.716  0.958   1.00 16.58 ? 36  TYR B CB  1 
ATOM   1151 C  CG  . TYR B 1 36  ? 7.562  -9.937  1.718   1.00 19.85 ? 36  TYR B CG  1 
ATOM   1152 C  CD1 . TYR B 1 36  ? 6.530  -9.884  2.611   1.00 21.85 ? 36  TYR B CD1 1 
ATOM   1153 C  CD2 . TYR B 1 36  ? 8.237  -11.139 1.561   1.00 22.74 ? 36  TYR B CD2 1 
ATOM   1154 C  CE1 . TYR B 1 36  ? 6.152  -11.008 3.323   1.00 23.35 ? 36  TYR B CE1 1 
ATOM   1155 C  CE2 . TYR B 1 36  ? 7.871  -12.288 2.273   1.00 24.49 ? 36  TYR B CE2 1 
ATOM   1156 C  CZ  . TYR B 1 36  ? 6.820  -12.218 3.165   1.00 24.93 ? 36  TYR B CZ  1 
ATOM   1157 O  OH  . TYR B 1 36  ? 6.431  -13.345 3.904   1.00 27.80 ? 36  TYR B OH  1 
ATOM   1158 N  N   . ILE B 1 37  ? 9.685  -5.623  1.003   1.00 13.51 ? 37  ILE B N   1 
ATOM   1159 C  CA  . ILE B 1 37  ? 10.335 -4.666  0.114   1.00 13.41 ? 37  ILE B CA  1 
ATOM   1160 C  C   . ILE B 1 37  ? 11.713 -4.341  0.665   1.00 13.30 ? 37  ILE B C   1 
ATOM   1161 O  O   . ILE B 1 37  ? 11.837 -3.908  1.816   1.00 14.39 ? 37  ILE B O   1 
ATOM   1162 C  CB  . ILE B 1 37  ? 9.516  -3.367  0.009   1.00 15.70 ? 37  ILE B CB  1 
ATOM   1163 C  CG1 . ILE B 1 37  ? 8.097  -3.634  -0.499  1.00 18.57 ? 37  ILE B CG1 1 
ATOM   1164 C  CG2 . ILE B 1 37  ? 10.258 -2.362  -0.866  1.00 16.49 ? 37  ILE B CG2 1 
ATOM   1165 C  CD1 . ILE B 1 37  ? 8.038  -3.928  -1.910  1.00 20.68 ? 37  ILE B CD1 1 
ATOM   1166 N  N   . ALA B 1 38  ? 12.739 -4.517  -0.152  1.00 12.71 ? 38  ALA B N   1 
ATOM   1167 C  CA  . ALA B 1 38  ? 14.091 -4.125  0.214   1.00 13.11 ? 38  ALA B CA  1 
ATOM   1168 C  C   . ALA B 1 38  ? 14.509 -3.007  -0.725  1.00 13.12 ? 38  ALA B C   1 
ATOM   1169 O  O   . ALA B 1 38  ? 14.208 -3.054  -1.920  1.00 14.18 ? 38  ALA B O   1 
ATOM   1170 C  CB  . ALA B 1 38  ? 15.055 -5.311  0.063   1.00 14.16 ? 38  ALA B CB  1 
ATOM   1171 N  N   . VAL B 1 39  ? 15.226 -2.028  -0.188  1.00 13.14 ? 39  VAL B N   1 
ATOM   1172 C  CA  . VAL B 1 39  ? 15.647 -0.860  -0.957  1.00 14.30 ? 39  VAL B CA  1 
ATOM   1173 C  C   . VAL B 1 39  ? 17.118 -0.589  -0.692  1.00 14.62 ? 39  VAL B C   1 
ATOM   1174 O  O   . VAL B 1 39  ? 17.607 -0.766  0.427   1.00 15.50 ? 39  VAL B O   1 
ATOM   1175 C  CB  . VAL B 1 39  ? 14.783 0.382   -0.629  1.00 15.93 ? 39  VAL B CB  1 
ATOM   1176 C  CG1 . VAL B 1 39  ? 13.318 0.126   -1.012  1.00 16.67 ? 39  VAL B CG1 1 
ATOM   1177 C  CG2 . VAL B 1 39  ? 14.847 0.752   0.842   1.00 18.07 ? 39  VAL B CG2 1 
ATOM   1178 N  N   . HIS B 1 40  ? 17.819 -0.133  -1.729  1.00 13.96 ? 40  HIS B N   1 
ATOM   1179 C  CA  . HIS B 1 40  ? 19.249 0.117   -1.647  1.00 13.56 ? 40  HIS B CA  1 
ATOM   1180 C  C   . HIS B 1 40  ? 19.546 1.341   -2.494  1.00 13.43 ? 40  HIS B C   1 
ATOM   1181 O  O   . HIS B 1 40  ? 19.246 1.352   -3.689  1.00 13.88 ? 40  HIS B O   1 
ATOM   1182 C  CB  . HIS B 1 40  ? 19.950 -1.122  -2.217  1.00 14.37 ? 40  HIS B CB  1 
ATOM   1183 C  CG  . HIS B 1 40  ? 21.437 -1.068  -2.209  1.00 15.01 ? 40  HIS B CG  1 
ATOM   1184 N  ND1 . HIS B 1 40  ? 22.204 -2.004  -2.872  1.00 15.52 ? 40  HIS B ND1 1 
ATOM   1185 C  CD2 . HIS B 1 40  ? 22.306 -0.214  -1.629  1.00 15.46 ? 40  HIS B CD2 1 
ATOM   1186 C  CE1 . HIS B 1 40  ? 23.484 -1.735  -2.692  1.00 16.39 ? 40  HIS B CE1 1 
ATOM   1187 N  NE2 . HIS B 1 40  ? 23.576 -0.645  -1.950  1.00 15.85 ? 40  HIS B NE2 1 
ATOM   1188 N  N   . VAL B 1 41  ? 20.130 2.371   -1.879  1.00 14.52 ? 41  VAL B N   1 
ATOM   1189 C  CA  . VAL B 1 41  ? 20.460 3.606   -2.580  1.00 14.90 ? 41  VAL B CA  1 
ATOM   1190 C  C   . VAL B 1 41  ? 21.954 3.795   -2.498  1.00 15.03 ? 41  VAL B C   1 
ATOM   1191 O  O   . VAL B 1 41  ? 22.516 3.734   -1.402  1.00 15.77 ? 41  VAL B O   1 
ATOM   1192 C  CB  . VAL B 1 41  ? 19.712 4.793   -1.951  1.00 16.16 ? 41  VAL B CB  1 
ATOM   1193 C  CG1 . VAL B 1 41  ? 20.176 6.107   -2.613  1.00 17.19 ? 41  VAL B CG1 1 
ATOM   1194 C  CG2 . VAL B 1 41  ? 18.178 4.583   -2.073  1.00 17.55 ? 41  VAL B CG2 1 
ATOM   1195 N  N   . VAL B 1 42  ? 22.580 4.042   -3.645  1.00 13.92 ? 42  VAL B N   1 
ATOM   1196 C  CA  . VAL B 1 42  ? 24.030 4.120   -3.771  1.00 13.91 ? 42  VAL B CA  1 
ATOM   1197 C  C   . VAL B 1 42  ? 24.386 5.466   -4.370  1.00 13.92 ? 42  VAL B C   1 
ATOM   1198 O  O   . VAL B 1 42  ? 24.384 5.630   -5.591  1.00 14.40 ? 42  VAL B O   1 
ATOM   1199 C  CB  . VAL B 1 42  ? 24.584 2.979   -4.638  1.00 14.61 ? 42  VAL B CB  1 
ATOM   1200 C  CG1 . VAL B 1 42  ? 26.078 2.912   -4.452  1.00 15.34 ? 42  VAL B CG1 1 
ATOM   1201 C  CG2 . VAL B 1 42  ? 23.943 1.642   -4.264  1.00 16.15 ? 42  VAL B CG2 1 
ATOM   1202 N  N   . PRO B 1 43  ? 24.741 6.439   -3.535  1.00 15.14 ? 43  PRO B N   1 
ATOM   1203 C  CA  . PRO B 1 43  ? 25.062 7.780   -4.037  1.00 15.51 ? 43  PRO B CA  1 
ATOM   1204 C  C   . PRO B 1 43  ? 26.536 7.887   -4.396  1.00 14.91 ? 43  PRO B C   1 
ATOM   1205 O  O   . PRO B 1 43  ? 27.331 6.935   -4.229  1.00 15.11 ? 43  PRO B O   1 
ATOM   1206 C  CB  . PRO B 1 43  ? 24.740 8.690   -2.844  1.00 17.38 ? 43  PRO B CB  1 
ATOM   1207 C  CG  . PRO B 1 43  ? 25.021 7.837   -1.685  1.00 18.63 ? 43  PRO B CG  1 
ATOM   1208 C  CD  . PRO B 1 43  ? 24.664 6.396   -2.071  1.00 17.02 ? 43  PRO B CD  1 
ATOM   1209 N  N   . ASP B 1 44  ? 26.920 9.063   -4.908  1.00 15.19 ? 44  ASP B N   1 
ATOM   1210 C  CA  . ASP B 1 44  ? 28.327 9.385   -5.126  1.00 16.45 ? 44  ASP B CA  1 
ATOM   1211 C  C   . ASP B 1 44  ? 29.026 8.494   -6.151  1.00 16.42 ? 44  ASP B C   1 
ATOM   1212 O  O   . ASP B 1 44  ? 30.255 8.366   -6.117  1.00 17.41 ? 44  ASP B O   1 
ATOM   1213 C  CB  . ASP B 1 44  ? 29.120 9.405   -3.815  1.00 19.66 ? 44  ASP B CB  1 
ATOM   1214 C  CG  . ASP B 1 44  ? 28.724 10.549  -2.922  1.00 24.27 ? 44  ASP B CG  1 
ATOM   1215 O  OD1 . ASP B 1 44  ? 28.951 11.707  -3.320  1.00 25.81 ? 44  ASP B OD1 1 
ATOM   1216 O  OD2 . ASP B 1 44  ? 28.199 10.282  -1.835  1.00 26.57 ? 44  ASP B OD2 1 
ATOM   1217 N  N   . GLN B 1 45  ? 28.285 7.931   -7.089  1.00 14.87 ? 45  GLN B N   1 
ATOM   1218 C  CA  . GLN B 1 45  ? 28.872 7.013   -8.040  1.00 14.23 ? 45  GLN B CA  1 
ATOM   1219 C  C   . GLN B 1 45  ? 29.514 7.746   -9.204  1.00 13.99 ? 45  GLN B C   1 
ATOM   1220 O  O   . GLN B 1 45  ? 29.130 8.845   -9.577  1.00 14.94 ? 45  GLN B O   1 
ATOM   1221 C  CB  . GLN B 1 45  ? 27.795 6.064   -8.563  1.00 14.39 ? 45  GLN B CB  1 
ATOM   1222 C  CG  . GLN B 1 45  ? 27.237 5.141   -7.452  1.00 14.80 ? 45  GLN B CG  1 
ATOM   1223 C  CD  . GLN B 1 45  ? 28.333 4.320   -6.828  1.00 15.76 ? 45  GLN B CD  1 
ATOM   1224 O  OE1 . GLN B 1 45  ? 28.780 3.340   -7.427  1.00 16.32 ? 45  GLN B OE1 1 
ATOM   1225 N  NE2 . GLN B 1 45  ? 28.805 4.713   -5.655  1.00 15.90 ? 45  GLN B NE2 1 
ATOM   1226 N  N   . LEU B 1 46  ? 30.469 7.069   -9.815  1.00 12.92 ? 46  LEU B N   1 
ATOM   1227 C  CA  . LEU B 1 46  ? 31.161 7.512   -11.014 1.00 13.18 ? 46  LEU B CA  1 
ATOM   1228 C  C   . LEU B 1 46  ? 30.373 6.980   -12.207 1.00 13.21 ? 46  LEU B C   1 
ATOM   1229 O  O   . LEU B 1 46  ? 30.471 5.809   -12.567 1.00 13.97 ? 46  LEU B O   1 
ATOM   1230 C  CB  . LEU B 1 46  ? 32.593 7.012   -10.972 1.00 15.25 ? 46  LEU B CB  1 
ATOM   1231 C  CG  . LEU B 1 46  ? 33.403 7.167   -12.227 1.00 18.03 ? 46  LEU B CG  1 
ATOM   1232 N  N   . MET B 1 47  ? 29.547 7.837   -12.801 1.00 13.80 ? 47  MET B N   1 
ATOM   1233 C  CA  . MET B 1 47  ? 28.594 7.407   -13.809 1.00 15.73 ? 47  MET B CA  1 
ATOM   1234 C  C   . MET B 1 47  ? 28.443 8.501   -14.842 1.00 15.41 ? 47  MET B C   1 
ATOM   1235 O  O   . MET B 1 47  ? 28.661 9.689   -14.566 1.00 17.85 ? 47  MET B O   1 
ATOM   1236 C  CB  . MET B 1 47  ? 27.185 7.244   -13.210 1.00 20.06 ? 47  MET B CB  1 
ATOM   1237 C  CG  . MET B 1 47  ? 27.089 6.345   -12.062 1.00 22.28 ? 47  MET B CG  1 
ATOM   1238 S  SD  . MET B 1 47  ? 25.467 6.333   -11.309 1.00 20.85 ? 47  MET B SD  1 
ATOM   1239 C  CE  . MET B 1 47  ? 24.490 6.653   -12.617 1.00 20.03 ? 47  MET B CE  1 
ATOM   1240 N  N   . ALA B 1 48  ? 28.005 8.091   -16.023 1.00 13.91 ? 48  ALA B N   1 
ATOM   1241 C  CA  . ALA B 1 48  ? 27.633 9.020   -17.075 1.00 14.62 ? 48  ALA B CA  1 
ATOM   1242 C  C   . ALA B 1 48  ? 26.392 8.477   -17.773 1.00 13.88 ? 48  ALA B C   1 
ATOM   1243 O  O   . ALA B 1 48  ? 26.147 7.262   -17.812 1.00 13.69 ? 48  ALA B O   1 
ATOM   1244 C  CB  . ALA B 1 48  ? 28.789 9.244   -18.064 1.00 15.57 ? 48  ALA B CB  1 
ATOM   1245 N  N   . PHE B 1 49  ? 25.590 9.391   -18.309 1.00 13.73 ? 49  PHE B N   1 
ATOM   1246 C  CA  . PHE B 1 49  ? 24.373 9.040   -19.027 1.00 13.96 ? 49  PHE B CA  1 
ATOM   1247 C  C   . PHE B 1 49  ? 24.390 9.881   -20.292 1.00 14.41 ? 49  PHE B C   1 
ATOM   1248 O  O   . PHE B 1 49  ? 24.462 11.108  -20.208 1.00 14.96 ? 49  PHE B O   1 
ATOM   1249 C  CB  . PHE B 1 49  ? 23.136 9.316   -18.155 1.00 14.97 ? 49  PHE B CB  1 
ATOM   1250 C  CG  . PHE B 1 49  ? 21.870 8.729   -18.690 1.00 15.63 ? 49  PHE B CG  1 
ATOM   1251 C  CD1 . PHE B 1 49  ? 21.267 9.267   -19.833 1.00 17.13 ? 49  PHE B CD1 1 
ATOM   1252 C  CD2 . PHE B 1 49  ? 21.216 7.708   -18.017 1.00 16.09 ? 49  PHE B CD2 1 
ATOM   1253 C  CE1 . PHE B 1 49  ? 20.090 8.734   -20.322 1.00 18.87 ? 49  PHE B CE1 1 
ATOM   1254 C  CE2 . PHE B 1 49  ? 20.042 7.164   -18.521 1.00 17.50 ? 49  PHE B CE2 1 
ATOM   1255 C  CZ  . PHE B 1 49  ? 19.476 7.692   -19.657 1.00 18.78 ? 49  PHE B CZ  1 
ATOM   1256 N  N   . GLY B 1 50  ? 24.393 9.231   -21.452 1.00 15.28 ? 50  GLY B N   1 
ATOM   1257 C  CA  . GLY B 1 50  ? 24.497 9.968   -22.703 1.00 16.31 ? 50  GLY B CA  1 
ATOM   1258 C  C   . GLY B 1 50  ? 25.795 10.733  -22.834 1.00 16.60 ? 50  GLY B C   1 
ATOM   1259 O  O   . GLY B 1 50  ? 25.838 11.732  -23.555 1.00 17.92 ? 50  GLY B O   1 
ATOM   1260 N  N   . GLY B 1 51  ? 26.865 10.297  -22.155 1.00 16.29 ? 51  GLY B N   1 
ATOM   1261 C  CA  . GLY B 1 51  ? 28.143 10.967  -22.251 1.00 16.98 ? 51  GLY B CA  1 
ATOM   1262 C  C   . GLY B 1 51  ? 28.282 12.112  -21.292 1.00 16.95 ? 51  GLY B C   1 
ATOM   1263 O  O   . GLY B 1 51  ? 29.307 12.792  -21.316 1.00 18.63 ? 51  GLY B O   1 
ATOM   1264 N  N   . SER B 1 52  ? 27.251 12.384  -20.498 1.00 15.79 ? 52  SER B N   1 
ATOM   1265 C  CA  . SER B 1 52  ? 27.204 13.527  -19.616 1.00 16.36 ? 52  SER B CA  1 
ATOM   1266 C  C   . SER B 1 52  ? 27.239 13.091  -18.161 1.00 16.53 ? 52  SER B C   1 
ATOM   1267 O  O   . SER B 1 52  ? 26.637 12.073  -17.770 1.00 15.58 ? 52  SER B O   1 
ATOM   1268 C  CB  . SER B 1 52  ? 25.903 14.305  -19.867 1.00 17.33 ? 52  SER B CB  1 
ATOM   1269 O  OG  . SER B 1 52  ? 25.617 15.139  -18.776 1.00 17.78 ? 52  SER B OG  1 
ATOM   1270 N  N   . SER B 1 53  ? 27.963 13.857  -17.373 1.00 17.64 ? 53  SER B N   1 
ATOM   1271 C  CA  . SER B 1 53  ? 28.093 13.639  -15.945 1.00 18.96 ? 53  SER B CA  1 
ATOM   1272 C  C   . SER B 1 53  ? 27.102 14.450  -15.117 1.00 18.59 ? 53  SER B C   1 
ATOM   1273 O  O   . SER B 1 53  ? 27.210 14.474  -13.879 1.00 18.42 ? 53  SER B O   1 
ATOM   1274 C  CB  . SER B 1 53  ? 29.518 13.939  -15.506 1.00 21.02 ? 53  SER B CB  1 
ATOM   1275 O  OG  . SER B 1 53  ? 29.892 15.280  -15.802 1.00 22.88 ? 53  SER B OG  1 
ATOM   1276 N  N   . GLU B 1 54  ? 26.111 15.073  -15.749 1.00 17.78 ? 54  GLU B N   1 
ATOM   1277 C  CA  . GLU B 1 54  ? 25.012 15.665  -14.989 1.00 18.42 ? 54  GLU B CA  1 
ATOM   1278 C  C   . GLU B 1 54  ? 24.257 14.602  -14.170 1.00 17.38 ? 54  GLU B C   1 
ATOM   1279 O  O   . GLU B 1 54  ? 24.376 13.393  -14.416 1.00 16.50 ? 54  GLU B O   1 
ATOM   1280 C  CB  . GLU B 1 54  ? 24.061 16.392  -15.943 1.00 21.17 ? 54  GLU B CB  1 
ATOM   1281 C  CG  . GLU B 1 54  ? 24.557 17.651  -16.655 1.00 24.65 ? 54  GLU B CG  1 
ATOM   1282 C  CD  . GLU B 1 54  ? 25.018 18.777  -15.714 1.00 28.83 ? 54  GLU B CD  1 
ATOM   1283 O  OE1 . GLU B 1 54  ? 25.633 19.752  -16.216 1.00 32.05 ? 54  GLU B OE1 1 
ATOM   1284 O  OE2 . GLU B 1 54  ? 24.653 18.764  -14.511 1.00 29.21 ? 54  GLU B OE2 1 
ATOM   1285 N  N   . PRO B 1 55  ? 23.490 15.017  -13.167 1.00 18.10 ? 55  PRO B N   1 
ATOM   1286 C  CA  . PRO B 1 55  ? 22.823 14.020  -12.317 1.00 17.76 ? 55  PRO B CA  1 
ATOM   1287 C  C   . PRO B 1 55  ? 22.056 12.976  -13.113 1.00 16.56 ? 55  PRO B C   1 
ATOM   1288 O  O   . PRO B 1 55  ? 21.339 13.292  -14.068 1.00 16.12 ? 55  PRO B O   1 
ATOM   1289 C  CB  . PRO B 1 55  ? 21.893 14.866  -11.452 1.00 18.45 ? 55  PRO B CB  1 
ATOM   1290 C  CG  . PRO B 1 55  ? 22.661 16.176  -11.321 1.00 18.86 ? 55  PRO B CG  1 
ATOM   1291 C  CD  . PRO B 1 55  ? 23.319 16.386  -12.648 1.00 19.38 ? 55  PRO B CD  1 
ATOM   1292 N  N   . CYS B 1 56  ? 22.233 11.711  -12.733 1.00 15.53 ? 56  CYS B N   1 
ATOM   1293 C  CA  . CYS B 1 56  ? 21.579 10.610  -13.433 1.00 15.44 ? 56  CYS B CA  1 
ATOM   1294 C  C   . CYS B 1 56  ? 21.371 9.474   -12.440 1.00 14.40 ? 56  CYS B C   1 
ATOM   1295 O  O   . CYS B 1 56  ? 21.918 9.488   -11.329 1.00 14.90 ? 56  CYS B O   1 
ATOM   1296 C  CB  . CYS B 1 56  ? 22.390 10.140  -14.664 1.00 15.50 ? 56  CYS B CB  1 
ATOM   1297 S  SG  . CYS B 1 56  ? 24.063 9.572   -14.298 1.00 16.97 ? 56  CYS B SG  1 
ATOM   1298 N  N   . ALA B 1 57  ? 20.602 8.456   -12.849 1.00 14.07 ? 57  ALA B N   1 
ATOM   1299 C  CA  . ALA B 1 57  ? 20.430 7.286   -12.005 1.00 14.84 ? 57  ALA B CA  1 
ATOM   1300 C  C   . ALA B 1 57  ? 20.216 6.058   -12.868 1.00 13.83 ? 57  ALA B C   1 
ATOM   1301 O  O   . ALA B 1 57  ? 19.581 6.127   -13.927 1.00 15.11 ? 57  ALA B O   1 
ATOM   1302 C  CB  . ALA B 1 57  ? 19.232 7.447   -11.078 1.00 16.01 ? 57  ALA B CB  1 
ATOM   1303 N  N   . LEU B 1 58  ? 20.737 4.927   -12.400 1.00 13.45 ? 58  LEU B N   1 
ATOM   1304 C  CA  . LEU B 1 58  ? 20.496 3.623   -13.002 1.00 13.86 ? 58  LEU B CA  1 
ATOM   1305 C  C   . LEU B 1 58  ? 19.890 2.778   -11.908 1.00 13.27 ? 58  LEU B C   1 
ATOM   1306 O  O   . LEU B 1 58  ? 20.473 2.655   -10.822 1.00 13.92 ? 58  LEU B O   1 
ATOM   1307 C  CB  . LEU B 1 58  ? 21.816 3.008   -13.452 1.00 15.27 ? 58  LEU B CB  1 
ATOM   1308 C  CG  . LEU B 1 58  ? 22.549 3.817   -14.496 1.00 17.07 ? 58  LEU B CG  1 
ATOM   1309 C  CD1 . LEU B 1 58  ? 23.899 3.131   -14.768 1.00 17.67 ? 58  LEU B CD1 1 
ATOM   1310 C  CD2 . LEU B 1 58  ? 21.706 3.911   -15.770 1.00 17.87 ? 58  LEU B CD2 1 
ATOM   1311 N  N   . CYS B 1 59  ? 18.721 2.230   -12.182 1.00 13.83 ? 59  CYS B N   1 
ATOM   1312 C  CA  . CYS B 1 59  ? 17.943 1.563   -11.153 1.00 14.17 ? 59  CYS B CA  1 
ATOM   1313 C  C   . CYS B 1 59  ? 17.458 0.210   -11.631 1.00 13.07 ? 59  CYS B C   1 
ATOM   1314 O  O   . CYS B 1 59  ? 17.441 -0.080  -12.831 1.00 13.34 ? 59  CYS B O   1 
ATOM   1315 C  CB  . CYS B 1 59  ? 16.689 2.368   -10.801 1.00 15.26 ? 59  CYS B CB  1 
ATOM   1316 S  SG  . CYS B 1 59  ? 16.929 4.119   -10.515 1.00 16.93 ? 59  CYS B SG  1 
ATOM   1317 N  N   . SER B 1 60  ? 17.057 -0.621  -10.679 1.00 12.91 ? 60  SER B N   1 
ATOM   1318 C  CA  . SER B 1 60  ? 16.402 -1.865  -11.029 1.00 13.36 ? 60  SER B CA  1 
ATOM   1319 C  C   . SER B 1 60  ? 15.309 -2.167  -10.030 1.00 13.33 ? 60  SER B C   1 
ATOM   1320 O  O   . SER B 1 60  ? 15.414 -1.844  -8.849  1.00 14.36 ? 60  SER B O   1 
ATOM   1321 C  CB  . SER B 1 60  ? 17.354 -3.061  -11.123 1.00 14.28 ? 60  SER B CB  1 
ATOM   1322 O  OG  . SER B 1 60  ? 17.987 -3.289  -9.879  1.00 15.63 ? 60  SER B OG  1 
ATOM   1323 N  N   . LEU B 1 61  ? 14.264 -2.807  -10.523 1.00 13.03 ? 61  LEU B N   1 
ATOM   1324 C  CA  . LEU B 1 61  ? 13.210 -3.350  -9.673  1.00 13.65 ? 61  LEU B CA  1 
ATOM   1325 C  C   . LEU B 1 61  ? 13.078 -4.828  -10.011 1.00 13.58 ? 61  LEU B C   1 
ATOM   1326 O  O   . LEU B 1 61  ? 12.800 -5.186  -11.157 1.00 13.63 ? 61  LEU B O   1 
ATOM   1327 C  CB  . LEU B 1 61  ? 11.888 -2.618  -9.943  1.00 13.67 ? 61  LEU B CB  1 
ATOM   1328 C  CG  . LEU B 1 61  ? 10.715 -3.142  -9.103  1.00 15.48 ? 61  LEU B CG  1 
ATOM   1329 C  CD1 . LEU B 1 61  ? 10.954 -2.900  -7.621  1.00 16.68 ? 61  LEU B CD1 1 
ATOM   1330 C  CD2 . LEU B 1 61  ? 9.393  -2.486  -9.576  1.00 17.01 ? 61  LEU B CD2 1 
ATOM   1331 N  N   . HIS B 1 62  ? 13.290 -5.688  -9.017  1.00 13.19 ? 62  HIS B N   1 
ATOM   1332 C  CA  . HIS B 1 62  ? 13.074 -7.130  -9.144  1.00 13.12 ? 62  HIS B CA  1 
ATOM   1333 C  C   . HIS B 1 62  ? 11.853 -7.485  -8.305  1.00 13.93 ? 62  HIS B C   1 
ATOM   1334 O  O   . HIS B 1 62  ? 11.777 -7.091  -7.139  1.00 14.42 ? 62  HIS B O   1 
ATOM   1335 C  CB  . HIS B 1 62  ? 14.280 -7.898  -8.587  1.00 14.06 ? 62  HIS B CB  1 
ATOM   1336 C  CG  . HIS B 1 62  ? 15.549 -7.710  -9.361  1.00 15.19 ? 62  HIS B CG  1 
ATOM   1337 N  ND1 . HIS B 1 62  ? 16.301 -6.555  -9.333  1.00 16.59 ? 62  HIS B ND1 1 
ATOM   1338 C  CD2 . HIS B 1 62  ? 16.202 -8.568  -10.184 1.00 16.40 ? 62  HIS B CD2 1 
ATOM   1339 C  CE1 . HIS B 1 62  ? 17.362 -6.713  -10.115 1.00 17.12 ? 62  HIS B CE1 1 
ATOM   1340 N  NE2 . HIS B 1 62  ? 17.326 -7.929  -10.636 1.00 17.27 ? 62  HIS B NE2 1 
ATOM   1341 N  N   . SER B 1 63  ? 10.929 -8.252  -8.874  1.00 14.37 ? 63  SER B N   1 
ATOM   1342 C  CA  . SER B 1 63  ? 9.742  -8.628  -8.124  1.00 14.45 ? 63  SER B CA  1 
ATOM   1343 C  C   . SER B 1 63  ? 9.265  -9.960  -8.655  1.00 13.94 ? 63  SER B C   1 
ATOM   1344 O  O   . SER B 1 63  ? 9.396  -10.246 -9.849  1.00 13.90 ? 63  SER B O   1 
ATOM   1345 C  CB  . SER B 1 63  ? 8.656  -7.563  -8.334  1.00 15.17 ? 63  SER B CB  1 
ATOM   1346 O  OG  . SER B 1 63  ? 7.422  -7.878  -7.694  1.00 16.31 ? 63  SER B OG  1 
ATOM   1347 N  N   . ILE B 1 64  ? 8.686  -10.770 -7.774  1.00 14.29 ? 64  ILE B N   1 
ATOM   1348 C  CA  . ILE B 1 64  ? 7.998  -11.996 -8.189  1.00 14.80 ? 64  ILE B CA  1 
ATOM   1349 C  C   . ILE B 1 64  ? 6.602  -11.571 -8.643  1.00 16.01 ? 64  ILE B C   1 
ATOM   1350 O  O   . ILE B 1 64  ? 5.696  -11.338 -7.832  1.00 16.56 ? 64  ILE B O   1 
ATOM   1351 C  CB  . ILE B 1 64  ? 7.964  -13.044 -7.070  1.00 14.77 ? 64  ILE B CB  1 
ATOM   1352 C  CG1 . ILE B 1 64  ? 9.396  -13.426 -6.676  1.00 15.56 ? 64  ILE B CG1 1 
ATOM   1353 C  CG2 . ILE B 1 64  ? 7.123  -14.281 -7.466  1.00 14.94 ? 64  ILE B CG2 1 
ATOM   1354 C  CD1 . ILE B 1 64  ? 9.483  -14.173 -5.354  1.00 16.43 ? 64  ILE B CD1 1 
ATOM   1355 N  N   . GLY B 1 65  ? 6.425  -11.445 -9.947  1.00 15.54 ? 65  GLY B N   1 
ATOM   1356 C  CA  . GLY B 1 65  ? 5.171  -10.937 -10.474 1.00 15.86 ? 65  GLY B CA  1 
ATOM   1357 C  C   . GLY B 1 65  ? 5.042  -9.439  -10.285 1.00 16.73 ? 65  GLY B C   1 
ATOM   1358 O  O   . GLY B 1 65  ? 5.963  -8.755  -9.829  1.00 17.11 ? 65  GLY B O   1 
ATOM   1359 N  N   . LYS B 1 66  ? 3.874  -8.929  -10.640 1.00 17.24 ? 66  LYS B N   1 
ATOM   1360 C  CA  . LYS B 1 66  ? 3.623  -7.491  -10.615 1.00 18.75 ? 66  LYS B CA  1 
ATOM   1361 C  C   . LYS B 1 66  ? 4.541  -6.709  -11.538 1.00 17.44 ? 66  LYS B C   1 
ATOM   1362 O  O   . LYS B 1 66  ? 4.816  -5.522  -11.304 1.00 17.57 ? 66  LYS B O   1 
ATOM   1363 C  CB  . LYS B 1 66  ? 3.381  -6.756  -9.278  1.00 22.25 ? 66  LYS B CB  1 
ATOM   1364 C  CG  . LYS B 1 66  ? 2.217  -7.266  -8.330  1.00 26.76 ? 66  LYS B CG  1 
ATOM   1365 C  CD  . LYS B 1 66  ? 1.008  -7.713  -9.176  1.00 30.06 ? 66  LYS B CD  1 
ATOM   1366 C  CE  . LYS B 1 66  ? -0.400 -7.208  -8.900  1.00 33.51 ? 66  LYS B CE  1 
ATOM   1367 N  NZ  . LYS B 1 66  ? -0.385 -5.694  -9.404  1.00 35.45 ? 66  LYS B NZ  1 
ATOM   1368 N  N   . ILE B 1 67  ? 4.963  -7.341  -12.636 1.00 16.66 ? 67  ILE B N   1 
ATOM   1369 C  CA  . ILE B 1 67  ? 5.804  -6.723  -13.660 1.00 16.74 ? 67  ILE B CA  1 
ATOM   1370 C  C   . ILE B 1 67  ? 5.136  -6.942  -15.016 1.00 17.07 ? 67  ILE B C   1 
ATOM   1371 O  O   . ILE B 1 67  ? 4.649  -8.039  -15.307 1.00 18.53 ? 67  ILE B O   1 
ATOM   1372 C  CB  . ILE B 1 67  ? 7.202  -7.377  -13.636 1.00 16.36 ? 67  ILE B CB  1 
ATOM   1373 C  CG1 . ILE B 1 67  ? 7.902  -7.141  -12.297 1.00 16.72 ? 67  ILE B CG1 1 
ATOM   1374 C  CG2 . ILE B 1 67  ? 8.067  -6.937  -14.841 1.00 17.10 ? 67  ILE B CG2 1 
ATOM   1375 C  CD1 . ILE B 1 67  ? 8.335  -5.691  -12.091 1.00 16.58 ? 67  ILE B CD1 1 
ATOM   1376 N  N   . GLY B 1 68  ? 5.081  -5.904  -15.834 1.00 17.07 ? 68  GLY B N   1 
ATOM   1377 C  CA  . GLY B 1 68  ? 4.489  -6.051  -17.155 1.00 18.16 ? 68  GLY B CA  1 
ATOM   1378 C  C   . GLY B 1 68  ? 4.427  -4.709  -17.826 1.00 18.77 ? 68  GLY B C   1 
ATOM   1379 O  O   . GLY B 1 68  ? 4.777  -3.701  -17.242 1.00 17.46 ? 68  GLY B O   1 
ATOM   1380 N  N   . GLY B 1 69  ? 3.929  -4.705  -19.054 1.00 19.89 ? 69  GLY B N   1 
ATOM   1381 C  CA  . GLY B 1 69  ? 3.927  -3.486  -19.852 1.00 20.19 ? 69  GLY B CA  1 
ATOM   1382 C  C   . GLY B 1 69  ? 3.304  -2.274  -19.169 1.00 20.14 ? 69  GLY B C   1 
ATOM   1383 O  O   . GLY B 1 69  ? 3.969  -1.255  -18.954 1.00 19.87 ? 69  GLY B O   1 
ATOM   1384 N  N   . ALA B 1 70  ? 2.030  -2.382  -18.788 1.00 20.41 ? 70  ALA B N   1 
ATOM   1385 C  CA  . ALA B 1 70  ? 1.360  -1.246  -18.167 1.00 20.45 ? 70  ALA B CA  1 
ATOM   1386 C  C   . ALA B 1 70  ? 1.902  -0.981  -16.772 1.00 19.78 ? 70  ALA B C   1 
ATOM   1387 O  O   . ALA B 1 70  ? 2.099  0.176   -16.388 1.00 19.68 ? 70  ALA B O   1 
ATOM   1388 C  CB  . ALA B 1 70  ? -0.148 -1.481  -18.112 1.00 21.38 ? 70  ALA B CB  1 
ATOM   1389 N  N   . GLN B 1 71  ? 2.152  -2.037  -15.995 1.00 18.16 ? 71  GLN B N   1 
ATOM   1390 C  CA  . GLN B 1 71  ? 2.646  -1.824  -14.636 1.00 17.64 ? 71  GLN B CA  1 
ATOM   1391 C  C   . GLN B 1 71  ? 3.990  -1.115  -14.658 1.00 18.04 ? 71  GLN B C   1 
ATOM   1392 O  O   . GLN B 1 71  ? 4.219  -0.204  -13.858 1.00 18.61 ? 71  GLN B O   1 
ATOM   1393 C  CB  . GLN B 1 71  ? 2.742  -3.148  -13.869 1.00 18.54 ? 71  GLN B CB  1 
ATOM   1394 C  CG  . GLN B 1 71  ? 1.385  -3.731  -13.546 1.00 19.94 ? 71  GLN B CG  1 
ATOM   1395 C  CD  . GLN B 1 71  ? 1.498  -5.115  -12.959 1.00 20.87 ? 71  GLN B CD  1 
ATOM   1396 O  OE1 . GLN B 1 71  ? 1.472  -5.288  -11.737 1.00 22.18 ? 71  GLN B OE1 1 
ATOM   1397 N  NE2 . GLN B 1 71  ? 1.631  -6.122  -13.825 1.00 21.01 ? 71  GLN B NE2 1 
ATOM   1398 N  N   . ASN B 1 72  ? 4.870  -1.492  -15.598 1.00 17.41 ? 72  ASN B N   1 
ATOM   1399 C  CA  . ASN B 1 72  ? 6.193  -0.898  -15.636 1.00 16.97 ? 72  ASN B CA  1 
ATOM   1400 C  C   . ASN B 1 72  ? 6.130  0.558   -16.071 1.00 18.10 ? 72  ASN B C   1 
ATOM   1401 O  O   . ASN B 1 72  ? 6.963  1.370   -15.650 1.00 18.13 ? 72  ASN B O   1 
ATOM   1402 C  CB  . ASN B 1 72  ? 7.115  -1.691  -16.566 1.00 16.47 ? 72  ASN B CB  1 
ATOM   1403 C  CG  . ASN B 1 72  ? 7.343  -3.117  -16.114 1.00 16.62 ? 72  ASN B CG  1 
ATOM   1404 O  OD1 . ASN B 1 72  ? 6.952  -3.523  -15.022 1.00 17.35 ? 72  ASN B OD1 1 
ATOM   1405 N  ND2 . ASN B 1 72  ? 8.023  -3.877  -16.956 1.00 16.12 ? 72  ASN B ND2 1 
ATOM   1406 N  N   . ARG B 1 73  ? 5.176  0.907   -16.937 1.00 19.21 ? 73  ARG B N   1 
ATOM   1407 C  CA  . ARG B 1 73  ? 4.996  2.317   -17.262 1.00 20.12 ? 73  ARG B CA  1 
ATOM   1408 C  C   . ARG B 1 73  ? 4.587  3.093   -16.019 1.00 20.33 ? 73  ARG B C   1 
ATOM   1409 O  O   . ARG B 1 73  ? 5.077  4.207   -15.781 1.00 20.41 ? 73  ARG B O   1 
ATOM   1410 C  CB  . ARG B 1 73  ? 3.949  2.486   -18.371 1.00 21.31 ? 73  ARG B CB  1 
ATOM   1411 C  CG  . ARG B 1 73  ? 4.479  2.223   -19.794 1.00 23.36 ? 73  ARG B CG  1 
ATOM   1412 C  CD  . ARG B 1 73  ? 3.447  2.534   -20.878 1.00 25.54 ? 73  ARG B CD  1 
ATOM   1413 N  NE  . ARG B 1 73  ? 2.400  1.510   -20.926 1.00 27.69 ? 73  ARG B NE  1 
ATOM   1414 C  CZ  . ARG B 1 73  ? 2.519  0.356   -21.580 1.00 28.93 ? 73  ARG B CZ  1 
ATOM   1415 N  NH1 . ARG B 1 73  ? 3.649  0.086   -22.243 1.00 29.07 ? 73  ARG B NH1 1 
ATOM   1416 N  NH2 . ARG B 1 73  ? 1.520  -0.530  -21.563 1.00 30.02 ? 73  ARG B NH2 1 
ATOM   1417 N  N   . SER B 1 74  ? 3.664  2.523   -15.224 1.00 19.78 ? 74  SER B N   1 
ATOM   1418 C  CA  . SER B 1 74  ? 3.238  3.181   -13.993 1.00 20.16 ? 74  SER B CA  1 
ATOM   1419 C  C   . SER B 1 74  ? 4.390  3.273   -12.996 1.00 19.18 ? 74  SER B C   1 
ATOM   1420 O  O   . SER B 1 74  ? 4.590  4.321   -12.368 1.00 19.82 ? 74  SER B O   1 
ATOM   1421 C  CB  . SER B 1 74  ? 2.059  2.409   -13.397 1.00 22.40 ? 74  SER B CB  1 
ATOM   1422 O  OG  . SER B 1 74  ? 1.610  3.074   -12.236 1.00 24.14 ? 74  SER B OG  1 
ATOM   1423 N  N   . TYR B 1 75  ? 5.160  2.191   -12.833 1.00 18.41 ? 75  TYR B N   1 
ATOM   1424 C  CA  . TYR B 1 75  ? 6.312  2.265   -11.927 1.00 18.15 ? 75  TYR B CA  1 
ATOM   1425 C  C   . TYR B 1 75  ? 7.299  3.327   -12.375 1.00 18.01 ? 75  TYR B C   1 
ATOM   1426 O  O   . TYR B 1 75  ? 7.899  4.016   -11.546 1.00 18.40 ? 75  TYR B O   1 
ATOM   1427 C  CB  . TYR B 1 75  ? 7.057  0.944   -11.887 1.00 17.66 ? 75  TYR B CB  1 
ATOM   1428 C  CG  . TYR B 1 75  ? 6.297  -0.223  -11.299 1.00 18.24 ? 75  TYR B CG  1 
ATOM   1429 C  CD1 . TYR B 1 75  ? 5.381  -0.062  -10.266 1.00 20.32 ? 75  TYR B CD1 1 
ATOM   1430 C  CD2 . TYR B 1 75  ? 6.502  -1.495  -11.789 1.00 17.91 ? 75  TYR B CD2 1 
ATOM   1431 C  CE1 . TYR B 1 75  ? 4.700  -1.153  -9.755  1.00 21.02 ? 75  TYR B CE1 1 
ATOM   1432 C  CE2 . TYR B 1 75  ? 5.835  -2.591  -11.285 1.00 18.50 ? 75  TYR B CE2 1 
ATOM   1433 C  CZ  . TYR B 1 75  ? 4.931  -2.414  -10.266 1.00 20.49 ? 75  TYR B CZ  1 
ATOM   1434 O  OH  . TYR B 1 75  ? 4.257  -3.497  -9.760  1.00 21.26 ? 75  TYR B OH  1 
ATOM   1435 N  N   . SER B 1 76  ? 7.508  3.437   -13.676 1.00 17.54 ? 76  SER B N   1 
ATOM   1436 C  CA  . SER B 1 76  ? 8.511  4.381   -14.167 1.00 18.00 ? 76  SER B CA  1 
ATOM   1437 C  C   . SER B 1 76  ? 8.082  5.820   -13.884 1.00 19.11 ? 76  SER B C   1 
ATOM   1438 O  O   . SER B 1 76  ? 8.910  6.669   -13.549 1.00 20.12 ? 76  SER B O   1 
ATOM   1439 C  CB  . SER B 1 76  ? 8.755  4.181   -15.666 1.00 18.78 ? 76  SER B CB  1 
ATOM   1440 O  OG  . SER B 1 76  ? 9.294  2.899   -15.881 1.00 19.36 ? 76  SER B OG  1 
ATOM   1441 N  N   . LYS B 1 77  ? 6.795  6.120   -14.043 1.00 19.50 ? 77  LYS B N   1 
ATOM   1442 C  CA  . LYS B 1 77  ? 6.307  7.456   -13.707 1.00 20.71 ? 77  LYS B CA  1 
ATOM   1443 C  C   . LYS B 1 77  ? 6.456  7.728   -12.213 1.00 20.67 ? 77  LYS B C   1 
ATOM   1444 O  O   . LYS B 1 77  ? 6.915  8.806   -11.815 1.00 21.40 ? 77  LYS B O   1 
ATOM   1445 C  CB  . LYS B 1 77  ? 4.852  7.601   -14.154 1.00 22.50 ? 77  LYS B CB  1 
ATOM   1446 C  CG  . LYS B 1 77  ? 4.285  8.983   -13.935 1.00 25.35 ? 77  LYS B CG  1 
ATOM   1447 C  CD  . LYS B 1 77  ? 2.839  9.023   -14.344 1.00 28.39 ? 77  LYS B CD  1 
ATOM   1448 C  CE  . LYS B 1 77  ? 2.225  10.379  -14.009 1.00 30.94 ? 77  LYS B CE  1 
ATOM   1449 N  NZ  . LYS B 1 77  ? 0.744  10.403  -14.187 1.00 32.94 ? 77  LYS B NZ  1 
ATOM   1450 N  N   . LEU B 1 78  ? 6.104  6.746   -11.374 1.00 20.61 ? 78  LEU B N   1 
ATOM   1451 C  CA  . LEU B 1 78  ? 6.238  6.900   -9.929  1.00 20.47 ? 78  LEU B CA  1 
ATOM   1452 C  C   . LEU B 1 78  ? 7.688  7.125   -9.536  1.00 19.79 ? 78  LEU B C   1 
ATOM   1453 O  O   . LEU B 1 78  ? 8.004  8.051   -8.780  1.00 20.46 ? 78  LEU B O   1 
ATOM   1454 C  CB  . LEU B 1 78  ? 5.690  5.645   -9.222  1.00 21.40 ? 78  LEU B CB  1 
ATOM   1455 C  CG  . LEU B 1 78  ? 5.993  5.481   -7.723  1.00 23.38 ? 78  LEU B CG  1 
ATOM   1456 C  CD1 . LEU B 1 78  ? 5.201  6.471   -6.896  1.00 24.58 ? 78  LEU B CD1 1 
ATOM   1457 C  CD2 . LEU B 1 78  ? 5.682  4.076   -7.236  1.00 23.95 ? 78  LEU B CD2 1 
ATOM   1458 N  N   . LEU B 1 79  ? 8.589  6.278   -10.047 1.00 19.06 ? 79  LEU B N   1 
ATOM   1459 C  CA  . LEU B 1 79  ? 9.991  6.302   -9.622  1.00 18.94 ? 79  LEU B CA  1 
ATOM   1460 C  C   . LEU B 1 79  ? 10.739 7.493   -10.207 1.00 19.30 ? 79  LEU B C   1 
ATOM   1461 O  O   . LEU B 1 79  ? 11.516 8.138   -9.499  1.00 19.16 ? 79  LEU B O   1 
ATOM   1462 C  CB  . LEU B 1 79  ? 10.658 4.964   -9.933  1.00 19.26 ? 79  LEU B CB  1 
ATOM   1463 C  CG  . LEU B 1 79  ? 10.098 3.807   -9.101  1.00 20.46 ? 79  LEU B CG  1 
ATOM   1464 C  CD1 . LEU B 1 79  ? 10.519 2.495   -9.728  1.00 20.35 ? 79  LEU B CD1 1 
ATOM   1465 C  CD2 . LEU B 1 79  ? 10.533 3.877   -7.633  1.00 21.76 ? 79  LEU B CD2 1 
ATOM   1466 N  N   . CYS B 1 80  ? 10.507 7.816   -11.482 1.00 19.85 ? 80  CYS B N   1 
ATOM   1467 C  CA  . CYS B 1 80  ? 11.105 9.034   -12.018 1.00 20.22 ? 80  CYS B CA  1 
ATOM   1468 C  C   . CYS B 1 80  ? 10.612 10.257  -11.261 1.00 20.68 ? 80  CYS B C   1 
ATOM   1469 O  O   . CYS B 1 80  ? 11.389 11.168  -10.958 1.00 21.31 ? 80  CYS B O   1 
ATOM   1470 C  CB  . CYS B 1 80  ? 10.809 9.166   -13.507 1.00 21.06 ? 80  CYS B CB  1 
ATOM   1471 S  SG  . CYS B 1 80  ? 11.723 7.989   -14.548 1.00 20.60 ? 80  CYS B SG  1 
ATOM   1472 N  N   . GLY B 1 81  ? 9.333  10.271  -10.902 1.00 20.81 ? 81  GLY B N   1 
ATOM   1473 C  CA  . GLY B 1 81  ? 8.825  11.386  -10.116 1.00 20.97 ? 81  GLY B CA  1 
ATOM   1474 C  C   . GLY B 1 81  ? 9.524  11.525  -8.775  1.00 21.69 ? 81  GLY B C   1 
ATOM   1475 O  O   . GLY B 1 81  ? 9.865  12.641  -8.352  1.00 22.33 ? 81  GLY B O   1 
ATOM   1476 N  N   . LEU B 1 82  ? 9.755  10.398  -8.090  1.00 21.38 ? 82  LEU B N   1 
ATOM   1477 C  CA  . LEU B 1 82  ? 10.441 10.442  -6.802  1.00 22.23 ? 82  LEU B CA  1 
ATOM   1478 C  C   . LEU B 1 82  ? 11.891 10.881  -6.964  1.00 21.62 ? 82  LEU B C   1 
ATOM   1479 O  O   . LEU B 1 82  ? 12.405 11.642  -6.142  1.00 22.36 ? 82  LEU B O   1 
ATOM   1480 C  CB  . LEU B 1 82  ? 10.397 9.068   -6.125  1.00 23.86 ? 82  LEU B CB  1 
ATOM   1481 C  CG  . LEU B 1 82  ? 9.079  8.666   -5.468  1.00 26.15 ? 82  LEU B CG  1 
ATOM   1482 C  CD1 . LEU B 1 82  ? 9.099  7.203   -5.082  1.00 26.64 ? 82  LEU B CD1 1 
ATOM   1483 C  CD2 . LEU B 1 82  ? 8.798  9.530   -4.253  1.00 27.06 ? 82  LEU B CD2 1 
ATOM   1484 N  N   . LEU B 1 83  ? 12.583 10.374  -7.992  1.00 20.29 ? 83  LEU B N   1 
ATOM   1485 C  CA  . LEU B 1 83  ? 13.973 10.754  -8.201  1.00 19.30 ? 83  LEU B CA  1 
ATOM   1486 C  C   . LEU B 1 83  ? 14.075 12.219  -8.574  1.00 19.86 ? 83  LEU B C   1 
ATOM   1487 O  O   . LEU B 1 83  ? 15.024 12.891  -8.163  1.00 20.13 ? 83  LEU B O   1 
ATOM   1488 C  CB  . LEU B 1 83  ? 14.602 9.864   -9.278  1.00 19.09 ? 83  LEU B CB  1 
ATOM   1489 C  CG  . LEU B 1 83  ? 14.717 8.406   -8.864  1.00 19.81 ? 83  LEU B CG  1 
ATOM   1490 C  CD1 . LEU B 1 83  ? 15.097 7.567   -10.068 1.00 20.91 ? 83  LEU B CD1 1 
ATOM   1491 C  CD2 . LEU B 1 83  ? 15.756 8.273   -7.784  1.00 20.97 ? 83  LEU B CD2 1 
ATOM   1492 N  N   . ALA B 1 84  ? 13.102 12.734  -9.333  1.00 20.67 ? 84  ALA B N   1 
ATOM   1493 C  CA  . ALA B 1 84  ? 13.124 14.143  -9.698  1.00 22.04 ? 84  ALA B CA  1 
ATOM   1494 C  C   . ALA B 1 84  ? 12.853 15.012  -8.477  1.00 23.25 ? 84  ALA B C   1 
ATOM   1495 O  O   . ALA B 1 84  ? 13.579 15.980  -8.218  1.00 24.23 ? 84  ALA B O   1 
ATOM   1496 C  CB  . ALA B 1 84  ? 12.108 14.417  -10.815 1.00 22.47 ? 84  ALA B CB  1 
ATOM   1497 N  N   . GLU B 1 85  ? 11.841 14.653  -7.682  1.00 23.91 ? 85  GLU B N   1 
ATOM   1498 C  CA  . GLU B 1 85  ? 11.454 15.491  -6.549  1.00 25.14 ? 85  GLU B CA  1 
ATOM   1499 C  C   . GLU B 1 85  ? 12.474 15.427  -5.418  1.00 25.38 ? 85  GLU B C   1 
ATOM   1500 O  O   . GLU B 1 85  ? 12.819 16.462  -4.828  1.00 27.08 ? 85  GLU B O   1 
ATOM   1501 C  CB  . GLU B 1 85  ? 10.083 15.064  -6.029  1.00 26.40 ? 85  GLU B CB  1 
ATOM   1502 N  N   . ARG B 1 86  ? 12.976 14.230  -5.104  1.00 24.42 ? 86  ARG B N   1 
ATOM   1503 C  CA  . ARG B 1 86  ? 13.833 14.060  -3.939  1.00 24.11 ? 86  ARG B CA  1 
ATOM   1504 C  C   . ARG B 1 86  ? 15.313 14.204  -4.256  1.00 23.43 ? 86  ARG B C   1 
ATOM   1505 O  O   . ARG B 1 86  ? 16.061 14.720  -3.425  1.00 24.80 ? 86  ARG B O   1 
ATOM   1506 C  CB  . ARG B 1 86  ? 13.607 12.696  -3.287  1.00 24.83 ? 86  ARG B CB  1 
ATOM   1507 C  CG  . ARG B 1 86  ? 12.172 12.460  -2.882  1.00 25.79 ? 86  ARG B CG  1 
ATOM   1508 C  CD  . ARG B 1 86  ? 11.638 13.556  -1.992  1.00 27.63 ? 86  ARG B CD  1 
ATOM   1509 N  NE  . ARG B 1 86  ? 10.367 13.116  -1.427  1.00 29.44 ? 86  ARG B NE  1 
ATOM   1510 C  CZ  . ARG B 1 86  ? 9.481  13.937  -0.880  1.00 30.94 ? 86  ARG B CZ  1 
ATOM   1511 N  NH1 . ARG B 1 86  ? 9.731  15.237  -0.851  1.00 31.81 ? 86  ARG B NH1 1 
ATOM   1512 N  NH2 . ARG B 1 86  ? 8.353  13.461  -0.377  1.00 30.99 ? 86  ARG B NH2 1 
ATOM   1513 N  N   . LEU B 1 87  ? 15.771 13.735  -5.415  1.00 22.36 ? 87  LEU B N   1 
ATOM   1514 C  CA  . LEU B 1 87  ? 17.187 13.781  -5.760  1.00 22.54 ? 87  LEU B CA  1 
ATOM   1515 C  C   . LEU B 1 87  ? 17.500 14.785  -6.855  1.00 22.70 ? 87  LEU B C   1 
ATOM   1516 O  O   . LEU B 1 87  ? 18.670 14.964  -7.197  1.00 23.01 ? 87  LEU B O   1 
ATOM   1517 C  CB  . LEU B 1 87  ? 17.686 12.394  -6.176  1.00 22.45 ? 87  LEU B CB  1 
ATOM   1518 C  CG  . LEU B 1 87  ? 17.538 11.269  -5.145  1.00 23.91 ? 87  LEU B CG  1 
ATOM   1519 C  CD1 . LEU B 1 87  ? 18.312 10.058  -5.569  1.00 23.13 ? 87  LEU B CD1 1 
ATOM   1520 C  CD2 . LEU B 1 87  ? 18.021 11.679  -3.785  1.00 25.39 ? 87  LEU B CD2 1 
ATOM   1521 N  N   . ARG B 1 88  ? 16.489 15.444  -7.416  1.00 22.59 ? 88  ARG B N   1 
ATOM   1522 C  CA  . ARG B 1 88  ? 16.679 16.465  -8.458  1.00 24.19 ? 88  ARG B CA  1 
ATOM   1523 C  C   . ARG B 1 88  ? 17.294 15.897  -9.732  1.00 23.00 ? 88  ARG B C   1 
ATOM   1524 O  O   . ARG B 1 88  ? 18.038 16.589  -10.436 1.00 24.07 ? 88  ARG B O   1 
ATOM   1525 C  CB  . ARG B 1 88  ? 17.485 17.684  -7.976  1.00 28.05 ? 88  ARG B CB  1 
ATOM   1526 C  CG  . ARG B 1 88  ? 17.201 18.094  -6.535  1.00 32.83 ? 88  ARG B CG  1 
ATOM   1527 C  CD  . ARG B 1 88  ? 15.742 18.359  -6.336  1.00 37.68 ? 88  ARG B CD  1 
ATOM   1528 N  NE  . ARG B 1 88  ? 15.289 19.473  -7.157  1.00 41.82 ? 88  ARG B NE  1 
ATOM   1529 C  CZ  . ARG B 1 88  ? 14.017 19.750  -7.431  1.00 44.84 ? 88  ARG B CZ  1 
ATOM   1530 N  NH1 . ARG B 1 88  ? 13.728 20.805  -8.189  1.00 46.03 ? 88  ARG B NH1 1 
ATOM   1531 N  NH2 . ARG B 1 88  ? 13.037 18.980  -6.956  1.00 45.36 ? 88  ARG B NH2 1 
ATOM   1532 N  N   . ILE B 1 89  ? 16.968 14.643  -10.065 1.00 21.12 ? 89  ILE B N   1 
ATOM   1533 C  CA  . ILE B 1 89  ? 17.458 14.001  -11.280 1.00 20.56 ? 89  ILE B CA  1 
ATOM   1534 C  C   . ILE B 1 89  ? 16.372 14.085  -12.346 1.00 20.14 ? 89  ILE B C   1 
ATOM   1535 O  O   . ILE B 1 89  ? 15.218 13.717  -12.100 1.00 20.74 ? 89  ILE B O   1 
ATOM   1536 C  CB  . ILE B 1 89  ? 17.824 12.530  -11.007 1.00 19.57 ? 89  ILE B CB  1 
ATOM   1537 C  CG1 . ILE B 1 89  ? 18.900 12.425  -9.911  1.00 19.34 ? 89  ILE B CG1 1 
ATOM   1538 C  CG2 . ILE B 1 89  ? 18.241 11.814  -12.303 1.00 20.09 ? 89  ILE B CG2 1 
ATOM   1539 C  CD1 . ILE B 1 89  ? 19.106 10.998  -9.383  1.00 19.73 ? 89  ILE B CD1 1 
ATOM   1540 N  N   . SER B 1 90  ? 16.736 14.551  -13.542 1.00 19.93 ? 90  SER B N   1 
ATOM   1541 C  CA  . SER B 1 90  ? 15.777 14.616  -14.643 1.00 21.25 ? 90  SER B CA  1 
ATOM   1542 C  C   . SER B 1 90  ? 15.329 13.220  -15.063 1.00 20.14 ? 90  SER B C   1 
ATOM   1543 O  O   . SER B 1 90  ? 16.167 12.324  -15.208 1.00 19.50 ? 90  SER B O   1 
ATOM   1544 C  CB  . SER B 1 90  ? 16.412 15.305  -15.851 1.00 23.68 ? 90  SER B CB  1 
ATOM   1545 O  OG  . SER B 1 90  ? 16.717 16.648  -15.551 1.00 26.54 ? 90  SER B OG  1 
ATOM   1546 N  N   . PRO B 1 91  ? 14.022 13.025  -15.313 1.00 20.26 ? 91  PRO B N   1 
ATOM   1547 C  CA  . PRO B 1 91  ? 13.539 11.697  -15.736 1.00 20.02 ? 91  PRO B CA  1 
ATOM   1548 C  C   . PRO B 1 91  ? 14.208 11.169  -16.989 1.00 19.61 ? 91  PRO B C   1 
ATOM   1549 O  O   . PRO B 1 91  ? 14.353 9.949   -17.129 1.00 19.28 ? 91  PRO B O   1 
ATOM   1550 C  CB  . PRO B 1 91  ? 12.040 11.926  -15.953 1.00 20.76 ? 91  PRO B CB  1 
ATOM   1551 C  CG  . PRO B 1 91  ? 11.684 13.043  -15.018 1.00 21.66 ? 91  PRO B CG  1 
ATOM   1552 C  CD  . PRO B 1 91  ? 12.905 13.948  -15.017 1.00 21.29 ? 91  PRO B CD  1 
ATOM   1553 N  N   . ASP B 1 92  ? 14.647 12.040  -17.901 1.00 18.99 ? 92  ASP B N   1 
ATOM   1554 C  CA  . ASP B 1 92  ? 15.309 11.544  -19.101 1.00 19.69 ? 92  ASP B CA  1 
ATOM   1555 C  C   . ASP B 1 92  ? 16.770 11.167  -18.849 1.00 18.28 ? 92  ASP B C   1 
ATOM   1556 O  O   . ASP B 1 92  ? 17.498 10.866  -19.801 1.00 18.29 ? 92  ASP B O   1 
ATOM   1557 C  CB  . ASP B 1 92  ? 15.131 12.513  -20.282 1.00 21.88 ? 92  ASP B CB  1 
ATOM   1558 C  CG  . ASP B 1 92  ? 15.831 13.855  -20.080 1.00 23.28 ? 92  ASP B CG  1 
ATOM   1559 O  OD1 . ASP B 1 92  ? 16.481 14.066  -19.032 1.00 22.86 ? 92  ASP B OD1 1 
ATOM   1560 O  OD2 . ASP B 1 92  ? 15.709 14.713  -20.999 1.00 25.34 ? 92  ASP B OD2 1 
ATOM   1561 N  N   . ARG B 1 93  ? 17.213 11.190  -17.587 1.00 17.36 ? 93  ARG B N   1 
ATOM   1562 C  CA  . ARG B 1 93  ? 18.533 10.716  -17.200 1.00 16.41 ? 93  ARG B CA  1 
ATOM   1563 C  C   . ARG B 1 93  ? 18.427 9.577   -16.187 1.00 15.88 ? 93  ARG B C   1 
ATOM   1564 O  O   . ARG B 1 93  ? 19.327 9.362   -15.365 1.00 15.84 ? 93  ARG B O   1 
ATOM   1565 C  CB  . ARG B 1 93  ? 19.404 11.868  -16.704 1.00 16.34 ? 93  ARG B CB  1 
ATOM   1566 C  CG  . ARG B 1 93  ? 19.645 12.890  -17.825 1.00 16.90 ? 93  ARG B CG  1 
ATOM   1567 C  CD  . ARG B 1 93  ? 20.543 14.043  -17.369 1.00 16.84 ? 93  ARG B CD  1 
ATOM   1568 N  NE  . ARG B 1 93  ? 21.830 13.549  -16.872 1.00 16.93 ? 93  ARG B NE  1 
ATOM   1569 C  CZ  . ARG B 1 93  ? 22.804 13.068  -17.646 1.00 16.66 ? 93  ARG B CZ  1 
ATOM   1570 N  NH1 . ARG B 1 93  ? 22.673 13.036  -18.983 1.00 16.78 ? 93  ARG B NH1 1 
ATOM   1571 N  NH2 . ARG B 1 93  ? 23.902 12.595  -17.075 1.00 16.63 ? 93  ARG B NH2 1 
ATOM   1572 N  N   . VAL B 1 94  ? 17.330 8.839   -16.260 1.00 16.68 ? 94  VAL B N   1 
ATOM   1573 C  CA  . VAL B 1 94  ? 17.068 7.699   -15.392 1.00 16.47 ? 94  VAL B CA  1 
ATOM   1574 C  C   . VAL B 1 94  ? 16.765 6.487   -16.265 1.00 16.37 ? 94  VAL B C   1 
ATOM   1575 O  O   . VAL B 1 94  ? 15.910 6.565   -17.153 1.00 16.84 ? 94  VAL B O   1 
ATOM   1576 C  CB  . VAL B 1 94  ? 15.866 7.971   -14.461 1.00 16.86 ? 94  VAL B CB  1 
ATOM   1577 C  CG1 . VAL B 1 94  ? 15.488 6.706   -13.666 1.00 17.31 ? 94  VAL B CG1 1 
ATOM   1578 C  CG2 . VAL B 1 94  ? 16.178 9.113   -13.524 1.00 16.98 ? 94  VAL B CG2 1 
ATOM   1579 N  N   . TYR B 1 95  ? 17.440 5.367   -15.999 1.00 15.30 ? 95  TYR B N   1 
ATOM   1580 C  CA  . TYR B 1 95  ? 16.988 4.081   -16.498 1.00 15.19 ? 95  TYR B CA  1 
ATOM   1581 C  C   . TYR B 1 95  ? 16.531 3.239   -15.318 1.00 14.94 ? 95  TYR B C   1 
ATOM   1582 O  O   . TYR B 1 95  ? 17.157 3.260   -14.252 1.00 15.08 ? 95  TYR B O   1 
ATOM   1583 C  CB  . TYR B 1 95  ? 18.122 3.329   -17.172 1.00 16.19 ? 95  TYR B CB  1 
ATOM   1584 C  CG  . TYR B 1 95  ? 18.408 3.718   -18.600 1.00 16.70 ? 95  TYR B CG  1 
ATOM   1585 C  CD1 . TYR B 1 95  ? 17.386 4.120   -19.457 1.00 18.71 ? 95  TYR B CD1 1 
ATOM   1586 C  CD2 . TYR B 1 95  ? 19.699 3.655   -19.103 1.00 17.01 ? 95  TYR B CD2 1 
ATOM   1587 C  CE1 . TYR B 1 95  ? 17.657 4.432   -20.774 1.00 19.32 ? 95  TYR B CE1 1 
ATOM   1588 C  CE2 . TYR B 1 95  ? 19.972 3.973   -20.423 1.00 17.54 ? 95  TYR B CE2 1 
ATOM   1589 C  CZ  . TYR B 1 95  ? 18.949 4.361   -21.237 1.00 18.80 ? 95  TYR B CZ  1 
ATOM   1590 O  OH  . TYR B 1 95  ? 19.215 4.665   -22.541 1.00 20.40 ? 95  TYR B OH  1 
ATOM   1591 N  N   . ILE B 1 96  ? 15.456 2.481   -15.525 1.00 14.43 ? 96  ILE B N   1 
ATOM   1592 C  CA  . ILE B 1 96  ? 15.016 1.490   -14.556 1.00 13.74 ? 96  ILE B CA  1 
ATOM   1593 C  C   . ILE B 1 96  ? 14.829 0.171   -15.282 1.00 13.69 ? 96  ILE B C   1 
ATOM   1594 O  O   . ILE B 1 96  ? 13.977 0.070   -16.162 1.00 15.27 ? 96  ILE B O   1 
ATOM   1595 C  CB  . ILE B 1 96  ? 13.688 1.880   -13.894 1.00 14.60 ? 96  ILE B CB  1 
ATOM   1596 C  CG1 . ILE B 1 96  ? 13.772 3.305   -13.300 1.00 16.49 ? 96  ILE B CG1 1 
ATOM   1597 C  CG2 . ILE B 1 96  ? 13.332 0.836   -12.850 1.00 15.29 ? 96  ILE B CG2 1 
ATOM   1598 C  CD1 . ILE B 1 96  ? 12.405 3.901   -13.098 1.00 18.58 ? 96  ILE B CD1 1 
ATOM   1599 N  N   . ASN B 1 97  ? 15.610 -0.845  -14.927 1.00 13.52 ? 97  ASN B N   1 
ATOM   1600 C  CA  . ASN B 1 97  ? 15.414 -2.181  -15.487 1.00 13.84 ? 97  ASN B CA  1 
ATOM   1601 C  C   . ASN B 1 97  ? 14.474 -2.981  -14.594 1.00 13.45 ? 97  ASN B C   1 
ATOM   1602 O  O   . ASN B 1 97  ? 14.640 -2.996  -13.367 1.00 14.05 ? 97  ASN B O   1 
ATOM   1603 C  CB  . ASN B 1 97  ? 16.757 -2.893  -15.647 1.00 14.80 ? 97  ASN B CB  1 
ATOM   1604 C  CG  . ASN B 1 97  ? 17.532 -2.376  -16.820 1.00 17.01 ? 97  ASN B CG  1 
ATOM   1605 O  OD1 . ASN B 1 97  ? 16.958 -1.925  -17.794 1.00 18.83 ? 97  ASN B OD1 1 
ATOM   1606 N  ND2 . ASN B 1 97  ? 18.836 -2.453  -16.737 1.00 18.48 ? 97  ASN B ND2 1 
ATOM   1607 N  N   . TYR B 1 98  ? 13.492 -3.625  -15.217 1.00 13.50 ? 98  TYR B N   1 
ATOM   1608 C  CA  . TYR B 1 98  ? 12.481 -4.385  -14.497 1.00 13.04 ? 98  TYR B CA  1 
ATOM   1609 C  C   . TYR B 1 98  ? 12.702 -5.863  -14.715 1.00 13.32 ? 98  TYR B C   1 
ATOM   1610 O  O   . TYR B 1 98  ? 12.972 -6.285  -15.840 1.00 13.82 ? 98  TYR B O   1 
ATOM   1611 C  CB  . TYR B 1 98  ? 11.073 -4.017  -15.012 1.00 13.44 ? 98  TYR B CB  1 
ATOM   1612 C  CG  . TYR B 1 98  ? 10.719 -2.585  -14.688 1.00 13.96 ? 98  TYR B CG  1 
ATOM   1613 C  CD1 . TYR B 1 98  ? 10.297 -2.230  -13.410 1.00 14.85 ? 98  TYR B CD1 1 
ATOM   1614 C  CD2 . TYR B 1 98  ? 10.864 -1.577  -15.650 1.00 14.36 ? 98  TYR B CD2 1 
ATOM   1615 C  CE1 . TYR B 1 98  ? 10.023 -0.918  -13.086 1.00 14.94 ? 98  TYR B CE1 1 
ATOM   1616 C  CE2 . TYR B 1 98  ? 10.597 -0.240  -15.320 1.00 14.81 ? 98  TYR B CE2 1 
ATOM   1617 C  CZ  . TYR B 1 98  ? 10.162 0.071   -14.053 1.00 15.02 ? 98  TYR B CZ  1 
ATOM   1618 O  OH  . TYR B 1 98  ? 9.894  1.365   -13.720 1.00 16.27 ? 98  TYR B OH  1 
ATOM   1619 N  N   . TYR B 1 99  ? 12.558 -6.647  -13.643 1.00 13.32 ? 99  TYR B N   1 
ATOM   1620 C  CA  . TYR B 1 99  ? 12.776 -8.092  -13.684 1.00 13.39 ? 99  TYR B CA  1 
ATOM   1621 C  C   . TYR B 1 99  ? 11.631 -8.790  -12.989 1.00 13.53 ? 99  TYR B C   1 
ATOM   1622 O  O   . TYR B 1 99  ? 11.424 -8.580  -11.791 1.00 14.33 ? 99  TYR B O   1 
ATOM   1623 C  CB  . TYR B 1 99  ? 14.077 -8.464  -12.979 1.00 13.63 ? 99  TYR B CB  1 
ATOM   1624 C  CG  . TYR B 1 99  ? 15.261 -7.765  -13.593 1.00 14.03 ? 99  TYR B CG  1 
ATOM   1625 C  CD1 . TYR B 1 99  ? 15.917 -8.327  -14.682 1.00 15.74 ? 99  TYR B CD1 1 
ATOM   1626 C  CD2 . TYR B 1 99  ? 15.666 -6.515  -13.153 1.00 13.92 ? 99  TYR B CD2 1 
ATOM   1627 C  CE1 . TYR B 1 99  ? 17.003 -7.696  -15.290 1.00 15.89 ? 99  TYR B CE1 1 
ATOM   1628 C  CE2 . TYR B 1 99  ? 16.759 -5.875  -13.753 1.00 15.11 ? 99  TYR B CE2 1 
ATOM   1629 C  CZ  . TYR B 1 99  ? 17.402 -6.475  -14.823 1.00 15.84 ? 99  TYR B CZ  1 
ATOM   1630 O  OH  . TYR B 1 99  ? 18.459 -5.855  -15.459 1.00 17.85 ? 99  TYR B OH  1 
ATOM   1631 N  N   . ASP B 1 100 ? 10.932 -9.636  -13.730 1.00 14.24 ? 100 ASP B N   1 
ATOM   1632 C  CA  . ASP B 1 100 ? 9.891  -10.511 -13.199 1.00 14.39 ? 100 ASP B CA  1 
ATOM   1633 C  C   . ASP B 1 100 ? 10.600 -11.811 -12.839 1.00 13.96 ? 100 ASP B C   1 
ATOM   1634 O  O   . ASP B 1 100 ? 10.940 -12.599 -13.719 1.00 15.35 ? 100 ASP B O   1 
ATOM   1635 C  CB  . ASP B 1 100 ? 8.829  -10.723 -14.278 1.00 16.26 ? 100 ASP B CB  1 
ATOM   1636 C  CG  . ASP B 1 100 ? 7.633  -11.502 -13.791 1.00 18.52 ? 100 ASP B CG  1 
ATOM   1637 O  OD1 . ASP B 1 100 ? 7.617  -11.900 -12.621 1.00 17.78 ? 100 ASP B OD1 1 
ATOM   1638 O  OD2 . ASP B 1 100 ? 6.706  -11.724 -14.603 1.00 21.86 ? 100 ASP B OD2 1 
ATOM   1639 N  N   . MET B 1 101 ? 10.840 -12.018 -11.545 1.00 13.29 ? 101 MET B N   1 
ATOM   1640 C  CA  . MET B 1 101 ? 11.571 -13.186 -11.063 1.00 13.86 ? 101 MET B CA  1 
ATOM   1641 C  C   . MET B 1 101 ? 10.636 -14.372 -10.827 1.00 13.93 ? 101 MET B C   1 
ATOM   1642 O  O   . MET B 1 101 ? 9.539  -14.232 -10.278 1.00 14.68 ? 101 MET B O   1 
ATOM   1643 C  CB  . MET B 1 101 ? 12.245 -12.854 -9.739  1.00 14.31 ? 101 MET B CB  1 
ATOM   1644 C  CG  . MET B 1 101 ? 13.228 -11.670 -9.819  1.00 15.74 ? 101 MET B CG  1 
ATOM   1645 S  SD  . MET B 1 101 ? 14.611 -11.962 -10.936 1.00 17.85 ? 101 MET B SD  1 
ATOM   1646 C  CE  . MET B 1 101 ? 15.417 -13.347 -10.102 1.00 17.46 ? 101 MET B CE  1 
ATOM   1647 N  N   . ASN B 1 102 ? 11.078 -15.553 -11.229 1.00 13.84 ? 102 ASN B N   1 
ATOM   1648 C  CA  . ASN B 1 102 ? 10.435 -16.784 -10.800 1.00 14.78 ? 102 ASN B CA  1 
ATOM   1649 C  C   . ASN B 1 102 ? 10.703 -16.992 -9.317  1.00 13.86 ? 102 ASN B C   1 
ATOM   1650 O  O   . ASN B 1 102 ? 11.819 -16.804 -8.845  1.00 13.96 ? 102 ASN B O   1 
ATOM   1651 C  CB  . ASN B 1 102 ? 11.044 -17.965 -11.554 1.00 16.96 ? 102 ASN B CB  1 
ATOM   1652 C  CG  . ASN B 1 102 ? 10.708 -17.957 -13.020 1.00 20.65 ? 102 ASN B CG  1 
ATOM   1653 O  OD1 . ASN B 1 102 ? 9.918  -17.143 -13.484 1.00 22.43 ? 102 ASN B OD1 1 
ATOM   1654 N  ND2 . ASN B 1 102 ? 11.286 -18.894 -13.759 1.00 22.91 ? 102 ASN B ND2 1 
ATOM   1655 N  N   . ALA B 1 103 ? 9.683  -17.450 -8.590  1.00 13.84 ? 103 ALA B N   1 
ATOM   1656 C  CA  . ALA B 1 103 ? 9.831  -17.663 -7.154  1.00 13.93 ? 103 ALA B CA  1 
ATOM   1657 C  C   . ALA B 1 103 ? 11.003 -18.593 -6.837  1.00 13.91 ? 103 ALA B C   1 
ATOM   1658 O  O   . ALA B 1 103 ? 11.670 -18.419 -5.818  1.00 14.96 ? 103 ALA B O   1 
ATOM   1659 C  CB  . ALA B 1 103 ? 8.511  -18.221 -6.584  1.00 14.60 ? 103 ALA B CB  1 
ATOM   1660 N  N   . ALA B 1 104 ? 11.247 -19.626 -7.679  1.00 13.88 ? 104 ALA B N   1 
ATOM   1661 C  CA  . ALA B 1 104 ? 12.337 -20.549 -7.418  1.00 14.62 ? 104 ALA B CA  1 
ATOM   1662 C  C   . ALA B 1 104 ? 13.706 -19.894 -7.523  1.00 13.69 ? 104 ALA B C   1 
ATOM   1663 O  O   . ALA B 1 104 ? 14.682 -20.463 -7.033  1.00 14.36 ? 104 ALA B O   1 
ATOM   1664 C  CB  . ALA B 1 104 ? 12.277 -21.717 -8.395  1.00 15.73 ? 104 ALA B CB  1 
ATOM   1665 N  N   . ASN B 1 105 ? 13.792 -18.707 -8.136  1.00 12.68 ? 105 ASN B N   1 
ATOM   1666 C  CA  . ASN B 1 105 ? 15.050 -17.998 -8.316  1.00 12.55 ? 105 ASN B CA  1 
ATOM   1667 C  C   . ASN B 1 105 ? 15.213 -16.843 -7.348  1.00 12.79 ? 105 ASN B C   1 
ATOM   1668 O  O   . ASN B 1 105 ? 16.112 -16.031 -7.544  1.00 13.14 ? 105 ASN B O   1 
ATOM   1669 C  CB  . ASN B 1 105 ? 15.164 -17.537 -9.764  1.00 13.35 ? 105 ASN B CB  1 
ATOM   1670 C  CG  . ASN B 1 105 ? 15.355 -18.696 -10.699 1.00 14.75 ? 105 ASN B CG  1 
ATOM   1671 O  OD1 . ASN B 1 105 ? 15.883 -19.735 -10.298 1.00 15.36 ? 105 ASN B OD1 1 
ATOM   1672 N  ND2 . ASN B 1 105 ? 14.978 -18.519 -11.958 1.00 15.19 ? 105 ASN B ND2 1 
ATOM   1673 N  N   . VAL B 1 106 ? 14.407 -16.783 -6.289  1.00 13.17 ? 106 VAL B N   1 
ATOM   1674 C  CA  . VAL B 1 106 ? 14.565 -15.758 -5.248  1.00 13.41 ? 106 VAL B CA  1 
ATOM   1675 C  C   . VAL B 1 106 ? 14.769 -16.469 -3.918  1.00 12.96 ? 106 VAL B C   1 
ATOM   1676 O  O   . VAL B 1 106 ? 13.838 -17.091 -3.384  1.00 13.74 ? 106 VAL B O   1 
ATOM   1677 C  CB  . VAL B 1 106 ? 13.397 -14.760 -5.202  1.00 14.13 ? 106 VAL B CB  1 
ATOM   1678 C  CG1 . VAL B 1 106 ? 13.704 -13.690 -4.135  1.00 14.63 ? 106 VAL B CG1 1 
ATOM   1679 C  CG2 . VAL B 1 106 ? 13.206 -14.127 -6.593  1.00 14.53 ? 106 VAL B CG2 1 
ATOM   1680 N  N   . GLY B 1 107 ? 16.008 -16.422 -3.417  1.00 12.75 ? 107 GLY B N   1 
ATOM   1681 C  CA  . GLY B 1 107 ? 16.322 -16.984 -2.119  1.00 12.74 ? 107 GLY B CA  1 
ATOM   1682 C  C   . GLY B 1 107 ? 16.025 -16.018 -0.994  1.00 12.93 ? 107 GLY B C   1 
ATOM   1683 O  O   . GLY B 1 107 ? 16.163 -14.809 -1.125  1.00 13.35 ? 107 GLY B O   1 
ATOM   1684 N  N   . TRP B 1 108 ? 15.649 -16.593 0.140   1.00 13.32 ? 108 TRP B N   1 
ATOM   1685 C  CA  . TRP B 1 108 ? 15.281 -15.836 1.320   1.00 13.72 ? 108 TRP B CA  1 
ATOM   1686 C  C   . TRP B 1 108 ? 15.221 -16.825 2.462   1.00 13.86 ? 108 TRP B C   1 
ATOM   1687 O  O   . TRP B 1 108 ? 14.691 -17.917 2.300   1.00 14.36 ? 108 TRP B O   1 
ATOM   1688 C  CB  . TRP B 1 108 ? 13.897 -15.178 1.141   1.00 13.99 ? 108 TRP B CB  1 
ATOM   1689 C  CG  . TRP B 1 108 ? 13.393 -14.529 2.402   1.00 14.82 ? 108 TRP B CG  1 
ATOM   1690 C  CD1 . TRP B 1 108 ? 13.893 -13.422 3.017   1.00 14.26 ? 108 TRP B CD1 1 
ATOM   1691 C  CD2 . TRP B 1 108 ? 12.261 -14.940 3.186   1.00 16.72 ? 108 TRP B CD2 1 
ATOM   1692 N  NE1 . TRP B 1 108 ? 13.160 -13.121 4.145   1.00 14.98 ? 108 TRP B NE1 1 
ATOM   1693 C  CE2 . TRP B 1 108 ? 12.143 -14.034 4.253   1.00 16.94 ? 108 TRP B CE2 1 
ATOM   1694 C  CE3 . TRP B 1 108 ? 11.345 -16.004 3.094   1.00 19.05 ? 108 TRP B CE3 1 
ATOM   1695 C  CZ2 . TRP B 1 108 ? 11.168 -14.169 5.217   1.00 19.37 ? 108 TRP B CZ2 1 
ATOM   1696 C  CZ3 . TRP B 1 108 ? 10.380 -16.115 4.030   1.00 20.62 ? 108 TRP B CZ3 1 
ATOM   1697 C  CH2 . TRP B 1 108 ? 10.288 -15.207 5.076   1.00 20.60 ? 108 TRP B CH2 1 
ATOM   1698 N  N   . ASN B 1 109 ? 15.756 -16.442 3.613   1.00 13.80 ? 109 ASN B N   1 
ATOM   1699 C  CA  . ASN B 1 109 ? 15.484 -17.181 4.841   1.00 14.74 ? 109 ASN B CA  1 
ATOM   1700 C  C   . ASN B 1 109 ? 15.765 -18.679 4.687   1.00 15.42 ? 109 ASN B C   1 
ATOM   1701 O  O   . ASN B 1 109 ? 14.930 -19.536 4.984   1.00 16.45 ? 109 ASN B O   1 
ATOM   1702 C  CB  . ASN B 1 109 ? 14.060 -16.891 5.332   1.00 16.53 ? 109 ASN B CB  1 
ATOM   1703 C  CG  . ASN B 1 109 ? 13.846 -17.296 6.751   1.00 18.24 ? 109 ASN B CG  1 
ATOM   1704 O  OD1 . ASN B 1 109 ? 14.786 -17.545 7.493   1.00 19.97 ? 109 ASN B OD1 1 
ATOM   1705 N  ND2 . ASN B 1 109 ? 12.604 -17.197 7.187   1.00 18.88 ? 109 ASN B ND2 1 
ATOM   1706 N  N   . ASN B 1 110 ? 16.955 -18.994 4.187   1.00 15.04 ? 110 ASN B N   1 
ATOM   1707 C  CA  . ASN B 1 110 ? 17.500 -20.349 4.073   1.00 15.93 ? 110 ASN B CA  1 
ATOM   1708 C  C   . ASN B 1 110 ? 16.829 -21.189 2.994   1.00 15.62 ? 110 ASN B C   1 
ATOM   1709 O  O   . ASN B 1 110 ? 17.129 -22.373 2.869   1.00 16.68 ? 110 ASN B O   1 
ATOM   1710 C  CB  . ASN B 1 110 ? 17.447 -21.128 5.390   1.00 18.27 ? 110 ASN B CB  1 
ATOM   1711 C  CG  . ASN B 1 110 ? 18.294 -20.493 6.438   1.00 21.08 ? 110 ASN B CG  1 
ATOM   1712 O  OD1 . ASN B 1 110 ? 19.455 -20.156 6.169   1.00 23.43 ? 110 ASN B OD1 1 
ATOM   1713 N  ND2 . ASN B 1 110 ? 17.755 -20.365 7.654   1.00 22.70 ? 110 ASN B ND2 1 
