data_7EE8
# 
_entry.id   7EE8 
# 
_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   7EE8         pdb_00007ee8 10.2210/pdb7ee8/pdb 
WWPDB D_1300021264 ?            ?                   
# 
_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                        7EE8 
_pdbx_database_status.recvd_initial_deposition_date   2021-03-17 
_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 'CHLORIDE ION'                              35.453    9   ?                ? ? ? 
3 non-polymer syn '3-[(2R)-2-azanyl-1-oxidanyl-propyl]phenol' 167.205   1   ?                ? ? ? 
4 non-polymer syn '3-[(2S)-2-azanyl-1-oxidanyl-propyl]phenol' 167.205   1   ?                ? ? ? 
5 water       nat water                                       18.015    428 ?                ? ? ? 
# 
_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 'CHLORIDE ION'                              CL  
3 '3-[(2R)-2-azanyl-1-oxidanyl-propyl]phenol' 7Y8 
4 '3-[(2S)-2-azanyl-1-oxidanyl-propyl]phenol' J23 
5 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 
7Y8 non-polymer         . '3-[(2R)-2-azanyl-1-oxidanyl-propyl]phenol' ? 'C9 H13 N O2'    167.205 
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  
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 
J23 non-polymer         . '3-[(2S)-2-azanyl-1-oxidanyl-propyl]phenol' ? 'C9 H13 N O2'    167.205 
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        7Y8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   7Y8 
_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 CL  1   201 1   CL  CL  A . 
E 2 CL  1   202 5   CL  CL  A . 
F 2 CL  1   203 7   CL  CL  A . 
G 3 7Y8 1   204 1   7Y8 MAL A . 
H 2 CL  1   201 2   CL  CL  B . 
I 2 CL  1   202 3   CL  CL  B . 
J 2 CL  1   203 6   CL  CL  B . 
K 4 J23 1   204 2   J23 MAL B . 
L 2 CL  1   201 4   CL  CL  C . 
M 2 CL  1   202 8   CL  CL  C . 
N 2 CL  1   203 9   CL  CL  C . 
O 5 HOH 1   301 317 HOH HOH A . 
O 5 HOH 2   302 290 HOH HOH A . 
O 5 HOH 3   303 129 HOH HOH A . 
O 5 HOH 4   304 67  HOH HOH A . 
O 5 HOH 5   305 407 HOH HOH A . 
O 5 HOH 6   306 172 HOH HOH A . 
O 5 HOH 7   307 245 HOH HOH A . 
O 5 HOH 8   308 377 HOH HOH A . 
O 5 HOH 9   309 136 HOH HOH A . 
O 5 HOH 10  310 159 HOH HOH A . 
O 5 HOH 11  311 283 HOH HOH A . 
O 5 HOH 12  312 25  HOH HOH A . 
O 5 HOH 13  313 125 HOH HOH A . 
O 5 HOH 14  314 375 HOH HOH A . 
O 5 HOH 15  315 397 HOH HOH A . 
O 5 HOH 16  316 28  HOH HOH A . 
O 5 HOH 17  317 97  HOH HOH A . 
O 5 HOH 18  318 83  HOH HOH A . 
O 5 HOH 19  319 367 HOH HOH A . 
O 5 HOH 20  320 357 HOH HOH A . 
O 5 HOH 21  321 17  HOH HOH A . 
O 5 HOH 22  322 55  HOH HOH A . 
O 5 HOH 23  323 272 HOH HOH A . 
O 5 HOH 24  324 232 HOH HOH A . 
O 5 HOH 25  325 304 HOH HOH A . 
O 5 HOH 26  326 127 HOH HOH A . 
O 5 HOH 27  327 15  HOH HOH A . 
O 5 HOH 28  328 264 HOH HOH A . 
O 5 HOH 29  329 43  HOH HOH A . 
O 5 HOH 30  330 204 HOH HOH A . 
O 5 HOH 31  331 65  HOH HOH A . 
O 5 HOH 32  332 82  HOH HOH A . 
O 5 HOH 33  333 288 HOH HOH A . 
O 5 HOH 34  334 332 HOH HOH A . 
O 5 HOH 35  335 162 HOH HOH A . 
O 5 HOH 36  336 181 HOH HOH A . 
O 5 HOH 37  337 243 HOH HOH A . 
O 5 HOH 38  338 21  HOH HOH A . 
O 5 HOH 39  339 392 HOH HOH A . 
O 5 HOH 40  340 13  HOH HOH A . 
O 5 HOH 41  341 14  HOH HOH A . 
O 5 HOH 42  342 103 HOH HOH A . 
O 5 HOH 43  343 191 HOH HOH A . 
O 5 HOH 44  344 66  HOH HOH A . 
O 5 HOH 45  345 163 HOH HOH A . 
O 5 HOH 46  346 130 HOH HOH A . 
O 5 HOH 47  347 269 HOH HOH A . 
O 5 HOH 48  348 398 HOH HOH A . 
O 5 HOH 49  349 142 HOH HOH A . 
O 5 HOH 50  350 147 HOH HOH A . 
O 5 HOH 51  351 155 HOH HOH A . 
O 5 HOH 52  352 80  HOH HOH A . 
O 5 HOH 53  353 145 HOH HOH A . 
O 5 HOH 54  354 75  HOH HOH A . 
O 5 HOH 55  355 53  HOH HOH A . 
O 5 HOH 56  356 135 HOH HOH A . 
O 5 HOH 57  357 89  HOH HOH A . 
O 5 HOH 58  358 113 HOH HOH A . 
O 5 HOH 59  359 47  HOH HOH A . 
O 5 HOH 60  360 86  HOH HOH A . 
O 5 HOH 61  361 119 HOH HOH A . 
O 5 HOH 62  362 222 HOH HOH A . 
O 5 HOH 63  363 399 HOH HOH A . 
O 5 HOH 64  364 342 HOH HOH A . 
O 5 HOH 65  365 24  HOH HOH A . 
O 5 HOH 66  366 106 HOH HOH A . 
O 5 HOH 67  367 91  HOH HOH A . 
O 5 HOH 68  368 310 HOH HOH A . 
O 5 HOH 69  369 177 HOH HOH A . 
O 5 HOH 70  370 372 HOH HOH A . 
O 5 HOH 71  371 87  HOH HOH A . 
O 5 HOH 72  372 313 HOH HOH A . 
O 5 HOH 73  373 250 HOH HOH A . 
O 5 HOH 74  374 6   HOH HOH A . 
O 5 HOH 75  375 380 HOH HOH A . 
O 5 HOH 76  376 370 HOH HOH A . 
O 5 HOH 77  377 2   HOH HOH A . 
O 5 HOH 78  378 196 HOH HOH A . 
O 5 HOH 79  379 175 HOH HOH A . 
O 5 HOH 80  380 64  HOH HOH A . 
O 5 HOH 81  381 140 HOH HOH A . 
O 5 HOH 82  382 201 HOH HOH A . 
O 5 HOH 83  383 5   HOH HOH A . 
O 5 HOH 84  384 121 HOH HOH A . 
O 5 HOH 85  385 109 HOH HOH A . 
O 5 HOH 86  386 38  HOH HOH A . 
O 5 HOH 87  387 85  HOH HOH A . 
O 5 HOH 88  388 11  HOH HOH A . 
O 5 HOH 89  389 280 HOH HOH A . 
O 5 HOH 90  390 373 HOH HOH A . 
O 5 HOH 91  391 26  HOH HOH A . 
O 5 HOH 92  392 261 HOH HOH A . 
O 5 HOH 93  393 302 HOH HOH A . 
O 5 HOH 94  394 320 HOH HOH A . 
O 5 HOH 95  395 395 HOH HOH A . 
O 5 HOH 96  396 139 HOH HOH A . 
O 5 HOH 97  397 54  HOH HOH A . 
O 5 HOH 98  398 403 HOH HOH A . 
O 5 HOH 99  399 79  HOH HOH A . 
O 5 HOH 100 400 42  HOH HOH A . 
O 5 HOH 101 401 202 HOH HOH A . 
O 5 HOH 102 402 78  HOH HOH A . 
O 5 HOH 103 403 72  HOH HOH A . 
O 5 HOH 104 404 267 HOH HOH A . 
O 5 HOH 105 405 84  HOH HOH A . 
O 5 HOH 106 406 68  HOH HOH A . 
O 5 HOH 107 407 256 HOH HOH A . 
O 5 HOH 108 408 426 HOH HOH A . 
O 5 HOH 109 409 241 HOH HOH A . 
O 5 HOH 110 410 221 HOH HOH A . 
O 5 HOH 111 411 312 HOH HOH A . 
O 5 HOH 112 412 344 HOH HOH A . 
O 5 HOH 113 413 308 HOH HOH A . 
O 5 HOH 114 414 422 HOH HOH A . 
O 5 HOH 115 415 61  HOH HOH A . 
O 5 HOH 116 416 396 HOH HOH A . 
O 5 HOH 117 417 359 HOH HOH A . 
O 5 HOH 118 418 362 HOH HOH A . 
O 5 HOH 119 419 418 HOH HOH A . 
O 5 HOH 120 420 262 HOH HOH A . 
O 5 HOH 121 421 419 HOH HOH A . 
O 5 HOH 122 422 77  HOH HOH A . 
O 5 HOH 123 423 255 HOH HOH A . 
O 5 HOH 124 424 150 HOH HOH A . 
O 5 HOH 125 425 200 HOH HOH A . 
O 5 HOH 126 426 322 HOH HOH A . 
O 5 HOH 127 427 345 HOH HOH A . 
O 5 HOH 128 428 231 HOH HOH A . 
O 5 HOH 129 429 96  HOH HOH A . 
O 5 HOH 130 430 209 HOH HOH A . 
O 5 HOH 131 431 356 HOH HOH A . 
O 5 HOH 132 432 263 HOH HOH A . 
O 5 HOH 133 433 390 HOH HOH A . 
O 5 HOH 134 434 303 HOH HOH A . 
O 5 HOH 135 435 318 HOH HOH A . 
O 5 HOH 136 436 354 HOH HOH A . 
O 5 HOH 137 437 411 HOH HOH A . 
O 5 HOH 138 438 414 HOH HOH A . 
O 5 HOH 139 439 382 HOH HOH A . 
O 5 HOH 140 440 253 HOH HOH A . 
O 5 HOH 141 441 381 HOH HOH A . 
O 5 HOH 142 442 230 HOH HOH A . 
O 5 HOH 143 443 374 HOH HOH A . 
O 5 HOH 144 444 368 HOH HOH A . 
O 5 HOH 145 445 117 HOH HOH A . 
O 5 HOH 146 446 229 HOH HOH A . 
O 5 HOH 147 447 386 HOH HOH A . 
O 5 HOH 148 448 36  HOH HOH A . 
O 5 HOH 149 449 16  HOH HOH A . 
O 5 HOH 150 450 348 HOH HOH A . 
P 5 HOH 1   301 248 HOH HOH B . 
P 5 HOH 2   302 179 HOH HOH B . 
P 5 HOH 3   303 265 HOH HOH B . 
P 5 HOH 4   304 358 HOH HOH B . 
P 5 HOH 5   305 252 HOH HOH B . 
P 5 HOH 6   306 58  HOH HOH B . 
P 5 HOH 7   307 180 HOH HOH B . 
P 5 HOH 8   308 19  HOH HOH B . 
P 5 HOH 9   309 410 HOH HOH B . 
P 5 HOH 10  310 360 HOH HOH B . 
P 5 HOH 11  311 305 HOH HOH B . 
P 5 HOH 12  312 420 HOH HOH B . 
P 5 HOH 13  313 110 HOH HOH B . 
P 5 HOH 14  314 120 HOH HOH B . 
P 5 HOH 15  315 220 HOH HOH B . 
P 5 HOH 16  316 101 HOH HOH B . 
P 5 HOH 17  317 266 HOH HOH B . 
P 5 HOH 18  318 76  HOH HOH B . 
P 5 HOH 19  319 226 HOH HOH B . 
P 5 HOH 20  320 299 HOH HOH B . 
P 5 HOH 21  321 173 HOH HOH B . 
P 5 HOH 22  322 22  HOH HOH B . 
P 5 HOH 23  323 278 HOH HOH B . 
P 5 HOH 24  324 108 HOH HOH B . 
P 5 HOH 25  325 50  HOH HOH B . 
P 5 HOH 26  326 225 HOH HOH B . 
P 5 HOH 27  327 138 HOH HOH B . 
P 5 HOH 28  328 115 HOH HOH B . 
P 5 HOH 29  329 393 HOH HOH B . 
P 5 HOH 30  330 378 HOH HOH B . 
P 5 HOH 31  331 228 HOH HOH B . 
P 5 HOH 32  332 165 HOH HOH B . 
P 5 HOH 33  333 18  HOH HOH B . 
P 5 HOH 34  334 287 HOH HOH B . 
P 5 HOH 35  335 49  HOH HOH B . 
P 5 HOH 36  336 421 HOH HOH B . 
P 5 HOH 37  337 112 HOH HOH B . 
P 5 HOH 38  338 289 HOH HOH B . 
P 5 HOH 39  339 122 HOH HOH B . 
P 5 HOH 40  340 237 HOH HOH B . 
P 5 HOH 41  341 244 HOH HOH B . 
P 5 HOH 42  342 33  HOH HOH B . 
P 5 HOH 43  343 99  HOH HOH B . 
P 5 HOH 44  344 137 HOH HOH B . 
P 5 HOH 45  345 143 HOH HOH B . 
P 5 HOH 46  346 189 HOH HOH B . 
P 5 HOH 47  347 153 HOH HOH B . 
P 5 HOH 48  348 246 HOH HOH B . 
P 5 HOH 49  349 92  HOH HOH B . 
P 5 HOH 50  350 73  HOH HOH B . 
P 5 HOH 51  351 168 HOH HOH B . 
P 5 HOH 52  352 178 HOH HOH B . 
P 5 HOH 53  353 118 HOH HOH B . 
P 5 HOH 54  354 347 HOH HOH B . 
P 5 HOH 55  355 29  HOH HOH B . 
P 5 HOH 56  356 285 HOH HOH B . 
P 5 HOH 57  357 338 HOH HOH B . 
P 5 HOH 58  358 391 HOH HOH B . 
P 5 HOH 59  359 146 HOH HOH B . 
P 5 HOH 60  360 343 HOH HOH B . 
P 5 HOH 61  361 346 HOH HOH B . 
P 5 HOH 62  362 238 HOH HOH B . 
P 5 HOH 63  363 133 HOH HOH B . 
P 5 HOH 64  364 218 HOH HOH B . 
P 5 HOH 65  365 114 HOH HOH B . 
P 5 HOH 66  366 170 HOH HOH B . 
P 5 HOH 67  367 3   HOH HOH B . 
P 5 HOH 68  368 270 HOH HOH B . 
P 5 HOH 69  369 171 HOH HOH B . 