ATOM   1714 N  N   . SER B 1 111 ? 15.985 -20.597 2.159   1.00 14.90 ? 111 SER B N   1 
ATOM   1715 C  CA  . SER B 1 111 ? 15.251 -21.353 1.154   1.00 14.99 ? 111 SER B CA  1 
ATOM   1716 C  C   . SER B 1 111 ? 14.973 -20.415 -0.015  1.00 14.60 ? 111 SER B C   1 
ATOM   1717 O  O   . SER B 1 111 ? 15.682 -19.428 -0.206  1.00 14.71 ? 111 SER B O   1 
ATOM   1718 C  CB  . SER B 1 111 ? 13.965 -21.951 1.758   1.00 16.02 ? 111 SER B CB  1 
ATOM   1719 O  OG  . SER B 1 111 ? 13.337 -22.860 0.853   1.00 17.98 ? 111 SER B OG  1 
ATOM   1720 N  N   . THR B 1 112 ? 13.956 -20.720 -0.813  1.00 14.50 ? 112 THR B N   1 
ATOM   1721 C  CA  . THR B 1 112 ? 13.482 -19.812 -1.855  1.00 14.50 ? 112 THR B CA  1 
ATOM   1722 C  C   . THR B 1 112 ? 11.982 -19.629 -1.680  1.00 15.09 ? 112 THR B C   1 
ATOM   1723 O  O   . THR B 1 112 ? 11.335 -20.268 -0.833  1.00 16.36 ? 112 THR B O   1 
ATOM   1724 C  CB  . THR B 1 112 ? 13.741 -20.326 -3.264  1.00 14.97 ? 112 THR B CB  1 
ATOM   1725 O  OG1 . THR B 1 112 ? 12.909 -21.467 -3.473  1.00 16.10 ? 112 THR B OG1 1 
ATOM   1726 C  CG2 . THR B 1 112 ? 15.225 -20.673 -3.470  1.00 15.07 ? 112 THR B CG2 1 
ATOM   1727 N  N   . PHE B 1 113 ? 11.412 -18.731 -2.480  1.00 14.64 ? 113 PHE B N   1 
ATOM   1728 C  CA  . PHE B 1 113 ? 9.983  -18.488 -2.402  1.00 15.46 ? 113 PHE B CA  1 
ATOM   1729 C  C   . PHE B 1 113 ? 9.156  -19.541 -3.128  1.00 15.82 ? 113 PHE B C   1 
ATOM   1730 O  O   . PHE B 1 113 ? 7.929  -19.473 -3.052  1.00 16.85 ? 113 PHE B O   1 
ATOM   1731 C  CB  . PHE B 1 113 ? 9.672  -17.094 -2.944  1.00 15.96 ? 113 PHE B CB  1 
ATOM   1732 C  CG  . PHE B 1 113 ? 9.987  -15.991 -1.968  1.00 17.24 ? 113 PHE B CG  1 
ATOM   1733 C  CD1 . PHE B 1 113 ? 9.197  -15.798 -0.826  1.00 19.26 ? 113 PHE B CD1 1 
ATOM   1734 C  CD2 . PHE B 1 113 ? 11.094 -15.166 -2.148  1.00 17.25 ? 113 PHE B CD2 1 
ATOM   1735 C  CE1 . PHE B 1 113 ? 9.475  -14.797 0.082   1.00 19.72 ? 113 PHE B CE1 1 
ATOM   1736 C  CE2 . PHE B 1 113 ? 11.397 -14.130 -1.229  1.00 17.52 ? 113 PHE B CE2 1 
ATOM   1737 C  CZ  . PHE B 1 113 ? 10.561 -13.962 -0.112  1.00 18.41 ? 113 PHE B CZ  1 
ATOM   1738 N  N   . ALA B 1 114 ? 9.762  -20.469 -3.869  1.00 15.42 ? 114 ALA B N   1 
ATOM   1739 C  CA  . ALA B 1 114 ? 8.962  -21.446 -4.608  1.00 16.82 ? 114 ALA B CA  1 
ATOM   1740 C  C   . ALA B 1 114 ? 8.144  -22.330 -3.695  1.00 18.72 ? 114 ALA B C   1 
ATOM   1741 O  O   . ALA B 1 114 ? 8.577  -22.697 -2.598  1.00 19.69 ? 114 ALA B O   1 
ATOM   1742 C  CB  . ALA B 1 114 ? 9.834  -22.287 -5.507  1.00 17.04 ? 114 ALA B CB  1 
ATOM   1743 O  OXT . ALA B 1 114 ? 7.025  -22.680 -4.090  1.00 19.77 ? 114 ALA B OXT 1 
ATOM   1744 N  N   . PRO C 1 1   ? 21.687 1.422   -23.929 1.00 17.68 ? 1   PRO C N   1 
ATOM   1745 C  CA  . PRO C 1 1   ? 22.346 0.359   -23.170 1.00 17.78 ? 1   PRO C CA  1 
ATOM   1746 C  C   . PRO C 1 1   ? 22.976 0.889   -21.899 1.00 16.18 ? 1   PRO C C   1 
ATOM   1747 O  O   . PRO C 1 1   ? 23.175 2.101   -21.739 1.00 16.46 ? 1   PRO C O   1 
ATOM   1748 C  CB  . PRO C 1 1   ? 23.447 -0.138  -24.124 1.00 19.07 ? 1   PRO C CB  1 
ATOM   1749 C  CG  . PRO C 1 1   ? 22.897 0.149   -25.497 1.00 19.98 ? 1   PRO C CG  1 
ATOM   1750 C  CD  . PRO C 1 1   ? 22.167 1.474   -25.323 1.00 19.19 ? 1   PRO C CD  1 
ATOM   1751 N  N   . MET C 1 2   ? 23.342 -0.033  -21.022 1.00 15.08 ? 2   MET C N   1 
ATOM   1752 C  CA  . MET C 1 2   ? 23.949 0.309   -19.748 1.00 15.18 ? 2   MET C CA  1 
ATOM   1753 C  C   . MET C 1 2   ? 25.116 -0.631  -19.522 1.00 13.53 ? 2   MET C C   1 
ATOM   1754 O  O   . MET C 1 2   ? 24.964 -1.854  -19.638 1.00 13.74 ? 2   MET C O   1 
ATOM   1755 C  CB  . MET C 1 2   ? 22.897 0.093   -18.662 1.00 20.10 ? 2   MET C CB  1 
ATOM   1756 C  CG  . MET C 1 2   ? 23.307 0.287   -17.251 1.00 24.81 ? 2   MET C CG  1 
ATOM   1757 S  SD  . MET C 1 2   ? 21.871 -0.227  -16.268 1.00 27.64 ? 2   MET C SD  1 
ATOM   1758 C  CE  . MET C 1 2   ? 20.524 0.518   -17.172 1.00 28.36 ? 2   MET C CE  1 
ATOM   1759 N  N   . PHE C 1 3   ? 26.278 -0.076  -19.209 1.00 12.88 ? 3   PHE C N   1 
ATOM   1760 C  CA  . PHE C 1 3   ? 27.480 -0.862  -18.938 1.00 12.83 ? 3   PHE C CA  1 
ATOM   1761 C  C   . PHE C 1 3   ? 27.989 -0.523  -17.557 1.00 12.67 ? 3   PHE C C   1 
ATOM   1762 O  O   . PHE C 1 3   ? 28.216 0.648   -17.256 1.00 13.30 ? 3   PHE C O   1 
ATOM   1763 C  CB  . PHE C 1 3   ? 28.565 -0.612  -19.993 1.00 13.59 ? 3   PHE C CB  1 
ATOM   1764 C  CG  . PHE C 1 3   ? 29.796 -1.406  -19.759 1.00 14.70 ? 3   PHE C CG  1 
ATOM   1765 C  CD1 . PHE C 1 3   ? 29.764 -2.798  -19.862 1.00 15.18 ? 3   PHE C CD1 1 
ATOM   1766 C  CD2 . PHE C 1 3   ? 30.975 -0.786  -19.424 1.00 16.85 ? 3   PHE C CD2 1 
ATOM   1767 C  CE1 . PHE C 1 3   ? 30.896 -3.563  -19.604 1.00 16.19 ? 3   PHE C CE1 1 
ATOM   1768 C  CE2 . PHE C 1 3   ? 32.119 -1.525  -19.206 1.00 18.35 ? 3   PHE C CE2 1 
ATOM   1769 C  CZ  . PHE C 1 3   ? 32.075 -2.930  -19.282 1.00 17.59 ? 3   PHE C CZ  1 
ATOM   1770 N  N   . ILE C 1 4   ? 28.188 -1.550  -16.729 1.00 11.69 ? 4   ILE C N   1 
ATOM   1771 C  CA  . ILE C 1 4   ? 28.674 -1.383  -15.372 1.00 12.23 ? 4   ILE C CA  1 
ATOM   1772 C  C   . ILE C 1 4   ? 29.935 -2.204  -15.221 1.00 11.80 ? 4   ILE C C   1 
ATOM   1773 O  O   . ILE C 1 4   ? 29.981 -3.361  -15.643 1.00 12.33 ? 4   ILE C O   1 
ATOM   1774 C  CB  . ILE C 1 4   ? 27.626 -1.845  -14.356 1.00 13.87 ? 4   ILE C CB  1 
ATOM   1775 C  CG1 . ILE C 1 4   ? 26.282 -1.162  -14.605 1.00 16.40 ? 4   ILE C CG1 1 
ATOM   1776 C  CG2 . ILE C 1 4   ? 28.105 -1.568  -12.929 1.00 14.83 ? 4   ILE C CG2 1 
ATOM   1777 C  CD1 . ILE C 1 4   ? 25.115 -1.857  -13.964 1.00 18.68 ? 4   ILE C CD1 1 
ATOM   1778 N  N   . VAL C 1 5   ? 30.955 -1.615  -14.617 1.00 12.05 ? 5   VAL C N   1 
ATOM   1779 C  CA  . VAL C 1 5   ? 32.189 -2.319  -14.269 1.00 13.30 ? 5   VAL C CA  1 
ATOM   1780 C  C   . VAL C 1 5   ? 32.458 -2.146  -12.788 1.00 12.70 ? 5   VAL C C   1 
ATOM   1781 O  O   . VAL C 1 5   ? 32.529 -1.018  -12.290 1.00 13.43 ? 5   VAL C O   1 
ATOM   1782 C  CB  . VAL C 1 5   ? 33.405 -1.877  -15.107 1.00 16.60 ? 5   VAL C CB  1 
ATOM   1783 C  CG1 . VAL C 1 5   ? 33.514 -0.449  -15.213 1.00 19.70 ? 5   VAL C CG1 1 
ATOM   1784 C  CG2 . VAL C 1 5   ? 34.668 -2.444  -14.507 1.00 17.59 ? 5   VAL C CG2 1 
ATOM   1785 N  N   . ASN C 1 6   ? 32.572 -3.268  -12.082 1.00 11.86 ? 6   ASN C N   1 
ATOM   1786 C  CA  . ASN C 1 6   ? 32.983 -3.301  -10.688 1.00 12.21 ? 6   ASN C CA  1 
ATOM   1787 C  C   . ASN C 1 6   ? 34.395 -3.871  -10.656 1.00 11.58 ? 6   ASN C C   1 
ATOM   1788 O  O   . ASN C 1 6   ? 34.659 -4.922  -11.249 1.00 11.89 ? 6   ASN C O   1 
ATOM   1789 C  CB  . ASN C 1 6   ? 32.030 -4.167  -9.848  1.00 13.74 ? 6   ASN C CB  1 
ATOM   1790 C  CG  . ASN C 1 6   ? 30.815 -3.385  -9.373  1.00 17.64 ? 6   ASN C CG  1 
ATOM   1791 O  OD1 . ASN C 1 6   ? 30.842 -2.811  -8.293  1.00 19.08 ? 6   ASN C OD1 1 
ATOM   1792 N  ND2 . ASN C 1 6   ? 29.822 -3.302  -10.182 1.00 20.25 ? 6   ASN C ND2 1 
ATOM   1793 N  N   . THR C 1 7   ? 35.297 -3.218  -9.927  1.00 11.38 ? 7   THR C N   1 
ATOM   1794 C  CA  . THR C 1 7   ? 36.675 -3.648  -9.926  1.00 12.57 ? 7   THR C CA  1 
ATOM   1795 C  C   . THR C 1 7   ? 37.314 -3.323  -8.591  1.00 12.34 ? 7   THR C C   1 
ATOM   1796 O  O   . THR C 1 7   ? 36.907 -2.391  -7.889  1.00 12.52 ? 7   THR C O   1 
ATOM   1797 C  CB  . THR C 1 7   ? 37.441 -3.004  -11.098 1.00 12.93 ? 7   THR C CB  1 
ATOM   1798 O  OG1 . THR C 1 7   ? 38.809 -3.394  -11.069 1.00 13.29 ? 7   THR C OG1 1 
ATOM   1799 C  CG2 . THR C 1 7   ? 37.430 -1.495  -11.011 1.00 13.49 ? 7   THR C CG2 1 
ATOM   1800 N  N   . ASN C 1 8   ? 38.330 -4.108  -8.245  1.00 11.82 ? 8   ASN C N   1 
ATOM   1801 C  CA  . ASN C 1 8   ? 39.167 -3.840  -7.075  1.00 13.15 ? 8   ASN C CA  1 
ATOM   1802 C  C   . ASN C 1 8   ? 40.286 -2.851  -7.366  1.00 14.75 ? 8   ASN C C   1 
ATOM   1803 O  O   . ASN C 1 8   ? 40.959 -2.425  -6.429  1.00 16.67 ? 8   ASN C O   1 
ATOM   1804 C  CB  . ASN C 1 8   ? 39.703 -5.134  -6.459  1.00 14.32 ? 8   ASN C CB  1 
ATOM   1805 C  CG  . ASN C 1 8   ? 40.478 -6.007  -7.450  1.00 14.98 ? 8   ASN C CG  1 
ATOM   1806 O  OD1 . ASN C 1 8   ? 40.416 -5.831  -8.667  1.00 14.21 ? 8   ASN C OD1 1 
ATOM   1807 N  ND2 . ASN C 1 8   ? 41.205 -6.990  -6.913  1.00 17.94 ? 8   ASN C ND2 1 
ATOM   1808 N  N   . VAL C 1 9   ? 40.458 -2.430  -8.620  1.00 13.94 ? 9   VAL C N   1 
ATOM   1809 C  CA  . VAL C 1 9   ? 41.489 -1.433  -8.938  1.00 15.75 ? 9   VAL C CA  1 
ATOM   1810 C  C   . VAL C 1 9   ? 41.139 -0.127  -8.236  1.00 15.88 ? 9   VAL C C   1 
ATOM   1811 O  O   . VAL C 1 9   ? 39.942 0.232   -8.159  1.00 16.11 ? 9   VAL C O   1 
ATOM   1812 C  CB  . VAL C 1 9   ? 41.560 -1.244  -10.475 1.00 18.08 ? 9   VAL C CB  1 
ATOM   1813 C  CG1 . VAL C 1 9   ? 42.289 -0.012  -10.905 1.00 20.73 ? 9   VAL C CG1 1 
ATOM   1814 C  CG2 . VAL C 1 9   ? 42.123 -2.498  -11.124 1.00 18.30 ? 9   VAL C CG2 1 
ATOM   1815 N  N   . PRO C 1 10  ? 42.108 0.595   -7.678  1.00 17.68 ? 10  PRO C N   1 
ATOM   1816 C  CA  . PRO C 1 10  ? 41.771 1.813   -6.933  1.00 18.48 ? 10  PRO C CA  1 
ATOM   1817 C  C   . PRO C 1 10  ? 41.325 2.936   -7.848  1.00 17.69 ? 10  PRO C C   1 
ATOM   1818 O  O   . PRO C 1 10  ? 41.686 2.996   -9.024  1.00 17.03 ? 10  PRO C O   1 
ATOM   1819 C  CB  . PRO C 1 10  ? 43.072 2.167   -6.199  1.00 20.28 ? 10  PRO C CB  1 
ATOM   1820 C  CG  . PRO C 1 10  ? 44.155 1.445   -6.918  1.00 20.99 ? 10  PRO C CG  1 
ATOM   1821 C  CD  . PRO C 1 10  ? 43.537 0.227   -7.546  1.00 19.24 ? 10  PRO C CD  1 
ATOM   1822 N  N   . ARG C 1 11  ? 40.549 3.860   -7.261  1.00 18.05 ? 11  ARG C N   1 
ATOM   1823 C  CA  . ARG C 1 11  ? 39.979 4.954   -8.044  1.00 18.97 ? 11  ARG C CA  1 
ATOM   1824 C  C   . ARG C 1 11  ? 41.061 5.752   -8.759  1.00 18.68 ? 11  ARG C C   1 
ATOM   1825 O  O   . ARG C 1 11  ? 40.878 6.159   -9.911  1.00 18.77 ? 11  ARG C O   1 
ATOM   1826 C  CB  . ARG C 1 11  ? 39.130 5.875   -7.150  1.00 22.02 ? 11  ARG C CB  1 
ATOM   1827 C  CG  . ARG C 1 11  ? 38.724 7.199   -7.804  1.00 26.71 ? 11  ARG C CG  1 
ATOM   1828 C  CD  . ARG C 1 11  ? 37.663 7.018   -8.888  1.00 31.14 ? 11  ARG C CD  1 
ATOM   1829 N  NE  . ARG C 1 11  ? 37.284 8.284   -9.533  1.00 34.75 ? 11  ARG C NE  1 
ATOM   1830 C  CZ  . ARG C 1 11  ? 37.835 8.747   -10.653 1.00 36.73 ? 11  ARG C CZ  1 
ATOM   1831 N  NH1 . ARG C 1 11  ? 38.792 8.053   -11.263 1.00 37.21 ? 11  ARG C NH1 1 
ATOM   1832 N  NH2 . ARG C 1 11  ? 37.422 9.892   -11.176 1.00 37.78 ? 11  ARG C NH2 1 
ATOM   1833 N  N   . ALA C 1 12  ? 42.208 5.952   -8.106  1.00 19.73 ? 12  ALA C N   1 
ATOM   1834 C  CA  . ALA C 1 12  ? 43.248 6.775   -8.695  1.00 21.77 ? 12  ALA C CA  1 
ATOM   1835 C  C   . ALA C 1 12  ? 43.877 6.149   -9.928  1.00 21.78 ? 12  ALA C C   1 
ATOM   1836 O  O   . ALA C 1 12  ? 44.553 6.858   -10.686 1.00 23.93 ? 12  ALA C O   1 
ATOM   1837 C  CB  . ALA C 1 12  ? 44.330 7.109   -7.664  1.00 23.17 ? 12  ALA C CB  1 
ATOM   1838 N  N   A SER C 1 13  ? 43.690 4.837   -10.118 0.83 20.95 ? 13  SER C N   1 
ATOM   1839 N  N   B SER C 1 13  ? 43.709 4.857   -10.165 0.17 21.11 ? 13  SER C N   1 
ATOM   1840 C  CA  A SER C 1 13  ? 44.172 4.105   -11.277 0.83 21.79 ? 13  SER C CA  1 
ATOM   1841 C  CA  B SER C 1 13  ? 44.238 4.298   -11.397 0.17 21.92 ? 13  SER C CA  1 
ATOM   1842 C  C   A SER C 1 13  ? 43.151 4.046   -12.409 0.83 21.60 ? 13  SER C C   1 
ATOM   1843 C  C   B SER C 1 13  ? 43.169 4.109   -12.465 0.17 21.59 ? 13  SER C C   1 
ATOM   1844 O  O   A SER C 1 13  ? 43.447 3.485   -13.461 0.83 23.56 ? 13  SER C O   1 
ATOM   1845 O  O   B SER C 1 13  ? 43.448 3.512   -13.507 0.17 23.43 ? 13  SER C O   1 
ATOM   1846 C  CB  A SER C 1 13  ? 44.607 2.699   -10.863 0.83 23.59 ? 13  SER C CB  1 
ATOM   1847 C  CB  B SER C 1 13  ? 45.023 3.023   -11.134 0.17 23.76 ? 13  SER C CB  1 
ATOM   1848 O  OG  A SER C 1 13  ? 45.680 2.769   -9.934  0.83 25.45 ? 13  SER C OG  1 
ATOM   1849 O  OG  B SER C 1 13  ? 44.138 1.974   -10.917 0.17 25.66 ? 13  SER C OG  1 
ATOM   1850 N  N   . VAL C 1 14  ? 41.960 4.609   -12.236 1.00 19.50 ? 14  VAL C N   1 
ATOM   1851 C  CA  . VAL C 1 14  ? 40.986 4.734   -13.320 1.00 18.35 ? 14  VAL C CA  1 
ATOM   1852 C  C   . VAL C 1 14  ? 41.360 6.031   -14.037 1.00 18.51 ? 14  VAL C C   1 
ATOM   1853 O  O   . VAL C 1 14  ? 41.283 7.113   -13.434 1.00 19.46 ? 14  VAL C O   1 
ATOM   1854 C  CB  . VAL C 1 14  ? 39.548 4.784   -12.793 1.00 18.26 ? 14  VAL C CB  1 
ATOM   1855 C  CG1 . VAL C 1 14  ? 38.568 4.957   -13.960 1.00 19.03 ? 14  VAL C CG1 1 
ATOM   1856 C  CG2 . VAL C 1 14  ? 39.225 3.528   -12.014 1.00 18.36 ? 14  VAL C CG2 1 
ATOM   1857 N  N   . PRO C 1 15  ? 41.804 5.987   -15.284 1.00 18.07 ? 15  PRO C N   1 
ATOM   1858 C  CA  . PRO C 1 15  ? 42.324 7.213   -15.909 1.00 18.43 ? 15  PRO C CA  1 
ATOM   1859 C  C   . PRO C 1 15  ? 41.231 8.228   -16.182 1.00 17.71 ? 15  PRO C C   1 
ATOM   1860 O  O   . PRO C 1 15  ? 40.066 7.892   -16.421 1.00 17.53 ? 15  PRO C O   1 
ATOM   1861 C  CB  . PRO C 1 15  ? 42.945 6.715   -17.209 1.00 19.39 ? 15  PRO C CB  1 
ATOM   1862 C  CG  . PRO C 1 15  ? 42.326 5.423   -17.470 1.00 20.16 ? 15  PRO C CG  1 
ATOM   1863 C  CD  . PRO C 1 15  ? 41.912 4.805   -16.157 1.00 18.93 ? 15  PRO C CD  1 
ATOM   1864 N  N   . ASP C 1 16  ? 41.636 9.495   -16.222 1.00 16.27 ? 16  ASP C N   1 
ATOM   1865 C  CA  . ASP C 1 16  ? 40.734 10.537  -16.665 1.00 16.03 ? 16  ASP C CA  1 
ATOM   1866 C  C   . ASP C 1 16  ? 40.191 10.181  -18.037 1.00 15.52 ? 16  ASP C C   1 
ATOM   1867 O  O   . ASP C 1 16  ? 40.918 9.675   -18.910 1.00 17.18 ? 16  ASP C O   1 
ATOM   1868 C  CB  . ASP C 1 16  ? 41.495 11.852  -16.849 1.00 17.15 ? 16  ASP C CB  1 
ATOM   1869 C  CG  . ASP C 1 16  ? 41.902 12.493  -15.557 1.00 18.53 ? 16  ASP C CG  1 
ATOM   1870 O  OD1 . ASP C 1 16  ? 41.547 11.997  -14.480 1.00 19.45 ? 16  ASP C OD1 1 
ATOM   1871 O  OD2 . ASP C 1 16  ? 42.595 13.532  -15.635 1.00 18.90 ? 16  ASP C OD2 1 
ATOM   1872 N  N   . GLY C 1 17  ? 38.899 10.440  -18.221 1.00 14.52 ? 17  GLY C N   1 
ATOM   1873 C  CA  . GLY C 1 17  ? 38.271 10.235  -19.510 1.00 15.26 ? 17  GLY C CA  1 
ATOM   1874 C  C   . GLY C 1 17  ? 37.797 8.818   -19.754 1.00 14.60 ? 17  GLY C C   1 
ATOM   1875 O  O   . GLY C 1 17  ? 37.245 8.541   -20.830 1.00 15.99 ? 17  GLY C O   1 
ATOM   1876 N  N   . PHE C 1 18  ? 37.927 7.925   -18.772 1.00 14.24 ? 18  PHE C N   1 
ATOM   1877 C  CA  . PHE C 1 18  ? 37.562 6.532   -19.005 1.00 15.28 ? 18  PHE C CA  1 
ATOM   1878 C  C   . PHE C 1 18  ? 36.071 6.365   -19.296 1.00 15.49 ? 18  PHE C C   1 
ATOM   1879 O  O   . PHE C 1 18  ? 35.693 5.580   -20.162 1.00 15.62 ? 18  PHE C O   1 
ATOM   1880 C  CB  . PHE C 1 18  ? 37.976 5.711   -17.790 1.00 16.98 ? 18  PHE C CB  1 
ATOM   1881 C  CG  . PHE C 1 18  ? 37.783 4.232   -17.964 1.00 18.99 ? 18  PHE C CG  1 
ATOM   1882 C  CD1 . PHE C 1 18  ? 38.389 3.577   -19.020 1.00 20.63 ? 18  PHE C CD1 1 
ATOM   1883 C  CD2 . PHE C 1 18  ? 37.014 3.487   -17.071 1.00 19.62 ? 18  PHE C CD2 1 
ATOM   1884 C  CE1 . PHE C 1 18  ? 38.252 2.197   -19.176 1.00 20.79 ? 18  PHE C CE1 1 
ATOM   1885 C  CE2 . PHE C 1 18  ? 36.856 2.108   -17.259 1.00 20.66 ? 18  PHE C CE2 1 
ATOM   1886 C  CZ  . PHE C 1 18  ? 37.478 1.480   -18.298 1.00 21.03 ? 18  PHE C CZ  1 
ATOM   1887 N  N   . LEU C 1 19  ? 35.197 7.046   -18.549 1.00 14.73 ? 19  LEU C N   1 
ATOM   1888 C  CA  . LEU C 1 19  ? 33.762 6.913   -18.808 1.00 16.15 ? 19  LEU C CA  1 
ATOM   1889 C  C   . LEU C 1 19  ? 33.409 7.371   -20.212 1.00 15.72 ? 19  LEU C C   1 
ATOM   1890 O  O   . LEU C 1 19  ? 32.559 6.767   -20.867 1.00 15.46 ? 19  LEU C O   1 
ATOM   1891 C  CB  . LEU C 1 19  ? 32.932 7.687   -17.783 1.00 18.16 ? 19  LEU C CB  1 
ATOM   1892 C  CG  . LEU C 1 19  ? 32.913 7.168   -16.355 1.00 20.82 ? 19  LEU C CG  1 
ATOM   1893 C  CD1 . LEU C 1 19  ? 31.994 8.017   -15.489 1.00 22.25 ? 19  LEU C CD1 1 
ATOM   1894 C  CD2 . LEU C 1 19  ? 32.442 5.785   -16.369 1.00 22.90 ? 19  LEU C CD2 1 
ATOM   1895 N  N   . SER C 1 20  ? 34.032 8.457   -20.681 1.00 15.88 ? 20  SER C N   1 
ATOM   1896 C  CA  . SER C 1 20  ? 33.735 8.934   -22.024 1.00 16.46 ? 20  SER C CA  1 
ATOM   1897 C  C   . SER C 1 20  ? 34.205 7.941   -23.073 1.00 16.44 ? 20  SER C C   1 
ATOM   1898 O  O   . SER C 1 20  ? 33.500 7.685   -24.058 1.00 17.14 ? 20  SER C O   1 
ATOM   1899 C  CB  . SER C 1 20  ? 34.369 10.310  -22.216 1.00 18.45 ? 20  SER C CB  1 
ATOM   1900 O  OG  . SER C 1 20  ? 34.238 10.719  -23.562 1.00 20.83 ? 20  SER C OG  1 
ATOM   1901 N  N   . GLU C 1 21  ? 35.400 7.381   -22.888 1.00 17.12 ? 21  GLU C N   1 
ATOM   1902 C  CA  . GLU C 1 21  ? 35.859 6.349   -23.809 1.00 17.71 ? 21  GLU C CA  1 
ATOM   1903 C  C   . GLU C 1 21  ? 34.900 5.166   -23.840 1.00 16.02 ? 21  GLU C C   1 
ATOM   1904 O  O   . GLU C 1 21  ? 34.586 4.654   -24.919 1.00 16.58 ? 21  GLU C O   1 
ATOM   1905 C  CB  . GLU C 1 21  ? 37.249 5.887   -23.415 1.00 20.74 ? 21  GLU C CB  1 
ATOM   1906 C  CG  . GLU C 1 21  ? 37.860 5.019   -24.484 1.00 24.84 ? 21  GLU C CG  1 
ATOM   1907 C  CD  . GLU C 1 21  ? 39.305 4.649   -24.194 1.00 28.69 ? 21  GLU C CD  1 
ATOM   1908 O  OE1 . GLU C 1 21  ? 39.726 4.716   -23.012 1.00 30.03 ? 21  GLU C OE1 1 
ATOM   1909 O  OE2 . GLU C 1 21  ? 40.018 4.313   -25.173 1.00 30.37 ? 21  GLU C OE2 1 
ATOM   1910 N  N   . LEU C 1 22  ? 34.427 4.713   -22.667 1.00 14.54 ? 22  LEU C N   1 
ATOM   1911 C  CA  . LEU C 1 22  ? 33.462 3.620   -22.666 1.00 15.31 ? 22  LEU C CA  1 
ATOM   1912 C  C   . LEU C 1 22  ? 32.200 4.018   -23.418 1.00 14.30 ? 22  LEU C C   1 
ATOM   1913 O  O   . LEU C 1 22  ? 31.683 3.243   -24.222 1.00 15.09 ? 22  LEU C O   1 
ATOM   1914 C  CB  . LEU C 1 22  ? 33.117 3.210   -21.231 1.00 15.65 ? 22  LEU C CB  1 
ATOM   1915 C  CG  . LEU C 1 22  ? 34.198 2.461   -20.447 1.00 15.98 ? 22  LEU C CG  1 
ATOM   1916 C  CD1 . LEU C 1 22  ? 33.761 2.349   -18.974 1.00 16.76 ? 22  LEU C CD1 1 
ATOM   1917 C  CD2 . LEU C 1 22  ? 34.402 1.108   -21.107 1.00 17.29 ? 22  LEU C CD2 1 
ATOM   1918 N  N   . THR C 1 23  ? 31.690 5.231   -23.184 1.00 13.33 ? 23  THR C N   1 
ATOM   1919 C  CA  . THR C 1 23  ? 30.478 5.663   -23.868 1.00 13.85 ? 23  THR C CA  1 
ATOM   1920 C  C   . THR C 1 23  ? 30.655 5.623   -25.376 1.00 14.32 ? 23  THR C C   1 
ATOM   1921 O  O   . THR C 1 23  ? 29.796 5.096   -26.096 1.00 15.23 ? 23  THR C O   1 
ATOM   1922 C  CB  . THR C 1 23  ? 30.112 7.070   -23.416 1.00 14.32 ? 23  THR C CB  1 
ATOM   1923 O  OG1 . THR C 1 23  ? 29.860 7.050   -22.003 1.00 14.76 ? 23  THR C OG1 1 
ATOM   1924 C  CG2 . THR C 1 23  ? 28.881 7.574   -24.173 1.00 15.56 ? 23  THR C CG2 1 
ATOM   1925 N  N   . GLN C 1 24  ? 31.762 6.183   -25.869 1.00 15.29 ? 24  GLN C N   1 
ATOM   1926 C  CA  . GLN C 1 24  ? 31.965 6.283   -27.303 1.00 15.98 ? 24  GLN C CA  1 
ATOM   1927 C  C   . GLN C 1 24  ? 32.165 4.915   -27.926 1.00 16.11 ? 24  GLN C C   1 
ATOM   1928 O  O   . GLN C 1 24  ? 31.598 4.617   -28.983 1.00 16.77 ? 24  GLN C O   1 
ATOM   1929 C  CB  . GLN C 1 24  ? 33.213 7.125   -27.548 1.00 17.90 ? 24  GLN C CB  1 
ATOM   1930 C  CG  . GLN C 1 24  ? 33.057 8.564   -27.130 1.00 19.63 ? 24  GLN C CG  1 
ATOM   1931 C  CD  . GLN C 1 24  ? 34.347 9.347   -27.331 1.00 23.61 ? 24  GLN C CD  1 
ATOM   1932 O  OE1 . GLN C 1 24  ? 35.445 8.772   -27.473 1.00 25.64 ? 24  GLN C OE1 1 
ATOM   1933 N  NE2 . GLN C 1 24  ? 34.219 10.649  -27.400 1.00 25.53 ? 24  GLN C NE2 1 
ATOM   1934 N  N   . GLN C 1 25  ? 32.971 4.077   -27.288 1.00 15.56 ? 25  GLN C N   1 
ATOM   1935 C  CA  . GLN C 1 25  ? 33.227 2.763   -27.847 1.00 16.98 ? 25  GLN C CA  1 
ATOM   1936 C  C   . GLN C 1 25  ? 31.984 1.890   -27.816 1.00 15.77 ? 25  GLN C C   1 
ATOM   1937 O  O   . GLN C 1 25  ? 31.762 1.101   -28.740 1.00 16.05 ? 25  GLN C O   1 
ATOM   1938 C  CB  . GLN C 1 25  ? 34.356 2.113   -27.062 1.00 19.21 ? 25  GLN C CB  1 
ATOM   1939 C  CG  . GLN C 1 25  ? 35.721 2.761   -27.232 1.00 23.29 ? 25  GLN C CG  1 
ATOM   1940 C  CD  . GLN C 1 25  ? 36.238 2.546   -28.612 1.00 28.70 ? 25  GLN C CD  1 
ATOM   1941 O  OE1 . GLN C 1 25  ? 36.419 1.396   -29.038 1.00 31.38 ? 25  GLN C OE1 1 
ATOM   1942 N  NE2 . GLN C 1 25  ? 36.491 3.625   -29.326 1.00 30.88 ? 25  GLN C NE2 1 
ATOM   1943 N  N   . LEU C 1 26  ? 31.163 2.013   -26.767 1.00 14.91 ? 26  LEU C N   1 
ATOM   1944 C  CA  . LEU C 1 26  ? 29.941 1.224   -26.715 1.00 15.85 ? 26  LEU C CA  1 
ATOM   1945 C  C   . LEU C 1 26  ? 28.920 1.718   -27.724 1.00 16.82 ? 26  LEU C C   1 
ATOM   1946 O  O   . LEU C 1 26  ? 28.211 0.913   -28.334 1.00 17.70 ? 26  LEU C O   1 
ATOM   1947 C  CB  . LEU C 1 26  ? 29.328 1.279   -25.321 1.00 16.13 ? 26  LEU C CB  1 
ATOM   1948 C  CG  . LEU C 1 26  ? 30.083 0.393   -24.359 1.00 17.68 ? 26  LEU C CG  1 
ATOM   1949 C  CD1 . LEU C 1 26  ? 29.693 0.765   -22.969 1.00 19.16 ? 26  LEU C CD1 1 
ATOM   1950 C  CD2 . LEU C 1 26  ? 29.770 -1.070  -24.687 1.00 18.80 ? 26  LEU C CD2 1 
ATOM   1951 N  N   . ALA C 1 27  ? 28.818 3.028   -27.919 1.00 18.06 ? 27  ALA C N   1 
ATOM   1952 C  CA  . ALA C 1 27  ? 27.913 3.516   -28.956 1.00 20.19 ? 27  ALA C CA  1 
ATOM   1953 C  C   . ALA C 1 27  ? 28.273 2.898   -30.305 1.00 21.01 ? 27  ALA C C   1 
ATOM   1954 O  O   . ALA C 1 27  ? 27.402 2.409   -31.042 1.00 22.73 ? 27  ALA C O   1 
ATOM   1955 C  CB  . ALA C 1 27  ? 27.988 5.042   -29.027 1.00 20.65 ? 27  ALA C CB  1 
ATOM   1956 N  N   . GLN C 1 28  ? 29.567 2.879   -30.631 1.00 20.75 ? 28  GLN C N   1 
ATOM   1957 C  CA  . GLN C 1 28  ? 30.010 2.324   -31.904 1.00 22.10 ? 28  GLN C CA  1 
ATOM   1958 C  C   . GLN C 1 28  ? 29.753 0.825   -31.972 1.00 21.08 ? 28  GLN C C   1 
ATOM   1959 O  O   . GLN C 1 28  ? 29.257 0.312   -32.985 1.00 22.05 ? 28  GLN C O   1 
ATOM   1960 C  CB  . GLN C 1 28  ? 31.505 2.591   -32.067 1.00 25.56 ? 28  GLN C CB  1 
ATOM   1961 C  CG  . GLN C 1 28  ? 31.897 4.046   -32.264 1.00 30.31 ? 28  GLN C CG  1 
ATOM   1962 C  CD  . GLN C 1 28  ? 31.835 4.498   -33.706 1.00 34.48 ? 28  GLN C CD  1 
ATOM   1963 O  OE1 . GLN C 1 28  ? 31.393 3.761   -34.596 1.00 37.00 ? 28  GLN C OE1 1 
ATOM   1964 N  NE2 . GLN C 1 28  ? 32.313 5.693   -33.952 1.00 35.13 ? 28  GLN C NE2 1 
ATOM   1965 N  N   . ALA C 1 29  ? 30.097 0.103   -30.902 1.00 18.70 ? 29  ALA C N   1 
ATOM   1966 C  CA  . ALA C 1 29  ? 30.009 -1.349  -30.931 1.00 18.00 ? 29  ALA C CA  1 
ATOM   1967 C  C   . ALA C 1 29  ? 28.569 -1.812  -30.986 1.00 18.60 ? 29  ALA C C   1 
ATOM   1968 O  O   . ALA C 1 29  ? 28.249 -2.760  -31.714 1.00 19.23 ? 29  ALA C O   1 
ATOM   1969 C  CB  . ALA C 1 29  ? 30.683 -1.932  -29.687 1.00 17.76 ? 29  ALA C CB  1 
ATOM   1970 N  N   . THR C 1 30  ? 27.693 -1.200  -30.189 1.00 18.13 ? 30  THR C N   1 
ATOM   1971 C  CA  . THR C 1 30  ? 26.310 -1.652  -30.150 1.00 18.57 ? 30  THR C CA  1 
ATOM   1972 C  C   . THR C 1 30  ? 25.477 -1.046  -31.270 1.00 18.62 ? 30  THR C C   1 
ATOM   1973 O  O   . THR C 1 30  ? 24.370 -1.517  -31.520 1.00 18.39 ? 30  THR C O   1 
ATOM   1974 C  CB  . THR C 1 30  ? 25.638 -1.313  -28.807 1.00 19.41 ? 30  THR C CB  1 
ATOM   1975 O  OG1 . THR C 1 30  ? 25.571 0.114   -28.663 1.00 19.23 ? 30  THR C OG1 1 
ATOM   1976 C  CG2 . THR C 1 30  ? 26.350 -1.964  -27.599 1.00 20.06 ? 30  THR C CG2 1 
ATOM   1977 N  N   . GLY C 1 31  ? 25.951 0.004   -31.940 1.00 19.52 ? 31  GLY C N   1 
ATOM   1978 C  CA  . GLY C 1 31  ? 25.114 0.724   -32.893 1.00 20.75 ? 31  GLY C CA  1 
ATOM   1979 C  C   . GLY C 1 31  ? 24.115 1.689   -32.266 1.00 22.24 ? 31  GLY C C   1 
ATOM   1980 O  O   . GLY C 1 31  ? 23.428 2.427   -32.995 1.00 25.86 ? 31  GLY C O   1 
ATOM   1981 N  N   . LYS C 1 32  ? 24.093 1.789   -31.122 1.00 20.59 ? 32  LYS C N   1 
ATOM   1982 C  CA  . LYS C 1 32  ? 23.096 2.618   -30.478 1.00 19.62 ? 32  LYS C CA  1 
ATOM   1983 C  C   . LYS C 1 32  ? 23.575 4.066   -30.375 1.00 19.44 ? 32  LYS C C   1 
ATOM   1984 O  O   . LYS C 1 32  ? 24.786 4.333   -30.355 1.00 20.97 ? 32  LYS C O   1 
ATOM   1985 C  CB  . LYS C 1 32  ? 22.788 2.079   -29.085 1.00 19.93 ? 32  LYS C CB  1 
ATOM   1986 C  CG  . LYS C 1 32  ? 22.337 0.650   -29.048 1.00 20.99 ? 32  LYS C CG  1 
ATOM   1987 C  CD  . LYS C 1 32  ? 20.836 0.635   -29.117 1.00 21.57 ? 32  LYS C CD  1 
ATOM   1988 C  CE  . LYS C 1 32  ? 20.323 -0.734  -28.711 1.00 20.90 ? 32  LYS C CE  1 
ATOM   1989 N  NZ  . LYS C 1 32  ? 18.852 -0.694  -28.719 1.00 20.60 ? 32  LYS C NZ  1 
ATOM   1990 N  N   . PRO C 1 33  ? 22.660 5.022   -30.310 1.00 20.03 ? 33  PRO C N   1 
ATOM   1991 C  CA  . PRO C 1 33  ? 23.067 6.414   -30.187 1.00 20.25 ? 33  PRO C CA  1 
ATOM   1992 C  C   . PRO C 1 33  ? 23.749 6.675   -28.861 1.00 19.51 ? 33  PRO C C   1 
ATOM   1993 O  O   . PRO C 1 33  ? 23.337 6.139   -27.823 1.00 18.82 ? 33  PRO C O   1 
ATOM   1994 C  CB  . PRO C 1 33  ? 21.739 7.184   -30.279 1.00 21.09 ? 33  PRO C CB  1 
ATOM   1995 C  CG  . PRO C 1 33  ? 20.718 6.206   -30.852 1.00 20.76 ? 33  PRO C CG  1 
ATOM   1996 C  CD  . PRO C 1 33  ? 21.197 4.866   -30.341 1.00 20.06 ? 33  PRO C CD  1 
ATOM   1997 N  N   . PRO C 1 34  ? 24.761 7.538   -28.858 1.00 19.04 ? 34  PRO C N   1 
ATOM   1998 C  CA  . PRO C 1 34  ? 25.430 7.869   -27.595 1.00 18.11 ? 34  PRO C CA  1 
ATOM   1999 C  C   . PRO C 1 34  ? 24.484 8.362   -26.526 1.00 17.28 ? 34  PRO C C   1 
ATOM   2000 O  O   . PRO C 1 34  ? 24.700 8.050   -25.348 1.00 17.11 ? 34  PRO C O   1 
ATOM   2001 C  CB  . PRO C 1 34  ? 26.498 8.896   -28.005 1.00 20.56 ? 34  PRO C CB  1 
ATOM   2002 C  CG  . PRO C 1 34  ? 26.292 9.160   -29.403 1.00 23.00 ? 34  PRO C CG  1 
ATOM   2003 C  CD  . PRO C 1 34  ? 25.470 8.096   -30.022 1.00 21.20 ? 34  PRO C CD  1 
ATOM   2004 N  N   . GLN C 1 35  ? 23.408 9.062   -26.913 1.00 18.05 ? 35  GLN C N   1 
ATOM   2005 C  CA  . GLN C 1 35  ? 22.415 9.553   -25.960 1.00 21.06 ? 35  GLN C CA  1 
ATOM   2006 C  C   . GLN C 1 35  ? 21.844 8.452   -25.074 1.00 18.75 ? 35  GLN C C   1 
ATOM   2007 O  O   . GLN C 1 35  ? 21.479 8.691   -23.914 1.00 19.93 ? 35  GLN C O   1 
ATOM   2008 C  CB  . GLN C 1 35  ? 21.282 10.233  -26.766 1.00 27.54 ? 35  GLN C CB  1 
ATOM   2009 C  CG  . GLN C 1 35  ? 19.933 10.386  -26.052 1.00 29.71 ? 35  GLN C CG  1 
ATOM   2010 C  CD  . GLN C 1 35  ? 18.782 10.861  -26.968 1.00 30.06 ? 35  GLN C CD  1 
ATOM   2011 O  OE1 . GLN C 1 35  ? 18.909 10.917  -28.197 1.00 30.41 ? 35  GLN C OE1 1 
ATOM   2012 N  NE2 . GLN C 1 35  ? 17.650 11.181  -26.355 1.00 30.24 ? 35  GLN C NE2 1 
ATOM   2013 N  N   . TYR C 1 36  ? 21.757 7.242   -25.589 1.00 16.94 ? 36  TYR C N   1 
ATOM   2014 C  CA  . TYR C 1 36  ? 21.123 6.147   -24.871 1.00 17.49 ? 36  TYR C CA  1 
ATOM   2015 C  C   . TYR C 1 36  ? 22.116 5.276   -24.116 1.00 16.70 ? 36  TYR C C   1 
ATOM   2016 O  O   . TYR C 1 36  ? 21.725 4.271   -23.522 1.00 17.04 ? 36  TYR C O   1 
ATOM   2017 C  CB  . TYR C 1 36  ? 20.278 5.313   -25.828 1.00 20.19 ? 36  TYR C CB  1 
ATOM   2018 C  CG  . TYR C 1 36  ? 19.073 6.054   -26.324 1.00 23.43 ? 36  TYR C CG  1 
ATOM   2019 C  CD1 . TYR C 1 36  ? 18.006 6.359   -25.471 1.00 25.30 ? 36  TYR C CD1 1 
ATOM   2020 C  CD2 . TYR C 1 36  ? 18.997 6.492   -27.642 1.00 24.89 ? 36  TYR C CD2 1 
ATOM   2021 C  CE1 . TYR C 1 36  ? 16.883 7.036   -25.930 1.00 26.96 ? 36  TYR C CE1 1 
ATOM   2022 C  CE2 . TYR C 1 36  ? 17.886 7.195   -28.110 1.00 26.26 ? 36  TYR C CE2 1 
ATOM   2023 C  CZ  . TYR C 1 36  ? 16.840 7.450   -27.250 1.00 27.49 ? 36  TYR C CZ  1 
ATOM   2024 O  OH  . TYR C 1 36  ? 15.743 8.133   -27.711 1.00 29.58 ? 36  TYR C OH  1 
ATOM   2025 N  N   . ILE C 1 37  ? 23.388 5.618   -24.138 1.00 15.43 ? 37  ILE C N   1 
ATOM   2026 C  CA  . ILE C 1 37  ? 24.427 4.826   -23.484 1.00 14.67 ? 37  ILE C CA  1 
ATOM   2027 C  C   . ILE C 1 37  ? 24.679 5.377   -22.088 1.00 13.73 ? 37  ILE C C   1 
ATOM   2028 O  O   . ILE C 1 37  ? 25.021 6.550   -21.926 1.00 14.50 ? 37  ILE C O   1 
ATOM   2029 C  CB  . ILE C 1 37  ? 25.732 4.838   -24.304 1.00 15.75 ? 37  ILE C CB  1 
ATOM   2030 C  CG1 . ILE C 1 37  ? 25.522 4.262   -25.704 1.00 18.15 ? 37  ILE C CG1 1 
ATOM   2031 C  CG2 . ILE C 1 37  ? 26.867 4.094   -23.567 1.00 15.36 ? 37  ILE C CG2 1 
ATOM   2032 C  CD1 . ILE C 1 37  ? 25.486 2.770   -25.767 1.00 20.58 ? 37  ILE C CD1 1 
ATOM   2033 N  N   . ALA C 1 38  ? 24.561 4.526   -21.073 1.00 12.82 ? 38  ALA C N   1 
ATOM   2034 C  CA  . ALA C 1 38  ? 24.912 4.885   -19.700 1.00 13.11 ? 38  ALA C CA  1 
ATOM   2035 C  C   . ALA C 1 38  ? 26.038 3.983   -19.237 1.00 12.70 ? 38  ALA C C   1 
ATOM   2036 O  O   . ALA C 1 38  ? 26.051 2.798   -19.565 1.00 12.96 ? 38  ALA C O   1 
ATOM   2037 C  CB  . ALA C 1 38  ? 23.715 4.719   -18.769 1.00 14.31 ? 38  ALA C CB  1 
ATOM   2038 N  N   . VAL C 1 39  ? 26.968 4.544   -18.470 1.00 12.69 ? 39  VAL C N   1 
ATOM   2039 C  CA  . VAL C 1 39  ? 28.150 3.825   -18.017 1.00 12.89 ? 39  VAL C CA  1 
ATOM   2040 C  C   . VAL C 1 39  ? 28.392 4.101   -16.545 1.00 12.78 ? 39  VAL C C   1 
ATOM   2041 O  O   . VAL C 1 39  ? 28.152 5.205   -16.055 1.00 13.51 ? 39  VAL C O   1 
ATOM   2042 C  CB  . VAL C 1 39  ? 29.399 4.188   -18.848 1.00 14.25 ? 39  VAL C CB  1 
ATOM   2043 C  CG1 . VAL C 1 39  ? 29.229 3.767   -20.303 1.00 15.46 ? 39  VAL C CG1 1 
ATOM   2044 C  CG2 . VAL C 1 39  ? 29.740 5.646   -18.746 1.00 16.70 ? 39  VAL C CG2 1 
ATOM   2045 N  N   . HIS C 1 40  ? 28.893 3.080   -15.835 1.00 12.88 ? 40  HIS C N   1 
ATOM   2046 C  CA  . HIS C 1 40  ? 29.091 3.210   -14.395 1.00 12.51 ? 40  HIS C CA  1 
ATOM   2047 C  C   . HIS C 1 40  ? 30.316 2.402   -14.030 1.00 12.42 ? 40  HIS C C   1 
ATOM   2048 O  O   . HIS C 1 40  ? 30.379 1.225   -14.369 1.00 13.43 ? 40  HIS C O   1 
ATOM   2049 C  CB  . HIS C 1 40  ? 27.837 2.658   -13.720 1.00 13.17 ? 40  HIS C CB  1 
ATOM   2050 C  CG  . HIS C 1 40  ? 27.855 2.672   -12.231 1.00 14.08 ? 40  HIS C CG  1 
ATOM   2051 N  ND1 . HIS C 1 40  ? 26.910 1.996   -11.490 1.00 14.80 ? 40  HIS C ND1 1 
ATOM   2052 C  CD2 . HIS C 1 40  ? 28.668 3.285   -11.344 1.00 14.93 ? 40  HIS C CD2 1 
ATOM   2053 C  CE1 . HIS C 1 40  ? 27.153 2.180   -10.208 1.00 15.81 ? 40  HIS C CE1 1 
ATOM   2054 N  NE2 . HIS C 1 40  ? 28.211 2.963   -10.090 1.00 15.74 ? 40  HIS C NE2 1 
ATOM   2055 N  N   . VAL C 1 41  ? 31.301 3.018   -13.400 1.00 12.50 ? 41  VAL C N   1 
ATOM   2056 C  CA  . VAL C 1 41  ? 32.537 2.350   -12.989 1.00 12.89 ? 41  VAL C CA  1 
ATOM   2057 C  C   . VAL C 1 41  ? 32.645 2.440   -11.483 1.00 12.60 ? 41  VAL C C   1 
ATOM   2058 O  O   . VAL C 1 41  ? 32.470 3.528   -10.915 1.00 13.21 ? 41  VAL C O   1 
ATOM   2059 C  CB  . VAL C 1 41  ? 33.771 2.977   -13.668 1.00 15.36 ? 41  VAL C CB  1 
ATOM   2060 C  CG1 . VAL C 1 41  ? 35.078 2.313   -13.205 1.00 15.66 ? 41  VAL C CG1 1 
ATOM   2061 C  CG2 . VAL C 1 41  ? 33.607 2.890   -15.182 1.00 17.65 ? 41  VAL C CG2 1 
ATOM   2062 N  N   . VAL C 1 42  ? 32.912 1.297   -10.853 1.00 12.41 ? 42  VAL C N   1 
ATOM   2063 C  CA  . VAL C 1 42  ? 32.920 1.173   -9.402  1.00 12.75 ? 42  VAL C CA  1 
ATOM   2064 C  C   . VAL C 1 42  ? 34.273 0.635   -8.974  1.00 12.79 ? 42  VAL C C   1 
ATOM   2065 O  O   . VAL C 1 42  ? 34.493 -0.576  -9.013  1.00 13.13 ? 42  VAL C O   1 
ATOM   2066 C  CB  . VAL C 1 42  ? 31.787 0.272   -8.894  1.00 14.38 ? 42  VAL C CB  1 
ATOM   2067 C  CG1 . VAL C 1 42  ? 31.701 0.466   -7.405  1.00 16.40 ? 42  VAL C CG1 1 
ATOM   2068 C  CG2 . VAL C 1 42  ? 30.459 0.660   -9.537  1.00 15.54 ? 42  VAL C CG2 1 
ATOM   2069 N  N   . PRO C 1 43  ? 35.201 1.494   -8.617  1.00 13.40 ? 43  PRO C N   1 
ATOM   2070 C  CA  . PRO C 1 43  ? 36.537 1.020   -8.222  1.00 13.93 ? 43  PRO C CA  1 
ATOM   2071 C  C   . PRO C 1 43  ? 36.610 0.716   -6.738  1.00 13.13 ? 43  PRO C C   1 
ATOM   2072 O  O   . PRO C 1 43  ? 35.622 0.843   -6.002  1.00 13.75 ? 43  PRO C O   1 
ATOM   2073 C  CB  . PRO C 1 43  ? 37.447 2.198   -8.594  1.00 15.44 ? 43  PRO C CB  1 
ATOM   2074 C  CG  . PRO C 1 43  ? 36.554 3.414   -8.379  1.00 16.69 ? 43  PRO C CG  1 
ATOM   2075 C  CD  . PRO C 1 43  ? 35.130 2.969   -8.731  1.00 15.09 ? 43  PRO C CD  1 
ATOM   2076 N  N   . ASP C 1 44  ? 37.779 0.269   -6.296  1.00 13.84 ? 44  ASP C N   1 
ATOM   2077 C  CA  . ASP C 1 44  ? 38.065 0.086   -4.866  1.00 15.54 ? 44  ASP C CA  1 
ATOM   2078 C  C   . ASP C 1 44  ? 37.195 -0.987  -4.223  1.00 14.58 ? 44  ASP C C   1 
ATOM   2079 O  O   . ASP C 1 44  ? 36.991 -0.976  -3.014  1.00 15.58 ? 44  ASP C O   1 
ATOM   2080 C  CB  . ASP C 1 44  ? 37.963 1.396   -4.068  1.00 19.84 ? 44  ASP C CB  1 
ATOM   2081 C  CG  . ASP C 1 44  ? 39.020 2.373   -4.448  1.00 25.23 ? 44  ASP C CG  1 
ATOM   2082 O  OD1 . ASP C 1 44  ? 40.194 2.035   -4.222  1.00 26.54 ? 44  ASP C OD1 1 
ATOM   2083 O  OD2 . ASP C 1 44  ? 38.676 3.447   -4.976  1.00 28.18 ? 44  ASP C OD2 1 
ATOM   2084 N  N   . GLN C 1 45  ? 36.718 -1.954  -5.007  1.00 13.20 ? 45  GLN C N   1 
ATOM   2085 C  CA  . GLN C 1 45  ? 35.836 -2.970  -4.453  1.00 12.90 ? 45  GLN C CA  1 
ATOM   2086 C  C   . GLN C 1 45  ? 36.591 -4.115  -3.793  1.00 13.08 ? 45  GLN C C   1 
ATOM   2087 O  O   . GLN C 1 45  ? 37.732 -4.407  -4.125  1.00 14.52 ? 45  GLN C O   1 
ATOM   2088 C  CB  . GLN C 1 45  ? 34.947 -3.519  -5.565  1.00 12.98 ? 45  GLN C CB  1 
ATOM   2089 C  CG  . GLN C 1 45  ? 34.012 -2.460  -6.140  1.00 13.21 ? 45  GLN C CG  1 
ATOM   2090 C  CD  . GLN C 1 45  ? 33.158 -1.877  -5.054  1.00 13.51 ? 45  GLN C CD  1 
ATOM   2091 O  OE1 . GLN C 1 45  ? 32.215 -2.515  -4.598  1.00 14.89 ? 45  GLN C OE1 1 
ATOM   2092 N  NE2 . GLN C 1 45  ? 33.481 -0.676  -4.610  1.00 14.06 ? 45  GLN C NE2 1 
ATOM   2093 N  N   . LEU C 1 46  ? 35.924 -4.770  -2.849  1.00 12.56 ? 46  LEU C N   1 
ATOM   2094 C  CA  . LEU C 1 46  ? 36.415 -5.970  -2.171  1.00 12.57 ? 46  LEU C CA  1 
ATOM   2095 C  C   . LEU C 1 46  ? 35.950 -7.158  -2.999  1.00 11.75 ? 46  LEU C C   1 
ATOM   2096 O  O   . LEU C 1 46  ? 34.775 -7.550  -2.951  1.00 12.99 ? 46  LEU C O   1 
ATOM   2097 C  CB  . LEU C 1 46  ? 35.818 -6.023  -0.765  1.00 14.11 ? 46  LEU C CB  1 
ATOM   2098 C  CG  . LEU C 1 46  ? 36.165 -7.223  0.126   1.00 17.00 ? 46  LEU C CG  1 
ATOM   2099 C  CD1 . LEU C 1 46  ? 37.661 -7.330  0.354   1.00 18.11 ? 46  LEU C CD1 1 
ATOM   2100 C  CD2 . LEU C 1 46  ? 35.443 -7.117  1.467   1.00 18.26 ? 46  LEU C CD2 1 
ATOM   2101 N  N   . MET C 1 47  ? 36.848 -7.707  -3.808  1.00 12.59 ? 47  MET C N   1 
ATOM   2102 C  CA  . MET C 1 47  ? 36.468 -8.726  -4.773  1.00 13.82 ? 47  MET C CA  1 
ATOM   2103 C  C   . MET C 1 47  ? 37.597 -9.723  -4.914  1.00 13.09 ? 47  MET C C   1 
ATOM   2104 O  O   . MET C 1 47  ? 38.767 -9.414  -4.686  1.00 14.08 ? 47  MET C O   1 
ATOM   2105 C  CB  . MET C 1 47  ? 36.294 -8.102  -6.174  1.00 18.64 ? 47  MET C CB  1 
ATOM   2106 C  CG  . MET C 1 47  ? 35.286 -7.022  -6.271  1.00 20.35 ? 47  MET C CG  1 
ATOM   2107 S  SD  . MET C 1 47  ? 35.269 -6.205  -7.854  1.00 18.88 ? 47  MET C SD  1 
ATOM   2108 C  CE  . MET C 1 47  ? 35.862 -7.402  -8.793  1.00 15.71 ? 47  MET C CE  1 
ATOM   2109 N  N   . ALA C 1 48  ? 37.239 -10.908 -5.384  1.00 12.24 ? 48  ALA C N   1 
ATOM   2110 C  CA  . ALA C 1 48  ? 38.220 -11.923 -5.730  1.00 12.56 ? 48  ALA C CA  1 
ATOM   2111 C  C   . ALA C 1 48  ? 37.735 -12.635 -6.983  1.00 12.14 ? 48  ALA C C   1 
ATOM   2112 O  O   . ALA C 1 48  ? 36.527 -12.722 -7.254  1.00 11.92 ? 48  ALA C O   1 
ATOM   2113 C  CB  . ALA C 1 48  ? 38.438 -12.962 -4.618  1.00 14.34 ? 48  ALA C CB  1 
ATOM   2114 N  N   . PHE C 1 49  ? 38.682 -13.153 -7.747  1.00 12.22 ? 49  PHE C N   1 
ATOM   2115 C  CA  . PHE C 1 49  ? 38.386 -13.884 -8.972  1.00 12.55 ? 49  PHE C CA  1 
ATOM   2116 C  C   . PHE C 1 49  ? 39.263 -15.128 -8.890  1.00 12.75 ? 49  PHE C C   1 
ATOM   2117 O  O   . PHE C 1 49  ? 40.493 -15.012 -8.794  1.00 13.07 ? 49  PHE C O   1 
ATOM   2118 C  CB  . PHE C 1 49  ? 38.710 -13.022 -10.201 1.00 12.98 ? 49  PHE C CB  1 
ATOM   2119 C  CG  . PHE C 1 49  ? 38.239 -13.600 -11.504 1.00 13.50 ? 49  PHE C CG  1 
ATOM   2120 C  CD1 . PHE C 1 49  ? 38.856 -14.733 -12.047 1.00 14.70 ? 49  PHE C CD1 1 
ATOM   2121 C  CD2 . PHE C 1 49  ? 37.196 -13.022 -12.208 1.00 14.86 ? 49  PHE C CD2 1 
ATOM   2122 C  CE1 . PHE C 1 49  ? 38.427 -15.278 -13.253 1.00 16.03 ? 49  PHE C CE1 1 
ATOM   2123 C  CE2 . PHE C 1 49  ? 36.767 -13.567 -13.422 1.00 16.00 ? 49  PHE C CE2 1 
ATOM   2124 C  CZ  . PHE C 1 49  ? 37.385 -14.683 -13.943 1.00 16.35 ? 49  PHE C CZ  1 
ATOM   2125 N  N   . GLY C 1 50  ? 38.646 -16.310 -8.854  1.00 13.32 ? 50  GLY C N   1 
ATOM   2126 C  CA  . GLY C 1 50  ? 39.403 -17.546 -8.664  1.00 14.77 ? 50  GLY C CA  1 
ATOM   2127 C  C   . GLY C 1 50  ? 40.123 -17.586 -7.330  1.00 15.29 ? 50  GLY C C   1 
ATOM   2128 O  O   . GLY C 1 50  ? 41.151 -18.252 -7.208  1.00 16.93 ? 50  GLY C O   1 
ATOM   2129 N  N   . GLY C 1 51  ? 39.612 -16.882 -6.314  1.00 14.82 ? 51  GLY C N   1 
ATOM   2130 C  CA  . GLY C 1 51  ? 40.222 -16.853 -5.003  1.00 15.91 ? 51  GLY C CA  1 
ATOM   2131 C  C   . GLY C 1 51  ? 41.313 -15.831 -4.837  1.00 16.98 ? 51  GLY C C   1 
ATOM   2132 O  O   . GLY C 1 51  ? 41.766 -15.628 -3.706  1.00 19.30 ? 51  GLY C O   1 
ATOM   2133 N  N   . SER C 1 52  ? 41.704 -15.142 -5.903  1.00 16.15 ? 52  SER C N   1 
ATOM   2134 C  CA  . SER C 1 52  ? 42.814 -14.193 -5.895  1.00 17.07 ? 52  SER C CA  1 
ATOM   2135 C  C   . SER C 1 52  ? 42.265 -12.777 -5.985  1.00 16.21 ? 52  SER C C   1 
ATOM   2136 O  O   . SER C 1 52  ? 41.269 -12.526 -6.669  1.00 14.93 ? 52  SER C O   1 
ATOM   2137 C  CB  . SER C 1 52  ? 43.693 -14.426 -7.143  1.00 19.16 ? 52  SER C CB  1 
ATOM   2138 O  OG  . SER C 1 52  ? 44.552 -13.319 -7.437  1.00 21.93 ? 52  SER C OG  1 
ATOM   2139 N  N   . SER C 1 53  ? 42.879 -11.849 -5.257  1.00 16.82 ? 53  SER C N   1 
ATOM   2140 C  CA  . SER C 1 53  ? 42.484 -10.455 -5.296  1.00 17.99 ? 53  SER C CA  1 
ATOM   2141 C  C   . SER C 1 53  ? 43.455 -9.614  -6.097  1.00 17.62 ? 53  SER C C   1 
ATOM   2142 O  O   . SER C 1 53  ? 43.490 -8.393  -5.928  1.00 17.79 ? 53  SER C O   1 
ATOM   2143 C  CB  . SER C 1 53  ? 42.231 -9.891  -3.896  1.00 20.12 ? 53  SER C CB  1 
ATOM   2144 O  OG  . SER C 1 53  ? 40.992 -10.414 -3.423  1.00 20.99 ? 53  SER C OG  1 
ATOM   2145 N  N   . GLU C 1 54  ? 44.197 -10.240 -7.009  1.00 17.33 ? 54  GLU C N   1 
ATOM   2146 C  CA  . GLU C 1 54  ? 44.839 -9.477  -8.064  1.00 18.73 ? 54  GLU C CA  1 
ATOM   2147 C  C   . GLU C 1 54  ? 43.767 -8.714  -8.848  1.00 16.00 ? 54  GLU C C   1 
ATOM   2148 O  O   . GLU C 1 54  ? 42.583 -9.060  -8.810  1.00 15.53 ? 54  GLU C O   1 
ATOM   2149 C  CB  . GLU C 1 54  ? 45.654 -10.423 -8.960  1.00 23.39 ? 54  GLU C CB  1 
ATOM   2150 C  CG  . GLU C 1 54  ? 46.747 -11.132 -8.132  1.00 29.67 ? 54  GLU C CG  1 
ATOM   2151 C  CD  . GLU C 1 54  ? 47.616 -10.158 -7.344  1.00 35.68 ? 54  GLU C CD  1 
ATOM   2152 O  OE1 . GLU C 1 54  ? 47.857 -9.025  -7.839  1.00 37.80 ? 54  GLU C OE1 1 
ATOM   2153 O  OE2 . GLU C 1 54  ? 47.981 -10.498 -6.188  1.00 37.62 ? 54  GLU C OE2 1 
ATOM   2154 N  N   . PRO C 1 55  ? 44.143 -7.681  -9.601  1.00 15.79 ? 55  PRO C N   1 
ATOM   2155 C  CA  . PRO C 1 55  ? 43.120 -6.879  -10.295 1.00 15.16 ? 55  PRO C CA  1 
ATOM   2156 C  C   . PRO C 1 55  ? 42.175 -7.750  -11.113 1.00 13.91 ? 55  PRO C C   1 
ATOM   2157 O  O   . PRO C 1 55  ? 42.579 -8.685  -11.807 1.00 13.86 ? 55  PRO C O   1 
ATOM   2158 C  CB  . PRO C 1 55  ? 43.954 -5.944  -11.172 1.00 15.89 ? 55  PRO C CB  1 
ATOM   2159 C  CG  . PRO C 1 55  ? 45.243 -5.756  -10.368 1.00 17.04 ? 55  PRO C CG  1 
ATOM   2160 C  CD  . PRO C 1 55  ? 45.497 -7.104  -9.731  1.00 16.99 ? 55  PRO C CD  1 
ATOM   2161 N  N   . CYS C 1 56  ? 40.883 -7.466  -10.989 1.00 12.38 ? 56  CYS C N   1 
ATOM   2162 C  CA  . CYS C 1 56  ? 39.844 -8.219  -11.686 1.00 12.69 ? 56  CYS C CA  1 
ATOM   2163 C  C   . CYS C 1 56  ? 38.671 -7.287  -11.903 1.00 12.46 ? 56  CYS C C   1 
ATOM   2164 O  O   . CYS C 1 56  ? 38.625 -6.182  -11.353 1.00 12.83 ? 56  CYS C O   1 
ATOM   2165 C  CB  . CYS C 1 56  ? 39.447 -9.477  -10.889 1.00 13.87 ? 56  CYS C CB  1 
ATOM   2166 S  SG  . CYS C 1 56  ? 38.763 -9.162  -9.244  1.00 15.39 ? 56  CYS C SG  1 
ATOM   2167 N  N   . ALA C 1 57  ? 37.713 -7.738  -12.701 1.00 12.29 ? 57  ALA C N   1 
ATOM   2168 C  CA  . ALA C 1 57  ? 36.519 -6.951  -12.922 1.00 13.02 ? 57  ALA C CA  1 
ATOM   2169 C  C   . ALA C 1 57  ? 35.324 -7.854  -13.164 1.00 11.59 ? 57  ALA C C   1 
ATOM   2170 O  O   . ALA C 1 57  ? 35.437 -8.897  -13.821 1.00 12.61 ? 57  ALA C O   1 
ATOM   2171 C  CB  . ALA C 1 57  ? 36.657 -6.005  -14.122 1.00 14.24 ? 57  ALA C CB  1 
ATOM   2172 N  N   . LEU C 1 58  ? 34.171 -7.424  -12.656 1.00 11.76 ? 58  LEU C N   1 
ATOM   2173 C  CA  . LEU C 1 58  ? 32.883 -8.055  -12.914 1.00 12.28 ? 58  LEU C CA  1 
ATOM   2174 C  C   . LEU C 1 58  ? 32.013 -6.987  -13.535 1.00 11.39 ? 58  LEU C C   1 
ATOM   2175 O  O   . LEU C 1 58  ? 31.849 -5.896  -12.970 1.00 11.65 ? 58  LEU C O   1 
ATOM   2176 C  CB  . LEU C 1 58  ? 32.246 -8.564  -11.626 1.00 13.28 ? 58  LEU C CB  1 
ATOM   2177 C  CG  . LEU C 1 58  ? 33.093 -9.613  -10.907 1.00 15.39 ? 58  LEU C CG  1 
ATOM   2178 C  CD1 . LEU C 1 58  ? 32.430 -9.985  -9.605  1.00 17.17 ? 58  LEU C CD1 1 
ATOM   2179 C  CD2 . LEU C 1 58  ? 33.284 -10.858 -11.792 1.00 15.84 ? 58  LEU C CD2 1 
ATOM   2180 N  N   . CYS C 1 59  ? 31.487 -7.272  -14.712 1.00 11.57 ? 59  CYS C N   1 
ATOM   2181 C  CA  . CYS C 1 59  ? 30.805 -6.261  -15.506 1.00 11.85 ? 59  CYS C CA  1 
ATOM   2182 C  C   . CYS C 1 59  ? 29.480 -6.774  -16.019 1.00 11.42 ? 59  CYS C C   1 
ATOM   2183 O  O   . CYS C 1 59  ? 29.252 -7.982  -16.113 1.00 11.93 ? 59  CYS C O   1 
ATOM   2184 C  CB  . CYS C 1 59  ? 31.640 -5.903  -16.743 1.00 12.71 ? 59  CYS C CB  1 
ATOM   2185 S  SG  . CYS C 1 59  ? 33.365 -5.532  -16.454 1.00 14.99 ? 59  CYS C SG  1 
ATOM   2186 N  N   . SER C 1 60  ? 28.644 -5.837  -16.458 1.00 11.86 ? 60  SER C N   1 
ATOM   2187 C  CA  . SER C 1 60  ? 27.431 -6.238  -17.146 1.00 12.56 ? 60  SER C CA  1 
ATOM   2188 C  C   . SER C 1 60  ? 27.116 -5.255  -18.254 1.00 11.87 ? 60  SER C C   1 
ATOM   2189 O  O   . SER C 1 60  ? 27.400 -4.060  -18.149 1.00 12.31 ? 60  SER C O   1 
ATOM   2190 C  CB  . SER C 1 60  ? 26.240 -6.320  -16.207 1.00 13.75 ? 60  SER C CB  1 
ATOM   2191 O  OG  . SER C 1 60  ? 25.982 -5.067  -15.587 1.00 14.49 ? 60  SER C OG  1 
ATOM   2192 N  N   . LEU C 1 61  ? 26.485 -5.763  -19.311 1.00 12.00 ? 61  LEU C N   1 
ATOM   2193 C  CA  . LEU C 1 61  ? 25.952 -4.926  -20.383 1.00 12.60 ? 61  LEU C CA  1 
ATOM   2194 C  C   . LEU C 1 61  ? 24.491 -5.308  -20.579 1.00 12.29 ? 61  LEU C C   1 
ATOM   2195 O  O   . LEU C 1 61  ? 24.183 -6.461  -20.917 1.00 12.63 ? 61  LEU C O   1 
ATOM   2196 C  CB  . LEU C 1 61  ? 26.709 -5.179  -21.688 1.00 12.98 ? 61  LEU C CB  1 
ATOM   2197 C  CG  . LEU C 1 61  ? 26.214 -4.360  -22.890 1.00 14.18 ? 61  LEU C CG  1 
ATOM   2198 C  CD1 . LEU C 1 61  ? 26.419 -2.860  -22.648 1.00 15.27 ? 61  LEU C CD1 1 
ATOM   2199 C  CD2 . LEU C 1 61  ? 26.940 -4.781  -24.157 1.00 16.12 ? 61  LEU C CD2 1 
ATOM   2200 N  N   . HIS C 1 62  ? 23.597 -4.343  -20.383 1.00 12.70 ? 62  HIS C N   1 
ATOM   2201 C  CA  . HIS C 1 62  ? 22.170 -4.504  -20.645 1.00 12.86 ? 62  HIS C CA  1 
ATOM   2202 C  C   . HIS C 1 62  ? 21.827 -3.671  -21.867 1.00 13.23 ? 62  HIS C C   1 
ATOM   2203 O  O   . HIS C 1 62  ? 22.237 -2.508  -21.971 1.00 13.74 ? 62  HIS C O   1 
ATOM   2204 C  CB  . HIS C 1 62  ? 21.331 -3.988  -19.463 1.00 14.04 ? 62  HIS C CB  1 
ATOM   2205 C  CG  . HIS C 1 62  ? 21.463 -4.784  -18.206 1.00 15.72 ? 62  HIS C CG  1 
ATOM   2206 N  ND1 . HIS C 1 62  ? 22.575 -4.746  -17.396 1.00 16.81 ? 62  HIS C ND1 1 
ATOM   2207 C  CD2 . HIS C 1 62  ? 20.592 -5.627  -17.616 1.00 16.41 ? 62  HIS C CD2 1 
ATOM   2208 C  CE1 . HIS C 1 62  ? 22.378 -5.534  -16.352 1.00 16.72 ? 62  HIS C CE1 1 
ATOM   2209 N  NE2 . HIS C 1 62  ? 21.183 -6.088  -16.467 1.00 17.54 ? 62  HIS C NE2 1 
ATOM   2210 N  N   . SER C 1 63  ? 21.082 -4.253  -22.794 1.00 13.22 ? 63  SER C N   1 
ATOM   2211 C  CA  . SER C 1 63  ? 20.715 -3.524  -23.992 1.00 13.62 ? 63  SER C CA  1 
ATOM   2212 C  C   . SER C 1 63  ? 19.405 -4.071  -24.502 1.00 13.29 ? 63  SER C C   1 
ATOM   2213 O  O   . SER C 1 63  ? 19.137 -5.262  -24.387 1.00 13.40 ? 63  SER C O   1 
ATOM   2214 C  CB  . SER C 1 63  ? 21.782 -3.732  -25.084 1.00 14.06 ? 63  SER C CB  1 
ATOM   2215 O  OG  . SER C 1 63  ? 21.485 -3.026  -26.284 1.00 15.12 ? 63  SER C OG  1 
ATOM   2216 N  N   . ILE C 1 64  ? 18.602 -3.199  -25.107 1.00 13.25 ? 64  ILE C N   1 
ATOM   2217 C  CA  . ILE C 1 64  ? 17.396 -3.627  -25.820 1.00 13.94 ? 64  ILE C CA  1 
ATOM   2218 C  C   . ILE C 1 64  ? 17.847 -4.095  -27.199 1.00 14.15 ? 64  ILE C C   1 
ATOM   2219 O  O   . ILE C 1 64  ? 18.092 -3.282  -28.089 1.00 15.64 ? 64  ILE C O   1 
ATOM   2220 C  CB  . ILE C 1 64  ? 16.371 -2.498  -25.915 1.00 14.84 ? 64  ILE C CB  1 
ATOM   2221 C  CG1 . ILE C 1 64  ? 15.967 -2.060  -24.496 1.00 15.72 ? 64  ILE C CG1 1 
ATOM   2222 C  CG2 . ILE C 1 64  ? 15.163 -2.973  -26.738 1.00 15.69 ? 64  ILE C CG2 1 
ATOM   2223 C  CD1 . ILE C 1 64  ? 15.169 -0.733  -24.487 1.00 16.45 ? 64  ILE C CD1 1 
ATOM   2224 N  N   . GLY C 1 65  ? 18.010 -5.406  -27.371 1.00 14.56 ? 65  GLY C N   1 
ATOM   2225 C  CA  . GLY C 1 65  ? 18.582 -5.921  -28.591 1.00 15.53 ? 65  GLY C CA  1 
ATOM   2226 C  C   . GLY C 1 65  ? 20.085 -5.701  -28.659 1.00 15.07 ? 65  GLY C C   1 
ATOM   2227 O  O   . GLY C 1 65  ? 20.724 -5.265  -27.706 1.00 15.48 ? 65  GLY C O   1 
ATOM   2228 N  N   . LYS C 1 66  ? 20.647 -6.035  -29.820 1.00 15.14 ? 66  LYS C N   1 
ATOM   2229 C  CA  . LYS C 1 66  ? 22.084 -5.958  -30.055 1.00 15.53 ? 66  LYS C CA  1 
ATOM   2230 C  C   . LYS C 1 66  ? 22.860 -6.870  -29.104 1.00 15.73 ? 66  LYS C C   1 
ATOM   2231 O  O   . LYS C 1 66  ? 24.023 -6.622  -28.783 1.00 16.94 ? 66  LYS C O   1 
ATOM   2232 C  CB  . LYS C 1 66  ? 22.584 -4.512  -30.019 1.00 16.62 ? 66  LYS C CB  1 
ATOM   2233 C  CG  . LYS C 1 66  ? 21.852 -3.595  -30.965 1.00 18.12 ? 66  LYS C CG  1 
ATOM   2234 C  CD  . LYS C 1 66  ? 22.009 -4.131  -32.407 1.00 20.97 ? 66  LYS C CD  1 
ATOM   2235 C  CE  . LYS C 1 66  ? 21.568 -3.139  -33.431 1.00 23.76 ? 66  LYS C CE  1 
ATOM   2236 N  NZ  . LYS C 1 66  ? 22.508 -2.007  -33.449 1.00 25.08 ? 66  LYS C NZ  1 
ATOM   2237 N  N   . ILE C 1 67  ? 22.244 -7.975  -28.694 1.00 14.50 ? 67  ILE C N   1 
ATOM   2238 C  CA  . ILE C 1 67  ? 22.870 -8.984  -27.836 1.00 14.33 ? 67  ILE C CA  1 
ATOM   2239 C  C   . ILE C 1 67  ? 22.755 -10.328 -28.554 1.00 15.60 ? 67  ILE C C   1 
ATOM   2240 O  O   . ILE C 1 67  ? 21.684 -10.660 -29.079 1.00 17.53 ? 67  ILE C O   1 
ATOM   2241 C  CB  . ILE C 1 67  ? 22.165 -9.045  -26.468 1.00 14.99 ? 67  ILE C CB  1 
ATOM   2242 C  CG1 . ILE C 1 67  ? 22.312 -7.719  -25.723 1.00 15.30 ? 67  ILE C CG1 1 
ATOM   2243 C  CG2 . ILE C 1 67  ? 22.651 -10.218 -25.617 1.00 14.68 ? 67  ILE C CG2 1 
ATOM   2244 C  CD1 . ILE C 1 67  ? 23.716 -7.420  -25.217 1.00 16.43 ? 67  ILE C CD1 1 
ATOM   2245 N  N   . GLY C 1 68  ? 23.835 -11.095 -28.598 1.00 15.87 ? 68  GLY C N   1 
ATOM   2246 C  CA  . GLY C 1 68  ? 23.745 -12.374 -29.287 1.00 15.95 ? 68  GLY C CA  1 
ATOM   2247 C  C   . GLY C 1 68  ? 25.111 -13.016 -29.307 1.00 15.42 ? 68  GLY C C   1 
ATOM   2248 O  O   . GLY C 1 68  ? 26.081 -12.436 -28.846 1.00 15.37 ? 68  GLY C O   1 
ATOM   2249 N  N   . GLY C 1 69  ? 25.189 -14.225 -29.862 1.00 16.00 ? 69  GLY C N   1 
ATOM   2250 C  CA  . GLY C 1 69  ? 26.428 -14.986 -29.822 1.00 16.55 ? 69  GLY C CA  1 
ATOM   2251 C  C   . GLY C 1 69  ? 27.620 -14.227 -30.371 1.00 16.33 ? 69  GLY C C   1 
ATOM   2252 O  O   . GLY C 1 69  ? 28.628 -14.033 -29.675 1.00 16.04 ? 69  GLY C O   1 
ATOM   2253 N  N   . ALA C 1 70  ? 27.533 -13.821 -31.643 1.00 16.16 ? 70  ALA C N   1 
ATOM   2254 C  CA  . ALA C 1 70  ? 28.649 -13.143 -32.299 1.00 17.12 ? 70  ALA C CA  1 
ATOM   2255 C  C   . ALA C 1 70  ? 28.862 -11.762 -31.707 1.00 16.09 ? 70  ALA C C   1 
ATOM   2256 O  O   . ALA C 1 70  ? 30.008 -11.345 -31.441 1.00 15.47 ? 70  ALA C O   1 
ATOM   2257 C  CB  . ALA C 1 70  ? 28.377 -13.045 -33.808 1.00 18.44 ? 70  ALA C CB  1 
ATOM   2258 N  N   . GLN C 1 71  ? 27.772 -11.040 -31.472 1.00 15.41 ? 71  GLN C N   1 
ATOM   2259 C  CA  . GLN C 1 71  ? 27.922 -9.698  -30.931 1.00 14.77 ? 71  GLN C CA  1 
ATOM   2260 C  C   . GLN C 1 71  ? 28.588 -9.731  -29.573 1.00 14.47 ? 71  GLN C C   1 
ATOM   2261 O  O   . GLN C 1 71  ? 29.446 -8.896  -29.282 1.00 14.43 ? 71  GLN C O   1 
ATOM   2262 C  CB  . GLN C 1 71  ? 26.569 -9.028  -30.849 1.00 16.29 ? 71  GLN C CB  1 
ATOM   2263 C  CG  . GLN C 1 71  ? 26.007 -8.728  -32.217 1.00 18.14 ? 71  GLN C CG  1 
ATOM   2264 C  CD  . GLN C 1 71  ? 24.603 -8.208  -32.145 1.00 19.71 ? 71  GLN C CD  1 
ATOM   2265 O  OE1 . GLN C 1 71  ? 24.382 -6.993  -32.168 1.00 20.85 ? 71  GLN C OE1 1 
ATOM   2266 N  NE2 . GLN C 1 71  ? 23.639 -9.110  -32.014 1.00 19.77 ? 71  GLN C NE2 1 
ATOM   2267 N  N   . ASN C 1 72  ? 28.220 -10.696 -28.726 1.00 13.62 ? 72  ASN C N   1 
ATOM   2268 C  CA  . ASN C 1 72  ? 28.786 -10.709 -27.383 1.00 13.65 ? 72  ASN C CA  1 
ATOM   2269 C  C   . ASN C 1 72  ? 30.255 -11.097 -27.404 1.00 13.38 ? 72  ASN C C   1 
ATOM   2270 O  O   . ASN C 1 72  ? 31.036 -10.634 -26.567 1.00 13.66 ? 72  ASN C O   1 
ATOM   2271 C  CB  . ASN C 1 72  ? 28.023 -11.659 -26.462 1.00 13.54 ? 72  ASN C CB  1 
ATOM   2272 C  CG  . ASN C 1 72  ? 26.568 -11.264 -26.259 1.00 13.52 ? 72  ASN C CG  1 
ATOM   2273 O  OD1 . ASN C 1 72  ? 26.121 -10.184 -26.670 1.00 13.50 ? 72  ASN C OD1 1 
ATOM   2274 N  ND2 . ASN C 1 72  ? 25.820 -12.142 -25.609 1.00 13.69 ? 72  ASN C ND2 1 
ATOM   2275 N  N   . ARG C 1 73  ? 30.655 -11.963 -28.323 1.00 13.48 ? 73  ARG C N   1 
ATOM   2276 C  CA  . ARG C 1 73  ? 32.083 -12.219 -28.488 1.00 14.23 ? 73  ARG C CA  1 