P 5 HOH 70  370 131 HOH HOH B . 
P 5 HOH 71  371 157 HOH HOH B . 
P 5 HOH 72  372 176 HOH HOH B . 
P 5 HOH 73  373 9   HOH HOH B . 
P 5 HOH 74  374 81  HOH HOH B . 
P 5 HOH 75  375 71  HOH HOH B . 
P 5 HOH 76  376 423 HOH HOH B . 
P 5 HOH 77  377 350 HOH HOH B . 
P 5 HOH 78  378 336 HOH HOH B . 
P 5 HOH 79  379 128 HOH HOH B . 
P 5 HOH 80  380 198 HOH HOH B . 
P 5 HOH 81  381 100 HOH HOH B . 
P 5 HOH 82  382 8   HOH HOH B . 
P 5 HOH 83  383 307 HOH HOH B . 
P 5 HOH 84  384 4   HOH HOH B . 
P 5 HOH 85  385 186 HOH HOH B . 
P 5 HOH 86  386 69  HOH HOH B . 
P 5 HOH 87  387 406 HOH HOH B . 
P 5 HOH 88  388 59  HOH HOH B . 
P 5 HOH 89  389 251 HOH HOH B . 
P 5 HOH 90  390 340 HOH HOH B . 
P 5 HOH 91  391 333 HOH HOH B . 
P 5 HOH 92  392 416 HOH HOH B . 
P 5 HOH 93  393 273 HOH HOH B . 
P 5 HOH 94  394 206 HOH HOH B . 
P 5 HOH 95  395 149 HOH HOH B . 
P 5 HOH 96  396 400 HOH HOH B . 
P 5 HOH 97  397 156 HOH HOH B . 
P 5 HOH 98  398 32  HOH HOH B . 
P 5 HOH 99  399 281 HOH HOH B . 
P 5 HOH 100 400 208 HOH HOH B . 
P 5 HOH 101 401 46  HOH HOH B . 
P 5 HOH 102 402 274 HOH HOH B . 
P 5 HOH 103 403 328 HOH HOH B . 
P 5 HOH 104 404 294 HOH HOH B . 
P 5 HOH 105 405 195 HOH HOH B . 
P 5 HOH 106 406 394 HOH HOH B . 
P 5 HOH 107 407 277 HOH HOH B . 
P 5 HOH 108 408 301 HOH HOH B . 
P 5 HOH 109 409 384 HOH HOH B . 
P 5 HOH 110 410 355 HOH HOH B . 
P 5 HOH 111 411 216 HOH HOH B . 
P 5 HOH 112 412 279 HOH HOH B . 
P 5 HOH 113 413 296 HOH HOH B . 
P 5 HOH 114 414 70  HOH HOH B . 
P 5 HOH 115 415 260 HOH HOH B . 
P 5 HOH 116 416 324 HOH HOH B . 
P 5 HOH 117 417 161 HOH HOH B . 
P 5 HOH 118 418 309 HOH HOH B . 
P 5 HOH 119 419 271 HOH HOH B . 
P 5 HOH 120 420 401 HOH HOH B . 
P 5 HOH 121 421 207 HOH HOH B . 
P 5 HOH 122 422 247 HOH HOH B . 
P 5 HOH 123 423 203 HOH HOH B . 
P 5 HOH 124 424 234 HOH HOH B . 
P 5 HOH 125 425 364 HOH HOH B . 
P 5 HOH 126 426 351 HOH HOH B . 
P 5 HOH 127 427 300 HOH HOH B . 
P 5 HOH 128 428 298 HOH HOH B . 
P 5 HOH 129 429 102 HOH HOH B . 
P 5 HOH 130 430 335 HOH HOH B . 
P 5 HOH 131 431 409 HOH HOH B . 
P 5 HOH 132 432 334 HOH HOH B . 
P 5 HOH 133 433 321 HOH HOH B . 
P 5 HOH 134 434 327 HOH HOH B . 
P 5 HOH 135 435 402 HOH HOH B . 
P 5 HOH 136 436 214 HOH HOH B . 
P 5 HOH 137 437 151 HOH HOH B . 
P 5 HOH 138 438 339 HOH HOH B . 
P 5 HOH 139 439 37  HOH HOH B . 
P 5 HOH 140 440 314 HOH HOH B . 
Q 5 HOH 1   301 319 HOH HOH C . 
Q 5 HOH 2   302 211 HOH HOH C . 
Q 5 HOH 3   303 383 HOH HOH C . 
Q 5 HOH 4   304 94  HOH HOH C . 
Q 5 HOH 5   305 123 HOH HOH C . 
Q 5 HOH 6   306 284 HOH HOH C . 
Q 5 HOH 7   307 323 HOH HOH C . 
Q 5 HOH 8   308 282 HOH HOH C . 
Q 5 HOH 9   309 326 HOH HOH C . 
Q 5 HOH 10  310 349 HOH HOH C . 
Q 5 HOH 11  311 295 HOH HOH C . 
Q 5 HOH 12  312 44  HOH HOH C . 
Q 5 HOH 13  313 90  HOH HOH C . 
Q 5 HOH 14  314 10  HOH HOH C . 
Q 5 HOH 15  315 40  HOH HOH C . 
Q 5 HOH 16  316 134 HOH HOH C . 
Q 5 HOH 17  317 95  HOH HOH C . 
Q 5 HOH 18  318 233 HOH HOH C . 
Q 5 HOH 19  319 185 HOH HOH C . 
Q 5 HOH 20  320 166 HOH HOH C . 
Q 5 HOH 21  321 371 HOH HOH C . 
Q 5 HOH 22  322 30  HOH HOH C . 
Q 5 HOH 23  323 353 HOH HOH C . 
Q 5 HOH 24  324 427 HOH HOH C . 
Q 5 HOH 25  325 291 HOH HOH C . 
Q 5 HOH 26  326 132 HOH HOH C . 
Q 5 HOH 27  327 23  HOH HOH C . 
Q 5 HOH 28  328 385 HOH HOH C . 
Q 5 HOH 29  329 268 HOH HOH C . 
Q 5 HOH 30  330 217 HOH HOH C . 
Q 5 HOH 31  331 88  HOH HOH C . 
Q 5 HOH 32  332 34  HOH HOH C . 
Q 5 HOH 33  333 365 HOH HOH C . 
Q 5 HOH 34  334 249 HOH HOH C . 
Q 5 HOH 35  335 52  HOH HOH C . 
Q 5 HOH 36  336 98  HOH HOH C . 
Q 5 HOH 37  337 183 HOH HOH C . 
Q 5 HOH 38  338 39  HOH HOH C . 
Q 5 HOH 39  339 213 HOH HOH C . 
Q 5 HOH 40  340 169 HOH HOH C . 
Q 5 HOH 41  341 223 HOH HOH C . 
Q 5 HOH 42  342 93  HOH HOH C . 
Q 5 HOH 43  343 154 HOH HOH C . 
Q 5 HOH 44  344 239 HOH HOH C . 
Q 5 HOH 45  345 389 HOH HOH C . 
Q 5 HOH 46  346 20  HOH HOH C . 
Q 5 HOH 47  347 152 HOH HOH C . 
Q 5 HOH 48  348 219 HOH HOH C . 
Q 5 HOH 49  349 227 HOH HOH C . 
Q 5 HOH 50  350 417 HOH HOH C . 
Q 5 HOH 51  351 56  HOH HOH C . 
Q 5 HOH 52  352 190 HOH HOH C . 
Q 5 HOH 53  353 341 HOH HOH C . 
Q 5 HOH 54  354 194 HOH HOH C . 
Q 5 HOH 55  355 158 HOH HOH C . 
Q 5 HOH 56  356 182 HOH HOH C . 
Q 5 HOH 57  357 210 HOH HOH C . 
Q 5 HOH 58  358 276 HOH HOH C . 
Q 5 HOH 59  359 174 HOH HOH C . 
Q 5 HOH 60  360 240 HOH HOH C . 
Q 5 HOH 61  361 188 HOH HOH C . 
Q 5 HOH 62  362 254 HOH HOH C . 
Q 5 HOH 63  363 366 HOH HOH C . 
Q 5 HOH 64  364 215 HOH HOH C . 
Q 5 HOH 65  365 63  HOH HOH C . 
Q 5 HOH 66  366 45  HOH HOH C . 
Q 5 HOH 67  367 316 HOH HOH C . 
Q 5 HOH 68  368 212 HOH HOH C . 
Q 5 HOH 69  369 1   HOH HOH C . 
Q 5 HOH 70  370 111 HOH HOH C . 
Q 5 HOH 71  371 51  HOH HOH C . 
Q 5 HOH 72  372 144 HOH HOH C . 
Q 5 HOH 73  373 388 HOH HOH C . 
Q 5 HOH 74  374 141 HOH HOH C . 
Q 5 HOH 75  375 12  HOH HOH C . 
Q 5 HOH 76  376 74  HOH HOH C . 
Q 5 HOH 77  377 413 HOH HOH C . 
Q 5 HOH 78  378 41  HOH HOH C . 
Q 5 HOH 79  379 297 HOH HOH C . 
Q 5 HOH 80  380 331 HOH HOH C . 
Q 5 HOH 81  381 104 HOH HOH C . 
Q 5 HOH 82  382 160 HOH HOH C . 
Q 5 HOH 83  383 60  HOH HOH C . 
Q 5 HOH 84  384 361 HOH HOH C . 
Q 5 HOH 85  385 7   HOH HOH C . 
Q 5 HOH 86  386 167 HOH HOH C . 
Q 5 HOH 87  387 376 HOH HOH C . 
Q 5 HOH 88  388 124 HOH HOH C . 
Q 5 HOH 89  389 292 HOH HOH C . 
Q 5 HOH 90  390 415 HOH HOH C . 
Q 5 HOH 91  391 205 HOH HOH C . 
Q 5 HOH 92  392 62  HOH HOH C . 
Q 5 HOH 93  393 31  HOH HOH C . 
Q 5 HOH 94  394 192 HOH HOH C . 
Q 5 HOH 95  395 224 HOH HOH C . 
Q 5 HOH 96  396 35  HOH HOH C . 
Q 5 HOH 97  397 187 HOH HOH C . 
Q 5 HOH 98  398 164 HOH HOH C . 
Q 5 HOH 99  399 293 HOH HOH C . 
Q 5 HOH 100 400 236 HOH HOH C . 
Q 5 HOH 101 401 363 HOH HOH C . 
Q 5 HOH 102 402 105 HOH HOH C . 
Q 5 HOH 103 403 352 HOH HOH C . 
Q 5 HOH 104 404 197 HOH HOH C . 
Q 5 HOH 105 405 148 HOH HOH C . 
Q 5 HOH 106 406 379 HOH HOH C . 
Q 5 HOH 107 407 235 HOH HOH C . 
Q 5 HOH 108 408 199 HOH HOH C . 
Q 5 HOH 109 409 184 HOH HOH C . 
Q 5 HOH 110 410 126 HOH HOH C . 
Q 5 HOH 111 411 325 HOH HOH C . 
Q 5 HOH 112 412 27  HOH HOH C . 
Q 5 HOH 113 413 404 HOH HOH C . 
Q 5 HOH 114 414 275 HOH HOH C . 
Q 5 HOH 115 415 48  HOH HOH C . 
Q 5 HOH 116 416 405 HOH HOH C . 
Q 5 HOH 117 417 408 HOH HOH C . 
Q 5 HOH 118 418 286 HOH HOH C . 
Q 5 HOH 119 419 315 HOH HOH C . 
Q 5 HOH 120 420 424 HOH HOH C . 
Q 5 HOH 121 421 387 HOH HOH C . 
Q 5 HOH 122 422 425 HOH HOH C . 
Q 5 HOH 123 423 428 HOH HOH C . 
Q 5 HOH 124 424 257 HOH HOH C . 
Q 5 HOH 125 425 107 HOH HOH C . 
Q 5 HOH 126 426 242 HOH HOH C . 
Q 5 HOH 127 427 116 HOH HOH C . 
Q 5 HOH 128 428 258 HOH HOH C . 
Q 5 HOH 129 429 412 HOH HOH C . 
Q 5 HOH 130 430 337 HOH HOH C . 
Q 5 HOH 131 431 329 HOH HOH C . 
Q 5 HOH 132 432 306 HOH HOH C . 
Q 5 HOH 133 433 369 HOH HOH C . 
Q 5 HOH 134 434 330 HOH HOH C . 
Q 5 HOH 135 435 259 HOH HOH C . 
Q 5 HOH 136 436 311 HOH HOH C . 
Q 5 HOH 137 437 193 HOH HOH C . 
Q 5 HOH 138 438 57  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 GLU 85 ? CG  ? B GLU 85 CG  
2 1 Y 1 B GLU 85 ? CD  ? B GLU 85 CD  
3 1 Y 1 B GLU 85 ? OE1 ? B GLU 85 OE1 
4 1 Y 1 B GLU 85 ? OE2 ? B GLU 85 OE2 
5 1 Y 1 C LYS 77 ? CE  ? C LYS 77 CE  
6 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'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALEPACK   ? ? ? .           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                     7EE8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.775 
_cell.length_a_esd                 ? 
_cell.length_b                     68.144 
_cell.length_b_esd                 ? 