ATOM   2277 C  C   . ARG C 1 73  ? 32.820 -10.934 -28.879 1.00 14.46 ? 73  ARG C C   1 
ATOM   2278 O  O   . ARG C 1 73  ? 33.881 -10.623 -28.334 1.00 14.23 ? 73  ARG C O   1 
ATOM   2279 C  CB  . ARG C 1 73  ? 32.290 -13.304 -29.541 1.00 15.45 ? 73  ARG C CB  1 
ATOM   2280 C  CG  . ARG C 1 73  ? 32.031 -14.717 -29.009 1.00 17.41 ? 73  ARG C CG  1 
ATOM   2281 C  CD  . ARG C 1 73  ? 32.428 -15.746 -30.061 1.00 19.81 ? 73  ARG C CD  1 
ATOM   2282 N  NE  . ARG C 1 73  ? 31.481 -15.844 -31.170 1.00 21.89 ? 73  ARG C NE  1 
ATOM   2283 C  CZ  . ARG C 1 73  ? 30.343 -16.548 -31.107 1.00 23.30 ? 73  ARG C CZ  1 
ATOM   2284 N  NH1 . ARG C 1 73  ? 30.026 -17.193 -29.969 1.00 22.90 ? 73  ARG C NH1 1 
ATOM   2285 N  NH2 . ARG C 1 73  ? 29.509 -16.583 -32.155 1.00 24.14 ? 73  ARG C NH2 1 
ATOM   2286 N  N   . SER C 1 74  ? 32.246 -10.150 -29.779 1.00 15.00 ? 74  SER C N   1 
ATOM   2287 C  CA  . SER C 1 74  ? 32.876 -8.903  -30.186 1.00 15.68 ? 74  SER C CA  1 
ATOM   2288 C  C   . SER C 1 74  ? 32.919 -7.910  -29.033 1.00 14.82 ? 74  SER C C   1 
ATOM   2289 O  O   . SER C 1 74  ? 33.940 -7.249  -28.815 1.00 15.04 ? 74  SER C O   1 
ATOM   2290 C  CB  . SER C 1 74  ? 32.106 -8.332  -31.374 1.00 18.65 ? 74  SER C CB  1 
ATOM   2291 O  OG  . SER C 1 74  ? 32.763 -7.173  -31.837 1.00 20.85 ? 74  SER C OG  1 
ATOM   2292 N  N   . TYR C 1 75  ? 31.823 -7.787  -28.269 1.00 13.55 ? 75  TYR C N   1 
ATOM   2293 C  CA  . TYR C 1 75  ? 31.855 -6.874  -27.129 1.00 13.30 ? 75  TYR C CA  1 
ATOM   2294 C  C   . TYR C 1 75  ? 32.906 -7.309  -26.122 1.00 12.84 ? 75  TYR C C   1 
ATOM   2295 O  O   . TYR C 1 75  ? 33.536 -6.467  -25.480 1.00 13.41 ? 75  TYR C O   1 
ATOM   2296 C  CB  . TYR C 1 75  ? 30.505 -6.847  -26.421 1.00 13.32 ? 75  TYR C CB  1 
ATOM   2297 C  CG  . TYR C 1 75  ? 29.328 -6.392  -27.257 1.00 14.57 ? 75  TYR C CG  1 
ATOM   2298 C  CD1 . TYR C 1 75  ? 29.481 -5.477  -28.301 1.00 17.34 ? 75  TYR C CD1 1 
ATOM   2299 C  CD2 . TYR C 1 75  ? 28.049 -6.872  -26.993 1.00 14.65 ? 75  TYR C CD2 1 
ATOM   2300 C  CE1 . TYR C 1 75  ? 28.402 -5.063  -29.052 1.00 18.35 ? 75  TYR C CE1 1 
ATOM   2301 C  CE2 . TYR C 1 75  ? 26.959 -6.452  -27.716 1.00 16.05 ? 75  TYR C CE2 1 
ATOM   2302 C  CZ  . TYR C 1 75  ? 27.148 -5.550  -28.757 1.00 17.82 ? 75  TYR C CZ  1 
ATOM   2303 O  OH  . TYR C 1 75  ? 26.083 -5.135  -29.526 1.00 19.06 ? 75  TYR C OH  1 
ATOM   2304 N  N   . SER C 1 76  ? 33.045 -8.624  -25.911 1.00 12.84 ? 76  SER C N   1 
ATOM   2305 C  CA  . SER C 1 76  ? 33.985 -9.096  -24.901 1.00 12.64 ? 76  SER C CA  1 
ATOM   2306 C  C   . SER C 1 76  ? 35.414 -8.760  -25.297 1.00 13.31 ? 76  SER C C   1 
ATOM   2307 O  O   . SER C 1 76  ? 36.216 -8.378  -24.455 1.00 14.04 ? 76  SER C O   1 
ATOM   2308 C  CB  . SER C 1 76  ? 33.823 -10.599 -24.700 1.00 12.89 ? 76  SER C CB  1 
ATOM   2309 O  OG  . SER C 1 76  ? 32.554 -10.877 -24.161 1.00 14.01 ? 76  SER C OG  1 
ATOM   2310 N  N   . LYS C 1 77  ? 35.758 -8.913  -26.578 1.00 13.19 ? 77  LYS C N   1 
ATOM   2311 C  CA  . LYS C 1 77  ? 37.091 -8.534  -27.024 1.00 14.10 ? 77  LYS C CA  1 
ATOM   2312 C  C   . LYS C 1 77  ? 37.301 -7.030  -26.856 1.00 14.13 ? 77  LYS C C   1 
ATOM   2313 O  O   . LYS C 1 77  ? 38.358 -6.596  -26.388 1.00 14.56 ? 77  LYS C O   1 
ATOM   2314 C  CB  . LYS C 1 77  ? 37.281 -8.963  -28.481 1.00 15.92 ? 77  LYS C CB  1 
ATOM   2315 C  CG  . LYS C 1 77  ? 38.648 -8.638  -29.055 1.00 17.65 ? 77  LYS C CG  1 
ATOM   2316 C  CD  . LYS C 1 77  ? 38.719 -9.125  -30.492 1.00 19.80 ? 77  LYS C CD  1 
ATOM   2317 N  N   . LEU C 1 78  ? 36.305 -6.215  -27.229 1.00 14.06 ? 78  LEU C N   1 
ATOM   2318 C  CA  . LEU C 1 78  ? 36.428 -4.770  -27.084 1.00 14.50 ? 78  LEU C CA  1 
ATOM   2319 C  C   . LEU C 1 78  ? 36.600 -4.379  -25.621 1.00 14.18 ? 78  LEU C C   1 
ATOM   2320 O  O   . LEU C 1 78  ? 37.489 -3.593  -25.272 1.00 14.58 ? 78  LEU C O   1 
ATOM   2321 C  CB  . LEU C 1 78  ? 35.152 -4.142  -27.630 1.00 15.55 ? 78  LEU C CB  1 
ATOM   2322 C  CG  . LEU C 1 78  ? 35.000 -2.656  -27.305 1.00 17.98 ? 78  LEU C CG  1 
ATOM   2323 C  CD1 . LEU C 1 78  ? 35.983 -1.857  -28.139 1.00 19.44 ? 78  LEU C CD1 1 
ATOM   2324 C  CD2 . LEU C 1 78  ? 33.550 -2.185  -27.546 1.00 18.71 ? 78  LEU C CD2 1 
ATOM   2325 N  N   . LEU C 1 79  ? 35.724 -4.884  -24.751 1.00 13.66 ? 79  LEU C N   1 
ATOM   2326 C  CA  . LEU C 1 79  ? 35.698 -4.449  -23.358 1.00 13.12 ? 79  LEU C CA  1 
ATOM   2327 C  C   . LEU C 1 79  ? 36.876 -5.003  -22.572 1.00 14.14 ? 79  LEU C C   1 
ATOM   2328 O  O   . LEU C 1 79  ? 37.472 -4.276  -21.775 1.00 14.37 ? 79  LEU C O   1 
ATOM   2329 C  CB  . LEU C 1 79  ? 34.355 -4.805  -22.729 1.00 14.12 ? 79  LEU C CB  1 
ATOM   2330 C  CG  . LEU C 1 79  ? 33.190 -4.051  -23.372 1.00 15.57 ? 79  LEU C CG  1 
ATOM   2331 C  CD1 . LEU C 1 79  ? 31.871 -4.700  -22.973 1.00 15.68 ? 79  LEU C CD1 1 
ATOM   2332 C  CD2 . LEU C 1 79  ? 33.218 -2.576  -22.976 1.00 17.24 ? 79  LEU C CD2 1 
ATOM   2333 N  N   . CYS C 1 80  ? 37.214 -6.283  -22.753 1.00 14.01 ? 80  CYS C N   1 
ATOM   2334 C  CA  . CYS C 1 80  ? 38.434 -6.780  -22.121 1.00 13.80 ? 80  CYS C CA  1 
ATOM   2335 C  C   . CYS C 1 80  ? 39.648 -6.006  -22.600 1.00 14.53 ? 80  CYS C C   1 
ATOM   2336 O  O   . CYS C 1 80  ? 40.530 -5.672  -21.809 1.00 14.75 ? 80  CYS C O   1 
ATOM   2337 C  CB  . CYS C 1 80  ? 38.631 -8.273  -22.415 1.00 14.70 ? 80  CYS C CB  1 
ATOM   2338 S  SG  . CYS C 1 80  ? 37.433 -9.332  -21.548 1.00 15.83 ? 80  CYS C SG  1 
ATOM   2339 N  N   . GLY C 1 81  ? 39.697 -5.653  -23.883 1.00 15.11 ? 81  GLY C N   1 
ATOM   2340 C  CA  . GLY C 1 81  ? 40.820 -4.851  -24.348 1.00 15.41 ? 81  GLY C CA  1 
ATOM   2341 C  C   . GLY C 1 81  ? 40.903 -3.508  -23.645 1.00 15.78 ? 81  GLY C C   1 
ATOM   2342 O  O   . GLY C 1 81  ? 41.987 -3.086  -23.234 1.00 16.27 ? 81  GLY C O   1 
ATOM   2343 N  N   . LEU C 1 82  ? 39.757 -2.827  -23.475 1.00 15.93 ? 82  LEU C N   1 
ATOM   2344 C  CA  . LEU C 1 82  ? 39.776 -1.537  -22.781 1.00 15.85 ? 82  LEU C CA  1 
ATOM   2345 C  C   . LEU C 1 82  ? 40.175 -1.702  -21.324 1.00 15.41 ? 82  LEU C C   1 
ATOM   2346 O  O   . LEU C 1 82  ? 40.916 -0.880  -20.773 1.00 16.24 ? 82  LEU C O   1 
ATOM   2347 C  CB  . LEU C 1 82  ? 38.394 -0.884  -22.871 1.00 17.20 ? 82  LEU C CB  1 
ATOM   2348 C  CG  . LEU C 1 82  ? 38.064 -0.256  -24.214 1.00 18.63 ? 82  LEU C CG  1 
ATOM   2349 C  CD1 . LEU C 1 82  ? 36.576 0.065   -24.286 1.00 19.17 ? 82  LEU C CD1 1 
ATOM   2350 C  CD2 . LEU C 1 82  ? 38.916 1.022   -24.418 1.00 21.24 ? 82  LEU C CD2 1 
ATOM   2351 N  N   . LEU C 1 83  ? 39.679 -2.756  -20.672 1.00 14.65 ? 83  LEU C N   1 
ATOM   2352 C  CA  . LEU C 1 83  ? 40.024 -2.959  -19.271 1.00 14.78 ? 83  LEU C CA  1 
ATOM   2353 C  C   . LEU C 1 83  ? 41.499 -3.286  -19.111 1.00 14.90 ? 83  LEU C C   1 
ATOM   2354 O  O   . LEU C 1 83  ? 42.131 -2.878  -18.127 1.00 15.13 ? 83  LEU C O   1 
ATOM   2355 C  CB  . LEU C 1 83  ? 39.134 -4.052  -18.654 1.00 15.82 ? 83  LEU C CB  1 
ATOM   2356 C  CG  . LEU C 1 83  ? 37.663 -3.664  -18.528 1.00 16.48 ? 83  LEU C CG  1 
ATOM   2357 C  CD1 . LEU C 1 83  ? 36.840 -4.861  -18.126 1.00 18.00 ? 83  LEU C CD1 1 
ATOM   2358 C  CD2 . LEU C 1 83  ? 37.467 -2.528  -17.508 1.00 17.48 ? 83  LEU C CD2 1 
ATOM   2359 N  N   . ALA C 1 84  ? 42.063 -4.036  -20.063 1.00 15.02 ? 84  ALA C N   1 
ATOM   2360 C  CA  . ALA C 1 84  ? 43.484 -4.351  -20.018 1.00 15.77 ? 84  ALA C CA  1 
ATOM   2361 C  C   . ALA C 1 84  ? 44.313 -3.103  -20.258 1.00 16.52 ? 84  ALA C C   1 
ATOM   2362 O  O   . ALA C 1 84  ? 45.288 -2.834  -19.545 1.00 17.99 ? 84  ALA C O   1 
ATOM   2363 C  CB  . ALA C 1 84  ? 43.800 -5.418  -21.064 1.00 16.55 ? 84  ALA C CB  1 
ATOM   2364 N  N   . GLU C 1 85  ? 43.942 -2.325  -21.263 1.00 17.58 ? 85  GLU C N   1 
ATOM   2365 C  CA  . GLU C 1 85  ? 44.756 -1.177  -21.633 1.00 20.15 ? 85  GLU C CA  1 
ATOM   2366 C  C   . GLU C 1 85  ? 44.663 -0.068  -20.593 1.00 18.94 ? 85  GLU C C   1 
ATOM   2367 O  O   . GLU C 1 85  ? 45.673 0.541   -20.238 1.00 20.39 ? 85  GLU C O   1 
ATOM   2368 C  CB  . GLU C 1 85  ? 44.340 -0.667  -23.018 1.00 25.20 ? 85  GLU C CB  1 
ATOM   2369 C  CG  . GLU C 1 85  ? 44.836 0.721   -23.387 1.00 31.66 ? 85  GLU C CG  1 
ATOM   2370 C  CD  . GLU C 1 85  ? 44.205 1.236   -24.689 1.00 37.30 ? 85  GLU C CD  1 
ATOM   2371 O  OE1 . GLU C 1 85  ? 43.049 0.848   -25.035 1.00 39.16 ? 85  GLU C OE1 1 
ATOM   2372 O  OE2 . GLU C 1 85  ? 44.873 2.042   -25.363 1.00 39.45 ? 85  GLU C OE2 1 
ATOM   2373 N  N   . ARG C 1 86  ? 43.468 0.206   -20.088 1.00 17.54 ? 86  ARG C N   1 
ATOM   2374 C  CA  . ARG C 1 86  ? 43.261 1.373   -19.231 1.00 17.81 ? 86  ARG C CA  1 
ATOM   2375 C  C   . ARG C 1 86  ? 43.346 1.062   -17.747 1.00 17.71 ? 86  ARG C C   1 
ATOM   2376 O  O   . ARG C 1 86  ? 43.798 1.920   -16.981 1.00 18.94 ? 86  ARG C O   1 
ATOM   2377 C  CB  . ARG C 1 86  ? 41.895 2.011   -19.505 1.00 19.46 ? 86  ARG C CB  1 
ATOM   2378 C  CG  . ARG C 1 86  ? 41.690 2.455   -20.917 1.00 22.17 ? 86  ARG C CG  1 
ATOM   2379 C  CD  . ARG C 1 86  ? 42.738 3.436   -21.329 1.00 26.12 ? 86  ARG C CD  1 
ATOM   2380 N  NE  . ARG C 1 86  ? 42.371 4.053   -22.591 1.00 29.52 ? 86  ARG C NE  1 
ATOM   2381 C  CZ  . ARG C 1 86  ? 43.214 4.751   -23.338 1.00 32.09 ? 86  ARG C CZ  1 
ATOM   2382 N  NH1 . ARG C 1 86  ? 44.475 4.913   -22.943 1.00 33.53 ? 86  ARG C NH1 1 
ATOM   2383 N  NH2 . ARG C 1 86  ? 42.806 5.270   -24.483 1.00 32.62 ? 86  ARG C NH2 1 
ATOM   2384 N  N   . LEU C 1 87  ? 42.869 -0.106  -17.311 1.00 16.74 ? 87  LEU C N   1 
ATOM   2385 C  CA  . LEU C 1 87  ? 42.879 -0.447  -15.895 1.00 16.60 ? 87  LEU C CA  1 
ATOM   2386 C  C   . LEU C 1 87  ? 43.910 -1.508  -15.577 1.00 16.58 ? 87  LEU C C   1 
ATOM   2387 O  O   . LEU C 1 87  ? 44.098 -1.833  -14.404 1.00 17.01 ? 87  LEU C O   1 
ATOM   2388 C  CB  . LEU C 1 87  ? 41.491 -0.918  -15.416 1.00 16.76 ? 87  LEU C CB  1 
ATOM   2389 C  CG  . LEU C 1 87  ? 40.335 0.057   -15.538 1.00 18.61 ? 87  LEU C CG  1 
ATOM   2390 C  CD1 . LEU C 1 87  ? 39.101 -0.435  -14.792 1.00 18.68 ? 87  LEU C CD1 1 
ATOM   2391 C  CD2 . LEU C 1 87  ? 40.708 1.453   -15.086 1.00 19.79 ? 87  LEU C CD2 1 
ATOM   2392 N  N   . ARG C 1 88  ? 44.595 -2.034  -16.589 1.00 15.60 ? 88  ARG C N   1 
ATOM   2393 C  CA  . ARG C 1 88  ? 45.639 -3.037  -16.380 1.00 17.19 ? 88  ARG C CA  1 
ATOM   2394 C  C   . ARG C 1 88  ? 45.093 -4.319  -15.760 1.00 16.42 ? 88  ARG C C   1 
ATOM   2395 O  O   . ARG C 1 88  ? 45.758 -4.979  -14.954 1.00 18.05 ? 88  ARG C O   1 
ATOM   2396 C  CB  . ARG C 1 88  ? 46.840 -2.497  -15.590 1.00 19.82 ? 88  ARG C CB  1 
ATOM   2397 C  CG  . ARG C 1 88  ? 47.242 -1.059  -15.955 1.00 24.09 ? 88  ARG C CG  1 
ATOM   2398 C  CD  . ARG C 1 88  ? 47.510 -0.895  -17.425 1.00 28.93 ? 88  ARG C CD  1 
ATOM   2399 N  NE  . ARG C 1 88  ? 48.648 -1.684  -17.876 1.00 33.26 ? 88  ARG C NE  1 
ATOM   2400 C  CZ  . ARG C 1 88  ? 48.930 -1.920  -19.151 1.00 35.97 ? 88  ARG C CZ  1 
ATOM   2401 N  NH1 . ARG C 1 88  ? 50.002 -2.642  -19.469 1.00 36.78 ? 88  ARG C NH1 1 
ATOM   2402 N  NH2 . ARG C 1 88  ? 48.150 -1.423  -20.106 1.00 36.36 ? 88  ARG C NH2 1 
ATOM   2403 N  N   . ILE C 1 89  ? 43.872 -4.683  -16.122 1.00 14.33 ? 89  ILE C N   1 
ATOM   2404 C  CA  . ILE C 1 89  ? 43.251 -5.920  -15.677 1.00 14.21 ? 89  ILE C CA  1 
ATOM   2405 C  C   . ILE C 1 89  ? 43.417 -6.963  -16.768 1.00 14.53 ? 89  ILE C C   1 
ATOM   2406 O  O   . ILE C 1 89  ? 43.040 -6.733  -17.915 1.00 15.07 ? 89  ILE C O   1 
ATOM   2407 C  CB  . ILE C 1 89  ? 41.762 -5.703  -15.377 1.00 13.96 ? 89  ILE C CB  1 
ATOM   2408 C  CG1 . ILE C 1 89  ? 41.600 -4.644  -14.282 1.00 14.78 ? 89  ILE C CG1 1 
ATOM   2409 C  CG2 . ILE C 1 89  ? 41.121 -7.019  -14.952 1.00 14.68 ? 89  ILE C CG2 1 
ATOM   2410 C  CD1 . ILE C 1 89  ? 40.175 -4.165  -14.149 1.00 15.15 ? 89  ILE C CD1 1 
ATOM   2411 N  N   . SER C 1 90  ? 43.956 -8.126  -16.406 1.00 14.51 ? 90  SER C N   1 
ATOM   2412 C  CA  . SER C 1 90  ? 44.111 -9.200  -17.378 1.00 15.19 ? 90  SER C CA  1 
ATOM   2413 C  C   . SER C 1 90  ? 42.738 -9.671  -17.868 1.00 14.00 ? 90  SER C C   1 
ATOM   2414 O  O   . SER C 1 90  ? 41.817 -9.840  -17.066 1.00 13.92 ? 90  SER C O   1 
ATOM   2415 C  CB  . SER C 1 90  ? 44.801 -10.387 -16.705 1.00 17.85 ? 90  SER C CB  1 
ATOM   2416 O  OG  . SER C 1 90  ? 46.111 -10.028 -16.331 1.00 21.08 ? 90  SER C OG  1 
ATOM   2417 N  N   . PRO C 1 91  ? 42.582 -9.930  -19.174 1.00 14.63 ? 91  PRO C N   1 
ATOM   2418 C  CA  . PRO C 1 91  ? 41.283 -10.388 -19.683 1.00 14.08 ? 91  PRO C CA  1 
ATOM   2419 C  C   . PRO C 1 91  ? 40.779 -11.677 -19.064 1.00 13.27 ? 91  PRO C C   1 
ATOM   2420 O  O   . PRO C 1 91  ? 39.555 -11.895 -19.068 1.00 13.50 ? 91  PRO C O   1 
ATOM   2421 C  CB  . PRO C 1 91  ? 41.514 -10.509 -21.199 1.00 14.84 ? 91  PRO C CB  1 
ATOM   2422 C  CG  . PRO C 1 91  ? 42.577 -9.511  -21.483 1.00 17.10 ? 91  PRO C CG  1 
ATOM   2423 C  CD  . PRO C 1 91  ? 43.500 -9.548  -20.267 1.00 16.63 ? 91  PRO C CD  1 
ATOM   2424 N  N   . ASP C 1 92  ? 41.671 -12.545 -18.579 1.00 13.36 ? 92  ASP C N   1 
ATOM   2425 C  CA  . ASP C 1 92  ? 41.216 -13.780 -17.945 1.00 14.85 ? 92  ASP C CA  1 
ATOM   2426 C  C   . ASP C 1 92  ? 40.796 -13.568 -16.506 1.00 14.13 ? 92  ASP C C   1 
ATOM   2427 O  O   . ASP C 1 92  ? 40.471 -14.553 -15.829 1.00 14.65 ? 92  ASP C O   1 
ATOM   2428 C  CB  . ASP C 1 92  ? 42.228 -14.921 -18.114 1.00 16.83 ? 92  ASP C CB  1 
ATOM   2429 C  CG  . ASP C 1 92  ? 43.517 -14.692 -17.375 1.00 18.62 ? 92  ASP C CG  1 
ATOM   2430 O  OD1 . ASP C 1 92  ? 43.666 -13.661 -16.700 1.00 18.71 ? 92  ASP C OD1 1 
ATOM   2431 O  OD2 . ASP C 1 92  ? 44.422 -15.568 -17.470 1.00 21.10 ? 92  ASP C OD2 1 
ATOM   2432 N  N   . ARG C 1 93  ? 40.743 -12.316 -16.060 1.00 13.38 ? 93  ARG C N   1 
ATOM   2433 C  CA  . ARG C 1 93  ? 40.214 -11.964 -14.744 1.00 13.06 ? 93  ARG C CA  1 
ATOM   2434 C  C   . ARG C 1 93  ? 39.016 -11.025 -14.865 1.00 12.40 ? 93  ARG C C   1 
ATOM   2435 O  O   . ARG C 1 93  ? 38.763 -10.224 -13.969 1.00 12.88 ? 93  ARG C O   1 
ATOM   2436 C  CB  . ARG C 1 93  ? 41.313 -11.415 -13.843 1.00 14.08 ? 93  ARG C CB  1 
ATOM   2437 C  CG  . ARG C 1 93  ? 42.361 -12.455 -13.559 1.00 14.97 ? 93  ARG C CG  1 
ATOM   2438 C  CD  . ARG C 1 93  ? 43.488 -11.972 -12.609 1.00 15.33 ? 93  ARG C CD  1 
ATOM   2439 N  NE  . ARG C 1 93  ? 42.963 -11.495 -11.334 1.00 14.87 ? 93  ARG C NE  1 
ATOM   2440 C  CZ  . ARG C 1 93  ? 42.475 -12.285 -10.375 1.00 15.12 ? 93  ARG C CZ  1 
ATOM   2441 N  NH1 . ARG C 1 93  ? 42.474 -13.607 -10.528 1.00 15.31 ? 93  ARG C NH1 1 
ATOM   2442 N  NH2 . ARG C 1 93  ? 41.928 -11.738 -9.292  1.00 15.63 ? 93  ARG C NH2 1 
ATOM   2443 N  N   . VAL C 1 94  ? 38.283 -11.132 -15.987 1.00 12.56 ? 94  VAL C N   1 
ATOM   2444 C  CA  . VAL C 1 94  ? 37.112 -10.311 -16.258 1.00 12.55 ? 94  VAL C CA  1 
ATOM   2445 C  C   . VAL C 1 94  ? 35.951 -11.233 -16.600 1.00 11.73 ? 94  VAL C C   1 
ATOM   2446 O  O   . VAL C 1 94  ? 36.087 -12.118 -17.459 1.00 12.87 ? 94  VAL C O   1 
ATOM   2447 C  CB  . VAL C 1 94  ? 37.353 -9.374  -17.451 1.00 12.99 ? 94  VAL C CB  1 
ATOM   2448 C  CG1 . VAL C 1 94  ? 36.083 -8.582  -17.817 1.00 13.74 ? 94  VAL C CG1 1 
ATOM   2449 C  CG2 . VAL C 1 94  ? 38.510 -8.444  -17.162 1.00 13.16 ? 94  VAL C CG2 1 
ATOM   2450 N  N   . TYR C 1 95  ? 34.801 -11.027 -15.945 1.00 11.68 ? 95  TYR C N   1 
ATOM   2451 C  CA  . TYR C 1 95  ? 33.543 -11.579 -16.436 1.00 11.84 ? 95  TYR C CA  1 
ATOM   2452 C  C   . TYR C 1 95  ? 32.657 -10.430 -16.877 1.00 11.66 ? 95  TYR C C   1 
ATOM   2453 O  O   . TYR C 1 95  ? 32.606 -9.388  -16.212 1.00 12.34 ? 95  TYR C O   1 
ATOM   2454 C  CB  . TYR C 1 95  ? 32.808 -12.351 -15.361 1.00 12.15 ? 95  TYR C CB  1 
ATOM   2455 C  CG  . TYR C 1 95  ? 33.333 -13.753 -15.058 1.00 12.29 ? 95  TYR C CG  1 
ATOM   2456 C  CD1 . TYR C 1 95  ? 33.899 -14.574 -16.044 1.00 12.88 ? 95  TYR C CD1 1 
ATOM   2457 C  CD2 . TYR C 1 95  ? 33.255 -14.238 -13.750 1.00 12.64 ? 95  TYR C CD2 1 
ATOM   2458 C  CE1 . TYR C 1 95  ? 34.301 -15.872 -15.730 1.00 13.31 ? 95  TYR C CE1 1 
ATOM   2459 C  CE2 . TYR C 1 95  ? 33.679 -15.528 -13.415 1.00 12.95 ? 95  TYR C CE2 1 
ATOM   2460 C  CZ  . TYR C 1 95  ? 34.212 -16.324 -14.439 1.00 12.70 ? 95  TYR C CZ  1 
ATOM   2461 O  OH  . TYR C 1 95  ? 34.627 -17.615 -14.194 1.00 13.84 ? 95  TYR C OH  1 
ATOM   2462 N  N   . ILE C 1 96  ? 31.921 -10.632 -17.967 1.00 11.45 ? 96  ILE C N   1 
ATOM   2463 C  CA  . ILE C 1 96  ? 30.906 -9.671  -18.432 1.00 12.20 ? 96  ILE C CA  1 
ATOM   2464 C  C   . ILE C 1 96  ? 29.618 -10.449 -18.668 1.00 12.18 ? 96  ILE C C   1 
ATOM   2465 O  O   . ILE C 1 96  ? 29.583 -11.344 -19.513 1.00 12.92 ? 96  ILE C O   1 
ATOM   2466 C  CB  . ILE C 1 96  ? 31.312 -8.983  -19.741 1.00 13.45 ? 96  ILE C CB  1 
ATOM   2467 C  CG1 . ILE C 1 96  ? 32.720 -8.367  -19.644 1.00 15.11 ? 96  ILE C CG1 1 
ATOM   2468 C  CG2 . ILE C 1 96  ? 30.239 -7.972  -20.126 1.00 13.37 ? 96  ILE C CG2 1 
ATOM   2469 C  CD1 . ILE C 1 96  ? 33.330 -8.088  -20.978 1.00 16.61 ? 96  ILE C CD1 1 
ATOM   2470 N  N   . ASN C 1 97  ? 28.563 -10.136 -17.925 1.00 11.70 ? 97  ASN C N   1 
ATOM   2471 C  CA  . ASN C 1 97  ? 27.257 -10.722 -18.188 1.00 12.05 ? 97  ASN C CA  1 
ATOM   2472 C  C   . ASN C 1 97  ? 26.469 -9.818  -19.128 1.00 11.90 ? 97  ASN C C   1 
ATOM   2473 O  O   . ASN C 1 97  ? 26.415 -8.597  -18.944 1.00 12.19 ? 97  ASN C O   1 
ATOM   2474 C  CB  . ASN C 1 97  ? 26.508 -10.888 -16.872 1.00 13.06 ? 97  ASN C CB  1 
ATOM   2475 C  CG  . ASN C 1 97  ? 27.050 -12.035 -16.063 1.00 14.95 ? 97  ASN C CG  1 
ATOM   2476 O  OD1 . ASN C 1 97  ? 27.563 -13.008 -16.622 1.00 16.34 ? 97  ASN C OD1 1 
ATOM   2477 N  ND2 . ASN C 1 97  ? 26.958 -11.932 -14.753 1.00 16.33 ? 97  ASN C ND2 1 
ATOM   2478 N  N   . TYR C 1 98  ? 25.868 -10.439 -20.136 1.00 12.08 ? 98  TYR C N   1 
ATOM   2479 C  CA  . TYR C 1 98  ? 25.101 -9.764  -21.168 1.00 11.71 ? 98  TYR C CA  1 
ATOM   2480 C  C   . TYR C 1 98  ? 23.625 -10.036 -20.973 1.00 11.91 ? 98  TYR C C   1 
ATOM   2481 O  O   . TYR C 1 98  ? 23.233 -11.174 -20.676 1.00 12.52 ? 98  TYR C O   1 
ATOM   2482 C  CB  . TYR C 1 98  ? 25.532 -10.265 -22.563 1.00 11.94 ? 98  TYR C CB  1 
ATOM   2483 C  CG  . TYR C 1 98  ? 26.950 -9.902  -22.867 1.00 11.82 ? 98  TYR C CG  1 
ATOM   2484 C  CD1 . TYR C 1 98  ? 27.256 -8.608  -23.285 1.00 12.59 ? 98  TYR C CD1 1 
ATOM   2485 C  CD2 . TYR C 1 98  ? 27.999 -10.809 -22.685 1.00 12.51 ? 98  TYR C CD2 1 
ATOM   2486 C  CE1 . TYR C 1 98  ? 28.573 -8.230  -23.508 1.00 12.99 ? 98  TYR C CE1 1 
ATOM   2487 C  CE2 . TYR C 1 98  ? 29.325 -10.431 -22.926 1.00 12.50 ? 98  TYR C CE2 1 
ATOM   2488 C  CZ  . TYR C 1 98  ? 29.593 -9.128  -23.322 1.00 12.56 ? 98  TYR C CZ  1 
ATOM   2489 O  OH  . TYR C 1 98  ? 30.877 -8.720  -23.539 1.00 12.91 ? 98  TYR C OH  1 
ATOM   2490 N  N   . TYR C 1 99  ? 22.815 -8.988  -21.148 1.00 12.38 ? 99  TYR C N   1 
ATOM   2491 C  CA  . TYR C 1 99  ? 21.373 -9.063  -20.942 1.00 12.95 ? 99  TYR C CA  1 
ATOM   2492 C  C   . TYR C 1 99  ? 20.666 -8.392  -22.099 1.00 12.81 ? 99  TYR C C   1 
ATOM   2493 O  O   . TYR C 1 99  ? 20.857 -7.192  -22.332 1.00 13.55 ? 99  TYR C O   1 
ATOM   2494 C  CB  . TYR C 1 99  ? 20.966 -8.357  -19.652 1.00 13.26 ? 99  TYR C CB  1 
ATOM   2495 C  CG  . TYR C 1 99  ? 21.632 -8.955  -18.440 1.00 14.54 ? 99  TYR C CG  1 
ATOM   2496 C  CD1 . TYR C 1 99  ? 22.883 -8.503  -18.008 1.00 14.12 ? 99  TYR C CD1 1 
ATOM   2497 C  CD2 . TYR C 1 99  ? 21.035 -10.014 -17.768 1.00 16.52 ? 99  TYR C CD2 1 
ATOM   2498 C  CE1 . TYR C 1 99  ? 23.502 -9.063  -16.919 1.00 15.13 ? 99  TYR C CE1 1 
ATOM   2499 C  CE2 . TYR C 1 99  ? 21.653 -10.589 -16.672 1.00 17.17 ? 99  TYR C CE2 1 
ATOM   2500 C  CZ  . TYR C 1 99  ? 22.889 -10.123 -16.259 1.00 16.74 ? 99  TYR C CZ  1 
ATOM   2501 O  OH  . TYR C 1 99  ? 23.507 -10.704 -15.172 1.00 18.40 ? 99  TYR C OH  1 
ATOM   2502 N  N   . ASP C 1 100 ? 19.835 -9.154  -22.799 1.00 12.88 ? 100 ASP C N   1 
ATOM   2503 C  CA  . ASP C 1 100 ? 18.968 -8.643  -23.861 1.00 14.61 ? 100 ASP C CA  1 
ATOM   2504 C  C   . ASP C 1 100 ? 17.635 -8.299  -23.217 1.00 14.49 ? 100 ASP C C   1 
ATOM   2505 O  O   . ASP C 1 100 ? 16.882 -9.203  -22.810 1.00 15.49 ? 100 ASP C O   1 
ATOM   2506 C  CB  . ASP C 1 100 ? 18.808 -9.703  -24.948 1.00 15.71 ? 100 ASP C CB  1 
ATOM   2507 C  CG  . ASP C 1 100 ? 18.053 -9.214  -26.155 1.00 17.80 ? 100 ASP C CG  1 
ATOM   2508 O  OD1 . ASP C 1 100 ? 17.627 -8.051  -26.182 1.00 16.97 ? 100 ASP C OD1 1 
ATOM   2509 O  OD2 . ASP C 1 100 ? 17.884 -10.037 -27.068 1.00 20.74 ? 100 ASP C OD2 1 
ATOM   2510 N  N   . MET C 1 101 ? 17.390 -7.004  -23.027 1.00 13.73 ? 101 MET C N   1 
ATOM   2511 C  CA  . MET C 1 101 ? 16.187 -6.549  -22.352 1.00 14.38 ? 101 MET C CA  1 
ATOM   2512 C  C   . MET C 1 101 ? 15.039 -6.324  -23.322 1.00 14.40 ? 101 MET C C   1 
ATOM   2513 O  O   . MET C 1 101 ? 15.221 -5.758  -24.399 1.00 15.62 ? 101 MET C O   1 
ATOM   2514 C  CB  . MET C 1 101 ? 16.451 -5.231  -21.642 1.00 14.52 ? 101 MET C CB  1 
ATOM   2515 C  CG  . MET C 1 101 ? 17.542 -5.282  -20.614 1.00 15.74 ? 101 MET C CG  1 
ATOM   2516 S  SD  . MET C 1 101 ? 17.225 -6.381  -19.230 1.00 17.76 ? 101 MET C SD  1 
ATOM   2517 C  CE  . MET C 1 101 ? 15.816 -5.574  -18.479 1.00 17.83 ? 101 MET C CE  1 
ATOM   2518 N  N   . ASN C 1 102 ? 13.851 -6.752  -22.918 1.00 15.05 ? 102 ASN C N   1 
ATOM   2519 C  CA  . ASN C 1 102 ? 12.637 -6.373  -23.616 1.00 15.69 ? 102 ASN C CA  1 
ATOM   2520 C  C   . ASN C 1 102 ? 12.388 -4.896  -23.364 1.00 15.70 ? 102 ASN C C   1 
ATOM   2521 O  O   . ASN C 1 102 ? 12.539 -4.393  -22.255 1.00 15.29 ? 102 ASN C O   1 
ATOM   2522 C  CB  . ASN C 1 102 ? 11.444 -7.144  -23.038 1.00 18.28 ? 102 ASN C CB  1 
ATOM   2523 C  CG  . ASN C 1 102 ? 11.467 -8.617  -23.347 1.00 22.64 ? 102 ASN C CG  1 
ATOM   2524 O  OD1 . ASN C 1 102 ? 12.277 -9.102  -24.136 1.00 24.91 ? 102 ASN C OD1 1 
ATOM   2525 N  ND2 . ASN C 1 102 ? 10.534 -9.353  -22.723 1.00 24.59 ? 102 ASN C ND2 1 
ATOM   2526 N  N   . ALA C 1 103 ? 11.962 -4.200  -24.403 1.00 16.40 ? 103 ALA C N   1 
ATOM   2527 C  CA  . ALA C 1 103 ? 11.691 -2.767  -24.296 1.00 17.20 ? 103 ALA C CA  1 
ATOM   2528 C  C   . ALA C 1 103 ? 10.679 -2.454  -23.193 1.00 17.06 ? 103 ALA C C   1 
ATOM   2529 O  O   . ALA C 1 103 ? 10.767 -1.392  -22.548 1.00 17.20 ? 103 ALA C O   1 
ATOM   2530 C  CB  . ALA C 1 103 ? 11.187 -2.229  -25.643 1.00 17.83 ? 103 ALA C CB  1 
ATOM   2531 N  N   . ALA C 1 104 ? 9.701  -3.346  -22.971 1.00 16.60 ? 104 ALA C N   1 
ATOM   2532 C  CA  . ALA C 1 104 ? 8.711  -3.126  -21.918 1.00 16.51 ? 104 ALA C CA  1 
ATOM   2533 C  C   . ALA C 1 104 ? 9.306  -3.154  -20.521 1.00 16.04 ? 104 ALA C C   1 
ATOM   2534 O  O   . ALA C 1 104 ? 8.647  -2.709  -19.572 1.00 16.25 ? 104 ALA C O   1 
ATOM   2535 C  CB  . ALA C 1 104 ? 7.612  -4.182  -22.009 1.00 17.98 ? 104 ALA C CB  1 
ATOM   2536 N  N   . ASN C 1 105 ? 10.518 -3.687  -20.383 1.00 15.20 ? 105 ASN C N   1 
ATOM   2537 C  CA  . ASN C 1 105 ? 11.176 -3.842  -19.093 1.00 14.73 ? 105 ASN C CA  1 
ATOM   2538 C  C   . ASN C 1 105 ? 12.277 -2.829  -18.875 1.00 14.53 ? 105 ASN C C   1 
ATOM   2539 O  O   . ASN C 1 105 ? 13.093 -2.996  -17.965 1.00 14.49 ? 105 ASN C O   1 
ATOM   2540 C  CB  . ASN C 1 105 ? 11.683 -5.276  -18.938 1.00 15.28 ? 105 ASN C CB  1 
ATOM   2541 C  CG  . ASN C 1 105 ? 10.553 -6.260  -18.790 1.00 16.29 ? 105 ASN C CG  1 
ATOM   2542 O  OD1 . ASN C 1 105 ? 9.500  -5.897  -18.290 1.00 17.62 ? 105 ASN C OD1 1 
ATOM   2543 N  ND2 . ASN C 1 105 ? 10.762 -7.503  -19.183 1.00 15.96 ? 105 ASN C ND2 1 
ATOM   2544 N  N   . VAL C 1 106 ? 12.319 -1.776  -19.677 1.00 14.64 ? 106 VAL C N   1 
ATOM   2545 C  CA  . VAL C 1 106 ? 13.292 -0.699  -19.500 1.00 15.03 ? 106 VAL C CA  1 
ATOM   2546 C  C   . VAL C 1 106 ? 12.537 0.615   -19.372 1.00 15.15 ? 106 VAL C C   1 
ATOM   2547 O  O   . VAL C 1 106 ? 11.933 1.108   -20.346 1.00 16.42 ? 106 VAL C O   1 
ATOM   2548 C  CB  . VAL C 1 106 ? 14.321 -0.629  -20.631 1.00 15.38 ? 106 VAL C CB  1 
ATOM   2549 C  CG1 . VAL C 1 106 ? 15.333 0.495   -20.339 1.00 16.86 ? 106 VAL C CG1 1 
ATOM   2550 C  CG2 . VAL C 1 106 ? 15.016 -1.986  -20.800 1.00 15.87 ? 106 VAL C CG2 1 
ATOM   2551 N  N   . GLY C 1 107 ? 12.557 1.174   -18.165 1.00 14.89 ? 107 GLY C N   1 
ATOM   2552 C  CA  . GLY C 1 107 ? 11.964 2.465   -17.913 1.00 15.89 ? 107 GLY C CA  1 
ATOM   2553 C  C   . GLY C 1 107 ? 12.940 3.599   -18.181 1.00 15.95 ? 107 GLY C C   1 
ATOM   2554 O  O   . GLY C 1 107 ? 14.146 3.496   -17.936 1.00 15.79 ? 107 GLY C O   1 
ATOM   2555 N  N   . TRP C 1 108 ? 12.404 4.720   -18.648 1.00 16.44 ? 108 TRP C N   1 
ATOM   2556 C  CA  . TRP C 1 108 ? 13.199 5.901   -18.974 1.00 17.49 ? 108 TRP C CA  1 
ATOM   2557 C  C   . TRP C 1 108 ? 12.207 7.029   -19.194 1.00 17.97 ? 108 TRP C C   1 
ATOM   2558 O  O   . TRP C 1 108 ? 11.168 6.830   -19.821 1.00 18.55 ? 108 TRP C O   1 
ATOM   2559 C  CB  . TRP C 1 108 ? 13.983 5.682   -20.272 1.00 18.27 ? 108 TRP C CB  1 
ATOM   2560 C  CG  . TRP C 1 108 ? 14.709 6.923   -20.753 1.00 19.35 ? 108 TRP C CG  1 
ATOM   2561 C  CD1 . TRP C 1 108 ? 15.783 7.533   -20.152 1.00 19.71 ? 108 TRP C CD1 1 
ATOM   2562 C  CD2 . TRP C 1 108 ? 14.421 7.685   -21.928 1.00 21.77 ? 108 TRP C CD2 1 
ATOM   2563 N  NE1 . TRP C 1 108 ? 16.165 8.638   -20.886 1.00 20.65 ? 108 TRP C NE1 1 
ATOM   2564 C  CE2 . TRP C 1 108 ? 15.352 8.742   -21.979 1.00 21.80 ? 108 TRP C CE2 1 
ATOM   2565 C  CE3 . TRP C 1 108 ? 13.464 7.581   -22.942 1.00 24.17 ? 108 TRP C CE3 1 
ATOM   2566 C  CZ2 . TRP C 1 108 ? 15.352 9.692   -22.993 1.00 23.76 ? 108 TRP C CZ2 1 
ATOM   2567 C  CZ3 . TRP C 1 108 ? 13.474 8.529   -23.953 1.00 25.33 ? 108 TRP C CZ3 1 
ATOM   2568 C  CH2 . TRP C 1 108 ? 14.420 9.559   -23.972 1.00 25.16 ? 108 TRP C CH2 1 
ATOM   2569 N  N   . ASN C 1 109 ? 12.509 8.213   -18.670 1.00 18.66 ? 109 ASN C N   1 
ATOM   2570 C  CA  . ASN C 1 109 ? 11.730 9.413   -18.983 1.00 19.56 ? 109 ASN C CA  1 
ATOM   2571 C  C   . ASN C 1 109 ? 10.231 9.225   -18.711 1.00 20.22 ? 109 ASN C C   1 
ATOM   2572 O  O   . ASN C 1 109 ? 9.380  9.517   -19.556 1.00 21.48 ? 109 ASN C O   1 
ATOM   2573 C  CB  . ASN C 1 109 ? 11.964 9.814   -20.434 1.00 21.59 ? 109 ASN C CB  1 
ATOM   2574 C  CG  . ASN C 1 109 ? 11.500 11.226  -20.730 1.00 24.32 ? 109 ASN C CG  1 
ATOM   2575 O  OD1 . ASN C 1 109 ? 11.470 12.056  -19.839 1.00 25.02 ? 109 ASN C OD1 1 
ATOM   2576 N  ND2 . ASN C 1 109 ? 11.074 11.475  -21.963 1.00 25.98 ? 109 ASN C ND2 1 
ATOM   2577 N  N   . ASN C 1 110 ? 9.912  8.688   -17.525 1.00 19.69 ? 110 ASN C N   1 
ATOM   2578 C  CA  . ASN C 1 110 ? 8.540  8.543   -17.040 1.00 21.24 ? 110 ASN C CA  1 
ATOM   2579 C  C   . ASN C 1 110 ? 7.738  7.466   -17.748 1.00 21.17 ? 110 ASN C C   1 
ATOM   2580 O  O   . ASN C 1 110 ? 6.535  7.343   -17.484 1.00 22.90 ? 110 ASN C O   1 
ATOM   2581 C  CB  . ASN C 1 110 ? 7.783  9.872   -17.056 1.00 23.07 ? 110 ASN C CB  1 
ATOM   2582 C  CG  . ASN C 1 110 ? 8.266  10.802  -15.992 1.00 25.01 ? 110 ASN C CG  1 
ATOM   2583 O  OD1 . ASN C 1 110 ? 8.320  10.421  -14.829 1.00 27.28 ? 110 ASN C OD1 1 
ATOM   2584 N  ND2 . ASN C 1 110 ? 8.585  12.041  -16.362 1.00 25.71 ? 110 ASN C ND2 1 
ATOM   2585 N  N   . SER C 1 111 ? 8.362  6.642   -18.582 1.00 20.26 ? 111 SER C N   1 
ATOM   2586 C  CA  . SER C 1 111 ? 7.627  5.623   -19.307 1.00 20.93 ? 111 SER C CA  1 
ATOM   2587 C  C   . SER C 1 111 ? 8.573  4.455   -19.526 1.00 18.95 ? 111 SER C C   1 
ATOM   2588 O  O   . SER C 1 111 ? 9.576  4.318   -18.820 1.00 18.30 ? 111 SER C O   1 
ATOM   2589 C  CB  . SER C 1 111 ? 7.097  6.214   -20.623 1.00 23.30 ? 111 SER C CB  1 
ATOM   2590 O  OG  . SER C 1 111 ? 6.236  5.305   -21.285 1.00 24.75 ? 111 SER C OG  1 
ATOM   2591 N  N   . THR C 1 112 ? 8.282  3.633   -20.526 1.00 18.31 ? 112 THR C N   1 
ATOM   2592 C  CA  . THR C 1 112 ? 9.210  2.598   -20.949 1.00 18.41 ? 112 THR C CA  1 
ATOM   2593 C  C   . THR C 1 112 ? 9.413  2.686   -22.455 1.00 19.37 ? 112 THR C C   1 
ATOM   2594 O  O   . THR C 1 112 ? 8.719  3.427   -23.157 1.00 21.18 ? 112 THR C O   1 
ATOM   2595 C  CB  . THR C 1 112 ? 8.729  1.185   -20.602 1.00 18.45 ? 112 THR C CB  1 
ATOM   2596 O  OG1 . THR C 1 112 ? 7.578  0.901   -21.411 1.00 19.13 ? 112 THR C OG1 1 
ATOM   2597 C  CG2 . THR C 1 112 ? 8.387  1.016   -19.102 1.00 18.40 ? 112 THR C CG2 1 
ATOM   2598 N  N   . PHE C 1 113 ? 10.349 1.882   -22.958 1.00 19.49 ? 113 PHE C N   1 
ATOM   2599 C  CA  . PHE C 1 113 ? 10.662 1.897   -24.383 1.00 21.15 ? 113 PHE C CA  1 
ATOM   2600 C  C   . PHE C 1 113 ? 9.663  1.126   -25.236 1.00 22.87 ? 113 PHE C C   1 
ATOM   2601 O  O   . PHE C 1 113 ? 9.736  1.217   -26.467 1.00 24.16 ? 113 PHE C O   1 
ATOM   2602 C  CB  . PHE C 1 113 ? 12.083 1.364   -24.633 1.00 21.63 ? 113 PHE C CB  1 
ATOM   2603 C  CG  . PHE C 1 113 ? 13.163 2.350   -24.316 1.00 21.70 ? 113 PHE C CG  1 
ATOM   2604 C  CD1 . PHE C 1 113 ? 13.563 3.284   -25.262 1.00 23.85 ? 113 PHE C CD1 1 
ATOM   2605 C  CD2 . PHE C 1 113 ? 13.768 2.358   -23.085 1.00 20.41 ? 113 PHE C CD2 1 
ATOM   2606 C  CE1 . PHE C 1 113 ? 14.554 4.205   -24.955 1.00 24.55 ? 113 PHE C CE1 1 
ATOM   2607 C  CE2 . PHE C 1 113 ? 14.748 3.260   -22.798 1.00 21.12 ? 113 PHE C CE2 1 
ATOM   2608 C  CZ  . PHE C 1 113 ? 15.130 4.193   -23.718 1.00 23.13 ? 113 PHE C CZ  1 
ATOM   2609 N  N   . ALA C 1 114 ? 8.740  0.387   -24.638 1.00 23.93 ? 114 ALA C N   1 
ATOM   2610 C  CA  . ALA C 1 114 ? 7.783  -0.381  -25.430 1.00 25.47 ? 114 ALA C CA  1 
ATOM   2611 C  C   . ALA C 1 114 ? 6.880  0.518   -26.268 1.00 27.89 ? 114 ALA C C   1 
ATOM   2612 O  O   . ALA C 1 114 ? 6.499  1.614   -25.837 1.00 28.28 ? 114 ALA C O   1 
ATOM   2613 C  CB  . ALA C 1 114 ? 6.940  -1.260  -24.547 1.00 25.23 ? 114 ALA C CB  1 
ATOM   2614 O  OXT . ALA C 1 114 ? 6.516  0.170   -27.401 1.00 30.08 ? 114 ALA C OXT 1 
HETATM 2615 C  C1  . HFC D 2 .   ? 39.501 -20.353 -16.501 1.00 37.46 ? 201 HFC A C1  1 
HETATM 2616 C  C2  . HFC D 2 .   ? 39.746 -19.749 -15.303 1.00 37.44 ? 201 HFC A C2  1 
HETATM 2617 C  C3  . HFC D 2 .   ? 40.959 -20.010 -14.614 1.00 37.69 ? 201 HFC A C3  1 
HETATM 2618 C  C4  . HFC D 2 .   ? 41.874 -20.895 -15.174 1.00 37.70 ? 201 HFC A C4  1 
HETATM 2619 C  C5  . HFC D 2 .   ? 41.619 -21.512 -16.399 1.00 37.90 ? 201 HFC A C5  1 
HETATM 2620 C  C6  . HFC D 2 .   ? 40.440 -21.261 -17.075 1.00 37.70 ? 201 HFC A C6  1 
HETATM 2621 O  O7  . HFC D 2 .   ? 38.348 -20.102 -17.148 1.00 37.09 ? 201 HFC A O7  1 
HETATM 2622 C  C8  . HFC D 2 .   ? 37.413 -19.279 -16.725 1.00 37.33 ? 201 HFC A C8  1 
HETATM 2623 C  C9  . HFC D 2 .   ? 37.561 -18.606 -15.509 1.00 37.43 ? 201 HFC A C9  1 
HETATM 2624 C  C10 . HFC D 2 .   ? 38.759 -18.824 -14.757 1.00 37.33 ? 201 HFC A C10 1 
HETATM 2625 O  O11 . HFC D 2 .   ? 36.444 -19.137 -17.387 1.00 36.78 ? 201 HFC A O11 1 
HETATM 2626 O  O12 . HFC D 2 .   ? 42.579 -22.392 -16.930 1.00 38.03 ? 201 HFC A O12 1 
HETATM 2627 O  O13 . HFC D 2 .   ? 43.079 -21.185 -14.509 1.00 36.90 ? 201 HFC A O13 1 
HETATM 2628 CL CL  . CL  E 3 .   ? 29.544 -19.729 -14.622 1.00 26.53 ? 202 CL  A CL  1 
HETATM 2629 CL CL  . CL  F 3 .   ? 17.564 -28.192 -9.242  1.00 29.00 ? 203 CL  A CL  1 
HETATM 2630 CL CL  . CL  G 3 .   ? 21.208 -15.620 -20.112 1.00 19.86 ? 204 CL  A CL  1 
HETATM 2631 CL CL  . CL  H 3 .   ? 9.148  -10.260 -4.655  1.00 37.51 ? 201 CL  B CL  1 
HETATM 2632 CL CL  . CL  I 3 .   ? 13.788 -15.662 -12.878 1.00 19.94 ? 202 CL  B CL  1 
HETATM 2633 CL CL  . CL  J 3 .   ? 19.133 -0.038  -24.722 1.00 26.25 ? 201 CL  C CL  1 
HETATM 2634 CL CL  . CL  K 3 .   ? 24.829 -11.976 -32.574 1.00 28.00 ? 202 CL  C CL  1 
HETATM 2635 CL CL  . CL  L 3 .   ? 13.653 -8.441  -20.284 1.00 20.33 ? 203 CL  C CL  1 
HETATM 2636 O  O   . HOH M 4 .   ? 34.722 -31.409 -0.065  1.00 29.48 ? 301 HOH A O   1 
HETATM 2637 O  O   . HOH M 4 .   ? 32.483 1.445   7.933   1.00 43.73 ? 302 HOH A O   1 
HETATM 2638 O  O   . HOH M 4 .   ? 18.283 -17.090 -16.979 1.00 32.88 ? 303 HOH A O   1 
HETATM 2639 O  O   . HOH M 4 .   ? 35.400 -18.522 -26.113 1.00 27.36 ? 304 HOH A O   1 
HETATM 2640 O  O   . HOH M 4 .   ? 23.975 -7.496  -4.442  1.00 30.76 ? 305 HOH A O   1 
HETATM 2641 O  O   . HOH M 4 .   ? 20.228 -20.340 -19.167 1.00 30.99 ? 306 HOH A O   1 
HETATM 2642 O  O   . HOH M 4 .   ? 32.493 -3.104  13.120  1.00 40.07 ? 307 HOH A O   1 
HETATM 2643 O  O   . HOH M 4 .   ? 22.238 -2.028  11.109  1.00 32.75 ? 308 HOH A O   1 
HETATM 2644 O  O   . HOH M 4 .   ? 26.226 -12.483 -8.917  1.00 18.24 ? 309 HOH A O   1 
HETATM 2645 O  O   . HOH M 4 .   ? 33.294 -3.804  -2.210  1.00 18.70 ? 310 HOH A O   1 
HETATM 2646 O  O   . HOH M 4 .   ? 34.930 -15.803 6.725   1.00 34.86 ? 311 HOH A O   1 
HETATM 2647 O  O   . HOH M 4 .   ? 10.747 -14.041 9.660   1.00 37.52 ? 312 HOH A O   1 
HETATM 2648 O  O   . HOH M 4 .   ? 36.587 -15.775 8.410   1.00 33.48 ? 313 HOH A O   1 
HETATM 2649 O  O   . HOH M 4 .   ? 10.400 -10.516 -1.941  1.00 43.55 ? 314 HOH A O   1 
HETATM 2650 O  O   . HOH M 4 .   ? 24.364 -27.506 -7.398  1.00 30.64 ? 315 HOH A O   1 
HETATM 2651 O  O   . HOH M 4 .   ? 29.807 -22.913 -29.633 1.00 37.76 ? 316 HOH A O   1 
HETATM 2652 O  O   . HOH M 4 .   ? 21.763 -29.687 -0.220  1.00 42.59 ? 317 HOH A O   1 
HETATM 2653 O  O   . HOH M 4 .   ? 43.306 -13.523 9.817   1.00 17.45 ? 318 HOH A O   1 
HETATM 2654 O  O   . HOH M 4 .   ? 19.963 -24.026 -18.247 1.00 30.43 ? 319 HOH A O   1 
HETATM 2655 O  O   . HOH M 4 .   ? 28.593 -15.409 -27.301 1.00 17.32 ? 320 HOH A O   1 
HETATM 2656 O  O   . HOH M 4 .   ? 24.549 -26.068 -2.004  1.00 26.36 ? 321 HOH A O   1 
HETATM 2657 O  O   . HOH M 4 .   ? 26.510 -22.266 5.612   1.00 24.33 ? 322 HOH A O   1 
HETATM 2658 O  O   . HOH M 4 .   ? 17.227 -22.589 -14.877 1.00 43.73 ? 323 HOH A O   1 
HETATM 2659 O  O   . HOH M 4 .   ? 22.718 -14.284 -26.599 1.00 28.57 ? 324 HOH A O   1 
HETATM 2660 O  O   . HOH M 4 .   ? 16.868 -15.427 -13.038 1.00 15.07 ? 325 HOH A O   1 
HETATM 2661 O  O   . HOH M 4 .   ? 22.645 -30.185 -11.848 1.00 42.09 ? 326 HOH A O   1 
HETATM 2662 O  O   . HOH M 4 .   ? 23.852 -8.477  -6.886  1.00 24.90 ? 327 HOH A O   1 
HETATM 2663 O  O   . HOH M 4 .   ? 44.492 -14.633 -21.424 1.00 27.06 ? 328 HOH A O   1 
HETATM 2664 O  O   . HOH M 4 .   ? 39.466 -15.962 -26.063 1.00 23.65 ? 329 HOH A O   1 
HETATM 2665 O  O   . HOH M 4 .   ? 31.478 -0.368  0.346   1.00 24.07 ? 330 HOH A O   1 
HETATM 2666 O  O   . HOH M 4 .   ? 31.880 -18.099 -27.832 1.00 20.40 ? 331 HOH A O   1 
HETATM 2667 O  O   . HOH M 4 .   ? 20.114 -8.924  -5.161  1.00 26.32 ? 332 HOH A O   1 
HETATM 2668 O  O   . HOH M 4 .   ? 19.923 -9.185  10.710  1.00 16.39 ? 333 HOH A O   1 
HETATM 2669 O  O   . HOH M 4 .   ? 32.615 -23.649 -24.380 1.00 18.17 ? 334 HOH A O   1 
HETATM 2670 O  O   . HOH M 4 .   ? 28.918 3.427   1.671   1.00 27.20 ? 335 HOH A O   1 
HETATM 2671 O  O   . HOH M 4 .   ? 12.283 -10.145 7.603   1.00 21.08 ? 336 HOH A O   1 
HETATM 2672 O  O   . HOH M 4 .   ? 21.730 -14.937 6.756   1.00 18.11 ? 337 HOH A O   1 
HETATM 2673 O  O   . HOH M 4 .   ? 29.634 -6.745  -9.117  1.00 20.18 ? 338 HOH A O   1 
HETATM 2674 O  O   . HOH M 4 .   ? 40.195 -19.810 3.395   1.00 35.04 ? 339 HOH A O   1 
HETATM 2675 O  O   . HOH M 4 .   ? 35.955 -15.336 -29.760 1.00 20.79 ? 340 HOH A O   1 
HETATM 2676 O  O   . HOH M 4 .   ? 37.064 -15.763 -5.985  1.00 13.69 ? 341 HOH A O   1 
HETATM 2677 O  O   . HOH M 4 .   ? 22.810 -22.219 -18.832 1.00 20.35 ? 342 HOH A O   1 
HETATM 2678 O  O   . HOH M 4 .   ? 20.567 -24.889 -14.619 1.00 21.23 ? 343 HOH A O   1 
HETATM 2679 O  O   . HOH M 4 .   ? 36.137 -12.527 -29.549 1.00 21.88 ? 344 HOH A O   1 
HETATM 2680 O  O   . HOH M 4 .   ? 26.122 -7.468  11.947  1.00 32.91 ? 345 HOH A O   1 
HETATM 2681 O  O   . HOH M 4 .   ? 17.564 -28.400 -1.704  1.00 23.43 ? 346 HOH A O   1 
HETATM 2682 O  O   . HOH M 4 .   ? 30.665 -9.761  11.935  1.00 29.66 ? 347 HOH A O   1 
HETATM 2683 O  O   . HOH M 4 .   ? 33.100 -22.983 -27.872 1.00 42.42 ? 348 HOH A O   1 
HETATM 2684 O  O   . HOH M 4 .   ? 29.195 -28.093 -11.828 1.00 27.90 ? 349 HOH A O   1 
HETATM 2685 O  O   . HOH M 4 .   ? 14.312 -10.093 -6.096  1.00 20.79 ? 350 HOH A O   1 
HETATM 2686 O  O   . HOH M 4 .   ? 41.230 -7.411  -26.699 1.00 22.56 ? 351 HOH A O   1 
HETATM 2687 O  O   . HOH M 4 .   ? 41.044 -17.734 -11.884 1.00 20.67 ? 352 HOH A O   1 
HETATM 2688 O  O   . HOH M 4 .   ? 29.649 -25.820 -0.019  1.00 26.26 ? 353 HOH A O   1 
HETATM 2689 O  O   . HOH M 4 .   ? 7.567  -3.260  7.970   1.00 22.37 ? 354 HOH A O   1 
HETATM 2690 O  O   . HOH M 4 .   ? 25.937 0.944   6.433   1.00 29.84 ? 355 HOH A O   1 
HETATM 2691 O  O   . HOH M 4 .   ? 21.783 -9.515  -12.927 1.00 31.24 ? 356 HOH A O   1 
HETATM 2692 O  O   . HOH M 4 .   ? 37.605 -9.475  4.792   1.00 33.98 ? 357 HOH A O   1 
HETATM 2693 O  O   . HOH M 4 .   ? 39.062 -17.961 5.056   1.00 25.81 ? 358 HOH A O   1 
HETATM 2694 O  O   . HOH M 4 .   ? 42.649 -13.258 -24.401 1.00 22.96 ? 359 HOH A O   1 
HETATM 2695 O  O   . HOH M 4 .   ? 22.952 -26.239 1.707   1.00 24.91 ? 360 HOH A O   1 
HETATM 2696 O  O   . HOH M 4 .   ? 35.661 -27.868 -5.709  1.00 28.47 ? 361 HOH A O   1 
HETATM 2697 O  O   . HOH M 4 .   ? 14.550 -10.105 11.290  1.00 26.31 ? 362 HOH A O   1 
HETATM 2698 O  O   . HOH M 4 .   ? 28.807 -4.133  13.273  1.00 38.41 ? 363 HOH A O   1 
HETATM 2699 O  O   . HOH M 4 .   ? 44.673 -9.238  8.927   1.00 28.24 ? 364 HOH A O   1 
HETATM 2700 O  O   . HOH M 4 .   ? 24.824 -19.850 10.525  1.00 39.24 ? 365 HOH A O   1 
HETATM 2701 O  O   . HOH M 4 .   ? 43.304 -19.503 -12.204 1.00 35.34 ? 366 HOH A O   1 
HETATM 2702 O  O   . HOH M 4 .   ? 22.851 -26.430 -4.824  1.00 31.69 ? 367 HOH A O   1 
HETATM 2703 O  O   . HOH M 4 .   ? 16.906 -13.700 13.491  1.00 41.78 ? 368 HOH A O   1 
HETATM 2704 O  O   . HOH M 4 .   ? 11.074 -25.845 -6.698  1.00 32.64 ? 369 HOH A O   1 
HETATM 2705 O  O   . HOH M 4 .   ? 17.551 -9.167  12.721  1.00 25.00 ? 370 HOH A O   1 
HETATM 2706 O  O   . HOH M 4 .   ? 34.016 -0.291  9.258   1.00 24.24 ? 371 HOH A O   1 
HETATM 2707 O  O   . HOH M 4 .   ? 21.587 -8.808  13.388  1.00 39.35 ? 372 HOH A O   1 
HETATM 2708 O  O   . HOH M 4 .   ? 17.705 -17.424 -14.717 1.00 20.57 ? 373 HOH A O   1 
HETATM 2709 O  O   . HOH M 4 .   ? 21.790 -22.186 7.236   1.00 25.16 ? 374 HOH A O   1 
HETATM 2710 O  O   . HOH M 4 .   ? 45.042 -23.467 -10.929 1.00 34.87 ? 375 HOH A O   1 
HETATM 2711 O  O   . HOH M 4 .   ? 24.442 -22.365 -21.525 1.00 20.43 ? 376 HOH A O   1 
HETATM 2712 O  O   . HOH M 4 .   ? 35.387 -8.612  11.612  1.00 42.05 ? 377 HOH A O   1 
HETATM 2713 O  O   . HOH M 4 .   ? 26.843 -1.001  -4.227  1.00 28.67 ? 378 HOH A O   1 
HETATM 2714 O  O   . HOH M 4 .   ? 44.353 -23.706 -13.539 1.00 23.59 ? 379 HOH A O   1 
HETATM 2715 O  O   . HOH M 4 .   ? 14.561 -29.402 -2.162  1.00 36.60 ? 380 HOH A O   1 
HETATM 2716 O  O   . HOH M 4 .   ? 29.102 2.388   -1.983  1.00 25.16 ? 381 HOH A O   1 
HETATM 2717 O  O   . HOH M 4 .   ? 39.003 -12.928 -29.043 1.00 30.03 ? 382 HOH A O   1 
HETATM 2718 O  O   . HOH M 4 .   ? 29.576 -25.463 -17.336 1.00 38.13 ? 383 HOH A O   1 
HETATM 2719 O  O   . HOH M 4 .   ? 27.590 -21.515 8.071   1.00 34.54 ? 384 HOH A O   1 
HETATM 2720 O  O   . HOH M 4 .   ? 22.068 -17.770 -25.905 1.00 29.44 ? 385 HOH A O   1 
HETATM 2721 O  O   . HOH M 4 .   ? 20.004 -9.106  -8.350  1.00 7.78  ? 386 HOH A O   1 
HETATM 2722 O  O   . HOH M 4 .   ? 38.963 -10.830 11.235  1.00 21.94 ? 387 HOH A O   1 
HETATM 2723 O  O   . HOH M 4 .   ? 14.339 -26.677 -11.510 1.00 30.59 ? 388 HOH A O   1 
HETATM 2724 O  O   . HOH M 4 .   ? 13.093 -8.204  9.489   1.00 17.98 ? 389 HOH A O   1 
HETATM 2725 O  O   . HOH M 4 .   ? 14.375 -28.764 -8.781  1.00 39.85 ? 390 HOH A O   1 
HETATM 2726 O  O   . HOH M 4 .   ? 21.436 1.532   6.048   1.00 24.38 ? 391 HOH A O   1 
HETATM 2727 O  O   . HOH M 4 .   ? 15.872 -15.463 10.390  1.00 25.75 ? 392 HOH A O   1 
HETATM 2728 O  O   . HOH M 4 .   ? 28.689 -27.167 -14.309 1.00 26.68 ? 393 HOH A O   1 
HETATM 2729 O  O   . HOH M 4 .   ? 31.968 -29.973 -6.010  1.00 37.64 ? 394 HOH A O   1 
HETATM 2730 O  O   . HOH M 4 .   ? 19.724 -15.288 -16.561 1.00 24.20 ? 395 HOH A O   1 
HETATM 2731 O  O   . HOH M 4 .   ? 23.393 -27.628 -15.262 1.00 33.05 ? 396 HOH A O   1 
HETATM 2732 O  O   . HOH M 4 .   ? 22.291 0.569   8.392   1.00 19.40 ? 397 HOH A O   1 
HETATM 2733 O  O   . HOH M 4 .   ? 19.441 -13.747 -24.426 1.00 20.85 ? 398 HOH A O   1 
HETATM 2734 O  O   . HOH M 4 .   ? 15.367 1.113   11.265  1.00 22.57 ? 399 HOH A O   1 
HETATM 2735 O  O   . HOH M 4 .   ? 21.593 -27.810 -13.353 1.00 23.26 ? 400 HOH A O   1 
HETATM 2736 O  O   . HOH M 4 .   ? 27.165 -3.867  -6.202  1.00 22.69 ? 401 HOH A O   1 
HETATM 2737 O  O   . HOH M 4 .   ? 37.800 -11.014 2.713   1.00 17.45 ? 402 HOH A O   1 
HETATM 2738 O  O   . HOH M 4 .   ? 43.925 -27.262 -9.356  1.00 12.88 ? 403 HOH A O   1 
HETATM 2739 O  O   . HOH M 4 .   ? 20.774 -28.166 1.624   1.00 29.12 ? 404 HOH A O   1 
HETATM 2740 O  O   . HOH M 4 .   ? 25.045 -5.981  -7.161  1.00 34.17 ? 405 HOH A O   1 
HETATM 2741 O  O   . HOH M 4 .   ? 20.999 -22.661 -21.092 1.00 32.24 ? 406 HOH A O   1 
HETATM 2742 O  O   . HOH M 4 .   ? 40.949 -7.130  2.045   1.00 44.08 ? 407 HOH A O   1 
HETATM 2743 O  O   . HOH M 4 .   ? 33.623 -14.886 12.195  1.00 25.22 ? 408 HOH A O   1 
HETATM 2744 O  O   . HOH M 4 .   ? 18.012 -21.602 -18.713 1.00 44.11 ? 409 HOH A O   1 
HETATM 2745 O  O   . HOH M 4 .   ? 26.410 -26.000 -17.787 1.00 40.25 ? 410 HOH A O   1 
HETATM 2746 O  O   . HOH M 4 .   ? 30.464 -16.389 -14.241 1.00 23.03 ? 411 HOH A O   1 
HETATM 2747 O  O   . HOH M 4 .   ? 43.359 -7.759  -24.189 1.00 20.36 ? 412 HOH A O   1 
HETATM 2748 O  O   . HOH M 4 .   ? 22.216 -9.165  -10.463 1.00 26.09 ? 413 HOH A O   1 
HETATM 2749 O  O   . HOH M 4 .   ? 42.571 -22.854 -6.906  1.00 34.30 ? 414 HOH A O   1 
HETATM 2750 O  O   . HOH M 4 .   ? 24.749 -2.887  10.309  1.00 27.66 ? 415 HOH A O   1 
HETATM 2751 O  O   . HOH M 4 .   ? 24.455 -24.039 6.444   1.00 42.04 ? 416 HOH A O   1 
HETATM 2752 O  O   . HOH M 4 .   ? 44.634 -9.852  -26.251 1.00 38.69 ? 417 HOH A O   1 
HETATM 2753 O  O   . HOH M 4 .   ? 38.459 -17.558 7.957   1.00 29.27 ? 418 HOH A O   1 
HETATM 2754 O  O   . HOH M 4 .   ? 43.950 -21.779 -8.149  1.00 39.12 ? 419 HOH A O   1 
HETATM 2755 O  O   . HOH M 4 .   ? 18.186 -27.357 0.919   1.00 20.18 ? 420 HOH A O   1 
HETATM 2756 O  O   . HOH M 4 .   ? 35.606 -2.639  1.351   1.00 42.66 ? 421 HOH A O   1 
HETATM 2757 O  O   . HOH M 4 .   ? 24.240 -24.867 -18.724 1.00 28.56 ? 422 HOH A O   1 
HETATM 2758 O  O   . HOH M 4 .   ? 32.438 -31.882 1.315   1.00 40.41 ? 423 HOH A O   1 
HETATM 2759 O  O   . HOH M 4 .   ? 20.278 -29.794 -4.795  1.00 30.40 ? 424 HOH A O   1 
HETATM 2760 O  O   . HOH M 4 .   ? 23.587 -3.835  -6.609  1.00 30.11 ? 425 HOH A O   1 
HETATM 2761 O  O   . HOH M 4 .   ? 42.335 -9.610  -28.179 1.00 26.55 ? 426 HOH A O   1 
HETATM 2762 O  O   . HOH M 4 .   ? 19.916 3.889   7.033   1.00 39.65 ? 427 HOH A O   1 
HETATM 2763 O  O   . HOH M 4 .   ? 13.674 -28.025 0.948   1.00 43.46 ? 428 HOH A O   1 
HETATM 2764 O  O   . HOH M 4 .   ? 45.538 -21.088 -18.914 1.00 44.60 ? 429 HOH A O   1 
HETATM 2765 O  O   . HOH M 4 .   ? 24.134 -25.732 4.253   1.00 23.60 ? 430 HOH A O   1 
HETATM 2766 O  O   . HOH M 4 .   ? 26.944 3.909   -0.287  1.00 29.50 ? 431 HOH A O   1 
HETATM 2767 O  O   . HOH M 4 .   ? 36.436 -15.329 10.984  1.00 40.24 ? 432 HOH A O   1 
HETATM 2768 O  O   . HOH M 4 .   ? 21.578 -6.711  -5.211  1.00 30.94 ? 433 HOH A O   1 
HETATM 2769 O  O   . HOH M 4 .   ? 22.282 -29.136 -4.473  1.00 38.78 ? 434 HOH A O   1 
HETATM 2770 O  O   . HOH M 4 .   ? 22.479 -21.881 -23.845 1.00 20.44 ? 435 HOH A O   1 
HETATM 2771 O  O   . HOH M 4 .   ? 35.062 -33.466 -2.008  1.00 30.87 ? 436 HOH A O   1 
HETATM 2772 O  O   . HOH M 4 .   ? 36.358 -20.683 12.287  1.00 38.13 ? 437 HOH A O   1 
HETATM 2773 O  O   . HOH M 4 .   ? 18.181 -15.430 -21.501 1.00 42.19 ? 438 HOH A O   1 
HETATM 2774 O  O   . HOH M 4 .   ? 25.238 -18.794 13.118  1.00 37.47 ? 439 HOH A O   1 
HETATM 2775 O  O   . HOH M 4 .   ? 31.180 2.538   0.428   1.00 33.70 ? 440 HOH A O   1 
HETATM 2776 O  O   . HOH M 4 .   ? 31.826 -27.154 5.591   1.00 44.71 ? 441 HOH A O   1 
HETATM 2777 O  O   . HOH M 4 .   ? 45.335 -12.237 -24.294 1.00 42.29 ? 442 HOH A O   1 
HETATM 2778 O  O   . HOH M 4 .   ? 20.879 -15.463 12.687  1.00 34.39 ? 443 HOH A O   1 
HETATM 2779 O  O   . HOH M 4 .   ? 19.365 -30.645 -2.179  1.00 45.46 ? 444 HOH A O   1 
HETATM 2780 O  O   . HOH M 4 .   ? 19.157 -30.953 -7.733  1.00 42.34 ? 445 HOH A O   1 
HETATM 2781 O  O   . HOH M 4 .   ? 38.498 -13.409 12.172  1.00 42.20 ? 446 HOH A O   1 
HETATM 2782 O  O   . HOH M 4 .   ? 18.019 5.258   6.525   1.00 40.72 ? 447 HOH A O   1 
HETATM 2783 O  O   . HOH M 4 .   ? 32.910 -0.213  12.054  1.00 36.89 ? 448 HOH A O   1 
HETATM 2784 O  O   . HOH M 4 .   ? 26.367 -4.702  11.776  1.00 24.28 ? 449 HOH A O   1 
HETATM 2785 O  O   . HOH M 4 .   ? 20.408 -17.958 12.075  1.00 37.64 ? 450 HOH A O   1 
HETATM 2786 O  O   . HOH M 4 .   ? 38.812 -13.190 -31.777 1.00 43.58 ? 451 HOH A O   1 
HETATM 2787 O  O   . HOH M 4 .   ? 16.444 -13.400 -14.957 1.00 20.60 ? 452 HOH A O   1 
HETATM 2788 O  O   . HOH M 4 .   ? 16.216 -28.949 2.490   1.00 41.76 ? 453 HOH A O   1 
HETATM 2789 O  O   . HOH M 4 .   ? 15.681 -14.959 -17.001 1.00 36.62 ? 454 HOH A O   1 
HETATM 2790 O  O   . HOH N 4 .   ? 12.232 -12.512 -15.806 1.00 20.74 ? 301 HOH B O   1 
HETATM 2791 O  O   . HOH N 4 .   ? 28.570 8.219   -0.325  1.00 43.63 ? 302 HOH B O   1 
HETATM 2792 O  O   . HOH N 4 .   ? 6.435  -11.438 -3.606  1.00 36.72 ? 303 HOH B O   1 
HETATM 2793 O  O   . HOH N 4 .   ? 29.562 13.130  -1.240  1.00 40.72 ? 304 HOH B O   1 
HETATM 2794 O  O   . HOH N 4 .   ? 16.515 -4.422  -7.852  1.00 26.81 ? 305 HOH B O   1 
HETATM 2795 O  O   . HOH N 4 .   ? 12.142 11.267  0.958   1.00 35.36 ? 306 HOH B O   1 
HETATM 2796 O  O   . HOH N 4 .   ? 8.894  -14.753 -13.916 1.00 28.06 ? 307 HOH B O   1 
HETATM 2797 O  O   . HOH N 4 .   ? 31.528 13.221  -19.945 1.00 26.78 ? 308 HOH B O   1 
HETATM 2798 O  O   . HOH N 4 .   ? 18.210 16.520  -2.882  1.00 39.90 ? 309 HOH B O   1 
HETATM 2799 O  O   . HOH N 4 .   ? 20.460 -2.343  -10.015 1.00 23.11 ? 310 HOH B O   1 
HETATM 2800 O  O   . HOH N 4 .   ? -2.238 -6.333  -2.362  1.00 41.61 ? 311 HOH B O   1 
HETATM 2801 O  O   . HOH N 4 .   ? 6.512  -25.317 -4.141  1.00 28.45 ? 312 HOH B O   1 
HETATM 2802 O  O   . HOH N 4 .   ? 14.120 -25.281 1.720   1.00 21.59 ? 313 HOH B O   1 
HETATM 2803 O  O   . HOH N 4 .   ? 15.438 -22.128 -11.442 1.00 27.80 ? 314 HOH B O   1 
HETATM 2804 O  O   . HOH N 4 .   ? 13.914 -22.885 -5.529  1.00 19.89 ? 315 HOH B O   1 
HETATM 2805 O  O   . HOH N 4 .   ? 11.143 -7.766  6.715   1.00 27.03 ? 316 HOH B O   1 
HETATM 2806 O  O   . HOH N 4 .   ? 2.709  2.324   -9.888  1.00 26.64 ? 317 HOH B O   1 
HETATM 2807 O  O   . HOH N 4 .   ? 5.147  -13.871 -14.098 1.00 32.68 ? 318 HOH B O   1 
HETATM 2808 O  O   . HOH N 4 .   ? 7.135  -13.197 6.515   1.00 31.15 ? 319 HOH B O   1 
HETATM 2809 O  O   . HOH N 4 .   ? 19.474 15.265  -14.050 1.00 19.38 ? 320 HOH B O   1 
HETATM 2810 O  O   . HOH N 4 .   ? 26.592 15.954  -11.687 1.00 30.97 ? 321 HOH B O   1 
HETATM 2811 O  O   . HOH N 4 .   ? 11.238 -23.213 -2.231  1.00 22.05 ? 322 HOH B O   1 
HETATM 2812 O  O   . HOH N 4 .   ? 24.739 2.437   -0.522  1.00 18.84 ? 323 HOH B O   1 
HETATM 2813 O  O   . HOH N 4 .   ? 19.971 -0.460  -13.789 1.00 24.55 ? 324 HOH B O   1 
HETATM 2814 O  O   . HOH N 4 .   ? -0.910 -3.853  -7.450  1.00 48.79 ? 325 HOH B O   1 
HETATM 2815 O  O   . HOH N 4 .   ? 23.577 16.692  -19.735 1.00 20.98 ? 326 HOH B O   1 
HETATM 2816 O  O   . HOH N 4 .   ? 6.272  9.921   -7.781  1.00 25.44 ? 327 HOH B O   1 
HETATM 2817 O  O   . HOH N 4 .   ? 6.567  -23.742 -1.048  1.00 23.46 ? 328 HOH B O   1 
HETATM 2818 O  O   . HOH N 4 .   ? 21.285 0.202   -9.894  1.00 24.14 ? 329 HOH B O   1 
HETATM 2819 O  O   . HOH N 4 .   ? 12.768 -1.634  3.055   1.00 15.87 ? 330 HOH B O   1 
HETATM 2820 O  O   . HOH N 4 .   ? 28.217 5.418   -2.102  1.00 27.59 ? 331 HOH B O   1 
HETATM 2821 O  O   . HOH N 4 .   ? 9.928  8.936   4.601   1.00 28.95 ? 332 HOH B O   1 
HETATM 2822 O  O   . HOH N 4 .   ? 18.988 12.188  -21.731 1.00 20.95 ? 333 HOH B O   1 
HETATM 2823 O  O   . HOH N 4 .   ? -0.122 2.008   -19.883 1.00 34.40 ? 334 HOH B O   1 
HETATM 2824 O  O   . HOH N 4 .   ? 13.779 -8.546  -17.235 1.00 16.31 ? 335 HOH B O   1 
HETATM 2825 O  O   . HOH N 4 .   ? 5.661  -6.710  10.710  1.00 24.59 ? 336 HOH B O   1 
HETATM 2826 O  O   . HOH N 4 .   ? 6.166  -15.273 1.907   1.00 14.02 ? 337 HOH B O   1 
HETATM 2827 O  O   . HOH N 4 .   ? 20.077 18.473  -10.174 1.00 34.14 ? 338 HOH B O   1 
HETATM 2828 O  O   . HOH N 4 .   ? 15.502 -17.962 10.159  1.00 42.38 ? 339 HOH B O   1 
HETATM 2829 O  O   . HOH N 4 .   ? 22.134 -4.403  -4.300  1.00 20.69 ? 340 HOH B O   1 
HETATM 2830 O  O   . HOH N 4 .   ? 16.936 -25.052 2.058   1.00 20.54 ? 341 HOH B O   1 
HETATM 2831 O  O   . HOH N 4 .   ? 4.271  -10.312 -13.706 1.00 23.38 ? 342 HOH B O   1 
HETATM 2832 O  O   . HOH N 4 .   ? 1.314  -3.131  -9.948  1.00 30.58 ? 343 HOH B O   1 
HETATM 2833 O  O   . HOH N 4 .   ? 13.954 2.903   6.333   1.00 30.51 ? 344 HOH B O   1 
HETATM 2834 O  O   . HOH N 4 .   ? 0.450  2.381   -16.944 1.00 29.07 ? 345 HOH B O   1 
HETATM 2835 O  O   . HOH N 4 .   ? 18.508 15.945  -19.581 1.00 32.38 ? 346 HOH B O   1 
HETATM 2836 O  O   . HOH N 4 .   ? 19.418 -8.026  -12.524 1.00 36.74 ? 347 HOH B O   1 
HETATM 2837 O  O   . HOH N 4 .   ? 2.499  6.051   -11.589 1.00 26.40 ? 348 HOH B O   1 
HETATM 2838 O  O   . HOH N 4 .   ? 31.833 6.646   -4.524  1.00 30.38 ? 349 HOH B O   1 
HETATM 2839 O  O   . HOH N 4 .   ? 6.986  -14.428 -11.474 1.00 24.25 ? 350 HOH B O   1 
HETATM 2840 O  O   . HOH N 4 .   ? 19.072 -1.522  -19.626 1.00 25.61 ? 351 HOH B O   1 