_cell.length_c                     86.162 
_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                         7EE8 
_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                   7EE8 
_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            2.68 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         54.17 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            310 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2.0M Ammonium sulfate, pH7.50' 
_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         2017-04-20 
_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   0.97776 
_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        0.97776 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          13.53 
_reflns.entry_id                                       7EE8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.22 
_reflns.d_resolution_low                               50 
_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                                     117071 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                17.4 
_reflns.pdbx_Rmerge_I_obs                              0.103 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.103 
_reflns.pdbx_netI_over_av_sigmaI                       27.78 
_reflns.pdbx_netI_over_sigmaI                          27.78 
_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                                0.107 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.937 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.22 
_reflns_shell.d_res_low                                     1.26 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.76 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             11499 
_reflns_shell.percent_possible_all                          98.1 
_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                                  1.052 
_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                               15.4 
_reflns_shell.pdbx_Rsym_value                               1.052 
_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                               1.089 
_reflns_shell.pdbx_Rpim_I_all                               0.879 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.879 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                                62.320 
_refine.B_iso_mean                               19.2074 
_refine.B_iso_min                                8.160 
_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                                 7EE8 
_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                            1.2200 
_refine.ls_d_res_low                             36.4140 
_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                     114435 
_refine.ls_number_reflns_R_free                  1965 
_refine.ls_number_reflns_R_work                  112470 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.1700 
_refine.ls_percent_reflns_R_free                 1.7200 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2144 
_refine.ls_R_factor_R_free                       0.2416 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2139 
_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                          1.330 
_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                 32.0200 
_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                            0.2300 
_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                       1.2200 
_refine_hist.d_res_low                        36.4140 
_refine_hist.number_atoms_solvent             428 
_refine_hist.number_atoms_total               3056 
_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           24.98 
_refine_hist.pdbx_B_iso_mean_solvent          29.59 
_refine_hist.pdbx_number_atoms_protein        2595 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.008 ? 2747 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.949 ? 3755 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.092 ? 416  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 500  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.998 ? 1576 ? 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 1472 8.438 ? 1 
'X-RAY DIFFRACTION' 2 ? ? ? ? ? 2 TORSIONAL ? B 1472 8.438 ? 1 
'X-RAY DIFFRACTION' 3 ? ? ? ? ? 3 TORSIONAL ? C 1472 8.438 ? 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' 1.2200 1.2505 . . 121 6986 85.0000  . . . 0.4964 0.0000 0.4998 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.2505 1.2844 . . 125 7027 85.0000  . . . 0.5436 0.0000 0.5629 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.2844 1.3222 . . 145 8035 97.0000  . . . 0.4706 0.0000 0.4228 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.3222 1.3648 . . 141 8140 98.0000  . . . 0.2953 0.0000 0.3023 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.3648 1.4136 . . 142 7962 96.0000  . . . 0.3874 0.0000 0.3473 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.4136 1.4702 . . 138 8077 98.0000  . . . 0.3552 0.0000 0.3191 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.4702 1.5371 . . 143 8063 97.0000  . . . 0.3452 0.0000 0.3343 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.5371 1.6182 . . 142 8258 99.0000  . . . 0.1930 0.0000 0.1688 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.6182 1.7196 . . 146 8285 99.0000  . . . 0.1885 0.0000 0.1591 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.7196 1.8523 . . 144 8314 100.0000 . . . 0.2228 0.0000 0.1672 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.8523 2.0387 . . 143 8231 98.0000  . . . 0.2368 0.0000 0.1947 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.0387 2.3337 . . 140 8099 96.0000  . . . 0.2387 0.0000 0.1994 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.3337 2.9400 . . 148 8464 100.0000 . . . 0.2027 0.0000 0.1838 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.9400 36.414 . . 147 8529 97.0000  . . . 0.1917 0.0000 0.1671 . . . . . . . . . . . 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 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 ILE 4   . A PRO 1  A ILE 4   ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 2  A ASN 6  . A ALA 12  . A ASN 6  A ALA 12  ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 3  A VAL 14 . A LEU 19  . A VAL 14 A LEU 19  ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 4  A MET 2  . A MET 2   . A MET 2  A MET 2   ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 5  A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 6  A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 7  A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 8  A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 9  A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 1 10 A PRO 1  . A ALA 114 . A PRO 1  A ALA 114 ? 
;(chain A and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 1  B PRO 1  . B ILE 4   . B PRO 1  B ILE 4   ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 2  B ASN 6  . B ALA 12  . B ASN 6  B ALA 12  ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 3  B VAL 14 . B LEU 19  . B VAL 14 B LEU 19  ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 4  B GLU 54 . B SER 76  . B GLU 54 B SER 76  ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 5  B MET 2  . B MET 2   . B MET 2  B MET 2   ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 6  B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 7  B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 8  B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 9  B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 10 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 11 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 12 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 2 13 B PRO 1  . B ALA 114 . B PRO 1  B ALA 114 ? 
;(chain B and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 1  C PRO 1  . C ILE 4   . C PRO 1  C ILE 4   ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 2  C ASN 6  . C ALA 12  . C ASN 6  C ALA 12  ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 3  C VAL 14 . C LEU 19  . C VAL 14 C LEU 19  ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 4  C GLU 21 . C TYR 36  . C GLU 21 C TYR 36  ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 5  C ALA 38 . C SER 52  . C ALA 38 C SER 52  ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 6  C GLU 54 . C ALA 84  . C GLU 54 C ALA 84  ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 7  C GLU 85 . C GLU 85  . C GLU 85 C GLU 85  ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 8  C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 9  C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 10 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
1 3 11 C PRO 1  . C ALA 114 . C PRO 1  C ALA 114 ? 
;(chain C and (resid 1 through 4 or resid 6 through 12 or resid 14 through 19 or resid 21 through 36 or resid 38 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 89 or resid 91 through 114))
;
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     7EE8 
_struct.title                        'The crystal structure of MIF bound to compound D5' 
_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        7EE8 
_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 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 4 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
# 
_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 7EE8 A 1 ? 114 ? P14174 2 ? 115 ? 1 114 
2 1 7EE8 B 1 ? 114 ? P14174 2 ? 115 ? 1 114 
3 1 7EE8 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)' 7910  ? 
1 MORE         -123  ? 
1 'SSA (A^2)'  13220 ? 
# 
_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,P,Q 
# 
_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 TYR A 95  ? O TYR A 95  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 LEU A 46  ? N LEU A 46  O VAL B 41  ? O VAL B 41  
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 HIS C 62  ? O HIS C 62  N MET C 2   ? N MET C 2   
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 41  ? O VAL C 41  N LEU B 46  ? N LEU B 46  
# 
_pdbx_entry_details.entry_id                   7EE8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG B SER 53  ? A O B HOH 301 ? ? 2.06 
2 1 O  C HOH 431 ? ? O C HOH 434 ? ? 2.08 