HETATM 2841 O  O   . HOH N 4 .   ? 13.716 11.314  -12.560 1.00 21.56 ? 352 HOH B O   1 
HETATM 2842 O  O   . HOH N 4 .   ? 15.076 17.335  -20.133 1.00 42.58 ? 353 HOH B O   1 
HETATM 2843 O  O   . HOH N 4 .   ? 29.454 11.402  -7.709  1.00 37.37 ? 354 HOH B O   1 
HETATM 2844 O  O   . HOH N 4 .   ? 27.597 0.564   -6.828  1.00 25.86 ? 355 HOH B O   1 
HETATM 2845 O  O   . HOH N 4 .   ? 6.650  -10.490 -17.170 1.00 41.00 ? 356 HOH B O   1 
HETATM 2846 O  O   . HOH N 4 .   ? 5.519  -20.483 -1.903  1.00 19.87 ? 357 HOH B O   1 
HETATM 2847 O  O   . HOH N 4 .   ? 10.459 -19.235 1.680   1.00 32.35 ? 358 HOH B O   1 
HETATM 2848 O  O   . HOH N 4 .   ? 0.370  -4.726  -18.882 1.00 38.00 ? 359 HOH B O   1 
HETATM 2849 O  O   . HOH N 4 .   ? 8.645  14.919  -9.627  1.00 37.19 ? 360 HOH B O   1 
HETATM 2850 O  O   . HOH N 4 .   ? 11.687 -10.232 -16.458 1.00 19.07 ? 361 HOH B O   1 
HETATM 2851 O  O   . HOH N 4 .   ? 2.829  4.260   -4.811  1.00 27.87 ? 362 HOH B O   1 
HETATM 2852 O  O   . HOH N 4 .   ? 27.631 14.256  0.344   1.00 25.07 ? 363 HOH B O   1 
HETATM 2853 O  O   . HOH N 4 .   ? 19.157 9.644   3.555   1.00 47.03 ? 364 HOH B O   1 
HETATM 2854 O  O   . HOH N 4 .   ? 14.301 6.074   5.673   1.00 28.66 ? 365 HOH B O   1 
HETATM 2855 O  O   . HOH N 4 .   ? 10.339 -22.498 0.793   1.00 26.45 ? 366 HOH B O   1 
HETATM 2856 O  O   . HOH N 4 .   ? 26.163 22.148  -14.607 1.00 24.62 ? 367 HOH B O   1 
HETATM 2857 O  O   . HOH N 4 .   ? 17.361 17.962  -12.950 1.00 38.53 ? 368 HOH B O   1 
HETATM 2858 O  O   . HOH N 4 .   ? 0.535  -7.818  -5.196  1.00 29.87 ? 369 HOH B O   1 
HETATM 2859 O  O   . HOH N 4 .   ? 6.606  11.628  -12.697 1.00 31.21 ? 370 HOH B O   1 
HETATM 2860 O  O   . HOH N 4 .   ? 6.941  -17.313 -9.755  1.00 20.62 ? 371 HOH B O   1 
HETATM 2861 O  O   . HOH N 4 .   ? 20.603 14.280  -20.740 1.00 20.09 ? 372 HOH B O   1 
HETATM 2862 O  O   . HOH N 4 .   ? 19.899 -3.671  -13.924 1.00 8.83  ? 373 HOH B O   1 
HETATM 2863 O  O   . HOH N 4 .   ? 30.855 2.818   -4.453  1.00 26.86 ? 374 HOH B O   1 
HETATM 2864 O  O   . HOH N 4 .   ? 2.697  -7.201  -20.295 1.00 37.26 ? 375 HOH B O   1 
HETATM 2865 O  O   . HOH N 4 .   ? 18.766 17.633  -17.591 1.00 38.72 ? 376 HOH B O   1 
HETATM 2866 O  O   . HOH N 4 .   ? 28.753 17.717  -14.280 1.00 30.67 ? 377 HOH B O   1 
HETATM 2867 O  O   . HOH N 4 .   ? 10.038 -10.530 5.080   1.00 43.03 ? 378 HOH B O   1 
HETATM 2868 O  O   . HOH N 4 .   ? 12.083 -19.582 3.755   1.00 32.33 ? 379 HOH B O   1 
HETATM 2869 O  O   . HOH N 4 .   ? 18.968 16.238  1.328   1.00 44.20 ? 380 HOH B O   1 
HETATM 2870 O  O   . HOH N 4 .   ? 24.722 -1.558  -6.514  1.00 20.18 ? 381 HOH B O   1 
HETATM 2871 O  O   . HOH N 4 .   ? 28.976 16.324  -19.041 1.00 14.70 ? 382 HOH B O   1 
HETATM 2872 O  O   . HOH N 4 .   ? 16.712 15.680  4.924   1.00 38.94 ? 383 HOH B O   1 
HETATM 2873 O  O   . HOH N 4 .   ? 13.389 14.901  -18.318 1.00 30.60 ? 384 HOH B O   1 
HETATM 2874 O  O   . HOH N 4 .   ? 3.476  -2.816  -23.499 1.00 30.25 ? 385 HOH B O   1 
HETATM 2875 O  O   . HOH N 4 .   ? 17.991 -19.514 10.713  1.00 34.42 ? 386 HOH B O   1 
HETATM 2876 O  O   . HOH N 4 .   ? 1.293  -9.102  -12.755 1.00 23.64 ? 387 HOH B O   1 
HETATM 2877 O  O   . HOH N 4 .   ? 14.026 -12.070 -14.405 1.00 23.48 ? 388 HOH B O   1 
HETATM 2878 O  O   . HOH N 4 .   ? 1.698  -10.143 -5.690  1.00 25.16 ? 389 HOH B O   1 
HETATM 2879 O  O   . HOH N 4 .   ? 29.204 13.085  -11.571 1.00 35.86 ? 390 HOH B O   1 
HETATM 2880 O  O   . HOH N 4 .   ? 15.927 -20.065 -14.636 1.00 20.91 ? 391 HOH B O   1 
HETATM 2881 O  O   . HOH N 4 .   ? 1.069  -5.067  -16.836 1.00 18.68 ? 392 HOH B O   1 
HETATM 2882 O  O   . HOH N 4 .   ? 6.951  12.449  -6.879  1.00 30.53 ? 393 HOH B O   1 
HETATM 2883 O  O   . HOH N 4 .   ? 25.796 14.875  -9.187  1.00 34.58 ? 394 HOH B O   1 
HETATM 2884 O  O   . HOH N 4 .   ? 11.423 -17.473 10.252  1.00 31.67 ? 395 HOH B O   1 
HETATM 2885 O  O   . HOH N 4 .   ? 9.367  2.093   6.986   1.00 23.05 ? 396 HOH B O   1 
HETATM 2886 O  O   . HOH N 4 .   ? 7.573  7.125   4.148   1.00 40.41 ? 397 HOH B O   1 
HETATM 2887 O  O   . HOH N 4 .   ? -0.988 -7.820  -11.923 1.00 47.05 ? 398 HOH B O   1 
HETATM 2888 O  O   . HOH N 4 .   ? 16.941 7.216   4.453   1.00 22.47 ? 399 HOH B O   1 
HETATM 2889 O  O   . HOH N 4 .   ? 12.781 -9.731  -3.627  1.00 28.51 ? 400 HOH B O   1 
HETATM 2890 O  O   . HOH N 4 .   ? 12.896 16.414  -0.284  1.00 34.04 ? 401 HOH B O   1 
HETATM 2891 O  O   . HOH N 4 .   ? 0.611  5.976   -13.766 1.00 34.20 ? 402 HOH B O   1 
HETATM 2892 O  O   . HOH N 4 .   ? 5.683  7.483   1.711   1.00 27.69 ? 403 HOH B O   1 
HETATM 2893 O  O   . HOH N 4 .   ? 13.495 6.760   8.499   1.00 32.01 ? 404 HOH B O   1 
HETATM 2894 O  O   . HOH N 4 .   ? 6.433  -16.741 -13.103 1.00 30.58 ? 405 HOH B O   1 
HETATM 2895 O  O   . HOH N 4 .   ? 17.849 2.588   -25.084 1.00 35.83 ? 406 HOH B O   1 
HETATM 2896 O  O   . HOH N 4 .   ? 25.255 -1.674  -9.954  1.00 25.03 ? 407 HOH B O   1 
HETATM 2897 O  O   . HOH N 4 .   ? 10.315 -13.009 -17.230 1.00 33.16 ? 408 HOH B O   1 
HETATM 2898 O  O   . HOH N 4 .   ? 20.016 -5.765  -11.668 1.00 27.40 ? 409 HOH B O   1 
HETATM 2899 O  O   . HOH N 4 .   ? 4.320  -14.383 -10.102 1.00 25.68 ? 410 HOH B O   1 
HETATM 2900 O  O   . HOH N 4 .   ? 7.678  15.271  -3.882  1.00 45.94 ? 411 HOH B O   1 
HETATM 2901 O  O   . HOH N 4 .   ? 1.366  5.104   -16.438 1.00 27.32 ? 412 HOH B O   1 
HETATM 2902 O  O   . HOH N 4 .   ? 14.636 17.343  -11.695 1.00 43.23 ? 413 HOH B O   1 
HETATM 2903 O  O   . HOH N 4 .   ? -0.714 -0.552  -14.082 1.00 30.71 ? 414 HOH B O   1 
HETATM 2904 O  O   . HOH N 4 .   ? 2.938  8.586   -10.456 1.00 26.50 ? 415 HOH B O   1 
HETATM 2905 O  O   . HOH N 4 .   ? 22.181 -0.408  -12.276 1.00 28.77 ? 416 HOH B O   1 
HETATM 2906 O  O   . HOH N 4 .   ? 7.494  -19.491 -11.687 1.00 21.63 ? 417 HOH B O   1 
HETATM 2907 O  O   . HOH N 4 .   ? 14.111 -17.201 -15.706 1.00 38.55 ? 418 HOH B O   1 
HETATM 2908 O  O   . HOH N 4 .   ? 32.610 4.710   -6.517  1.00 30.56 ? 419 HOH B O   1 
HETATM 2909 O  O   . HOH N 4 .   ? 12.030 13.987  2.050   1.00 39.81 ? 420 HOH B O   1 
HETATM 2910 O  O   . HOH N 4 .   ? 27.131 7.118   1.949   1.00 48.30 ? 421 HOH B O   1 
HETATM 2911 O  O   . HOH N 4 .   ? 22.754 15.401  -22.133 1.00 26.55 ? 422 HOH B O   1 
HETATM 2912 O  O   . HOH N 4 .   ? 19.771 -23.712 8.390   1.00 31.06 ? 423 HOH B O   1 
HETATM 2913 O  O   . HOH N 4 .   ? 30.985 5.424   -2.398  1.00 34.00 ? 424 HOH B O   1 
HETATM 2914 O  O   . HOH N 4 .   ? 20.580 17.799  -15.440 1.00 21.12 ? 425 HOH B O   1 
HETATM 2915 O  O   . HOH N 4 .   ? 7.896  13.123  -4.810  1.00 43.00 ? 426 HOH B O   1 
HETATM 2916 O  O   . HOH N 4 .   ? 20.834 19.237  -13.108 1.00 44.42 ? 427 HOH B O   1 
HETATM 2917 O  O   . HOH N 4 .   ? 13.216 17.207  -13.481 1.00 33.77 ? 428 HOH B O   1 
HETATM 2918 O  O   . HOH N 4 .   ? 10.137 -25.608 0.675   1.00 25.56 ? 429 HOH B O   1 
HETATM 2919 O  O   . HOH N 4 .   ? -1.766 -3.393  -15.197 1.00 43.26 ? 430 HOH B O   1 
HETATM 2920 O  O   . HOH N 4 .   ? 25.234 22.115  -11.891 1.00 43.74 ? 431 HOH B O   1 
HETATM 2921 O  O   . HOH N 4 .   ? 21.535 17.702  -18.084 1.00 38.05 ? 432 HOH B O   1 
HETATM 2922 O  O   . HOH N 4 .   ? -0.896 3.059   -6.884  1.00 44.65 ? 433 HOH B O   1 
HETATM 2923 O  O   . HOH N 4 .   ? 1.682  3.850   -7.519  1.00 42.72 ? 434 HOH B O   1 
HETATM 2924 O  O   . HOH N 4 .   ? 23.818 16.531  -7.893  1.00 33.52 ? 435 HOH B O   1 
HETATM 2925 O  O   . HOH N 4 .   ? 10.637 16.458  -13.920 1.00 43.32 ? 436 HOH B O   1 
HETATM 2926 O  O   . HOH N 4 .   ? 13.929 -12.483 -17.789 1.00 31.10 ? 437 HOH B O   1 
HETATM 2927 O  O   . HOH N 4 .   ? 15.854 -10.337 -17.532 1.00 22.08 ? 438 HOH B O   1 
HETATM 2928 O  O   . HOH N 4 .   ? 18.002 -11.181 -15.968 1.00 15.82 ? 439 HOH B O   1 
HETATM 2929 O  O   . HOH O 4 .   ? 22.312 4.177   -33.695 1.00 24.02 ? 301 HOH C O   1 
HETATM 2930 O  O   . HOH O 4 .   ? 41.121 0.430   -2.937  1.00 44.18 ? 302 HOH C O   1 
HETATM 2931 O  O   . HOH O 4 .   ? 33.646 6.317   -35.827 1.00 29.80 ? 303 HOH C O   1 
HETATM 2932 O  O   . HOH O 4 .   ? 14.577 7.871   -29.822 1.00 26.16 ? 304 HOH C O   1 
HETATM 2933 O  O   . HOH O 4 .   ? 40.229 6.252   -21.165 1.00 31.72 ? 305 HOH C O   1 
HETATM 2934 O  O   . HOH O 4 .   ? 17.019 -11.350 -21.511 1.00 25.40 ? 306 HOH C O   1 
HETATM 2935 O  O   . HOH O 4 .   ? 36.768 6.614   -27.607 1.00 41.04 ? 307 HOH C O   1 
HETATM 2936 O  O   . HOH O 4 .   ? 5.237  1.228   -29.330 1.00 41.24 ? 308 HOH C O   1 
HETATM 2937 O  O   . HOH O 4 .   ? 41.411 4.173   -3.415  1.00 40.47 ? 309 HOH C O   1 
HETATM 2938 O  O   . HOH O 4 .   ? 3.863  5.949   -20.432 1.00 31.76 ? 310 HOH C O   1 
HETATM 2939 O  O   . HOH O 4 .   ? 37.833 -0.028  -30.702 1.00 42.33 ? 311 HOH C O   1 
HETATM 2940 O  O   . HOH O 4 .   ? 24.697 -3.216  -17.162 1.00 18.02 ? 312 HOH C O   1 
HETATM 2941 O  O   . HOH O 4 .   ? 45.463 -13.972 -14.803 1.00 29.09 ? 313 HOH C O   1 
HETATM 2942 O  O   . HOH O 4 .   ? 45.378 2.074   -14.582 1.00 34.52 ? 314 HOH C O   1 
HETATM 2943 O  O   . HOH O 4 .   ? 14.801 -9.793  -24.555 1.00 35.02 ? 315 HOH C O   1 
HETATM 2944 O  O   . HOH O 4 .   ? 6.334  -1.213  -20.387 1.00 21.93 ? 316 HOH C O   1 
HETATM 2945 O  O   . HOH O 4 .   ? 45.339 -16.567 -19.758 1.00 28.00 ? 317 HOH C O   1 
HETATM 2946 O  O   . HOH O 4 .   ? 41.127 -11.942 -1.249  1.00 26.35 ? 318 HOH C O   1 
HETATM 2947 O  O   . HOH O 4 .   ? 32.399 -19.000 -14.756 1.00 34.03 ? 319 HOH C O   1 
HETATM 2948 O  O   . HOH O 4 .   ? 31.132 4.453   -8.779  1.00 17.39 ? 320 HOH C O   1 
HETATM 2949 O  O   . HOH O 4 .   ? 44.926 -6.186  -6.454  1.00 31.19 ? 321 HOH C O   1 
HETATM 2950 O  O   . HOH O 4 .   ? 46.532 3.979   -7.687  1.00 33.17 ? 322 HOH C O   1 
HETATM 2951 O  O   . HOH O 4 .   ? 7.265  -7.326  -18.744 1.00 26.27 ? 323 HOH C O   1 
HETATM 2952 O  O   . HOH O 4 .   ? 13.110 -8.999  -26.696 1.00 46.67 ? 324 HOH C O   1 
HETATM 2953 O  O   . HOH O 4 .   ? 26.952 -5.266  -13.081 1.00 23.88 ? 325 HOH C O   1 
HETATM 2954 O  O   . HOH O 4 .   ? 32.128 -4.823  -30.652 1.00 28.29 ? 326 HOH C O   1 
HETATM 2955 O  O   . HOH O 4 .   ? 43.645 -18.044 -8.242  1.00 36.09 ? 327 HOH C O   1 
HETATM 2956 O  O   . HOH O 4 .   ? 5.782  2.020   -23.256 1.00 25.97 ? 328 HOH C O   1 
HETATM 2957 O  O   . HOH O 4 .   ? 50.103 -9.658  -4.725  1.00 35.84 ? 329 HOH C O   1 
HETATM 2958 O  O   . HOH O 4 .   ? 47.119 -11.764 -14.509 1.00 30.40 ? 330 HOH C O   1 
HETATM 2959 O  O   . HOH O 4 .   ? 29.374 -4.893  -12.331 1.00 26.91 ? 331 HOH C O   1 
HETATM 2960 O  O   . HOH O 4 .   ? 7.364  4.133   -26.353 1.00 44.04 ? 332 HOH C O   1 
HETATM 2961 O  O   . HOH O 4 .   ? 39.433 -2.718  -26.972 1.00 20.98 ? 333 HOH C O   1 
HETATM 2962 O  O   . HOH O 4 .   ? 35.377 6.028   -29.980 1.00 39.82 ? 334 HOH C O   1 
HETATM 2963 O  O   . HOH O 4 .   ? 40.233 -2.404  -3.798  1.00 31.09 ? 335 HOH C O   1 
HETATM 2964 O  O   . HOH O 4 .   ? 43.311 14.430  -18.112 1.00 16.43 ? 336 HOH C O   1 
HETATM 2965 O  O   . HOH O 4 .   ? 21.009 -12.609 -19.986 1.00 15.45 ? 337 HOH C O   1 
HETATM 2966 O  O   . HOH O 4 .   ? 41.792 7.626   -20.500 1.00 33.58 ? 338 HOH C O   1 
HETATM 2967 O  O   . HOH O 4 .   ? 26.458 -5.199  -32.335 1.00 25.97 ? 339 HOH C O   1 
HETATM 2968 O  O   . HOH O 4 .   ? 42.530 15.597  -13.816 1.00 26.09 ? 340 HOH C O   1 
HETATM 2969 O  O   . HOH O 4 .   ? 15.719 -9.828  -28.756 1.00 41.72 ? 341 HOH C O   1 
HETATM 2970 O  O   . HOH O 4 .   ? 27.315 7.743   -20.977 1.00 14.99 ? 342 HOH C O   1 
HETATM 2971 O  O   . HOH O 4 .   ? 45.561 -2.451  -12.152 1.00 33.72 ? 343 HOH C O   1 
HETATM 2972 O  O   . HOH O 4 .   ? 24.570 0.538   -11.488 1.00 20.49 ? 344 HOH C O   1 
HETATM 2973 O  O   . HOH O 4 .   ? 44.601 -8.658  -13.693 1.00 15.92 ? 345 HOH C O   1 
HETATM 2974 O  O   . HOH O 4 .   ? 45.876 -14.255 -9.683  1.00 31.05 ? 346 HOH C O   1 
HETATM 2975 O  O   . HOH O 4 .   ? 32.258 -11.867 -32.980 1.00 22.42 ? 347 HOH C O   1 
HETATM 2976 O  O   . HOH O 4 .   ? 47.609 -10.144 -18.668 1.00 45.61 ? 348 HOH C O   1 
HETATM 2977 O  O   . HOH O 4 .   ? 47.595 -4.619  -12.900 1.00 30.13 ? 349 HOH C O   1 
HETATM 2978 O  O   . HOH O 4 .   ? 17.243 12.722  -24.078 1.00 30.51 ? 350 HOH C O   1 
HETATM 2979 O  O   . HOH O 4 .   ? 15.082 -7.041  -26.861 1.00 21.52 ? 351 HOH C O   1 
HETATM 2980 O  O   . HOH O 4 .   ? 41.816 -16.429 -14.275 1.00 18.68 ? 352 HOH C O   1 
HETATM 2981 O  O   . HOH O 4 .   ? 28.845 -9.109  -13.600 1.00 25.11 ? 353 HOH C O   1 
HETATM 2982 O  O   . HOH O 4 .   ? 40.694 -7.255  -19.519 1.00 15.90 ? 354 HOH C O   1 
HETATM 2983 O  O   . HOH O 4 .   ? 21.373 11.228  -22.757 1.00 23.01 ? 355 HOH C O   1 
HETATM 2984 O  O   . HOH O 4 .   ? 19.335 -9.181  -29.411 1.00 20.45 ? 356 HOH C O   1 
HETATM 2985 O  O   . HOH O 4 .   ? 46.351 -9.383  -4.209  1.00 25.75 ? 357 HOH C O   1 
HETATM 2986 O  O   . HOH O 4 .   ? 35.640 -6.453  -30.887 1.00 22.40 ? 358 HOH C O   1 
HETATM 2987 O  O   . HOH O 4 .   ? 45.078 -12.075 -3.542  1.00 24.61 ? 359 HOH C O   1 
HETATM 2988 O  O   . HOH O 4 .   ? 26.001 5.046   -32.776 1.00 23.58 ? 360 HOH C O   1 
HETATM 2989 O  O   . HOH O 4 .   ? 28.180 -14.807 -14.560 1.00 20.34 ? 361 HOH C O   1 
HETATM 2990 O  O   . HOH O 4 .   ? 13.709 6.203   -28.004 1.00 36.95 ? 362 HOH C O   1 
HETATM 2991 O  O   . HOH O 4 .   ? 31.426 10.848  -23.794 1.00 13.38 ? 363 HOH C O   1 
HETATM 2992 O  O   . HOH O 4 .   ? 33.914 2.994   -5.321  1.00 24.18 ? 364 HOH C O   1 
HETATM 2993 O  O   . HOH O 4 .   ? 37.864 -2.412  -0.723  1.00 29.50 ? 365 HOH C O   1 
HETATM 2994 O  O   . HOH O 4 .   ? 35.260 0.634   -1.437  1.00 25.15 ? 366 HOH C O   1 
HETATM 2995 O  O   . HOH O 4 .   ? 30.768 9.520   -20.929 1.00 22.28 ? 367 HOH C O   1 
HETATM 2996 O  O   . HOH O 4 .   ? 3.896  6.283   -17.540 1.00 33.94 ? 368 HOH C O   1 
HETATM 2997 O  O   . HOH O 4 .   ? 38.275 8.634   -14.317 1.00 34.44 ? 369 HOH C O   1 
HETATM 2998 O  O   . HOH O 4 .   ? 41.850 -1.497  -26.188 1.00 29.28 ? 370 HOH C O   1 
HETATM 2999 O  O   . HOH O 4 .   ? 22.943 -6.730  -34.645 1.00 42.07 ? 371 HOH C O   1 
HETATM 3000 O  O   . HOH O 4 .   ? 28.223 1.505   -35.403 1.00 31.64 ? 372 HOH C O   1 
HETATM 3001 O  O   . HOH O 4 .   ? 38.397 10.253  -22.856 1.00 27.24 ? 373 HOH C O   1 
HETATM 3002 O  O   . HOH O 4 .   ? 33.820 0.168   -30.551 1.00 26.89 ? 374 HOH C O   1 
HETATM 3003 O  O   . HOH O 4 .   ? 19.270 -11.881 -21.977 1.00 19.68 ? 375 HOH C O   1 
HETATM 3004 O  O   . HOH O 4 .   ? 36.826 11.025  -24.847 1.00 31.77 ? 376 HOH C O   1 
HETATM 3005 O  O   . HOH O 4 .   ? 42.701 5.684   -5.243  1.00 24.73 ? 377 HOH C O   1 
HETATM 3006 O  O   . HOH O 4 .   ? 47.233 -7.402  -15.710 1.00 28.24 ? 378 HOH C O   1 
HETATM 3007 O  O   . HOH O 4 .   ? 39.860 -4.199  -2.104  1.00 47.07 ? 379 HOH C O   1 
HETATM 3008 O  O   . HOH O 4 .   ? 43.747 -15.371 -12.531 1.00 21.59 ? 380 HOH C O   1 
HETATM 3009 O  O   . HOH O 4 .   ? 36.656 12.375  -27.450 1.00 20.85 ? 381 HOH C O   1 
HETATM 3010 O  O   . HOH O 4 .   ? 32.004 -14.726 -33.925 1.00 34.33 ? 382 HOH C O   1 
HETATM 3011 O  O   . HOH O 4 .   ? 18.768 -6.206  -32.197 1.00 24.61 ? 383 HOH C O   1 
HETATM 3012 O  O   . HOH O 4 .   ? 25.680 -9.167  -13.708 1.00 15.31 ? 384 HOH C O   1 
HETATM 3013 O  O   . HOH O 4 .   ? 30.387 -4.728  -32.627 1.00 37.80 ? 385 HOH C O   1 
HETATM 3014 O  O   . HOH O 4 .   ? 8.009  -8.121  -21.527 1.00 37.12 ? 386 HOH C O   1 
HETATM 3015 O  O   . HOH O 4 .   ? 31.622 0.442   -2.461  1.00 24.71 ? 387 HOH C O   1 
HETATM 3016 O  O   . HOH O 4 .   ? 25.269 -15.062 -33.278 1.00 35.33 ? 388 HOH C O   1 
HETATM 3017 O  O   . HOH O 4 .   ? 44.588 10.064  -15.598 1.00 25.39 ? 389 HOH C O   1 
HETATM 3018 O  O   . HOH O 4 .   ? 12.033 -5.536  -27.177 1.00 23.44 ? 390 HOH C O   1 
HETATM 3019 O  O   . HOH O 4 .   ? 20.678 -8.271  -32.214 1.00 26.69 ? 391 HOH C O   1 
HETATM 3020 O  O   . HOH O 4 .   ? 17.347 -9.870  -19.835 1.00 26.63 ? 392 HOH C O   1 
HETATM 3021 O  O   . HOH O 4 .   ? 27.317 -18.526 -30.620 1.00 25.51 ? 393 HOH C O   1 
HETATM 3022 O  O   . HOH O 4 .   ? 22.510 -15.292 -30.983 1.00 31.79 ? 394 HOH C O   1 
HETATM 3023 O  O   . HOH O 4 .   ? 8.696  -5.497  -25.009 1.00 23.07 ? 395 HOH C O   1 
HETATM 3024 O  O   . HOH O 4 .   ? 34.708 -5.113  -33.194 1.00 45.14 ? 396 HOH C O   1 
HETATM 3025 O  O   . HOH O 4 .   ? 35.984 9.053   -16.229 1.00 22.86 ? 397 HOH C O   1 
HETATM 3026 O  O   . HOH O 4 .   ? 27.463 -1.671  -8.792  1.00 22.69 ? 398 HOH C O   1 
HETATM 3027 O  O   . HOH O 4 .   ? 39.998 -14.426 -1.280  1.00 36.58 ? 399 HOH C O   1 
HETATM 3028 O  O   . HOH O 4 .   ? 42.118 -6.021  -3.955  1.00 21.73 ? 400 HOH C O   1 
HETATM 3029 O  O   . HOH O 4 .   ? 9.172  -10.196 -18.309 1.00 19.58 ? 401 HOH C O   1 
HETATM 3030 O  O   . HOH O 4 .   ? 20.001 -8.685  -14.911 1.00 38.70 ? 402 HOH C O   1 
HETATM 3031 O  O   . HOH O 4 .   ? 44.540 -7.196  -3.078  1.00 37.24 ? 403 HOH C O   1 
HETATM 3032 O  O   . HOH O 4 .   ? 40.465 -5.119  -28.426 1.00 33.37 ? 404 HOH C O   1 
HETATM 3033 O  O   . HOH O 4 .   ? 40.024 -6.826  -3.058  1.00 19.09 ? 405 HOH C O   1 
HETATM 3034 O  O   . HOH O 4 .   ? 10.212 5.961   -24.703 1.00 41.11 ? 406 HOH C O   1 
HETATM 3035 O  O   . HOH O 4 .   ? 44.884 -12.608 -19.631 1.00 27.93 ? 407 HOH C O   1 
HETATM 3036 O  O   . HOH O 4 .   ? 38.940 3.484   -31.624 1.00 42.34 ? 408 HOH C O   1 
HETATM 3037 O  O   . HOH O 4 .   ? 23.286 -16.627 -28.432 1.00 29.03 ? 409 HOH C O   1 
HETATM 3038 O  O   . HOH O 4 .   ? 41.350 9.702   -22.279 1.00 30.03 ? 410 HOH C O   1 
HETATM 3039 O  O   . HOH O 4 .   ? 45.697 4.892   -19.760 1.00 26.84 ? 411 HOH C O   1 
HETATM 3040 O  O   . HOH O 4 .   ? 26.521 -3.985  -10.703 1.00 28.99 ? 412 HOH C O   1 
HETATM 3041 O  O   . HOH O 4 .   ? 44.079 -3.606  -7.154  1.00 32.56 ? 413 HOH C O   1 
HETATM 3042 O  O   . HOH O 4 .   ? 35.739 -8.598  -32.726 1.00 28.10 ? 414 HOH C O   1 
HETATM 3043 O  O   . HOH O 4 .   ? 19.553 0.667   -21.331 1.00 26.60 ? 415 HOH C O   1 
HETATM 3044 O  O   . HOH O 4 .   ? 51.367 -3.453  -16.384 1.00 48.48 ? 416 HOH C O   1 
HETATM 3045 O  O   . HOH O 4 .   ? 46.742 -5.860  -18.458 1.00 36.48 ? 417 HOH C O   1 
HETATM 3046 O  O   . HOH O 4 .   ? 51.330 -9.890  -7.321  1.00 32.60 ? 418 HOH C O   1 
HETATM 3047 O  O   . HOH O 4 .   ? 23.410 -7.082  -13.804 1.00 22.24 ? 419 HOH C O   1 
HETATM 3048 O  O   . HOH O 4 .   ? 34.970 -11.262 -31.887 1.00 19.22 ? 420 HOH C O   1 
HETATM 3049 O  O   . HOH O 4 .   ? 15.158 -5.775  -29.598 1.00 27.73 ? 421 HOH C O   1 
HETATM 3050 O  O   . HOH O 4 .   ? 28.881 -7.434  -11.524 1.00 35.80 ? 422 HOH C O   1 
HETATM 3051 O  O   . HOH O 4 .   ? 29.190 -9.169  -34.274 1.00 31.13 ? 423 HOH C O   1 
HETATM 3052 O  O   . HOH O 4 .   ? 46.667 -3.529  -23.393 1.00 37.75 ? 424 HOH C O   1 
HETATM 3053 O  O   . HOH O 4 .   ? 27.212 -5.261  -8.519  1.00 24.78 ? 425 HOH C O   1 
HETATM 3054 O  O   . HOH O 4 .   ? 16.592 -12.806 -23.623 1.00 43.42 ? 426 HOH C O   1 
HETATM 3055 O  O   . HOH O 4 .   ? 45.491 7.679   -25.398 1.00 31.62 ? 427 HOH C O   1 
HETATM 3056 O  O   . HOH O 4 .   ? 41.053 -8.126  -0.425  1.00 26.00 ? 428 HOH C O   1 
HETATM 3057 O  O   . HOH O 4 .   ? 8.902  13.787  -12.985 1.00 32.98 ? 429 HOH C O   1 
HETATM 3058 O  O   . HOH O 4 .   ? 38.260 -5.164  -30.334 1.00 20.67 ? 430 HOH C O   1 
HETATM 3059 O  O   . HOH O 4 .   ? 7.288  -7.517  -23.596 1.00 39.71 ? 431 HOH C O   1 
HETATM 3060 O  O   . HOH O 4 .   ? 13.226 13.261  -24.621 1.00 49.91 ? 432 HOH C O   1 
HETATM 3061 O  O   . HOH O 4 .   ? 23.465 -9.155  -35.912 1.00 36.27 ? 433 HOH C O   1 
HETATM 3062 O  O   . HOH O 4 .   ? 35.233 -16.051 -32.322 1.00 47.13 ? 434 HOH C O   1 
HETATM 3063 O  O   . HOH O 4 .   ? 47.008 -10.146 -12.501 1.00 34.96 ? 435 HOH C O   1 
HETATM 3064 O  O   . HOH O 4 .   ? 12.341 -11.424 -19.885 1.00 40.96 ? 436 HOH C O   1 
HETATM 3065 O  O   . HOH O 4 .   ? 46.824 -12.327 -11.211 1.00 38.95 ? 437 HOH C O   1 
HETATM 3066 O  O   . HOH O 4 .   ? 4.998  12.654  -14.775 1.00 39.69 ? 438 HOH C O   1 
HETATM 3067 O  O   . HOH O 4 .   ? 33.905 2.670   -2.499  1.00 32.96 ? 439 HOH C O   1 
HETATM 3068 O  O   . HOH O 4 .   ? 33.581 -1.581  -0.728  1.00 27.62 ? 440 HOH C O   1 
HETATM 3069 O  O   . HOH O 4 .   ? 41.548 9.902   -8.443  1.00 31.11 ? 441 HOH C O   1 
HETATM 3070 O  O   . HOH O 4 .   ? 4.585  11.553  -17.191 1.00 36.28 ? 442 HOH C O   1 
HETATM 3071 O  O   . HOH O 4 .   ? 28.976 -6.661  -33.389 1.00 39.94 ? 443 HOH C O   1 
HETATM 3072 O  O   . HOH O 4 .   ? 25.603 -10.833 -35.247 1.00 35.88 ? 444 HOH C O   1 
HETATM 3073 O  O   . HOH O 4 .   ? 46.696 -7.870  -19.891 1.00 29.93 ? 445 HOH C O   1 
HETATM 3074 O  O   . HOH O 4 .   ? 14.898 1.170   -28.334 1.00 39.41 ? 446 HOH C O   1 
HETATM 3075 O  O   . HOH O 4 .   ? 16.757 -8.210  -31.046 1.00 45.65 ? 447 HOH C O   1 
HETATM 3076 O  O   . HOH O 4 .   ? 45.427 -2.173  -9.202  1.00 29.36 ? 448 HOH C O   1 
HETATM 3077 O  O   . HOH O 4 .   ? 45.623 4.648   -5.196  1.00 40.50 ? 449 HOH C O   1 
HETATM 3078 O  O   . HOH O 4 .   ? 12.682 -3.535  -29.229 1.00 36.97 ? 450 HOH C O   1 
HETATM 3079 O  O   . HOH O 4 .   ? 45.980 -8.297  -22.428 1.00 26.60 ? 451 HOH C O   1 
HETATM 3080 O  O   . HOH O 4 .   ? 19.114 -12.968 -17.879 1.00 21.58 ? 452 HOH C O   1 
HETATM 3081 O  O   . HOH O 4 .   ? 17.059 -13.572 -19.581 1.00 34.62 ? 453 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   . PRO A 1   ? 0.1620 0.1732 0.2081 0.0488  0.0003  -0.0105 1   PRO A N   
2    C  CA  . PRO A 1   ? 0.1623 0.1783 0.2061 0.0297  0.0144  -0.0196 1   PRO A CA  
3    C  C   . PRO A 1   ? 0.1589 0.1905 0.1861 0.0231  -0.0010 -0.0319 1   PRO A C   
4    O  O   . PRO A 1   ? 0.1545 0.2087 0.1860 0.0153  -0.0065 -0.0378 1   PRO A O   
5    C  CB  . PRO A 1   ? 0.1970 0.1978 0.2228 0.0105  0.0255  -0.0219 1   PRO A CB  
6    C  CG  . PRO A 1   ? 0.2055 0.2083 0.2307 0.0200  0.0271  -0.0139 1   PRO A CG  
7    C  CD  . PRO A 1   ? 0.1925 0.1922 0.2208 0.0320  0.0120  -0.0016 1   PRO A CD  
8    N  N   . MET A 2   ? 0.1687 0.1780 0.1834 0.0313  0.0097  -0.0302 2   MET A N   
9    C  CA  . MET A 2   ? 0.1938 0.1853 0.1980 0.0117  0.0394  -0.0241 2   MET A CA  
10   C  C   . MET A 2   ? 0.1623 0.1673 0.1827 0.0178  0.0228  -0.0134 2   MET A C   
11   O  O   . MET A 2   ? 0.1467 0.1889 0.1765 0.0060  0.0206  -0.0193 2   MET A O   
12   C  CB  . MET A 2   ? 0.2888 0.2419 0.2483 -0.0139 0.0832  0.0058  2   MET A CB  
13   C  CG  . MET A 2   ? 0.3255 0.3273 0.2959 0.0222  0.0656  0.0467  2   MET A CG  
14   S  SD  . MET A 2   ? 0.3089 0.3522 0.3122 0.0579  0.0505  0.0963  2   MET A SD  
15   C  CE  . MET A 2   ? 0.2526 0.3432 0.2952 0.0954  0.0395  0.1017  2   MET A CE  
16   N  N   . PHE A 3   ? 0.1437 0.1451 0.1734 0.0169  0.0166  -0.0110 3   PHE A N   
17   C  CA  . PHE A 3   ? 0.1446 0.1365 0.1698 0.0206  0.0173  -0.0091 3   PHE A CA  
18   C  C   . PHE A 3   ? 0.1379 0.1434 0.1665 0.0028  0.0163  -0.0069 3   PHE A C   
19   O  O   . PHE A 3   ? 0.1309 0.1571 0.1862 0.0061  -0.0018 -0.0270 3   PHE A O   
20   C  CB  . PHE A 3   ? 0.1717 0.1525 0.1747 0.0187  0.0138  0.0080  3   PHE A CB  
21   C  CG  . PHE A 3   ? 0.1791 0.1689 0.1836 0.0285  0.0085  0.0212  3   PHE A CG  
22   C  CD1 . PHE A 3   ? 0.1831 0.1593 0.2042 0.0299  0.0218  0.0296  3   PHE A CD1 
23   C  CD2 . PHE A 3   ? 0.1969 0.2421 0.1882 0.0389  -0.0006 0.0149  3   PHE A CD2 
24   C  CE1 . PHE A 3   ? 0.1944 0.1963 0.2049 0.0329  0.0149  0.0409  3   PHE A CE1 
25   C  CE2 . PHE A 3   ? 0.1976 0.2722 0.2033 0.0393  0.0011  0.0211  3   PHE A CE2 
26   C  CZ  . PHE A 3   ? 0.2010 0.2483 0.2104 0.0304  0.0124  0.0335  3   PHE A CZ  
27   N  N   . ILE A 4   ? 0.1569 0.1391 0.1518 0.0175  0.0138  -0.0002 4   ILE A N   
28   C  CA  . ILE A 4   ? 0.1593 0.1467 0.1489 0.0183  0.0201  -0.0022 4   ILE A CA  
29   C  C   . ILE A 4   ? 0.1341 0.1490 0.1575 0.0049  0.0103  -0.0187 4   ILE A C   
30   O  O   . ILE A 4   ? 0.1335 0.1593 0.1762 0.0070  0.0061  -0.0295 4   ILE A O   
31   C  CB  . ILE A 4   ? 0.2071 0.1680 0.1700 0.0307  0.0318  0.0154  4   ILE A CB  
32   C  CG1 . ILE A 4   ? 0.2466 0.2036 0.1774 0.0090  0.0175  0.0273  4   ILE A CG1 
33   C  CG2 . ILE A 4   ? 0.2244 0.1621 0.2020 0.0361  0.0385  0.0169  4   ILE A CG2 
34   C  CD1 . ILE A 4   ? 0.2681 0.2394 0.1982 0.0070  -0.0128 0.0165  4   ILE A CD1 
35   N  N   . VAL A 5   ? 0.1442 0.1525 0.1590 -0.0008 0.0196  -0.0224 5   VAL A N   
36   C  CA  . VAL A 5   ? 0.1742 0.1764 0.1621 0.0037  0.0238  -0.0256 5   VAL A CA  
37   C  C   . VAL A 5   ? 0.1487 0.1694 0.1747 -0.0025 0.0207  -0.0323 5   VAL A C   
38   O  O   . VAL A 5   ? 0.1443 0.1590 0.2019 0.0051  0.0057  -0.0332 5   VAL A O   
39   C  CB  . VAL A 5   ? 0.2540 0.2312 0.1779 0.0282  0.0316  -0.0059 5   VAL A CB  
40   C  CG1 . VAL A 5   ? 0.2948 0.2809 0.2009 0.0215  0.0205  -0.0107 5   VAL A CG1 
41   C  CG2 . VAL A 5   ? 0.2769 0.2438 0.1594 0.0342  0.0470  0.0029  5   VAL A CG2 
42   N  N   . ASN A 6   ? 0.1417 0.1500 0.1627 0.0068  0.0198  -0.0281 6   ASN A N   
43   C  CA  . ASN A 6   ? 0.1589 0.1490 0.1656 0.0153  0.0136  -0.0243 6   ASN A CA  
44   C  C   . ASN A 6   ? 0.1552 0.1536 0.1647 -0.0017 0.0261  -0.0301 6   ASN A C   
45   O  O   . ASN A 6   ? 0.1531 0.1732 0.1792 -0.0109 0.0214  -0.0335 6   ASN A O   
46   C  CB  . ASN A 6   ? 0.1881 0.1883 0.1944 0.0431  0.0248  0.0031  6   ASN A CB  
47   C  CG  . ASN A 6   ? 0.2378 0.2692 0.2377 0.0850  0.0186  0.0265  6   ASN A CG  
48   O  OD1 . ASN A 6   ? 0.2001 0.3223 0.2610 0.0593  0.0325  0.0691  6   ASN A OD1 
49   N  ND2 . ASN A 6   ? 0.3088 0.3173 0.2399 0.1437  0.0031  0.0350  6   ASN A ND2 
50   N  N   . THR A 7   ? 0.1664 0.1593 0.1590 0.0023  0.0344  -0.0281 7   THR A N   
51   C  CA  . THR A 7   ? 0.1651 0.1771 0.1667 0.0118  0.0237  -0.0198 7   THR A CA  
52   C  C   . THR A 7   ? 0.1520 0.1808 0.1738 0.0054  0.0163  -0.0247 7   THR A C   
53   O  O   . THR A 7   ? 0.1479 0.1684 0.1813 -0.0072 0.0025  -0.0287 7   THR A O   
54   C  CB  . THR A 7   ? 0.1697 0.1782 0.1667 0.0007  0.0163  0.0042  7   THR A CB  
55   O  OG1 . THR A 7   ? 0.1860 0.1837 0.1591 -0.0123 0.0123  -0.0012 7   THR A OG1 
56   C  CG2 . THR A 7   ? 0.1611 0.1889 0.1769 0.0087  -0.0018 0.0053  7   THR A CG2 
57   N  N   . ASN A 8   ? 0.1742 0.1681 0.1782 0.0095  0.0249  -0.0408 8   ASN A N   
58   C  CA  . ASN A 8   ? 0.1840 0.1849 0.1867 0.0049  0.0231  -0.0497 8   ASN A CA  
59   C  C   . ASN A 8   ? 0.1857 0.2103 0.1941 -0.0069 0.0043  -0.0435 8   ASN A C   
60   O  O   . ASN A 8   ? 0.2064 0.2175 0.2193 -0.0059 -0.0141 -0.0478 8   ASN A O   
61   C  CB  . ASN A 8   ? 0.1854 0.1940 0.2004 -0.0133 0.0459  -0.0513 8   ASN A CB  
62   C  CG  . ASN A 8   ? 0.2000 0.2015 0.2029 -0.0204 0.0495  -0.0613 8   ASN A CG  
63   O  OD1 . ASN A 8   ? 0.1881 0.2185 0.1981 -0.0128 0.0436  -0.0449 8   ASN A OD1 
64   N  ND2 . ASN A 8   ? 0.2221 0.2251 0.2366 -0.0192 0.0740  -0.0591 8   ASN A ND2 
65   N  N   . VAL A 9   ? 0.1671 0.2275 0.1850 -0.0107 0.0041  -0.0247 9   VAL A N   
66   C  CA  . VAL A 9   ? 0.1809 0.2410 0.2020 -0.0253 -0.0071 -0.0129 9   VAL A CA  
67   C  C   . VAL A 9   ? 0.1885 0.2494 0.1968 -0.0184 -0.0109 -0.0128 9   VAL A C   
68   O  O   . VAL A 9   ? 0.1771 0.2698 0.1929 -0.0238 -0.0013 0.0009  9   VAL A O   
69   C  CB  . VAL A 9   ? 0.2145 0.2697 0.2259 -0.0526 -0.0266 0.0166  9   VAL A CB  
70   C  CG1 . VAL A 9   ? 0.2595 0.3003 0.2372 -0.0485 -0.0344 0.0137  9   VAL A CG1 
71   C  CG2 . VAL A 9   ? 0.2159 0.2841 0.2275 -0.0538 -0.0194 0.0187  9   VAL A CG2 
72   N  N   . PRO A 10  ? 0.2069 0.2570 0.2184 -0.0284 -0.0067 -0.0366 10  PRO A N   
73   C  CA  . PRO A 10  ? 0.2029 0.2786 0.2294 -0.0374 -0.0029 -0.0418 10  PRO A CA  
74   C  C   . PRO A 10  ? 0.1790 0.2693 0.2289 -0.0321 -0.0113 -0.0348 10  PRO A C   
75   O  O   . PRO A 10  ? 0.1622 0.2733 0.2241 -0.0313 -0.0138 -0.0348 10  PRO A O   
76   C  CB  . PRO A 10  ? 0.2378 0.2989 0.2399 -0.0471 -0.0069 -0.0615 10  PRO A CB  
77   C  CG  . PRO A 10  ? 0.2603 0.3052 0.2366 -0.0605 -0.0112 -0.0636 10  PRO A CG  
78   C  CD  . PRO A 10  ? 0.2435 0.2822 0.2277 -0.0379 -0.0023 -0.0526 10  PRO A CD  
79   N  N   . ARG A 11  ? 0.1813 0.2879 0.2348 -0.0290 -0.0121 -0.0393 11  ARG A N   
80   C  CA  . ARG A 11  ? 0.1887 0.3304 0.2460 -0.0193 0.0020  -0.0410 11  ARG A CA  
81   C  C   . ARG A 11  ? 0.1975 0.3408 0.2392 -0.0142 -0.0176 -0.0412 11  ARG A C   
82   O  O   . ARG A 11  ? 0.2119 0.3445 0.2456 -0.0018 -0.0115 -0.0312 11  ARG A O   
83   C  CB  . ARG A 11  ? 0.2104 0.3696 0.2735 -0.0094 0.0250  -0.0552 11  ARG A CB  
84   C  CG  . ARG A 11  ? 0.2632 0.4319 0.3164 0.0214  0.0184  -0.0616 11  ARG A CG  
85   C  CD  . ARG A 11  ? 0.3043 0.4864 0.3589 0.0583  0.0072  -0.0570 11  ARG A CD  
86   N  NE  . ARG A 11  ? 0.3330 0.5234 0.3929 0.0800  -0.0002 -0.0497 11  ARG A NE  
87   C  CZ  . ARG A 11  ? 0.3524 0.5513 0.4139 0.1008  -0.0168 -0.0426 11  ARG A CZ  
88   N  NH1 . ARG A 11  ? 0.3654 0.5555 0.4283 0.0951  -0.0186 -0.0335 11  ARG A NH1 
89   N  NH2 . ARG A 11  ? 0.3700 0.5626 0.4184 0.1167  -0.0265 -0.0465 11  ARG A NH2 
90   N  N   . ALA A 12  ? 0.1981 0.3570 0.2373 -0.0161 -0.0448 -0.0438 12  ALA A N   
91   C  CA  . ALA A 12  ? 0.2534 0.3704 0.2402 0.0036  -0.0579 -0.0407 12  ALA A CA  
92   C  C   . ALA A 12  ? 0.2547 0.3669 0.2382 0.0232  -0.0418 -0.0307 12  ALA A C   
93   O  O   . ALA A 12  ? 0.2694 0.3799 0.2707 0.0247  -0.0473 -0.0124 12  ALA A O   
94   C  CB  . ALA A 12  ? 0.2868 0.3827 0.2451 -0.0112 -0.0722 -0.0574 12  ALA A CB  
95   N  N   . SER A 13  ? 0.2523 0.3444 0.2176 0.0269  -0.0071 -0.0423 13  SER A N   
96   C  CA  . SER A 13  ? 0.2746 0.3398 0.2273 0.0275  0.0128  -0.0397 13  SER A CA  
97   C  C   . SER A 13  ? 0.2797 0.3200 0.2188 0.0286  0.0155  -0.0185 13  SER A C   
98   O  O   . SER A 13  ? 0.3115 0.3329 0.2283 0.0058  0.0331  -0.0006 13  SER A O   
99   C  CB  . SER A 13  ? 0.3077 0.3737 0.2515 0.0197  0.0137  -0.0429 13  SER A CB  
100  O  OG  . SER A 13  ? 0.3394 0.4010 0.2739 0.0155  0.0211  -0.0389 13  SER A OG  
101  N  N   . VAL A 14  ? 0.2397 0.2919 0.2068 0.0577  0.0010  -0.0136 14  VAL A N   
102  C  CA  . VAL A 14  ? 0.2271 0.2793 0.2185 0.0578  -0.0033 -0.0030 14  VAL A CA  
103  C  C   . VAL A 14  ? 0.2114 0.2841 0.2340 0.0381  -0.0114 0.0035  14  VAL A C   
104  O  O   . VAL A 14  ? 0.2234 0.3130 0.2613 0.0201  0.0055  0.0027  14  VAL A O   
105  C  CB  . VAL A 14  ? 0.2432 0.2686 0.2217 0.0599  -0.0072 0.0002  14  VAL A CB  
106  C  CG1 . VAL A 14  ? 0.2710 0.2548 0.2231 0.0605  0.0000  -0.0035 14  VAL A CG1 
107  C  CG2 . VAL A 14  ? 0.2397 0.2840 0.2240 0.0595  -0.0238 0.0046  14  VAL A CG2 
108  N  N   . PRO A 15  ? 0.1911 0.2809 0.2290 0.0349  -0.0165 0.0103  15  PRO A N   
109  C  CA  . PRO A 15  ? 0.2048 0.2940 0.2354 0.0373  -0.0167 0.0079  15  PRO A CA  
110  C  C   . PRO A 15  ? 0.1870 0.2929 0.2251 0.0404  -0.0250 -0.0099 15  PRO A C   
111  O  O   . PRO A 15  ? 0.1801 0.2901 0.2247 0.0445  -0.0242 -0.0098 15  PRO A O   
112  C  CB  . PRO A 15  ? 0.2170 0.3043 0.2472 0.0426  -0.0066 0.0259  15  PRO A CB  
113  C  CG  . PRO A 15  ? 0.2188 0.3094 0.2547 0.0527  -0.0142 0.0224  15  PRO A CG  
114  C  CD  . PRO A 15  ? 0.2033 0.2970 0.2408 0.0462  -0.0165 0.0220  15  PRO A CD  
115  N  N   . ASP A 16  ? 0.1778 0.3030 0.2336 0.0499  -0.0216 -0.0205 16  ASP A N   
116  C  CA  . ASP A 16  ? 0.1747 0.2915 0.2429 0.0484  -0.0388 -0.0289 16  ASP A CA  
117  C  C   . ASP A 16  ? 0.1893 0.3050 0.2283 0.0471  -0.0452 -0.0318 16  ASP A C   
118  O  O   . ASP A 16  ? 0.2308 0.3206 0.2342 0.0345  -0.0452 -0.0394 16  ASP A O   
119  C  CB  . ASP A 16  ? 0.1882 0.2800 0.2733 0.0269  -0.0474 -0.0269 16  ASP A CB  
120  C  CG  . ASP A 16  ? 0.2178 0.2741 0.3043 0.0206  -0.0451 -0.0301 16  ASP A CG  
121  O  OD1 . ASP A 16  ? 0.2302 0.2803 0.3336 0.0292  -0.0391 -0.0186 16  ASP A OD1 
122  O  OD2 . ASP A 16  ? 0.2250 0.2612 0.3030 0.0217  -0.0421 -0.0363 16  ASP A OD2 
123  N  N   . GLY A 17  ? 0.1632 0.2899 0.2144 0.0553  -0.0378 -0.0377 17  GLY A N   
124  C  CA  . GLY A 17  ? 0.1652 0.2605 0.2135 0.0354  -0.0419 -0.0240 17  GLY A CA  
125  C  C   . GLY A 17  ? 0.1784 0.2318 0.2023 0.0272  -0.0410 -0.0017 17  GLY A C   
126  O  O   . GLY A 17  ? 0.1988 0.2149 0.2240 0.0301  -0.0486 0.0202  17  GLY A O   
127  N  N   . PHE A 18  ? 0.1728 0.2300 0.1802 0.0309  -0.0267 0.0003  18  PHE A N   
128  C  CA  . PHE A 18  ? 0.1706 0.2404 0.1772 0.0319  -0.0213 -0.0050 18  PHE A CA  
129  C  C   . PHE A 18  ? 0.1647 0.2134 0.1826 0.0210  -0.0212 -0.0031 18  PHE A C   
130  O  O   . PHE A 18  ? 0.1761 0.1936 0.1944 0.0292  -0.0285 -0.0008 18  PHE A O   
131  C  CB  . PHE A 18  ? 0.1749 0.2901 0.1822 0.0319  0.0095  -0.0187 18  PHE A CB  
132  C  CG  . PHE A 18  ? 0.1865 0.3272 0.1916 0.0267  0.0099  -0.0233 18  PHE A CG  
133  C  CD1 . PHE A 18  ? 0.2001 0.3605 0.2028 0.0214  0.0090  -0.0212 18  PHE A CD1 
134  C  CD2 . PHE A 18  ? 0.1904 0.3381 0.1923 0.0475  0.0093  -0.0242 18  PHE A CD2 
135  C  CE1 . PHE A 18  ? 0.2141 0.3796 0.2093 0.0203  0.0167  -0.0220 18  PHE A CE1 
136  C  CE2 . PHE A 18  ? 0.1972 0.3558 0.1965 0.0557  0.0069  -0.0211 18  PHE A CE2 
137  C  CZ  . PHE A 18  ? 0.2025 0.3712 0.2056 0.0417  0.0168  -0.0193 18  PHE A CZ  
138  N  N   . LEU A 19  ? 0.1572 0.2088 0.1776 0.0277  -0.0193 -0.0057 19  LEU A N   
139  C  CA  . LEU A 19  ? 0.1930 0.1953 0.1787 0.0449  -0.0154 -0.0083 19  LEU A CA  
140  C  C   . LEU A 19  ? 0.1887 0.1797 0.1798 0.0479  -0.0195 0.0085  19  LEU A C   
141  O  O   . LEU A 19  ? 0.2169 0.1703 0.1763 0.0380  -0.0146 0.0046  19  LEU A O   
142  C  CB  . LEU A 19  ? 0.2473 0.2026 0.1996 0.0503  -0.0182 -0.0043 19  LEU A CB  
143  C  CG  . LEU A 19  ? 0.2814 0.2183 0.2170 0.0555  -0.0217 -0.0100 19  LEU A CG  
144  C  CD1 . LEU A 19  ? 0.3240 0.2182 0.2146 0.0311  0.0059  0.0066  19  LEU A CD1 
145  C  CD2 . LEU A 19  ? 0.2847 0.2357 0.2498 0.0640  -0.0494 -0.0304 19  LEU A CD2 
146  N  N   . SER A 20  ? 0.1978 0.1964 0.1864 0.0740  -0.0170 0.0298  20  SER A N   
147  C  CA  . SER A 20  ? 0.2245 0.2183 0.2135 0.0790  -0.0362 0.0287  20  SER A CA  
148  C  C   . SER A 20  ? 0.2305 0.2181 0.1935 0.0546  -0.0356 0.0174  20  SER A C   
149  O  O   . SER A 20  ? 0.2493 0.2092 0.2037 0.0511  -0.0137 0.0168  20  SER A O   
150  C  CB  . SER A 20  ? 0.2313 0.2508 0.2580 0.1104  -0.0497 0.0178  20  SER A CB  
151  O  OG  . SER A 20  ? 0.2589 0.2899 0.3040 0.0910  -0.0573 -0.0029 20  SER A OG  
152  N  N   . GLU A 21  ? 0.2457 0.2331 0.1787 0.0505  -0.0394 0.0188  21  GLU A N   
153  C  CA  . GLU A 21  ? 0.2688 0.2250 0.1882 0.0505  -0.0093 0.0182  21  GLU A CA  
154  C  C   . GLU A 21  ? 0.2465 0.1992 0.1787 0.0354  0.0116  0.0204  21  GLU A C   
155  O  O   . GLU A 21  ? 0.2704 0.1807 0.1808 0.0325  0.0171  0.0228  21  GLU A O   
156  C  CB  . GLU A 21  ? 0.3139 0.2400 0.2115 0.0623  0.0051  0.0206  21  GLU A CB  
157  C  CG  . GLU A 21  ? 0.3574 0.2903 0.2353 0.0692  0.0168  0.0218  21  GLU A CG  
158  C  CD  . GLU A 21  ? 0.4090 0.3338 0.2666 0.0674  0.0238  0.0309  21  GLU A CD  
159  O  OE1 . GLU A 21  ? 0.4262 0.3546 0.2779 0.0758  0.0293  0.0332  21  GLU A OE1 
160  O  OE2 . GLU A 21  ? 0.4282 0.3598 0.2843 0.0566  0.0181  0.0363  21  GLU A OE2 
161  N  N   . LEU A 22  ? 0.2101 0.1974 0.1754 0.0505  0.0126  0.0199  22  LEU A N   
162  C  CA  . LEU A 22  ? 0.1847 0.1976 0.1882 0.0476  0.0062  0.0249  22  LEU A CA  
163  C  C   . LEU A 22  ? 0.1899 0.1903 0.1853 0.0413  0.0020  0.0308  22  LEU A C   
164  O  O   . LEU A 22  ? 0.1983 0.1862 0.1961 0.0296  -0.0019 0.0224  22  LEU A O   
165  C  CB  . LEU A 22  ? 0.1943 0.2019 0.2031 0.0461  0.0196  0.0080  22  LEU A CB  
166  C  CG  . LEU A 22  ? 0.1781 0.2158 0.2201 0.0334  0.0120  -0.0061 22  LEU A CG  
167  C  CD1 . LEU A 22  ? 0.1819 0.2044 0.2280 0.0260  0.0091  -0.0009 22  LEU A CD1 
168  C  CD2 . LEU A 22  ? 0.1817 0.2376 0.2396 0.0211  0.0081  -0.0123 22  LEU A CD2 
169  N  N   . THR A 23  ? 0.1865 0.1987 0.1634 0.0454  0.0055  0.0247  23  THR A N   
170  C  CA  . THR A 23  ? 0.1929 0.1919 0.1669 0.0487  -0.0048 0.0175  23  THR A CA  
171  C  C   . THR A 23  ? 0.1971 0.1928 0.1763 0.0420  -0.0139 0.0141  23  THR A C   
172  O  O   . THR A 23  ? 0.1992 0.1864 0.1843 0.0355  -0.0156 0.0231  23  THR A O   
173  C  CB  . THR A 23  ? 0.2038 0.1839 0.1677 0.0367  0.0045  0.0264  23  THR A CB  
174  O  OG1 . THR A 23  ? 0.1983 0.1658 0.1630 0.0309  0.0071  0.0304  23  THR A OG1 
175  C  CG2 . THR A 23  ? 0.2154 0.1950 0.1720 0.0333  0.0105  0.0136  23  THR A CG2 
176  N  N   . GLN A 24  ? 0.2129 0.1883 0.1957 0.0611  -0.0046 0.0116  24  GLN A N   
177  C  CA  . GLN A 24  ? 0.2502 0.2030 0.2338 0.0440  -0.0165 0.0231  24  GLN A CA  
178  C  C   . GLN A 24  ? 0.2413 0.1733 0.2121 0.0560  0.0015  0.0310  24  GLN A C   
179  O  O   . GLN A 24  ? 0.2438 0.1641 0.2095 0.0458  0.0033  0.0181  24  GLN A O   
180  C  CB  . GLN A 24  ? 0.3427 0.3233 0.3200 0.0142  -0.0085 0.0100  24  GLN A CB  
181  C  CG  . GLN A 24  ? 0.3713 0.3669 0.3646 0.0064  -0.0044 0.0015  24  GLN A CG  
182  C  CD  . GLN A 24  ? 0.3760 0.3794 0.3774 -0.0013 -0.0016 -0.0002 24  GLN A CD  
183  O  OE1 . GLN A 24  ? 0.3827 0.3833 0.3822 -0.0050 -0.0117 0.0034  24  GLN A OE1 
184  N  NE2 . GLN A 24  ? 0.3820 0.3834 0.3815 -0.0008 0.0005  0.0003  24  GLN A NE2 
185  N  N   . GLN A 25  ? 0.2460 0.1803 0.2009 0.0502  0.0062  0.0357  25  GLN A N   
186  C  CA  . GLN A 25  ? 0.2612 0.2006 0.2055 0.0408  0.0095  0.0348  25  GLN A CA  
187  C  C   . GLN A 25  ? 0.2391 0.1805 0.2024 0.0349  0.0084  0.0272  25  GLN A C   
188  O  O   . GLN A 25  ? 0.2436 0.1699 0.2081 0.0198  0.0210  0.0235  25  GLN A O   
189  C  CB  . GLN A 25  ? 0.2957 0.2390 0.2168 0.0415  0.0238  0.0473  25  GLN A CB  
190  C  CG  . GLN A 25  ? 0.3555 0.2747 0.2639 0.0224  0.0198  0.0675  25  GLN A CG  
191  C  CD  . GLN A 25  ? 0.4126 0.3308 0.3326 0.0099  0.0196  0.0746  25  GLN A CD  
192  O  OE1 . GLN A 25  ? 0.4347 0.3723 0.3732 -0.0020 0.0382  0.0947  25  GLN A OE1 
193  N  NE2 . GLN A 25  ? 0.4392 0.3344 0.3396 0.0060  0.0098  0.0659  25  GLN A NE2 
194  N  N   . LEU A 26  ? 0.2143 0.1726 0.1862 0.0398  0.0149  0.0264  26  LEU A N   
195  C  CA  . LEU A 26  ? 0.2251 0.1730 0.1861 0.0388  0.0041  0.0150  26  LEU A CA  
196  C  C   . LEU A 26  ? 0.2404 0.1808 0.1918 0.0351  0.0073  0.0084  26  LEU A C   
197  O  O   . LEU A 26  ? 0.2433 0.1900 0.2013 0.0382  0.0042  0.0070  26  LEU A O   
198  C  CB  . LEU A 26  ? 0.2307 0.1919 0.1845 0.0384  0.0009  0.0066  26  LEU A CB  
199  C  CG  . LEU A 26  ? 0.2460 0.2152 0.2000 0.0468  -0.0129 0.0036  26  LEU A CG  
200  C  CD1 . LEU A 26  ? 0.2981 0.2202 0.2044 0.0440  -0.0139 0.0088  26  LEU A CD1 
201  C  CD2 . LEU A 26  ? 0.2303 0.2475 0.2189 0.0512  -0.0078 -0.0008 26  LEU A CD2 
202  N  N   . ALA A 27  ? 0.2564 0.1865 0.2004 0.0559  0.0090  0.0006  27  ALA A N   
203  C  CA  . ALA A 27  ? 0.2681 0.1987 0.2269 0.0669  0.0113  -0.0196 27  ALA A CA  
204  C  C   . ALA A 27  ? 0.3036 0.1950 0.2494 0.0648  0.0131  -0.0347 27  ALA A C   
205  O  O   . ALA A 27  ? 0.3119 0.2087 0.2564 0.0587  0.0109  -0.0567 27  ALA A O   
206  C  CB  . ALA A 27  ? 0.2451 0.2106 0.2324 0.0817  0.0121  -0.0250 27  ALA A CB  
207  N  N   . GLN A 28  ? 0.3217 0.1784 0.2687 0.0715  0.0180  -0.0170 28  GLN A N   
208  C  CA  . GLN A 28  ? 0.3436 0.1896 0.3092 0.0641  0.0079  0.0054  28  GLN A CA  
209  C  C   . GLN A 28  ? 0.3321 0.1959 0.2979 0.0435  0.0145  -0.0002 28  GLN A C   
210  O  O   . GLN A 28  ? 0.3442 0.2069 0.3154 0.0417  0.0082  -0.0176 28  GLN A O   
211  C  CB  . GLN A 28  ? 0.3845 0.2389 0.3712 0.0759  0.0034  0.0254  28  GLN A CB  
212  C  CG  . GLN A 28  ? 0.4316 0.3194 0.4358 0.0735  0.0022  0.0428  28  GLN A CG  
213  C  CD  . GLN A 28  ? 0.4694 0.3962 0.4895 0.0821  0.0034  0.0675  28  GLN A CD  
214  O  OE1 . GLN A 28  ? 0.5123 0.4258 0.5118 0.0797  0.0039  0.0811  28  GLN A OE1 
215  N  NE2 . GLN A 28  ? 0.4566 0.4291 0.5061 0.0881  0.0061  0.0780  28  GLN A NE2 
216  N  N   . ALA A 29  ? 0.2957 0.1944 0.2634 0.0500  0.0150  0.0029  29  ALA A N   
217  C  CA  . ALA A 29  ? 0.2797 0.2074 0.2388 0.0223  0.0211  -0.0061 29  ALA A CA  
218  C  C   . ALA A 29  ? 0.2919 0.2019 0.2311 0.0089  0.0359  -0.0076 29  ALA A C   
219  O  O   . ALA A 29  ? 0.3035 0.2084 0.2479 0.0037  0.0366  -0.0160 29  ALA A O   
220  C  CB  . ALA A 29  ? 0.2489 0.2072 0.2295 0.0193  0.0309  -0.0085 29  ALA A CB  
221  N  N   . THR A 30  ? 0.2931 0.1843 0.2222 0.0047  0.0341  -0.0011 30  THR A N   
222  C  CA  . THR A 30  ? 0.3018 0.1827 0.2345 0.0057  0.0113  -0.0026 30  THR A CA  
223  C  C   . THR A 30  ? 0.2927 0.2019 0.2472 0.0036  0.0069  0.0004  30  THR A C   
224  O  O   . THR A 30  ? 0.2885 0.2278 0.2435 0.0157  -0.0119 -0.0069 30  THR A O   
225  C  CB  . THR A 30  ? 0.2950 0.1787 0.2421 0.0150  -0.0072 -0.0049 30  THR A CB  
226  O  OG1 . THR A 30  ? 0.2713 0.1765 0.2285 0.0137  -0.0166 -0.0117 30  THR A OG1 
227  C  CG2 . THR A 30  ? 0.3128 0.1854 0.2643 0.0280  -0.0086 -0.0097 30  THR A CG2 
228  N  N   . GLY A 31  ? 0.2710 0.1872 0.2568 -0.0052 0.0295  0.0129  31  GLY A N   
229  C  CA  . GLY A 31  ? 0.2849 0.1980 0.2673 -0.0061 0.0345  -0.0007 31  GLY A CA  
230  C  C   . GLY A 31  ? 0.2937 0.2222 0.2762 -0.0168 0.0236  -0.0156 31  GLY A C   
231  O  O   . GLY A 31  ? 0.3164 0.2301 0.3023 -0.0034 0.0294  -0.0262 31  GLY A O   
232  N  N   . LYS A 32  ? 0.2858 0.2427 0.2746 -0.0424 0.0183  0.0023  32  LYS A N   
233  C  CA  . LYS A 32  ? 0.2860 0.2620 0.2747 -0.0323 0.0222  0.0021  32  LYS A CA  
234  C  C   . LYS A 32  ? 0.2819 0.2472 0.2459 -0.0277 0.0332  -0.0281 32  LYS A C   
235  O  O   . LYS A 32  ? 0.2724 0.2453 0.2320 -0.0160 0.0187  -0.0283 32  LYS A O   
236  C  CB  . LYS A 32  ? 0.2819 0.3103 0.3078 -0.0289 0.0074  0.0315  32  LYS A CB  
237  C  CG  . LYS A 32  ? 0.2852 0.3554 0.3368 -0.0286 0.0070  0.0383  32  LYS A CG  
238  C  CD  . LYS A 32  ? 0.2689 0.3755 0.3441 -0.0199 0.0069  0.0315  32  LYS A CD  
239  C  CE  . LYS A 32  ? 0.2772 0.3693 0.3427 -0.0008 0.0012  0.0284  32  LYS A CE  
240  N  NZ  . LYS A 32  ? 0.2900 0.3718 0.3446 0.0101  0.0049  0.0153  32  LYS A NZ  
241  N  N   . PRO A 33  ? 0.2922 0.2398 0.2442 -0.0537 0.0460  -0.0547 33  PRO A N   
242  C  CA  . PRO A 33  ? 0.2929 0.2260 0.2344 -0.0288 0.0386  -0.0606 33  PRO A CA  
243  C  C   . PRO A 33  ? 0.2648 0.1659 0.2126 0.0130  0.0344  -0.0209 33  PRO A C   
244  O  O   . PRO A 33  ? 0.2587 0.1570 0.2072 0.0032  0.0338  -0.0041 33  PRO A O   
245  C  CB  . PRO A 33  ? 0.3275 0.2745 0.2609 -0.0392 0.0429  -0.0763 33  PRO A CB  
246  C  CG  . PRO A 33  ? 0.3312 0.2909 0.2751 -0.0554 0.0457  -0.0834 33  PRO A CG  
247  C  CD  . PRO A 33  ? 0.3165 0.2802 0.2621 -0.0692 0.0499  -0.0754 33  PRO A CD  
248  N  N   . PRO A 34  ? 0.2416 0.1474 0.2216 0.0350  0.0083  -0.0063 34  PRO A N   
249  C  CA  . PRO A 34  ? 0.2396 0.1517 0.2026 0.0429  0.0008  0.0123  34  PRO A CA  
250  C  C   . PRO A 34  ? 0.2114 0.1449 0.1883 0.0395  -0.0091 0.0067  34  PRO A C   
251  O  O   . PRO A 34  ? 0.2054 0.1474 0.1747 0.0467  -0.0141 -0.0019 34  PRO A O   
252  C  CB  . PRO A 34  ? 0.2584 0.1801 0.2233 0.0591  -0.0119 0.0259  34  PRO A CB  
253  C  CG  . PRO A 34  ? 0.2631 0.1856 0.2442 0.0430  -0.0167 0.0139  34  PRO A CG  
254  C  CD  . PRO A 34  ? 0.2493 0.1610 0.2400 0.0285  -0.0114 0.0085  34  PRO A CD  
255  N  N   . GLN A 35  ? 0.1909 0.1598 0.1927 0.0466  -0.0010 0.0104  35  GLN A N   
256  C  CA  . GLN A 35  ? 0.1862 0.1847 0.1981 0.0512  0.0015  0.0026  35  GLN A CA  
257  C  C   . GLN A 35  ? 0.1771 0.1662 0.1874 0.0251  0.0076  0.0088  35  GLN A C   
258  O  O   . GLN A 35  ? 0.1857 0.1749 0.1918 0.0117  -0.0009 0.0240  35  GLN A O   
259  C  CB  . GLN A 35  ? 0.1741 0.2285 0.2231 0.0563  0.0028  -0.0071 35  GLN A CB  
260  C  CG  . GLN A 35  ? 0.1989 0.2525 0.2568 0.0703  -0.0067 -0.0242 35  GLN A CG  
261  C  CD  . GLN A 35  ? 0.2218 0.2626 0.2762 0.0793  -0.0067 -0.0388 35  GLN A CD  
262  O  OE1 . GLN A 35  ? 0.2090 0.2587 0.2765 0.0682  0.0160  -0.0282 35  GLN A OE1 
263  N  NE2 . GLN A 35  ? 0.2390 0.2673 0.2817 0.0844  -0.0285 -0.0556 35  GLN A NE2 
264  N  N   . TYR A 36  ? 0.1678 0.1639 0.1761 0.0193  0.0036  -0.0030 36  TYR A N   
265  C  CA  . TYR A 36  ? 0.1755 0.1843 0.1823 0.0368  0.0026  -0.0196 36  TYR A CA  
266  C  C   . TYR A 36  ? 0.1950 0.1754 0.1648 0.0515  -0.0005 -0.0016 36  TYR A C   
267  O  O   . TYR A 36  ? 0.2045 0.1872 0.1647 0.0492  0.0005  0.0076  36  TYR A O   
268  C  CB  . TYR A 36  ? 0.1740 0.2240 0.2154 0.0430  0.0116  -0.0519 36  TYR A CB  
269  C  CG  . TYR A 36  ? 0.1915 0.2706 0.2573 0.0406  0.0085  -0.0860 36  TYR A CG  
270  C  CD1 . TYR A 36  ? 0.2125 0.3003 0.2903 0.0559  -0.0017 -0.1091 36  TYR A CD1 
271  C  CD2 . TYR A 36  ? 0.2286 0.3036 0.2707 0.0363  0.0260  -0.0979 36  TYR A CD2 
272  C  CE1 . TYR A 36  ? 0.2169 0.3225 0.3120 0.0448  0.0064  -0.1301 36  TYR A CE1 
273  C  CE2 . TYR A 36  ? 0.2416 0.3216 0.2882 0.0467  0.0366  -0.1227 36  TYR A CE2 
274  C  CZ  . TYR A 36  ? 0.2200 0.3325 0.3130 0.0454  0.0320  -0.1401 36  TYR A CZ  
275  O  OH  . TYR A 36  ? 0.2241 0.3536 0.3357 0.0352  0.0264  -0.1649 36  TYR A OH  
276  N  N   . ILE A 37  ? 0.1830 0.1538 0.1554 0.0263  0.0125  0.0019  37  ILE A N   
277  C  CA  . ILE A 37  ? 0.1693 0.1578 0.1591 0.0240  0.0239  -0.0036 37  ILE A CA  
278  C  C   . ILE A 37  ? 0.1550 0.1524 0.1576 0.0272  0.0059  -0.0056 37  ILE A C   
279  O  O   . ILE A 37  ? 0.1482 0.1570 0.1770 0.0272  -0.0088 -0.0075 37  ILE A O   
280  C  CB  . ILE A 37  ? 0.2095 0.1575 0.1797 0.0222  0.0243  -0.0041 37  ILE A CB  
281  C  CG1 . ILE A 37  ? 0.2326 0.1672 0.2167 0.0208  0.0000  -0.0105 37  ILE A CG1 
282  C  CG2 . ILE A 37  ? 0.2298 0.1681 0.1875 0.0316  0.0368  0.0048  37  ILE A CG2 
283  C  CD1 . ILE A 37  ? 0.2576 0.1957 0.2398 0.0155  -0.0171 0.0025  37  ILE A CD1 
284  N  N   . ALA A 38  ? 0.1584 0.1260 0.1510 0.0167  0.0051  0.0010  38  ALA A N   
285  C  CA  . ALA A 38  ? 0.1348 0.1323 0.1569 0.0234  0.0055  0.0110  38  ALA A CA  
286  C  C   . ALA A 38  ? 0.1350 0.1405 0.1638 0.0308  0.0073  0.0039  38  ALA A C   
287  O  O   . ALA A 38  ? 0.1435 0.1622 0.1696 0.0271  0.0023  0.0026  38  ALA A O   
288  C  CB  . ALA A 38  ? 0.1580 0.1507 0.1628 0.0137  0.0053  0.0213  38  ALA A CB  
289  N  N   . VAL A 39  ? 0.1349 0.1498 0.1613 0.0238  0.0121  -0.0119 39  VAL A N   
290  C  CA  . VAL A 39  ? 0.1415 0.1604 0.1616 0.0172  0.0086  -0.0062 39  VAL A CA  
291  C  C   . VAL A 39  ? 0.1246 0.1652 0.1645 0.0267  0.0101  -0.0043 39  VAL A C   
292  O  O   . VAL A 39  ? 0.1173 0.1846 0.1778 0.0205  0.0065  -0.0201 39  VAL A O   
293  C  CB  . VAL A 39  ? 0.1827 0.1637 0.1770 0.0168  0.0038  0.0026  39  VAL A CB  
294  C  CG1 . VAL A 39  ? 0.2028 0.1589 0.1851 0.0142  -0.0063 0.0214  39  VAL A CG1 
295  C  CG2 . VAL A 39  ? 0.2177 0.1994 0.2054 0.0036  0.0051  -0.0065 39  VAL A CG2 
296  N  N   . HIS A 40  ? 0.1507 0.1475 0.1648 0.0068  0.0043  -0.0168 40  HIS A N   
297  C  CA  . HIS A 40  ? 0.1568 0.1323 0.1643 0.0090  0.0101  -0.0149 40  HIS A CA  
298  C  C   . HIS A 40  ? 0.1446 0.1432 0.1672 0.0048  0.0142  -0.0197 40  HIS A C   
299  O  O   . HIS A 40  ? 0.1372 0.1605 0.1851 0.0077  0.0132  -0.0239 40  HIS A O   
300  C  CB  . HIS A 40  ? 0.1521 0.1512 0.1824 0.0119  0.0071  0.0021  40  HIS A CB  
301  C  CG  . HIS A 40  ? 0.1490 0.1573 0.1953 0.0145  0.0248  0.0115  40  HIS A CG  
302  N  ND1 . HIS A 40  ? 0.1592 0.1749 0.1998 0.0136  0.0296  0.0154  40  HIS A ND1 
303  C  CD2 . HIS A 40  ? 0.1646 0.1647 0.2055 0.0187  0.0229  0.0194  40  HIS A CD2 
304  C  CE1 . HIS A 40  ? 0.1636 0.1673 0.2091 0.0129  0.0296  0.0216  40  HIS A CE1 
305  N  NE2 . HIS A 40  ? 0.1680 0.1693 0.2067 0.0109  0.0297  0.0162  40  HIS A NE2 
306  N  N   . VAL A 41  ? 0.1366 0.1535 0.1618 0.0120  -0.0005 -0.0212 41  VAL A N   
307  C  CA  . VAL A 41  ? 0.1534 0.1786 0.1638 0.0133  -0.0029 -0.0133 41  VAL A CA  
308  C  C   . VAL A 41  ? 0.1396 0.1749 0.1666 0.0046  0.0107  -0.0011 41  VAL A C   
309  O  O   . VAL A 41  ? 0.1477 0.1832 0.1790 -0.0035 -0.0040 -0.0176 41  VAL A O   
310  C  CB  . VAL A 41  ? 0.2129 0.1919 0.1740 0.0432  -0.0133 -0.0163 41  VAL A CB  
311  C  CG1 . VAL A 41  ? 0.2497 0.2108 0.1616 0.0300  -0.0191 -0.0074 41  VAL A CG1 
312  C  CG2 . VAL A 41  ? 0.2459 0.1933 0.2000 0.0313  -0.0088 -0.0106 41  VAL A CG2 
313  N  N   . VAL A 42  ? 0.1436 0.1594 0.1748 0.0140  0.0085  -0.0123 42  VAL A N   
314  C  CA  . VAL A 42  ? 0.1494 0.1664 0.1814 0.0202  0.0117  -0.0229 42  VAL A CA  
315  C  C   . VAL A 42  ? 0.1294 0.1750 0.1758 0.0037  0.0173  -0.0263 42  VAL A C   
316  O  O   . VAL A 42  ? 0.1424 0.1804 0.1806 -0.0039 0.0148  -0.0351 42  VAL A O   
317  C  CB  . VAL A 42  ? 0.1587 0.1697 0.1948 0.0251  0.0055  -0.0262 42  VAL A CB  
318  C  CG1 . VAL A 42  ? 0.2055 0.1704 0.2092 0.0313  0.0140  -0.0155 42  VAL A CG1 
319  C  CG2 . VAL A 42  ? 0.1648 0.2036 0.1924 0.0252  0.0123  -0.0302 42  VAL A CG2 
320  N  N   . PRO A 43  ? 0.1438 0.2216 0.1756 0.0103  0.0065  -0.0293 43  PRO A N   
321  C  CA  . PRO A 43  ? 0.1510 0.2218 0.1750 0.0108  -0.0004 -0.0300 43  PRO A CA  
322  C  C   . PRO A 43  ? 0.1410 0.2040 0.1889 0.0058  -0.0026 -0.0285 43  PRO A C   
323  O  O   . PRO A 43  ? 0.1397 0.1905 0.1998 -0.0011 0.0142  -0.0384 43  PRO A O   
324  C  CB  . PRO A 43  ? 0.1684 0.2582 0.1881 0.0194  0.0051  -0.0207 43  PRO A CB  
325  C  CG  . PRO A 43  ? 0.1724 0.2904 0.1928 0.0149  -0.0076 -0.0162 43  PRO A CG  
326  C  CD  . PRO A 43  ? 0.1462 0.2648 0.1817 0.0110  -0.0085 -0.0192 43  PRO A CD  
327  N  N   . ASP A 44  ? 0.1541 0.2024 0.1983 0.0051  -0.0050 -0.0391 44  ASP A N   
328  C  CA  . ASP A 44  ? 0.1691 0.1989 0.2222 -0.0125 -0.0071 -0.0502 44  ASP A CA  
329  C  C   . ASP A 44  ? 0.1749 0.1817 0.2052 -0.0147 0.0060  -0.0398 44  ASP A C   
330  O  O   . ASP A 44  ? 0.2093 0.1823 0.2155 -0.0314 -0.0032 -0.0288 44  ASP A O   
331  C  CB  . ASP A 44  ? 0.2112 0.2331 0.2722 -0.0332 -0.0168 -0.0636 44  ASP A CB  
332  C  CG  . ASP A 44  ? 0.2798 0.3024 0.3298 -0.0320 -0.0192 -0.0627 44  ASP A CG  
333  O  OD1 . ASP A 44  ? 0.3333 0.3491 0.3414 -0.0451 -0.0403 -0.0537 44  ASP A OD1 
334  O  OD2 . ASP A 44  ? 0.3063 0.3449 0.3688 -0.0141 -0.0184 -0.0601 44  ASP A OD2 
335  N  N   . GLN A 45  ? 0.1495 0.1714 0.1976 -0.0152 0.0155  -0.0271 45  GLN A N   
336  C  CA  . GLN A 45  ? 0.1575 0.1635 0.1956 -0.0018 0.0261  -0.0267 45  GLN A CA  
337  C  C   . GLN A 45  ? 0.1525 0.1737 0.2125 0.0021  0.0366  -0.0294 45  GLN A C   
338  O  O   . GLN A 45  ? 0.1826 0.1958 0.2146 0.0227  0.0390  -0.0155 45  GLN A O   
339  C  CB  . GLN A 45  ? 0.1848 0.1552 0.1856 -0.0015 0.0298  -0.0164 45  GLN A CB  
340  C  CG  . GLN A 45  ? 0.1749 0.1632 0.1852 -0.0023 0.0294  -0.0138 45  GLN A CG  
341  C  CD  . GLN A 45  ? 0.1768 0.1769 0.1878 -0.0103 0.0137  -0.0088 45  GLN A CD  
342  O  OE1 . GLN A 45  ? 0.1874 0.2107 0.1850 -0.0177 -0.0019 0.0171  45  GLN A OE1 
343  N  NE2 . GLN A 45  ? 0.1813 0.1772 0.1971 -0.0190 0.0190  -0.0299 45  GLN A NE2 
344  N  N   . LEU A 46  ? 0.1305 0.1602 0.2314 -0.0027 0.0183  -0.0368 46  LEU A N   
345  C  CA  . LEU A 46  ? 0.1445 0.1571 0.2354 -0.0051 0.0208  -0.0320 46  LEU A CA  
346  C  C   . LEU A 46  ? 0.1433 0.1718 0.2181 -0.0094 0.0300  -0.0404 46  LEU A C   
347  O  O   . LEU A 46  ? 0.1701 0.1796 0.2228 -0.0230 0.0261  -0.0289 46  LEU A O   
348  C  CB  . LEU A 46  ? 0.1705 0.1663 0.2586 0.0012  0.0215  -0.0254 46  LEU A CB  
349  C  CG  . LEU A 46  ? 0.2165 0.2093 0.2953 0.0193  0.0171  -0.0141 46  LEU A CG  
350  C  CD1 . LEU A 46  ? 0.2309 0.2305 0.3093 0.0185  0.0136  -0.0277 46  LEU A CD1 
351  C  CD2 . LEU A 46  ? 0.2263 0.2248 0.3071 0.0225  0.0120  -0.0026 46  LEU A CD2 
352  N  N   . MET A 47  ? 0.1669 0.1773 0.2293 -0.0119 0.0389  -0.0412 47  MET A N   
353  C  CA  . MET A 47  ? 0.1901 0.1882 0.2466 -0.0251 0.0445  -0.0566 47  MET A CA  
354  C  C   . MET A 47  ? 0.1931 0.2006 0.2336 -0.0426 0.0275  -0.0411 47  MET A C   
355  O  O   . MET A 47  ? 0.1999 0.2348 0.2289 -0.0542 0.0163  -0.0463 47  MET A O   
356  C  CB  . MET A 47  ? 0.2247 0.2017 0.2936 -0.0283 0.0538  -0.0711 47  MET A CB  
357  C  CG  . MET A 47  ? 0.2338 0.2264 0.3293 0.0083  0.0306  -0.0502 47  MET A CG  
358  S  SD  . MET A 47  ? 0.2053 0.2066 0.3415 0.0205  -0.0067 -0.0288 47  MET A SD  
359  C  CE  . MET A 47  ? 0.1626 0.2122 0.3413 0.0234  0.0306  0.0446  47  MET A CE  
360  N  N   . ALA A 48  ? 0.1789 0.1858 0.2285 -0.0455 0.0284  -0.0246 48  ALA A N   
361  C  CA  . ALA A 48  ? 0.1827 0.1941 0.2262 -0.0405 0.0386  -0.0351 48  ALA A CA  
362  C  C   . ALA A 48  ? 0.1673 0.1814 0.2112 -0.0297 0.0361  -0.0360 48  ALA A C   
363  O  O   . ALA A 48  ? 0.1678 0.1746 0.2127 -0.0303 0.0367  -0.0390 48  ALA A O   
364  C  CB  . ALA A 48  ? 0.1715 0.2168 0.2411 -0.0428 0.0516  -0.0366 48  ALA A CB  
365  N  N   . PHE A 49  ? 0.1724 0.1584 0.2021 -0.0182 0.0308  -0.0303 49  PHE A N   
366  C  CA  . PHE A 49  ? 0.1764 0.1525 0.2017 -0.0183 0.0249  -0.0212 49  PHE A CA  
367  C  C   . PHE A 49  ? 0.1636 0.1668 0.2076 -0.0279 0.0160  -0.0153 49  PHE A C   
368  O  O   . PHE A 49  ? 0.1808 0.1896 0.1954 -0.0039 0.0255  -0.0041 49  PHE A O   
369  C  CB  . PHE A 49  ? 0.1888 0.1735 0.2053 -0.0082 0.0165  -0.0304 49  PHE A CB  
370  C  CG  . PHE A 49  ? 0.2079 0.1868 0.2042 0.0043  0.0035  -0.0283 49  PHE A CG  
371  C  CD1 . PHE A 49  ? 0.2197 0.1793 0.2210 -0.0077 -0.0018 -0.0156 49  PHE A CD1 
372  C  CD2 . PHE A 49  ? 0.2384 0.2040 0.1993 0.0170  -0.0023 -0.0344 49  PHE A CD2 
373  C  CE1 . PHE A 49  ? 0.2351 0.1773 0.2246 -0.0153 -0.0124 -0.0152 49  PHE A CE1 
374  C  CE2 . PHE A 49  ? 0.2582 0.1986 0.2082 0.0186  -0.0103 -0.0343 49  PHE A CE2 
375  C  CZ  . PHE A 49  ? 0.2547 0.1902 0.2164 0.0066  -0.0192 -0.0338 49  PHE A CZ  
376  N  N   . GLY A 50  ? 0.1446 0.1806 0.2224 -0.0292 0.0149  -0.0099 50  GLY A N   
377  C  CA  . GLY A 50  ? 0.1723 0.2306 0.2455 -0.0210 0.0257  -0.0004 50  GLY A CA  
378  C  C   . GLY A 50  ? 0.1905 0.2695 0.2356 0.0241  0.0302  -0.0054 50  GLY A C   
379  O  O   . GLY A 50  ? 0.2184 0.3366 0.2375 0.0257  0.0474  0.0046  50  GLY A O   
380  N  N   . GLY A 51  ? 0.2132 0.2299 0.2292 0.0360  0.0074  -0.0280 51  GLY A N   
381  C  CA  . GLY A 51  ? 0.2638 0.2319 0.2327 0.0452  -0.0038 -0.0326 51  GLY A CA  
382  C  C   . GLY A 51  ? 0.2828 0.2227 0.2272 0.0391  0.0050  -0.0314 51  GLY A C   
383  O  O   . GLY A 51  ? 0.3314 0.2195 0.2489 0.0344  -0.0165 -0.0278 51  GLY A O   
384  N  N   . SER A 52  ? 0.2177 0.2174 0.2053 0.0211  0.0279  -0.0159 52  SER A N   
385  C  CA  . SER A 52  ? 0.2085 0.2180 0.2001 -0.0008 0.0352  -0.0303 52  SER A CA  
386  C  C   . SER A 52  ? 0.2083 0.2342 0.2198 -0.0252 0.0493  -0.0540 52  SER A C   
387  O  O   . SER A 52  ? 0.2029 0.2149 0.2069 -0.0198 0.0353  -0.0469 52  SER A O   
388  C  CB  . SER A 52  ? 0.2394 0.2138 0.2000 -0.0021 0.0338  -0.0153 52  SER A CB  
389  O  OG  . SER A 52  ? 0.2567 0.2212 0.2163 0.0238  0.0340  -0.0220 52  SER A OG  
390  N  N   A SER A 53  ? 0.2227 0.2637 0.2431 -0.0250 0.0551  -0.0714 53  SER A N   
391  N  N   B SER A 53  ? 0.2057 0.2686 0.2427 -0.0250 0.0670  -0.0822 53  SER A N   
392  C  CA  A SER A 53  ? 0.2337 0.2829 0.2616 -0.0255 0.0564  -0.0819 53  SER A CA  
393  C  CA  B SER A 53  ? 0.2093 0.2838 0.2584 -0.0311 0.0677  -0.0922 53  SER A CA  
394  C  C   A SER A 53  ? 0.2238 0.2859 0.2569 -0.0310 0.0588  -0.0933 53  SER A C   
395  C  C   B SER A 53  ? 0.2090 0.2734 0.2595 -0.0404 0.0658  -0.1045 53  SER A C   
396  O  O   A SER A 53  ? 0.2287 0.2880 0.2687 -0.0238 0.0557  -0.0995 53  SER A O   
397  O  O   B SER A 53  ? 0.2092 0.2603 0.2803 -0.0255 0.0643  -0.1209 53  SER A O   
398  C  CB  A SER A 53  ? 0.2565 0.2930 0.2802 -0.0231 0.0546  -0.0752 53  SER A CB  
399  C  CB  B SER A 53  ? 0.2247 0.3042 0.2673 -0.0321 0.0618  -0.0790 53  SER A CB  
400  O  OG  A SER A 53  ? 0.2649 0.2944 0.2924 -0.0228 0.0551  -0.0725 53  SER A OG  
401  O  OG  B SER A 53  ? 0.2102 0.3126 0.2705 -0.0268 0.0607  -0.0808 53  SER A OG  
402  N  N   . GLU A 54  ? 0.2097 0.2883 0.2390 -0.0358 0.0670  -0.0955 54  GLU A N   
403  C  CA  . GLU A 54  ? 0.2274 0.3148 0.2237 -0.0506 0.0677  -0.0889 54  GLU A CA  
404  C  C   . GLU A 54  ? 0.2165 0.2852 0.2024 -0.0460 0.0586  -0.0903 54  GLU A C   
405  O  O   . GLU A 54  ? 0.2178 0.2660 0.2013 -0.0364 0.0625  -0.0750 54  GLU A O   
406  C  CB  . GLU A 54  ? 0.2529 0.3500 0.2304 -0.0444 0.0683  -0.0913 54  GLU A CB  
407  C  CG  . GLU A 54  ? 0.2628 0.3577 0.2503 -0.0148 0.0532  -0.0853 54  GLU A CG  
408  C  CD  . GLU A 54  ? 0.2667 0.3502 0.2681 -0.0106 0.0430  -0.0790 54  GLU A CD  
409  O  OE1 . GLU A 54  ? 0.2631 0.3398 0.2885 0.0095  0.0484  -0.0767 54  GLU A OE1 
410  O  OE2 . GLU A 54  ? 0.2656 0.3373 0.2655 -0.0159 0.0336  -0.0782 54  GLU A OE2 
411  N  N   . PRO A 55  ? 0.2254 0.2944 0.1972 -0.0360 0.0373  -0.0845 55  PRO A N   
412  C  CA  . PRO A 55  ? 0.2143 0.2734 0.1916 -0.0138 0.0368  -0.0765 55  PRO A CA  
413  C  C   . PRO A 55  ? 0.1820 0.2363 0.1866 -0.0180 0.0316  -0.0515 55  PRO A C   
414  O  O   . PRO A 55  ? 0.1815 0.2296 0.1854 -0.0205 0.0387  -0.0486 55  PRO A O   
415  C  CB  . PRO A 55  ? 0.2322 0.3105 0.1855 -0.0229 0.0296  -0.0703 55  PRO A CB  
416  C  CG  . PRO A 55  ? 0.2333 0.3345 0.1926 -0.0282 0.0317  -0.0710 55  PRO A CG  
417  C  CD  . PRO A 55  ? 0.2327 0.3256 0.1934 -0.0309 0.0319  -0.0743 55  PRO A CD  
418  N  N   . CYS A 56  ? 0.1731 0.2198 0.1790 -0.0157 0.0260  -0.0502 56  CYS A N   
419  C  CA  . CYS A 56  ? 0.1607 0.2102 0.1785 0.0008  0.0216  -0.0410 56  CYS A CA  
420  C  C   . CYS A 56  ? 0.1639 0.2056 0.1740 -0.0022 0.0286  -0.0319 56  CYS A C   
421  O  O   . CYS A 56  ? 0.1604 0.1963 0.1714 -0.0157 0.0349  -0.0240 56  CYS A O   
422  C  CB  . CYS A 56  ? 0.1649 0.1801 0.2079 -0.0182 0.0173  -0.0290 56  CYS A CB  
423  S  SG  . CYS A 56  ? 0.1809 0.1885 0.2512 -0.0149 0.0215  -0.0089 56  CYS A SG  
424  N  N   . ALA A 57  ? 0.1671 0.1890 0.1560 0.0023  0.0283  -0.0312 57  ALA A N   
425  C  CA  . ALA A 57  ? 0.1601 0.1785 0.1592 -0.0037 0.0203  -0.0252 57  ALA A CA  
426  C  C   . ALA A 57  ? 0.1515 0.1643 0.1637 -0.0204 0.0240  -0.0269 57  ALA A C   
427  O  O   . ALA A 57  ? 0.1511 0.1751 0.1782 -0.0256 0.0307  -0.0295 57  ALA A O   
428  C  CB  . ALA A 57  ? 0.1670 0.1900 0.1718 0.0262  0.0105  -0.0223 57  ALA A CB  
429  N  N   . LEU A 58  ? 0.1487 0.1620 0.1555 -0.0007 0.0214  -0.0264 58  LEU A N   
430  C  CA  . LEU A 58  ? 0.1424 0.1589 0.1725 0.0091  0.0174  -0.0125 58  LEU A CA  
431  C  C   . LEU A 58  ? 0.1360 0.1517 0.1720 -0.0112 0.0252  -0.0053 58  LEU A C   
432  O  O   . LEU A 58  ? 0.1316 0.1644 0.1809 -0.0110 0.0243  -0.0215 58  LEU A O   
433  C  CB  . LEU A 58  ? 0.1489 0.1622 0.2090 0.0037  0.0307  -0.0145 58  LEU A CB  
434  C  CG  . LEU A 58  ? 0.1455 0.1806 0.2667 0.0182  0.0399  -0.0101 58  LEU A CG  
435  C  CD1 . LEU A 58  ? 0.1755 0.1993 0.2960 0.0251  0.0440  0.0010  58  LEU A CD1 
436  C  CD2 . LEU A 58  ? 0.1435 0.2228 0.2860 0.0172  0.0291  -0.0068 58  LEU A CD2 
437  N  N   . CYS A 59  ? 0.1342 0.1538 0.1718 0.0015  0.0210  -0.0158 59  CYS A N   
438  C  CA  . CYS A 59  ? 0.1413 0.1551 0.1687 0.0076  0.0222  -0.0106 59  CYS A CA  
439  C  C   . CYS A 59  ? 0.1272 0.1423 0.1670 -0.0030 0.0265  -0.0151 59  CYS A C   
440  O  O   . CYS A 59  ? 0.1273 0.1536 0.1755 -0.0010 0.0189  -0.0114 59  CYS A O   
441  C  CB  . CYS A 59  ? 0.1555 0.1688 0.1612 0.0163  0.0177  -0.0110 59  CYS A CB  
442  S  SG  . CYS A 59  ? 0.1834 0.1953 0.1597 0.0068  0.0128  0.0034  59  CYS A SG  
443  N  N   . SER A 60  ? 0.1420 0.1495 0.1605 -0.0043 0.0167  -0.0212 60  SER A N   
444  C  CA  . SER A 60  ? 0.1464 0.1548 0.1647 0.0143  0.0139  -0.0119 60  SER A CA  
445  C  C   . SER A 60  ? 0.1323 0.1421 0.1603 0.0010  0.0174  0.0033  60  SER A C   
446  O  O   . SER A 60  ? 0.1200 0.1551 0.1753 -0.0014 0.0012  -0.0137 60  SER A O   
447  C  CB  . SER A 60  ? 0.1656 0.1786 0.1837 0.0185  0.0239  0.0032  60  SER A CB  
448  O  OG  . SER A 60  ? 0.1875 0.1828 0.1977 0.0339  0.0315  0.0180  60  SER A OG  
449  N  N   . LEU A 61  ? 0.1575 0.1440 0.1516 0.0129  0.0161  -0.0114 61  LEU A N   
450  C  CA  . LEU A 61  ? 0.1533 0.1426 0.1595 0.0010  0.0073  -0.0093 61  LEU A CA  
451  C  C   . LEU A 61  ? 0.1390 0.1544 0.1566 -0.0152 0.0177  -0.0170 61  LEU A C   
452  O  O   . LEU A 61  ? 0.1569 0.1718 0.1570 -0.0076 0.0243  -0.0151 61  LEU A O   
453  C  CB  . LEU A 61  ? 0.1839 0.1475 0.1812 0.0124  0.0166  -0.0006 61  LEU A CB  
454  C  CG  . LEU A 61  ? 0.1696 0.1429 0.2072 0.0140  0.0271  0.0115  61  LEU A CG  
455  C  CD1 . LEU A 61  ? 0.1628 0.1769 0.2226 0.0078  0.0236  0.0168  61  LEU A CD1 
456  C  CD2 . LEU A 61  ? 0.2011 0.1458 0.2195 0.0025  0.0426  0.0118  61  LEU A CD2 
457  N  N   . HIS A 62  ? 0.1295 0.1672 0.1485 0.0082  0.0170  -0.0134 62  HIS A N   
458  C  CA  . HIS A 62  ? 0.1366 0.1631 0.1562 0.0186  0.0259  -0.0114 62  HIS A CA  
459  C  C   . HIS A 62  ? 0.1303 0.1556 0.1595 0.0226  0.0167  -0.0150 62  HIS A C   
460  O  O   . HIS A 62  ? 0.1370 0.1657 0.1790 0.0272  0.0039  -0.0222 62  HIS A O   
461  C  CB  . HIS A 62  ? 0.1570 0.1638 0.1764 0.0007  0.0235  0.0080  62  HIS A CB  
462  C  CG  . HIS A 62  ? 0.1675 0.1605 0.1746 -0.0036 0.0197  0.0211  62  HIS A CG  
463  N  ND1 . HIS A 62  ? 0.2095 0.1695 0.2031 0.0073  0.0235  0.0214  62  HIS A ND1 
464  C  CD2 . HIS A 62  ? 0.1745 0.1650 0.1937 0.0004  0.0131  0.0234  62  HIS A CD2 
465  C  CE1 . HIS A 62  ? 0.2024 0.1631 0.2073 0.0088  0.0317  0.0237  62  HIS A CE1 
466  N  NE2 . HIS A 62  ? 0.2005 0.1716 0.2123 -0.0095 0.0260  0.0154  62  HIS A NE2 
467  N  N   . SER A 63  ? 0.1553 0.1532 0.1568 0.0192  0.0202  -0.0145 63  SER A N   
468  C  CA  . SER A 63  ? 0.1747 0.1597 0.1611 0.0219  0.0133  -0.0117 63  SER A CA  
469  C  C   . SER A 63  ? 0.1605 0.1562 0.1587 0.0005  0.0179  -0.0163 63  SER A C   
470  O  O   . SER A 63  ? 0.1487 0.1673 0.1634 0.0164  0.0216  -0.0067 63  SER A O   
471  C  CB  . SER A 63  ? 0.2121 0.1684 0.1780 0.0274  0.0121  0.0028  63  SER A CB  
472  O  OG  . SER A 63  ? 0.2255 0.1616 0.1989 0.0275  -0.0001 0.0002  63  SER A OG  
473  N  N   . ILE A 64  ? 0.1702 0.1667 0.1552 0.0152  0.0132  -0.0216 64  ILE A N   
474  C  CA  . ILE A 64  ? 0.1816 0.1681 0.1707 0.0097  0.0327  -0.0178 64  ILE A CA  
475  C  C   . ILE A 64  ? 0.2149 0.1697 0.1760 0.0097  0.0316  -0.0153 64  ILE A C   
476  O  O   . ILE A 64  ? 0.2252 0.1735 0.1847 0.0105  0.0191  -0.0223 64  ILE A O   
477  C  CB  . ILE A 64  ? 0.1782 0.1690 0.1840 0.0152  0.0432  -0.0103 64  ILE A CB  
478  C  CG1 . ILE A 64  ? 0.1603 0.1624 0.1987 0.0221  0.0446  0.0031  64  ILE A CG1 
479  C  CG2 . ILE A 64  ? 0.1906 0.1813 0.1805 0.0101  0.0385  -0.0196 64  ILE A CG2 
480  C  CD1 . ILE A 64  ? 0.1638 0.1678 0.2155 0.0080  0.0462  0.0155  64  ILE A CD1 
481  N  N   . GLY A 65  ? 0.2346 0.1549 0.1691 -0.0018 0.0403  -0.0082 65  GLY A N   
482  C  CA  . GLY A 65  ? 0.2560 0.1577 0.1702 -0.0089 0.0348  0.0083  65  GLY A CA  
483  C  C   . GLY A 65  ? 0.2326 0.1557 0.1751 0.0005  0.0348  0.0003  65  GLY A C   
484  O  O   . GLY A 65  ? 0.2207 0.1665 0.1849 0.0025  0.0367  -0.0218 65  GLY A O   
485  N  N   . LYS A 66  ? 0.2378 0.1569 0.1764 -0.0025 0.0403  0.0096  66  LYS A N   
486  C  CA  . LYS A 66  ? 0.2341 0.1548 0.1832 0.0022  0.0343  -0.0049 66  LYS A CA  
487  C  C   . LYS A 66  ? 0.2469 0.1540 0.1904 0.0013  0.0193  -0.0134 66  LYS A C   
488  O  O   . LYS A 66  ? 0.2687 0.1763 0.1888 0.0089  0.0034  -0.0246 66  LYS A O   
489  C  CB  . LYS A 66  ? 0.2506 0.1805 0.2042 0.0065  0.0437  -0.0165 66  LYS A CB  
490  C  CG  . LYS A 66  ? 0.2848 0.2000 0.2387 0.0193  0.0471  -0.0239 66  LYS A CG  
491  C  CD  . LYS A 66  ? 0.3277 0.2282 0.2873 0.0245  0.0375  -0.0183 66  LYS A CD  
492  C  CE  . LYS A 66  ? 0.3718 0.2463 0.3318 0.0190  0.0230  -0.0149 66  LYS A CE  
493  N  NZ  . LYS A 66  ? 0.4055 0.2627 0.3635 0.0132  0.0140  -0.0068 66  LYS A NZ  
494  N  N   . ILE A 67  ? 0.2267 0.1554 0.1919 -0.0048 0.0184  -0.0080 67  ILE A N   
495  C  CA  . ILE A 67  ? 0.2264 0.1750 0.1827 -0.0028 0.0216  -0.0124 67  ILE A CA  
496  C  C   . ILE A 67  ? 0.2425 0.1983 0.1888 -0.0141 0.0296  -0.0144 67  ILE A C   
497  O  O   . ILE A 67  ? 0.2529 0.2143 0.1988 -0.0265 0.0296  -0.0234 67  ILE A O   
498  C  CB  . ILE A 67  ? 0.2206 0.1868 0.1866 0.0058  0.0263  -0.0157 67  ILE A CB  
499  C  CG1 . ILE A 67  ? 0.2163 0.1919 0.1874 0.0047  0.0339  -0.0150 67  ILE A CG1 
500  C  CG2 . ILE A 67  ? 0.2245 0.2091 0.1952 0.0241  0.0300  -0.0001 67  ILE A CG2 
501  C  CD1 . ILE A 67  ? 0.2042 0.2100 0.1882 0.0123  0.0309  -0.0001 67  ILE A CD1 
502  N  N   . GLY A 68  ? 0.2304 0.1837 0.1909 -0.0181 0.0328  -0.0091 68  GLY A N   
503  C  CA  . GLY A 68  ? 0.2290 0.2012 0.2000 -0.0252 0.0458  -0.0082 68  GLY A CA  
504  C  C   . GLY A 68  ? 0.2216 0.1960 0.2019 -0.0293 0.0389  -0.0029 68  GLY A C   
505  O  O   . GLY A 68  ? 0.2194 0.1890 0.1972 -0.0344 0.0218  -0.0047 68  GLY A O   
506  N  N   . GLY A 69  ? 0.2191 0.2141 0.2123 -0.0246 0.0365  -0.0140 69  GLY A N   
507  C  CA  . GLY A 69  ? 0.2259 0.2237 0.2168 -0.0174 0.0331  -0.0067 69  GLY A CA  
508  C  C   . GLY A 69  ? 0.2252 0.2016 0.2222 -0.0331 0.0310  -0.0103 69  GLY A C   
509  O  O   . GLY A 69  ? 0.2240 0.1842 0.2130 -0.0350 0.0321  -0.0144 69  GLY A O   
510  N  N   . ALA A 70  ? 0.2538 0.1894 0.2439 -0.0308 0.0385  0.0017  70  ALA A N   
511  C  CA  . ALA A 70  ? 0.2875 0.1744 0.2576 -0.0345 0.0277  0.0036  70  ALA A CA  
512  C  C   . ALA A 70  ? 0.2799 0.1630 0.2337 -0.0166 0.0412  0.0029  70  ALA A C   
513  O  O   . ALA A 70  ? 0.2822 0.1573 0.2253 -0.0112 0.0391  0.0092  70  ALA A O   
514  C  CB  . ALA A 70  ? 0.2964 0.1544 0.2837 -0.0406 0.0115  -0.0041 70  ALA A CB  
515  N  N   . GLN A 71  ? 0.2553 0.1577 0.2261 -0.0042 0.0552  0.0067  71  GLN A N   
516  C  CA  . GLN A 71  ? 0.2474 0.1513 0.2124 -0.0032 0.0503  -0.0014 71  GLN A CA  
517  C  C   . GLN A 71  ? 0.2261 0.1427 0.2034 -0.0023 0.0356  0.0014  71  GLN A C   
518  O  O   . GLN A 71  ? 0.2269 0.1525 0.2035 -0.0044 0.0226  0.0146  71  GLN A O   
519  C  CB  . GLN A 71  ? 0.2673 0.1586 0.2214 -0.0035 0.0599  -0.0122 71  GLN A CB  
520  C  CG  . GLN A 71  ? 0.2846 0.1725 0.2338 -0.0123 0.0643  -0.0277 71  GLN A CG  
521  C  CD  . GLN A 71  ? 0.2897 0.2021 0.2481 -0.0223 0.0571  -0.0258 71  GLN A CD  
522  O  OE1 . GLN A 71  ? 0.2964 0.2348 0.2575 -0.0192 0.0631  -0.0182 71  GLN A OE1 
523  N  NE2 . GLN A 71  ? 0.2920 0.2122 0.2597 -0.0195 0.0443  -0.0258 71  GLN A NE2 
524  N  N   . ASN A 72  ? 0.2138 0.1466 0.1976 0.0041  0.0439  0.0016  72  ASN A N   
525  C  CA  . ASN A 72  ? 0.2005 0.1467 0.1859 0.0028  0.0395  -0.0002 72  ASN A CA  
526  C  C   . ASN A 72  ? 0.2080 0.1504 0.1796 -0.0187 0.0305  -0.0007 72  ASN A C   
527  O  O   . ASN A 72  ? 0.2289 0.1541 0.1792 -0.0232 0.0133  0.0010  72  ASN A O   
528  C  CB  . ASN A 72  ? 0.1962 0.1628 0.1817 0.0151  0.0305  0.0075  72  ASN A CB  
529  C  CG  . ASN A 72  ? 0.1903 0.1416 0.1866 0.0122  0.0315  -0.0027 72  ASN A CG  
530  O  OD1 . ASN A 72  ? 0.1873 0.1456 0.1893 0.0092  0.0165  -0.0009 72  ASN A OD1 
531  N  ND2 . ASN A 72  ? 0.1991 0.1308 0.1923 -0.0146 0.0139  0.0049  72  ASN A ND2 
532  N  N   . ARG A 73  ? 0.2049 0.1748 0.1877 -0.0227 0.0426  0.0053  73  ARG A N   
533  C  CA  . ARG A 73  ? 0.2244 0.1792 0.2060 -0.0270 0.0439  0.0098  73  ARG A CA  
534  C  C   . ARG A 73  ? 0.2300 0.1813 0.1979 -0.0094 0.0302  0.0157  73  ARG A C   
535  O  O   . ARG A 73  ? 0.2388 0.1925 0.1997 -0.0119 0.0400  0.0198  73  ARG A O   
536  C  CB  . ARG A 73  ? 0.2226 0.1979 0.2454 -0.0305 0.0519  0.0140  73  ARG A CB  
537  C  CG  . ARG A 73  ? 0.2393 0.2206 0.2838 -0.0417 0.0623  0.0269  73  ARG A CG  
538  C  CD  . ARG A 73  ? 0.2865 0.2684 0.3242 -0.0505 0.0673  0.0285  73  ARG A CD  
539  N  NE  . ARG A 73  ? 0.3187 0.3061 0.3557 -0.0601 0.0641  0.0218  73  ARG A NE  
540  C  CZ  . ARG A 73  ? 0.3385 0.3213 0.3819 -0.0496 0.0692  0.0061  73  ARG A CZ  
541  N  NH1 . ARG A 73  ? 0.3415 0.3204 0.3926 -0.0224 0.0690  -0.0089 73  ARG A NH1 
542  N  NH2 . ARG A 73  ? 0.3402 0.3272 0.3904 -0.0655 0.0855  0.0021  73  ARG A NH2 
543  N  N   . SER A 74  ? 0.2161 0.1861 0.1951 -0.0046 0.0170  0.0156  74  SER A N   
544  C  CA  . SER A 74  ? 0.2340 0.1920 0.1990 0.0054  0.0325  -0.0008 74  SER A CA  
545  C  C   . SER A 74  ? 0.2413 0.1696 0.1865 0.0044  0.0316  0.0082  74  SER A C   
546  O  O   . SER A 74  ? 0.2547 0.1604 0.1881 -0.0015 0.0175  0.0090  74  SER A O   
547  C  CB  . SER A 74  ? 0.2745 0.2223 0.2371 0.0130  0.0272  -0.0165 74  SER A CB  
548  O  OG  . SER A 74  ? 0.3116 0.2506 0.2688 0.0133  0.0205  -0.0218 74  SER A OG  
549  N  N   . TYR A 75  ? 0.2305 0.1537 0.1780 0.0031  0.0408  0.0157  75  TYR A N   
550  C  CA  . TYR A 75  ? 0.2192 0.1530 0.1781 -0.0066 0.0262  0.0187  75  TYR A CA  
551  C  C   . TYR A 75  ? 0.2067 0.1635 0.1700 0.0043  0.0233  0.0100  75  TYR A C   
552  O  O   . TYR A 75  ? 0.1992 0.1825 0.1738 0.0126  0.0127  0.0106  75  TYR A O   
553  C  CB  . TYR A 75  ? 0.2121 0.1711 0.1753 0.0010  0.0343  0.0136  75  TYR A CB  
554  C  CG  . TYR A 75  ? 0.2181 0.1855 0.1811 0.0068  0.0323  -0.0081 75  TYR A CG  
555  C  CD1 . TYR A 75  ? 0.2345 0.2429 0.1961 0.0386  0.0268  -0.0384 75  TYR A CD1 
556  C  CD2 . TYR A 75  ? 0.2233 0.1750 0.1782 -0.0040 0.0321  -0.0192 75  TYR A CD2 
557  C  CE1 . TYR A 75  ? 0.2475 0.2771 0.1973 0.0588  0.0216  -0.0416 75  TYR A CE1 
558  C  CE2 . TYR A 75  ? 0.2100 0.1951 0.1806 0.0032  0.0405  -0.0323 75  TYR A CE2 
559  C  CZ  . TYR A 75  ? 0.2349 0.2553 0.1893 0.0475  0.0196  -0.0453 75  TYR A CZ  
560  O  OH  . TYR A 75  ? 0.2513 0.2968 0.1994 0.0816  -0.0000 -0.0550 75  TYR A OH  
561  N  N   . SER A 76  ? 0.2094 0.1623 0.1769 0.0100  0.0317  0.0090  76  SER A N   
562  C  CA  . SER A 76  ? 0.1900 0.1777 0.1749 0.0070  0.0332  0.0140  76  SER A CA  
563  C  C   . SER A 76  ? 0.1881 0.1705 0.1792 -0.0057 0.0339  0.0169  76  SER A C   
564  O  O   . SER A 76  ? 0.1928 0.1649 0.1936 -0.0122 0.0392  -0.0142 76  SER A O   
565  C  CB  . SER A 76  ? 0.1901 0.2027 0.1798 -0.0031 0.0284  0.0248  76  SER A CB  
566  O  OG  . SER A 76  ? 0.2049 0.2140 0.1940 -0.0140 0.0204  0.0524  76  SER A OG  
567  N  N   . LYS A 77  ? 0.2065 0.1712 0.1759 -0.0089 0.0326  0.0333  77  LYS A N   
568  C  CA  . LYS A 77  ? 0.2463 0.1870 0.1917 -0.0094 0.0231  0.0364  77  LYS A CA  
569  C  C   . LYS A 77  ? 0.2437 0.1964 0.1847 -0.0046 0.0206  0.0291  77  LYS A C   
570  O  O   . LYS A 77  ? 0.2473 0.2118 0.1865 -0.0013 0.0135  0.0319  77  LYS A O   
571  C  CB  . LYS A 77  ? 0.2897 0.1847 0.2131 -0.0084 0.0171  0.0563  77  LYS A CB  
572  C  CG  . LYS A 77  ? 0.3506 0.1935 0.2424 -0.0109 0.0237  0.0667  77  LYS A CG  
573  C  CD  . LYS A 77  ? 0.4037 0.2244 0.2764 -0.0075 0.0229  0.0817  77  LYS A CD  
574  C  CE  . LYS A 77  ? 0.4457 0.2690 0.3108 -0.0092 0.0211  0.0867  77  LYS A CE  
575  N  NZ  . LYS A 77  ? 0.4803 0.3006 0.3396 -0.0143 0.0188  0.0833  77  LYS A NZ  
576  N  N   . LEU A 78  ? 0.2258 0.1875 0.1726 0.0009  0.0223  0.0197  78  LEU A N   
577  C  CA  . LEU A 78  ? 0.2368 0.2041 0.1772 0.0210  0.0192  0.0039  78  LEU A CA  
578  C  C   . LEU A 78  ? 0.2229 0.1952 0.1693 0.0114  0.0120  0.0140  78  LEU A C   
579  O  O   . LEU A 78  ? 0.2126 0.1998 0.1731 0.0218  0.0029  0.0122  78  LEU A O   
580  C  CB  . LEU A 78  ? 0.2480 0.2289 0.1888 0.0320  0.0298  -0.0057 78  LEU A CB  
581  C  CG  . LEU A 78  ? 0.2649 0.2646 0.2058 0.0646  0.0364  -0.0051 78  LEU A CG  
582  C  CD1 . LEU A 78  ? 0.2892 0.2928 0.2161 0.0689  0.0423  0.0099  78  LEU A CD1 
583  C  CD2 . LEU A 78  ? 0.2690 0.2851 0.2056 0.0593  0.0446  -0.0083 78  LEU A CD2 
584  N  N   . LEU A 79  ? 0.2114 0.1760 0.1669 0.0002  0.0172  0.0229  79  LEU A N   
585  C  CA  . LEU A 79  ? 0.2097 0.1862 0.1621 -0.0036 0.0082  0.0124  79  LEU A CA  
586  C  C   . LEU A 79  ? 0.1919 0.1978 0.1772 -0.0032 0.0125  -0.0028 79  LEU A C   
587  O  O   . LEU A 79  ? 0.2020 0.1909 0.1706 -0.0111 0.0160  -0.0095 79  LEU A O   
588  C  CB  . LEU A 79  ? 0.2120 0.2214 0.1571 -0.0045 0.0159  0.0077  79  LEU A CB  
589  C  CG  . LEU A 79  ? 0.1941 0.2620 0.1682 -0.0149 0.0210  0.0064  79  LEU A CG  
590  C  CD1 . LEU A 79  ? 0.2083 0.2740 0.1564 -0.0282 0.0046  0.0181  79  LEU A CD1 
591  C  CD2 . LEU A 79  ? 0.1886 0.2783 0.1954 -0.0151 0.0191  0.0048  79  LEU A CD2 
592  N  N   . CYS A 80  ? 0.1746 0.2069 0.1796 0.0006  0.0207  -0.0048 80  CYS A N   
593  C  CA  . CYS A 80  ? 0.1790 0.2131 0.1828 0.0063  0.0195  -0.0076 80  CYS A CA  
594  C  C   . CYS A 80  ? 0.1817 0.2052 0.1841 0.0045  0.0198  -0.0026 80  CYS A C   
595  O  O   . CYS A 80  ? 0.2044 0.2047 0.1860 0.0031  0.0052  -0.0090 80  CYS A O   
596  C  CB  . CYS A 80  ? 0.1929 0.2180 0.1894 -0.0007 0.0208  -0.0060 80  CYS A CB  
597  S  SG  . CYS A 80  ? 0.2005 0.1923 0.2097 -0.0015 0.0195  -0.0021 80  CYS A SG  
598  N  N   . GLY A 81  ? 0.1926 0.2238 0.1845 0.0000  0.0308  0.0084  81  GLY A N   
599  C  CA  . GLY A 81  ? 0.2078 0.2376 0.1874 0.0045  0.0109  0.0247  81  GLY A CA  
600  C  C   . GLY A 81  ? 0.2117 0.2290 0.1783 0.0197  -0.0014 0.0225  81  GLY A C   
601  O  O   . GLY A 81  ? 0.2201 0.2500 0.1812 0.0196  -0.0075 0.0148  81  GLY A O   
602  N  N   . LEU A 82  ? 0.2094 0.2223 0.1742 0.0281  0.0132  0.0156  82  LEU A N   
603  C  CA  . LEU A 82  ? 0.2215 0.2287 0.1743 0.0323  0.0146  0.0005  82  LEU A CA  
604  C  C   . LEU A 82  ? 0.2071 0.2218 0.1648 0.0248  -0.0108 0.0065  82  LEU A C   
605  O  O   . LEU A 82  ? 0.1982 0.2488 0.1664 0.0185  -0.0023 0.0031  82  LEU A O   
606  C  CB  . LEU A 82  ? 0.2449 0.2540 0.1942 0.0555  0.0323  0.0005  82  LEU A CB  
607  C  CG  . LEU A 82  ? 0.2716 0.2933 0.2218 0.0576  0.0331  -0.0002 82  LEU A CG  
608  C  CD1 . LEU A 82  ? 0.2880 0.3042 0.2254 0.0517  0.0585  -0.0059 82  LEU A CD1 
609  C  CD2 . LEU A 82  ? 0.2811 0.3155 0.2443 0.0638  0.0073  -0.0005 82  LEU A CD2 
610  N  N   . LEU A 83  ? 0.1929 0.2153 0.1619 0.0167  -0.0050 0.0069  83  LEU A N   
611  C  CA  . LEU A 83  ? 0.2002 0.2153 0.1540 0.0096  -0.0059 0.0039  83  LEU A CA  
612  C  C   . LEU A 83  ? 0.2106 0.2163 0.1631 -0.0043 0.0035  0.0025  83  LEU A C   
613  O  O   . LEU A 83  ? 0.2095 0.2124 0.1725 -0.0166 0.0066  0.0051  83  LEU A O   
614  C  CB  . LEU A 83  ? 0.1963 0.2298 0.1524 0.0137  -0.0023 0.0092  83  LEU A CB  
615  C  CG  . LEU A 83  ? 0.2027 0.2431 0.1696 0.0046  -0.0010 0.0015  83  LEU A CG  
616  C  CD1 . LEU A 83  ? 0.2054 0.2634 0.1722 0.0329  -0.0020 0.0067  83  LEU A CD1 
617  C  CD2 . LEU A 83  ? 0.2132 0.2620 0.2063 -0.0095 0.0106  0.0086  83  LEU A CD2 
618  N  N   . ALA A 84  ? 0.2140 0.2181 0.1545 -0.0041 0.0155  0.0065  84  ALA A N   
619  C  CA  . ALA A 84  ? 0.2263 0.2488 0.1551 -0.0106 0.0234  0.0101  84  ALA A CA  
620  C  C   . ALA A 84  ? 0.2478 0.2733 0.1541 0.0034  0.0067  0.0102  84  ALA A C   
621  O  O   . ALA A 84  ? 0.2700 0.2945 0.1578 0.0115  -0.0011 0.0043  84  ALA A O   
622  C  CB  . ALA A 84  ? 0.2321 0.2557 0.1719 -0.0188 0.0331  0.0071  84  ALA A CB  
623  N  N   . GLU A 85  ? 0.2529 0.2771 0.1606 0.0172  0.0074  0.0188  85  GLU A N   
624  C  CA  . GLU A 85  ? 0.2661 0.3101 0.2073 0.0449  -0.0154 0.0210  85  GLU A CA  
625  C  C   . GLU A 85  ? 0.2294 0.3121 0.1969 0.0292  -0.0252 0.0062  85  GLU A C   
626  O  O   . GLU A 85  ? 0.2387 0.3320 0.2020 0.0227  -0.0341 0.0144  85  GLU A O   
627  C  CB  . GLU A 85  ? 0.3102 0.3501 0.2695 0.0835  -0.0380 0.0304  85  GLU A CB  
628  C  CG  . GLU A 85  ? 0.3861 0.4081 0.3301 0.0854  -0.0461 0.0409  85  GLU A CG  
629  C  CD  . GLU A 85  ? 0.4590 0.4664 0.3794 0.0811  -0.0505 0.0546  85  GLU A CD  
630  O  OE1 . GLU A 85  ? 0.4931 0.4909 0.3992 0.0675  -0.0463 0.0599  85  GLU A OE1 
631  O  OE2 . GLU A 85  ? 0.4785 0.4828 0.3992 0.0837  -0.0545 0.0580  85  GLU A OE2 
632  N  N   . ARG A 86  ? 0.1978 0.2935 0.1938 0.0254  -0.0094 -0.0061 86  ARG A N   
633  C  CA  . ARG A 86  ? 0.1973 0.2871 0.2056 0.0200  -0.0055 -0.0074 86  ARG A CA  
634  C  C   . ARG A 86  ? 0.1936 0.2839 0.2182 0.0116  -0.0180 -0.0154 86  ARG A C   
635  O  O   . ARG A 86  ? 0.2179 0.2986 0.2354 0.0055  -0.0301 -0.0297 86  ARG A O   
636  C  CB  . ARG A 86  ? 0.2408 0.2972 0.2153 0.0395  0.0011  0.0085  86  ARG A CB  
637  C  CG  . ARG A 86  ? 0.2793 0.3167 0.2394 0.0628  -0.0193 0.0196  86  ARG A CG  
638  C  CD  . ARG A 86  ? 0.3217 0.3436 0.2636 0.0934  -0.0159 0.0418  86  ARG A CD  
639  N  NE  . ARG A 86  ? 0.3528 0.3684 0.2868 0.1246  -0.0127 0.0476  86  ARG A NE  
640  C  CZ  . ARG A 86  ? 0.4054 0.3928 0.3103 0.1357  0.0006  0.0414  86  ARG A CZ  
641  N  NH1 . ARG A 86  ? 0.4274 0.4075 0.3156 0.1309  0.0041  0.0253  86  ARG A NH1 
642  N  NH2 . ARG A 86  ? 0.4203 0.3909 0.3290 0.1543  0.0027  0.0429  86  ARG A NH2 
643  N  N   . LEU A 87  ? 0.1834 0.2494 0.2133 0.0133  -0.0157 0.0076  87  LEU A N   
644  C  CA  . LEU A 87  ? 0.1930 0.2399 0.2107 0.0054  -0.0078 0.0086  87  LEU A CA  
645  C  C   . LEU A 87  ? 0.1936 0.2435 0.1974 -0.0054 -0.0047 -0.0048 87  LEU A C   
646  O  O   . LEU A 87  ? 0.2031 0.2495 0.2040 -0.0054 -0.0087 -0.0129 87  LEU A O   
647  C  CB  . LEU A 87  ? 0.1969 0.2439 0.2166 0.0121  -0.0049 0.0148  87  LEU A CB  
648  C  CG  . LEU A 87  ? 0.1822 0.2695 0.2329 0.0335  0.0002  0.0210  87  LEU A CG  
649  C  CD1 . LEU A 87  ? 0.1988 0.2571 0.2280 0.0419  0.0067  0.0275  87  LEU A CD1 
650  C  CD2 . LEU A 87  ? 0.1948 0.3003 0.2520 0.0167  -0.0028 0.0204  87  LEU A CD2 
651  N  N   . ARG A 88  ? 0.1987 0.2513 0.1867 -0.0032 -0.0058 -0.0134 88  ARG A N   
652  C  CA  . ARG A 88  ? 0.2251 0.2777 0.1942 -0.0053 0.0065  -0.0380 88  ARG A CA  
653  C  C   . ARG A 88  ? 0.2209 0.2515 0.1889 0.0051  0.0093  -0.0246 88  ARG A C   
654  O  O   . ARG A 88  ? 0.2531 0.2736 0.2024 0.0091  -0.0076 -0.0432 88  ARG A O   
655  C  CB  . ARG A 88  ? 0.2796 0.3331 0.2256 -0.0101 0.0038  -0.0601 88  ARG A CB  
656  C  CG  . ARG A 88  ? 0.3604 0.3962 0.2732 -0.0216 0.0027  -0.0600 88  ARG A CG  
657  C  CD  . ARG A 88  ? 0.4467 0.4546 0.3253 -0.0357 0.0198  -0.0477 88  ARG A CD  
658  N  NE  . ARG A 88  ? 0.5289 0.5053 0.3747 -0.0395 0.0366  -0.0356 88  ARG A NE  
659  C  CZ  . ARG A 88  ? 0.5868 0.5413 0.4080 -0.0367 0.0563  -0.0225 88  ARG A CZ  
660  N  NH1 . ARG A 88  ? 0.6040 0.5587 0.4224 -0.0411 0.0601  -0.0155 88  ARG A NH1 
661  N  NH2 . ARG A 88  ? 0.6046 0.5480 0.4142 -0.0294 0.0664  -0.0229 88  ARG A NH2 
662  N  N   . ILE A 89  ? 0.1971 0.2291 0.1790 -0.0011 0.0010  -0.0063 89  ILE A N   
663  C  CA  . ILE A 89  ? 0.1915 0.2345 0.1747 -0.0124 0.0078  -0.0048 89  ILE A CA  
664  C  C   . ILE A 89  ? 0.1979 0.2352 0.1773 -0.0150 0.0170  -0.0196 89  ILE A C   
665  O  O   . ILE A 89  ? 0.2128 0.2367 0.2017 -0.0032 0.0130  -0.0215 89  ILE A O   
666  C  CB  . ILE A 89  ? 0.1803 0.2191 0.1736 -0.0072 0.0054  -0.0043 89  ILE A CB  
667  C  CG1 . ILE A 89  ? 0.1852 0.2261 0.1672 -0.0088 0.0135  0.0035  89  ILE A CG1 
668  C  CG2 . ILE A 89  ? 0.1790 0.2163 0.1807 -0.0026 0.0059  -0.0135 89  ILE A CG2 
669  C  CD1 . ILE A 89  ? 0.2048 0.2049 0.1612 -0.0086 0.0209  -0.0126 89  ILE A CD1 
670  N  N   . SER A 90  ? 0.1827 0.2336 0.1740 -0.0197 0.0371  -0.0230 90  SER A N   
671  C  CA  . SER A 90  ? 0.2162 0.2393 0.1704 -0.0326 0.0559  -0.0336 90  SER A CA  
672  C  C   . SER A 90  ? 0.1890 0.2018 0.1644 -0.0169 0.0476  -0.0098 90  SER A C   
673  O  O   . SER A 90  ? 0.1746 0.1931 0.1701 -0.0137 0.0379  -0.0106 90  SER A O   
674  C  CB  . SER A 90  ? 0.2694 0.2925 0.1901 -0.0433 0.0605  -0.0611 90  SER A CB  
675  O  OG  . SER A 90  ? 0.3237 0.3485 0.2303 -0.0692 0.0361  -0.0566 90  SER A OG  
676  N  N   . PRO A 91  ? 0.1998 0.1947 0.1687 -0.0081 0.0285  -0.0032 91  PRO A N   
677  C  CA  . PRO A 91  ? 0.1968 0.1771 0.1786 -0.0032 0.0191  -0.0035 91  PRO A CA  
678  C  C   . PRO A 91  ? 0.1713 0.1823 0.1839 0.0002  0.0314  -0.0052 91  PRO A C   
679  O  O   . PRO A 91  ? 0.1649 0.1901 0.1782 -0.0127 0.0236  -0.0098 91  PRO A O   
680  C  CB  . PRO A 91  ? 0.2207 0.1714 0.1862 -0.0037 0.0035  0.0028  91  PRO A CB  
681  C  CG  . PRO A 91  ? 0.2451 0.1993 0.1828 -0.0011 0.0062  -0.0032 91  PRO A CG  
682  C  CD  . PRO A 91  ? 0.2439 0.1988 0.1752 0.0011  0.0059  0.0012  91  PRO A CD  
683  N  N   . ASP A 92  ? 0.1530 0.1828 0.1938 0.0080  0.0359  -0.0238 92  ASP A N   
684  C  CA  . ASP A 92  ? 0.1723 0.1835 0.2016 -0.0168 0.0486  -0.0275 92  ASP A CA  
685  C  C   . ASP A 92  ? 0.1787 0.1784 0.1858 -0.0198 0.0444  -0.0355 92  ASP A C   
686  O  O   . ASP A 92  ? 0.1745 0.1865 0.1870 -0.0147 0.0408  -0.0351 92  ASP A O   
687  C  CB  . ASP A 92  ? 0.2112 0.2120 0.2172 -0.0394 0.0821  -0.0243 92  ASP A CB  
688  C  CG  . ASP A 92  ? 0.2419 0.2523 0.2297 -0.0610 0.1092  -0.0288 92  ASP A CG  
689  O  OD1 . ASP A 92  ? 0.2516 0.2478 0.2243 -0.0539 0.0957  -0.0564 92  ASP A OD1 
690  O  OD2 . ASP A 92  ? 0.2892 0.2974 0.2526 -0.0668 0.1248  -0.0253 92  ASP A OD2 
691  N  N   . ARG A 93  ? 0.1745 0.1758 0.1698 -0.0203 0.0484  -0.0163 93  ARG A N   
692  C  CA  . ARG A 93  ? 0.1709 0.1806 0.1591 -0.0213 0.0460  -0.0249 93  ARG A CA  
693  C  C   . ARG A 93  ? 0.1630 0.1709 0.1550 -0.0217 0.0326  -0.0127 93  ARG A C   
694  O  O   . ARG A 93  ? 0.1723 0.1842 0.1683 -0.0234 0.0390  -0.0136 93  ARG A O   
695  C  CB  . ARG A 93  ? 0.1594 0.1990 0.1557 -0.0204 0.0458  -0.0431 93  ARG A CB  
696  C  CG  . ARG A 93  ? 0.1862 0.1844 0.1595 -0.0077 0.0530  -0.0386 93  ARG A CG  
697  C  CD  . ARG A 93  ? 0.1958 0.1836 0.1630 -0.0044 0.0478  -0.0360 93  ARG A CD  
698  N  NE  . ARG A 93  ? 0.1984 0.1819 0.1697 -0.0014 0.0519  -0.0331 93  ARG A NE  
699  C  CZ  . ARG A 93  ? 0.2042 0.1793 0.1745 -0.0015 0.0442  -0.0286 93  ARG A CZ  
700  N  NH1 . ARG A 93  ? 0.1933 0.1899 0.1849 0.0132  0.0381  -0.0401 93  ARG A NH1 
701  N  NH2 . ARG A 93  ? 0.2182 0.1892 0.1791 -0.0182 0.0414  -0.0180 93  ARG A NH2 
702  N  N   . VAL A 94  ? 0.1601 0.1764 0.1564 -0.0115 0.0374  -0.0166 94  VAL A N   
703  C  CA  . VAL A 94  ? 0.1660 0.1669 0.1540 -0.0125 0.0390  -0.0235 94  VAL A CA  
704  C  C   . VAL A 94  ? 0.1462 0.1679 0.1597 -0.0106 0.0406  -0.0180 94  VAL A C   
705  O  O   . VAL A 94  ? 0.1619 0.1719 0.1765 -0.0186 0.0382  -0.0228 94  VAL A O   
706  C  CB  . VAL A 94  ? 0.1748 0.1968 0.1532 0.0052  0.0226  -0.0275 94  VAL A CB  
707  C  CG1 . VAL A 94  ? 0.1848 0.2198 0.1532 0.0263  0.0408  -0.0158 94  VAL A CG1 
708  C  CG2 . VAL A 94  ? 0.1609 0.2229 0.1682 0.0106  0.0174  -0.0227 94  VAL A CG2 
709  N  N   . TYR A 95  ? 0.1430 0.1746 0.1639 0.0060  0.0253  -0.0159 95  TYR A N   
710  C  CA  . TYR A 95  ? 0.1431 0.1717 0.1628 0.0001  0.0287  -0.0145 95  TYR A CA  
711  C  C   . TYR A 95  ? 0.1518 0.1522 0.1592 -0.0110 0.0389  -0.0106 95  TYR A C   
712  O  O   . TYR A 95  ? 0.1663 0.1594 0.1694 -0.0136 0.0428  -0.0101 95  TYR A O   
713  C  CB  . TYR A 95  ? 0.1316 0.1716 0.1826 -0.0025 0.0227  -0.0099 95  TYR A CB  
714  C  CG  . TYR A 95  ? 0.1324 0.1677 0.1964 -0.0074 0.0258  -0.0103 95  TYR A CG  
715  C  CD1 . TYR A 95  ? 0.1351 0.1788 0.2158 0.0038  0.0304  -0.0019 95  TYR A CD1 
716  C  CD2 . TYR A 95  ? 0.1572 0.1771 0.1997 0.0079  0.0188  -0.0175 95  TYR A CD2 
717  C  CE1 . TYR A 95  ? 0.1379 0.1751 0.2246 0.0136  0.0240  -0.0125 95  TYR A CE1 
718  C  CE2 . TYR A 95  ? 0.1482 0.1814 0.2067 0.0058  0.0197  -0.0210 95  TYR A CE2 
719  C  CZ  . TYR A 95  ? 0.1368 0.1757 0.2208 0.0159  0.0245  -0.0119 95  TYR A CZ  
720  O  OH  . TYR A 95  ? 0.1428 0.1907 0.2454 0.0159  0.0285  -0.0168 95  TYR A OH  
721  N  N   . ILE A 96  ? 0.1713 0.1395 0.1506 0.0050  0.0259  -0.0144 96  ILE A N   
722  C  CA  . ILE A 96  ? 0.1738 0.1402 0.1418 0.0101  0.0127  -0.0140 96  ILE A CA  
723  C  C   . ILE A 96  ? 0.1642 0.1562 0.1457 -0.0087 0.0072  -0.0105 96  ILE A C   
724  O  O   . ILE A 96  ? 0.1635 0.1676 0.1612 -0.0309 0.0214  -0.0086 96  ILE A O   
725  C  CB  . ILE A 96  ? 0.1736 0.1551 0.1533 0.0039  0.0227  -0.0035 96  ILE A CB  
726  C  CG1 . ILE A 96  ? 0.1963 0.1641 0.1644 0.0197  0.0139  -0.0012 96  ILE A CG1 
727  C  CG2 . ILE A 96  ? 0.1646 0.1672 0.1631 0.0018  0.0390  -0.0101 96  ILE A CG2 
728  C  CD1 . ILE A 96  ? 0.2054 0.1929 0.1930 0.0313  0.0165  0.0021  96  ILE A CD1 
729  N  N   . ASN A 97  ? 0.1383 0.1519 0.1532 0.0096  0.0004  -0.0047 97  ASN A N   
730  C  CA  . ASN A 97  ? 0.1534 0.1472 0.1627 0.0095  0.0041  -0.0116 97  ASN A CA  
731  C  C   . ASN A 97  ? 0.1399 0.1563 0.1567 0.0054  0.0119  -0.0147 97  ASN A C   
732  O  O   . ASN A 97  ? 0.1298 0.1688 0.1742 0.0059  0.0094  -0.0179 97  ASN A O   
733  C  CB  . ASN A 97  ? 0.1651 0.1688 0.1816 0.0137  0.0163  0.0103  97  ASN A CB  
734  C  CG  . ASN A 97  ? 0.1866 0.1843 0.2079 0.0289  0.0244  0.0039  97  ASN A CG  
735  O  OD1 . ASN A 97  ? 0.1914 0.1976 0.2267 0.0349  0.0322  -0.0074 97  ASN A OD1 
736  N  ND2 . ASN A 97  ? 0.2139 0.1905 0.2228 0.0328  0.0298  0.0009  97  ASN A ND2 
737  N  N   . TYR A 98  ? 0.1628 0.1345 0.1496 0.0054  0.0190  -0.0007 98  TYR A N   
738  C  CA  . TYR A 98  ? 0.1695 0.1482 0.1513 -0.0049 0.0136  -0.0060 98  TYR A CA  
739  C  C   . TYR A 98  ? 0.1618 0.1434 0.1531 -0.0001 0.0098  0.0007  98  TYR A C   
740  O  O   . TYR A 98  ? 0.1402 0.1625 0.1616 -0.0020 -0.0018 -0.0051 98  TYR A O   
741  C  CB  . TYR A 98  ? 0.1782 0.1501 0.1574 -0.0179 0.0062  -0.0069 98  TYR A CB  
742  C  CG  . TYR A 98  ? 0.1811 0.1429 0.1542 -0.0097 0.0138  -0.0103 98  TYR A CG  
743  C  CD1 . TYR A 98  ? 0.1785 0.1394 0.1603 0.0100  0.0100  0.0054  98  TYR A CD1 
744  C  CD2 . TYR A 98  ? 0.1925 0.1394 0.1501 -0.0125 0.0191  -0.0147 98  TYR A CD2 
745  C  CE1 . TYR A 98  ? 0.1733 0.1338 0.1594 0.0030  0.0177  0.0098  98  TYR A CE1 
746  C  CE2 . TYR A 98  ? 0.1969 0.1189 0.1572 0.0004  0.0092  0.0047  98  TYR A CE2 
747  C  CZ  . TYR A 98  ? 0.1866 0.1330 0.1595 0.0005  0.0072  -0.0032 98  TYR A CZ  
748  O  OH  . TYR A 98  ? 0.1970 0.1522 0.1597 0.0047  0.0118  0.0054  98  TYR A OH  
749  N  N   . TYR A 99  ? 0.1650 0.1375 0.1445 0.0124  0.0144  -0.0044 99  TYR A N   
750  C  CA  . TYR A 99  ? 0.1716 0.1507 0.1514 0.0112  0.0186  -0.0118 99  TYR A CA  
751  C  C   . TYR A 99  ? 0.1551 0.1610 0.1538 0.0041  0.0133  -0.0167 99  TYR A C   
752  O  O   . TYR A 99  ? 0.1503 0.1649 0.1648 0.0040  0.0176  -0.0177 99  TYR A O   
753  C  CB  . TYR A 99  ? 0.1670 0.1427 0.1762 0.0156  0.0029  -0.0008 99  TYR A CB  
754  C  CG  . TYR A 99  ? 0.1620 0.1465 0.2041 0.0185  -0.0022 0.0016  99  TYR A CG  
755  C  CD1 . TYR A 99  ? 0.1592 0.1521 0.2083 -0.0051 0.0154  -0.0043 99  TYR A CD1 
756  C  CD2 . TYR A 99  ? 0.2053 0.1730 0.2379 0.0439  -0.0228 -0.0122 99  TYR A CD2 
757  C  CE1 . TYR A 99  ? 0.1659 0.1665 0.2288 0.0178  0.0060  -0.0122 99  TYR A CE1 
758  C  CE2 . TYR A 99  ? 0.2183 0.1986 0.2540 0.0581  -0.0197 -0.0290 99  TYR A CE2 
759  C  CZ  . TYR A 99  ? 0.2055 0.1974 0.2517 0.0469  -0.0096 -0.0364 99  TYR A CZ  
760  O  OH  . TYR A 99  ? 0.2296 0.2251 0.2743 0.0693  -0.0204 -0.0370 99  TYR A OH  
761  N  N   . ASP A 100 ? 0.1634 0.1727 0.1600 0.0020  0.0197  -0.0116 100 ASP A N   
762  C  CA  . ASP A 100 ? 0.1702 0.1740 0.1600 -0.0184 0.0321  -0.0178 100 ASP A CA  
763  C  C   . ASP A 100 ? 0.1595 0.1750 0.1476 -0.0057 0.0163  -0.0142 100 ASP A C   
764  O  O   . ASP A 100 ? 0.1844 0.2177 0.1606 -0.0086 -0.0075 -0.0155 100 ASP A O   
765  C  CB  . ASP A 100 ? 0.2031 0.1957 0.1929 -0.0300 0.0281  -0.0409 100 ASP A CB  
766  C  CG  . ASP A 100 ? 0.2216 0.1969 0.2287 -0.0301 0.0140  -0.0495 100 ASP A CG  
767  O  OD1 . ASP A 100 ? 0.2187 0.1854 0.2229 -0.0113 0.0157  -0.0543 100 ASP A OD1 
768  O  OD2 . ASP A 100 ? 0.2647 0.2185 0.2858 -0.0279 0.0001  -0.0491 100 ASP A OD2 
769  N  N   . MET A 101 ? 0.1496 0.1584 0.1530 -0.0103 0.0262  -0.0145 101 MET A N   
770  C  CA  . MET A 101 ? 0.1522 0.1522 0.1660 0.0051  0.0200  -0.0074 101 MET A CA  
771  C  C   . MET A 101 ? 0.1743 0.1465 0.1590 0.0049  0.0106  -0.0207 101 MET A C   
772  O  O   . MET A 101 ? 0.2053 0.1371 0.1726 0.0194  0.0125  -0.0141 101 MET A O   
773  C  CB  . MET A 101 ? 0.1629 0.1608 0.1832 0.0131  0.0157  -0.0024 101 MET A CB  
774  C  CG  . MET A 101 ? 0.2056 0.1587 0.1993 0.0247  0.0149  -0.0090 101 MET A CG  
775  S  SD  . MET A 101 ? 0.2229 0.1813 0.2223 0.0118  0.0279  -0.0223 101 MET A SD  
776  C  CE  . MET A 101 ? 0.2450 0.1707 0.2200 -0.0006 0.0201  0.0080  101 MET A CE  
777  N  N   . ASN A 102 ? 0.1620 0.1645 0.1526 0.0140  0.0077  -0.0148 102 ASN A N   
778  C  CA  . ASN A 102 ? 0.1616 0.1915 0.1602 -0.0037 -0.0041 -0.0128 102 ASN A CA  
779  C  C   . ASN A 102 ? 0.1640 0.1688 0.1661 -0.0029 0.0045  -0.0147 102 ASN A C   
780  O  O   . ASN A 102 ? 0.1691 0.1622 0.1657 -0.0105 0.0250  -0.0176 102 ASN A O   
781  C  CB  . ASN A 102 ? 0.1571 0.2313 0.1868 -0.0014 -0.0239 -0.0055 102 ASN A CB  
782  C  CG  . ASN A 102 ? 0.2109 0.2926 0.2316 -0.0170 -0.0314 -0.0095 102 ASN A CG  
783  O  OD1 . ASN A 102 ? 0.2107 0.3308 0.2494 -0.0512 -0.0214 -0.0200 102 ASN A OD1 
784  N  ND2 . ASN A 102 ? 0.2465 0.3207 0.2571 -0.0018 -0.0454 0.0023  102 ASN A ND2 
785  N  N   . ALA A 103 ? 0.1484 0.1472 0.1724 -0.0014 0.0049  -0.0088 103 ALA A N   
786  C  CA  . ALA A 103 ? 0.1551 0.1455 0.1807 0.0114  0.0053  -0.0122 103 ALA A CA  
787  C  C   . ALA A 103 ? 0.1685 0.1459 0.1760 0.0156  0.0016  -0.0154 103 ALA A C   
788  O  O   . ALA A 103 ? 0.1824 0.1403 0.1790 0.0084  0.0195  -0.0169 103 ALA A O   
789  C  CB  . ALA A 103 ? 0.1880 0.1376 0.1921 0.0213  0.0097  -0.0185 103 ALA A CB  
790  N  N   . ALA A 104 ? 0.1837 0.1422 0.1654 0.0086  0.0057  -0.0037 104 ALA A N   
791  C  CA  . ALA A 104 ? 0.1955 0.1534 0.1656 0.0219  0.0084  0.0057  104 ALA A CA  
792  C  C   . ALA A 104 ? 0.1747 0.1373 0.1714 0.0043  0.0135  0.0016  104 ALA A C   
793  O  O   . ALA A 104 ? 0.1715 0.1563 0.1828 0.0154  0.0233  0.0104  104 ALA A O   
794  C  CB  . ALA A 104 ? 0.2336 0.2014 0.1739 0.0231  -0.0036 0.0145  104 ALA A CB  
795  N  N   . ASN A 105 ? 0.1679 0.1404 0.1662 0.0154  0.0046  -0.0111 105 ASN A N   
796  C  CA  . ASN A 105 ? 0.1544 0.1459 0.1590 0.0041  0.0120  -0.0085 105 ASN A CA  
797  C  C   . ASN A 105 ? 0.1445 0.1474 0.1587 0.0197  0.0180  -0.0026 105 ASN A C   
798  O  O   . ASN A 105 ? 0.1693 0.1311 0.1713 0.0146  0.0116  -0.0041 105 ASN A O   
799  C  CB  . ASN A 105 ? 0.1485 0.1624 0.1724 0.0003  0.0016  -0.0069 105 ASN A CB  
800  C  CG  . ASN A 105 ? 0.1501 0.1956 0.1831 -0.0100 -0.0027 0.0047  105 ASN A CG  
801  O  OD1 . ASN A 105 ? 0.1720 0.2194 0.1889 -0.0294 0.0013  0.0197  105 ASN A OD1 
802  N  ND2 . ASN A 105 ? 0.1525 0.2321 0.1836 0.0031  -0.0053 -0.0023 105 ASN A ND2 
803  N  N   . VAL A 106 ? 0.1258 0.1491 0.1663 0.0121  0.0016  0.0063  106 VAL A N   
804  C  CA  . VAL A 106 ? 0.1456 0.1437 0.1708 0.0106  0.0041  0.0094  106 VAL A CA  
805  C  C   . VAL A 106 ? 0.1709 0.1433 0.1740 0.0217  0.0084  0.0077  106 VAL A C   
806  O  O   . VAL A 106 ? 0.1614 0.1556 0.1841 0.0228  0.0236  0.0018  106 VAL A O   
807  C  CB  . VAL A 106 ? 0.1713 0.1519 0.1633 0.0150  0.0035  0.0050  106 VAL A CB  
808  C  CG1 . VAL A 106 ? 0.1983 0.1626 0.1577 0.0164  -0.0138 0.0002  106 VAL A CG1 
809  C  CG2 . VAL A 106 ? 0.1746 0.1577 0.1692 0.0208  0.0266  -0.0032 106 VAL A CG2 
810  N  N   . GLY A 107 ? 0.1676 0.1403 0.1687 0.0023  -0.0014 0.0159  107 GLY A N   
811  C  CA  . GLY A 107 ? 0.1664 0.1580 0.1643 -0.0032 -0.0008 0.0050  107 GLY A CA  
812  C  C   . GLY A 107 ? 0.1611 0.1381 0.1554 0.0142  0.0138  0.0008  107 GLY A C   
813  O  O   . GLY A 107 ? 0.1686 0.1482 0.1554 0.0128  0.0126  -0.0033 107 GLY A O   
814  N  N   . TRP A 108 ? 0.1554 0.1539 0.1712 0.0317  0.0140  0.0084  108 TRP A N   
815  C  CA  . TRP A 108 ? 0.1511 0.1574 0.1781 0.0248  0.0161  0.0229  108 TRP A CA  
816  C  C   . TRP A 108 ? 0.1592 0.1574 0.1752 0.0228  0.0133  0.0198  108 TRP A C   
817  O  O   . TRP A 108 ? 0.1796 0.1482 0.1691 0.0066  0.0055  0.0063  108 TRP A O   
818  C  CB  . TRP A 108 ? 0.1754 0.1649 0.1757 0.0210  0.0168  0.0238  108 TRP A CB  
819  C  CG  . TRP A 108 ? 0.1823 0.1665 0.1851 0.0296  0.0145  0.0148  108 TRP A CG  
820  C  CD1 . TRP A 108 ? 0.1530 0.1779 0.1912 0.0142  0.0051  0.0120  108 TRP A CD1 
821  C  CD2 . TRP A 108 ? 0.2317 0.1613 0.1999 0.0484  0.0208  0.0021  108 TRP A CD2 
822  N  NE1 . TRP A 108 ? 0.1869 0.1703 0.1939 0.0344  0.0162  0.0230  108 TRP A NE1 
823  C  CE2 . TRP A 108 ? 0.2291 0.1704 0.2022 0.0504  0.0199  0.0243  108 TRP A CE2 
824  C  CE3 . TRP A 108 ? 0.2694 0.1636 0.2181 0.0461  0.0313  -0.0116 108 TRP A CE3 
825  C  CZ2 . TRP A 108 ? 0.2698 0.2101 0.2273 0.0624  0.0157  0.0057  108 TRP A CZ2 
826  C  CZ3 . TRP A 108 ? 0.2987 0.2040 0.2372 0.0562  0.0239  0.0007  108 TRP A CZ3 
827  C  CH2 . TRP A 108 ? 0.3015 0.2205 0.2437 0.0717  0.0205  -0.0031 108 TRP A CH2 
828  N  N   . ASN A 109 ? 0.1622 0.1467 0.1922 0.0205  0.0247  0.0180  109 ASN A N   
829  C  CA  . ASN A 109 ? 0.1534 0.1362 0.2067 0.0243  0.0100  0.0175  109 ASN A CA  
830  C  C   . ASN A 109 ? 0.1730 0.1439 0.1983 0.0219  0.0123  0.0091  109 ASN A C   
831  O  O   . ASN A 109 ? 0.1905 0.1740 0.2050 0.0254  0.0056  0.0017  109 ASN A O   
832  C  CB  . ASN A 109 ? 0.1622 0.1549 0.2381 0.0235  0.0126  0.0038  109 ASN A CB  
833  C  CG  . ASN A 109 ? 0.1793 0.1733 0.2631 0.0299  0.0225  0.0075  109 ASN A CG  
834  O  OD1 . ASN A 109 ? 0.1691 0.1946 0.2436 0.0124  0.0130  0.0059  109 ASN A OD1 
835  N  ND2 . ASN A 109 ? 0.1857 0.1707 0.2980 0.0537  0.0406  0.0039  109 ASN A ND2 
836  N  N   . ASN A 110 ? 0.1573 0.1394 0.1860 0.0105  0.0098  0.0266  110 ASN A N   
837  C  CA  . ASN A 110 ? 0.1603 0.1762 0.1886 -0.0033 0.0243  0.0262  110 ASN A CA  
838  C  C   . ASN A 110 ? 0.1765 0.1790 0.1932 -0.0038 0.0104  0.0222  110 ASN A C   
839  O  O   . ASN A 110 ? 0.1966 0.1893 0.2014 -0.0057 0.0083  0.0255  110 ASN A O   
840  C  CB  . ASN A 110 ? 0.1855 0.1870 0.1979 -0.0101 0.0399  0.0155  110 ASN A CB  
841  C  CG  . ASN A 110 ? 0.2053 0.2061 0.2313 -0.0046 0.0313  0.0090  110 ASN A CG  
842  O  OD1 . ASN A 110 ? 0.2284 0.2062 0.2505 -0.0038 0.0455  -0.0134 110 ASN A OD1 
843  N  ND2 . ASN A 110 ? 0.2174 0.2465 0.2345 -0.0056 0.0067  0.0104  110 ASN A ND2 
844  N  N   . SER A 111 ? 0.1630 0.1638 0.1879 0.0078  0.0164  0.0114  111 SER A N   
845  C  CA  . SER A 111 ? 0.1852 0.1742 0.1943 -0.0002 0.0234  -0.0108 111 SER A CA  
846  C  C   . SER A 111 ? 0.1885 0.1623 0.1800 -0.0013 0.0151  0.0029  111 SER A C   
847  O  O   . SER A 111 ? 0.1840 0.1722 0.1794 -0.0040 0.0146  0.0075  111 SER A O   
848  C  CB  . SER A 111 ? 0.2047 0.2372 0.2100 -0.0231 0.0379  -0.0563 111 SER A CB  
849  O  OG  . SER A 111 ? 0.2398 0.2754 0.2332 -0.0326 0.0343  -0.0445 111 SER A OG  
850  N  N   . THR A 112 ? 0.1914 0.1626 0.1791 -0.0078 0.0061  0.0058  112 THR A N   
851  C  CA  . THR A 112 ? 0.1787 0.1668 0.1858 -0.0061 0.0123  0.0054  112 THR A CA  
852  C  C   . THR A 112 ? 0.1885 0.1769 0.2071 -0.0082 0.0157  -0.0058 112 THR A C   
853  O  O   . THR A 112 ? 0.1889 0.1908 0.2404 0.0020  0.0271  -0.0115 112 THR A O   
854  C  CB  . THR A 112 ? 0.1731 0.1618 0.1867 0.0121  0.0007  -0.0150 112 THR A CB  
855  O  OG1 . THR A 112 ? 0.1767 0.1983 0.1990 0.0177  0.0165  -0.0296 112 THR A OG1 
856  C  CG2 . THR A 112 ? 0.1890 0.1605 0.1948 0.0084  0.0066  -0.0039 112 THR A CG2 
857  N  N   . PHE A 113 ? 0.1782 0.1553 0.2049 0.0040  0.0091  0.0024  113 PHE A N   
858  C  CA  . PHE A 113 ? 0.1802 0.1507 0.2175 0.0204  0.0143  -0.0046 113 PHE A CA  
859  C  C   . PHE A 113 ? 0.1767 0.1486 0.2233 0.0225  0.0099  -0.0015 113 PHE A C   
860  O  O   . PHE A 113 ? 0.2091 0.1443 0.2528 0.0259  0.0007  -0.0174 113 PHE A O   
861  C  CB  . PHE A 113 ? 0.1868 0.1686 0.2120 0.0224  0.0008  -0.0048 113 PHE A CB  
862  C  CG  . PHE A 113 ? 0.2062 0.1694 0.2255 0.0379  -0.0067 0.0000  113 PHE A CG  
863  C  CD1 . PHE A 113 ? 0.1950 0.1617 0.2271 0.0170  -0.0055 -0.0033 113 PHE A CD1 
864  C  CD2 . PHE A 113 ? 0.2558 0.2024 0.2545 0.0293  -0.0188 -0.0097 113 PHE A CD2 
865  C  CE1 . PHE A 113 ? 0.2147 0.1577 0.2426 0.0300  -0.0061 -0.0085 113 PHE A CE1 
866  C  CE2 . PHE A 113 ? 0.2792 0.2157 0.2703 0.0325  -0.0199 -0.0244 113 PHE A CE2 
867  C  CZ  . PHE A 113 ? 0.2660 0.1898 0.2668 0.0310  -0.0151 -0.0245 113 PHE A CZ  
868  N  N   . ALA A 114 ? 0.1805 0.1736 0.2096 0.0057  0.0069  -0.0186 114 ALA A N   
869  C  CA  . ALA A 114 ? 0.2076 0.1865 0.2174 0.0120  0.0047  -0.0343 114 ALA A CA  
870  C  C   . ALA A 114 ? 0.2321 0.1961 0.2498 0.0016  0.0399  -0.0433 114 ALA A C   
871  O  O   . ALA A 114 ? 0.2680 0.2177 0.2660 0.0024  0.0631  -0.0445 114 ALA A O   
872  C  CB  . ALA A 114 ? 0.2405 0.1856 0.2192 0.0327  -0.0042 -0.0273 114 ALA A CB  
873  O  OXT . ALA A 114 ? 0.2309 0.1946 0.2665 0.0019  0.0398  -0.0552 114 ALA A OXT 
874  N  N   . PRO B 1   ? 0.1701 0.2212 0.2149 -0.0436 0.0494  0.0063  1   PRO B N   
875  C  CA  . PRO B 1   ? 0.1750 0.2274 0.2054 -0.0498 0.0260  0.0112  1   PRO B CA  
876  C  C   . PRO B 1   ? 0.1943 0.2164 0.1968 -0.0471 0.0195  0.0010  1   PRO B C   
877  O  O   . PRO B 1   ? 0.1963 0.2176 0.1825 -0.0574 0.0193  -0.0136 1   PRO B O   
878  C  CB  . PRO B 1   ? 0.1818 0.2449 0.2220 -0.0446 0.0240  0.0072  1   PRO B CB  
879  C  CG  . PRO B 1   ? 0.1907 0.2625 0.2421 -0.0465 0.0255  0.0045  1   PRO B CG  
880  C  CD  . PRO B 1   ? 0.1821 0.2507 0.2378 -0.0400 0.0429  0.0058  1   PRO B CD  
881  N  N   . MET B 2   ? 0.1953 0.2003 0.2045 -0.0497 0.0203  0.0039  2   MET B N   
882  C  CA  . MET B 2   ? 0.2145 0.2001 0.2316 -0.0556 0.0165  0.0132  2   MET B CA  
883  C  C   . MET B 2   ? 0.1855 0.1865 0.2110 -0.0430 0.0175  -0.0046 2   MET B C   
884  O  O   . MET B 2   ? 0.1890 0.1797 0.2001 -0.0367 -0.0006 -0.0096 2   MET B O   
885  C  CB  . MET B 2   ? 0.2782 0.2573 0.2916 -0.0376 0.0112  0.0364  2   MET B CB  
886  C  CG  . MET B 2   ? 0.3434 0.3024 0.3158 0.0131  0.0351  0.0337  2   MET B CG  
887  S  SD  . MET B 2   ? 0.3639 0.3079 0.3132 0.0640  0.0577  0.0221  2   MET B SD  
888  C  CE  . MET B 2   ? 0.3730 0.2947 0.2870 0.0652  0.0738  0.0063  2   MET B CE  
889  N  N   . PHE B 3   ? 0.1601 0.1778 0.2083 -0.0283 0.0453  0.0036  3   PHE B N   
890  C  CA  . PHE B 3   ? 0.1393 0.1741 0.2081 -0.0209 0.0403  -0.0058 3   PHE B CA  
891  C  C   . PHE B 3   ? 0.1452 0.1631 0.1994 -0.0174 0.0303  -0.0081 3   PHE B C   
892  O  O   . PHE B 3   ? 0.1653 0.1794 0.2046 -0.0302 0.0291  -0.0131 3   PHE B O   
893  C  CB  . PHE B 3   ? 0.1469 0.2010 0.2271 -0.0042 0.0282  0.0053  3   PHE B CB  
894  C  CG  . PHE B 3   ? 0.1647 0.1978 0.2365 0.0008  0.0364  0.0130  3   PHE B CG  
895  C  CD1 . PHE B 3   ? 0.1576 0.2054 0.2442 0.0301  0.0251  0.0270  3   PHE B CD1 
896  C  CD2 . PHE B 3   ? 0.2337 0.2097 0.2479 0.0013  0.0513  0.0098  3   PHE B CD2 
897  C  CE1 . PHE B 3   ? 0.1883 0.2028 0.2581 0.0325  0.0371  0.0153  3   PHE B CE1 
898  C  CE2 . PHE B 3   ? 0.2666 0.2174 0.2601 0.0014  0.0472  0.0050  3   PHE B CE2 
899  C  CZ  . PHE B 3   ? 0.2449 0.2196 0.2647 0.0256  0.0372  0.0071  3   PHE B CZ  
900  N  N   . ILE B 4   ? 0.1360 0.1520 0.2048 -0.0112 0.0300  0.0050  4   ILE B N   
901  C  CA  . ILE B 4   ? 0.1387 0.1518 0.2163 -0.0043 0.0380  0.0035  4   ILE B CA  
902  C  C   . ILE B 4   ? 0.1610 0.1454 0.2218 -0.0047 0.0316  0.0040  4   ILE B C   
903  O  O   . ILE B 4   ? 0.1543 0.1610 0.2194 -0.0104 0.0144  0.0149  4   ILE B O   
904  C  CB  . ILE B 4   ? 0.1341 0.1688 0.2479 -0.0028 0.0320  0.0005  4   ILE B CB  
905  C  CG1 . ILE B 4   ? 0.1725 0.1756 0.2849 0.0026  0.0232  -0.0033 4   ILE B CG1 
906  C  CG2 . ILE B 4   ? 0.1302 0.2042 0.2579 0.0021  0.0294  0.0187  4   ILE B CG2 