3 1 O  C HOH 363 ? ? O C HOH 431 ? ? 2.11 
4 1 O  C HOH 411 ? ? O C HOH 419 ? ? 2.13 
5 1 O  A HOH 375 ? ? O A HOH 411 ? ? 2.13 
6 1 O  A HOH 411 ? ? O A HOH 434 ? ? 2.14 
7 1 O  A HOH 426 ? ? O A HOH 431 ? ? 2.18 
8 1 O  B HOH 301 ? ? O B HOH 390 ? ? 2.18 
9 1 O  A HOH 388 ? ? O A HOH 420 ? ? 2.18 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     111 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -150.53 
_pdbx_validate_torsion.psi             -158.91 
# 
_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                       450 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.83 
_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 
7Y8 C1   C  N N 1   
7Y8 C2   C  N R 2   
7Y8 C11  C  Y N 3   
7Y8 C12  C  Y N 4   
7Y8 C13  C  Y N 5   
7Y8 C14  C  Y N 6   
7Y8 C15  C  Y N 7   
7Y8 C17  C  Y N 8   
7Y8 C8   C  N N 9   
7Y8 N4   N  N N 10  
7Y8 O10  O  N N 11  
7Y8 O16  O  N N 12  
7Y8 H1   H  N N 13  
7Y8 H2   H  N N 14  
7Y8 H3   H  N N 15  
7Y8 H4   H  N N 16  
7Y8 H5   H  N N 17  
7Y8 H6   H  N N 18  
7Y8 H7   H  N N 19  
7Y8 H8   H  N N 20  
7Y8 H9   H  N N 21  
7Y8 H10  H  N N 22  
7Y8 H12  H  N N 23  
7Y8 H13  H  N N 24  
7Y8 H11  H  N N 25  
ALA N    N  N N 26  
ALA CA   C  N S 27  
ALA C    C  N N 28  
ALA O    O  N N 29  
ALA CB   C  N N 30  
ALA OXT  O  N N 31  
ALA H    H  N N 32  
ALA H2   H  N N 33  
ALA HA   H  N N 34  
ALA HB1  H  N N 35  
ALA HB2  H  N N 36  
ALA HB3  H  N N 37  
ALA HXT  H  N N 38  
ARG N    N  N N 39  
ARG CA   C  N S 40  
ARG C    C  N N 41  
ARG O    O  N N 42  
ARG CB   C  N N 43  
ARG CG   C  N N 44  
ARG CD   C  N N 45  
ARG NE   N  N N 46  
ARG CZ   C  N N 47  
ARG NH1  N  N N 48  
ARG NH2  N  N N 49  
ARG OXT  O  N N 50  
ARG H    H  N N 51  
ARG H2   H  N N 52  
ARG HA   H  N N 53  
ARG HB2  H  N N 54  
ARG HB3  H  N N 55  
ARG HG2  H  N N 56  
ARG HG3  H  N N 57  
ARG HD2  H  N N 58  
ARG HD3  H  N N 59  
ARG HE   H  N N 60  
ARG HH11 H  N N 61  
ARG HH12 H  N N 62  
ARG HH21 H  N N 63  
ARG HH22 H  N N 64  
ARG HXT  H  N N 65  
ASN N    N  N N 66  
ASN CA   C  N S 67  
ASN C    C  N N 68  
ASN O    O  N N 69  
ASN CB   C  N N 70  
ASN CG   C  N N 71  
ASN OD1  O  N N 72  
ASN ND2  N  N N 73  
ASN OXT  O  N N 74  
ASN H    H  N N 75  
ASN H2   H  N N 76  
ASN HA   H  N N 77  
ASN HB2  H  N N 78  
ASN HB3  H  N N 79  
ASN HD21 H  N N 80  
ASN HD22 H  N N 81  
ASN HXT  H  N N 82  
ASP N    N  N N 83  
ASP CA   C  N S 84  
ASP C    C  N N 85  
ASP O    O  N N 86  
ASP CB   C  N N 87  
ASP CG   C  N N 88  
ASP OD1  O  N N 89  
ASP OD2  O  N N 90  
ASP OXT  O  N N 91  
ASP H    H  N N 92  
ASP H2   H  N N 93  
ASP HA   H  N N 94  
ASP HB2  H  N N 95  
ASP HB3  H  N N 96  
ASP HD2  H  N N 97  
ASP HXT  H  N N 98  
CL  CL   CL N N 99  
CYS N    N  N N 100 
CYS CA   C  N R 101 
CYS C    C  N N 102 
CYS O    O  N N 103 
CYS CB   C  N N 104 
CYS SG   S  N N 105 
CYS OXT  O  N N 106 
CYS H    H  N N 107 
CYS H2   H  N N 108 
CYS HA   H  N N 109 
CYS HB2  H  N N 110 
CYS HB3  H  N N 111 
CYS HG   H  N N 112 
CYS HXT  H  N N 113 
GLN N    N  N N 114 
GLN CA   C  N S 115 
GLN C    C  N N 116 
GLN O    O  N N 117 
GLN CB   C  N N 118 
GLN CG   C  N N 119 
GLN CD   C  N N 120 
GLN OE1  O  N N 121 
GLN NE2  N  N N 122 
GLN OXT  O  N N 123 
GLN H    H  N N 124 
GLN H2   H  N N 125 
GLN HA   H  N N 126 
GLN HB2  H  N N 127 
GLN HB3  H  N N 128 
GLN HG2  H  N N 129 
GLN HG3  H  N N 130 
GLN HE21 H  N N 131 
GLN HE22 H  N N 132 
GLN HXT  H  N N 133 
GLU N    N  N N 134 
GLU CA   C  N S 135 
GLU C    C  N N 136 
GLU O    O  N N 137 
GLU CB   C  N N 138 
GLU CG   C  N N 139 
GLU CD   C  N N 140 
GLU OE1  O  N N 141 
GLU OE2  O  N N 142 
GLU OXT  O  N N 143 
GLU H    H  N N 144 
GLU H2   H  N N 145 
GLU HA   H  N N 146 
GLU HB2  H  N N 147 
GLU HB3  H  N N 148 
GLU HG2  H  N N 149 
GLU HG3  H  N N 150 
GLU HE2  H  N N 151 
GLU HXT  H  N N 152 
GLY N    N  N N 153 
GLY CA   C  N N 154 
GLY C    C  N N 155 
GLY O    O  N N 156 
GLY OXT  O  N N 157 
GLY H    H  N N 158 
GLY H2   H  N N 159 
GLY HA2  H  N N 160 
GLY HA3  H  N N 161 
GLY HXT  H  N N 162 
HIS N    N  N N 163 
HIS CA   C  N S 164 
HIS C    C  N N 165 
HIS O    O  N N 166 
HIS CB   C  N N 167 
HIS CG   C  Y N 168 
HIS ND1  N  Y N 169 
HIS CD2  C  Y N 170 
HIS CE1  C  Y N 171 
HIS NE2  N  Y N 172 
HIS OXT  O  N N 173 
HIS H    H  N N 174 
HIS H2   H  N N 175 
HIS HA   H  N N 176 
HIS HB2  H  N N 177 
HIS HB3  H  N N 178 
HIS HD1  H  N N 179 
HIS HD2  H  N N 180 
HIS HE1  H  N N 181 
HIS HE2  H  N N 182 
HIS HXT  H  N N 183 
HOH O    O  N N 184 
HOH H1   H  N N 185 
HOH H2   H  N N 186 
ILE N    N  N N 187 
ILE CA   C  N S 188 
ILE C    C  N N 189 
ILE O    O  N N 190 
ILE CB   C  N S 191 
ILE CG1  C  N N 192 
ILE CG2  C  N N 193 
ILE CD1  C  N N 194 
ILE OXT  O  N N 195 
ILE H    H  N N 196 
ILE H2   H  N N 197 
ILE HA   H  N N 198 
ILE HB   H  N N 199 
ILE HG12 H  N N 200 
ILE HG13 H  N N 201 
ILE HG21 H  N N 202 
ILE HG22 H  N N 203 
ILE HG23 H  N N 204 
ILE HD11 H  N N 205 
ILE HD12 H  N N 206 
ILE HD13 H  N N 207 
ILE HXT  H  N N 208 
J23 C1   C  N N 209 
J23 C2   C  N S 210 
J23 C11  C  Y N 211 
J23 C12  C  Y N 212 
J23 C13  C  Y N 213 
J23 C14  C  Y N 214 
J23 C15  C  Y N 215 
J23 C17  C  Y N 216 
J23 C8   C  N N 217 
J23 N4   N  N N 218 
J23 O10  O  N N 219 
J23 O16  O  N N 220 
J23 H1   H  N N 221 
J23 H2   H  N N 222 
J23 H3   H  N N 223 
J23 H4   H  N N 224 
J23 H5   H  N N 225 
J23 H6   H  N N 226 
J23 H7   H  N N 227 
J23 H8   H  N N 228 
J23 H9   H  N N 229 
J23 H10  H  N N 230 
J23 H12  H  N N 231 
J23 H13  H  N N 232 
J23 H11  H  N N 233 
LEU N    N  N N 234 
LEU CA   C  N S 235 
LEU C    C  N N 236 
LEU O    O  N N 237 
LEU CB   C  N N 238 
LEU CG   C  N N 239 
LEU CD1  C  N N 240 
LEU CD2  C  N N 241 
LEU OXT  O  N N 242 
LEU H    H  N N 243 
LEU H2   H  N N 244 
LEU HA   H  N N 245 
LEU HB2  H  N N 246 
LEU HB3  H  N N 247 
LEU HG   H  N N 248 
LEU HD11 H  N N 249 
LEU HD12 H  N N 250 
LEU HD13 H  N N 251 
LEU HD21 H  N N 252 
LEU HD22 H  N N 253 
LEU HD23 H  N N 254 
LEU HXT  H  N N 255 
LYS N    N  N N 256 
LYS CA   C  N S 257 
LYS C    C  N N 258 
LYS O    O  N N 259 
LYS CB   C  N N 260 
LYS CG   C  N N 261 
LYS CD   C  N N 262 
LYS CE   C  N N 263 
LYS NZ   N  N N 264 
LYS OXT  O  N N 265 
LYS H    H  N N 266 
LYS H2   H  N N 267 
LYS HA   H  N N 268 
LYS HB2  H  N N 269 
LYS HB3  H  N N 270 
LYS HG2  H  N N 271 
LYS HG3  H  N N 272 
LYS HD2  H  N N 273 
LYS HD3  H  N N 274 
LYS HE2  H  N N 275 
LYS HE3  H  N N 276 
LYS HZ1  H  N N 277 
LYS HZ2  H  N N 278 
LYS HZ3  H  N N 279 
LYS HXT  H  N N 280 
MET N    N  N N 281 
MET CA   C  N S 282 
MET C    C  N N 283 
MET O    O  N N 284 
MET CB   C  N N 285 
MET CG   C  N N 286 
MET SD   S  N N 287 
MET CE   C  N N 288 
MET OXT  O  N N 289 
MET H    H  N N 290 
MET H2   H  N N 291 
MET HA   H  N N 292 
MET HB2  H  N N 293 
MET HB3  H  N N 294 
MET HG2  H  N N 295 
MET HG3  H  N N 296 
MET HE1  H  N N 297 
MET HE2  H  N N 298 
MET HE3  H  N N 299 
MET HXT  H  N N 300 
PHE N    N  N N 301 
PHE CA   C  N S 302 
PHE C    C  N N 303 
PHE O    O  N N 304 
PHE CB   C  N N 305 
PHE CG   C  Y N 306 
PHE CD1  C  Y N 307 
PHE CD2  C  Y N 308 
PHE CE1  C  Y N 309 
PHE CE2  C  Y N 310 
PHE CZ   C  Y N 311 
PHE OXT  O  N N 312 
PHE H    H  N N 313 
PHE H2   H  N N 314 
PHE HA   H  N N 315 
PHE HB2  H  N N 316 
PHE HB3  H  N N 317 
PHE HD1  H  N N 318 
PHE HD2  H  N N 319 
PHE HE1  H  N N 320 
PHE HE2  H  N N 321 
PHE HZ   H  N N 322 
PHE HXT  H  N N 323 
PRO N    N  N N 324 
PRO CA   C  N S 325 
PRO C    C  N N 326 
PRO O    O  N N 327 
PRO CB   C  N N 328 
PRO CG   C  N N 329 
PRO CD   C  N N 330 
PRO OXT  O  N N 331 
PRO H    H  N N 332 
PRO HA   H  N N 333 
PRO HB2  H  N N 334 
PRO HB3  H  N N 335 
PRO HG2  H  N N 336 
PRO HG3  H  N N 337 
PRO HD2  H  N N 338 
PRO HD3  H  N N 339 
PRO HXT  H  N N 340 
SER N    N  N N 341 
SER CA   C  N S 342 
SER C    C  N N 343 
SER O    O  N N 344 
SER CB   C  N N 345 
SER OG   O  N N 346 
SER OXT  O  N N 347 
SER H    H  N N 348 
SER H2   H  N N 349 
SER HA   H  N N 350 
SER HB2  H  N N 351 
SER HB3  H  N N 352 
SER HG   H  N N 353 
SER HXT  H  N N 354 
THR N    N  N N 355 
THR CA   C  N S 356 
THR C    C  N N 357 
THR O    O  N N 358 
THR CB   C  N R 359 
THR OG1  O  N N 360 
THR CG2  C  N N 361 
THR OXT  O  N N 362 
THR H    H  N N 363 
THR H2   H  N N 364 
THR HA   H  N N 365 
THR HB   H  N N 366 
THR HG1  H  N N 367 
THR HG21 H  N N 368 
THR HG22 H  N N 369 
THR HG23 H  N N 370 
THR HXT  H  N N 371 
TRP N    N  N N 372 
TRP CA   C  N S 373 
TRP C    C  N N 374 
TRP O    O  N N 375 
TRP CB   C  N N 376 
TRP CG   C  Y N 377 
TRP CD1  C  Y N 378 
TRP CD2  C  Y N 379 
TRP NE1  N  Y N 380 
TRP CE2  C  Y N 381 
TRP CE3  C  Y N 382 
TRP CZ2  C  Y N 383 
TRP CZ3  C  Y N 384 
TRP CH2  C  Y N 385 
TRP OXT  O  N N 386 
TRP H    H  N N 387 
TRP H2   H  N N 388 
TRP HA   H  N N 389 
TRP HB2  H  N N 390 
TRP HB3  H  N N 391 
TRP HD1  H  N N 392 
TRP HE1  H  N N 393 
TRP HE3  H  N N 394 
TRP HZ2  H  N N 395 
TRP HZ3  H  N N 396 
TRP HH2  H  N N 397 
TRP HXT  H  N N 398 
TYR N    N  N N 399 
TYR CA   C  N S 400 
TYR C    C  N N 401 
TYR O    O  N N 402 
TYR CB   C  N N 403 
TYR CG   C  Y N 404 
TYR CD1  C  Y N 405 
TYR CD2  C  Y N 406 
TYR CE1  C  Y N 407 
TYR CE2  C  Y N 408 
TYR CZ   C  Y N 409 
TYR OH   O  N N 410 
TYR OXT  O  N N 411 
TYR H    H  N N 412 
TYR H2   H  N N 413 
TYR HA   H  N N 414 
TYR HB2  H  N N 415 
TYR HB3  H  N N 416 
TYR HD1  H  N N 417 
TYR HD2  H  N N 418 
TYR HE1  H  N N 419 
TYR HE2  H  N N 420 
TYR HH   H  N N 421 
TYR HXT  H  N N 422 
VAL N    N  N N 423 
VAL CA   C  N S 424 
VAL C    C  N N 425 
VAL O    O  N N 426 
VAL CB   C  N N 427 
VAL CG1  C  N N 428 
VAL CG2  C  N N 429 
VAL OXT  O  N N 430 
VAL H    H  N N 431 
VAL H2   H  N N 432 
VAL HA   H  N N 433 
VAL HB   H  N N 434 
VAL HG11 H  N N 435 
VAL HG12 H  N N 436 
VAL HG13 H  N N 437 
VAL HG21 H  N N 438 
VAL HG22 H  N N 439 
VAL HG23 H  N N 440 
VAL HXT  H  N N 441 
# 
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 
7Y8 C13 C12  doub Y N 1   
7Y8 C13 C14  sing Y N 2   
7Y8 C12 C11  sing Y N 3   
7Y8 C14 C15  doub Y N 4   
7Y8 N4  C2   sing N N 5   
7Y8 C11 C8   sing N N 6   
7Y8 C11 C17  doub Y N 7   
7Y8 C15 C17  sing Y N 8   
7Y8 C15 O16  sing N N 9   
7Y8 C8  C2   sing N N 10  
7Y8 C8  O10  sing N N 11  
7Y8 C2  C1   sing N N 12  
7Y8 C1  H1   sing N N 13  
7Y8 C1  H2   sing N N 14  
7Y8 C1  H3   sing N N 15  
7Y8 C2  H4   sing N N 16  