907  C  CD1 . ILE B 4   ? 0.2363 0.2015 0.2990 0.0120  0.0284  -0.0067 4   ILE B CD1 
908  N  N   . VAL B 5   ? 0.1643 0.1286 0.2356 -0.0101 0.0344  0.0024  5   VAL B N   
909  C  CA  . VAL B 5   ? 0.1959 0.1290 0.2514 -0.0186 0.0346  0.0120  5   VAL B CA  
910  C  C   . VAL B 5   ? 0.1758 0.1438 0.2233 -0.0118 0.0306  -0.0025 5   VAL B C   
911  O  O   . VAL B 5   ? 0.1776 0.1733 0.2163 -0.0248 0.0209  -0.0038 5   VAL B O   
912  C  CB  . VAL B 5   ? 0.2549 0.1542 0.2961 0.0056  0.0571  0.0325  5   VAL B CB  
913  C  CG1 . VAL B 5   ? 0.3046 0.2006 0.3267 0.0306  0.0473  0.0288  5   VAL B CG1 
914  C  CG2 . VAL B 5   ? 0.2601 0.1403 0.3094 0.0097  0.0733  0.0367  5   VAL B CG2 
915  N  N   . ASN B 6   ? 0.1451 0.1304 0.2136 -0.0017 0.0225  -0.0029 6   ASN B N   
916  C  CA  . ASN B 6   ? 0.1481 0.1335 0.2276 0.0036  0.0308  0.0050  6   ASN B CA  
917  C  C   . ASN B 6   ? 0.1493 0.1298 0.2297 -0.0118 0.0170  0.0100  6   ASN B C   
918  O  O   . ASN B 6   ? 0.1681 0.1412 0.2243 0.0006  -0.0018 0.0188  6   ASN B O   
919  C  CB  . ASN B 6   ? 0.1771 0.1444 0.2321 0.0271  0.0491  0.0087  6   ASN B CB  
920  C  CG  . ASN B 6   ? 0.2331 0.1765 0.2507 0.0263  0.0569  0.0089  6   ASN B CG  
921  O  OD1 . ASN B 6   ? 0.2547 0.1909 0.2660 0.0339  0.0511  0.0007  6   ASN B OD1 
922  N  ND2 . ASN B 6   ? 0.2650 0.1848 0.2628 0.0478  0.0863  0.0127  6   ASN B ND2 
923  N  N   . THR B 7   ? 0.1424 0.1210 0.2401 -0.0154 0.0279  0.0046  7   THR B N   
924  C  CA  . THR B 7   ? 0.1503 0.1228 0.2482 -0.0108 0.0306  -0.0023 7   THR B CA  
925  C  C   . THR B 7   ? 0.1625 0.1247 0.2524 -0.0041 0.0228  -0.0038 7   THR B C   
926  O  O   . THR B 7   ? 0.1724 0.1254 0.2428 -0.0035 0.0298  -0.0070 7   THR B O   
927  C  CB  . THR B 7   ? 0.1650 0.1321 0.2462 0.0114  0.0261  -0.0068 7   THR B CB  
928  O  OG1 . THR B 7   ? 0.1661 0.1317 0.2622 0.0129  0.0254  -0.0062 7   THR B OG1 
929  C  CG2 . THR B 7   ? 0.1761 0.1716 0.2414 0.0124  0.0335  -0.0176 7   THR B CG2 
930  N  N   . ASN B 8   ? 0.1657 0.1315 0.2647 -0.0198 0.0294  0.0049  8   ASN B N   
931  C  CA  . ASN B 8   ? 0.1947 0.1362 0.2699 -0.0124 0.0467  -0.0101 8   ASN B CA  
932  C  C   . ASN B 8   ? 0.2202 0.1627 0.2880 -0.0234 0.0536  -0.0239 8   ASN B C   
933  O  O   . ASN B 8   ? 0.2453 0.1847 0.3160 -0.0404 0.0542  -0.0277 8   ASN B O   
934  C  CB  . ASN B 8   ? 0.2058 0.1615 0.2606 -0.0179 0.0403  0.0058  8   ASN B CB  
935  C  CG  . ASN B 8   ? 0.2090 0.1591 0.2601 -0.0246 0.0343  0.0160  8   ASN B CG  
936  O  OD1 . ASN B 8   ? 0.1935 0.1557 0.2649 -0.0195 0.0155  0.0077  8   ASN B OD1 
937  N  ND2 . ASN B 8   ? 0.2315 0.1779 0.2633 -0.0371 0.0331  0.0341  8   ASN B ND2 
938  N  N   . VAL B 9   ? 0.2125 0.1605 0.2811 -0.0059 0.0407  -0.0260 9   VAL B N   
939  C  CA  . VAL B 9   ? 0.2225 0.1901 0.2907 0.0026  0.0206  -0.0362 9   VAL B CA  
940  C  C   . VAL B 9   ? 0.2303 0.1901 0.2928 0.0004  0.0208  -0.0321 9   VAL B C   
941  O  O   . VAL B 9   ? 0.2333 0.2015 0.2815 0.0301  0.0244  -0.0301 9   VAL B O   
942  C  CB  . VAL B 9   ? 0.2416 0.2378 0.3106 0.0318  -0.0024 -0.0376 9   VAL B CB  
943  C  CG1 . VAL B 9   ? 0.2488 0.2324 0.3115 0.0487  -0.0170 -0.0470 9   VAL B CG1 
944  C  CG2 . VAL B 9   ? 0.2515 0.2591 0.3267 0.0332  -0.0055 -0.0307 9   VAL B CG2 
945  N  N   . PRO B 10  ? 0.2558 0.2058 0.3147 -0.0203 0.0123  -0.0278 10  PRO B N   
946  C  CA  . PRO B 10  ? 0.2689 0.2326 0.3174 -0.0374 0.0131  -0.0339 10  PRO B CA  
947  C  C   . PRO B 10  ? 0.2758 0.2329 0.3154 -0.0233 0.0219  -0.0660 10  PRO B C   
948  O  O   . PRO B 10  ? 0.2669 0.2307 0.3139 -0.0191 0.0205  -0.0714 10  PRO B O   
949  C  CB  . PRO B 10  ? 0.3066 0.2493 0.3334 -0.0462 0.0036  -0.0254 10  PRO B CB  
950  C  CG  . PRO B 10  ? 0.3139 0.2289 0.3409 -0.0361 -0.0011 -0.0316 10  PRO B CG  
951  C  CD  . PRO B 10  ? 0.2954 0.2102 0.3289 -0.0270 0.0037  -0.0211 10  PRO B CD  
952  N  N   . ARG B 11  ? 0.2868 0.2263 0.3233 -0.0311 0.0253  -0.0826 11  ARG B N   
953  C  CA  . ARG B 11  ? 0.3269 0.2585 0.3403 -0.0322 0.0390  -0.0984 11  ARG B CA  
954  C  C   . ARG B 11  ? 0.3345 0.2434 0.3418 -0.0343 0.0394  -0.1022 11  ARG B C   
955  O  O   . ARG B 11  ? 0.3202 0.2495 0.3341 -0.0379 0.0545  -0.0979 11  ARG B O   
956  C  CB  . ARG B 11  ? 0.3646 0.3118 0.3575 -0.0366 0.0470  -0.1147 11  ARG B CB  
957  C  CG  . ARG B 11  ? 0.4329 0.3807 0.3898 -0.0442 0.0619  -0.1147 11  ARG B CG  
958  C  CD  . ARG B 11  ? 0.5029 0.4411 0.4141 -0.0350 0.0841  -0.1205 11  ARG B CD  
959  N  NE  . ARG B 11  ? 0.5583 0.4872 0.4344 -0.0239 0.1046  -0.1219 11  ARG B NE  
960  C  CZ  . ARG B 11  ? 0.5961 0.5155 0.4421 -0.0154 0.1247  -0.1269 11  ARG B CZ  
961  N  NH1 . ARG B 11  ? 0.6082 0.5207 0.4494 -0.0083 0.1210  -0.1273 11  ARG B NH1 
962  N  NH2 . ARG B 11  ? 0.6090 0.5254 0.4385 -0.0143 0.1421  -0.1293 11  ARG B NH2 
963  N  N   . ALA B 12  ? 0.3522 0.2328 0.3598 -0.0171 0.0373  -0.1035 12  ALA B N   
964  C  CA  . ALA B 12  ? 0.3578 0.2307 0.3891 -0.0144 0.0378  -0.1041 12  ALA B CA  
965  C  C   . ALA B 12  ? 0.3514 0.2408 0.4122 -0.0037 0.0570  -0.0967 12  ALA B C   
966  O  O   . ALA B 12  ? 0.3670 0.2679 0.4207 0.0234  0.0776  -0.1041 12  ALA B O   
967  C  CB  . ALA B 12  ? 0.3735 0.2271 0.3972 -0.0346 0.0204  -0.1036 12  ALA B CB  
968  N  N   A SER B 13  ? 0.3435 0.2277 0.4176 -0.0097 0.0509  -0.0959 13  SER B N   
969  N  N   B SER B 13  ? 0.3423 0.2373 0.4220 -0.0051 0.0515  -0.0885 13  SER B N   
970  C  CA  A SER B 13  ? 0.3338 0.2334 0.4218 -0.0104 0.0470  -0.0834 13  SER B CA  
971  C  CA  B SER B 13  ? 0.3313 0.2492 0.4303 -0.0006 0.0487  -0.0710 13  SER B CA  
972  C  C   A SER B 13  ? 0.3245 0.2450 0.4282 -0.0207 0.0452  -0.0701 13  SER B C   
973  C  C   B SER B 13  ? 0.3235 0.2493 0.4329 -0.0138 0.0458  -0.0646 13  SER B C   
974  O  O   A SER B 13  ? 0.3342 0.2592 0.4382 -0.0320 0.0386  -0.0546 13  SER B O   
975  O  O   B SER B 13  ? 0.3339 0.2571 0.4435 -0.0236 0.0381  -0.0496 13  SER B O   
976  C  CB  A SER B 13  ? 0.3385 0.2281 0.4189 -0.0077 0.0408  -0.0819 13  SER B CB  
977  C  CB  B SER B 13  ? 0.3336 0.2619 0.4353 0.0105  0.0461  -0.0580 13  SER B CB  
978  O  OG  A SER B 13  ? 0.3352 0.2119 0.4132 -0.0101 0.0342  -0.0842 13  SER B OG  
979  O  OG  B SER B 13  ? 0.3318 0.2659 0.4371 0.0176  0.0441  -0.0490 13  SER B OG  
980  N  N   . VAL B 14  ? 0.3104 0.2439 0.4237 -0.0182 0.0504  -0.0762 14  VAL B N   
981  C  CA  . VAL B 14  ? 0.2995 0.2535 0.4186 -0.0201 0.0472  -0.0875 14  VAL B CA  
982  C  C   . VAL B 14  ? 0.3079 0.2722 0.4169 -0.0184 0.0523  -0.0990 14  VAL B C   
983  O  O   . VAL B 14  ? 0.3181 0.2987 0.4166 -0.0184 0.0496  -0.0832 14  VAL B O   
984  C  CB  . VAL B 14  ? 0.2899 0.2557 0.4228 -0.0063 0.0435  -0.0755 14  VAL B CB  
985  C  CG1 . VAL B 14  ? 0.2970 0.2569 0.4284 -0.0086 0.0323  -0.0659 14  VAL B CG1 
986  C  CG2 . VAL B 14  ? 0.2714 0.2458 0.4182 0.0116  0.0536  -0.0864 14  VAL B CG2 
987  N  N   . PRO B 15  ? 0.3005 0.2759 0.4183 -0.0044 0.0608  -0.1183 15  PRO B N   
988  C  CA  . PRO B 15  ? 0.3157 0.3160 0.4238 -0.0081 0.0656  -0.1145 15  PRO B CA  
989  C  C   . PRO B 15  ? 0.3314 0.3344 0.4268 -0.0456 0.0570  -0.1121 15  PRO B C   
990  O  O   . PRO B 15  ? 0.3210 0.3178 0.4307 -0.0563 0.0545  -0.1019 15  PRO B O   
991  C  CB  . PRO B 15  ? 0.3184 0.3232 0.4282 0.0246  0.0742  -0.1143 15  PRO B CB  
992  C  CG  . PRO B 15  ? 0.3144 0.3159 0.4295 0.0321  0.0767  -0.1153 15  PRO B CG  
993  C  CD  . PRO B 15  ? 0.3027 0.2908 0.4210 0.0250  0.0772  -0.1227 15  PRO B CD  
994  N  N   . ASP B 16  ? 0.3611 0.3826 0.4292 -0.0717 0.0495  -0.1152 16  ASP B N   
995  C  CA  . ASP B 16  ? 0.3915 0.4279 0.4411 -0.0881 0.0421  -0.1260 16  ASP B CA  
996  C  C   . ASP B 16  ? 0.3861 0.4117 0.4334 -0.0727 0.0580  -0.1303 16  ASP B C   
997  O  O   . ASP B 16  ? 0.3929 0.4319 0.4455 -0.0753 0.0671  -0.1203 16  ASP B O   
998  C  CB  . ASP B 16  ? 0.4184 0.4861 0.4619 -0.1163 0.0170  -0.1305 16  ASP B CB  
999  C  CG  . ASP B 16  ? 0.4583 0.5489 0.4860 -0.1144 -0.0016 -0.1234 16  ASP B CG  
1000 O  OD1 . ASP B 16  ? 0.4697 0.5738 0.4948 -0.1162 -0.0094 -0.1166 16  ASP B OD1 
1001 O  OD2 . ASP B 16  ? 0.4830 0.5718 0.5011 -0.1162 -0.0071 -0.1135 16  ASP B OD2 
1002 N  N   . GLY B 17  ? 0.3606 0.3616 0.4152 -0.0575 0.0613  -0.1516 17  GLY B N   
1003 C  CA  . GLY B 17  ? 0.3193 0.3315 0.4010 -0.0316 0.0676  -0.1552 17  GLY B CA  
1004 C  C   . GLY B 17  ? 0.2834 0.2957 0.3917 -0.0071 0.0756  -0.1529 17  GLY B C   
1005 O  O   . GLY B 17  ? 0.2816 0.3093 0.3976 -0.0176 0.0746  -0.1544 17  GLY B O   
1006 N  N   . PHE B 18  ? 0.2579 0.2630 0.3827 0.0045  0.0681  -0.1306 18  PHE B N   
1007 C  CA  . PHE B 18  ? 0.2368 0.2335 0.3729 -0.0071 0.0596  -0.1081 18  PHE B CA  
1008 C  C   . PHE B 18  ? 0.2132 0.2295 0.3727 -0.0060 0.0511  -0.1024 18  PHE B C   
1009 O  O   . PHE B 18  ? 0.2027 0.2201 0.3723 -0.0214 0.0542  -0.0895 18  PHE B O   
1010 C  CB  . PHE B 18  ? 0.2437 0.2160 0.3712 -0.0180 0.0610  -0.0801 18  PHE B CB  
1011 C  CG  . PHE B 18  ? 0.2801 0.2091 0.3698 -0.0078 0.0551  -0.0622 18  PHE B CG  
1012 C  CD1 . PHE B 18  ? 0.3229 0.2207 0.3718 -0.0005 0.0473  -0.0456 18  PHE B CD1 
1013 C  CD2 . PHE B 18  ? 0.2932 0.2124 0.3657 -0.0186 0.0518  -0.0650 18  PHE B CD2 
1014 C  CE1 . PHE B 18  ? 0.3442 0.2216 0.3729 -0.0049 0.0427  -0.0426 18  PHE B CE1 
1015 C  CE2 . PHE B 18  ? 0.3156 0.2243 0.3713 -0.0408 0.0497  -0.0516 18  PHE B CE2 
1016 C  CZ  . PHE B 18  ? 0.3311 0.2184 0.3693 -0.0283 0.0477  -0.0457 18  PHE B CZ  
1017 N  N   . LEU B 19  ? 0.1870 0.2228 0.3695 0.0196  0.0619  -0.1061 19  LEU B N   
1018 C  CA  . LEU B 19  ? 0.1831 0.2338 0.3723 0.0011  0.0577  -0.0989 19  LEU B CA  
1019 C  C   . LEU B 19  ? 0.2012 0.2425 0.3750 0.0100  0.0610  -0.0949 19  LEU B C   
1020 O  O   . LEU B 19  ? 0.2031 0.2443 0.3682 0.0092  0.0493  -0.0981 19  LEU B O   
1021 C  CB  . LEU B 19  ? 0.1811 0.2631 0.3804 -0.0189 0.0462  -0.0806 19  LEU B CB  
1022 C  CG  . LEU B 19  ? 0.2005 0.2986 0.3900 -0.0284 0.0564  -0.0625 19  LEU B CG  
1023 C  CD1 . LEU B 19  ? 0.2179 0.3158 0.3996 -0.0403 0.0530  -0.0288 19  LEU B CD1 
1024 C  CD2 . LEU B 19  ? 0.2114 0.3235 0.3938 -0.0486 0.0618  -0.0791 19  LEU B CD2 
1025 N  N   A SER B 20  ? 0.2212 0.2500 0.3818 0.0147  0.0705  -0.0889 20  SER B N   
1026 N  N   B SER B 20  ? 0.2210 0.2508 0.3818 0.0145  0.0713  -0.0886 20  SER B N   
1027 C  CA  A SER B 20  ? 0.2363 0.2765 0.3900 0.0131  0.0923  -0.0800 20  SER B CA  
1028 C  CA  B SER B 20  ? 0.2363 0.2766 0.3903 0.0132  0.0925  -0.0801 20  SER B CA  
1029 C  C   A SER B 20  ? 0.2245 0.2593 0.3789 0.0116  0.0933  -0.0761 20  SER B C   
1030 C  C   B SER B 20  ? 0.2253 0.2599 0.3793 0.0122  0.0926  -0.0762 20  SER B C   
1031 O  O   A SER B 20  ? 0.2179 0.2706 0.3795 0.0151  0.0874  -0.0754 20  SER B O   
1032 O  O   B SER B 20  ? 0.2185 0.2704 0.3795 0.0148  0.0879  -0.0752 20  SER B O   
1033 C  CB  A SER B 20  ? 0.2660 0.3234 0.4146 0.0164  0.1094  -0.0772 20  SER B CB  
1034 C  CB  B SER B 20  ? 0.2670 0.3235 0.4146 0.0158  0.1087  -0.0771 20  SER B CB  
1035 O  OG  A SER B 20  ? 0.3028 0.3596 0.4340 0.0157  0.1105  -0.0705 20  SER B OG  
1036 O  OG  B SER B 20  ? 0.3055 0.3608 0.4331 0.0149  0.1070  -0.0711 20  SER B OG  
1037 N  N   . GLU B 21  ? 0.2353 0.2483 0.3736 0.0231  0.0869  -0.0758 21  GLU B N   
1038 C  CA  . GLU B 21  ? 0.2470 0.2396 0.3655 0.0247  0.0688  -0.0633 21  GLU B CA  
1039 C  C   . GLU B 21  ? 0.2311 0.2301 0.3366 0.0012  0.0623  -0.0497 21  GLU B C   
1040 O  O   . GLU B 21  ? 0.2307 0.2238 0.3301 -0.0006 0.0542  -0.0415 21  GLU B O   
1041 C  CB  . GLU B 21  ? 0.2760 0.2514 0.3915 0.0289  0.0581  -0.0621 21  GLU B CB  
1042 C  CG  . GLU B 21  ? 0.3239 0.2731 0.4198 0.0492  0.0550  -0.0526 21  GLU B CG  
1043 C  CD  . GLU B 21  ? 0.3605 0.2879 0.4427 0.0566  0.0532  -0.0516 21  GLU B CD  
1044 O  OE1 . GLU B 21  ? 0.3808 0.3101 0.4532 0.0696  0.0585  -0.0501 21  GLU B OE1 
1045 O  OE2 . GLU B 21  ? 0.3663 0.2708 0.4492 0.0391  0.0482  -0.0563 21  GLU B OE2 
1046 N  N   . LEU B 22  ? 0.2105 0.2128 0.3207 0.0036  0.0620  -0.0505 22  LEU B N   
1047 C  CA  . LEU B 22  ? 0.2118 0.2190 0.3006 -0.0040 0.0701  -0.0426 22  LEU B CA  
1048 C  C   . LEU B 22  ? 0.2041 0.2324 0.2863 -0.0046 0.0622  -0.0417 22  LEU B C   
1049 O  O   . LEU B 22  ? 0.1884 0.2480 0.2835 -0.0045 0.0502  -0.0345 22  LEU B O   
1050 C  CB  . LEU B 22  ? 0.2078 0.2073 0.3094 -0.0197 0.0765  -0.0347 22  LEU B CB  
1051 C  CG  . LEU B 22  ? 0.2191 0.2117 0.3191 -0.0347 0.0737  -0.0224 22  LEU B CG  
1052 C  CD1 . LEU B 22  ? 0.2102 0.2292 0.3230 -0.0304 0.0726  -0.0231 22  LEU B CD1 
1053 C  CD2 . LEU B 22  ? 0.2492 0.2232 0.3271 -0.0407 0.0695  -0.0008 22  LEU B CD2 
1054 N  N   . THR B 23  ? 0.2203 0.2219 0.2796 -0.0038 0.0572  -0.0582 23  THR B N   
1055 C  CA  . THR B 23  ? 0.2249 0.2325 0.2914 -0.0143 0.0640  -0.0555 23  THR B CA  
1056 C  C   . THR B 23  ? 0.2199 0.2564 0.2963 -0.0044 0.0759  -0.0581 23  THR B C   
1057 O  O   . THR B 23  ? 0.2177 0.2682 0.2994 -0.0068 0.0703  -0.0468 23  THR B O   
1058 C  CB  . THR B 23  ? 0.2026 0.2102 0.3004 -0.0152 0.0669  -0.0405 23  THR B CB  
1059 O  OG1 . THR B 23  ? 0.1853 0.2093 0.3129 -0.0041 0.0698  -0.0516 23  THR B OG1 
1060 C  CG2 . THR B 23  ? 0.2092 0.2127 0.3031 -0.0196 0.0691  -0.0114 23  THR B CG2 
1061 N  N   . GLN B 24  ? 0.1991 0.2823 0.3046 0.0144  0.0740  -0.0797 24  GLN B N   
1062 C  CA  . GLN B 24  ? 0.2081 0.2987 0.3272 0.0128  0.0734  -0.0791 24  GLN B CA  
1063 C  C   . GLN B 24  ? 0.1989 0.2597 0.3318 0.0128  0.0587  -0.0592 24  GLN B C   
1064 O  O   . GLN B 24  ? 0.1914 0.2638 0.3382 0.0007  0.0433  -0.0548 24  GLN B O   
1065 C  CB  . GLN B 24  ? 0.2580 0.3430 0.3625 0.0036  0.0738  -0.0799 24  GLN B CB  
1066 C  CG  . GLN B 24  ? 0.3276 0.3822 0.4099 -0.0025 0.0702  -0.0647 24  GLN B CG  
1067 C  CD  . GLN B 24  ? 0.3845 0.4099 0.4435 0.0005  0.0747  -0.0619 24  GLN B CD  
1068 O  OE1 . GLN B 24  ? 0.4259 0.4337 0.4582 -0.0159 0.0692  -0.0648 24  GLN B OE1 
1069 N  NE2 . GLN B 24  ? 0.3949 0.3950 0.4578 0.0284  0.0832  -0.0684 24  GLN B NE2 
1070 N  N   . GLN B 25  ? 0.2163 0.2222 0.3350 0.0310  0.0600  -0.0592 25  GLN B N   
1071 C  CA  . GLN B 25  ? 0.2239 0.2307 0.3543 0.0317  0.0449  -0.0510 25  GLN B CA  
1072 C  C   . GLN B 25  ? 0.1908 0.2278 0.3333 0.0276  0.0399  -0.0462 25  GLN B C   
1073 O  O   . GLN B 25  ? 0.1870 0.2283 0.3307 0.0221  0.0296  -0.0402 25  GLN B O   
1074 C  CB  . GLN B 25  ? 0.2896 0.2373 0.3930 0.0490  0.0377  -0.0550 25  GLN B CB  
1075 C  CG  . GLN B 25  ? 0.3466 0.2900 0.4253 0.0745  0.0339  -0.0552 25  GLN B CG  
1076 C  CD  . GLN B 25  ? 0.3851 0.3483 0.4511 0.1027  0.0352  -0.0555 25  GLN B CD  
1077 O  OE1 . GLN B 25  ? 0.4031 0.3756 0.4646 0.1237  0.0257  -0.0484 25  GLN B OE1 
1078 N  NE2 . GLN B 25  ? 0.3883 0.3663 0.4610 0.1035  0.0485  -0.0605 25  GLN B NE2 
1079 N  N   . LEU B 26  ? 0.1966 0.2200 0.3220 0.0263  0.0654  -0.0413 26  LEU B N   
1080 C  CA  . LEU B 26  ? 0.2054 0.2108 0.3182 0.0135  0.0722  -0.0276 26  LEU B CA  
1081 C  C   . LEU B 26  ? 0.2231 0.2278 0.3123 -0.0123 0.0736  -0.0339 26  LEU B C   
1082 O  O   . LEU B 26  ? 0.2282 0.2431 0.3157 -0.0092 0.0704  -0.0384 26  LEU B O   
1083 C  CB  . LEU B 26  ? 0.1919 0.2004 0.3221 0.0282  0.0746  -0.0199 26  LEU B CB  
1084 C  CG  . LEU B 26  ? 0.2067 0.2313 0.3319 0.0303  0.0773  -0.0105 26  LEU B CG  
1085 C  CD1 . LEU B 26  ? 0.2140 0.2491 0.3503 0.0462  0.0741  -0.0001 26  LEU B CD1 
1086 C  CD2 . LEU B 26  ? 0.2427 0.2520 0.3312 0.0116  0.0761  0.0028  26  LEU B CD2 
1087 N  N   . ALA B 27  ? 0.2044 0.2323 0.3032 -0.0378 0.0736  -0.0393 27  ALA B N   
1088 C  CA  . ALA B 27  ? 0.2053 0.2521 0.3002 -0.0369 0.0631  -0.0569 27  ALA B CA  
1089 C  C   . ALA B 27  ? 0.2124 0.2828 0.3094 -0.0337 0.0592  -0.0643 27  ALA B C   
1090 O  O   . ALA B 27  ? 0.2296 0.2990 0.3186 -0.0396 0.0535  -0.0781 27  ALA B O   
1091 C  CB  . ALA B 27  ? 0.2101 0.2640 0.2952 -0.0317 0.0608  -0.0603 27  ALA B CB  
1092 N  N   . GLN B 28  ? 0.2059 0.2977 0.3115 -0.0182 0.0589  -0.0602 28  GLN B N   
1093 C  CA  . GLN B 28  ? 0.2198 0.3249 0.3255 -0.0075 0.0437  -0.0622 28  GLN B CA  
1094 C  C   . GLN B 28  ? 0.2184 0.3224 0.3297 -0.0053 0.0421  -0.0603 28  GLN B C   
1095 O  O   . GLN B 28  ? 0.2292 0.3425 0.3427 -0.0324 0.0379  -0.0620 28  GLN B O   
1096 C  CB  . GLN B 28  ? 0.2412 0.3479 0.3384 -0.0050 0.0403  -0.0628 28  GLN B CB  
1097 C  CG  . GLN B 28  ? 0.2585 0.3699 0.3494 -0.0052 0.0499  -0.0538 28  GLN B CG  
1098 N  N   . ALA B 29  ? 0.2058 0.2951 0.3225 0.0059  0.0431  -0.0480 29  ALA B N   
1099 C  CA  . ALA B 29  ? 0.1965 0.2989 0.3147 0.0061  0.0262  -0.0337 29  ALA B CA  
1100 C  C   . ALA B 29  ? 0.2103 0.2964 0.3087 -0.0002 0.0220  -0.0347 29  ALA B C   
1101 O  O   . ALA B 29  ? 0.2100 0.2963 0.3012 -0.0149 0.0235  -0.0138 29  ALA B O   
1102 C  CB  . ALA B 29  ? 0.1839 0.3058 0.3145 0.0038  0.0352  -0.0277 29  ALA B CB  
1103 N  N   . THR B 30  ? 0.2368 0.2773 0.3134 0.0038  0.0144  -0.0613 30  THR B N   
1104 C  CA  . THR B 30  ? 0.2653 0.2663 0.3194 0.0018  0.0038  -0.0673 30  THR B CA  
1105 C  C   . THR B 30  ? 0.2832 0.2728 0.3202 0.0045  -0.0118 -0.0617 30  THR B C   
1106 O  O   . THR B 30  ? 0.3185 0.2861 0.3265 -0.0138 -0.0279 -0.0748 30  THR B O   
1107 C  CB  . THR B 30  ? 0.2752 0.2643 0.3208 0.0093  0.0116  -0.0592 30  THR B CB  
1108 O  OG1 . THR B 30  ? 0.2850 0.2568 0.3210 0.0123  0.0213  -0.0522 30  THR B OG1 
1109 C  CG2 . THR B 30  ? 0.2751 0.2933 0.3267 0.0227  0.0202  -0.0595 30  THR B CG2 
1110 N  N   . GLY B 31  ? 0.2601 0.2754 0.3188 0.0097  -0.0130 -0.0415 31  GLY B N   
1111 C  CA  . GLY B 31  ? 0.2458 0.2895 0.3309 0.0187  -0.0125 -0.0216 31  GLY B CA  
1112 C  C   . GLY B 31  ? 0.2637 0.2976 0.3538 0.0165  -0.0167 -0.0161 31  GLY B C   
1113 O  O   . GLY B 31  ? 0.2924 0.3445 0.3792 0.0240  -0.0112 -0.0039 31  GLY B O   
1114 N  N   . LYS B 32  ? 0.2652 0.2683 0.3487 0.0204  -0.0320 -0.0245 32  LYS B N   
1115 C  CA  . LYS B 32  ? 0.2845 0.2435 0.3383 0.0202  -0.0329 -0.0284 32  LYS B CA  
1116 C  C   . LYS B 32  ? 0.2394 0.1903 0.3429 0.0030  -0.0196 -0.0272 32  LYS B C   
1117 O  O   . LYS B 32  ? 0.2119 0.1781 0.3429 0.0033  -0.0097 -0.0229 32  LYS B O   
1118 C  CB  . LYS B 32  ? 0.3555 0.2991 0.3319 0.0371  -0.0319 -0.0482 32  LYS B CB  
1119 C  CG  . LYS B 32  ? 0.4112 0.3478 0.3317 0.0332  -0.0258 -0.0448 32  LYS B CG  
1120 C  CD  . LYS B 32  ? 0.4291 0.3652 0.3275 0.0184  -0.0046 -0.0427 32  LYS B CD  
1121 C  CE  . LYS B 32  ? 0.4156 0.3673 0.3236 0.0047  0.0247  -0.0425 32  LYS B CE  
1122 N  NZ  . LYS B 32  ? 0.4210 0.3634 0.3193 -0.0155 0.0570  -0.0338 32  LYS B NZ  
1123 N  N   . PRO B 33  ? 0.2359 0.1806 0.3533 -0.0156 -0.0166 -0.0364 33  PRO B N   
1124 C  CA  . PRO B 33  ? 0.2220 0.1868 0.3468 -0.0177 0.0024  -0.0286 33  PRO B CA  
1125 C  C   . PRO B 33  ? 0.1685 0.1828 0.3261 0.0045  0.0271  -0.0371 33  PRO B C   
1126 O  O   . PRO B 33  ? 0.1695 0.1824 0.3149 0.0131  0.0298  -0.0461 33  PRO B O   
1127 C  CB  . PRO B 33  ? 0.2708 0.1877 0.3610 -0.0283 -0.0084 -0.0223 33  PRO B CB  
1128 C  CG  . PRO B 33  ? 0.2854 0.1954 0.3681 -0.0384 -0.0185 -0.0231 33  PRO B CG  
1129 C  CD  . PRO B 33  ? 0.2700 0.1897 0.3681 -0.0284 -0.0216 -0.0329 33  PRO B CD  
1130 N  N   . PRO B 34  ? 0.1527 0.1845 0.3183 0.0009  0.0386  -0.0516 34  PRO B N   
1131 C  CA  . PRO B 34  ? 0.1610 0.1779 0.2960 0.0012  0.0338  -0.0508 34  PRO B CA  
1132 C  C   . PRO B 34  ? 0.1671 0.1745 0.2487 0.0035  0.0444  -0.0444 34  PRO B C   
1133 O  O   . PRO B 34  ? 0.1639 0.1798 0.2383 -0.0147 0.0418  -0.0387 34  PRO B O   
1134 C  CB  . PRO B 34  ? 0.1818 0.2054 0.3252 -0.0068 0.0361  -0.0742 34  PRO B CB  
1135 C  CG  . PRO B 34  ? 0.1881 0.2290 0.3346 -0.0098 0.0475  -0.0877 34  PRO B CG  
1136 C  CD  . PRO B 34  ? 0.1668 0.2048 0.3309 -0.0014 0.0538  -0.0765 34  PRO B CD  
1137 N  N   . GLN B 35  ? 0.1893 0.1846 0.2237 -0.0094 0.0473  -0.0388 35  GLN B N   
1138 C  CA  . GLN B 35  ? 0.2001 0.1903 0.1990 -0.0269 0.0645  -0.0399 35  GLN B CA  
1139 C  C   . GLN B 35  ? 0.1875 0.1853 0.1934 -0.0185 0.0508  -0.0324 35  GLN B C   
1140 O  O   . GLN B 35  ? 0.1975 0.2076 0.2027 -0.0063 0.0326  -0.0200 35  GLN B O   
1141 C  CB  . GLN B 35  ? 0.2168 0.2080 0.1974 -0.0420 0.0852  -0.0321 35  GLN B CB  
1142 C  CG  . GLN B 35  ? 0.2522 0.2256 0.2168 -0.0476 0.0870  -0.0477 35  GLN B CG  
1143 C  CD  . GLN B 35  ? 0.2764 0.2298 0.2402 -0.0404 0.1009  -0.0437 35  GLN B CD  
1144 O  OE1 . GLN B 35  ? 0.2090 0.2447 0.2595 -0.0310 0.0964  -0.0422 35  GLN B OE1 
1145 N  NE2 . GLN B 35  ? 0.3325 0.2280 0.2431 -0.0242 0.1227  -0.0379 35  GLN B NE2 
1146 N  N   . TYR B 36  ? 0.1780 0.1648 0.1844 -0.0326 0.0529  -0.0216 36  TYR B N   
1147 C  CA  . TYR B 36  ? 0.1833 0.1701 0.1942 -0.0252 0.0650  -0.0225 36  TYR B CA  
1148 C  C   . TYR B 36  ? 0.1779 0.1687 0.2069 -0.0151 0.0549  -0.0087 36  TYR B C   
1149 O  O   . TYR B 36  ? 0.1995 0.1795 0.2154 -0.0061 0.0661  -0.0095 36  TYR B O   
1150 C  CB  . TYR B 36  ? 0.2255 0.1877 0.2167 -0.0605 0.0916  -0.0318 36  TYR B CB  
1151 C  CG  . TYR B 36  ? 0.2973 0.1994 0.2576 -0.0637 0.1261  -0.0305 36  TYR B CG  
1152 C  CD1 . TYR B 36  ? 0.3280 0.2175 0.2845 -0.0709 0.1278  -0.0305 36  TYR B CD1 
1153 C  CD2 . TYR B 36  ? 0.3458 0.2147 0.3035 -0.0610 0.1541  0.0011  36  TYR B CD2 
1154 C  CE1 . TYR B 36  ? 0.3662 0.2143 0.3066 -0.0849 0.1414  -0.0127 36  TYR B CE1 
1155 C  CE2 . TYR B 36  ? 0.3797 0.2216 0.3293 -0.0734 0.1651  0.0167  36  TYR B CE2 
1156 C  CZ  . TYR B 36  ? 0.3923 0.2230 0.3319 -0.0932 0.1564  0.0147  36  TYR B CZ  
1157 O  OH  . TYR B 36  ? 0.4431 0.2543 0.3589 -0.1039 0.1499  0.0351  36  TYR B OH  
1158 N  N   . ILE B 37  ? 0.1484 0.1593 0.2057 -0.0176 0.0372  -0.0026 37  ILE B N   
1159 C  CA  . ILE B 37  ? 0.1350 0.1537 0.2209 -0.0261 0.0313  0.0115  37  ILE B CA  
1160 C  C   . ILE B 37  ? 0.1365 0.1622 0.2067 -0.0105 0.0399  -0.0040 37  ILE B C   
1161 O  O   . ILE B 37  ? 0.1581 0.1890 0.1997 -0.0082 0.0367  -0.0263 37  ILE B O   
1162 C  CB  . ILE B 37  ? 0.1582 0.1808 0.2575 -0.0169 0.0271  0.0170  37  ILE B CB  
1163 C  CG1 . ILE B 37  ? 0.1997 0.2241 0.2818 -0.0263 0.0293  0.0017  37  ILE B CG1 
1164 C  CG2 . ILE B 37  ? 0.1737 0.1829 0.2697 -0.0082 0.0183  0.0278  37  ILE B CG2 
1165 C  CD1 . ILE B 37  ? 0.2365 0.2505 0.2988 -0.0326 0.0171  -0.0236 37  ILE B CD1 
1166 N  N   . ALA B 38  ? 0.1195 0.1662 0.1973 -0.0063 0.0337  -0.0028 38  ALA B N   
1167 C  CA  . ALA B 38  ? 0.1308 0.1651 0.2022 -0.0052 0.0286  -0.0165 38  ALA B CA  
1168 C  C   . ALA B 38  ? 0.1422 0.1710 0.1853 -0.0179 0.0400  -0.0230 38  ALA B C   
1169 O  O   . ALA B 38  ? 0.1720 0.1933 0.1736 -0.0440 0.0380  -0.0279 38  ALA B O   
1170 C  CB  . ALA B 38  ? 0.1432 0.1729 0.2219 0.0164  0.0279  -0.0345 38  ALA B CB  
1171 N  N   . VAL B 39  ? 0.1393 0.1677 0.1922 -0.0341 0.0426  -0.0152 39  VAL B N   
1172 C  CA  . VAL B 39  ? 0.1609 0.1754 0.2071 -0.0168 0.0388  -0.0081 39  VAL B CA  
1173 C  C   . VAL B 39  ? 0.1682 0.1820 0.2053 -0.0293 0.0300  -0.0156 39  VAL B C   
1174 O  O   . VAL B 39  ? 0.1763 0.2031 0.2097 -0.0456 0.0318  -0.0157 39  VAL B O   
1175 C  CB  . VAL B 39  ? 0.1672 0.2025 0.2357 0.0116  0.0262  -0.0116 39  VAL B CB  
1176 C  CG1 . VAL B 39  ? 0.1572 0.2186 0.2575 0.0191  0.0274  -0.0126 39  VAL B CG1 
1177 C  CG2 . VAL B 39  ? 0.1961 0.2362 0.2545 0.0146  0.0199  -0.0173 39  VAL B CG2 
1178 N  N   . HIS B 40  ? 0.1426 0.1758 0.2122 -0.0280 0.0272  -0.0165 40  HIS B N   
1179 C  CA  . HIS B 40  ? 0.1439 0.1650 0.2063 -0.0202 0.0290  -0.0069 40  HIS B CA  
1180 C  C   . HIS B 40  ? 0.1532 0.1571 0.2001 -0.0230 0.0211  -0.0220 40  HIS B C   
1181 O  O   . HIS B 40  ? 0.1707 0.1697 0.1871 -0.0265 0.0129  -0.0107 40  HIS B O   
1182 C  CB  . HIS B 40  ? 0.1704 0.1679 0.2075 -0.0116 0.0284  -0.0016 40  HIS B CB  
1183 C  CG  . HIS B 40  ? 0.1800 0.1882 0.2023 0.0194  0.0311  0.0210  40  HIS B CG  
1184 N  ND1 . HIS B 40  ? 0.1904 0.1886 0.2108 0.0249  0.0375  0.0212  40  HIS B ND1 
1185 C  CD2 . HIS B 40  ? 0.1700 0.2179 0.1996 0.0073  0.0275  0.0258  40  HIS B CD2 
1186 C  CE1 . HIS B 40  ? 0.1969 0.2102 0.2156 0.0236  0.0344  0.0286  40  HIS B CE1 
1187 N  NE2 . HIS B 40  ? 0.1794 0.2170 0.2059 0.0062  0.0296  0.0278  40  HIS B NE2 
1188 N  N   . VAL B 41  ? 0.1560 0.1719 0.2239 -0.0286 0.0399  -0.0254 41  VAL B N   
1189 C  CA  . VAL B 41  ? 0.1468 0.1666 0.2527 -0.0051 0.0424  -0.0366 41  VAL B CA  
1190 C  C   . VAL B 41  ? 0.1659 0.1684 0.2369 -0.0119 0.0265  -0.0413 41  VAL B C   
1191 O  O   . VAL B 41  ? 0.1789 0.2000 0.2202 -0.0281 0.0241  -0.0321 41  VAL B O   
1192 C  CB  . VAL B 41  ? 0.1560 0.1604 0.2974 0.0064  0.0522  -0.0244 41  VAL B CB  
1193 C  CG1 . VAL B 41  ? 0.1708 0.1541 0.3282 -0.0080 0.0419  -0.0279 41  VAL B CG1 
1194 C  CG2 . VAL B 41  ? 0.1736 0.1815 0.3116 0.0068  0.0518  -0.0117 41  VAL B CG2 
1195 N  N   . VAL B 42  ? 0.1596 0.1394 0.2300 -0.0056 0.0330  -0.0325 42  VAL B N   
1196 C  CA  . VAL B 42  ? 0.1668 0.1393 0.2225 -0.0072 0.0335  -0.0158 42  VAL B CA  
1197 C  C   . VAL B 42  ? 0.1726 0.1504 0.2060 -0.0079 0.0341  -0.0135 42  VAL B C   
1198 O  O   . VAL B 42  ? 0.1793 0.1594 0.2086 -0.0232 0.0079  -0.0074 42  VAL B O   
1199 C  CB  . VAL B 42  ? 0.1724 0.1423 0.2405 0.0128  0.0499  -0.0061 42  VAL B CB  
1200 C  CG1 . VAL B 42  ? 0.1575 0.1731 0.2524 0.0314  0.0316  -0.0072 42  VAL B CG1 
1201 C  CG2 . VAL B 42  ? 0.2155 0.1463 0.2517 0.0027  0.0577  0.0044  42  VAL B CG2 
1202 N  N   . PRO B 43  ? 0.2068 0.1512 0.2173 -0.0080 0.0374  -0.0208 43  PRO B N   
1203 C  CA  . PRO B 43  ? 0.2115 0.1554 0.2225 -0.0065 0.0361  -0.0349 43  PRO B CA  
1204 C  C   . PRO B 43  ? 0.1956 0.1544 0.2164 -0.0161 0.0276  -0.0336 43  PRO B C   
1205 O  O   . PRO B 43  ? 0.1946 0.1589 0.2205 -0.0221 0.0145  -0.0299 43  PRO B O   
1206 C  CB  . PRO B 43  ? 0.2499 0.1776 0.2328 -0.0187 0.0452  -0.0411 43  PRO B CB  
1207 C  CG  . PRO B 43  ? 0.2802 0.1901 0.2376 -0.0187 0.0439  -0.0402 43  PRO B CG  
1208 C  CD  . PRO B 43  ? 0.2522 0.1701 0.2243 -0.0287 0.0420  -0.0299 43  PRO B CD  
1209 N  N   . ASP B 44  ? 0.1976 0.1616 0.2181 -0.0363 0.0272  -0.0270 44  ASP B N   
1210 C  CA  . ASP B 44  ? 0.1959 0.1989 0.2302 -0.0312 0.0208  -0.0483 44  ASP B CA  
1211 C  C   . ASP B 44  ? 0.2005 0.1830 0.2406 -0.0294 0.0155  -0.0325 44  ASP B C   
1212 O  O   . ASP B 44  ? 0.2005 0.1960 0.2650 -0.0349 0.0164  -0.0368 44  ASP B O   
1213 C  CB  . ASP B 44  ? 0.2412 0.2477 0.2580 -0.0489 0.0071  -0.0789 44  ASP B CB  
1214 C  CG  . ASP B 44  ? 0.3014 0.3116 0.3091 -0.0360 0.0100  -0.0689 44  ASP B CG  
1215 O  OD1 . ASP B 44  ? 0.3260 0.3209 0.3335 -0.0253 0.0069  -0.0770 44  ASP B OD1 
1216 O  OD2 . ASP B 44  ? 0.3233 0.3565 0.3298 -0.0398 0.0122  -0.0619 44  ASP B OD2 
1217 N  N   . GLN B 45  ? 0.1957 0.1412 0.2283 -0.0173 0.0228  -0.0163 45  GLN B N   
1218 C  CA  . GLN B 45  ? 0.1823 0.1346 0.2238 -0.0066 0.0138  -0.0025 45  GLN B CA  
1219 C  C   . GLN B 45  ? 0.1758 0.1401 0.2156 0.0037  0.0143  0.0060  45  GLN B C   
1220 O  O   . GLN B 45  ? 0.1832 0.1483 0.2361 0.0116  0.0242  0.0126  45  GLN B O   
1221 C  CB  . GLN B 45  ? 0.1783 0.1431 0.2255 -0.0182 0.0110  0.0114  45  GLN B CB  
1222 C  CG  . GLN B 45  ? 0.1788 0.1665 0.2170 -0.0189 0.0297  0.0110  45  GLN B CG  
1223 C  CD  . GLN B 45  ? 0.2016 0.1842 0.2129 -0.0053 0.0159  0.0003  45  GLN B CD  
1224 O  OE1 . GLN B 45  ? 0.2303 0.1796 0.2103 0.0354  0.0021  -0.0054 45  GLN B OE1 
1225 N  NE2 . GLN B 45  ? 0.2042 0.1847 0.2151 -0.0115 0.0149  0.0003  45  GLN B NE2 
1226 N  N   . LEU B 46  ? 0.1606 0.1412 0.1891 -0.0015 0.0203  0.0038  46  LEU B N   
1227 C  CA  . LEU B 46  ? 0.1659 0.1403 0.1945 -0.0055 0.0369  0.0010  46  LEU B CA  
1228 C  C   . LEU B 46  ? 0.1772 0.1302 0.1947 -0.0059 0.0160  -0.0028 46  LEU B C   
1229 O  O   . LEU B 46  ? 0.1889 0.1378 0.2039 -0.0056 0.0055  0.0023  46  LEU B O   
1230 C  CB  . LEU B 46  ? 0.1933 0.1589 0.2272 0.0023  0.0405  0.0117  46  LEU B CB  
1231 C  CG  . LEU B 46  ? 0.2387 0.1885 0.2578 0.0169  0.0281  0.0065  46  LEU B CG  
1232 N  N   . MET B 47  ? 0.1721 0.1467 0.2057 -0.0070 0.0101  -0.0015 47  MET B N   
1233 C  CA  . MET B 47  ? 0.1915 0.1760 0.2300 -0.0426 -0.0124 0.0117  47  MET B CA  
1234 C  C   . MET B 47  ? 0.2014 0.1441 0.2400 -0.0032 -0.0320 0.0075  47  MET B C   
1235 O  O   . MET B 47  ? 0.2576 0.1542 0.2665 -0.0030 -0.0554 -0.0057 47  MET B O   
1236 C  CB  . MET B 47  ? 0.2243 0.2773 0.2607 -0.0655 -0.0237 0.0153  47  MET B CB  
1237 C  CG  . MET B 47  ? 0.2386 0.3245 0.2834 -0.0544 0.0057  -0.0026 47  MET B CG  
1238 S  SD  . MET B 47  ? 0.2055 0.3042 0.2828 -0.0330 0.0482  -0.0274 47  MET B SD  
1239 C  CE  . MET B 47  ? 0.1794 0.3011 0.2805 0.0469  0.0639  0.0155  47  MET B CE  
1240 N  N   . ALA B 48  ? 0.1764 0.1311 0.2209 0.0033  -0.0167 0.0212  48  ALA B N   
1241 C  CA  . ALA B 48  ? 0.1820 0.1433 0.2303 -0.0039 -0.0107 0.0428  48  ALA B CA  
1242 C  C   . ALA B 48  ? 0.1737 0.1291 0.2244 0.0149  -0.0017 0.0355  48  ALA B C   
1243 O  O   . ALA B 48  ? 0.1724 0.1259 0.2220 0.0198  -0.0027 0.0349  48  ALA B O   
1244 C  CB  . ALA B 48  ? 0.1788 0.1718 0.2410 -0.0196 -0.0089 0.0535  48  ALA B CB  
1245 N  N   . PHE B 49  ? 0.1589 0.1431 0.2196 -0.0010 -0.0061 0.0414  49  PHE B N   
1246 C  CA  . PHE B 49  ? 0.1487 0.1596 0.2220 0.0064  0.0024  0.0426  49  PHE B CA  
1247 C  C   . PHE B 49  ? 0.1593 0.1625 0.2257 0.0001  0.0048  0.0419  49  PHE B C   
1248 O  O   . PHE B 49  ? 0.1712 0.1579 0.2392 -0.0027 0.0238  0.0361  49  PHE B O   
1249 C  CB  . PHE B 49  ? 0.1498 0.1812 0.2379 -0.0048 0.0128  0.0294  49  PHE B CB  
1250 C  CG  . PHE B 49  ? 0.1517 0.1887 0.2533 0.0039  0.0076  0.0264  49  PHE B CG  
1251 C  CD1 . PHE B 49  ? 0.1464 0.2330 0.2714 0.0128  -0.0088 0.0238  49  PHE B CD1 
1252 C  CD2 . PHE B 49  ? 0.1710 0.1724 0.2679 0.0016  0.0128  0.0257  49  PHE B CD2 
1253 C  CE1 . PHE B 49  ? 0.1686 0.2548 0.2938 0.0052  -0.0087 0.0186  49  PHE B CE1 
1254 C  CE2 . PHE B 49  ? 0.1835 0.1904 0.2908 0.0087  0.0043  0.0218  49  PHE B CE2 
1255 C  CZ  . PHE B 49  ? 0.1844 0.2294 0.2999 -0.0027 -0.0070 0.0151  49  PHE B CZ  
1256 N  N   . GLY B 50  ? 0.1694 0.1830 0.2281 -0.0010 0.0017  0.0382  50  GLY B N   
1257 C  CA  . GLY B 50  ? 0.1775 0.2088 0.2334 -0.0071 0.0031  0.0378  50  GLY B CA  
1258 C  C   . GLY B 50  ? 0.1890 0.2075 0.2343 -0.0161 0.0012  0.0539  50  GLY B C   
1259 O  O   . GLY B 50  ? 0.2210 0.2207 0.2393 -0.0093 0.0108  0.0747  50  GLY B O   
1260 N  N   . GLY B 51  ? 0.1796 0.2052 0.2340 -0.0262 0.0070  0.0478  51  GLY B N   
1261 C  CA  . GLY B 51  ? 0.2079 0.1929 0.2443 -0.0238 0.0166  0.0302  51  GLY B CA  
1262 C  C   . GLY B 51  ? 0.2098 0.1724 0.2619 -0.0294 0.0233  0.0152  51  GLY B C   
1263 O  O   . GLY B 51  ? 0.2332 0.1841 0.2904 -0.0474 0.0381  0.0272  51  GLY B O   
1264 N  N   . SER B 52  ? 0.2019 0.1483 0.2497 -0.0016 0.0120  0.0194  52  SER B N   
1265 C  CA  . SER B 52  ? 0.2250 0.1394 0.2573 -0.0062 0.0097  0.0293  52  SER B CA  
1266 C  C   . SER B 52  ? 0.2251 0.1306 0.2724 -0.0142 0.0025  0.0213  52  SER B C   
1267 O  O   . SER B 52  ? 0.2015 0.1155 0.2752 -0.0072 0.0085  0.0287  52  SER B O   
1268 C  CB  . SER B 52  ? 0.2355 0.1604 0.2624 0.0235  0.0178  0.0320  52  SER B CB  
1269 O  OG  . SER B 52  ? 0.2360 0.1727 0.2668 0.0037  0.0220  0.0432  52  SER B OG  
1270 N  N   . SER B 53  ? 0.2385 0.1432 0.2884 -0.0237 -0.0079 0.0143  53  SER B N   
1271 C  CA  . SER B 53  ? 0.2401 0.1758 0.3046 -0.0388 -0.0348 0.0057  53  SER B CA  
1272 C  C   . SER B 53  ? 0.2328 0.1642 0.3094 -0.0379 -0.0134 0.0200  53  SER B C   
1273 O  O   . SER B 53  ? 0.2385 0.1611 0.3004 -0.0434 -0.0160 0.0132  53  SER B O   
1274 C  CB  . SER B 53  ? 0.2507 0.2198 0.3282 -0.0399 -0.0547 0.0007  53  SER B CB  
1275 O  OG  . SER B 53  ? 0.2710 0.2524 0.3458 -0.0494 -0.0538 -0.0031 53  SER B OG  
1276 N  N   . GLU B 54  ? 0.2165 0.1428 0.3163 -0.0302 0.0096  0.0274  54  GLU B N   
1277 C  CA  . GLU B 54  ? 0.2378 0.1349 0.3273 0.0038  0.0336  0.0344  54  GLU B CA  
1278 C  C   . GLU B 54  ? 0.2336 0.1241 0.3027 -0.0002 0.0325  0.0261  54  GLU B C   
1279 O  O   . GLU B 54  ? 0.2311 0.1129 0.2828 -0.0002 0.0252  0.0216  54  GLU B O   
1280 C  CB  . GLU B 54  ? 0.2890 0.1507 0.3648 -0.0089 0.0572  0.0443  54  GLU B CB  
1281 C  CG  . GLU B 54  ? 0.3505 0.1843 0.4016 -0.0425 0.0867  0.0266  54  GLU B CG  
1282 C  CD  . GLU B 54  ? 0.4133 0.2508 0.4313 -0.0739 0.1123  0.0102  54  GLU B CD  
1283 O  OE1 . GLU B 54  ? 0.4628 0.3105 0.4446 -0.1005 0.1212  -0.0031 54  GLU B OE1 
1284 O  OE2 . GLU B 54  ? 0.4314 0.2383 0.4401 -0.0637 0.1135  0.0171  54  GLU B OE2 
1285 N  N   . PRO B 55  ? 0.2530 0.1353 0.2994 -0.0183 0.0409  0.0103  55  PRO B N   
1286 C  CA  . PRO B 55  ? 0.2400 0.1461 0.2889 -0.0149 0.0372  -0.0052 55  PRO B CA  
1287 C  C   . PRO B 55  ? 0.2155 0.1372 0.2766 -0.0082 0.0288  0.0124  55  PRO B C   
1288 O  O   . PRO B 55  ? 0.1865 0.1457 0.2802 0.0121  0.0188  0.0221  55  PRO B O   
1289 C  CB  . PRO B 55  ? 0.2500 0.1571 0.2939 -0.0068 0.0453  -0.0356 55  PRO B CB  
1290 C  CG  . PRO B 55  ? 0.2632 0.1581 0.2952 -0.0145 0.0661  -0.0422 55  PRO B CG  
1291 C  CD  . PRO B 55  ? 0.2779 0.1584 0.3001 -0.0171 0.0659  -0.0202 55  PRO B CD  
1292 N  N   . CYS B 56  ? 0.2052 0.1254 0.2596 -0.0154 0.0482  0.0264  56  CYS B N   
1293 C  CA  . CYS B 56  ? 0.2009 0.1355 0.2503 -0.0089 0.0276  0.0209  56  CYS B CA  
1294 C  C   . CYS B 56  ? 0.1855 0.1173 0.2443 -0.0011 0.0198  0.0236  56  CYS B C   
1295 O  O   . CYS B 56  ? 0.2015 0.1251 0.2394 0.0023  0.0139  0.0202  56  CYS B O   
1296 C  CB  . CYS B 56  ? 0.1828 0.1600 0.2462 0.0029  0.0122  0.0174  56  CYS B CB  
1297 S  SG  . CYS B 56  ? 0.1923 0.1942 0.2582 0.0151  0.0085  0.0125  56  CYS B SG  
1298 N  N   . ALA B 57  ? 0.1756 0.1103 0.2488 -0.0012 0.0228  0.0245  57  ALA B N   
1299 C  CA  . ALA B 57  ? 0.1896 0.1353 0.2390 0.0114  0.0254  0.0255  57  ALA B CA  
1300 C  C   . ALA B 57  ? 0.1759 0.1255 0.2240 0.0068  0.0125  0.0323  57  ALA B C   
1301 O  O   . ALA B 57  ? 0.1905 0.1500 0.2336 -0.0016 -0.0110 0.0331  57  ALA B O   
1302 C  CB  . ALA B 57  ? 0.2107 0.1582 0.2395 -0.0064 0.0376  0.0222  57  ALA B CB  
1303 N  N   . LEU B 58  ? 0.1683 0.1209 0.2221 0.0062  0.0293  0.0276  58  LEU B N   
1304 C  CA  . LEU B 58  ? 0.1813 0.1404 0.2050 -0.0008 0.0232  0.0200  58  LEU B CA  
1305 C  C   . LEU B 58  ? 0.1759 0.1306 0.1977 -0.0070 0.0135  0.0128  58  LEU B C   
1306 O  O   . LEU B 58  ? 0.1794 0.1456 0.2037 -0.0062 0.0152  0.0091  58  LEU B O   
1307 C  CB  . LEU B 58  ? 0.1872 0.1817 0.2112 0.0086  0.0249  0.0137  58  LEU B CB  
1308 C  CG  . LEU B 58  ? 0.1984 0.2186 0.2315 0.0103  0.0222  0.0197  58  LEU B CG  
1309 C  CD1 . LEU B 58  ? 0.1884 0.2346 0.2483 0.0141  0.0261  0.0146  58  LEU B CD1 
1310 C  CD2 . LEU B 58  ? 0.2180 0.2254 0.2356 0.0102  0.0090  0.0295  58  LEU B CD2 
1311 N  N   . CYS B 59  ? 0.1812 0.1434 0.2007 -0.0175 0.0114  0.0114  59  CYS B N   
1312 C  CA  . CYS B 59  ? 0.1776 0.1476 0.2130 -0.0079 0.0175  0.0132  59  CYS B CA  
1313 C  C   . CYS B 59  ? 0.1660 0.1440 0.1864 -0.0031 0.0181  0.0192  59  CYS B C   
1314 O  O   . CYS B 59  ? 0.1732 0.1538 0.1798 -0.0050 0.0152  0.0119  59  CYS B O   
1315 C  CB  . CYS B 59  ? 0.1910 0.1362 0.2527 0.0106  0.0059  0.0125  59  CYS B CB  
1316 S  SG  . CYS B 59  ? 0.2094 0.1572 0.2765 0.0074  0.0199  0.0121  59  CYS B SG  
1317 N  N   . SER B 60  ? 0.1687 0.1303 0.1914 -0.0039 0.0258  0.0156  60  SER B N   
1318 C  CA  . SER B 60  ? 0.1728 0.1401 0.1947 -0.0099 0.0205  0.0102  60  SER B CA  
1319 C  C   . SER B 60  ? 0.1645 0.1502 0.1919 -0.0128 0.0088  0.0131  60  SER B C   
1320 O  O   . SER B 60  ? 0.1762 0.1816 0.1880 -0.0293 0.0023  -0.0014 60  SER B O   
1321 C  CB  . SER B 60  ? 0.1968 0.1483 0.1975 0.0135  0.0188  0.0080  60  SER B CB  
1322 O  OG  . SER B 60  ? 0.2072 0.1747 0.2121 0.0193  0.0196  0.0110  60  SER B OG  
1323 N  N   . LEU B 61  ? 0.1341 0.1551 0.2059 -0.0130 0.0069  0.0140  61  LEU B N   
1324 C  CA  . LEU B 61  ? 0.1478 0.1661 0.2046 -0.0041 0.0065  0.0104  61  LEU B CA  
1325 C  C   . LEU B 61  ? 0.1625 0.1593 0.1941 -0.0096 0.0160  0.0101  61  LEU B C   
1326 O  O   . LEU B 61  ? 0.1731 0.1547 0.1901 -0.0258 0.0090  0.0061  61  LEU B O   
1327 C  CB  . LEU B 61  ? 0.1353 0.1725 0.2116 0.0110  0.0069  0.0159  61  LEU B CB  
1328 C  CG  . LEU B 61  ? 0.1417 0.2220 0.2246 0.0084  0.0288  0.0113  61  LEU B CG  
1329 C  CD1 . LEU B 61  ? 0.1667 0.2441 0.2228 0.0087  0.0381  0.0207  61  LEU B CD1 
1330 C  CD2 . LEU B 61  ? 0.1536 0.2463 0.2466 0.0131  0.0286  0.0188  61  LEU B CD2 
1331 N  N   . HIS B 62  ? 0.1580 0.1432 0.1999 -0.0190 0.0227  0.0201  62  HIS B N   
1332 C  CA  . HIS B 62  ? 0.1368 0.1550 0.2066 -0.0255 0.0251  0.0179  62  HIS B CA  
1333 C  C   . HIS B 62  ? 0.1623 0.1710 0.1958 -0.0427 0.0318  0.0080  62  HIS B C   
1334 O  O   . HIS B 62  ? 0.1872 0.1766 0.1842 -0.0375 0.0264  0.0040  62  HIS B O   
1335 C  CB  . HIS B 62  ? 0.1341 0.1785 0.2216 -0.0008 0.0080  0.0322  62  HIS B CB  
1336 C  CG  . HIS B 62  ? 0.1451 0.1961 0.2358 0.0003  -0.0145 0.0398  62  HIS B CG  
1337 N  ND1 . HIS B 62  ? 0.1723 0.2063 0.2516 -0.0146 -0.0168 0.0376  62  HIS B ND1 
1338 C  CD2 . HIS B 62  ? 0.1627 0.2184 0.2421 0.0023  -0.0149 0.0503  62  HIS B CD2 
1339 C  CE1 . HIS B 62  ? 0.1846 0.2066 0.2593 -0.0112 -0.0157 0.0527  62  HIS B CE1 
1340 N  NE2 . HIS B 62  ? 0.1694 0.2272 0.2595 0.0006  -0.0172 0.0646  62  HIS B NE2 
1341 N  N   . SER B 63  ? 0.1702 0.1759 0.1999 -0.0416 0.0287  0.0143  63  SER B N   
1342 C  CA  . SER B 63  ? 0.1632 0.1692 0.2167 -0.0168 0.0337  0.0013  63  SER B CA  
1343 C  C   . SER B 63  ? 0.1576 0.1666 0.2053 -0.0239 0.0195  -0.0038 63  SER B C   
1344 O  O   . SER B 63  ? 0.1754 0.1659 0.1868 -0.0172 0.0253  0.0051  63  SER B O   
1345 C  CB  . SER B 63  ? 0.1612 0.1822 0.2330 -0.0048 0.0446  -0.0069 63  SER B CB  
1346 O  OG  . SER B 63  ? 0.1724 0.2089 0.2384 -0.0120 0.0380  -0.0164 63  SER B OG  
1347 N  N   . ILE B 64  ? 0.1593 0.1760 0.2076 -0.0447 0.0200  0.0032  64  ILE B N   
1348 C  CA  . ILE B 64  ? 0.1638 0.1836 0.2149 -0.0392 0.0224  0.0160  64  ILE B CA  
1349 C  C   . ILE B 64  ? 0.1762 0.2000 0.2321 -0.0297 0.0259  0.0134  64  ILE B C   
1350 O  O   . ILE B 64  ? 0.1845 0.2048 0.2401 -0.0376 0.0346  0.0011  64  ILE B O   
1351 C  CB  . ILE B 64  ? 0.1673 0.1823 0.2118 -0.0237 0.0239  0.0128  64  ILE B CB  
1352 C  CG1 . ILE B 64  ? 0.1807 0.2090 0.2016 -0.0112 0.0181  0.0228  64  ILE B CG1 
1353 C  CG2 . ILE B 64  ? 0.1841 0.1707 0.2128 -0.0329 0.0298  0.0002  64  ILE B CG2 
1354 C  CD1 . ILE B 64  ? 0.2104 0.2163 0.1977 -0.0045 0.0189  0.0331  64  ILE B CD1 
1355 N  N   . GLY B 65  ? 0.1658 0.1897 0.2348 -0.0243 0.0099  0.0090  65  GLY B N   
1356 C  CA  . GLY B 65  ? 0.1595 0.1935 0.2497 -0.0338 0.0030  0.0108  65  GLY B CA  
1357 C  C   . GLY B 65  ? 0.1690 0.2111 0.2556 -0.0449 0.0050  0.0180  65  GLY B C   
1358 O  O   . GLY B 65  ? 0.1809 0.2166 0.2526 -0.0430 0.0059  0.0197  65  GLY B O   
1359 N  N   . LYS B 66  ? 0.1636 0.2293 0.2620 -0.0436 0.0164  0.0091  66  LYS B N   
1360 C  CA  . LYS B 66  ? 0.1931 0.2457 0.2734 -0.0376 0.0279  0.0137  66  LYS B CA  
1361 C  C   . LYS B 66  ? 0.1670 0.2314 0.2641 -0.0144 0.0290  0.0239  66  LYS B C   
1362 O  O   . LYS B 66  ? 0.1836 0.2131 0.2710 -0.0121 0.0430  0.0167  66  LYS B O   
1363 C  CB  . LYS B 66  ? 0.2566 0.2872 0.3015 -0.0550 0.0362  0.0033  66  LYS B CB  
1364 C  CG  . LYS B 66  ? 0.3186 0.3524 0.3456 -0.0653 0.0303  -0.0030 66  LYS B CG  
1365 C  CD  . LYS B 66  ? 0.3545 0.3911 0.3967 -0.0601 0.0215  -0.0048 66  LYS B CD  
1366 C  CE  . LYS B 66  ? 0.4158 0.4201 0.4373 -0.0340 0.0236  -0.0014 66  LYS B CE  
1367 N  NZ  . LYS B 66  ? 0.4500 0.4373 0.4595 -0.0218 0.0282  0.0054  66  LYS B NZ  
1368 N  N   . ILE B 67  ? 0.1650 0.2289 0.2391 -0.0096 0.0166  0.0408  67  ILE B N   
1369 C  CA  . ILE B 67  ? 0.1739 0.2266 0.2356 -0.0147 0.0040  0.0406  67  ILE B CA  
1370 C  C   . ILE B 67  ? 0.1775 0.2320 0.2391 -0.0122 -0.0068 0.0453  67  ILE B C   
1371 O  O   . ILE B 67  ? 0.2095 0.2405 0.2542 -0.0218 -0.0117 0.0429  67  ILE B O   
1372 C  CB  . ILE B 67  ? 0.1805 0.1999 0.2412 0.0129  -0.0045 0.0235  67  ILE B CB  
1373 C  CG1 . ILE B 67  ? 0.1841 0.1988 0.2526 0.0167  -0.0066 0.0190  67  ILE B CG1 
1374 C  CG2 . ILE B 67  ? 0.1999 0.2042 0.2458 -0.0020 0.0034  0.0122  67  ILE B CG2 
1375 C  CD1 . ILE B 67  ? 0.1947 0.1834 0.2517 0.0224  -0.0094 0.0261  67  ILE B CD1 
1376 N  N   . GLY B 68  ? 0.1731 0.2387 0.2368 0.0102  -0.0207 0.0534  68  GLY B N   
1377 C  CA  . GLY B 68  ? 0.1957 0.2434 0.2509 0.0097  -0.0259 0.0432  68  GLY B CA  
1378 C  C   . GLY B 68  ? 0.2007 0.2492 0.2634 0.0209  -0.0238 0.0342  68  GLY B C   
1379 O  O   . GLY B 68  ? 0.1836 0.2168 0.2631 0.0091  -0.0192 0.0203  68  GLY B O   
1380 N  N   . GLY B 69  ? 0.2186 0.2735 0.2636 0.0030  -0.0280 0.0391  69  GLY B N   
1381 C  CA  . GLY B 69  ? 0.2186 0.2832 0.2654 -0.0056 -0.0106 0.0439  69  GLY B CA  
1382 C  C   . GLY B 69  ? 0.1896 0.2967 0.2788 0.0127  -0.0037 0.0424  69  GLY B C   
1383 O  O   . GLY B 69  ? 0.1844 0.2933 0.2775 0.0102  -0.0018 0.0339  69  GLY B O   
1384 N  N   . ALA B 70  ? 0.1765 0.3062 0.2927 0.0190  -0.0014 0.0436  70  ALA B N   
1385 C  CA  . ALA B 70  ? 0.1659 0.3072 0.3040 0.0166  -0.0061 0.0333  70  ALA B CA  
1386 C  C   . ALA B 70  ? 0.1670 0.2812 0.3033 0.0127  -0.0067 0.0388  70  ALA B C   
1387 O  O   . ALA B 70  ? 0.1661 0.2689 0.3126 0.0130  -0.0131 0.0401  70  ALA B O   
1388 C  CB  . ALA B 70  ? 0.1570 0.3421 0.3133 0.0215  -0.0063 0.0173  70  ALA B CB  
1389 N  N   . GLN B 71  ? 0.1429 0.2598 0.2871 0.0096  -0.0043 0.0451  71  GLN B N   
1390 C  CA  . GLN B 71  ? 0.1480 0.2371 0.2852 0.0193  0.0015  0.0384  71  GLN B CA  
1391 C  C   . GLN B 71  ? 0.1509 0.2401 0.2942 0.0366  0.0096  0.0245  71  GLN B C   
1392 O  O   . GLN B 71  ? 0.1585 0.2454 0.3033 0.0425  0.0002  0.0242  71  GLN B O   
1393 C  CB  . GLN B 71  ? 0.1716 0.2363 0.2965 0.0070  0.0087  0.0342  71  GLN B CB  
1394 C  CG  . GLN B 71  ? 0.1932 0.2626 0.3017 -0.0156 0.0128  0.0294  71  GLN B CG  
1395 C  CD  . GLN B 71  ? 0.2174 0.2825 0.2932 -0.0111 0.0122  0.0316  71  GLN B CD  
1396 O  OE1 . GLN B 71  ? 0.2559 0.2951 0.2917 0.0044  0.0192  0.0467  71  GLN B OE1 
1397 N  NE2 . GLN B 71  ? 0.2150 0.2911 0.2921 -0.0163 -0.0006 0.0263  71  GLN B NE2 
1398 N  N   . ASN B 72  ? 0.1390 0.2259 0.2967 0.0424  0.0054  0.0333  72  ASN B N   
1399 C  CA  . ASN B 72  ? 0.1344 0.2136 0.2967 0.0235  0.0098  0.0268  72  ASN B CA  
1400 C  C   . ASN B 72  ? 0.1525 0.2241 0.3111 0.0248  0.0064  0.0299  72  ASN B C   
1401 O  O   . ASN B 72  ? 0.1541 0.2195 0.3154 0.0244  0.0072  0.0339  72  ASN B O   
1402 C  CB  . ASN B 72  ? 0.1599 0.1930 0.2729 0.0217  0.0148  0.0220  72  ASN B CB  
1403 C  CG  . ASN B 72  ? 0.1693 0.1997 0.2625 -0.0022 0.0044  0.0262  72  ASN B CG  
1404 O  OD1 . ASN B 72  ? 0.1697 0.2213 0.2684 -0.0008 0.0009  0.0187  72  ASN B OD1 
1405 N  ND2 . ASN B 72  ? 0.1752 0.1905 0.2467 -0.0137 -0.0005 0.0244  72  ASN B ND2 
1406 N  N   . ARG B 73  ? 0.1814 0.2288 0.3195 0.0400  0.0075  0.0439  73  ARG B N   
1407 C  CA  . ARG B 73  ? 0.1895 0.2431 0.3317 0.0459  -0.0014 0.0492  73  ARG B CA  
1408 C  C   . ARG B 73  ? 0.1796 0.2510 0.3419 0.0428  0.0029  0.0292  73  ARG B C   
1409 O  O   . ARG B 73  ? 0.1889 0.2383 0.3482 0.0496  0.0005  0.0253  73  ARG B O   
1410 C  CB  . ARG B 73  ? 0.2110 0.2613 0.3376 0.0451  -0.0134 0.0641  73  ARG B CB  
1411 C  CG  . ARG B 73  ? 0.2461 0.2933 0.3482 0.0207  -0.0263 0.0745  73  ARG B CG  
1412 C  CD  . ARG B 73  ? 0.2735 0.3355 0.3614 0.0122  -0.0343 0.0787  73  ARG B CD  
1413 N  NE  . ARG B 73  ? 0.3103 0.3680 0.3738 -0.0016 -0.0396 0.0802  73  ARG B NE  
1414 C  CZ  . ARG B 73  ? 0.3292 0.3912 0.3787 -0.0227 -0.0390 0.0830  73  ARG B CZ  
1415 N  NH1 . ARG B 73  ? 0.3334 0.3975 0.3735 -0.0250 -0.0353 0.0887  73  ARG B NH1 
1416 N  NH2 . ARG B 73  ? 0.3492 0.4038 0.3877 -0.0403 -0.0326 0.0849  73  ARG B NH2 
1417 N  N   . SER B 74  ? 0.1579 0.2569 0.3368 0.0420  0.0171  0.0251  74  SER B N   
1418 C  CA  . SER B 74  ? 0.1514 0.2649 0.3498 0.0249  0.0297  0.0145  74  SER B CA  
1419 C  C   . SER B 74  ? 0.1500 0.2280 0.3509 0.0378  0.0236  0.0150  74  SER B C   
1420 O  O   . SER B 74  ? 0.1662 0.2158 0.3712 0.0453  0.0151  0.0061  74  SER B O   
1421 C  CB  . SER B 74  ? 0.1783 0.3034 0.3695 0.0125  0.0483  0.0024  74  SER B CB  
1422 O  OG  . SER B 74  ? 0.2054 0.3278 0.3840 0.0015  0.0463  -0.0094 74  SER B OG  
1423 N  N   . TYR B 75  ? 0.1435 0.2228 0.3332 0.0327  0.0264  0.0275  75  TYR B N   
1424 C  CA  . TYR B 75  ? 0.1453 0.2164 0.3281 0.0209  0.0344  0.0311  75  TYR B CA  
1425 C  C   . TYR B 75  ? 0.1489 0.2043 0.3313 0.0327  0.0378  0.0262  75  TYR B C   
1426 O  O   . TYR B 75  ? 0.1730 0.1892 0.3369 0.0320  0.0349  0.0150  75  TYR B O   
1427 C  CB  . TYR B 75  ? 0.1478 0.2004 0.3226 0.0112  0.0392  0.0353  75  TYR B CB  
1428 C  CG  . TYR B 75  ? 0.1649 0.2086 0.3193 -0.0047 0.0414  0.0240  75  TYR B CG  
1429 C  CD1 . TYR B 75  ? 0.2259 0.2242 0.3221 -0.0189 0.0629  0.0137  75  TYR B CD1 
1430 C  CD2 . TYR B 75  ? 0.1693 0.2006 0.3105 0.0013  0.0204  0.0271  75  TYR B CD2 
1431 C  CE1 . TYR B 75  ? 0.2478 0.2293 0.3216 -0.0138 0.0656  0.0156  75  TYR B CE1 
1432 C  CE2 . TYR B 75  ? 0.1857 0.2096 0.3075 -0.0120 0.0245  0.0344  75  TYR B CE2 
1433 C  CZ  . TYR B 75  ? 0.2300 0.2262 0.3223 -0.0187 0.0538  0.0214  75  TYR B CZ  
1434 O  OH  . TYR B 75  ? 0.2387 0.2317 0.3375 -0.0226 0.0776  0.0180  75  TYR B OH  
1435 N  N   . SER B 76  ? 0.1455 0.1954 0.3253 0.0242  0.0469  0.0380  76  SER B N   
1436 C  CA  . SER B 76  ? 0.1670 0.1824 0.3344 0.0236  0.0375  0.0392  76  SER B CA  
1437 C  C   . SER B 76  ? 0.1683 0.1955 0.3623 0.0409  0.0308  0.0327  76  SER B C   
1438 O  O   . SER B 76  ? 0.1854 0.2073 0.3717 0.0314  0.0282  0.0501  76  SER B O   
1439 C  CB  . SER B 76  ? 0.1867 0.2037 0.3232 0.0310  0.0226  0.0368  76  SER B CB  
1440 O  OG  . SER B 76  ? 0.1938 0.2326 0.3092 0.0560  0.0161  0.0332  76  SER B OG  
1441 N  N   . LYS B 77  ? 0.1560 0.2058 0.3792 0.0505  0.0286  0.0246  77  LYS B N   
1442 C  CA  . LYS B 77  ? 0.1607 0.2220 0.4042 0.0715  0.0203  0.0103  77  LYS B CA  
1443 C  C   . LYS B 77  ? 0.1723 0.2163 0.3968 0.0670  0.0128  0.0143  77  LYS B C   
1444 O  O   . LYS B 77  ? 0.1930 0.2154 0.4045 0.0339  0.0039  0.0070  77  LYS B O   
1445 C  CB  . LYS B 77  ? 0.1748 0.2404 0.4397 0.0741  0.0064  0.0037  77  LYS B CB  
1446 C  CG  . LYS B 77  ? 0.2168 0.2753 0.4712 0.0792  -0.0181 0.0078  77  LYS B CG  
1447 C  CD  . LYS B 77  ? 0.2525 0.3240 0.5021 0.1035  -0.0335 0.0163  77  LYS B CD  
1448 C  CE  . LYS B 77  ? 0.2731 0.3741 0.5282 0.1245  -0.0401 0.0186  77  LYS B CE  
1449 N  NZ  . LYS B 77  ? 0.2953 0.4156 0.5407 0.1231  -0.0427 0.0205  77  LYS B NZ  
1450 N  N   . LEU B 78  ? 0.1709 0.2283 0.3837 0.0600  0.0294  0.0243  78  LEU B N   
1451 C  CA  . LEU B 78  ? 0.1868 0.2192 0.3717 0.0433  0.0348  0.0235  78  LEU B CA  
1452 C  C   . LEU B 78  ? 0.1862 0.2037 0.3622 0.0431  0.0362  0.0074  78  LEU B C   
1453 O  O   . LEU B 78  ? 0.1977 0.2156 0.3640 0.0467  0.0534  -0.0121 78  LEU B O   
1454 C  CB  . LEU B 78  ? 0.2072 0.2359 0.3698 0.0131  0.0436  0.0236  78  LEU B CB  
1455 C  CG  . LEU B 78  ? 0.2601 0.2577 0.3707 0.0075  0.0550  0.0121  78  LEU B CG  
1456 C  CD1 . LEU B 78  ? 0.2741 0.2818 0.3779 0.0251  0.0632  0.0005  78  LEU B CD1 
1457 C  CD2 . LEU B 78  ? 0.2832 0.2604 0.3663 0.0035  0.0593  0.0237  78  LEU B CD2 
1458 N  N   . LEU B 79  ? 0.1784 0.1973 0.3484 0.0393  0.0359  0.0045  79  LEU B N   
1459 C  CA  . LEU B 79  ? 0.1894 0.1885 0.3417 0.0294  0.0295  -0.0061 79  LEU B CA  
1460 C  C   . LEU B 79  ? 0.1870 0.2039 0.3423 0.0210  0.0343  0.0046  79  LEU B C   
1461 O  O   . LEU B 79  ? 0.1869 0.2027 0.3386 0.0220  0.0339  0.0001  79  LEU B O   
1462 C  CB  . LEU B 79  ? 0.2211 0.1822 0.3287 0.0272  0.0128  -0.0270 79  LEU B CB  
1463 C  CG  . LEU B 79  ? 0.2463 0.2075 0.3236 0.0246  -0.0006 -0.0321 79  LEU B CG  
1464 C  CD1 . LEU B 79  ? 0.2417 0.2100 0.3213 0.0220  0.0032  -0.0386 79  LEU B CD1 
1465 C  CD2 . LEU B 79  ? 0.2723 0.2255 0.3289 0.0272  -0.0140 -0.0271 79  LEU B CD2 
1466 N  N   . CYS B 80  ? 0.2006 0.2033 0.3503 0.0161  0.0397  0.0092  80  CYS B N   
1467 C  CA  . CYS B 80  ? 0.2153 0.1969 0.3560 0.0080  0.0376  0.0022  80  CYS B CA  
1468 C  C   . CYS B 80  ? 0.2175 0.1967 0.3716 0.0179  0.0339  -0.0006 80  CYS B C   
1469 O  O   . CYS B 80  ? 0.2266 0.2054 0.3775 0.0154  0.0257  -0.0055 80  CYS B O   
1470 C  CB  . CYS B 80  ? 0.2396 0.2064 0.3542 0.0144  0.0319  0.0126  80  CYS B CB  
1471 S  SG  . CYS B 80  ? 0.2189 0.2087 0.3550 0.0209  0.0296  0.0160  80  CYS B SG  
1472 N  N   . GLY B 81  ? 0.2152 0.1923 0.3831 0.0272  0.0437  0.0029  81  GLY B N   
1473 C  CA  . GLY B 81  ? 0.2086 0.1905 0.3976 0.0421  0.0557  -0.0052 81  GLY B CA  
1474 C  C   . GLY B 81  ? 0.2100 0.2042 0.4098 0.0364  0.0631  -0.0065 81  GLY B C   
1475 O  O   . GLY B 81  ? 0.2191 0.2071 0.4222 0.0283  0.0606  -0.0027 81  GLY B O   
1476 N  N   . LEU B 82  ? 0.2040 0.2063 0.4021 0.0480  0.0676  -0.0153 82  LEU B N   
1477 C  CA  . LEU B 82  ? 0.2388 0.2071 0.3987 0.0377  0.0697  -0.0200 82  LEU B CA  
1478 C  C   . LEU B 82  ? 0.2328 0.2031 0.3857 0.0321  0.0723  -0.0147 82  LEU B C   
1479 O  O   . LEU B 82  ? 0.2472 0.2208 0.3815 0.0239  0.0820  -0.0233 82  LEU B O   
1480 C  CB  . LEU B 82  ? 0.2792 0.2167 0.4108 0.0179  0.0807  -0.0257 82  LEU B CB  
1481 C  CG  . LEU B 82  ? 0.3225 0.2469 0.4241 0.0238  0.0857  -0.0364 82  LEU B CG  
1482 C  CD1 . LEU B 82  ? 0.3276 0.2530 0.4316 0.0166  0.0761  -0.0195 82  LEU B CD1 