7Y8 C12 H5   sing N N 17  
7Y8 C13 H6   sing N N 18  
7Y8 C14 H7   sing N N 19  
7Y8 C17 H8   sing N N 20  
7Y8 N4  H9   sing N N 21  
7Y8 N4  H10  sing N N 22  
7Y8 O16 H12  sing N N 23  
7Y8 C8  H13  sing N N 24  
7Y8 O10 H11  sing N N 25  
ALA N   CA   sing N N 26  
ALA N   H    sing N N 27  
ALA N   H2   sing N N 28  
ALA CA  C    sing N N 29  
ALA CA  CB   sing N N 30  
ALA CA  HA   sing N N 31  
ALA C   O    doub N N 32  
ALA C   OXT  sing N N 33  
ALA CB  HB1  sing N N 34  
ALA CB  HB2  sing N N 35  
ALA CB  HB3  sing N N 36  
ALA OXT HXT  sing N N 37  
ARG N   CA   sing N N 38  
ARG N   H    sing N N 39  
ARG N   H2   sing N N 40  
ARG CA  C    sing N N 41  
ARG CA  CB   sing N N 42  
ARG CA  HA   sing N N 43  
ARG C   O    doub N N 44  
ARG C   OXT  sing N N 45  
ARG CB  CG   sing N N 46  
ARG CB  HB2  sing N N 47  
ARG CB  HB3  sing N N 48  
ARG CG  CD   sing N N 49  
ARG CG  HG2  sing N N 50  
ARG CG  HG3  sing N N 51  
ARG CD  NE   sing N N 52  
ARG CD  HD2  sing N N 53  
ARG CD  HD3  sing N N 54  
ARG NE  CZ   sing N N 55  
ARG NE  HE   sing N N 56  
ARG CZ  NH1  sing N N 57  
ARG CZ  NH2  doub N N 58  
ARG NH1 HH11 sing N N 59  
ARG NH1 HH12 sing N N 60  
ARG NH2 HH21 sing N N 61  
ARG NH2 HH22 sing N N 62  
ARG OXT HXT  sing N N 63  
ASN N   CA   sing N N 64  
ASN N   H    sing N N 65  
ASN N   H2   sing N N 66  
ASN CA  C    sing N N 67  
ASN CA  CB   sing N N 68  
ASN CA  HA   sing N N 69  
ASN C   O    doub N N 70  
ASN C   OXT  sing N N 71  
ASN CB  CG   sing N N 72  
ASN CB  HB2  sing N N 73  
ASN CB  HB3  sing N N 74  
ASN CG  OD1  doub N N 75  
ASN CG  ND2  sing N N 76  
ASN ND2 HD21 sing N N 77  
ASN ND2 HD22 sing N N 78  
ASN OXT HXT  sing N N 79  
ASP N   CA   sing N N 80  
ASP N   H    sing N N 81  
ASP N   H2   sing N N 82  
ASP CA  C    sing N N 83  
ASP CA  CB   sing N N 84  
ASP CA  HA   sing N N 85  
ASP C   O    doub N N 86  
ASP C   OXT  sing N N 87  
ASP CB  CG   sing N N 88  
ASP CB  HB2  sing N N 89  
ASP CB  HB3  sing N N 90  
ASP CG  OD1  doub N N 91  
ASP CG  OD2  sing N N 92  
ASP OD2 HD2  sing N N 93  
ASP OXT HXT  sing N N 94  
CYS N   CA   sing N N 95  
CYS N   H    sing N N 96  
CYS N   H2   sing N N 97  
CYS CA  C    sing N N 98  
CYS CA  CB   sing N N 99  
CYS CA  HA   sing N N 100 
CYS C   O    doub N N 101 
CYS C   OXT  sing N N 102 
CYS CB  SG   sing N N 103 
CYS CB  HB2  sing N N 104 
CYS CB  HB3  sing N N 105 
CYS SG  HG   sing N N 106 
CYS OXT HXT  sing N N 107 
GLN N   CA   sing N N 108 
GLN N   H    sing N N 109 
GLN N   H2   sing N N 110 
GLN CA  C    sing N N 111 
GLN CA  CB   sing N N 112 
GLN CA  HA   sing N N 113 
GLN C   O    doub N N 114 
GLN C   OXT  sing N N 115 
GLN CB  CG   sing N N 116 
GLN CB  HB2  sing N N 117 
GLN CB  HB3  sing N N 118 
GLN CG  CD   sing N N 119 
GLN CG  HG2  sing N N 120 
GLN CG  HG3  sing N N 121 
GLN CD  OE1  doub N N 122 
GLN CD  NE2  sing N N 123 
GLN NE2 HE21 sing N N 124 
GLN NE2 HE22 sing N N 125 
GLN OXT HXT  sing N N 126 
GLU N   CA   sing N N 127 
GLU N   H    sing N N 128 
GLU N   H2   sing N N 129 
GLU CA  C    sing N N 130 
GLU CA  CB   sing N N 131 
GLU CA  HA   sing N N 132 
GLU C   O    doub N N 133 
GLU C   OXT  sing N N 134 
GLU CB  CG   sing N N 135 
GLU CB  HB2  sing N N 136 
GLU CB  HB3  sing N N 137 
GLU CG  CD   sing N N 138 
GLU CG  HG2  sing N N 139 
GLU CG  HG3  sing N N 140 
GLU CD  OE1  doub N N 141 
GLU CD  OE2  sing N N 142 
GLU OE2 HE2  sing N N 143 
GLU OXT HXT  sing N N 144 
GLY N   CA   sing N N 145 
GLY N   H    sing N N 146 
GLY N   H2   sing N N 147 
GLY CA  C    sing N N 148 
GLY CA  HA2  sing N N 149 
GLY CA  HA3  sing N N 150 
GLY C   O    doub N N 151 
GLY C   OXT  sing N N 152 
GLY OXT HXT  sing N N 153 
HIS N   CA   sing N N 154 
HIS N   H    sing N N 155 
HIS N   H2   sing N N 156 
HIS CA  C    sing N N 157 
HIS CA  CB   sing N N 158 
HIS CA  HA   sing N N 159 
HIS C   O    doub N N 160 
HIS C   OXT  sing N N 161 
HIS CB  CG   sing N N 162 
HIS CB  HB2  sing N N 163 
HIS CB  HB3  sing N N 164 
HIS CG  ND1  sing Y N 165 
HIS CG  CD2  doub Y N 166 
HIS ND1 CE1  doub Y N 167 
HIS ND1 HD1  sing N N 168 
HIS CD2 NE2  sing Y N 169 
HIS CD2 HD2  sing N N 170 
HIS CE1 NE2  sing Y N 171 
HIS CE1 HE1  sing N N 172 
HIS NE2 HE2  sing N N 173 
HIS OXT HXT  sing N N 174 
HOH O   H1   sing N N 175 
HOH O   H2   sing N N 176 
ILE N   CA   sing N N 177 
ILE N   H    sing N N 178 
ILE N   H2   sing N N 179 
ILE CA  C    sing N N 180 
ILE CA  CB   sing N N 181 
ILE CA  HA   sing N N 182 
ILE C   O    doub N N 183 
ILE C   OXT  sing N N 184 
ILE CB  CG1  sing N N 185 
ILE CB  CG2  sing N N 186 
ILE CB  HB   sing N N 187 
ILE CG1 CD1  sing N N 188 
ILE CG1 HG12 sing N N 189 
ILE CG1 HG13 sing N N 190 
ILE CG2 HG21 sing N N 191 
ILE CG2 HG22 sing N N 192 
ILE CG2 HG23 sing N N 193 
ILE CD1 HD11 sing N N 194 
ILE CD1 HD12 sing N N 195 
ILE CD1 HD13 sing N N 196 
ILE OXT HXT  sing N N 197 
J23 C14 C13  doub Y N 198 
J23 C14 C15  sing Y N 199 
J23 O16 C15  sing N N 200 
J23 C13 C12  sing Y N 201 
J23 C15 C17  doub Y N 202 
J23 C12 C11  doub Y N 203 
J23 C17 C11  sing Y N 204 
J23 C11 C8   sing N N 205 
J23 C8  O10  sing N N 206 
J23 C8  C2   sing N N 207 
J23 N4  C2   sing N N 208 
J23 C2  C1   sing N N 209 
J23 C1  H1   sing N N 210 
J23 C1  H2   sing N N 211 
J23 C1  H3   sing N N 212 
J23 C2  H4   sing N N 213 
J23 C12 H5   sing N N 214 
J23 C13 H6   sing N N 215 
J23 C14 H7   sing N N 216 
J23 C17 H8   sing N N 217 
J23 N4  H9   sing N N 218 
J23 N4  H10  sing N N 219 
J23 O16 H12  sing N N 220 
J23 C8  H13  sing N N 221 
J23 O10 H11  sing N N 222 
LEU N   CA   sing N N 223 
LEU N   H    sing N N 224 
LEU N   H2   sing N N 225 
LEU CA  C    sing N N 226 
LEU CA  CB   sing N N 227 
LEU CA  HA   sing N N 228 
LEU C   O    doub N N 229 
LEU C   OXT  sing N N 230 
LEU CB  CG   sing N N 231 
LEU CB  HB2  sing N N 232 
LEU CB  HB3  sing N N 233 
LEU CG  CD1  sing N N 234 
LEU CG  CD2  sing N N 235 
LEU CG  HG   sing N N 236 
LEU CD1 HD11 sing N N 237 
LEU CD1 HD12 sing N N 238 
LEU CD1 HD13 sing N N 239 
LEU CD2 HD21 sing N N 240 
LEU CD2 HD22 sing N N 241 
LEU CD2 HD23 sing N N 242 
LEU OXT HXT  sing N N 243 
LYS N   CA   sing N N 244 
LYS N   H    sing N N 245 
LYS N   H2   sing N N 246 
LYS CA  C    sing N N 247 
LYS CA  CB   sing N N 248 
LYS CA  HA   sing N N 249 
LYS C   O    doub N N 250 
LYS C   OXT  sing N N 251 
LYS CB  CG   sing N N 252 
LYS CB  HB2  sing N N 253 
LYS CB  HB3  sing N N 254 
LYS CG  CD   sing N N 255 
LYS CG  HG2  sing N N 256 
LYS CG  HG3  sing N N 257 
LYS CD  CE   sing N N 258 
LYS CD  HD2  sing N N 259 
LYS CD  HD3  sing N N 260 
LYS CE  NZ   sing N N 261 
LYS CE  HE2  sing N N 262 
LYS CE  HE3  sing N N 263 
LYS NZ  HZ1  sing N N 264 
LYS NZ  HZ2  sing N N 265 
LYS NZ  HZ3  sing N N 266 
LYS OXT HXT  sing N N 267 
MET N   CA   sing N N 268 
MET N   H    sing N N 269 
MET N   H2   sing N N 270 
MET CA  C    sing N N 271 
MET CA  CB   sing N N 272 
MET CA  HA   sing N N 273 
MET C   O    doub N N 274 
MET C   OXT  sing N N 275 
MET CB  CG   sing N N 276 
MET CB  HB2  sing N N 277 
MET CB  HB3  sing N N 278 
MET CG  SD   sing N N 279 
MET CG  HG2  sing N N 280 
MET CG  HG3  sing N N 281 
MET SD  CE   sing N N 282 
MET CE  HE1  sing N N 283 
MET CE  HE2  sing N N 284 
MET CE  HE3  sing N N 285 
MET OXT HXT  sing N N 286 
PHE N   CA   sing N N 287 
PHE N   H    sing N N 288 
PHE N   H2   sing N N 289 
PHE CA  C    sing N N 290 
PHE CA  CB   sing N N 291 
PHE CA  HA   sing N N 292 
PHE C   O    doub N N 293 
PHE C   OXT  sing N N 294 
PHE CB  CG   sing N N 295 
PHE CB  HB2  sing N N 296 
PHE CB  HB3  sing N N 297 
PHE CG  CD1  doub Y N 298 
PHE CG  CD2  sing Y N 299 
PHE CD1 CE1  sing Y N 300 
PHE CD1 HD1  sing N N 301 
PHE CD2 CE2  doub Y N 302 
PHE CD2 HD2  sing N N 303 
PHE CE1 CZ   doub Y N 304 
PHE CE1 HE1  sing N N 305 
PHE CE2 CZ   sing Y N 306 
PHE CE2 HE2  sing N N 307 
PHE CZ  HZ   sing N N 308 
PHE OXT HXT  sing N N 309 
PRO N   CA   sing N N 310 
PRO N   CD   sing N N 311 
PRO N   H    sing N N 312 
PRO CA  C    sing N N 313 
PRO CA  CB   sing N N 314 
PRO CA  HA   sing N N 315 
PRO C   O    doub N N 316 
PRO C   OXT  sing N N 317 
PRO CB  CG   sing N N 318 
PRO CB  HB2  sing N N 319 
PRO CB  HB3  sing N N 320 
PRO CG  CD   sing N N 321 
PRO CG  HG2  sing N N 322 
PRO CG  HG3  sing N N 323 
PRO CD  HD2  sing N N 324 
PRO CD  HD3  sing N N 325 
PRO OXT HXT  sing N N 326 
SER N   CA   sing N N 327 
SER N   H    sing N N 328 
SER N   H2   sing N N 329 
SER CA  C    sing N N 330 
SER CA  CB   sing N N 331 
SER CA  HA   sing N N 332 
SER C   O    doub N N 333 
SER C   OXT  sing N N 334 
SER CB  OG   sing N N 335 
SER CB  HB2  sing N N 336 
SER CB  HB3  sing N N 337 
SER OG  HG   sing N N 338 
SER OXT HXT  sing N N 339 
THR N   CA   sing N N 340 
THR N   H    sing N N 341 
THR N   H2   sing N N 342 
THR CA  C    sing N N 343 
THR CA  CB   sing N N 344 
THR CA  HA   sing N N 345 
THR C   O    doub N N 346 
THR C   OXT  sing N N 347 
THR CB  OG1  sing N N 348 
THR CB  CG2  sing N N 349 
THR CB  HB   sing N N 350 
THR OG1 HG1  sing N N 351 
THR CG2 HG21 sing N N 352 
THR CG2 HG22 sing N N 353 
THR CG2 HG23 sing N N 354 
THR OXT HXT  sing N N 355 
TRP N   CA   sing N N 356 
TRP N   H    sing N N 357 
TRP N   H2   sing N N 358 
TRP CA  C    sing N N 359 
TRP CA  CB   sing N N 360 
TRP CA  HA   sing N N 361 
TRP C   O    doub N N 362 
TRP C   OXT  sing N N 363 
TRP CB  CG   sing N N 364 
TRP CB  HB2  sing N N 365 
TRP CB  HB3  sing N N 366 
TRP CG  CD1  doub Y N 367 
TRP CG  CD2  sing Y N 368 
TRP CD1 NE1  sing Y N 369 
TRP CD1 HD1  sing N N 370 
TRP CD2 CE2  doub Y N 371 
TRP CD2 CE3  sing Y N 372 
TRP NE1 CE2  sing Y N 373 
TRP NE1 HE1  sing N N 374 
TRP CE2 CZ2  sing Y N 375 
TRP CE3 CZ3  doub Y N 376 
TRP CE3 HE3  sing N N 377 
TRP CZ2 CH2  doub Y N 378 
TRP CZ2 HZ2  sing N N 379 
TRP CZ3 CH2  sing Y N 380 
TRP CZ3 HZ3  sing N N 381 
TRP CH2 HH2  sing N N 382 
TRP OXT HXT  sing N N 383 
TYR N   CA   sing N N 384 
TYR N   H    sing N N 385 
TYR N   H2   sing N N 386 
TYR CA  C    sing N N 387 
TYR CA  CB   sing N N 388 
TYR CA  HA   sing N N 389 
TYR C   O    doub N N 390 
TYR C   OXT  sing N N 391 
TYR CB  CG   sing N N 392 
TYR CB  HB2  sing N N 393 
TYR CB  HB3  sing N N 394 
TYR CG  CD1  doub Y N 395 
TYR CG  CD2  sing Y N 396 
TYR CD1 CE1  sing Y N 397 
TYR CD1 HD1  sing N N 398 
TYR CD2 CE2  doub Y N 399 
TYR CD2 HD2  sing N N 400 
TYR CE1 CZ   doub Y N 401 
TYR CE1 HE1  sing N N 402 
TYR CE2 CZ   sing Y N 403 
TYR CE2 HE2  sing N N 404 
TYR CZ  OH   sing N N 405 
TYR OH  HH   sing N N 406 
TYR OXT HXT  sing N N 407 
VAL N   CA   sing N N 408 
VAL N   H    sing N N 409 
VAL N   H2   sing N N 410 
VAL CA  C    sing N N 411 
VAL CA  CB   sing N N 412 
VAL CA  HA   sing N N 413 
VAL C   O    doub N N 414 
VAL C   OXT  sing N N 415 
VAL CB  CG1  sing N N 416 
VAL CB  CG2  sing N N 417 
VAL CB  HB   sing N N 418 
VAL CG1 HG11 sing N N 419 
VAL CG1 HG12 sing N N 420 
VAL CG1 HG13 sing N N 421 
VAL CG2 HG21 sing N N 422 
VAL CG2 HG22 sing N N 423 
VAL CG2 HG23 sing N N 424 
VAL OXT HXT  sing N N 425 
# 
_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                    7EE8 
_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]   0.014755 
_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]   0.014675 
_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]   0.011606 
_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   ? -30.570 -19.082 12.020  1.00 14.73 ? 1   PRO A N   1 
ATOM   2    C  CA  . PRO A 1 1   ? -29.427 -18.387 11.424  1.00 14.88 ? 1   PRO A CA  1 
ATOM   3    C  C   . PRO A 1 1   ? -29.875 -17.139 10.710  1.00 14.84 ? 1   PRO A C   1 
ATOM   4    O  O   . PRO A 1 1   ? -31.071 -16.953 10.491  1.00 14.13 ? 1   PRO A O   1 
ATOM   5    C  CB  . PRO A 1 1   ? -28.893 -19.391 10.388  1.00 15.69 ? 1   PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 1   ? -29.264 -20.695 10.927  1.00 15.36 ? 1   PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 1   ? -30.600 -20.506 11.636  1.00 14.69 ? 1   PRO A CD  1 
ATOM   8    N  N   . MET A 1 2   ? -28.913 -16.294 10.365  1.00 13.92 ? 2   MET A N   1 
ATOM   9    C  CA  . MET A 1 2   ? -29.174 -15.034 9.681   1.00 14.98 ? 2   MET A CA  1 
ATOM   10   C  C   . MET A 1 2   ? -28.184 -14.866 8.545   1.00 13.57 ? 2   MET A C   1 
ATOM   11   O  O   . MET A 1 2   ? -26.981 -15.020 8.754   1.00 13.58 ? 2   MET A O   1 
ATOM   12   C  CB  . MET A 1 2   ? -28.944 -13.888 10.670  1.00 19.55 ? 2   MET A CB  1 
ATOM   13   C  CG  . MET A 1 2   ? -29.181 -12.502 10.141  1.00 24.22 ? 2   MET A CG  1 
ATOM   14   S  SD  . MET A 1 2   ? -28.829 -11.283 11.440  1.00 28.14 ? 2   MET A SD  1 
ATOM   15   C  CE  . MET A 1 2   ? -27.057 -11.333 11.554  1.00 28.73 ? 2   MET A CE  1 
ATOM   16   N  N   . PHE A 1 3   ? -28.682 -14.528 7.353   1.00 12.46 ? 3   PHE A N   1 
ATOM   17   C  CA  . PHE A 1 3   ? -27.823 -14.270 6.199   1.00 12.21 ? 3   PHE A CA  1 
ATOM   18   C  C   . PHE A 1 3   ? -28.118 -12.882 5.657   1.00 12.24 ? 3   PHE A C   1 
ATOM   19   O  O   . PHE A 1 3   ? -29.277 -12.549 5.385   1.00 12.75 ? 3   PHE A O   1 
ATOM   20   C  CB  . PHE A 1 3   ? -27.998 -15.329 5.103   1.00 13.09 ? 3   PHE A CB  1 
ATOM   21   C  CG  . PHE A 1 3   ? -27.105 -15.123 3.906   1.00 14.36 ? 3   PHE A CG  1 
ATOM   22   C  CD1 . PHE A 1 3   ? -25.729 -15.214 4.014   1.00 14.95 ? 3   PHE A CD1 1 
ATOM   23   C  CD2 . PHE A 1 3   ? -27.648 -14.848 2.663   1.00 15.44 ? 3   PHE A CD2 1 
ATOM   24   C  CE1 . PHE A 1 3   ? -24.903 -15.009 2.907   1.00 16.45 ? 3   PHE A CE1 1 
ATOM   25   C  CE2 . PHE A 1 3   ? -26.832 -14.689 1.557   1.00 16.70 ? 3   PHE A CE2 1 
ATOM   26   C  CZ  . PHE A 1 3   ? -25.455 -14.751 1.691   1.00 17.46 ? 3   PHE A CZ  1 
ATOM   27   N  N   . ILE A 1 4   ? -27.068 -12.077 5.509   1.00 11.31 ? 4   ILE A N   1 
ATOM   28   C  CA  . ILE A 1 4   ? -27.192 -10.709 5.022   1.00 12.00 ? 4   ILE A CA  1 
ATOM   29   C  C   . ILE A 1 4   ? -26.298 -10.554 3.794   1.00 12.15 ? 4   ILE A C   1 
ATOM   30   O  O   . ILE A 1 4   ? -25.144 -11.001 3.801   1.00 11.87 ? 4   ILE A O   1 
ATOM   31   C  CB  . ILE A 1 4   ? -26.781 -9.694  6.098   1.00 13.60 ? 4   ILE A CB  1 
ATOM   32   C  CG1 . ILE A 1 4   ? -27.488 -9.940  7.443   1.00 15.72 ? 4   ILE A CG1 1 
ATOM   33   C  CG2 . ILE A 1 4   ? -27.065 -8.287  5.614   1.00 14.64 ? 4   ILE A CG2 1 
ATOM   34   C  CD1 . ILE A 1 4   ? -26.780 -9.269  8.636   1.00 18.06 ? 4   ILE A CD1 1 
ATOM   35   N  N   A VAL A 1 5   ? -26.815 -9.931  2.739   0.39 12.24 ? 5   VAL A N   1 
ATOM   36   N  N   B VAL A 1 5   ? -26.838 -9.936  2.745   0.61 12.05 ? 5   VAL A N   1 
ATOM   37   C  CA  A VAL A 1 5   ? -25.997 -9.635  1.568   0.39 13.19 ? 5   VAL A CA  1 
ATOM   38   C  CA  B VAL A 1 5   ? -26.097 -9.602  1.534   0.61 13.00 ? 5   VAL A CA  1 
ATOM   39   C  C   A VAL A 1 5   ? -26.151 -8.162  1.230   0.39 11.84 ? 5   VAL A C   1 
ATOM   40   C  C   B VAL A 1 5   ? -26.193 -8.097  1.371   0.61 11.59 ? 5   VAL A C   1 
ATOM   41   O  O   A VAL A 1 5   ? -27.253 -7.703  0.913   0.39 12.16 ? 5   VAL A O   1 
ATOM   42   O  O   B VAL A 1 5   ? -27.300 -7.552  1.297   0.61 12.49 ? 5   VAL A O   1 
ATOM   43   C  CB  A VAL A 1 5   ? -26.308 -10.529 0.350   0.39 15.84 ? 5   VAL A CB  1 
ATOM   44   C  CB  B VAL A 1 5   ? -26.683 -10.287 0.286   0.61 15.65 ? 5   VAL A CB  1 
ATOM   45   C  CG1 A VAL A 1 5   ? -27.797 -10.697 0.146   0.39 17.33 ? 5   VAL A CG1 1 
ATOM   46   C  CG1 B VAL A 1 5   ? -25.994 -9.795  -0.996  0.61 17.52 ? 5   VAL A CG1 1 
ATOM   47   C  CG2 A VAL A 1 5   ? -25.651 -9.976  -0.920  0.39 16.70 ? 5   VAL A CG2 1 
ATOM   48   C  CG2 B VAL A 1 5   ? -26.569 -11.777 0.389   0.61 16.35 ? 5   VAL A CG2 1 
ATOM   49   N  N   . ASN A 1 6   ? -25.049 -7.429  1.292   1.00 10.96 ? 6   ASN A N   1 
ATOM   50   C  CA  . ASN A 1 6   ? -25.002 -6.030  0.868   1.00 11.77 ? 6   ASN A CA  1 
ATOM   51   C  C   . ASN A 1 6   ? -24.370 -5.965  -0.515  1.00 11.74 ? 6   ASN A C   1 
ATOM   52   O  O   . ASN A 1 6   ? -23.293 -6.533  -0.729  1.00 11.92 ? 6   ASN A O   1 
ATOM   53   C  CB  . ASN A 1 6   ? -24.154 -5.191  1.823   1.00 14.92 ? 6   ASN A CB  1 
ATOM   54   C  CG  . ASN A 1 6   ? -24.851 -4.932  3.128   1.00 20.45 ? 6   ASN A CG  1 
ATOM   55   O  OD1 . ASN A 1 6   ? -25.561 -3.936  3.281   1.00 22.38 ? 6   ASN A OD1 1 
ATOM   56   N  ND2 . ASN A 1 6   ? -24.669 -5.841  4.074   1.00 22.69 ? 6   ASN A ND2 1 
ATOM   57   N  N   . THR A 1 7   ? -25.023 -5.273  -1.454  1.00 11.64 ? 7   THR A N   1 
ATOM   58   C  CA  . THR A 1 7   ? -24.541 -5.298  -2.829  1.00 12.83 ? 7   THR A CA  1 
ATOM   59   C  C   . THR A 1 7   ? -24.837 -3.971  -3.504  1.00 12.87 ? 7   THR A C   1 
ATOM   60   O  O   . THR A 1 7   ? -25.795 -3.264  -3.156  1.00 12.38 ? 7   THR A O   1 
ATOM   61   C  CB  . THR A 1 7   ? -25.133 -6.478  -3.640  1.00 12.91 ? 7   THR A CB  1 
ATOM   62   O  OG1 . THR A 1 7   ? -24.663 -6.447  -4.996  1.00 12.37 ? 7   THR A OG1 1 
ATOM   63   C  CG2 . THR A 1 7   ? -26.654 -6.457  -3.683  1.00 13.45 ? 7   THR A CG2 1 
ATOM   64   N  N   . ASN A 1 8   ? -24.008 -3.651  -4.490  1.00 12.56 ? 8   ASN A N   1 
ATOM   65   C  CA  . ASN A 1 8   ? -24.249 -2.496  -5.336  1.00 13.73 ? 8   ASN A CA  1 
ATOM   66   C  C   . ASN A 1 8   ? -25.182 -2.784  -6.509  1.00 14.86 ? 8   ASN A C   1 
ATOM   67   O  O   . ASN A 1 8   ? -25.553 -1.846  -7.218  1.00 16.38 ? 8   ASN A O   1 
ATOM   68   C  CB  . ASN A 1 8   ? -22.926 -1.887  -5.830  1.00 13.80 ? 8   ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 8   ? -22.036 -2.884  -6.543  1.00 15.17 ? 8   ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 8   ? -22.256 -4.080  -6.503  1.00 14.76 ? 8   ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 8   ? -21.022 -2.373  -7.209  1.00 16.03 ? 8   ASN A ND2 1 
ATOM   72   N  N   . VAL A 1 9   ? -25.579 -4.043  -6.716  1.00 13.47 ? 9   VAL A N   1 
ATOM   73   C  CA  . VAL A 1 9   ? -26.546 -4.369  -7.764  1.00 14.71 ? 9   VAL A CA  1 
ATOM   74   C  C   . VAL A 1 9   ? -27.851 -3.648  -7.456  1.00 15.41 ? 9   VAL A C   1 
ATOM   75   O  O   . VAL A 1 9   ? -28.276 -3.592  -6.282  1.00 16.12 ? 9   VAL A O   1 
ATOM   76   C  CB  . VAL A 1 9   ? -26.743 -5.901  -7.837  1.00 15.20 ? 9   VAL A CB  1 
ATOM   77   C  CG1 . VAL A 1 9   ? -27.942 -6.305  -8.718  1.00 17.45 ? 9   VAL A CG1 1 
ATOM   78   C  CG2 . VAL A 1 9   ? -25.453 -6.568  -8.320  1.00 15.68 ? 9   VAL A CG2 1 
ATOM   79   N  N   . PRO A 1 10  ? -28.516 -3.054  -8.430  1.00 16.90 ? 10  PRO A N   1 
ATOM   80   C  CA  . PRO A 1 10  ? -29.748 -2.313  -8.133  1.00 17.79 ? 10  PRO A CA  1 
ATOM   81   C  C   . PRO A 1 10  ? -30.922 -3.224  -7.790  1.00 17.84 ? 10  PRO A C   1 
ATOM   82   O  O   . PRO A 1 10  ? -30.969 -4.395  -8.170  1.00 17.74 ? 10  PRO A O   1 
ATOM   83   C  CB  . PRO A 1 10  ? -30.016 -1.528  -9.421  1.00 18.88 ? 10  PRO A CB  1 
ATOM   84   C  CG  . PRO A 1 10  ? -29.263 -2.249  -10.476 1.00 19.58 ? 10  PRO A CG  1 
ATOM   85   C  CD  . PRO A 1 10  ? -28.114 -2.942  -9.841  1.00 17.99 ? 10  PRO A CD  1 
ATOM   86   N  N   . ARG A 1 11  ? -31.897 -2.645  -7.068  1.00 18.48 ? 11  ARG A N   1 
ATOM   87   C  CA  . ARG A 1 11  ? -33.059 -3.404  -6.602  1.00 19.80 ? 11  ARG A CA  1 
ATOM   88   C  C   . ARG A 1 11  ? -33.792 -4.089  -7.749  1.00 21.07 ? 11  ARG A C   1 
ATOM   89   O  O   . ARG A 1 11  ? -34.243 -5.233  -7.611  1.00 20.77 ? 11  ARG A O   1 
ATOM   90   C  CB  . ARG A 1 11  ? -34.029 -2.485  -5.845  1.00 21.35 ? 11  ARG A CB  1 
ATOM   91   C  CG  . ARG A 1 11  ? -35.381 -3.159  -5.485  1.00 23.82 ? 11  ARG A CG  1 
ATOM   92   C  CD  . ARG A 1 11  ? -35.219 -4.392  -4.566  1.00 26.56 ? 11  ARG A CD  1 
ATOM   93   N  NE  . ARG A 1 11  ? -36.490 -5.029  -4.194  1.00 29.50 ? 11  ARG A NE  1 
ATOM   94   C  CZ  . ARG A 1 11  ? -36.955 -6.142  -4.760  1.00 31.21 ? 11  ARG A CZ  1 
ATOM   95   N  NH1 . ARG A 1 11  ? -36.247 -6.740  -5.708  1.00 32.23 ? 11  ARG A NH1 1 
ATOM   96   N  NH2 . ARG A 1 11  ? -38.118 -6.668  -4.375  1.00 31.42 ? 11  ARG A NH2 1 
ATOM   97   N  N   . ALA A 1 12  ? -33.906 -3.411  -8.894  1.00 21.76 ? 12  ALA A N   1 
ATOM   98   C  CA  . ALA A 1 12  ? -34.633 -3.962  -10.033 1.00 23.12 ? 12  ALA A CA  1 
ATOM   99   C  C   . ALA A 1 12  ? -33.990 -5.229  -10.567 1.00 23.37 ? 12  ALA A C   1 
ATOM   100  O  O   . ALA A 1 12  ? -34.648 -5.997  -11.283 1.00 24.84 ? 12  ALA A O   1 
ATOM   101  C  CB  . ALA A 1 12  ? -34.736 -2.921  -11.152 1.00 23.41 ? 12  ALA A CB  1 
ATOM   102  N  N   . SER A 1 13  ? -32.719 -5.460  -10.244 1.00 22.23 ? 13  SER A N   1 
ATOM   103  C  CA  . SER A 1 13  ? -31.996 -6.638  -10.692 1.00 22.34 ? 13  SER A CA  1 
ATOM   104  C  C   . SER A 1 13  ? -32.004 -7.758  -9.665  1.00 21.82 ? 13  SER A C   1 
ATOM   105  O  O   . SER A 1 13  ? -31.385 -8.802  -9.900  1.00 22.80 ? 13  SER A O   1 