1483 C  CD2 . LEU B 82  ? 0.3434 0.2582 0.4267 0.0242  0.1021  -0.0552 82  LEU B CD2 
1484 N  N   . LEU B 83  ? 0.2076 0.1853 0.3783 0.0412  0.0620  -0.0059 83  LEU B N   
1485 C  CA  . LEU B 83  ? 0.1959 0.1670 0.3704 0.0264  0.0536  -0.0119 83  LEU B CA  
1486 C  C   . LEU B 83  ? 0.1921 0.1764 0.3860 0.0292  0.0485  -0.0136 83  LEU B C   
1487 O  O   . LEU B 83  ? 0.1893 0.1862 0.3895 0.0034  0.0488  -0.0198 83  LEU B O   
1488 C  CB  . LEU B 83  ? 0.2111 0.1636 0.3508 0.0106  0.0452  -0.0142 83  LEU B CB  
1489 C  CG  . LEU B 83  ? 0.2322 0.1781 0.3425 0.0174  0.0354  -0.0041 83  LEU B CG  
1490 C  CD1 . LEU B 83  ? 0.2585 0.1937 0.3425 0.0292  0.0382  0.0027  83  LEU B CD1 
1491 C  CD2 . LEU B 83  ? 0.2536 0.1995 0.3437 0.0120  0.0201  -0.0049 83  LEU B CD2 
1492 N  N   . ALA B 84  ? 0.2087 0.1703 0.4063 0.0392  0.0412  -0.0121 84  ALA B N   
1493 C  CA  . ALA B 84  ? 0.2300 0.1776 0.4297 0.0381  0.0246  -0.0114 84  ALA B CA  
1494 C  C   . ALA B 84  ? 0.2583 0.1797 0.4452 0.0494  0.0355  -0.0251 84  ALA B C   
1495 O  O   . ALA B 84  ? 0.2904 0.1735 0.4568 0.0438  0.0324  -0.0261 84  ALA B O   
1496 C  CB  . ALA B 84  ? 0.2321 0.1897 0.4319 0.0334  0.0017  0.0041  84  ALA B CB  
1497 N  N   . GLU B 85  ? 0.2622 0.2015 0.4446 0.0432  0.0362  -0.0355 85  GLU B N   
1498 C  CA  . GLU B 85  ? 0.2832 0.2293 0.4427 0.0289  0.0495  -0.0531 85  GLU B CA  
1499 C  C   . GLU B 85  ? 0.3112 0.2137 0.4394 0.0216  0.0655  -0.0647 85  GLU B C   
1500 O  O   . GLU B 85  ? 0.3495 0.2357 0.4437 0.0098  0.0659  -0.0633 85  GLU B O   
1501 C  CB  . GLU B 85  ? 0.2930 0.2649 0.4452 0.0278  0.0526  -0.0523 85  GLU B CB  
1502 N  N   . ARG B 86  ? 0.2999 0.1941 0.4337 0.0209  0.0829  -0.0643 86  ARG B N   
1503 C  CA  . ARG B 86  ? 0.2943 0.1897 0.4319 0.0131  0.0938  -0.0764 86  ARG B CA  
1504 C  C   . ARG B 86  ? 0.2821 0.1925 0.4156 0.0090  0.0861  -0.0827 86  ARG B C   
1505 O  O   . ARG B 86  ? 0.2941 0.2359 0.4123 0.0012  0.0722  -0.0971 86  ARG B O   
1506 C  CB  . ARG B 86  ? 0.2940 0.2003 0.4492 0.0207  0.1153  -0.0808 86  ARG B CB  
1507 C  CG  . ARG B 86  ? 0.2939 0.2160 0.4698 0.0262  0.1354  -0.0719 86  ARG B CG  
1508 C  CD  . ARG B 86  ? 0.3046 0.2540 0.4912 0.0370  0.1476  -0.0546 86  ARG B CD  
1509 N  NE  . ARG B 86  ? 0.3194 0.2901 0.5090 0.0406  0.1542  -0.0522 86  ARG B NE  
1510 C  CZ  . ARG B 86  ? 0.3389 0.3063 0.5303 0.0482  0.1483  -0.0473 86  ARG B CZ  
1511 N  NH1 . ARG B 86  ? 0.3605 0.3115 0.5366 0.0473  0.1410  -0.0541 86  ARG B NH1 
1512 N  NH2 . ARG B 86  ? 0.3322 0.3067 0.5387 0.0535  0.1525  -0.0464 86  ARG B NH2 
1513 N  N   . LEU B 87  ? 0.2599 0.1833 0.4063 0.0227  0.0853  -0.0699 87  LEU B N   
1514 C  CA  . LEU B 87  ? 0.2641 0.1869 0.4054 0.0126  0.0614  -0.0544 87  LEU B CA  
1515 C  C   . LEU B 87  ? 0.2621 0.1865 0.4140 0.0021  0.0467  -0.0472 87  LEU B C   
1516 O  O   . LEU B 87  ? 0.2624 0.2018 0.4101 0.0075  0.0502  -0.0406 87  LEU B O   
1517 C  CB  . LEU B 87  ? 0.2692 0.1870 0.3970 0.0244  0.0451  -0.0531 87  LEU B CB  
1518 C  CG  . LEU B 87  ? 0.2863 0.2263 0.3958 0.0403  0.0345  -0.0422 87  LEU B CG  
1519 C  CD1 . LEU B 87  ? 0.2757 0.2170 0.3861 0.0445  0.0319  -0.0455 87  LEU B CD1 
1520 C  CD2 . LEU B 87  ? 0.3097 0.2576 0.3973 0.0512  0.0319  -0.0435 87  LEU B CD2 
1521 N  N   . ARG B 88  ? 0.2573 0.1739 0.4270 0.0115  0.0511  -0.0437 88  ARG B N   
1522 C  CA  . ARG B 88  ? 0.2841 0.1821 0.4527 -0.0044 0.0497  -0.0208 88  ARG B CA  
1523 C  C   . ARG B 88  ? 0.2691 0.1686 0.4362 -0.0021 0.0604  -0.0068 88  ARG B C   
1524 O  O   . ARG B 88  ? 0.2893 0.1768 0.4484 -0.0071 0.0578  -0.0015 88  ARG B O   
1525 C  CB  . ARG B 88  ? 0.3324 0.2325 0.5010 -0.0077 0.0417  -0.0173 88  ARG B CB  
1526 C  CG  . ARG B 88  ? 0.3963 0.2952 0.5560 -0.0101 0.0231  -0.0053 88  ARG B CG  
1527 C  CD  . ARG B 88  ? 0.4557 0.3660 0.6100 0.0007  0.0085  0.0149  88  ARG B CD  
1528 N  NE  . ARG B 88  ? 0.5049 0.4271 0.6570 0.0157  0.0003  0.0350  88  ARG B NE  
1529 C  CZ  . ARG B 88  ? 0.5428 0.4698 0.6913 0.0234  -0.0025 0.0517  88  ARG B CZ  
1530 N  NH1 . ARG B 88  ? 0.5620 0.4840 0.7029 0.0313  -0.0073 0.0552  88  ARG B NH1 
1531 N  NH2 . ARG B 88  ? 0.5467 0.4754 0.7013 0.0200  0.0019  0.0609  88  ARG B NH2 
1532 N  N   . ILE B 89  ? 0.2419 0.1506 0.4101 0.0122  0.0570  -0.0151 89  ILE B N   
1533 C  CA  . ILE B 89  ? 0.2222 0.1680 0.3912 0.0186  0.0377  -0.0153 89  ILE B CA  
1534 C  C   . ILE B 89  ? 0.1859 0.1849 0.3945 0.0190  0.0190  -0.0007 89  ILE B C   
1535 O  O   . ILE B 89  ? 0.1725 0.2146 0.4009 0.0077  0.0166  0.0011  89  ILE B O   
1536 C  CB  . ILE B 89  ? 0.2176 0.1503 0.3758 0.0130  0.0319  -0.0208 89  ILE B CB  
1537 C  CG1 . ILE B 89  ? 0.2093 0.1538 0.3718 -0.0096 0.0274  -0.0170 89  ILE B CG1 
1538 C  CG2 . ILE B 89  ? 0.2366 0.1549 0.3720 0.0136  0.0315  -0.0157 89  ILE B CG2 
1539 C  CD1 . ILE B 89  ? 0.2255 0.1509 0.3733 -0.0149 0.0243  -0.0223 89  ILE B CD1 
1540 N  N   . SER B 90  ? 0.1995 0.1669 0.3910 0.0080  0.0112  0.0168  90  SER B N   
1541 C  CA  . SER B 90  ? 0.2335 0.1706 0.4034 -0.0001 0.0172  0.0281  90  SER B CA  
1542 C  C   . SER B 90  ? 0.2078 0.1638 0.3936 0.0141  0.0036  0.0276  90  SER B C   
1543 O  O   . SER B 90  ? 0.1989 0.1643 0.3776 0.0222  0.0000  0.0300  90  SER B O   
1544 C  CB  . SER B 90  ? 0.2906 0.1812 0.4281 -0.0236 0.0403  0.0426  90  SER B CB  
1545 O  OG  . SER B 90  ? 0.3406 0.2187 0.4492 -0.0302 0.0309  0.0506  90  SER B OG  
1546 N  N   . PRO B 91  ? 0.2036 0.1671 0.3991 0.0241  0.0038  0.0237  91  PRO B N   
1547 C  CA  . PRO B 91  ? 0.2011 0.1736 0.3859 0.0266  0.0042  0.0242  91  PRO B CA  
1548 C  C   . PRO B 91  ? 0.1965 0.1913 0.3574 0.0223  0.0050  0.0384  91  PRO B C   
1549 O  O   . PRO B 91  ? 0.1854 0.2009 0.3463 0.0160  0.0073  0.0451  91  PRO B O   
1550 C  CB  . PRO B 91  ? 0.2112 0.1757 0.4020 0.0397  0.0186  0.0178  91  PRO B CB  
1551 C  CG  . PRO B 91  ? 0.2193 0.1888 0.4149 0.0346  0.0227  0.0107  91  PRO B CG  
1552 C  CD  . PRO B 91  ? 0.2076 0.1864 0.4149 0.0330  0.0126  0.0178  91  PRO B CD  
1553 N  N   . ASP B 92  ? 0.1840 0.1865 0.3508 0.0410  0.0122  0.0537  92  ASP B N   
1554 C  CA  . ASP B 92  ? 0.2049 0.2003 0.3431 0.0281  -0.0082 0.0784  92  ASP B CA  
1555 C  C   . ASP B 92  ? 0.1931 0.1813 0.3204 0.0202  -0.0036 0.0729  92  ASP B C   
1556 O  O   . ASP B 92  ? 0.2006 0.1862 0.3083 0.0074  -0.0023 0.0705  92  ASP B O   
1557 C  CB  . ASP B 92  ? 0.2562 0.2160 0.3592 0.0224  -0.0245 0.1110  92  ASP B CB  
1558 C  CG  . ASP B 92  ? 0.2848 0.2261 0.3735 0.0213  -0.0247 0.1286  92  ASP B CG  
1559 O  OD1 . ASP B 92  ? 0.2903 0.2021 0.3760 0.0253  -0.0225 0.1266  92  ASP B OD1 
1560 O  OD2 . ASP B 92  ? 0.3148 0.2617 0.3864 0.0094  -0.0225 0.1296  92  ASP B OD2 
1561 N  N   . ARG B 93  ? 0.1892 0.1607 0.3097 0.0136  0.0046  0.0627  93  ARG B N   
1562 C  CA  . ARG B 93  ? 0.1757 0.1474 0.3005 -0.0026 0.0053  0.0610  93  ARG B CA  
1563 C  C   . ARG B 93  ? 0.1816 0.1415 0.2801 0.0056  0.0103  0.0463  93  ARG B C   
1564 O  O   . ARG B 93  ? 0.1961 0.1418 0.2639 0.0157  0.0081  0.0369  93  ARG B O   
1565 C  CB  . ARG B 93  ? 0.1748 0.1371 0.3091 -0.0009 0.0169  0.0636  93  ARG B CB  
1566 C  CG  . ARG B 93  ? 0.1777 0.1449 0.3196 0.0157  0.0227  0.0581  93  ARG B CG  
1567 C  CD  . ARG B 93  ? 0.1791 0.1394 0.3213 0.0124  0.0241  0.0365  93  ARG B CD  
1568 N  NE  . ARG B 93  ? 0.1859 0.1423 0.3152 0.0010  0.0256  0.0286  93  ARG B NE  
1569 C  CZ  . ARG B 93  ? 0.1868 0.1394 0.3067 0.0013  0.0225  0.0236  93  ARG B CZ  
1570 N  NH1 . ARG B 93  ? 0.1977 0.1341 0.3056 -0.0013 0.0210  0.0233  93  ARG B NH1 
1571 N  NH2 . ARG B 93  ? 0.1830 0.1386 0.3103 -0.0071 0.0239  0.0179  93  ARG B NH2 
1572 N  N   . VAL B 94  ? 0.2070 0.1488 0.2780 -0.0004 0.0248  0.0462  94  VAL B N   
1573 C  CA  . VAL B 94  ? 0.2160 0.1399 0.2697 -0.0016 0.0407  0.0523  94  VAL B CA  
1574 C  C   . VAL B 94  ? 0.2140 0.1456 0.2623 0.0182  0.0174  0.0632  94  VAL B C   
1575 O  O   . VAL B 94  ? 0.2050 0.1681 0.2666 0.0096  -0.0078 0.0536  94  VAL B O   
1576 C  CB  . VAL B 94  ? 0.2103 0.1565 0.2738 -0.0006 0.0489  0.0363  94  VAL B CB  
1577 C  CG1 . VAL B 94  ? 0.2109 0.1723 0.2743 -0.0025 0.0531  0.0472  94  VAL B CG1 
1578 C  CG2 . VAL B 94  ? 0.2152 0.1592 0.2706 0.0108  0.0467  0.0233  94  VAL B CG2 
1579 N  N   . TYR B 95  ? 0.1863 0.1377 0.2572 0.0204  0.0233  0.0607  95  TYR B N   
1580 C  CA  . TYR B 95  ? 0.1700 0.1563 0.2508 0.0163  0.0215  0.0517  95  TYR B CA  
1581 C  C   . TYR B 95  ? 0.1677 0.1591 0.2408 0.0079  -0.0009 0.0498  95  TYR B C   
1582 O  O   . TYR B 95  ? 0.1794 0.1534 0.2400 -0.0012 -0.0031 0.0562  95  TYR B O   
1583 C  CB  . TYR B 95  ? 0.1743 0.1912 0.2498 0.0227  0.0218  0.0544  95  TYR B CB  
1584 C  CG  . TYR B 95  ? 0.1679 0.2189 0.2477 0.0154  0.0017  0.0568  95  TYR B CG  
1585 C  CD1 . TYR B 95  ? 0.1780 0.2758 0.2573 0.0114  -0.0066 0.0600  95  TYR B CD1 
1586 C  CD2 . TYR B 95  ? 0.1670 0.2306 0.2486 0.0070  0.0034  0.0658  95  TYR B CD2 
1587 C  CE1 . TYR B 95  ? 0.1723 0.3000 0.2616 -0.0026 0.0002  0.0664  95  TYR B CE1 
1588 C  CE2 . TYR B 95  ? 0.1624 0.2540 0.2500 0.0026  0.0003  0.0725  95  TYR B CE2 
1589 C  CZ  . TYR B 95  ? 0.1690 0.2908 0.2547 -0.0017 -0.0021 0.0720  95  TYR B CZ  
1590 O  OH  . TYR B 95  ? 0.1942 0.3245 0.2562 0.0126  -0.0045 0.0734  95  TYR B OH  
1591 N  N   . ILE B 96  ? 0.1568 0.1530 0.2385 0.0048  0.0048  0.0391  96  ILE B N   
1592 C  CA  . ILE B 96  ? 0.1362 0.1451 0.2408 0.0060  0.0048  0.0246  96  ILE B CA  
1593 C  C   . ILE B 96  ? 0.1445 0.1453 0.2304 0.0065  -0.0006 0.0229  96  ILE B C   
1594 O  O   . ILE B 96  ? 0.1609 0.1792 0.2401 0.0058  -0.0284 0.0243  96  ILE B O   
1595 C  CB  . ILE B 96  ? 0.1447 0.1478 0.2621 0.0130  0.0029  0.0293  96  ILE B CB  
1596 C  CG1 . ILE B 96  ? 0.1746 0.1532 0.2987 0.0348  0.0212  0.0176  96  ILE B CG1 
1597 C  CG2 . ILE B 96  ? 0.1578 0.1606 0.2626 -0.0021 -0.0100 0.0328  96  ILE B CG2 
1598 C  CD1 . ILE B 96  ? 0.2003 0.1707 0.3351 0.0293  0.0222  0.0032  96  ILE B CD1 
1599 N  N   . ASN B 97  ? 0.1540 0.1436 0.2162 0.0047  0.0063  0.0330  97  ASN B N   
1600 C  CA  . ASN B 97  ? 0.1510 0.1587 0.2163 -0.0022 0.0144  0.0285  97  ASN B CA  
1601 C  C   . ASN B 97  ? 0.1521 0.1646 0.1942 -0.0077 0.0048  0.0129  97  ASN B C   
1602 O  O   . ASN B 97  ? 0.1698 0.1732 0.1909 -0.0024 0.0009  0.0156  97  ASN B O   
1603 C  CB  . ASN B 97  ? 0.1404 0.1896 0.2325 0.0136  0.0151  0.0438  97  ASN B CB  
1604 C  CG  . ASN B 97  ? 0.1606 0.2251 0.2604 0.0105  0.0164  0.0609  97  ASN B CG  
1605 O  OD1 . ASN B 97  ? 0.1805 0.2751 0.2599 0.0108  0.0263  0.0778  97  ASN B OD1 
1606 N  ND2 . ASN B 97  ? 0.1757 0.2385 0.2882 0.0000  0.0272  0.0530  97  ASN B ND2 
1607 N  N   . TYR B 98  ? 0.1410 0.1719 0.2001 -0.0081 -0.0004 0.0201  98  TYR B N   
1608 C  CA  . TYR B 98  ? 0.1275 0.1669 0.2009 -0.0018 -0.0030 0.0312  98  TYR B CA  
1609 C  C   . TYR B 98  ? 0.1449 0.1715 0.1897 0.0022  -0.0014 0.0231  98  TYR B C   
1610 O  O   . TYR B 98  ? 0.1784 0.1671 0.1798 0.0063  0.0069  0.0233  98  TYR B O   
1611 C  CB  . TYR B 98  ? 0.1339 0.1556 0.2212 0.0017  -0.0047 0.0268  98  TYR B CB  
1612 C  CG  . TYR B 98  ? 0.1372 0.1560 0.2372 0.0031  0.0007  0.0340  98  TYR B CG  
1613 C  CD1 . TYR B 98  ? 0.1375 0.1710 0.2558 0.0113  0.0004  0.0333  98  TYR B CD1 
1614 C  CD2 . TYR B 98  ? 0.1530 0.1496 0.2432 0.0028  -0.0061 0.0374  98  TYR B CD2 
1615 C  CE1 . TYR B 98  ? 0.1465 0.1594 0.2618 0.0138  0.0011  0.0367  98  TYR B CE1 
1616 C  CE2 . TYR B 98  ? 0.1554 0.1513 0.2563 0.0102  0.0090  0.0259  98  TYR B CE2 
1617 C  CZ  . TYR B 98  ? 0.1504 0.1531 0.2672 0.0184  0.0015  0.0283  98  TYR B CZ  
1618 O  OH  . TYR B 98  ? 0.1678 0.1628 0.2877 0.0144  0.0075  0.0120  98  TYR B OH  
1619 N  N   . TYR B 99  ? 0.1504 0.1602 0.1955 -0.0069 -0.0104 0.0200  99  TYR B N   
1620 C  CA  . TYR B 99  ? 0.1499 0.1566 0.2021 -0.0241 -0.0057 0.0200  99  TYR B CA  
1621 C  C   . TYR B 99  ? 0.1698 0.1529 0.1915 -0.0302 0.0088  0.0159  99  TYR B C   
1622 O  O   . TYR B 99  ? 0.1940 0.1658 0.1848 -0.0191 0.0212  0.0141  99  TYR B O   
1623 C  CB  . TYR B 99  ? 0.1397 0.1776 0.2005 -0.0134 -0.0059 0.0146  99  TYR B CB  
1624 C  CG  . TYR B 99  ? 0.1476 0.1822 0.2034 -0.0034 0.0054  0.0105  99  TYR B CG  
1625 C  CD1 . TYR B 99  ? 0.1695 0.2082 0.2202 -0.0071 0.0114  -0.0084 99  TYR B CD1 
1626 C  CD2 . TYR B 99  ? 0.1542 0.1736 0.2010 -0.0139 0.0022  0.0294  99  TYR B CD2 
1627 C  CE1 . TYR B 99  ? 0.1629 0.2106 0.2303 -0.0188 0.0190  -0.0132 99  TYR B CE1 
1628 C  CE2 . TYR B 99  ? 0.1649 0.1868 0.2225 -0.0155 0.0135  0.0116  99  TYR B CE2 
1629 C  CZ  . TYR B 99  ? 0.1620 0.2029 0.2368 -0.0185 0.0283  -0.0038 99  TYR B CZ  
1630 O  OH  . TYR B 99  ? 0.1980 0.2263 0.2540 -0.0239 0.0471  0.0020  99  TYR B OH  
1631 N  N   . ASP B 100 ? 0.1828 0.1584 0.1998 -0.0268 -0.0004 0.0129  100 ASP B N   
1632 C  CA  . ASP B 100 ? 0.1827 0.1634 0.2005 -0.0318 -0.0081 0.0105  100 ASP B CA  
1633 C  C   . ASP B 100 ? 0.1832 0.1614 0.1857 -0.0258 0.0078  0.0054  100 ASP B C   
1634 O  O   . ASP B 100 ? 0.2292 0.1749 0.1792 -0.0270 0.0058  0.0022  100 ASP B O   
1635 C  CB  . ASP B 100 ? 0.1898 0.2113 0.2168 -0.0433 -0.0142 0.0012  100 ASP B CB  
1636 C  CG  . ASP B 100 ? 0.2037 0.2584 0.2418 -0.0506 -0.0161 -0.0143 100 ASP B CG  
1637 O  OD1 . ASP B 100 ? 0.1826 0.2445 0.2485 -0.0446 0.0130  -0.0194 100 ASP B OD1 
1638 O  OD2 . ASP B 100 ? 0.2432 0.3294 0.2579 -0.0672 -0.0242 -0.0175 100 ASP B OD2 
1639 N  N   . MET B 101 ? 0.1650 0.1542 0.1859 -0.0228 0.0129  0.0079  101 MET B N   
1640 C  CA  . MET B 101 ? 0.1630 0.1707 0.1930 -0.0262 0.0040  0.0166  101 MET B CA  
1641 C  C   . MET B 101 ? 0.1686 0.1703 0.1903 -0.0273 0.0133  0.0040  101 MET B C   
1642 O  O   . MET B 101 ? 0.1696 0.1798 0.2084 -0.0206 0.0213  -0.0066 101 MET B O   
1643 C  CB  . MET B 101 ? 0.1487 0.1878 0.2071 -0.0349 0.0032  0.0106  101 MET B CB  
1644 C  CG  . MET B 101 ? 0.1666 0.2062 0.2250 -0.0374 0.0063  0.0099  101 MET B CG  
1645 S  SD  . MET B 101 ? 0.1980 0.2376 0.2425 -0.0461 0.0208  0.0181  101 MET B SD  
1646 C  CE  . MET B 101 ? 0.2035 0.2190 0.2410 -0.0162 0.0254  0.0168  101 MET B CE  
1647 N  N   . ASN B 102 ? 0.1596 0.1715 0.1946 -0.0385 0.0238  0.0027  102 ASN B N   
1648 C  CA  . ASN B 102 ? 0.1881 0.1711 0.2025 -0.0352 0.0181  0.0008  102 ASN B CA  
1649 C  C   . ASN B 102 ? 0.1552 0.1767 0.1945 -0.0269 0.0148  0.0035  102 ASN B C   
1650 O  O   . ASN B 102 ? 0.1467 0.1827 0.2008 -0.0277 0.0078  0.0060  102 ASN B O   
1651 C  CB  . ASN B 102 ? 0.2362 0.1906 0.2177 -0.0236 0.0139  -0.0156 102 ASN B CB  
1652 C  CG  . ASN B 102 ? 0.3027 0.2392 0.2428 -0.0260 0.0108  -0.0391 102 ASN B CG  
1653 O  OD1 . ASN B 102 ? 0.3320 0.2720 0.2484 -0.0341 -0.0105 -0.0423 102 ASN B OD1 
1654 N  ND2 . ASN B 102 ? 0.3334 0.2781 0.2591 -0.0101 0.0290  -0.0418 102 ASN B ND2 
1655 N  N   . ALA B 103 ? 0.1416 0.1986 0.1858 -0.0264 0.0279  0.0003  103 ALA B N   
1656 C  CA  . ALA B 103 ? 0.1339 0.2041 0.1913 -0.0219 0.0291  0.0037  103 ALA B CA  
1657 C  C   . ALA B 103 ? 0.1568 0.1863 0.1854 -0.0306 0.0202  -0.0062 103 ALA B C   
1658 O  O   . ALA B 103 ? 0.1695 0.2145 0.1844 -0.0370 0.0263  -0.0055 103 ALA B O   
1659 C  CB  . ALA B 103 ? 0.1163 0.2303 0.2081 -0.0221 0.0229  0.0075  103 ALA B CB  
1660 N  N   . ALA B 104 ? 0.1498 0.1780 0.1995 -0.0270 0.0271  -0.0021 104 ALA B N   
1661 C  CA  . ALA B 104 ? 0.1656 0.1840 0.2061 -0.0319 0.0215  -0.0013 104 ALA B CA  
1662 C  C   . ALA B 104 ? 0.1479 0.1882 0.1842 -0.0280 0.0212  -0.0073 104 ALA B C   
1663 O  O   . ALA B 104 ? 0.1477 0.2073 0.1908 -0.0140 0.0170  -0.0020 104 ALA B O   
1664 C  CB  . ALA B 104 ? 0.1991 0.1767 0.2217 -0.0044 -0.0056 -0.0198 104 ALA B CB  
1665 N  N   . ASN B 105 ? 0.1466 0.1726 0.1625 -0.0442 0.0263  -0.0090 105 ASN B N   
1666 C  CA  . ASN B 105 ? 0.1487 0.1768 0.1514 -0.0254 0.0173  -0.0261 105 ASN B CA  
1667 C  C   . ASN B 105 ? 0.1464 0.1712 0.1685 -0.0101 0.0161  -0.0201 105 ASN B C   
1668 O  O   . ASN B 105 ? 0.1385 0.1795 0.1814 -0.0246 0.0179  -0.0091 105 ASN B O   
1669 C  CB  . ASN B 105 ? 0.1666 0.1907 0.1499 -0.0233 0.0022  -0.0235 105 ASN B CB  
1670 C  CG  . ASN B 105 ? 0.2004 0.1978 0.1623 0.0033  0.0025  -0.0186 105 ASN B CG  
1671 O  OD1 . ASN B 105 ? 0.2063 0.2069 0.1705 0.0106  -0.0074 -0.0146 105 ASN B OD1 
1672 N  ND2 . ASN B 105 ? 0.2178 0.1958 0.1633 0.0131  -0.0046 -0.0147 105 ASN B ND2 
1673 N  N   . VAL B 106 ? 0.1432 0.1806 0.1767 -0.0092 0.0198  -0.0225 106 VAL B N   
1674 C  CA  . VAL B 106 ? 0.1494 0.1840 0.1761 -0.0136 0.0246  -0.0072 106 VAL B CA  
1675 C  C   . VAL B 106 ? 0.1417 0.1713 0.1794 -0.0269 0.0279  -0.0073 106 VAL B C   
1676 O  O   . VAL B 106 ? 0.1575 0.1800 0.1844 -0.0353 0.0171  0.0017  106 VAL B O   
1677 C  CB  . VAL B 106 ? 0.1621 0.1947 0.1802 -0.0088 0.0269  -0.0019 106 VAL B CB  
1678 C  CG1 . VAL B 106 ? 0.1760 0.1934 0.1864 -0.0014 0.0327  -0.0173 106 VAL B CG1 
1679 C  CG2 . VAL B 106 ? 0.1651 0.1941 0.1930 0.0096  0.0220  0.0197  106 VAL B CG2 
1680 N  N   . GLY B 107 ? 0.1436 0.1717 0.1691 -0.0179 0.0213  -0.0130 107 GLY B N   
1681 C  CA  . GLY B 107 ? 0.1417 0.1784 0.1640 -0.0166 0.0218  -0.0208 107 GLY B CA  
1682 C  C   . GLY B 107 ? 0.1448 0.1774 0.1691 -0.0210 0.0198  -0.0170 107 GLY B C   
1683 O  O   . GLY B 107 ? 0.1565 0.1815 0.1691 -0.0106 0.0268  -0.0187 107 GLY B O   
1684 N  N   . TRP B 108 ? 0.1582 0.1723 0.1757 -0.0278 0.0366  -0.0270 108 TRP B N   
1685 C  CA  . TRP B 108 ? 0.1592 0.1818 0.1804 -0.0173 0.0454  -0.0200 108 TRP B CA  
1686 C  C   . TRP B 108 ? 0.1741 0.1757 0.1768 -0.0191 0.0426  -0.0175 108 TRP B C   
1687 O  O   . TRP B 108 ? 0.1868 0.1708 0.1878 -0.0307 0.0402  -0.0182 108 TRP B O   
1688 C  CB  . TRP B 108 ? 0.1558 0.1854 0.1905 -0.0308 0.0346  -0.0377 108 TRP B CB  
1689 C  CG  . TRP B 108 ? 0.1673 0.1998 0.1960 -0.0282 0.0385  -0.0258 108 TRP B CG  
1690 C  CD1 . TRP B 108 ? 0.1599 0.1868 0.1953 -0.0122 0.0389  -0.0112 108 TRP B CD1 
1691 C  CD2 . TRP B 108 ? 0.1911 0.2254 0.2189 -0.0520 0.0549  -0.0401 108 TRP B CD2 
1692 N  NE1 . TRP B 108 ? 0.1557 0.2073 0.2061 -0.0196 0.0396  -0.0239 108 TRP B NE1 
1693 C  CE2 . TRP B 108 ? 0.1854 0.2376 0.2208 -0.0386 0.0574  -0.0380 108 TRP B CE2 
1694 C  CE3 . TRP B 108 ? 0.2208 0.2618 0.2411 -0.0693 0.0739  -0.0337 108 TRP B CE3 
1695 C  CZ2 . TRP B 108 ? 0.2106 0.2781 0.2472 -0.0621 0.0715  -0.0444 108 TRP B CZ2 
1696 C  CZ3 . TRP B 108 ? 0.2303 0.2927 0.2605 -0.0747 0.0814  -0.0373 108 TRP B CZ3 
1697 C  CH2 . TRP B 108 ? 0.2164 0.3043 0.2620 -0.0784 0.0843  -0.0439 108 TRP B CH2 
1698 N  N   . ASN B 109 ? 0.1727 0.1870 0.1646 -0.0217 0.0370  -0.0216 109 ASN B N   
1699 C  CA  . ASN B 109 ? 0.1807 0.2036 0.1758 -0.0302 0.0373  -0.0206 109 ASN B CA  
1700 C  C   . ASN B 109 ? 0.1939 0.2051 0.1870 -0.0254 0.0229  -0.0031 109 ASN B C   
1701 O  O   . ASN B 109 ? 0.2097 0.2168 0.1986 -0.0326 0.0376  -0.0062 109 ASN B O   
1702 C  CB  . ASN B 109 ? 0.1930 0.2393 0.1955 -0.0465 0.0372  -0.0215 109 ASN B CB  
1703 C  CG  . ASN B 109 ? 0.2169 0.2647 0.2114 -0.0679 0.0485  -0.0326 109 ASN B CG  
1704 O  OD1 . ASN B 109 ? 0.2363 0.3132 0.2093 -0.0570 0.0582  -0.0390 109 ASN B OD1 
1705 N  ND2 . ASN B 109 ? 0.2359 0.2561 0.2255 -0.0812 0.0664  -0.0385 109 ASN B ND2 
1706 N  N   . ASN B 110 ? 0.1904 0.2038 0.1773 -0.0174 0.0186  0.0120  110 ASN B N   
1707 C  CA  . ASN B 110 ? 0.2222 0.2105 0.1724 -0.0195 0.0176  0.0040  110 ASN B CA  
1708 C  C   . ASN B 110 ? 0.2132 0.2055 0.1747 -0.0109 0.0222  0.0002  110 ASN B C   
1709 O  O   . ASN B 110 ? 0.2350 0.2083 0.1905 0.0044  0.0114  -0.0013 110 ASN B O   
1710 C  CB  . ASN B 110 ? 0.2897 0.2298 0.1746 -0.0311 0.0152  0.0087  110 ASN B CB  
1711 C  CG  . ASN B 110 ? 0.3499 0.2696 0.1815 -0.0419 0.0150  0.0277  110 ASN B CG  
1712 O  OD1 . ASN B 110 ? 0.3730 0.3135 0.2038 -0.0474 -0.0055 0.0375  110 ASN B OD1 
1713 N  ND2 . ASN B 110 ? 0.3994 0.2866 0.1765 -0.0318 0.0074  0.0184  110 ASN B ND2 
1714 N  N   . SER B 111 ? 0.1909 0.2056 0.1698 -0.0177 0.0150  0.0024  111 SER B N   
1715 C  CA  . SER B 111 ? 0.2145 0.1870 0.1682 -0.0381 0.0214  -0.0055 111 SER B CA  
1716 C  C   . SER B 111 ? 0.2044 0.1773 0.1732 -0.0229 0.0291  -0.0122 111 SER B C   
1717 O  O   . SER B 111 ? 0.1928 0.1736 0.1923 -0.0268 0.0218  -0.0244 111 SER B O   
1718 C  CB  . SER B 111 ? 0.2257 0.2095 0.1736 -0.0510 0.0324  -0.0043 111 SER B CB  
1719 O  OG  . SER B 111 ? 0.2457 0.2419 0.1956 -0.0425 0.0290  0.0146  111 SER B OG  
1720 N  N   . THR B 112 ? 0.1865 0.1877 0.1766 -0.0206 0.0317  -0.0009 112 THR B N   
1721 C  CA  . THR B 112 ? 0.1792 0.1890 0.1828 -0.0233 0.0126  -0.0090 112 THR B CA  
1722 C  C   . THR B 112 ? 0.1823 0.2021 0.1889 -0.0318 0.0159  0.0018  112 THR B C   
1723 O  O   . THR B 112 ? 0.1916 0.2325 0.1975 -0.0453 0.0282  0.0253  112 THR B O   
1724 C  CB  . THR B 112 ? 0.1783 0.1927 0.1977 -0.0377 0.0277  -0.0119 112 THR B CB  
1725 O  OG1 . THR B 112 ? 0.2010 0.2029 0.2077 -0.0543 0.0262  -0.0151 112 THR B OG1 
1726 C  CG2 . THR B 112 ? 0.1868 0.1888 0.1970 -0.0165 0.0087  0.0063  112 THR B CG2 
1727 N  N   . PHE B 113 ? 0.1703 0.1910 0.1950 -0.0178 0.0060  -0.0174 113 PHE B N   
1728 C  CA  . PHE B 113 ? 0.1664 0.2069 0.2142 -0.0331 0.0099  -0.0190 113 PHE B CA  
1729 C  C   . PHE B 113 ? 0.1742 0.2141 0.2129 -0.0401 0.0255  -0.0178 113 PHE B C   
1730 O  O   . PHE B 113 ? 0.1757 0.2341 0.2303 -0.0464 0.0264  -0.0141 113 PHE B O   
1731 C  CB  . PHE B 113 ? 0.1625 0.2107 0.2332 -0.0244 0.0249  -0.0383 113 PHE B CB  
1732 C  CG  . PHE B 113 ? 0.1663 0.2440 0.2449 -0.0315 0.0390  -0.0501 113 PHE B CG  
1733 C  CD1 . PHE B 113 ? 0.1921 0.2760 0.2635 -0.0462 0.0507  -0.0694 113 PHE B CD1 
1734 C  CD2 . PHE B 113 ? 0.1712 0.2500 0.2342 -0.0404 0.0380  -0.0341 113 PHE B CD2 
1735 C  CE1 . PHE B 113 ? 0.1924 0.2925 0.2642 -0.0668 0.0645  -0.0604 113 PHE B CE1 
1736 C  CE2 . PHE B 113 ? 0.1801 0.2543 0.2312 -0.0357 0.0558  -0.0352 113 PHE B CE2 
1737 C  CZ  . PHE B 113 ? 0.1772 0.2732 0.2492 -0.0662 0.0638  -0.0464 113 PHE B CZ  
1738 N  N   . ALA B 114 ? 0.1766 0.2060 0.2031 -0.0339 0.0181  -0.0160 114 ALA B N   
1739 C  CA  . ALA B 114 ? 0.2039 0.2250 0.2100 -0.0507 0.0353  -0.0107 114 ALA B CA  
1740 C  C   . ALA B 114 ? 0.2257 0.2628 0.2229 -0.0647 0.0269  0.0111  114 ALA B C   
1741 O  O   . ALA B 114 ? 0.2432 0.2646 0.2402 -0.0679 0.0168  0.0245  114 ALA B O   
1742 C  CB  . ALA B 114 ? 0.2155 0.2119 0.2202 -0.0316 0.0450  -0.0261 114 ALA B CB  
1743 O  OXT . ALA B 114 ? 0.2356 0.2933 0.2223 -0.0759 0.0384  0.0130  114 ALA B OXT 
1744 N  N   . PRO C 1   ? 0.2321 0.1999 0.2396 -0.0174 -0.0668 0.0769  1   PRO C N   
1745 C  CA  . PRO C 1   ? 0.2446 0.1909 0.2399 -0.0133 -0.0598 0.0565  1   PRO C CA  
1746 C  C   . PRO C 1   ? 0.2171 0.1714 0.2264 -0.0206 -0.0667 0.0440  1   PRO C C   
1747 O  O   . PRO C 1   ? 0.2216 0.1635 0.2403 -0.0138 -0.0701 0.0489  1   PRO C O   
1748 C  CB  . PRO C 1   ? 0.2756 0.2059 0.2431 -0.0143 -0.0563 0.0648  1   PRO C CB  
1749 C  CG  . PRO C 1   ? 0.2860 0.2280 0.2453 -0.0033 -0.0662 0.0651  1   PRO C CG  
1750 C  CD  . PRO C 1   ? 0.2688 0.2180 0.2422 -0.0097 -0.0659 0.0756  1   PRO C CD  
1751 N  N   . MET C 2   ? 0.1891 0.1747 0.2092 -0.0074 -0.0671 0.0288  2   MET C N   
1752 C  CA  . MET C 2   ? 0.1741 0.1877 0.2152 0.0228  -0.0496 0.0194  2   MET C CA  
1753 C  C   . MET C 2   ? 0.1674 0.1496 0.1970 0.0024  -0.0363 0.0121  2   MET C C   
1754 O  O   . MET C 2   ? 0.1685 0.1431 0.2105 -0.0121 -0.0267 0.0180  2   MET C O   
1755 C  CB  . MET C 2   ? 0.2205 0.2814 0.2618 0.0723  -0.0055 0.0179  2   MET C CB  
1756 C  CG  . MET C 2   ? 0.2812 0.3367 0.3247 0.0901  0.0506  0.0538  2   MET C CG  
1757 S  SD  . MET C 2   ? 0.3284 0.3503 0.3716 0.1051  0.1047  0.0979  2   MET C SD  
1758 C  CE  . MET C 2   ? 0.3404 0.3451 0.3920 0.1034  0.1031  0.1080  2   MET C CE  
1759 N  N   . PHE C 3   ? 0.1637 0.1377 0.1879 0.0055  -0.0260 0.0197  3   PHE C N   
1760 C  CA  . PHE C 3   ? 0.1663 0.1344 0.1866 0.0056  -0.0159 0.0263  3   PHE C CA  
1761 C  C   . PHE C 3   ? 0.1712 0.1254 0.1847 -0.0016 -0.0165 0.0189  3   PHE C C   
1762 O  O   . PHE C 3   ? 0.1883 0.1368 0.1803 -0.0050 -0.0240 0.0055  3   PHE C O   
1763 C  CB  . PHE C 3   ? 0.1831 0.1414 0.1919 0.0103  0.0051  0.0241  3   PHE C CB  
1764 C  CG  . PHE C 3   ? 0.1848 0.1662 0.2077 0.0076  0.0218  0.0308  3   PHE C CG  
1765 C  CD1 . PHE C 3   ? 0.1965 0.1730 0.2074 0.0236  0.0446  0.0201  3   PHE C CD1 
1766 C  CD2 . PHE C 3   ? 0.2002 0.1836 0.2565 0.0122  0.0054  0.0305  3   PHE C CD2 
1767 C  CE1 . PHE C 3   ? 0.1940 0.1917 0.2295 0.0206  0.0491  0.0317  3   PHE C CE1 
1768 C  CE2 . PHE C 3   ? 0.2059 0.2069 0.2845 0.0138  0.0179  0.0345  3   PHE C CE2 
1769 C  CZ  . PHE C 3   ? 0.2065 0.1991 0.2626 0.0234  0.0435  0.0435  3   PHE C CZ  
1770 N  N   . ILE C 4   ? 0.1536 0.1235 0.1668 -0.0016 -0.0177 0.0199  4   ILE C N   
1771 C  CA  . ILE C 4   ? 0.1636 0.1298 0.1712 0.0069  -0.0137 0.0057  4   ILE C CA  
1772 C  C   . ILE C 4   ? 0.1540 0.1259 0.1685 0.0110  -0.0156 0.0053  4   ILE C C   
1773 O  O   . ILE C 4   ? 0.1598 0.1259 0.1828 0.0136  -0.0263 -0.0070 4   ILE C O   
1774 C  CB  . ILE C 4   ? 0.1667 0.1752 0.1850 0.0297  -0.0001 0.0215  4   ILE C CB  
1775 C  CG1 . ILE C 4   ? 0.1821 0.2357 0.2053 0.0209  0.0174  0.0211  4   ILE C CG1 
1776 C  CG2 . ILE C 4   ? 0.1834 0.1914 0.1886 0.0331  0.0033  0.0098  4   ILE C CG2 
1777 C  CD1 . ILE C 4   ? 0.2181 0.2662 0.2253 0.0087  0.0256  0.0157  4   ILE C CD1 
1778 N  N   . VAL C 5   ? 0.1376 0.1502 0.1702 0.0087  -0.0162 -0.0079 5   VAL C N   
1779 C  CA  . VAL C 5   ? 0.1246 0.1936 0.1871 0.0131  -0.0193 0.0064  5   VAL C CA  
1780 C  C   . VAL C 5   ? 0.1463 0.1514 0.1849 0.0141  -0.0239 -0.0015 5   VAL C C   
1781 O  O   . VAL C 5   ? 0.1788 0.1331 0.1984 0.0069  -0.0377 0.0047  5   VAL C O   
1782 C  CB  . VAL C 5   ? 0.1413 0.2626 0.2268 0.0294  0.0048  0.0310  5   VAL C CB  
1783 C  CG1 . VAL C 5   ? 0.1766 0.3085 0.2635 0.0146  0.0116  0.0256  5   VAL C CG1 
1784 C  CG2 . VAL C 5   ? 0.1438 0.2891 0.2355 0.0576  0.0028  0.0389  5   VAL C CG2 
1785 N  N   . ASN C 6   ? 0.1388 0.1402 0.1716 0.0095  -0.0210 0.0074  6   ASN C N   
1786 C  CA  . ASN C 6   ? 0.1379 0.1510 0.1749 -0.0018 -0.0035 0.0121  6   ASN C CA  
1787 C  C   . ASN C 6   ? 0.1339 0.1462 0.1600 0.0012  -0.0133 -0.0016 6   ASN C C   
1788 O  O   . ASN C 6   ? 0.1417 0.1452 0.1650 0.0129  -0.0167 -0.0078 6   ASN C O   
1789 C  CB  . ASN C 6   ? 0.1485 0.1652 0.2083 0.0055  0.0143  0.0292  6   ASN C CB  
1790 C  CG  . ASN C 6   ? 0.1767 0.2332 0.2605 0.0085  0.0240  0.0681  6   ASN C CG  
1791 O  OD1 . ASN C 6   ? 0.2050 0.2311 0.2889 0.0445  0.0480  0.0635  6   ASN C OD1 
1792 N  ND2 . ASN C 6   ? 0.1803 0.2907 0.2983 0.0009  0.0239  0.1057  6   ASN C ND2 
1793 N  N   . THR C 7   ? 0.1266 0.1401 0.1658 -0.0043 -0.0159 0.0120  7   THR C N   
1794 C  CA  . THR C 7   ? 0.1382 0.1630 0.1764 0.0067  -0.0025 0.0067  7   THR C CA  
1795 C  C   . THR C 7   ? 0.1415 0.1594 0.1678 0.0098  -0.0070 0.0017  7   THR C C   
1796 O  O   . THR C 7   ? 0.1413 0.1585 0.1761 0.0124  -0.0117 -0.0083 7   THR C O   
1797 C  CB  . THR C 7   ? 0.1459 0.1516 0.1938 0.0107  0.0191  0.0192  7   THR C CB  
1798 O  OG1 . THR C 7   ? 0.1502 0.1520 0.2027 0.0101  0.0124  0.0016  7   THR C OG1 
1799 C  CG2 . THR C 7   ? 0.1699 0.1445 0.1980 0.0137  0.0320  0.0171  7   THR C CG2 
1800 N  N   . ASN C 8   ? 0.1277 0.1603 0.1612 0.0142  -0.0241 0.0126  8   ASN C N   
1801 C  CA  . ASN C 8   ? 0.1535 0.1659 0.1803 0.0013  -0.0349 0.0120  8   ASN C CA  
1802 C  C   . ASN C 8   ? 0.1626 0.1917 0.2060 -0.0081 -0.0267 0.0009  8   ASN C C   
1803 O  O   . ASN C 8   ? 0.1771 0.2329 0.2235 -0.0315 -0.0389 -0.0034 8   ASN C O   
1804 C  CB  . ASN C 8   ? 0.1720 0.1794 0.1928 0.0145  -0.0284 0.0096  8   ASN C CB  
1805 C  CG  . ASN C 8   ? 0.1816 0.1838 0.2039 0.0251  -0.0280 0.0090  8   ASN C CG  
1806 O  OD1 . ASN C 8   ? 0.1588 0.1823 0.1987 0.0197  -0.0112 -0.0042 8   ASN C OD1 
1807 N  ND2 . ASN C 8   ? 0.2458 0.2052 0.2307 0.0493  -0.0451 0.0204  8   ASN C ND2 
1808 N  N   . VAL C 9   ? 0.1525 0.1668 0.2104 -0.0053 -0.0099 0.0141  9   VAL C N   
1809 C  CA  . VAL C 9   ? 0.1879 0.1827 0.2277 -0.0288 0.0178  0.0010  9   VAL C CA  
1810 C  C   . VAL C 9   ? 0.1770 0.1857 0.2407 -0.0232 0.0054  0.0091  9   VAL C C   
1811 O  O   . VAL C 9   ? 0.1750 0.1892 0.2477 -0.0203 0.0103  0.0026  9   VAL C O   
1812 C  CB  . VAL C 9   ? 0.2230 0.2278 0.2360 -0.0518 0.0669  -0.0219 9   VAL C CB  
1813 C  CG1 . VAL C 9   ? 0.2570 0.2772 0.2534 -0.0388 0.0458  -0.0169 9   VAL C CG1 
1814 C  CG2 . VAL C 9   ? 0.2170 0.2376 0.2405 -0.0408 0.0719  -0.0424 9   VAL C CG2 
1815 N  N   . PRO C 10  ? 0.2062 0.2072 0.2585 -0.0219 -0.0129 -0.0017 10  PRO C N   
1816 C  CA  . PRO C 10  ? 0.2255 0.2028 0.2738 -0.0169 -0.0231 -0.0102 10  PRO C CA  
1817 C  C   . PRO C 10  ? 0.2050 0.1853 0.2820 -0.0182 -0.0102 -0.0093 10  PRO C C   
1818 O  O   . PRO C 10  ? 0.1826 0.1841 0.2805 -0.0193 -0.0071 -0.0155 10  PRO C O   
1819 C  CB  . PRO C 10  ? 0.2495 0.2394 0.2815 -0.0132 -0.0412 -0.0260 10  PRO C CB  
1820 C  CG  . PRO C 10  ? 0.2529 0.2586 0.2861 -0.0295 -0.0420 -0.0332 10  PRO C CG  
1821 C  CD  . PRO C 10  ? 0.2246 0.2320 0.2744 -0.0346 -0.0372 -0.0171 10  PRO C CD  
1822 N  N   . ARG C 11  ? 0.2087 0.1782 0.2990 -0.0251 -0.0104 -0.0151 11  ARG C N   
1823 C  CA  . ARG C 11  ? 0.2081 0.1922 0.3205 -0.0123 -0.0078 -0.0040 11  ARG C CA  
1824 C  C   . ARG C 11  ? 0.1928 0.2023 0.3148 -0.0177 -0.0085 0.0016  11  ARG C C   
1825 O  O   . ARG C 11  ? 0.1932 0.2156 0.3042 -0.0069 -0.0018 0.0135  11  ARG C O   
1826 C  CB  . ARG C 11  ? 0.2440 0.2328 0.3598 0.0025  -0.0124 0.0070  11  ARG C CB  
1827 C  CG  . ARG C 11  ? 0.3001 0.3007 0.4139 0.0052  -0.0265 0.0332  11  ARG C CG  
1828 C  CD  . ARG C 11  ? 0.3640 0.3515 0.4676 0.0038  -0.0389 0.0665  11  ARG C CD  
1829 N  NE  . ARG C 11  ? 0.4131 0.3976 0.5098 0.0043  -0.0413 0.0906  11  ARG C NE  
1830 C  CZ  . ARG C 11  ? 0.4422 0.4172 0.5361 -0.0009 -0.0418 0.1009  11  ARG C CZ  
1831 N  NH1 . ARG C 11  ? 0.4519 0.4208 0.5411 0.0126  -0.0371 0.0973  11  ARG C NH1 
1832 N  NH2 . ARG C 11  ? 0.4559 0.4302 0.5492 -0.0124 -0.0468 0.1006  11  ARG C NH2 
1833 N  N   . ALA C 12  ? 0.2003 0.2161 0.3332 -0.0536 -0.0024 -0.0031 12  ALA C N   
1834 C  CA  . ALA C 12  ? 0.2068 0.2653 0.3553 -0.0671 -0.0041 -0.0049 12  ALA C CA  
1835 C  C   . ALA C 12  ? 0.2050 0.2703 0.3524 -0.0479 -0.0056 0.0079  12  ALA C C   
1836 O  O   . ALA C 12  ? 0.2370 0.3038 0.3682 -0.0592 0.0179  0.0179  12  ALA C O   
1837 C  CB  . ALA C 12  ? 0.2141 0.2944 0.3717 -0.0645 -0.0195 -0.0109 12  ALA C CB  
1838 N  N   A SER C 13  ? 0.1903 0.2658 0.3399 -0.0153 -0.0257 0.0120  13  SER C N   
1839 N  N   B SER C 13  ? 0.1943 0.2670 0.3409 -0.0166 -0.0224 0.0133  13  SER C N   
1840 C  CA  A SER C 13  ? 0.2209 0.2771 0.3301 0.0115  -0.0192 0.0288  13  SER C CA  
1841 C  CA  B SER C 13  ? 0.2221 0.2795 0.3312 0.0125  -0.0197 0.0262  13  SER C CA  
1842 C  C   A SER C 13  ? 0.2246 0.2837 0.3122 0.0330  -0.0095 0.0298  13  SER C C   
1843 C  C   B SER C 13  ? 0.2254 0.2828 0.3119 0.0335  -0.0102 0.0297  13  SER C C   
1844 O  O   A SER C 13  ? 0.2531 0.3228 0.3194 0.0610  -0.0073 0.0081  13  SER C O   
1845 O  O   B SER C 13  ? 0.2513 0.3205 0.3185 0.0596  -0.0070 0.0101  13  SER C O   
1846 C  CB  A SER C 13  ? 0.2527 0.3000 0.3439 0.0182  -0.0155 0.0275  13  SER C CB  
1847 C  CB  B SER C 13  ? 0.2567 0.3025 0.3436 0.0204  -0.0176 0.0272  13  SER C CB  
1848 O  OG  A SER C 13  ? 0.2943 0.3247 0.3482 0.0245  -0.0159 0.0261  13  SER C OG  
1849 O  OG  B SER C 13  ? 0.2967 0.3269 0.3513 0.0250  -0.0149 0.0250  13  SER C OG  
1850 N  N   . VAL C 14  ? 0.2088 0.2429 0.2893 0.0262  -0.0062 0.0488  14  VAL C N   
1851 C  CA  . VAL C 14  ? 0.2177 0.2111 0.2684 0.0089  -0.0043 0.0496  14  VAL C CA  
1852 C  C   . VAL C 14  ? 0.2358 0.1922 0.2752 -0.0062 0.0062  0.0348  14  VAL C C   
1853 O  O   . VAL C 14  ? 0.2607 0.1937 0.2850 -0.0047 -0.0018 0.0237  14  VAL C O   
1854 C  CB  . VAL C 14  ? 0.2229 0.2134 0.2575 -0.0063 -0.0009 0.0358  14  VAL C CB  
1855 C  CG1 . VAL C 14  ? 0.2221 0.2389 0.2620 -0.0098 -0.0026 0.0141  14  VAL C CG1 
1856 C  CG2 . VAL C 14  ? 0.2361 0.2080 0.2536 -0.0145 -0.0059 0.0534  14  VAL C CG2 
1857 N  N   . PRO C 15  ? 0.2339 0.1783 0.2742 -0.0277 0.0335  0.0352  15  PRO C N   
1858 C  CA  . PRO C 15  ? 0.2323 0.1928 0.2752 -0.0247 0.0398  0.0421  15  PRO C CA  
1859 C  C   . PRO C 15  ? 0.2120 0.1978 0.2631 -0.0141 0.0179  0.0370  15  PRO C C   
1860 O  O   . PRO C 15  ? 0.2034 0.1927 0.2700 -0.0213 0.0179  0.0263  15  PRO C O   
1861 C  CB  . PRO C 15  ? 0.2479 0.2002 0.2887 -0.0145 0.0590  0.0292  15  PRO C CB  
1862 C  CG  . PRO C 15  ? 0.2679 0.2114 0.2868 -0.0367 0.0649  0.0175  15  PRO C CG  
1863 C  CD  . PRO C 15  ? 0.2501 0.1906 0.2785 -0.0470 0.0555  0.0192  15  PRO C CD  
1864 N  N   . ASP C 16  ? 0.2014 0.1749 0.2420 -0.0147 -0.0062 0.0390  16  ASP C N   
1865 C  CA  . ASP C 16  ? 0.2140 0.1621 0.2330 -0.0191 -0.0114 0.0218  16  ASP C CA  
1866 C  C   . ASP C 16  ? 0.1899 0.1730 0.2267 -0.0248 0.0026  0.0070  16  ASP C C   
1867 O  O   . ASP C 16  ? 0.2168 0.2027 0.2333 -0.0151 0.0186  -0.0086 16  ASP C O   
1868 C  CB  . ASP C 16  ? 0.2408 0.1738 0.2369 -0.0247 -0.0194 0.0176  16  ASP C CB  
1869 C  CG  . ASP C 16  ? 0.2655 0.1983 0.2401 -0.0214 -0.0217 0.0127  16  ASP C CG  
1870 O  OD1 . ASP C 16  ? 0.2798 0.2152 0.2442 -0.0231 -0.0284 0.0131  16  ASP C OD1 
1871 O  OD2 . ASP C 16  ? 0.2732 0.2085 0.2365 -0.0284 -0.0281 0.0058  16  ASP C OD2 
1872 N  N   . GLY C 17  ? 0.1780 0.1522 0.2216 -0.0309 -0.0212 0.0202  17  GLY C N   
1873 C  CA  . GLY C 17  ? 0.2014 0.1617 0.2167 -0.0442 -0.0217 0.0111  17  GLY C CA  
1874 C  C   . GLY C 17  ? 0.1949 0.1495 0.2103 -0.0459 0.0029  0.0192  17  GLY C C   
1875 O  O   . GLY C 17  ? 0.2302 0.1695 0.2078 -0.0467 0.0010  0.0232  17  GLY C O   
1876 N  N   . PHE C 18  ? 0.1847 0.1350 0.2213 -0.0311 0.0191  0.0207  18  PHE C N   
1877 C  CA  . PHE C 18  ? 0.1966 0.1417 0.2423 -0.0335 0.0112  0.0310  18  PHE C CA  
1878 C  C   . PHE C 18  ? 0.1979 0.1615 0.2291 -0.0275 0.0144  0.0312  18  PHE C C   
1879 O  O   . PHE C 18  ? 0.2061 0.1650 0.2225 -0.0342 0.0138  0.0255  18  PHE C O   
1880 C  CB  . PHE C 18  ? 0.2069 0.1566 0.2817 -0.0296 -0.0158 0.0410  18  PHE C CB  
1881 C  CG  . PHE C 18  ? 0.2124 0.1797 0.3295 -0.0287 -0.0297 0.0307  18  PHE C CG  
1882 C  CD1 . PHE C 18  ? 0.2333 0.1909 0.3598 -0.0033 -0.0279 0.0176  18  PHE C CD1 
1883 C  CD2 . PHE C 18  ? 0.2209 0.1797 0.3448 -0.0494 -0.0453 0.0357  18  PHE C CD2 
1884 C  CE1 . PHE C 18  ? 0.2396 0.1781 0.3724 0.0047  -0.0259 0.0215  18  PHE C CE1 
1885 C  CE2 . PHE C 18  ? 0.2327 0.1907 0.3615 -0.0353 -0.0426 0.0352  18  PHE C CE2 
1886 C  CZ  . PHE C 18  ? 0.2303 0.1987 0.3700 -0.0100 -0.0352 0.0330  18  PHE C CZ  
1887 N  N   . LEU C 19  ? 0.1666 0.1639 0.2293 -0.0126 0.0208  0.0327  19  LEU C N   
1888 C  CA  . LEU C 19  ? 0.1817 0.2087 0.2232 -0.0247 0.0161  0.0507  19  LEU C CA  
1889 C  C   . LEU C 19  ? 0.1842 0.1921 0.2212 -0.0395 0.0101  0.0521  19  LEU C C   
1890 O  O   . LEU C 19  ? 0.1820 0.1868 0.2185 -0.0322 0.0029  0.0392  19  LEU C O   
1891 C  CB  . LEU C 19  ? 0.2047 0.2615 0.2237 -0.0255 0.0176  0.0589  19  LEU C CB  
1892 C  CG  . LEU C 19  ? 0.2527 0.3023 0.2360 -0.0211 0.0050  0.0427  19  LEU C CG  
1893 C  CD1 . LEU C 19  ? 0.2644 0.3360 0.2448 0.0099  0.0153  0.0323  19  LEU C CD1 
1894 C  CD2 . LEU C 19  ? 0.3034 0.3179 0.2487 -0.0364 -0.0166 0.0389  19  LEU C CD2 
1895 N  N   . SER C 20  ? 0.1971 0.1837 0.2227 -0.0364 0.0163  0.0582  20  SER C N   
1896 C  CA  . SER C 20  ? 0.2149 0.1909 0.2197 -0.0474 0.0044  0.0483  20  SER C CA  
1897 C  C   . SER C 20  ? 0.1967 0.2083 0.2195 -0.0531 -0.0041 0.0509  20  SER C C   
1898 O  O   . SER C 20  ? 0.2152 0.2169 0.2190 -0.0547 -0.0133 0.0575  20  SER C O   
1899 C  CB  . SER C 20  ? 0.2629 0.2061 0.2320 -0.0716 -0.0028 0.0619  20  SER C CB  
1900 O  OG  . SER C 20  ? 0.3134 0.2263 0.2517 -0.0889 -0.0037 0.0687  20  SER C OG  
1901 N  N   . GLU C 21  ? 0.1827 0.2334 0.2344 -0.0462 0.0077  0.0397  21  GLU C N   
1902 C  CA  . GLU C 21  ? 0.1775 0.2593 0.2361 -0.0334 0.0168  0.0152  21  GLU C CA  
1903 C  C   . GLU C 21  ? 0.1715 0.2173 0.2199 -0.0191 0.0095  0.0014  21  GLU C C   
1904 O  O   . GLU C 21  ? 0.1876 0.2256 0.2170 -0.0194 0.0106  0.0024  21  GLU C O   
1905 C  CB  . GLU C 21  ? 0.2080 0.3115 0.2686 -0.0152 0.0128  -0.0009 21  GLU C CB  
1906 C  CG  . GLU C 21  ? 0.2696 0.3603 0.3138 0.0024  0.0253  -0.0018 21  GLU C CG  
1907 C  CD  . GLU C 21  ? 0.3267 0.4131 0.3503 0.0017  0.0421  0.0188  21  GLU C CD  
1908 O  OE1 . GLU C 21  ? 0.3373 0.4434 0.3603 0.0114  0.0389  0.0304  21  GLU C OE1 
1909 O  OE2 . GLU C 21  ? 0.3625 0.4210 0.3704 -0.0102 0.0534  0.0254  21  GLU C OE2 
1910 N  N   . LEU C 22  ? 0.1565 0.1771 0.2189 -0.0055 -0.0024 0.0088  22  LEU C N   
1911 C  CA  . LEU C 22  ? 0.1793 0.1745 0.2280 -0.0040 0.0054  0.0218  22  LEU C CA  
1912 C  C   . LEU C 22  ? 0.1827 0.1527 0.2080 -0.0021 0.0069  0.0282  22  LEU C C   
1913 O  O   . LEU C 22  ? 0.2132 0.1637 0.1966 -0.0117 -0.0020 0.0315  22  LEU C O   
1914 C  CB  . LEU C 22  ? 0.1839 0.1731 0.2376 0.0115  0.0092  0.0281  22  LEU C CB  
1915 C  CG  . LEU C 22  ? 0.1987 0.1594 0.2491 -0.0019 0.0119  0.0367  22  LEU C CG  
1916 C  CD1 . LEU C 22  ? 0.2190 0.1695 0.2483 -0.0053 0.0113  0.0390  22  LEU C CD1 
1917 C  CD2 . LEU C 22  ? 0.2195 0.1714 0.2660 0.0315  0.0210  0.0248  22  LEU C CD2 
1918 N  N   . THR C 23  ? 0.1530 0.1428 0.2106 -0.0031 0.0111  0.0305  23  THR C N   
1919 C  CA  . THR C 23  ? 0.1579 0.1538 0.2147 0.0120  0.0099  0.0296  23  THR C CA  
1920 C  C   . THR C 23  ? 0.1609 0.1653 0.2179 0.0029  0.0039  0.0421  23  THR C C   
1921 O  O   . THR C 23  ? 0.1686 0.1799 0.2301 -0.0006 -0.0011 0.0572  23  THR C O   
1922 C  CB  . THR C 23  ? 0.1729 0.1557 0.2154 0.0188  0.0039  0.0269  23  THR C CB  
1923 O  OG1 . THR C 23  ? 0.1734 0.1777 0.2095 -0.0030 0.0132  0.0226  23  THR C OG1 
1924 C  CG2 . THR C 23  ? 0.1924 0.1590 0.2397 0.0281  -0.0111 0.0367  23  THR C CG2 
1925 N  N   . GLN C 24  ? 0.1851 0.1786 0.2173 -0.0010 0.0189  0.0425  24  GLN C N   
1926 C  CA  . GLN C 24  ? 0.1969 0.1849 0.2255 -0.0144 0.0214  0.0380  24  GLN C CA  
1927 C  C   . GLN C 24  ? 0.2037 0.1929 0.2154 0.0080  0.0110  0.0257  24  GLN C C   
1928 O  O   . GLN C 24  ? 0.2214 0.2059 0.2097 0.0098  0.0111  0.0319  24  GLN C O   
1929 C  CB  . GLN C 24  ? 0.2252 0.1911 0.2638 -0.0277 0.0203  0.0382  24  GLN C CB  
1930 C  CG  . GLN C 24  ? 0.2366 0.1983 0.3109 -0.0290 0.0164  0.0271  24  GLN C CG  
1931 C  CD  . GLN C 24  ? 0.2725 0.2543 0.3703 -0.0393 0.0099  0.0076  24  GLN C CD  
1932 O  OE1 . GLN C 24  ? 0.2974 0.2792 0.3978 -0.0550 0.0056  0.0008  24  GLN C OE1 
1933 N  NE2 . GLN C 24  ? 0.2947 0.2825 0.3927 -0.0486 -0.0041 0.0112  24  GLN C NE2 
1934 N  N   . GLN C 25  ? 0.1952 0.1809 0.2151 0.0092  0.0101  0.0263  25  GLN C N   
1935 C  CA  . GLN C 25  ? 0.2151 0.1924 0.2377 -0.0033 -0.0138 0.0289  25  GLN C CA  
1936 C  C   . GLN C 25  ? 0.2054 0.1824 0.2112 -0.0115 -0.0110 0.0351  25  GLN C C   
1937 O  O   . GLN C 25  ? 0.2197 0.1853 0.2047 -0.0116 -0.0165 0.0301  25  GLN C O   
1938 C  CB  . GLN C 25  ? 0.2379 0.2113 0.2806 -0.0065 -0.0259 0.0245  25  GLN C CB  
1939 C  CG  . GLN C 25  ? 0.3054 0.2508 0.3287 -0.0187 0.0026  0.0120  25  GLN C CG  
1940 C  CD  . GLN C 25  ? 0.4017 0.3091 0.3797 -0.0277 0.0473  0.0197  25  GLN C CD  
1941 O  OE1 . GLN C 25  ? 0.4481 0.3389 0.4055 -0.0388 0.0651  0.0220  25  GLN C OE1 
1942 N  NE2 . GLN C 25  ? 0.4440 0.3365 0.3929 -0.0304 0.0634  0.0269  25  GLN C NE2 
1943 N  N   . LEU C 26  ? 0.1916 0.1671 0.2079 -0.0063 -0.0075 0.0427  26  LEU C N   
1944 C  CA  . LEU C 26  ? 0.1889 0.2004 0.2129 -0.0075 -0.0198 0.0432  26  LEU C CA  
1945 C  C   . LEU C 26  ? 0.2246 0.1940 0.2205 -0.0078 -0.0476 0.0566  26  LEU C C   
1946 O  O   . LEU C 26  ? 0.2433 0.2128 0.2166 -0.0088 -0.0557 0.0485  26  LEU C O   
1947 C  CB  . LEU C 26  ? 0.1717 0.2268 0.2143 -0.0093 -0.0103 0.0375  26  LEU C CB  
1948 C  CG  . LEU C 26  ? 0.1896 0.2556 0.2265 -0.0359 -0.0129 0.0324  26  LEU C CG  
1949 C  CD1 . LEU C 26  ? 0.2013 0.3013 0.2253 -0.0458 0.0137  0.0134  26  LEU C CD1 
1950 C  CD2 . LEU C 26  ? 0.2179 0.2390 0.2575 -0.0233 -0.0221 0.0468  26  LEU C CD2 
1951 N  N   . ALA C 27  ? 0.2484 0.1918 0.2459 0.0066  -0.0827 0.0571  27  ALA C N   
1952 C  CA  . ALA C 27  ? 0.2902 0.2125 0.2643 0.0121  -0.1038 0.0611  27  ALA C CA  
1953 C  C   . ALA C 27  ? 0.3158 0.2160 0.2664 0.0067  -0.1170 0.0539  27  ALA C C   
1954 O  O   . ALA C 27  ? 0.3399 0.2419 0.2820 0.0075  -0.1309 0.0389  27  ALA C O   
1955 C  CB  . ALA C 27  ? 0.2970 0.2111 0.2764 0.0064  -0.1036 0.0523  27  ALA C CB  
1956 N  N   . GLN C 28  ? 0.3279 0.2044 0.2560 -0.0067 -0.0920 0.0608  28  GLN C N   
1957 C  CA  . GLN C 28  ? 0.3551 0.2275 0.2571 -0.0366 -0.0624 0.0577  28  GLN C CA  
1958 C  C   . GLN C 28  ? 0.3385 0.2244 0.2381 -0.0256 -0.0567 0.0591  28  GLN C C   
1959 O  O   . GLN C 28  ? 0.3614 0.2371 0.2394 -0.0139 -0.0638 0.0625  28  GLN C O   
1960 C  CB  . GLN C 28  ? 0.4189 0.2638 0.2886 -0.0859 -0.0389 0.0514  28  GLN C CB  
1961 C  CG  . GLN C 28  ? 0.4999 0.3194 0.3323 -0.0831 -0.0256 0.0553  28  GLN C CG  
1962 C  CD  . GLN C 28  ? 0.5521 0.3725 0.3854 -0.0763 -0.0065 0.0566  28  GLN C CD  
1963 O  OE1 . GLN C 28  ? 0.5822 0.4053 0.4183 -0.0725 0.0037  0.0649  28  GLN C OE1 
1964 N  NE2 . GLN C 28  ? 0.5598 0.3757 0.3993 -0.0751 -0.0020 0.0442  28  GLN C NE2 
1965 N  N   . ALA C 29  ? 0.2847 0.2011 0.2249 -0.0264 -0.0405 0.0559  29  ALA C N   
1966 C  CA  . ALA C 29  ? 0.2587 0.2042 0.2211 -0.0173 -0.0516 0.0475  29  ALA C CA  
1967 C  C   . ALA C 29  ? 0.2660 0.2211 0.2196 -0.0323 -0.0575 0.0509  29  ALA C C   
1968 O  O   . ALA C 29  ? 0.2792 0.2371 0.2144 -0.0521 -0.0627 0.0333  29  ALA C O   
1969 C  CB  . ALA C 29  ? 0.2515 0.2034 0.2200 -0.0230 -0.0556 0.0443  29  ALA C CB  
1970 N  N   . THR C 30  ? 0.2558 0.2077 0.2254 -0.0069 -0.0697 0.0618  30  THR C N   
1971 C  CA  . THR C 30  ? 0.2582 0.2196 0.2277 -0.0172 -0.0668 0.0625  30  THR C CA  
1972 C  C   . THR C 30  ? 0.2645 0.2196 0.2234 -0.0168 -0.0755 0.0519  30  THR C C   
1973 O  O   . THR C 30  ? 0.2601 0.2089 0.2298 -0.0223 -0.0857 0.0403  30  THR C O   
1974 C  CB  . THR C 30  ? 0.2692 0.2320 0.2362 -0.0325 -0.0645 0.0667  30  THR C CB  
1975 O  OG1 . THR C 30  ? 0.2731 0.2227 0.2348 -0.0427 -0.0557 0.0551  30  THR C OG1 
1976 C  CG2 . THR C 30  ? 0.2723 0.2463 0.2436 -0.0509 -0.0644 0.0815  30  THR C CG2 
1977 N  N   . GLY C 31  ? 0.2681 0.2557 0.2180 -0.0187 -0.0637 0.0747  31  GLY C N   
1978 C  CA  . GLY C 31  ? 0.2722 0.2933 0.2231 0.0095  -0.0490 0.0970  31  GLY C CA  
1979 C  C   . GLY C 31  ? 0.2894 0.3124 0.2431 0.0241  -0.0463 0.1083  31  GLY C C   
1980 O  O   . GLY C 31  ? 0.3362 0.3808 0.2656 0.0451  -0.0351 0.0900  31  GLY C O   
1981 N  N   . LYS C 32  ? 0.2756 0.2552 0.2515 -0.0039 -0.0544 0.0871  32  LYS C N   
1982 C  CA  . LYS C 32  ? 0.2897 0.2022 0.2536 -0.0273 -0.0570 0.0793  32  LYS C CA  
1983 C  C   . LYS C 32  ? 0.2997 0.2027 0.2364 -0.0381 -0.0839 0.0685  32  LYS C C   
1984 O  O   . LYS C 32  ? 0.3091 0.2346 0.2533 -0.0560 -0.0824 0.0638  32  LYS C O   
1985 C  CB  . LYS C 32  ? 0.2962 0.1837 0.2773 -0.0317 -0.0393 0.0695  32  LYS C CB  
1986 C  CG  . LYS C 32  ? 0.3017 0.1969 0.2991 -0.0342 -0.0271 0.0513  32  LYS C CG  
1987 C  CD  . LYS C 32  ? 0.3080 0.2122 0.2992 -0.0362 -0.0190 0.0455  32  LYS C CD  
1988 C  CE  . LYS C 32  ? 0.2897 0.2141 0.2903 -0.0385 -0.0107 0.0605  32  LYS C CE  
1989 N  NZ  . LYS C 32  ? 0.2806 0.2196 0.2824 -0.0282 -0.0008 0.0674  32  LYS C NZ  
1990 N  N   . PRO C 33  ? 0.3399 0.1973 0.2238 -0.0406 -0.0753 0.0353  33  PRO C N   
1991 C  CA  . PRO C 33  ? 0.3498 0.1973 0.2224 -0.0352 -0.0842 0.0257  33  PRO C CA  
1992 C  C   . PRO C 33  ? 0.3241 0.1980 0.2194 -0.0454 -0.0551 0.0325  33  PRO C C   
1993 O  O   . PRO C 33  ? 0.3099 0.1855 0.2196 -0.0295 -0.0648 0.0385  33  PRO C O   
1994 C  CB  . PRO C 33  ? 0.3656 0.2048 0.2309 -0.0196 -0.0947 0.0192  33  PRO C CB  
1995 C  CG  . PRO C 33  ? 0.3633 0.1990 0.2265 -0.0299 -0.0863 0.0251  33  PRO C CG  
1996 C  CD  . PRO C 33  ? 0.3511 0.1911 0.2201 -0.0369 -0.0696 0.0195  33  PRO C CD  
1997 N  N   . PRO C 34  ? 0.3129 0.1957 0.2150 -0.0551 -0.0255 0.0364  34  PRO C N   
1998 C  CA  . PRO C 34  ? 0.2850 0.1888 0.2144 -0.0450 -0.0222 0.0305  34  PRO C CA  
1999 C  C   . PRO C 34  ? 0.2656 0.1687 0.2221 -0.0162 -0.0286 0.0433  34  PRO C C   
2000 O  O   . PRO C 34  ? 0.2512 0.1780 0.2209 -0.0185 -0.0166 0.0296  34  PRO C O   
2001 C  CB  . PRO C 34  ? 0.3159 0.2324 0.2330 -0.0518 -0.0078 0.0220  34  PRO C CB  
2002 C  CG  . PRO C 34  ? 0.3532 0.2754 0.2453 -0.0710 -0.0023 0.0207  34  PRO C CG  
2003 C  CD  . PRO C 34  ? 0.3414 0.2384 0.2258 -0.0597 -0.0065 0.0360  34  PRO C CD  
2004 N  N   . GLN C 35  ? 0.2656 0.1683 0.2518 -0.0004 -0.0392 0.0482  35  GLN C N   
2005 C  CA  . GLN C 35  ? 0.2894 0.2125 0.2981 0.0136  -0.0313 0.0514  35  GLN C CA  
2006 C  C   . GLN C 35  ? 0.2484 0.1772 0.2869 -0.0130 -0.0446 0.0487  35  GLN C C   
2007 O  O   . GLN C 35  ? 0.2757 0.1890 0.2927 -0.0185 -0.0376 0.0475  35  GLN C O   
2008 C  CB  . GLN C 35  ? 0.3582 0.3355 0.3526 0.0087  -0.0062 0.0235  35  GLN C CB  
2009 C  CG  . GLN C 35  ? 0.3775 0.3749 0.3764 0.0023  -0.0013 0.0061  35  GLN C CG  
2010 C  CD  . GLN C 35  ? 0.3808 0.3817 0.3796 0.0035  0.0009  0.0006  35  GLN C CD  
2011 O  OE1 . GLN C 35  ? 0.3844 0.3869 0.3841 0.0043  -0.0037 0.0039  35  GLN C OE1 
2012 N  NE2 . GLN C 35  ? 0.3810 0.3849 0.3832 -0.0002 -0.0008 -0.0002 35  GLN C NE2 
2013 N  N   . TYR C 36  ? 0.2026 0.1566 0.2845 -0.0039 -0.0562 0.0503  36  TYR C N   
2014 C  CA  . TYR C 36  ? 0.1981 0.1734 0.2930 -0.0090 -0.0628 0.0636  36  TYR C CA  
2015 C  C   . TYR C 36  ? 0.1891 0.1877 0.2577 0.0007  -0.0387 0.0675  36  TYR C C   
2016 O  O   . TYR C 36  ? 0.1733 0.2191 0.2548 -0.0021 -0.0101 0.0827  36  TYR C O   
2017 C  CB  . TYR C 36  ? 0.2149 0.2065 0.3457 -0.0004 -0.0952 0.0577  36  TYR C CB  
2018 C  CG  . TYR C 36  ? 0.2424 0.2487 0.3991 0.0110  -0.1123 0.0579  36  TYR C CG  
2019 C  CD1 . TYR C 36  ? 0.2463 0.2863 0.4286 0.0131  -0.1152 0.0713  36  TYR C CD1 
2020 C  CD2 . TYR C 36  ? 0.2616 0.2701 0.4142 0.0183  -0.1322 0.0470  36  TYR C CD2 
2021 C  CE1 . TYR C 36  ? 0.2669 0.3064 0.4512 0.0216  -0.1317 0.0724  36  TYR C CE1 
2022 C  CE2 . TYR C 36  ? 0.2705 0.2893 0.4379 0.0237  -0.1497 0.0493  36  TYR C CE2 
2023 C  CZ  . TYR C 36  ? 0.2684 0.3128 0.4632 0.0383  -0.1521 0.0591  36  TYR C CZ  
2024 O  OH  . TYR C 36  ? 0.2856 0.3388 0.4994 0.0752  -0.1443 0.0526  36  TYR C OH  
2025 N  N   . ILE C 37  ? 0.1778 0.1856 0.2229 -0.0047 -0.0297 0.0516  37  ILE C N   
2026 C  CA  . ILE C 37  ? 0.1656 0.1861 0.2055 -0.0064 -0.0272 0.0507  37  ILE C CA  
2027 C  C   . ILE C 37  ? 0.1629 0.1613 0.1977 -0.0114 -0.0139 0.0400  37  ILE C C   
2028 O  O   . ILE C 37  ? 0.1819 0.1541 0.2150 0.0005  -0.0214 0.0357  37  ILE C O   
2029 C  CB  . ILE C 37  ? 0.1804 0.2019 0.2163 -0.0163 -0.0224 0.0425  37  ILE C CB  
2030 C  CG1 . ILE C 37  ? 0.2172 0.2348 0.2377 -0.0411 -0.0462 0.0208  37  ILE C CG1 
2031 C  CG2 . ILE C 37  ? 0.1842 0.1834 0.2160 -0.0031 -0.0170 0.0493  37  ILE C CG2 
2032 C  CD1 . ILE C 37  ? 0.2648 0.2614 0.2558 -0.0372 -0.0356 0.0155  37  ILE C CD1 
2033 N  N   . ALA C 38  ? 0.1531 0.1518 0.1824 -0.0027 -0.0069 0.0351  38  ALA C N   
2034 C  CA  . ALA C 38  ? 0.1547 0.1489 0.1946 0.0112  -0.0105 0.0329  38  ALA C CA  
2035 C  C   . ALA C 38  ? 0.1463 0.1360 0.2002 -0.0013 -0.0078 0.0430  38  ALA C C   
2036 O  O   . ALA C 38  ? 0.1594 0.1190 0.2141 -0.0024 -0.0227 0.0265  38  ALA C O   
2037 C  CB  . ALA C 38  ? 0.1571 0.1810 0.2057 0.0140  -0.0062 0.0236  38  ALA C CB  
2038 N  N   . VAL C 39  ? 0.1450 0.1448 0.1922 0.0077  -0.0095 0.0381  39  VAL C N   
2039 C  CA  . VAL C 39  ? 0.1550 0.1453 0.1896 -0.0067 -0.0090 0.0308  39  VAL C CA  
2040 C  C   . VAL C 39  ? 0.1693 0.1300 0.1862 -0.0001 -0.0251 0.0162  39  VAL C C   
2041 O  O   . VAL C 39  ? 0.1826 0.1339 0.1969 0.0055  -0.0178 0.0107  39  VAL C O   
2042 C  CB  . VAL C 39  ? 0.1597 0.1702 0.2116 -0.0165 0.0050  0.0250  39  VAL C CB  
2043 C  CG1 . VAL C 39  ? 0.1700 0.2085 0.2088 -0.0001 0.0205  0.0256  39  VAL C CG1 
2044 C  CG2 . VAL C 39  ? 0.1869 0.1995 0.2480 -0.0282 0.0024  0.0149  39  VAL C CG2 
2045 N  N   . HIS C 40  ? 0.1879 0.1358 0.1655 0.0022  -0.0387 0.0121  40  HIS C N   
2046 C  CA  . HIS C 40  ? 0.1731 0.1417 0.1605 0.0040  -0.0425 0.0251  40  HIS C CA  
2047 C  C   . HIS C 40  ? 0.1682 0.1392 0.1646 0.0064  -0.0303 0.0170  40  HIS C C   
2048 O  O   . HIS C 40  ? 0.1916 0.1314 0.1872 0.0198  -0.0276 0.0041  40  HIS C O   
2049 C  CB  . HIS C 40  ? 0.1735 0.1459 0.1810 0.0008  -0.0117 0.0206  40  HIS C CB  
2050 C  CG  . HIS C 40  ? 0.1884 0.1447 0.2018 0.0179  0.0083  0.0207  40  HIS C CG  
2051 N  ND1 . HIS C 40  ? 0.1925 0.1519 0.2178 0.0348  0.0233  0.0247  40  HIS C ND1 
2052 C  CD2 . HIS C 40  ? 0.2143 0.1514 0.2017 0.0334  0.0089  0.0032  40  HIS C CD2 
2053 C  CE1 . HIS C 40  ? 0.2118 0.1681 0.2206 0.0373  0.0196  0.0146  40  HIS C CE1 
2054 N  NE2 . HIS C 40  ? 0.2117 0.1677 0.2188 0.0426  0.0172  0.0022  40  HIS C NE2 
2055 N  N   . VAL C 41  ? 0.1541 0.1480 0.1728 -0.0032 -0.0130 0.0238  41  VAL C N   
2056 C  CA  . VAL C 41  ? 0.1482 0.1540 0.1875 -0.0101 -0.0119 0.0338  41  VAL C CA  
2057 C  C   . VAL C 41  ? 0.1534 0.1360 0.1894 0.0016  -0.0055 0.0205  41  VAL C C   
2058 O  O   . VAL C 41  ? 0.1723 0.1405 0.1890 0.0076  -0.0000 -0.0005 41  VAL C O   
2059 C  CB  . VAL C 41  ? 0.1787 0.1955 0.2093 -0.0173 -0.0037 0.0314  41  VAL C CB  