ATOM   106  C  CB  . SER A 1 13  ? -30.556 -6.265  -11.075 1.00 23.71 ? 13  SER A CB  1 
ATOM   107  O  OG  . SER A 1 13  ? -30.526 -5.451  -12.242 1.00 25.58 ? 13  SER A OG  1 
ATOM   108  N  N   . VAL A 1 14  ? -32.671 -7.575  -8.528  1.00 19.97 ? 14  VAL A N   1 
ATOM   109  C  CA  . VAL A 1 14  ? -32.872 -8.648  -7.563  1.00 19.15 ? 14  VAL A CA  1 
ATOM   110  C  C   . VAL A 1 14  ? -34.140 -9.401  -7.975  1.00 19.25 ? 14  VAL A C   1 
ATOM   111  O  O   . VAL A 1 14  ? -35.232 -8.809  -7.936  1.00 19.62 ? 14  VAL A O   1 
ATOM   112  C  CB  . VAL A 1 14  ? -32.935 -8.109  -6.127  1.00 18.88 ? 14  VAL A CB  1 
ATOM   113  C  CG1 . VAL A 1 14  ? -33.162 -9.243  -5.136  1.00 18.65 ? 14  VAL A CG1 1 
ATOM   114  C  CG2 . VAL A 1 14  ? -31.643 -7.356  -5.805  1.00 19.77 ? 14  VAL A CG2 1 
ATOM   115  N  N   . PRO A 1 15  ? -34.047 -10.660 -8.394  1.00 19.12 ? 15  PRO A N   1 
ATOM   116  C  CA  . PRO A 1 15  ? -35.213 -11.343 -8.979  1.00 18.33 ? 15  PRO A CA  1 
ATOM   117  C  C   . PRO A 1 15  ? -36.267 -11.689 -7.941  1.00 17.12 ? 15  PRO A C   1 
ATOM   118  O  O   . PRO A 1 15  ? -35.982 -11.808 -6.750  1.00 17.37 ? 15  PRO A O   1 
ATOM   119  C  CB  . PRO A 1 15  ? -34.617 -12.620 -9.576  1.00 19.29 ? 15  PRO A CB  1 
ATOM   120  C  CG  . PRO A 1 15  ? -33.383 -12.847 -8.782  1.00 19.78 ? 15  PRO A CG  1 
ATOM   121  C  CD  . PRO A 1 15  ? -32.849 -11.509 -8.380  1.00 19.33 ? 15  PRO A CD  1 
ATOM   122  N  N   . ASP A 1 16  ? -37.503 -11.875 -8.421  1.00 16.74 ? 16  ASP A N   1 
ATOM   123  C  CA  . ASP A 1 16  ? -38.594 -12.315 -7.554  1.00 17.10 ? 16  ASP A CA  1 
ATOM   124  C  C   . ASP A 1 16  ? -38.216 -13.611 -6.855  1.00 17.41 ? 16  ASP A C   1 
ATOM   125  O  O   . ASP A 1 16  ? -37.546 -14.477 -7.424  1.00 18.48 ? 16  ASP A O   1 
ATOM   126  C  CB  . ASP A 1 16  ? -39.888 -12.560 -8.354  1.00 18.18 ? 16  ASP A CB  1 
ATOM   127  C  CG  . ASP A 1 16  ? -40.476 -11.302 -8.938  1.00 19.01 ? 16  ASP A CG  1 
ATOM   128  O  OD1 . ASP A 1 16  ? -39.998 -10.181 -8.629  1.00 20.42 ? 16  ASP A OD1 1 
ATOM   129  O  OD2 . ASP A 1 16  ? -41.471 -11.433 -9.682  1.00 19.42 ? 16  ASP A OD2 1 
ATOM   130  N  N   . GLY A 1 17  ? -38.627 -13.730 -5.598  1.00 16.31 ? 17  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 17  ? -38.391 -14.966 -4.868  1.00 15.54 ? 17  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 17  ? -36.987 -15.161 -4.345  1.00 15.39 ? 17  GLY A C   1 
ATOM   133  O  O   . GLY A 1 17  ? -36.708 -16.216 -3.767  1.00 16.15 ? 17  GLY A O   1 
ATOM   134  N  N   . PHE A 1 18  ? -36.111 -14.169 -4.485  1.00 15.20 ? 18  PHE A N   1 
ATOM   135  C  CA  . PHE A 1 18  ? -34.720 -14.349 -4.070  1.00 15.39 ? 18  PHE A CA  1 
ATOM   136  C  C   . PHE A 1 18  ? -34.594 -14.604 -2.570  1.00 15.45 ? 18  PHE A C   1 
ATOM   137  O  O   . PHE A 1 18  ? -33.798 -15.453 -2.141  1.00 15.80 ? 18  PHE A O   1 
ATOM   138  C  CB  . PHE A 1 18  ? -33.890 -13.139 -4.495  1.00 16.01 ? 18  PHE A CB  1 
ATOM   139  C  CG  . PHE A 1 18  ? -32.407 -13.312 -4.286  1.00 16.54 ? 18  PHE A CG  1 
ATOM   140  C  CD1 . PHE A 1 18  ? -31.730 -14.398 -4.840  1.00 17.99 ? 18  PHE A CD1 1 
ATOM   141  C  CD2 . PHE A 1 18  ? -31.691 -12.385 -3.544  1.00 17.73 ? 18  PHE A CD2 1 
ATOM   142  C  CE1 . PHE A 1 18  ? -30.367 -14.557 -4.651  1.00 18.89 ? 18  PHE A CE1 1 
ATOM   143  C  CE2 . PHE A 1 18  ? -30.328 -12.535 -3.354  1.00 17.86 ? 18  PHE A CE2 1 
ATOM   144  C  CZ  . PHE A 1 18  ? -29.658 -13.620 -3.927  1.00 18.51 ? 18  PHE A CZ  1 
ATOM   145  N  N   . LEU A 1 19  ? -35.379 -13.897 -1.757  1.00 15.19 ? 19  LEU A N   1 
ATOM   146  C  CA  . LEU A 1 19  ? -35.344 -14.141 -0.316  1.00 15.35 ? 19  LEU A CA  1 
ATOM   147  C  C   . LEU A 1 19  ? -35.785 -15.560 0.009   1.00 15.00 ? 19  LEU A C   1 
ATOM   148  O  O   . LEU A 1 19  ? -35.201 -16.212 0.883   1.00 15.21 ? 19  LEU A O   1 
ATOM   149  C  CB  . LEU A 1 19  ? -36.240 -13.153 0.427   1.00 16.83 ? 19  LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 19  ? -35.863 -11.677 0.432   1.00 18.31 ? 19  LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 19  ? -36.876 -10.874 1.251   1.00 19.09 ? 19  LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 19  ? -34.471 -11.456 0.985   1.00 19.72 ? 19  LEU A CD2 1 
ATOM   153  N  N   . SER A 1 20  ? -36.846 -16.041 -0.652  1.00 14.98 ? 20  SER A N   1 
ATOM   154  C  CA  . SER A 1 20  ? -37.294 -17.413 -0.416  1.00 15.37 ? 20  SER A CA  1 
ATOM   155  C  C   . SER A 1 20  ? -36.244 -18.420 -0.865  1.00 14.91 ? 20  SER A C   1 
ATOM   156  O  O   . SER A 1 20  ? -35.989 -19.424 -0.179  1.00 15.85 ? 20  SER A O   1 
ATOM   157  C  CB  . SER A 1 20  ? -38.634 -17.688 -1.107  1.00 15.76 ? 20  SER A CB  1 
ATOM   158  O  OG  . SER A 1 20  ? -39.079 -19.006 -0.806  1.00 17.54 ? 20  SER A OG  1 
ATOM   159  N  N   . GLU A 1 21  ? -35.618 -18.162 -2.010  1.00 14.78 ? 21  GLU A N   1 
ATOM   160  C  CA  . GLU A 1 21  ? -34.598 -19.062 -2.509  1.00 14.22 ? 21  GLU A CA  1 
ATOM   161  C  C   . GLU A 1 21  ? -33.445 -19.158 -1.521  1.00 13.93 ? 21  GLU A C   1 
ATOM   162  O  O   . GLU A 1 21  ? -32.984 -20.256 -1.193  1.00 14.24 ? 21  GLU A O   1 
ATOM   163  C  CB  . GLU A 1 21  ? -34.119 -18.560 -3.861  1.00 15.09 ? 21  GLU A CB  1 
ATOM   164  C  CG  . GLU A 1 21  ? -33.234 -19.540 -4.608  1.00 17.30 ? 21  GLU A CG  1 
ATOM   165  C  CD  . GLU A 1 21  ? -32.953 -19.097 -6.030  1.00 18.94 ? 21  GLU A CD  1 
ATOM   166  O  OE1 . GLU A 1 21  ? -33.344 -17.966 -6.417  1.00 20.30 ? 21  GLU A OE1 1 
ATOM   167  O  OE2 . GLU A 1 21  ? -32.326 -19.888 -6.757  1.00 20.66 ? 21  GLU A OE2 1 
ATOM   168  N  N   . LEU A 1 22  ? -32.977 -18.011 -1.017  1.00 13.64 ? 22  LEU A N   1 
ATOM   169  C  CA  . LEU A 1 22  ? -31.933 -18.036 0.003   1.00 13.83 ? 22  LEU A CA  1 
ATOM   170  C  C   . LEU A 1 22  ? -32.382 -18.807 1.237   1.00 14.20 ? 22  LEU A C   1 
ATOM   171  O  O   . LEU A 1 22  ? -31.616 -19.602 1.782   1.00 14.85 ? 22  LEU A O   1 
ATOM   172  C  CB  . LEU A 1 22  ? -31.542 -16.610 0.386   1.00 14.39 ? 22  LEU A CB  1 
ATOM   173  C  CG  . LEU A 1 22  ? -30.762 -15.891 -0.691  1.00 14.88 ? 22  LEU A CG  1 
ATOM   174  C  CD1 . LEU A 1 22  ? -30.648 -14.445 -0.259  1.00 15.40 ? 22  LEU A CD1 1 
ATOM   175  C  CD2 . LEU A 1 22  ? -29.393 -16.533 -0.914  1.00 16.40 ? 22  LEU A CD2 1 
ATOM   176  N  N   . THR A 1 23  ? -33.621 -18.588 1.683   1.00 13.92 ? 23  THR A N   1 
ATOM   177  C  CA  . THR A 1 23  ? -34.129 -19.244 2.888   1.00 14.36 ? 23  THR A CA  1 
ATOM   178  C  C   . THR A 1 23  ? -34.126 -20.749 2.713   1.00 15.57 ? 23  THR A C   1 
ATOM   179  O  O   . THR A 1 23  ? -33.672 -21.496 3.592   1.00 16.06 ? 23  THR A O   1 
ATOM   180  C  CB  . THR A 1 23  ? -35.555 -18.775 3.189   1.00 15.32 ? 23  THR A CB  1 
ATOM   181  O  OG1 . THR A 1 23  ? -35.563 -17.366 3.420   1.00 14.60 ? 23  THR A OG1 1 
ATOM   182  C  CG2 . THR A 1 23  ? -36.115 -19.485 4.407   1.00 16.68 ? 23  THR A CG2 1 
ATOM   183  N  N   . GLN A 1 24  ? -34.640 -21.213 1.572   1.00 16.89 ? 24  GLN A N   1 
ATOM   184  C  CA  . GLN A 1 24  ? -34.712 -22.643 1.332   1.00 18.62 ? 24  GLN A CA  1 
ATOM   185  C  C   . GLN A 1 24  ? -33.324 -23.248 1.239   1.00 17.41 ? 24  GLN A C   1 
ATOM   186  O  O   . GLN A 1 24  ? -33.065 -24.301 1.836   1.00 17.11 ? 24  GLN A O   1 
ATOM   187  C  CB  . GLN A 1 24  ? -35.465 -22.900 0.033   1.00 21.79 ? 24  GLN A CB  1 
ATOM   188  C  CG  . GLN A 1 24  ? -36.915 -22.542 0.090   1.00 24.93 ? 24  GLN A CG  1 
ATOM   189  C  CD  . GLN A 1 24  ? -37.594 -22.730 -1.250  1.00 26.84 ? 24  GLN A CD  1 
ATOM   190  O  OE1 . GLN A 1 24  ? -36.943 -22.705 -2.298  1.00 26.69 ? 24  GLN A OE1 1 
ATOM   191  N  NE2 . GLN A 1 24  ? -38.899 -22.903 -1.223  1.00 27.40 ? 24  GLN A NE2 1 
ATOM   192  N  N   . GLN A 1 25  ? -32.424 -22.612 0.474   1.00 16.44 ? 25  GLN A N   1 
ATOM   193  C  CA  . GLN A 1 25  ? -31.090 -23.187 0.296   1.00 16.86 ? 25  GLN A CA  1 
ATOM   194  C  C   . GLN A 1 25  ? -30.311 -23.199 1.604   1.00 16.26 ? 25  GLN A C   1 
ATOM   195  O  O   . GLN A 1 25  ? -29.569 -24.149 1.885   1.00 15.96 ? 25  GLN A O   1 
ATOM   196  C  CB  . GLN A 1 25  ? -30.321 -22.452 -0.803  1.00 18.54 ? 25  GLN A CB  1 
ATOM   197  C  CG  . GLN A 1 25  ? -30.888 -22.598 -2.233  1.00 20.49 ? 25  GLN A CG  1 
ATOM   198  C  CD  . GLN A 1 25  ? -30.844 -24.023 -2.762  1.00 23.11 ? 25  GLN A CD  1 
ATOM   199  O  OE1 . GLN A 1 25  ? -29.998 -24.831 -2.370  1.00 24.79 ? 25  GLN A OE1 1 
ATOM   200  N  NE2 . GLN A 1 25  ? -31.735 -24.321 -3.688  1.00 23.45 ? 25  GLN A NE2 1 
ATOM   201  N  N   . LEU A 1 26  ? -30.474 -22.160 2.416   1.00 15.67 ? 26  LEU A N   1 
ATOM   202  C  CA  . LEU A 1 26  ? -29.774 -22.101 3.697   1.00 14.87 ? 26  LEU A CA  1 
ATOM   203  C  C   . LEU A 1 26  ? -30.345 -23.096 4.695   1.00 16.30 ? 26  LEU A C   1 
ATOM   204  O  O   . LEU A 1 26  ? -29.603 -23.647 5.517   1.00 16.79 ? 26  LEU A O   1 
ATOM   205  C  CB  . LEU A 1 26  ? -29.861 -20.695 4.271   1.00 14.60 ? 26  LEU A CB  1 
ATOM   206  C  CG  . LEU A 1 26  ? -28.919 -19.761 3.529   1.00 15.86 ? 26  LEU A CG  1 
ATOM   207  C  CD1 . LEU A 1 26  ? -29.309 -18.337 3.866   1.00 16.73 ? 26  LEU A CD1 1 
ATOM   208  C  CD2 . LEU A 1 26  ? -27.463 -20.047 3.883   1.00 17.08 ? 26  LEU A CD2 1 
ATOM   209  N  N   . ALA A 1 27  ? -31.660 -23.318 4.668   1.00 17.41 ? 27  ALA A N   1 
ATOM   210  C  CA  . ALA A 1 27  ? -32.219 -24.324 5.563   1.00 18.11 ? 27  ALA A CA  1 
ATOM   211  C  C   . ALA A 1 27  ? -31.589 -25.683 5.289   1.00 18.95 ? 27  ALA A C   1 
ATOM   212  O  O   . ALA A 1 27  ? -31.203 -26.406 6.213   1.00 19.70 ? 27  ALA A O   1 
ATOM   213  C  CB  . ALA A 1 27  ? -33.737 -24.384 5.434   1.00 18.01 ? 27  ALA A CB  1 
ATOM   214  N  N   . GLN A 1 28  ? -31.426 -26.022 4.016   1.00 20.24 ? 28  GLN A N   1 
ATOM   215  C  CA  . GLN A 1 28  ? -30.852 -27.310 3.666   1.00 21.55 ? 28  GLN A CA  1 
ATOM   216  C  C   . GLN A 1 28  ? -29.367 -27.348 4.006   1.00 20.59 ? 28  GLN A C   1 
ATOM   217  O  O   . GLN A 1 28  ? -28.871 -28.346 4.548   1.00 21.32 ? 28  GLN A O   1 
ATOM   218  C  CB  . GLN A 1 28  ? -31.083 -27.506 2.176   1.00 23.97 ? 28  GLN A CB  1 
ATOM   219  C  CG  . GLN A 1 28  ? -32.558 -27.334 1.856   1.00 26.83 ? 28  GLN A CG  1 
ATOM   220  C  CD  . GLN A 1 28  ? -32.906 -27.659 0.443   1.00 29.40 ? 28  GLN A CD  1 
ATOM   221  O  OE1 . GLN A 1 28  ? -32.919 -26.766 -0.415  1.00 31.17 ? 28  GLN A OE1 1 
ATOM   222  N  NE2 . GLN A 1 28  ? -33.294 -28.903 0.200   1.00 28.64 ? 28  GLN A NE2 1 