2060 C  CG1 . VAL C 41  ? 0.1673 0.1992 0.2283 -0.0204 -0.0099 0.0231  41  VAL C CG1 
2061 C  CG2 . VAL C 41  ? 0.2187 0.2330 0.2191 -0.0149 0.0129  0.0296  41  VAL C CG2 
2062 N  N   . VAL C 42  ? 0.1426 0.1529 0.1759 -0.0138 -0.0070 0.0197  42  VAL C N   
2063 C  CA  . VAL C 42  ? 0.1416 0.1672 0.1759 -0.0113 -0.0143 0.0195  42  VAL C CA  
2064 C  C   . VAL C 42  ? 0.1535 0.1559 0.1767 0.0045  -0.0182 -0.0010 42  VAL C C   
2065 O  O   . VAL C 42  ? 0.1605 0.1573 0.1811 0.0097  -0.0165 -0.0005 42  VAL C O   
2066 C  CB  . VAL C 42  ? 0.1617 0.1880 0.1967 0.0001  0.0057  0.0321  42  VAL C CB  
2067 C  CG1 . VAL C 42  ? 0.2081 0.2162 0.1989 0.0102  0.0033  0.0211  42  VAL C CG1 
2068 C  CG2 . VAL C 42  ? 0.1768 0.1940 0.2197 0.0075  -0.0069 0.0314  42  VAL C CG2 
2069 N  N   . PRO C 43  ? 0.1473 0.1533 0.2085 0.0002  -0.0075 -0.0049 43  PRO C N   
2070 C  CA  . PRO C 43  ? 0.1473 0.1644 0.2174 -0.0169 -0.0002 0.0060  43  PRO C CA  
2071 C  C   . PRO C 43  ? 0.1520 0.1492 0.1975 -0.0259 -0.0018 0.0060  43  PRO C C   
2072 O  O   . PRO C 43  ? 0.1682 0.1560 0.1983 -0.0148 -0.0137 -0.0022 43  PRO C O   
2073 C  CB  . PRO C 43  ? 0.1675 0.1706 0.2487 -0.0239 -0.0000 0.0117  43  PRO C CB  
2074 C  CG  . PRO C 43  ? 0.1926 0.1748 0.2667 -0.0203 -0.0095 -0.0063 43  PRO C CG  
2075 C  CD  . PRO C 43  ? 0.1780 0.1505 0.2450 -0.0192 -0.0076 -0.0148 43  PRO C CD  
2076 N  N   . ASP C 44  ? 0.1593 0.1738 0.1930 -0.0235 -0.0200 0.0010  44  ASP C N   
2077 C  CA  . ASP C 44  ? 0.1909 0.1947 0.2048 -0.0324 -0.0208 -0.0082 44  ASP C CA  
2078 C  C   . ASP C 44  ? 0.1779 0.1836 0.1925 -0.0090 -0.0058 -0.0028 44  ASP C C   
2079 O  O   . ASP C 44  ? 0.2006 0.1919 0.1993 -0.0121 -0.0094 -0.0050 44  ASP C O   
2080 C  CB  . ASP C 44  ? 0.2656 0.2458 0.2424 -0.0787 -0.0300 -0.0229 44  ASP C CB  
2081 C  CG  . ASP C 44  ? 0.3470 0.3211 0.2904 -0.0755 -0.0312 -0.0325 44  ASP C CG  
2082 O  OD1 . ASP C 44  ? 0.3519 0.3502 0.3063 -0.0982 -0.0229 -0.0574 44  ASP C OD1 
2083 O  OD2 . ASP C 44  ? 0.3986 0.3578 0.3144 -0.0629 -0.0359 -0.0216 44  ASP C OD2 
2084 N  N   . GLN C 45  ? 0.1498 0.1700 0.1816 -0.0010 -0.0023 0.0028  45  GLN C N   
2085 C  CA  . GLN C 45  ? 0.1424 0.1685 0.1793 -0.0036 -0.0168 0.0088  45  GLN C CA  
2086 C  C   . GLN C 45  ? 0.1393 0.1816 0.1760 0.0143  -0.0118 0.0064  45  GLN C C   
2087 O  O   . GLN C 45  ? 0.1396 0.2191 0.1931 0.0348  0.0018  0.0307  45  GLN C O   
2088 C  CB  . GLN C 45  ? 0.1399 0.1690 0.1844 0.0062  -0.0213 0.0117  45  GLN C CB  
2089 C  CG  . GLN C 45  ? 0.1377 0.1694 0.1948 0.0198  -0.0038 0.0136  45  GLN C CG  
2090 C  CD  . GLN C 45  ? 0.1452 0.1592 0.2087 0.0110  -0.0016 -0.0016 45  GLN C CD  
2091 O  OE1 . GLN C 45  ? 0.1570 0.1828 0.2258 -0.0153 0.0279  -0.0161 45  GLN C OE1 
2092 N  NE2 . GLN C 45  ? 0.1662 0.1530 0.2148 0.0171  -0.0191 -0.0147 45  GLN C NE2 
2093 N  N   . LEU C 46  ? 0.1604 0.1574 0.1595 0.0091  -0.0212 -0.0075 46  LEU C N   
2094 C  CA  . LEU C 46  ? 0.1623 0.1570 0.1585 0.0140  -0.0191 -0.0034 46  LEU C CA  
2095 C  C   . LEU C 46  ? 0.1517 0.1385 0.1562 0.0066  -0.0116 -0.0066 46  LEU C C   
2096 O  O   . LEU C 46  ? 0.1580 0.1644 0.1713 0.0034  -0.0031 -0.0154 46  LEU C O   
2097 C  CB  . LEU C 46  ? 0.1667 0.1970 0.1725 0.0193  -0.0158 0.0093  46  LEU C CB  
2098 C  CG  . LEU C 46  ? 0.1786 0.2620 0.2051 0.0147  -0.0082 0.0070  46  LEU C CG  
2099 C  CD1 . LEU C 46  ? 0.1738 0.2861 0.2281 0.0017  -0.0213 0.0046  46  LEU C CD1 
2100 C  CD2 . LEU C 46  ? 0.2073 0.2802 0.2061 0.0180  0.0009  0.0004  46  LEU C CD2 
2101 N  N   . MET C 47  ? 0.1684 0.1570 0.1531 0.0227  -0.0165 -0.0034 47  MET C N   
2102 C  CA  . MET C 47  ? 0.1829 0.1752 0.1672 0.0399  -0.0317 -0.0124 47  MET C CA  
2103 C  C   . MET C 47  ? 0.1440 0.1796 0.1739 0.0300  -0.0049 -0.0197 47  MET C C   
2104 O  O   . MET C 47  ? 0.1425 0.1925 0.1998 0.0198  -0.0043 -0.0206 47  MET C O   
2105 C  CB  . MET C 47  ? 0.2809 0.2241 0.2031 0.0616  -0.0551 -0.0206 47  MET C CB  
2106 C  CG  . MET C 47  ? 0.3136 0.2341 0.2255 0.0344  -0.0329 -0.0033 47  MET C CG  
2107 S  SD  . MET C 47  ? 0.2931 0.1980 0.2264 -0.0029 -0.0158 0.0297  47  MET C SD  
2108 C  CE  . MET C 47  ? 0.2529 0.1359 0.2083 0.0473  0.0262  0.0612  47  MET C CE  
2109 N  N   . ALA C 48  ? 0.1353 0.1656 0.1642 0.0243  -0.0029 -0.0162 48  ALA C N   
2110 C  CA  . ALA C 48  ? 0.1445 0.1727 0.1598 0.0369  -0.0030 -0.0121 48  ALA C CA  
2111 C  C   . ALA C 48  ? 0.1440 0.1638 0.1536 0.0305  -0.0011 -0.0169 48  ALA C C   
2112 O  O   . ALA C 48  ? 0.1455 0.1492 0.1582 0.0176  0.0126  -0.0083 48  ALA C O   
2113 C  CB  . ALA C 48  ? 0.1884 0.1827 0.1738 0.0495  -0.0095 -0.0049 48  ALA C CB  
2114 N  N   . PHE C 49  ? 0.1536 0.1627 0.1479 0.0290  0.0075  -0.0065 49  PHE C N   
2115 C  CA  . PHE C 49  ? 0.1592 0.1630 0.1546 0.0268  0.0061  0.0024  49  PHE C CA  
2116 C  C   . PHE C 49  ? 0.1653 0.1523 0.1670 0.0262  0.0154  0.0112  49  PHE C C   
2117 O  O   . PHE C 49  ? 0.1557 0.1676 0.1735 0.0286  0.0071  0.0092  49  PHE C O   
2118 C  CB  . PHE C 49  ? 0.1619 0.1743 0.1571 0.0214  -0.0008 0.0138  49  PHE C CB  
2119 C  CG  . PHE C 49  ? 0.1624 0.1937 0.1568 0.0144  -0.0086 0.0302  49  PHE C CG  
2120 C  CD1 . PHE C 49  ? 0.1962 0.2015 0.1609 -0.0041 -0.0086 0.0182  49  PHE C CD1 
2121 C  CD2 . PHE C 49  ? 0.1659 0.2327 0.1661 0.0033  -0.0111 0.0425  49  PHE C CD2 
2122 C  CE1 . PHE C 49  ? 0.2246 0.2200 0.1643 -0.0218 -0.0024 0.0189  49  PHE C CE1 
2123 C  CE2 . PHE C 49  ? 0.1902 0.2484 0.1692 -0.0074 0.0022  0.0399  49  PHE C CE2 
2124 C  CZ  . PHE C 49  ? 0.2129 0.2353 0.1730 -0.0205 0.0057  0.0325  49  PHE C CZ  
2125 N  N   . GLY C 50  ? 0.1806 0.1489 0.1766 0.0225  0.0184  0.0168  50  GLY C N   
2126 C  CA  . GLY C 50  ? 0.1964 0.1718 0.1932 0.0317  0.0068  0.0164  50  GLY C CA  
2127 C  C   . GLY C 50  ? 0.1916 0.1888 0.2007 0.0441  0.0019  0.0213  50  GLY C C   
2128 O  O   . GLY C 50  ? 0.2097 0.2064 0.2271 0.0629  0.0029  0.0162  50  GLY C O   
2129 N  N   . GLY C 51  ? 0.1820 0.1990 0.1821 0.0330  -0.0211 0.0265  51  GLY C N   
2130 C  CA  . GLY C 51  ? 0.1812 0.2295 0.1936 0.0459  -0.0323 0.0328  51  GLY C CA  
2131 C  C   . GLY C 51  ? 0.1849 0.2473 0.2131 0.0542  -0.0389 0.0267  51  GLY C C   
2132 O  O   . GLY C 51  ? 0.2035 0.3061 0.2238 0.0461  -0.0556 0.0151  51  GLY C O   
2133 N  N   . SER C 52  ? 0.1713 0.2060 0.2363 0.0612  -0.0161 0.0377  52  SER C N   
2134 C  CA  . SER C 52  ? 0.1691 0.2213 0.2581 0.0395  0.0041  0.0305  52  SER C CA  
2135 C  C   . SER C 52  ? 0.1695 0.2143 0.2320 0.0252  -0.0221 0.0195  52  SER C C   
2136 O  O   . SER C 52  ? 0.1395 0.1951 0.2327 0.0342  -0.0206 0.0045  52  SER C O   
2137 C  CB  . SER C 52  ? 0.1776 0.2424 0.3080 0.0434  0.0379  0.0292  52  SER C CB  
2138 O  OG  . SER C 52  ? 0.2089 0.2842 0.3399 0.0673  0.0169  0.0324  52  SER C OG  
2139 N  N   . SER C 53  ? 0.1876 0.2238 0.2275 0.0251  -0.0376 0.0079  53  SER C N   
2140 C  CA  . SER C 53  ? 0.2014 0.2455 0.2366 0.0103  -0.0371 -0.0040 53  SER C CA  
2141 C  C   . SER C 53  ? 0.1790 0.2529 0.2376 0.0297  -0.0464 0.0127  53  SER C C   
2142 O  O   . SER C 53  ? 0.1878 0.2455 0.2427 0.0299  -0.0501 0.0147  53  SER C O   
2143 C  CB  . SER C 53  ? 0.2360 0.2744 0.2541 0.0076  -0.0250 0.0041  53  SER C CB  
2144 O  OG  . SER C 53  ? 0.2495 0.2857 0.2623 0.0206  -0.0340 0.0255  53  SER C OG  
2145 N  N   . GLU C 54  ? 0.1569 0.2573 0.2441 0.0432  -0.0322 0.0314  54  GLU C N   
2146 C  CA  . GLU C 54  ? 0.1681 0.2753 0.2681 0.0374  -0.0349 0.0216  54  GLU C CA  
2147 C  C   . GLU C 54  ? 0.1317 0.2396 0.2366 0.0149  -0.0285 0.0054  54  GLU C C   
2148 O  O   . GLU C 54  ? 0.1416 0.2254 0.2231 0.0226  -0.0210 0.0073  54  GLU C O   
2149 C  CB  . GLU C 54  ? 0.2023 0.3573 0.3291 0.0594  -0.0636 0.0369  54  GLU C CB  
2150 C  CG  . GLU C 54  ? 0.2799 0.4537 0.3936 0.0489  -0.0878 0.0512  54  GLU C CG  
2151 C  CD  . GLU C 54  ? 0.3739 0.5372 0.4447 0.0438  -0.1078 0.0684  54  GLU C CD  
2152 O  OE1 . GLU C 54  ? 0.4134 0.5575 0.4654 0.0433  -0.1001 0.0768  54  GLU C OE1 
2153 O  OE2 . GLU C 54  ? 0.3944 0.5746 0.4604 0.0345  -0.1339 0.0667  54  GLU C OE2 
2154 N  N   . PRO C 55  ? 0.1208 0.2366 0.2425 0.0071  -0.0204 0.0012  55  PRO C N   
2155 C  CA  . PRO C 55  ? 0.1341 0.2260 0.2159 0.0022  -0.0168 0.0040  55  PRO C CA  
2156 C  C   . PRO C 55  ? 0.1427 0.1920 0.1940 0.0134  -0.0127 0.0090  55  PRO C C   
2157 O  O   . PRO C 55  ? 0.1508 0.1946 0.1813 0.0128  -0.0105 0.0040  55  PRO C O   
2158 C  CB  . PRO C 55  ? 0.1475 0.2250 0.2313 -0.0144 -0.0138 0.0001  55  PRO C CB  
2159 C  CG  . PRO C 55  ? 0.1535 0.2378 0.2562 -0.0030 -0.0298 -0.0020 55  PRO C CG  
2160 C  CD  . PRO C 55  ? 0.1311 0.2531 0.2615 0.0143  -0.0305 0.0051  55  PRO C CD  
2161 N  N   . CYS C 56  ? 0.1245 0.1619 0.1839 0.0047  -0.0105 0.0183  56  CYS C N   
2162 C  CA  . CYS C 56  ? 0.1352 0.1601 0.1869 0.0105  -0.0025 0.0153  56  CYS C CA  
2163 C  C   . CYS C 56  ? 0.1338 0.1481 0.1918 0.0111  -0.0094 0.0200  56  CYS C C   
2164 O  O   . CYS C 56  ? 0.1303 0.1515 0.2057 0.0118  -0.0072 0.0095  56  CYS C O   
2165 C  CB  . CYS C 56  ? 0.1689 0.1763 0.1820 0.0094  0.0054  0.0136  56  CYS C CB  
2166 S  SG  . CYS C 56  ? 0.2003 0.1887 0.1958 -0.0029 0.0187  0.0101  56  CYS C SG  
2167 N  N   . ALA C 57  ? 0.1279 0.1517 0.1873 0.0097  -0.0070 0.0131  57  ALA C N   
2168 C  CA  . ALA C 57  ? 0.1351 0.1673 0.1925 0.0202  -0.0057 0.0173  57  ALA C CA  
2169 C  C   . ALA C 57  ? 0.1270 0.1449 0.1683 0.0265  -0.0114 0.0030  57  ALA C C   
2170 O  O   . ALA C 57  ? 0.1483 0.1536 0.1774 0.0173  0.0005  -0.0091 57  ALA C O   
2171 C  CB  . ALA C 57  ? 0.1540 0.1744 0.2125 0.0189  -0.0098 0.0423  57  ALA C CB  
2172 N  N   . LEU C 58  ? 0.1281 0.1517 0.1668 0.0201  -0.0143 0.0007  58  LEU C N   
2173 C  CA  . LEU C 58  ? 0.1496 0.1507 0.1662 0.0182  -0.0084 0.0080  58  LEU C CA  
2174 C  C   . LEU C 58  ? 0.1384 0.1280 0.1662 0.0100  -0.0088 0.0026  58  LEU C C   
2175 O  O   . LEU C 58  ? 0.1391 0.1352 0.1685 0.0016  -0.0034 -0.0062 58  LEU C O   
2176 C  CB  . LEU C 58  ? 0.2004 0.1501 0.1539 0.0305  0.0063  0.0161  58  LEU C CB  
2177 C  CG  . LEU C 58  ? 0.2642 0.1589 0.1617 0.0340  0.0009  0.0331  58  LEU C CG  
2178 C  CD1 . LEU C 58  ? 0.2999 0.1818 0.1705 0.0326  0.0201  0.0381  58  LEU C CD1 
2179 C  CD2 . LEU C 58  ? 0.2713 0.1491 0.1813 0.0357  -0.0017 0.0135  58  LEU C CD2 
2180 N  N   . CYS C 59  ? 0.1439 0.1296 0.1663 0.0141  -0.0134 0.0178  59  CYS C N   
2181 C  CA  . CYS C 59  ? 0.1417 0.1356 0.1729 0.0062  -0.0102 0.0146  59  CYS C CA  
2182 C  C   . CYS C 59  ? 0.1290 0.1382 0.1668 0.0065  -0.0109 0.0049  59  CYS C C   
2183 O  O   . CYS C 59  ? 0.1397 0.1367 0.1770 -0.0033 -0.0127 -0.0034 59  CYS C O   
2184 C  CB  . CYS C 59  ? 0.1320 0.1674 0.1837 0.0163  -0.0090 0.0117  59  CYS C CB  
2185 S  SG  . CYS C 59  ? 0.1612 0.1935 0.2148 -0.0002 0.0023  0.0149  59  CYS C SG  
2186 N  N   . SER C 60  ? 0.1223 0.1476 0.1809 0.0197  -0.0096 0.0175  60  SER C N   
2187 C  CA  . SER C 60  ? 0.1384 0.1502 0.1887 0.0103  -0.0128 0.0237  60  SER C CA  
2188 C  C   . SER C 60  ? 0.1373 0.1384 0.1755 0.0182  -0.0066 0.0195  60  SER C C   
2189 O  O   . SER C 60  ? 0.1622 0.1355 0.1698 0.0073  -0.0107 0.0154  60  SER C O   
2190 C  CB  . SER C 60  ? 0.1528 0.1705 0.1990 0.0154  -0.0103 0.0098  60  SER C CB  
2191 O  OG  . SER C 60  ? 0.1739 0.1790 0.1976 0.0336  0.0087  0.0177  60  SER C OG  
2192 N  N   . LEU C 61  ? 0.1468 0.1366 0.1724 0.0166  -0.0158 0.0281  61  LEU C N   
2193 C  CA  . LEU C 61  ? 0.1570 0.1555 0.1662 -0.0001 -0.0049 0.0239  61  LEU C CA  
2194 C  C   . LEU C 61  ? 0.1488 0.1441 0.1740 -0.0143 -0.0003 0.0195  61  LEU C C   
2195 O  O   . LEU C 61  ? 0.1608 0.1382 0.1811 -0.0102 -0.0176 0.0171  61  LEU C O   
2196 C  CB  . LEU C 61  ? 0.1720 0.1606 0.1606 0.0166  -0.0049 0.0300  61  LEU C CB  
2197 C  CG  . LEU C 61  ? 0.2141 0.1508 0.1739 0.0202  0.0040  0.0274  61  LEU C CG  
2198 C  CD1 . LEU C 61  ? 0.2380 0.1440 0.1981 0.0278  0.0070  0.0032  61  LEU C CD1 
2199 C  CD2 . LEU C 61  ? 0.2519 0.1846 0.1760 0.0164  0.0269  0.0175  61  LEU C CD2 
2200 N  N   . HIS C 62  ? 0.1434 0.1609 0.1781 0.0066  -0.0056 0.0103  62  HIS C N   
2201 C  CA  . HIS C 62  ? 0.1465 0.1640 0.1781 0.0118  -0.0069 0.0132  62  HIS C CA  
2202 C  C   . HIS C 62  ? 0.1669 0.1558 0.1801 -0.0002 -0.0215 0.0257  62  HIS C C   
2203 O  O   . HIS C 62  ? 0.1685 0.1607 0.1930 -0.0157 -0.0369 0.0330  62  HIS C O   
2204 C  CB  . HIS C 62  ? 0.1621 0.1822 0.1890 0.0275  0.0057  0.0051  62  HIS C CB  
2205 C  CG  . HIS C 62  ? 0.1832 0.2203 0.1940 0.0320  0.0092  -0.0036 62  HIS C CG  
2206 N  ND1 . HIS C 62  ? 0.1854 0.2489 0.2043 0.0203  0.0272  0.0061  62  HIS C ND1 
2207 C  CD2 . HIS C 62  ? 0.1975 0.2373 0.1887 0.0435  0.0186  0.0062  62  HIS C CD2 
2208 C  CE1 . HIS C 62  ? 0.1833 0.2546 0.1976 0.0366  0.0364  0.0100  62  HIS C CE1 
2209 N  NE2 . HIS C 62  ? 0.2049 0.2601 0.2014 0.0499  0.0296  0.0184  62  HIS C NE2 
2210 N  N   . SER C 63  ? 0.1714 0.1577 0.1732 -0.0076 -0.0237 0.0201  63  SER C N   
2211 C  CA  . SER C 63  ? 0.1700 0.1728 0.1749 -0.0033 -0.0268 0.0305  63  SER C CA  
2212 C  C   . SER C 63  ? 0.1642 0.1622 0.1786 0.0064  -0.0236 0.0250  63  SER C C   
2213 O  O   . SER C 63  ? 0.1624 0.1535 0.1932 -0.0030 -0.0217 0.0331  63  SER C O   
2214 C  CB  . SER C 63  ? 0.1747 0.1825 0.1771 -0.0072 -0.0190 0.0397  63  SER C CB  
2215 O  OG  . SER C 63  ? 0.1833 0.2026 0.1886 -0.0073 -0.0185 0.0344  63  SER C OG  
2216 N  N   . ILE C 64  ? 0.1590 0.1662 0.1783 0.0045  -0.0269 0.0206  64  ILE C N   
2217 C  CA  . ILE C 64  ? 0.1538 0.1878 0.1881 0.0167  -0.0281 0.0060  64  ILE C CA  
2218 C  C   . ILE C 64  ? 0.1675 0.1840 0.1861 0.0081  -0.0272 0.0070  64  ILE C C   
2219 O  O   . ILE C 64  ? 0.1829 0.2075 0.2039 0.0046  -0.0221 0.0154  64  ILE C O   
2220 C  CB  . ILE C 64  ? 0.1633 0.1999 0.2005 0.0275  -0.0237 0.0007  64  ILE C CB  
2221 C  CG1 . ILE C 64  ? 0.1771 0.2124 0.2078 0.0407  0.0019  0.0060  64  ILE C CG1 
2222 C  CG2 . ILE C 64  ? 0.1653 0.2128 0.2180 0.0071  -0.0459 0.0089  64  ILE C CG2 
2223 C  CD1 . ILE C 64  ? 0.1931 0.2163 0.2157 0.0488  0.0096  0.0156  64  ILE C CD1 
2224 N  N   . GLY C 65  ? 0.1821 0.1874 0.1838 0.0143  -0.0213 -0.0071 65  GLY C N   
2225 C  CA  . GLY C 65  ? 0.1941 0.2125 0.1836 0.0229  -0.0307 -0.0149 65  GLY C CA  
2226 C  C   . GLY C 65  ? 0.1866 0.1961 0.1901 0.0080  -0.0324 -0.0039 65  GLY C C   
2227 O  O   . GLY C 65  ? 0.1907 0.1988 0.1988 -0.0056 -0.0384 -0.0045 65  GLY C O   
2228 N  N   . LYS C 66  ? 0.1688 0.2080 0.1985 -0.0072 -0.0267 0.0130  66  LYS C N   
2229 C  CA  . LYS C 66  ? 0.1752 0.2104 0.2046 -0.0032 -0.0221 0.0214  66  LYS C CA  
2230 C  C   . LYS C 66  ? 0.1705 0.2186 0.2084 -0.0047 -0.0267 0.0306  66  LYS C C   
2231 O  O   . LYS C 66  ? 0.1657 0.2453 0.2325 -0.0063 -0.0237 0.0429  66  LYS C O   
2232 C  CB  . LYS C 66  ? 0.2149 0.2094 0.2070 0.0008  -0.0295 0.0127  66  LYS C CB  
2233 C  CG  . LYS C 66  ? 0.2598 0.2203 0.2086 -0.0033 -0.0340 0.0052  66  LYS C CG  
2234 C  CD  . LYS C 66  ? 0.3278 0.2362 0.2329 -0.0138 -0.0605 0.0153  66  LYS C CD  
2235 C  CE  . LYS C 66  ? 0.3679 0.2604 0.2746 -0.0486 -0.0778 0.0342  66  LYS C CE  
2236 N  NZ  . LYS C 66  ? 0.3903 0.2762 0.2866 -0.0722 -0.1020 0.0363  66  LYS C NZ  
2237 N  N   . ILE C 67  ? 0.1709 0.1854 0.1945 0.0010  -0.0078 0.0101  67  ILE C N   
2238 C  CA  . ILE C 67  ? 0.1808 0.1756 0.1880 0.0035  -0.0153 0.0106  67  ILE C CA  
2239 C  C   . ILE C 67  ? 0.1915 0.1914 0.2097 0.0089  -0.0175 -0.0027 67  ILE C C   
2240 O  O   . ILE C 67  ? 0.2014 0.2140 0.2507 -0.0121 -0.0249 -0.0084 67  ILE C O   
2241 C  CB  . ILE C 67  ? 0.1948 0.1774 0.1975 0.0139  -0.0009 0.0108  67  ILE C CB  
2242 C  CG1 . ILE C 67  ? 0.1874 0.1897 0.2042 0.0238  -0.0170 0.0080  67  ILE C CG1 
2243 C  CG2 . ILE C 67  ? 0.1847 0.1783 0.1945 0.0261  0.0016  0.0232  67  ILE C CG2 
2244 C  CD1 . ILE C 67  ? 0.1876 0.2125 0.2243 0.0069  -0.0190 0.0033  67  ILE C CD1 
2245 N  N   . GLY C 68  ? 0.2011 0.1952 0.2066 0.0078  -0.0053 -0.0028 68  GLY C N   
2246 C  CA  . GLY C 68  ? 0.1997 0.1989 0.2074 0.0058  0.0083  -0.0010 68  GLY C CA  
2247 C  C   . GLY C 68  ? 0.2059 0.1866 0.1932 0.0086  -0.0005 0.0036  68  GLY C C   
2248 O  O   . GLY C 68  ? 0.2110 0.1927 0.1804 -0.0147 -0.0099 -0.0036 68  GLY C O   
2249 N  N   . GLY C 69  ? 0.2195 0.1796 0.2088 0.0262  0.0014  -0.0003 69  GLY C N   
2250 C  CA  . GLY C 69  ? 0.2284 0.1910 0.2093 0.0051  -0.0053 0.0018  69  GLY C CA  
2251 C  C   . GLY C 69  ? 0.2374 0.1897 0.1933 -0.0012 -0.0036 -0.0032 69  GLY C C   
2252 O  O   . GLY C 69  ? 0.2339 0.1851 0.1903 0.0009  0.0091  -0.0165 69  GLY C O   
2253 N  N   . ALA C 70  ? 0.2357 0.2025 0.1760 0.0009  -0.0077 -0.0035 70  ALA C N   
2254 C  CA  . ALA C 70  ? 0.2547 0.2265 0.1692 -0.0015 -0.0055 -0.0098 70  ALA C CA  
2255 C  C   . ALA C 70  ? 0.2236 0.2189 0.1689 0.0104  -0.0028 0.0024  70  ALA C C   
2256 O  O   . ALA C 70  ? 0.2072 0.2151 0.1656 0.0070  -0.0043 0.0037  70  ALA C O   
2257 C  CB  . ALA C 70  ? 0.2935 0.2428 0.1645 -0.0120 -0.0061 -0.0401 70  ALA C CB  
2258 N  N   . GLN C 71  ? 0.2241 0.1938 0.1679 0.0146  -0.0030 0.0059  71  GLN C N   
2259 C  CA  . GLN C 71  ? 0.2023 0.1921 0.1666 0.0106  -0.0079 0.0191  71  GLN C CA  
2260 C  C   . GLN C 71  ? 0.1992 0.1940 0.1566 0.0041  0.0060  0.0223  71  GLN C C   
2261 O  O   . GLN C 71  ? 0.2138 0.1854 0.1488 -0.0089 0.0105  0.0180  71  GLN C O   
2262 C  CB  . GLN C 71  ? 0.2163 0.2238 0.1790 0.0162  -0.0153 0.0226  71  GLN C CB  
2263 C  CG  . GLN C 71  ? 0.2366 0.2655 0.1872 0.0227  -0.0172 0.0115  71  GLN C CG  
2264 C  CD  . GLN C 71  ? 0.2427 0.2938 0.2124 0.0066  -0.0152 0.0169  71  GLN C CD  
2265 O  OE1 . GLN C 71  ? 0.2539 0.3098 0.2283 0.0096  -0.0145 0.0329  71  GLN C OE1 
2266 N  NE2 . GLN C 71  ? 0.2260 0.3068 0.2184 -0.0113 -0.0190 0.0056  71  GLN C NE2 
2267 N  N   . ASN C 72  ? 0.1950 0.1776 0.1450 0.0065  0.0154  0.0183  72  ASN C N   
2268 C  CA  . ASN C 72  ? 0.1839 0.1749 0.1601 -0.0007 0.0013  0.0126  72  ASN C CA  
2269 C  C   . ASN C 72  ? 0.1842 0.1643 0.1601 0.0056  0.0117  0.0033  72  ASN C C   
2270 O  O   . ASN C 72  ? 0.1847 0.1792 0.1550 -0.0011 0.0079  -0.0023 72  ASN C O   
2271 C  CB  . ASN C 72  ? 0.1796 0.1685 0.1664 -0.0029 0.0068  0.0150  72  ASN C CB  
2272 C  CG  . ASN C 72  ? 0.1833 0.1702 0.1601 -0.0130 -0.0050 0.0077  72  ASN C CG  
2273 O  OD1 . ASN C 72  ? 0.1751 0.1744 0.1634 -0.0010 -0.0029 0.0088  72  ASN C OD1 
2274 N  ND2 . ASN C 72  ? 0.1922 0.1714 0.1566 -0.0147 0.0077  0.0036  72  ASN C ND2 
2275 N  N   . ARG C 73  ? 0.1850 0.1593 0.1678 0.0102  0.0259  -0.0014 73  ARG C N   
2276 C  CA  . ARG C 73  ? 0.1975 0.1640 0.1793 0.0056  0.0259  -0.0045 73  ARG C CA  
2277 C  C   . ARG C 73  ? 0.2013 0.1751 0.1729 0.0085  0.0161  0.0066  73  ARG C C   
2278 O  O   . ARG C 73  ? 0.1903 0.1723 0.1780 0.0055  0.0126  0.0057  73  ARG C O   
2279 C  CB  . ARG C 73  ? 0.2294 0.1642 0.1934 0.0125  0.0321  -0.0140 73  ARG C CB  
2280 C  CG  . ARG C 73  ? 0.2612 0.1950 0.2055 0.0080  0.0207  -0.0222 73  ARG C CG  
2281 C  CD  . ARG C 73  ? 0.2947 0.2328 0.2251 0.0201  0.0156  -0.0462 73  ARG C CD  
2282 N  NE  . ARG C 73  ? 0.3227 0.2610 0.2479 0.0380  0.0146  -0.0615 73  ARG C NE  
2283 C  CZ  . ARG C 73  ? 0.3417 0.2749 0.2686 0.0395  -0.0048 -0.0556 73  ARG C CZ  
2284 N  NH1 . ARG C 73  ? 0.3255 0.2688 0.2758 0.0190  -0.0097 -0.0413 73  ARG C NH1 
2285 N  NH2 . ARG C 73  ? 0.3686 0.2696 0.2790 0.0615  -0.0076 -0.0649 73  ARG C NH2 
2286 N  N   . SER C 74  ? 0.2044 0.1928 0.1727 0.0206  0.0182  0.0304  74  SER C N   
2287 C  CA  . SER C 74  ? 0.2134 0.2025 0.1799 0.0249  0.0086  0.0465  74  SER C CA  
2288 C  C   . SER C 74  ? 0.1968 0.1858 0.1805 0.0144  0.0091  0.0349  74  SER C C   
2289 O  O   . SER C 74  ? 0.1921 0.2031 0.1763 -0.0011 0.0134  0.0302  74  SER C O   
2290 C  CB  . SER C 74  ? 0.2640 0.2373 0.2073 0.0053  0.0033  0.0691  74  SER C CB  
2291 O  OG  . SER C 74  ? 0.3024 0.2545 0.2353 -0.0083 0.0029  0.0619  74  SER C OG  
2292 N  N   . TYR C 75  ? 0.1761 0.1667 0.1721 0.0215  0.0047  0.0234  75  TYR C N   
2293 C  CA  . TYR C 75  ? 0.1636 0.1599 0.1817 0.0112  -0.0011 0.0173  75  TYR C CA  
2294 C  C   . TYR C 75  ? 0.1671 0.1494 0.1713 0.0048  0.0020  0.0162  75  TYR C C   
2295 O  O   . TYR C 75  ? 0.1714 0.1709 0.1671 -0.0024 -0.0103 0.0265  75  TYR C O   
2296 C  CB  . TYR C 75  ? 0.1443 0.1652 0.1967 0.0090  -0.0145 0.0229  75  TYR C CB  
2297 C  CG  . TYR C 75  ? 0.1584 0.1827 0.2126 0.0190  -0.0222 0.0281  75  TYR C CG  
2298 C  CD1 . TYR C 75  ? 0.1901 0.2192 0.2498 0.0039  -0.0311 0.0622  75  TYR C CD1 
2299 C  CD2 . TYR C 75  ? 0.1598 0.1896 0.2074 0.0003  -0.0199 0.0112  75  TYR C CD2 
2300 C  CE1 . TYR C 75  ? 0.1925 0.2350 0.2696 -0.0137 -0.0358 0.0713  75  TYR C CE1 
2301 C  CE2 . TYR C 75  ? 0.1842 0.2036 0.2220 0.0006  -0.0284 0.0326  75  TYR C CE2 
2302 C  CZ  . TYR C 75  ? 0.1921 0.2216 0.2633 -0.0057 -0.0415 0.0789  75  TYR C CZ  
2303 O  OH  . TYR C 75  ? 0.2106 0.2253 0.2882 -0.0006 -0.0519 0.1059  75  TYR C OH  
2304 N  N   . SER C 76  ? 0.1601 0.1536 0.1740 0.0089  0.0146  0.0337  76  SER C N   
2305 C  CA  . SER C 76  ? 0.1563 0.1502 0.1740 -0.0053 0.0149  0.0345  76  SER C CA  
2306 C  C   . SER C 76  ? 0.1712 0.1677 0.1667 -0.0008 0.0140  0.0296  76  SER C C   
2307 O  O   . SER C 76  ? 0.1747 0.1898 0.1690 0.0021  0.0039  0.0157  76  SER C O   
2308 C  CB  . SER C 76  ? 0.1542 0.1510 0.1844 -0.0017 0.0329  0.0235  76  SER C CB  
2309 O  OG  . SER C 76  ? 0.1784 0.1623 0.1916 0.0022  0.0398  0.0273  76  SER C OG  
2310 N  N   . LYS C 77  ? 0.1588 0.1749 0.1675 -0.0016 0.0203  0.0207  77  LYS C N   
2311 C  CA  . LYS C 77  ? 0.1722 0.1763 0.1873 -0.0040 0.0255  0.0140  77  LYS C CA  
2312 C  C   . LYS C 77  ? 0.1798 0.1694 0.1879 0.0005  0.0297  0.0204  77  LYS C C   
2313 O  O   . LYS C 77  ? 0.1830 0.1709 0.1992 -0.0069 0.0200  0.0084  77  LYS C O   
2314 C  CB  . LYS C 77  ? 0.1898 0.2110 0.2040 -0.0095 0.0318  0.0062  77  LYS C CB  
2315 C  CG  . LYS C 77  ? 0.2028 0.2538 0.2139 -0.0066 0.0327  -0.0035 77  LYS C CG  
2316 C  CD  . LYS C 77  ? 0.2301 0.2955 0.2266 -0.0156 0.0445  -0.0051 77  LYS C CD  
2317 N  N   . LEU C 78  ? 0.1929 0.1561 0.1854 0.0087  0.0237  0.0277  78  LEU C N   
2318 C  CA  . LEU C 78  ? 0.1867 0.1627 0.2014 0.0097  -0.0057 0.0364  78  LEU C CA  
2319 C  C   . LEU C 78  ? 0.1752 0.1721 0.1915 0.0052  -0.0089 0.0294  78  LEU C C   
2320 O  O   . LEU C 78  ? 0.1890 0.1750 0.1899 -0.0176 -0.0062 0.0363  78  LEU C O   
2321 C  CB  . LEU C 78  ? 0.1922 0.1560 0.2426 0.0142  -0.0132 0.0402  78  LEU C CB  
2322 C  CG  . LEU C 78  ? 0.2229 0.1752 0.2851 -0.0012 -0.0189 0.0524  78  LEU C CG  
2323 C  CD1 . LEU C 78  ? 0.2492 0.1876 0.3020 -0.0211 -0.0020 0.0576  78  LEU C CD1 
2324 C  CD2 . LEU C 78  ? 0.2241 0.1848 0.3021 0.0063  -0.0318 0.0509  78  LEU C CD2 
2325 N  N   . LEU C 79  ? 0.1672 0.1694 0.1823 0.0139  0.0141  0.0177  79  LEU C N   
2326 C  CA  . LEU C 79  ? 0.1483 0.1570 0.1933 0.0043  0.0080  0.0081  79  LEU C CA  
2327 C  C   . LEU C 79  ? 0.1748 0.1652 0.1973 -0.0027 0.0085  0.0168  79  LEU C C   
2328 O  O   . LEU C 79  ? 0.1790 0.1760 0.1910 -0.0082 0.0144  0.0084  79  LEU C O   
2329 C  CB  . LEU C 79  ? 0.1387 0.1811 0.2167 0.0009  0.0110  0.0074  79  LEU C CB  
2330 C  CG  . LEU C 79  ? 0.1551 0.1848 0.2516 0.0057  0.0175  -0.0107 79  LEU C CG  
2331 C  CD1 . LEU C 79  ? 0.1411 0.2007 0.2541 0.0061  0.0229  -0.0086 79  LEU C CD1 
2332 C  CD2 . LEU C 79  ? 0.1917 0.1833 0.2801 0.0103  0.0008  -0.0211 79  LEU C CD2 
2333 N  N   . CYS C 80  ? 0.1647 0.1622 0.2056 0.0094  0.0051  0.0218  80  CYS C N   
2334 C  CA  . CYS C 80  ? 0.1629 0.1559 0.2056 0.0025  0.0016  0.0285  80  CYS C CA  
2335 C  C   . CYS C 80  ? 0.1821 0.1657 0.2041 0.0031  0.0119  0.0202  80  CYS C C   
2336 O  O   . CYS C 80  ? 0.1917 0.1655 0.2034 0.0015  0.0041  0.0255  80  CYS C O   
2337 C  CB  . CYS C 80  ? 0.1893 0.1611 0.2081 -0.0049 0.0054  0.0228  80  CYS C CB  
2338 S  SG  . CYS C 80  ? 0.2118 0.1793 0.2105 0.0147  0.0089  0.0174  80  CYS C SG  
2339 N  N   . GLY C 81  ? 0.1817 0.1920 0.2003 0.0047  0.0146  0.0168  81  GLY C N   
2340 C  CA  . GLY C 81  ? 0.1787 0.1988 0.2082 -0.0112 0.0085  0.0172  81  GLY C CA  
2341 C  C   . GLY C 81  ? 0.1841 0.2007 0.2147 -0.0051 0.0081  0.0285  81  GLY C C   
2342 O  O   . GLY C 81  ? 0.1879 0.2111 0.2192 -0.0259 0.0047  0.0190  81  GLY C O   
2343 N  N   . LEU C 82  ? 0.1969 0.1906 0.2177 0.0029  0.0084  0.0321  82  LEU C N   
2344 C  CA  . LEU C 82  ? 0.1828 0.1924 0.2269 -0.0138 -0.0025 0.0418  82  LEU C CA  
2345 C  C   . LEU C 82  ? 0.1693 0.1890 0.2271 -0.0194 -0.0055 0.0246  82  LEU C C   
2346 O  O   . LEU C 82  ? 0.1684 0.2070 0.2416 -0.0193 0.0096  0.0229  82  LEU C O   
2347 C  CB  . LEU C 82  ? 0.1942 0.2157 0.2435 0.0033  -0.0072 0.0591  82  LEU C CB  
2348 C  CG  . LEU C 82  ? 0.2089 0.2238 0.2752 0.0045  0.0076  0.0824  82  LEU C CG  
2349 C  CD1 . LEU C 82  ? 0.1972 0.2448 0.2862 0.0356  -0.0027 0.0777  82  LEU C CD1 
2350 C  CD2 . LEU C 82  ? 0.2726 0.2346 0.2999 -0.0173 0.0202  0.0984  82  LEU C CD2 
2351 N  N   . LEU C 83  ? 0.1466 0.1939 0.2160 -0.0172 0.0024  0.0267  83  LEU C N   
2352 C  CA  . LEU C 83  ? 0.1475 0.1915 0.2225 0.0025  -0.0015 0.0313  83  LEU C CA  
2353 C  C   . LEU C 83  ? 0.1536 0.1956 0.2168 0.0078  -0.0004 0.0275  83  LEU C C   
2354 O  O   . LEU C 83  ? 0.1497 0.2113 0.2140 -0.0149 -0.0061 0.0136  83  LEU C O   
2355 C  CB  . LEU C 83  ? 0.1640 0.1958 0.2414 -0.0002 0.0185  0.0321  83  LEU C CB  
2356 C  CG  . LEU C 83  ? 0.1794 0.1827 0.2639 -0.0040 0.0265  0.0223  83  LEU C CG  
2357 C  CD1 . LEU C 83  ? 0.1941 0.1993 0.2906 -0.0162 0.0348  0.0384  83  LEU C CD1 
2358 C  CD2 . LEU C 83  ? 0.1903 0.1985 0.2753 0.0077  0.0282  -0.0067 83  LEU C CD2 
2359 N  N   . ALA C 84  ? 0.1584 0.1921 0.2202 0.0061  0.0253  0.0212  84  ALA C N   
2360 C  CA  . ALA C 84  ? 0.1656 0.1962 0.2375 -0.0129 0.0257  0.0120  84  ALA C CA  
2361 C  C   . ALA C 84  ? 0.1673 0.2154 0.2448 -0.0251 0.0253  0.0248  84  ALA C C   
2362 O  O   . ALA C 84  ? 0.1805 0.2515 0.2517 -0.0210 0.0208  0.0264  84  ALA C O   
2363 C  CB  . ALA C 84  ? 0.1838 0.1993 0.2457 -0.0089 0.0281  0.0048  84  ALA C CB  
2364 N  N   . GLU C 85  ? 0.1994 0.2108 0.2579 -0.0381 0.0203  0.0343  85  GLU C N   
2365 C  CA  . GLU C 85  ? 0.2383 0.2350 0.2925 -0.0509 0.0184  0.0570  85  GLU C CA  
2366 C  C   . GLU C 85  ? 0.2035 0.2232 0.2928 -0.0454 0.0086  0.0454  85  GLU C C   
2367 O  O   . GLU C 85  ? 0.2172 0.2449 0.3127 -0.0568 0.0155  0.0253  85  GLU C O   
2368 C  CB  . GLU C 85  ? 0.3439 0.2809 0.3325 -0.0656 0.0336  0.0910  85  GLU C CB  
2369 C  CG  . GLU C 85  ? 0.4508 0.3680 0.3840 -0.0706 0.0453  0.1042  85  GLU C CG  
2370 C  CD  . GLU C 85  ? 0.5342 0.4497 0.4334 -0.0792 0.0579  0.1105  85  GLU C CD  
2371 O  OE1 . GLU C 85  ? 0.5668 0.4742 0.4468 -0.0766 0.0645  0.1162  85  GLU C OE1 
2372 O  OE2 . GLU C 85  ? 0.5640 0.4795 0.4555 -0.0852 0.0642  0.1067  85  GLU C OE2 
2373 N  N   . ARG C 86  ? 0.1890 0.1989 0.2786 -0.0237 0.0022  0.0540  86  ARG C N   
2374 C  CA  . ARG C 86  ? 0.1999 0.1928 0.2842 -0.0142 -0.0049 0.0584  86  ARG C CA  
2375 C  C   . ARG C 86  ? 0.2109 0.1905 0.2715 -0.0183 -0.0005 0.0376  86  ARG C C   
2376 O  O   . ARG C 86  ? 0.2457 0.1962 0.2779 -0.0319 0.0005  0.0214  86  ARG C O   
2377 C  CB  . ARG C 86  ? 0.2042 0.2271 0.3080 -0.0183 -0.0087 0.0779  86  ARG C CB  
2378 C  CG  . ARG C 86  ? 0.2292 0.2744 0.3387 -0.0315 -0.0103 0.0964  86  ARG C CG  
2379 C  CD  . ARG C 86  ? 0.2770 0.3403 0.3752 -0.0420 0.0036  0.1157  86  ARG C CD  
2380 N  NE  . ARG C 86  ? 0.3274 0.3862 0.4079 -0.0503 0.0184  0.1320  86  ARG C NE  
2381 C  CZ  . ARG C 86  ? 0.3536 0.4340 0.4315 -0.0468 0.0277  0.1358  86  ARG C CZ  
2382 N  NH1 . ARG C 86  ? 0.3645 0.4602 0.4492 -0.0473 0.0289  0.1267  86  ARG C NH1 
2383 N  NH2 . ARG C 86  ? 0.3686 0.4424 0.4286 -0.0371 0.0282  0.1512  86  ARG C NH2 
2384 N  N   . LEU C 87  ? 0.1907 0.1905 0.2549 -0.0120 0.0139  0.0301  87  LEU C N   
2385 C  CA  . LEU C 87  ? 0.1842 0.1895 0.2569 0.0015  0.0046  0.0176  87  LEU C CA  
2386 C  C   . LEU C 87  ? 0.1841 0.1945 0.2515 0.0092  0.0093  0.0172  87  LEU C C   
2387 O  O   . LEU C 87  ? 0.1931 0.1999 0.2534 -0.0025 0.0012  0.0169  87  LEU C O   
2388 C  CB  . LEU C 87  ? 0.1706 0.1879 0.2784 0.0026  0.0207  0.0177  87  LEU C CB  
2389 C  CG  . LEU C 87  ? 0.2065 0.1892 0.3115 0.0049  0.0518  0.0213  87  LEU C CG  
2390 C  CD1 . LEU C 87  ? 0.1978 0.1993 0.3128 0.0093  0.0718  0.0155  87  LEU C CD1 
2391 C  CD2 . LEU C 87  ? 0.2192 0.1932 0.3397 -0.0049 0.0534  0.0246  87  LEU C CD2 
2392 N  N   . ARG C 88  ? 0.1530 0.1917 0.2480 -0.0012 0.0092  0.0128  88  ARG C N   
2393 C  CA  . ARG C 88  ? 0.1654 0.2229 0.2651 -0.0106 0.0092  0.0231  88  ARG C CA  
2394 C  C   . ARG C 88  ? 0.1621 0.2057 0.2562 -0.0032 0.0045  0.0305  88  ARG C C   
2395 O  O   . ARG C 88  ? 0.1798 0.2297 0.2764 -0.0041 -0.0188 0.0361  88  ARG C O   
2396 C  CB  . ARG C 88  ? 0.1850 0.2654 0.3026 -0.0482 0.0080  0.0286  88  ARG C CB  
2397 C  CG  . ARG C 88  ? 0.2317 0.3338 0.3497 -0.0574 0.0068  0.0093  88  ARG C CG  
2398 C  CD  . ARG C 88  ? 0.2922 0.4113 0.3957 -0.0260 0.0161  -0.0184 88  ARG C CD  
2399 N  NE  . ARG C 88  ? 0.3527 0.4807 0.4305 0.0020  0.0280  -0.0334 88  ARG C NE  
2400 C  CZ  . ARG C 88  ? 0.3863 0.5291 0.4512 0.0370  0.0301  -0.0422 88  ARG C CZ  
2401 N  NH1 . ARG C 88  ? 0.3887 0.5487 0.4602 0.0515  0.0399  -0.0470 88  ARG C NH1 
2402 N  NH2 . ARG C 88  ? 0.3884 0.5397 0.4535 0.0461  0.0177  -0.0404 88  ARG C NH2 
2403 N  N   . ILE C 89  ? 0.1460 0.1691 0.2294 -0.0113 0.0130  0.0193  89  ILE C N   
2404 C  CA  . ILE C 89  ? 0.1490 0.1647 0.2262 -0.0021 0.0134  0.0034  89  ILE C CA  
2405 C  C   . ILE C 89  ? 0.1626 0.1750 0.2145 0.0157  0.0016  -0.0099 89  ILE C C   
2406 O  O   . ILE C 89  ? 0.1737 0.1956 0.2035 0.0078  -0.0123 -0.0000 89  ILE C O   
2407 C  CB  . ILE C 89  ? 0.1427 0.1653 0.2224 0.0025  0.0068  0.0131  89  ILE C CB  
2408 C  CG1 . ILE C 89  ? 0.1566 0.1882 0.2168 0.0145  0.0007  -0.0028 89  ILE C CG1 
2409 C  CG2 . ILE C 89  ? 0.1563 0.1784 0.2232 -0.0132 0.0025  0.0304  89  ILE C CG2 
2410 C  CD1 . ILE C 89  ? 0.1564 0.2032 0.2161 0.0159  0.0072  -0.0135 89  ILE C CD1 
2411 N  N   . SER C 90  ? 0.1558 0.1742 0.2214 0.0186  0.0157  -0.0145 90  SER C N   
2412 C  CA  . SER C 90  ? 0.1630 0.1854 0.2287 0.0184  0.0096  0.0026  90  SER C CA  
2413 C  C   . SER C 90  ? 0.1527 0.1698 0.2093 0.0204  0.0280  0.0090  90  SER C C   
2414 O  O   . SER C 90  ? 0.1584 0.1616 0.2090 0.0198  0.0218  -0.0071 90  SER C O   
2415 C  CB  . SER C 90  ? 0.1906 0.2225 0.2652 0.0357  -0.0227 0.0103  90  SER C CB  
2416 O  OG  . SER C 90  ? 0.2290 0.2689 0.3030 0.0193  -0.0337 0.0038  90  SER C OG  
2417 N  N   . PRO C 91  ? 0.1613 0.1914 0.2030 0.0113  0.0172  0.0125  91  PRO C N   
2418 C  CA  . PRO C 91  ? 0.1651 0.1764 0.1936 0.0136  0.0087  0.0253  91  PRO C CA  
2419 C  C   . PRO C 91  ? 0.1643 0.1554 0.1845 0.0209  0.0057  0.0164  91  PRO C C   
2420 O  O   . PRO C 91  ? 0.1635 0.1610 0.1886 0.0072  -0.0012 0.0032  91  PRO C O   
2421 C  CB  . PRO C 91  ? 0.1659 0.2057 0.1921 0.0245  0.0151  0.0060  91  PRO C CB  
2422 C  CG  . PRO C 91  ? 0.1912 0.2575 0.2010 0.0042  0.0198  -0.0133 91  PRO C CG  
2423 C  CD  . PRO C 91  ? 0.1773 0.2526 0.2018 -0.0071 0.0228  -0.0036 91  PRO C CD  
2424 N  N   . ASP C 92  ? 0.1691 0.1501 0.1884 0.0246  0.0204  0.0063  92  ASP C N   
2425 C  CA  . ASP C 92  ? 0.1895 0.1679 0.2067 0.0314  0.0255  0.0111  92  ASP C CA  
2426 C  C   . ASP C 92  ? 0.1682 0.1753 0.1935 0.0130  0.0129  0.0049  92  ASP C C   
2427 O  O   . ASP C 92  ? 0.1842 0.1759 0.1964 0.0204  0.0055  0.0228  92  ASP C O   
2428 C  CB  . ASP C 92  ? 0.1917 0.1945 0.2532 0.0508  0.0431  0.0185  92  ASP C CB  
2429 C  CG  . ASP C 92  ? 0.2013 0.2120 0.2943 0.0745  0.0470  0.0171  92  ASP C CG  
2430 O  OD1 . ASP C 92  ? 0.1920 0.2198 0.2990 0.0718  0.0402  0.0211  92  ASP C OD1 
2431 O  OD2 . ASP C 92  ? 0.2382 0.2351 0.3282 0.0837  0.0489  0.0102  92  ASP C OD2 
2432 N  N   . ARG C 93  ? 0.1494 0.1809 0.1781 0.0148  -0.0043 -0.0028 93  ARG C N   
2433 C  CA  . ARG C 93  ? 0.1425 0.1759 0.1776 0.0161  -0.0141 -0.0041 93  ARG C CA  
2434 C  C   . ARG C 93  ? 0.1461 0.1557 0.1693 0.0046  -0.0087 0.0000  93  ARG C C   
2435 O  O   . ARG C 93  ? 0.1461 0.1656 0.1778 0.0155  -0.0025 -0.0024 93  ARG C O   
2436 C  CB  . ARG C 93  ? 0.1382 0.2019 0.1950 0.0325  -0.0208 -0.0007 93  ARG C CB  
2437 C  CG  . ARG C 93  ? 0.1501 0.2203 0.1983 0.0581  -0.0196 0.0077  93  ARG C CG  
2438 C  CD  . ARG C 93  ? 0.1555 0.2331 0.1938 0.0400  -0.0173 -0.0013 93  ARG C CD  
2439 N  NE  . ARG C 93  ? 0.1470 0.2335 0.1846 0.0381  -0.0191 0.0042  93  ARG C NE  
2440 C  CZ  . ARG C 93  ? 0.1573 0.2217 0.1955 0.0457  -0.0232 0.0105  93  ARG C CZ  
2441 N  NH1 . ARG C 93  ? 0.1455 0.2222 0.2141 0.0424  -0.0279 0.0233  93  ARG C NH1 
2442 N  NH2 . ARG C 93  ? 0.1566 0.2405 0.1968 0.0451  -0.0088 0.0045  93  ARG C NH2 
2443 N  N   . VAL C 94  ? 0.1488 0.1581 0.1703 0.0167  -0.0120 0.0257  94  VAL C N   
2444 C  CA  . VAL C 94  ? 0.1397 0.1618 0.1752 0.0239  -0.0137 0.0176  94  VAL C CA  
2445 C  C   . VAL C 94  ? 0.1314 0.1446 0.1696 0.0253  -0.0037 0.0170  94  VAL C C   
2446 O  O   . VAL C 94  ? 0.1590 0.1569 0.1731 0.0285  0.0027  0.0049  94  VAL C O   
2447 C  CB  . VAL C 94  ? 0.1324 0.1659 0.1953 0.0106  -0.0176 0.0153  94  VAL C CB  
2448 C  CG1 . VAL C 94  ? 0.1388 0.1702 0.2130 0.0355  -0.0064 0.0302  94  VAL C CG1 
2449 C  CG2 . VAL C 94  ? 0.1395 0.1590 0.2015 -0.0106 -0.0151 0.0104  94  VAL C CG2 
2450 N  N   . TYR C 95  ? 0.1291 0.1371 0.1775 0.0044  0.0068  0.0267  95  TYR C N   
2451 C  CA  . TYR C 95  ? 0.1305 0.1437 0.1757 0.0073  0.0058  0.0208  95  TYR C CA  
2452 C  C   . TYR C 95  ? 0.1455 0.1380 0.1596 0.0261  0.0066  0.0127  95  TYR C C   
2453 O  O   . TYR C 95  ? 0.1630 0.1368 0.1693 0.0331  0.0053  -0.0008 95  TYR C O   
2454 C  CB  . TYR C 95  ? 0.1602 0.1265 0.1748 0.0048  0.0145  0.0138  95  TYR C CB  
2455 C  CG  . TYR C 95  ? 0.1720 0.1298 0.1651 0.0136  0.0031  0.0087  95  TYR C CG  
2456 C  CD1 . TYR C 95  ? 0.1921 0.1277 0.1695 0.0156  0.0017  -0.0069 95  TYR C CD1 
2457 C  CD2 . TYR C 95  ? 0.1681 0.1464 0.1657 0.0097  -0.0129 0.0165  95  TYR C CD2 
2458 C  CE1 . TYR C 95  ? 0.1929 0.1396 0.1732 0.0107  -0.0030 0.0029  95  TYR C CE1 
2459 C  CE2 . TYR C 95  ? 0.1719 0.1447 0.1756 0.0246  0.0002  0.0027  95  TYR C CE2 
2460 C  CZ  . TYR C 95  ? 0.1840 0.1295 0.1690 0.0162  0.0013  -0.0073 95  TYR C CZ  
2461 O  OH  . TYR C 95  ? 0.2051 0.1420 0.1787 0.0281  0.0079  0.0029  95  TYR C OH  
2462 N  N   . ILE C 96  ? 0.1429 0.1436 0.1487 0.0158  -0.0032 0.0092  96  ILE C N   
2463 C  CA  . ILE C 96  ? 0.1480 0.1598 0.1555 0.0221  0.0029  0.0222  96  ILE C CA  
2464 C  C   . ILE C 96  ? 0.1486 0.1488 0.1653 0.0219  0.0016  0.0106  96  ILE C C   
2465 O  O   . ILE C 96  ? 0.1597 0.1609 0.1703 0.0224  0.0082  -0.0074 96  ILE C O   
2466 C  CB  . ILE C 96  ? 0.1611 0.1839 0.1662 0.0216  0.0044  0.0245  96  ILE C CB  
2467 C  CG1 . ILE C 96  ? 0.1701 0.2229 0.1810 0.0047  0.0212  0.0291  96  ILE C CG1 
2468 C  CG2 . ILE C 96  ? 0.1673 0.1773 0.1634 0.0319  0.0003  0.0207  96  ILE C CG2 
2469 C  CD1 . ILE C 96  ? 0.1864 0.2582 0.1867 -0.0002 0.0234  0.0195  96  ILE C CD1 
2470 N  N   . ASN C 97  ? 0.1438 0.1387 0.1619 0.0141  -0.0035 0.0183  97  ASN C N   
2471 C  CA  . ASN C 97  ? 0.1503 0.1401 0.1674 -0.0016 -0.0062 0.0206  97  ASN C CA  
2472 C  C   . ASN C 97  ? 0.1525 0.1309 0.1689 0.0122  -0.0076 0.0099  97  ASN C C   
2473 O  O   . ASN C 97  ? 0.1643 0.1254 0.1736 0.0140  -0.0041 0.0136  97  ASN C O   
2474 C  CB  . ASN C 97  ? 0.1692 0.1629 0.1641 0.0169  0.0040  0.0321  97  ASN C CB  
2475 C  CG  . ASN C 97  ? 0.2040 0.1912 0.1729 0.0128  -0.0020 0.0287  97  ASN C CG  
2476 O  OD1 . ASN C 97  ? 0.2304 0.2045 0.1861 0.0075  -0.0036 0.0282  97  ASN C OD1 
2477 N  ND2 . ASN C 97  ? 0.2175 0.2273 0.1755 0.0051  0.0006  0.0328  97  ASN C ND2 
2478 N  N   . TYR C 98  ? 0.1478 0.1521 0.1591 0.0095  -0.0074 0.0109  98  TYR C N   
2479 C  CA  . TYR C 98  ? 0.1322 0.1596 0.1533 0.0029  -0.0103 0.0116  98  TYR C CA  
2480 C  C   . TYR C 98  ? 0.1404 0.1456 0.1663 -0.0055 -0.0102 0.0219  98  TYR C C   
2481 O  O   . TYR C 98  ? 0.1521 0.1513 0.1723 -0.0119 0.0029  0.0100  98  TYR C O   
2482 C  CB  . TYR C 98  ? 0.1342 0.1735 0.1459 0.0054  0.0020  0.0022  98  TYR C CB  
2483 C  CG  . TYR C 98  ? 0.1399 0.1608 0.1482 0.0070  -0.0104 0.0033  98  TYR C CG  
2484 C  CD1 . TYR C 98  ? 0.1581 0.1683 0.1518 0.0067  -0.0039 0.0105  98  TYR C CD1 
2485 C  CD2 . TYR C 98  ? 0.1502 0.1662 0.1591 0.0123  -0.0054 0.0048  98  TYR C CD2 
2486 C  CE1 . TYR C 98  ? 0.1555 0.1852 0.1531 0.0157  -0.0004 0.0101  98  TYR C CE1 
2487 C  CE2 . TYR C 98  ? 0.1452 0.1686 0.1611 -0.0019 0.0023  0.0073  98  TYR C CE2 
2488 C  CZ  . TYR C 98  ? 0.1397 0.1776 0.1601 0.0032  0.0136  0.0104  98  TYR C CZ  
2489 O  OH  . TYR C 98  ? 0.1398 0.1874 0.1633 -0.0074 0.0139  0.0200  98  TYR C OH  
2490 N  N   . TYR C 99  ? 0.1460 0.1536 0.1706 0.0093  -0.0067 0.0273  99  TYR C N   
2491 C  CA  . TYR C 99  ? 0.1462 0.1748 0.1711 0.0216  -0.0043 0.0177  99  TYR C CA  
2492 C  C   . TYR C 99  ? 0.1450 0.1698 0.1717 0.0103  -0.0106 0.0227  99  TYR C C   
2493 O  O   . TYR C 99  ? 0.1677 0.1664 0.1807 0.0064  -0.0167 0.0215  99  TYR C O   
2494 C  CB  . TYR C 99  ? 0.1529 0.1803 0.1709 0.0122  0.0069  0.0205  99  TYR C CB  
2495 C  CG  . TYR C 99  ? 0.1803 0.1857 0.1863 -0.0074 0.0002  0.0379  99  TYR C CG  
2496 C  CD1 . TYR C 99  ? 0.1883 0.1515 0.1966 0.0053  -0.0098 0.0294  99  TYR C CD1 
2497 C  CD2 . TYR C 99  ? 0.2121 0.2117 0.2039 -0.0245 -0.0094 0.0523  99  TYR C CD2 
2498 C  CE1 . TYR C 99  ? 0.2009 0.1700 0.2039 0.0069  -0.0100 0.0437  99  TYR C CE1 
2499 C  CE2 . TYR C 99  ? 0.2233 0.2203 0.2089 -0.0279 -0.0180 0.0621  99  TYR C CE2 
2500 C  CZ  . TYR C 99  ? 0.2178 0.2098 0.2085 -0.0068 -0.0187 0.0684  99  TYR C CZ  
2501 O  OH  . TYR C 99  ? 0.2436 0.2426 0.2128 -0.0150 -0.0350 0.0822  99  TYR C OH  
2502 N  N   . ASP C 100 ? 0.1373 0.1773 0.1747 0.0024  -0.0163 0.0100  100 ASP C N   
2503 C  CA  . ASP C 100 ? 0.1717 0.1882 0.1952 -0.0018 -0.0195 0.0056  100 ASP C CA  
2504 C  C   . ASP C 100 ? 0.1696 0.1699 0.2110 -0.0158 -0.0220 0.0072  100 ASP C C   
2505 O  O   . ASP C 100 ? 0.1796 0.1652 0.2438 -0.0125 -0.0176 0.0107  100 ASP C O   
2506 C  CB  . ASP C 100 ? 0.2103 0.1930 0.1936 0.0014  -0.0294 0.0033  100 ASP C CB  
2507 C  CG  . ASP C 100 ? 0.2615 0.2080 0.2070 -0.0232 -0.0490 0.0012  100 ASP C CG  
2508 O  OD1 . ASP C 100 ? 0.2406 0.1983 0.2058 -0.0098 -0.0455 0.0183  100 ASP C OD1 
2509 O  OD2 . ASP C 100 ? 0.3281 0.2440 0.2158 -0.0260 -0.0583 -0.0134 100 ASP C OD2 
2510 N  N   . MET C 101 ? 0.1613 0.1687 0.1916 -0.0055 -0.0263 0.0174  101 MET C N   
2511 C  CA  . MET C 101 ? 0.1739 0.1701 0.2025 0.0091  -0.0203 0.0240  101 MET C CA  
2512 C  C   . MET C 101 ? 0.1654 0.1751 0.2067 -0.0062 -0.0176 0.0278  101 MET C C   
2513 O  O   . MET C 101 ? 0.1696 0.2157 0.2082 -0.0136 -0.0074 0.0461  101 MET C O   
2514 C  CB  . MET C 101 ? 0.1693 0.1764 0.2061 0.0046  -0.0259 0.0242  101 MET C CB  
2515 C  CG  . MET C 101 ? 0.1836 0.2058 0.2085 0.0032  -0.0258 0.0232  101 MET C CG  
2516 S  SD  . MET C 101 ? 0.2171 0.2332 0.2243 0.0107  -0.0280 0.0150  101 MET C SD  
2517 C  CE  . MET C 101 ? 0.2114 0.2346 0.2315 -0.0011 0.0018  0.0330  101 MET C CE  
2518 N  N   . ASN C 102 ? 0.1679 0.1870 0.2168 -0.0012 -0.0269 0.0377  102 ASN C N   
2519 C  CA  . ASN C 102 ? 0.1529 0.2127 0.2306 -0.0057 -0.0357 0.0260  102 ASN C CA  
2520 C  C   . ASN C 102 ? 0.1605 0.2233 0.2126 0.0103  -0.0220 0.0303  102 ASN C C   
2521 O  O   . ASN C 102 ? 0.1557 0.2260 0.1992 0.0190  -0.0218 0.0334  102 ASN C O   
2522 C  CB  . ASN C 102 ? 0.1733 0.2467 0.2747 -0.0193 -0.0365 0.0096  102 ASN C CB  
2523 C  CG  . ASN C 102 ? 0.2322 0.3031 0.3251 -0.0374 -0.0235 -0.0008 102 ASN C CG  
2524 O  OD1 . ASN C 102 ? 0.2604 0.3295 0.3565 -0.0483 -0.0115 -0.0225 102 ASN C OD1 
2525 N  ND2 . ASN C 102 ? 0.2791 0.3159 0.3393 -0.0436 -0.0220 0.0060  102 ASN C ND2 
2526 N  N   . ALA C 103 ? 0.1914 0.2196 0.2120 0.0210  -0.0458 0.0362  103 ALA C N   
2527 C  CA  . ALA C 103 ? 0.2037 0.2202 0.2295 0.0291  -0.0484 0.0397  103 ALA C CA  
2528 C  C   . ALA C 103 ? 0.1913 0.2223 0.2348 0.0116  -0.0363 0.0399  103 ALA C C   
2529 O  O   . ALA C 103 ? 0.1868 0.2237 0.2429 0.0187  -0.0258 0.0439  103 ALA C O   
2530 C  CB  . ALA C 103 ? 0.2064 0.2368 0.2344 0.0368  -0.0678 0.0424  103 ALA C CB  
2531 N  N   . ALA C 104 ? 0.1675 0.2337 0.2295 0.0093  -0.0339 0.0483  104 ALA C N   
2532 C  CA  . ALA C 104 ? 0.1501 0.2438 0.2332 0.0045  -0.0234 0.0444  104 ALA C CA  
2533 C  C   . ALA C 104 ? 0.1564 0.2240 0.2290 0.0087  -0.0056 0.0431  104 ALA C C   
2534 O  O   . ALA C 104 ? 0.1579 0.2210 0.2386 0.0077  0.0032  0.0448  104 ALA C O   
2535 C  CB  . ALA C 104 ? 0.1629 0.2722 0.2482 -0.0085 -0.0207 0.0455  104 ALA C CB  
2536 N  N   . ASN C 105 ? 0.1517 0.2086 0.2175 0.0058  -0.0200 0.0491  105 ASN C N   
2537 C  CA  . ASN C 105 ? 0.1615 0.1824 0.2160 0.0063  -0.0123 0.0372  105 ASN C CA  
2538 C  C   . ASN C 105 ? 0.1633 0.1706 0.2182 0.0031  -0.0134 0.0294  105 ASN C C   
2539 O  O   . ASN C 105 ? 0.1569 0.1828 0.2107 0.0122  -0.0140 0.0346  105 ASN C O   
2540 C  CB  . ASN C 105 ? 0.1746 0.1832 0.2227 0.0046  -0.0060 0.0389  105 ASN C CB  
2541 C  CG  . ASN C 105 ? 0.1774 0.1967 0.2451 0.0004  0.0012  0.0236  105 ASN C CG  
2542 O  OD1 . ASN C 105 ? 0.1848 0.2193 0.2654 -0.0064 0.0124  0.0063  105 ASN C OD1 
2543 N  ND2 . ASN C 105 ? 0.1715 0.1838 0.2510 -0.0078 -0.0083 0.0308  105 ASN C ND2 
2544 N  N   . VAL C 106 ? 0.1751 0.1565 0.2249 0.0142  -0.0174 0.0285  106 VAL C N   
2545 C  CA  . VAL C 106 ? 0.1779 0.1683 0.2248 0.0021  -0.0155 0.0293  106 VAL C CA  
2546 C  C   . VAL C 106 ? 0.1721 0.1697 0.2337 0.0077  -0.0187 0.0292  106 VAL C C   
2547 O  O   . VAL C 106 ? 0.1863 0.1964 0.2413 0.0294  -0.0226 0.0162  106 VAL C O   
2548 C  CB  . VAL C 106 ? 0.1770 0.1867 0.2207 0.0050  0.0019  0.0254  106 VAL C CB  
2549 C  CG1 . VAL C 106 ? 0.1980 0.2108 0.2318 0.0005  0.0037  0.0291  106 VAL C CG1 
2550 C  CG2 . VAL C 106 ? 0.1891 0.1948 0.2191 0.0172  0.0124  0.0240  106 VAL C CG2 
2551 N  N   . GLY C 107 ? 0.1694 0.1531 0.2433 0.0013  -0.0074 0.0279  107 GLY C N   
2552 C  CA  . GLY C 107 ? 0.1922 0.1525 0.2591 -0.0010 -0.0040 0.0230  107 GLY C CA  
2553 C  C   . GLY C 107 ? 0.1894 0.1576 0.2591 0.0030  -0.0199 0.0373  107 GLY C C   
2554 O  O   . GLY C 107 ? 0.1776 0.1813 0.2412 0.0010  -0.0314 0.0356  107 GLY C O   
2555 N  N   . TRP C 108 ? 0.1726 0.1695 0.2825 0.0042  -0.0158 0.0501  108 TRP C N   
2556 C  CA  . TRP C 108 ? 0.1705 0.1932 0.3009 0.0056  -0.0138 0.0616  108 TRP C CA  
2557 C  C   . TRP C 108 ? 0.1587 0.1941 0.3301 0.0132  -0.0150 0.0600  108 TRP C C   
2558 O  O   . TRP C 108 ? 0.1646 0.1983 0.3419 0.0134  -0.0348 0.0627  108 TRP C O   
2559 C  CB  . TRP C 108 ? 0.1921 0.2077 0.2942 0.0040  -0.0169 0.0736  108 TRP C CB  
2560 C  CG  . TRP C 108 ? 0.2058 0.2309 0.2985 0.0056  -0.0058 0.0901  108 TRP C CG  
2561 C  CD1 . TRP C 108 ? 0.2175 0.2369 0.2946 0.0107  0.0175  0.0912  108 TRP C CD1 
2562 C  CD2 . TRP C 108 ? 0.2439 0.2680 0.3151 -0.0008 -0.0206 0.1048  108 TRP C CD2 
2563 N  NE1 . TRP C 108 ? 0.2351 0.2501 0.2995 0.0168  0.0179  0.1000  108 TRP C NE1 
2564 C  CE2 . TRP C 108 ? 0.2514 0.2583 0.3187 0.0065  -0.0066 0.1145  108 TRP C CE2 
2565 C  CE3 . TRP C 108 ? 0.2831 0.3033 0.3321 -0.0135 -0.0415 0.1224  108 TRP C CE3 
2566 C  CZ2 . TRP C 108 ? 0.2855 0.2795 0.3377 0.0057  -0.0226 0.1325  108 TRP C CZ2 
2567 C  CZ3 . TRP C 108 ? 0.3052 0.3125 0.3448 -0.0084 -0.0454 0.1332  108 TRP C CZ3 
2568 C  CH2 . TRP C 108 ? 0.3092 0.3020 0.3449 -0.0053 -0.0375 0.1408  108 TRP C CH2 
2569 N  N   . ASN C 109 ? 0.1729 0.1881 0.3478 0.0181  -0.0170 0.0411  109 ASN C N   
2570 C  CA  . ASN C 109 ? 0.1772 0.1918 0.3740 0.0302  -0.0195 0.0474  109 ASN C CA  
2571 C  C   . ASN C 109 ? 0.1814 0.2034 0.3836 0.0298  -0.0230 0.0377  109 ASN C C   
2572 O  O   . ASN C 109 ? 0.2125 0.2146 0.3890 0.0377  -0.0320 0.0401  109 ASN C O   
2573 C  CB  . ASN C 109 ? 0.2291 0.1971 0.3942 0.0453  -0.0131 0.0746  109 ASN C CB  
2574 C  CG  . ASN C 109 ? 0.2790 0.2319 0.4130 0.0563  -0.0116 0.0821  109 ASN C CG  
2575 O  OD1 . ASN C 109 ? 0.2942 0.2269 0.4297 0.0453  -0.0052 0.0670  109 ASN C OD1 
2576 N  ND2 . ASN C 109 ? 0.3067 0.2631 0.4173 0.0698  -0.0104 0.0941  109 ASN C ND2 
2577 N  N   . ASN C 110 ? 0.1596 0.2003 0.3881 0.0208  -0.0070 0.0315  110 ASN C N   
2578 C  CA  . ASN C 110 ? 0.1774 0.2239 0.4056 0.0466  -0.0131 0.0266  110 ASN C CA  
2579 C  C   . ASN C 110 ? 0.1635 0.2390 0.4020 0.0471  -0.0111 0.0217  110 ASN C C   
2580 O  O   . ASN C 110 ? 0.1661 0.2744 0.4295 0.0287  0.0176  0.0023  110 ASN C O   
2581 C  CB  . ASN C 110 ? 0.2185 0.2332 0.4249 0.0673  -0.0166 0.0316  110 ASN C CB  
2582 C  CG  . ASN C 110 ? 0.2723 0.2308 0.4473 0.0764  -0.0170 0.0283  110 ASN C CG  
2583 O  OD1 . ASN C 110 ? 0.3246 0.2494 0.4627 0.0931  -0.0247 0.0061  110 ASN C OD1 
2584 N  ND2 . ASN C 110 ? 0.2731 0.2437 0.4601 0.0622  -0.0054 0.0318  110 ASN C ND2 
2585 N  N   . SER C 111 ? 0.1788 0.2214 0.3698 0.0450  -0.0270 0.0392  111 SER C N   
2586 C  CA  . SER C 111 ? 0.2075 0.2416 0.3462 0.0573  -0.0470 0.0268  111 SER C CA  
2587 C  C   . SER C 111 ? 0.1724 0.2370 0.3105 0.0311  -0.0246 0.0229  111 SER C C   
2588 O  O   . SER C 111 ? 0.1566 0.2396 0.2993 0.0119  -0.0297 0.0069  111 SER C O   
2589 C  CB  . SER C 111 ? 0.2531 0.2717 0.3604 0.0655  -0.0741 0.0174  111 SER C CB  
2590 O  OG  . SER C 111 ? 0.2842 0.2826 0.3736 0.0618  -0.0901 0.0021  111 SER C OG  
2591 N  N   . THR C 112 ? 0.1733 0.2369 0.2855 0.0173  -0.0064 0.0404  112 THR C N   
2592 C  CA  . THR C 112 ? 0.1916 0.2360 0.2718 0.0188  -0.0001 0.0582  112 THR C CA  
2593 C  C   . THR C 112 ? 0.2163 0.2491 0.2704 0.0345  0.0100  0.0698  112 THR C C   
2594 O  O   . THR C 112 ? 0.2521 0.2727 0.2800 0.0464  0.0056  0.0772  112 THR C O   
2595 C  CB  . THR C 112 ? 0.1852 0.2444 0.2716 0.0022  -0.0132 0.0594  112 THR C CB  
2596 O  OG1 . THR C 112 ? 0.1840 0.2630 0.2799 0.0015  -0.0257 0.0584  112 THR C OG1 
2597 C  CG2 . THR C 112 ? 0.1758 0.2590 0.2644 0.0086  -0.0071 0.0586  112 THR C CG2 
2598 N  N   . PHE C 113 ? 0.2198 0.2559 0.2649 0.0368  0.0016  0.0622  113 PHE C N   
2599 C  CA  . PHE C 113 ? 0.2574 0.2864 0.2596 0.0322  -0.0315 0.0662  113 PHE C CA  
2600 C  C   . PHE C 113 ? 0.2904 0.3126 0.2662 0.0614  -0.0568 0.0540  113 PHE C C   
2601 O  O   . PHE C 113 ? 0.3128 0.3462 0.2589 0.0827  -0.0641 0.0476  113 PHE C O   
2602 C  CB  . PHE C 113 ? 0.2664 0.2976 0.2580 0.0036  -0.0265 0.0717  113 PHE C CB  
2603 C  CG  . PHE C 113 ? 0.2799 0.2972 0.2476 -0.0317 -0.0241 0.0712  113 PHE C CG  
2604 C  CD1 . PHE C 113 ? 0.3176 0.3239 0.2648 -0.0772 -0.0383 0.0801  113 PHE C CD1 
2605 C  CD2 . PHE C 113 ? 0.2559 0.2801 0.2394 -0.0194 -0.0190 0.0561  113 PHE C CD2 
2606 C  CE1 . PHE C 113 ? 0.3274 0.3352 0.2701 -0.0787 -0.0553 0.0836  113 PHE C CE1 
2607 C  CE2 . PHE C 113 ? 0.2770 0.2800 0.2454 -0.0324 -0.0352 0.0618  113 PHE C CE2 
2608 C  CZ  . PHE C 113 ? 0.3055 0.3128 0.2605 -0.0557 -0.0579 0.0755  113 PHE C CZ  
2609 N  N   . ALA C 114 ? 0.3069 0.3176 0.2845 0.0504  -0.0726 0.0329  114 ALA C N   
2610 C  CA  . ALA C 114 ? 0.3274 0.3410 0.2992 0.0332  -0.0983 0.0223  114 ALA C CA  
2611 C  C   . ALA C 114 ? 0.3615 0.3847 0.3137 0.0363  -0.0975 0.0138  114 ALA C C   
2612 O  O   . ALA C 114 ? 0.3459 0.4089 0.3199 0.0609  -0.1029 0.0127  114 ALA C O   
2613 C  CB  . ALA C 114 ? 0.3257 0.3279 0.3048 0.0122  -0.1081 0.0260  114 ALA C CB  
2614 O  OXT . ALA C 114 ? 0.4036 0.4133 0.3260 0.0227  -0.0821 0.0122  114 ALA C OXT 
2615 C  C1  . HFC D .   ? 0.4374 0.4962 0.4896 0.0585  -0.0530 0.0899  201 HFC A C1  
2616 C  C2  . HFC D .   ? 0.4374 0.4960 0.4891 0.0496  -0.0518 0.0915  201 HFC A C2  
2617 C  C3  . HFC D .   ? 0.4427 0.4942 0.4950 0.0588  -0.0645 0.0856  201 HFC A C3  
2618 C  C4  . HFC D .   ? 0.4437 0.4906 0.4982 0.0758  -0.0817 0.0755  201 HFC A C4  
2619 C  C5  . HFC D .   ? 0.4492 0.4912 0.4995 0.0764  -0.0760 0.0622  201 HFC A C5  
2620 C  C6  . HFC D .   ? 0.4423 0.4959 0.4944 0.0627  -0.0634 0.0751  201 HFC A C6  
2621 O  O7  . HFC D .   ? 0.4293 0.4964 0.4835 0.0639  -0.0438 0.0967  201 HFC A O7  
2622 C  C8  . HFC D .   ? 0.4264 0.5086 0.4834 0.0543  -0.0387 0.0998  201 HFC A C8  
2623 C  C9  . HFC D .   ? 0.4306 0.5071 0.4843 0.0492  -0.0335 0.0967  201 HFC A C9  
2624 C  C10 . HFC D .   ? 0.4326 0.5014 0.4845 0.0434  -0.0383 0.0940  201 HFC A C10 
2625 O  O11 . HFC D .   ? 0.4129 0.5064 0.4782 0.0525  -0.0464 0.1053  201 HFC A O11 
2626 O  O12 . HFC D .   ? 0.4577 0.4855 0.5020 0.0829  -0.0773 0.0407  201 HFC A O12 
2627 O  O13 . HFC D .   ? 0.4293 0.4794 0.4935 0.0915  -0.1096 0.0863  201 HFC A O13 
2628 CL CL  . CL  E .   ? 0.2432 0.5246 0.2403 0.0845  -0.0254 -0.0981 202 CL  A CL  
2629 CL CL  . CL  F .   ? 0.3711 0.3740 0.3569 0.0395  0.0406  0.0080  203 CL  A CL  
2630 CL CL  . CL  G .   ? 0.2513 0.2513 0.2522 0.0152  0.0089  0.0247  204 CL  A CL  
2631 CL CL  . CL  H .   ? 0.8514 0.2771 0.2967 -0.1678 0.1324  -0.0350 201 CL  B CL  
2632 CL CL  . CL  I .   ? 0.2513 0.2550 0.2513 -0.0069 0.0361  0.0174  202 CL  B CL  
2633 CL CL  . CL  J .   ? 0.2318 0.2069 0.5587 -0.0007 -0.0939 0.0148  201 CL  C CL  
2634 CL CL  . CL  K .   ? 0.3493 0.3606 0.3541 0.0124  0.0029  0.0369  202 CL  C CL  
2635 CL CL  . CL  L .   ? 0.2549 0.2664 0.2513 0.0074  0.0126  0.0403  203 CL  C CL  
# 