ATOM   223  N  N   . ALA A 1 29  ? -28.648 -26.254 3.738   1.00 18.98 ? 29  ALA A N   1 
ATOM   224  C  CA  . ALA A 1 29  ? -27.205 -26.255 3.962   1.00 19.26 ? 29  ALA A CA  1 
ATOM   225  C  C   . ALA A 1 29  ? -26.866 -26.298 5.442   1.00 18.83 ? 29  ALA A C   1 
ATOM   226  O  O   . ALA A 1 29  ? -25.962 -27.033 5.851   1.00 19.12 ? 29  ALA A O   1 
ATOM   227  C  CB  . ALA A 1 29  ? -26.571 -25.034 3.316   1.00 19.74 ? 29  ALA A CB  1 
ATOM   228  N  N   . THR A 1 30  ? -27.563 -25.511 6.256   1.00 18.43 ? 30  THR A N   1 
ATOM   229  C  CA  . THR A 1 30  ? -27.259 -25.497 7.682   1.00 18.14 ? 30  THR A CA  1 
ATOM   230  C  C   . THR A 1 30  ? -27.921 -26.632 8.435   1.00 18.11 ? 30  THR A C   1 
ATOM   231  O  O   . THR A 1 30  ? -27.560 -26.886 9.599   1.00 18.43 ? 30  THR A O   1 
ATOM   232  C  CB  . THR A 1 30  ? -27.692 -24.181 8.333   1.00 18.84 ? 30  THR A CB  1 
ATOM   233  O  OG1 . THR A 1 30  ? -29.116 -24.058 8.244   1.00 17.80 ? 30  THR A OG1 1 
ATOM   234  C  CG2 . THR A 1 30  ? -26.995 -22.988 7.683   1.00 19.33 ? 30  THR A CG2 1 
ATOM   235  N  N   . GLY A 1 31  ? -28.896 -27.295 7.829   1.00 18.13 ? 31  GLY A N   1 
ATOM   236  C  CA  . GLY A 1 31  ? -29.635 -28.284 8.574   1.00 17.93 ? 31  GLY A CA  1 
ATOM   237  C  C   . GLY A 1 31  ? -30.667 -27.717 9.519   1.00 19.19 ? 31  GLY A C   1 
ATOM   238  O  O   . GLY A 1 31  ? -31.357 -28.496 10.183  1.00 20.94 ? 31  GLY A O   1 
ATOM   239  N  N   . LYS A 1 32  ? -30.806 -26.385 9.596   1.00 18.42 ? 32  LYS A N   1 
ATOM   240  C  CA  . LYS A 1 32  ? -31.749 -25.765 10.518  1.00 17.89 ? 32  LYS A CA  1 
ATOM   241  C  C   . LYS A 1 32  ? -33.138 -25.687 9.884   1.00 16.84 ? 32  LYS A C   1 
ATOM   242  O  O   . LYS A 1 32  ? -33.272 -25.557 8.656   1.00 16.20 ? 32  LYS A O   1 
ATOM   243  C  CB  . LYS A 1 32  ? -31.289 -24.341 10.853  1.00 18.40 ? 32  LYS A CB  1 
ATOM   244  C  CG  . LYS A 1 32  ? -29.877 -24.234 11.429  1.00 19.51 ? 32  LYS A CG  1 
ATOM   245  C  CD  . LYS A 1 32  ? -29.847 -24.425 12.934  1.00 20.44 ? 32  LYS A CD  1 
ATOM   246  C  CE  . LYS A 1 32  ? -28.465 -24.126 13.501  1.00 21.13 ? 32  LYS A CE  1 
ATOM   247  N  NZ  . LYS A 1 32  ? -28.450 -24.256 14.985  1.00 20.94 ? 32  LYS A NZ  1 
ATOM   248  N  N   . PRO A 1 33  ? -34.198 -25.669 10.680  1.00 16.50 ? 33  PRO A N   1 
ATOM   249  C  CA  . PRO A 1 33  ? -35.548 -25.516 10.109  1.00 16.89 ? 33  PRO A CA  1 
ATOM   250  C  C   . PRO A 1 33  ? -35.677 -24.160 9.432   1.00 15.96 ? 33  PRO A C   1 
ATOM   251  O  O   . PRO A 1 33  ? -35.159 -23.156 9.935   1.00 15.44 ? 33  PRO A O   1 
ATOM   252  C  CB  . PRO A 1 33  ? -36.462 -25.607 11.336  1.00 18.10 ? 33  PRO A CB  1 
ATOM   253  C  CG  . PRO A 1 33  ? -35.611 -26.260 12.418  1.00 18.65 ? 33  PRO A CG  1 
ATOM   254  C  CD  . PRO A 1 33  ? -34.212 -25.794 12.146  1.00 17.72 ? 33  PRO A CD  1 
ATOM   255  N  N   . PRO A 1 34  ? -36.348 -24.087 8.277   1.00 15.69 ? 34  PRO A N   1 
ATOM   256  C  CA  . PRO A 1 34  ? -36.509 -22.783 7.600   1.00 15.55 ? 34  PRO A CA  1 
ATOM   257  C  C   . PRO A 1 34  ? -37.179 -21.728 8.464   1.00 15.15 ? 34  PRO A C   1 
ATOM   258  O  O   . PRO A 1 34  ? -36.906 -20.535 8.289   1.00 14.41 ? 34  PRO A O   1 
ATOM   259  C  CB  . PRO A 1 34  ? -37.324 -23.113 6.333   1.00 17.30 ? 34  PRO A CB  1 
ATOM   260  C  CG  . PRO A 1 34  ? -37.966 -24.441 6.607   1.00 17.78 ? 34  PRO A CG  1 
ATOM   261  C  CD  . PRO A 1 34  ? -37.026 -25.180 7.555   1.00 16.30 ? 34  PRO A CD  1 
ATOM   262  N  N   . GLN A 1 35  ? -38.036 -22.140 9.402   1.00 16.00 ? 35  GLN A N   1 
ATOM   263  C  CA  . GLN A 1 35  ? -38.658 -21.201 10.321  1.00 17.18 ? 35  GLN A CA  1 
ATOM   264  C  C   . GLN A 1 35  ? -37.635 -20.391 11.111  1.00 16.38 ? 35  GLN A C   1 
ATOM   265  O  O   . GLN A 1 35  ? -37.953 -19.290 11.569  1.00 17.65 ? 35  GLN A O   1 
ATOM   266  C  CB  . GLN A 1 35  ? -39.610 -21.943 11.281  1.00 19.09 ? 35  GLN A CB  1 
ATOM   267  C  CG  . GLN A 1 35  ? -40.864 -22.598 10.652  1.00 21.02 ? 35  GLN A CG  1 
ATOM   268  C  CD  . GLN A 1 35  ? -40.688 -24.001 10.012  1.00 21.60 ? 35  GLN A CD  1 
ATOM   269  O  OE1 . GLN A 1 35  ? -39.577 -24.550 9.899   1.00 20.31 ? 35  GLN A OE1 1 
ATOM   270  N  NE2 . GLN A 1 35  ? -41.819 -24.608 9.657   1.00 23.27 ? 35  GLN A NE2 1 
ATOM   271  N  N   . TYR A 1 36  ? -36.414 -20.892 11.265  1.00 15.11 ? 36  TYR A N   1 
ATOM   272  C  CA  . TYR A 1 36  ? -35.377 -20.218 12.031  1.00 14.75 ? 36  TYR A CA  1 
ATOM   273  C  C   . TYR A 1 36  ? -34.393 -19.432 11.161  1.00 13.48 ? 36  TYR A C   1 
ATOM   274  O  O   . TYR A 1 36  ? -33.483 -18.790 11.694  1.00 14.28 ? 36  TYR A O   1 
ATOM   275  C  CB  . TYR A 1 36  ? -34.619 -21.249 12.871  1.00 15.49 ? 36  TYR A CB  1 
ATOM   276  C  CG  . TYR A 1 36  ? -35.385 -21.775 14.063  1.00 17.16 ? 36  TYR A CG  1 
ATOM   277  C  CD1 . TYR A 1 36  ? -36.281 -22.829 13.940  1.00 18.20 ? 36  TYR A CD1 1 
ATOM   278  C  CD2 . TYR A 1 36  ? -35.209 -21.203 15.317  1.00 18.34 ? 36  TYR A CD2 1 
ATOM   279  C  CE1 . TYR A 1 36  ? -36.968 -23.310 15.026  1.00 19.25 ? 36  TYR A CE1 1 
ATOM   280  C  CE2 . TYR A 1 36  ? -35.898 -21.678 16.414  1.00 19.74 ? 36  TYR A CE2 1 
ATOM   281  C  CZ  . TYR A 1 36  ? -36.771 -22.739 16.262  1.00 20.43 ? 36  TYR A CZ  1 
ATOM   282  O  OH  . TYR A 1 36  ? -37.476 -23.242 17.324  1.00 22.76 ? 36  TYR A OH  1 
ATOM   283  N  N   . ILE A 1 37  ? -34.562 -19.433 9.841   1.00 12.41 ? 37  ILE A N   1 
ATOM   284  C  CA  . ILE A 1 37  ? -33.643 -18.756 8.931   1.00 12.49 ? 37  ILE A CA  1 
ATOM   285  C  C   . ILE A 1 37  ? -34.185 -17.371 8.626   1.00 12.24 ? 37  ILE A C   1 
ATOM   286  O  O   . ILE A 1 37  ? -35.321 -17.230 8.170   1.00 13.91 ? 37  ILE A O   1 
ATOM   287  C  CB  . ILE A 1 37  ? -33.500 -19.542 7.614   1.00 13.71 ? 37  ILE A CB  1 
ATOM   288  C  CG1 . ILE A 1 37  ? -33.008 -20.976 7.848   1.00 16.21 ? 37  ILE A CG1 1 
ATOM   289  C  CG2 . ILE A 1 37  ? -32.588 -18.792 6.625   1.00 14.24 ? 37  ILE A CG2 1 
ATOM   290  C  CD1 . ILE A 1 37  ? -31.577 -21.095 8.149   1.00 17.81 ? 37  ILE A CD1 1 
ATOM   291  N  N   . ALA A 1 38  ? -33.364 -16.344 8.852   1.00 11.44 ? 38  ALA A N   1 
ATOM   292  C  CA  . ALA A 1 38  ? -33.684 -14.980 8.459   1.00 11.66 ? 38  ALA A CA  1 
ATOM   293  C  C   . ALA A 1 38  ? -32.716 -14.522 7.378   1.00 12.21 ? 38  ALA A C   1 
ATOM   294  O  O   . ALA A 1 38  ? -31.520 -14.839 7.434   1.00 12.54 ? 38  ALA A O   1 
ATOM   295  C  CB  . ALA A 1 38  ? -33.605 -14.033 9.660   1.00 12.14 ? 38  ALA A CB  1 
ATOM   296  N  N   . VAL A 1 39  ? -33.242 -13.785 6.399   1.00 11.75 ? 39  VAL A N   1 
ATOM   297  C  CA  . VAL A 1 39  ? -32.448 -13.318 5.266   1.00 12.22 ? 39  VAL A CA  1 
ATOM   298  C  C   . VAL A 1 39  ? -32.704 -11.835 5.028   1.00 12.12 ? 39  VAL A C   1 
ATOM   299  O  O   . VAL A 1 39  ? -33.819 -11.340 5.223   1.00 12.65 ? 39  VAL A O   1 
ATOM   300  C  CB  . VAL A 1 39  ? -32.721 -14.157 3.981   1.00 13.87 ? 39  VAL A CB  1 
ATOM   301  C  CG1 . VAL A 1 39  ? -32.359 -15.625 4.199   1.00 13.42 ? 39  VAL A CG1 1 
ATOM   302  C  CG2 . VAL A 1 39  ? -34.172 -14.100 3.559   1.00 16.68 ? 39  VAL A CG2 1 
ATOM   303  N  N   . HIS A 1 40  ? -31.661 -11.128 4.589   1.00 12.50 ? 40  HIS A N   1 
ATOM   304  C  CA  . HIS A 1 40  ? -31.729 -9.677  4.440   1.00 11.15 ? 40  HIS A CA  1 
ATOM   305  C  C   . HIS A 1 40  ? -30.864 -9.315  3.246   1.00 11.30 ? 40  HIS A C   1 
ATOM   306  O  O   . HIS A 1 40  ? -29.678 -9.662  3.225   1.00 13.13 ? 40  HIS A O   1 
ATOM   307  C  CB  . HIS A 1 40  ? -31.197 -9.039  5.723   1.00 12.52 ? 40  HIS A CB  1 
ATOM   308  C  CG  . HIS A 1 40  ? -31.187 -7.546  5.738   1.00 12.86 ? 40  HIS A CG  1 
ATOM   309  N  ND1 . HIS A 1 40  ? -30.507 -6.842  6.709   1.00 13.83 ? 40  HIS A ND1 1 
ATOM   310  C  CD2 . HIS A 1 40  ? -31.713 -6.622  4.897   1.00 12.79 ? 40  HIS A CD2 1 
ATOM   311  C  CE1 . HIS A 1 40  ? -30.649 -5.548  6.492   1.00 13.15 ? 40  HIS A CE1 1 
ATOM   312  N  NE2 . HIS A 1 40  ? -31.386 -5.388  5.406   1.00 13.07 ? 40  HIS A NE2 1 
ATOM   313  N  N   . VAL A 1 41  ? -31.460 -8.679  2.234   1.00 11.40 ? 41  VAL A N   1 
ATOM   314  C  CA  . VAL A 1 41  ? -30.748 -8.302  1.015   1.00 12.05 ? 41  VAL A CA  1 
ATOM   315  C  C   . VAL A 1 41  ? -30.804 -6.795  0.901   1.00 11.76 ? 41  VAL A C   1 
ATOM   316  O  O   . VAL A 1 41  ? -31.877 -6.200  1.037   1.00 13.10 ? 41  VAL A O   1 
ATOM   317  C  CB  . VAL A 1 41  ? -31.355 -8.972  -0.234  1.00 13.10 ? 41  VAL A CB  1 
ATOM   318  C  CG1 . VAL A 1 41  ? -30.646 -8.508  -1.513  1.00 13.96 ? 41  VAL A CG1 1 
ATOM   319  C  CG2 . VAL A 1 41  ? -31.244 -10.478 -0.122  1.00 14.76 ? 41  VAL A CG2 1 
ATOM   320  N  N   . VAL A 1 42  ? -29.653 -6.175  0.688   1.00 11.19 ? 42  VAL A N   1 
ATOM   321  C  CA  . VAL A 1 42  ? -29.535 -4.724  0.687   1.00 12.04 ? 42  VAL A CA  1 
ATOM   322  C  C   . VAL A 1 42  ? -28.936 -4.297  -0.642  1.00 12.31 ? 42  VAL A C   1 
ATOM   323  O  O   . VAL A 1 42  ? -27.720 -4.286  -0.810  1.00 12.10 ? 42  VAL A O   1 
ATOM   324  C  CB  . VAL A 1 42  ? -28.682 -4.208  1.860   1.00 12.93 ? 42  VAL A CB  1 
ATOM   325  C  CG1 . VAL A 1 42  ? -28.808 -2.680  1.988   1.00 13.98 ? 42  VAL A CG1 1 
ATOM   326  C  CG2 . VAL A 1 42  ? -29.099 -4.866  3.165   1.00 13.32 ? 42  VAL A CG2 1 
ATOM   327  N  N   . PRO A 1 43  ? -29.767 -3.925  -1.609  1.00 12.27 ? 43  PRO A N   1 
ATOM   328  C  CA  . PRO A 1 43  ? -29.253 -3.540  -2.927  1.00 13.31 ? 43  PRO A CA  1 
ATOM   329  C  C   . PRO A 1 43  ? -28.892 -2.065  -2.981  1.00 12.98 ? 43  PRO A C   1 
ATOM   330  O  O   . PRO A 1 43  ? -29.039 -1.329  -1.999  1.00 13.11 ? 43  PRO A O   1 
ATOM   331  C  CB  . PRO A 1 43  ? -30.431 -3.870  -3.856  1.00 14.09 ? 43  PRO A CB  1 
ATOM   332  C  CG  . PRO A 1 43  ? -31.639 -3.663  -2.992  1.00 15.00 ? 43  PRO A CG  1 
ATOM   333  C  CD  . PRO A 1 43  ? -31.236 -3.977  -1.566  1.00 13.91 ? 43  PRO A CD  1 
ATOM   334  N  N   . ASP A 1 44  ? -28.387 -1.636  -4.128  1.00 12.86 ? 44  ASP A N   1 
ATOM   335  C  CA  . ASP A 1 44  ? -28.169 -0.222  -4.431  1.00 14.32 ? 44  ASP A CA  1 
ATOM   336  C  C   . ASP A 1 44  ? -27.111 0.434   -3.544  1.00 14.05 ? 44  ASP A C   1 
ATOM   337  O  O   . ASP A 1 44  ? -27.124 1.663   -3.380  1.00 15.66 ? 44  ASP A O   1 
ATOM   338  C  CB  . ASP A 1 44  ? -29.468 0.583   -4.382  1.00 17.33 ? 44  ASP A CB  1 
ATOM   339  C  CG  . ASP A 1 44  ? -30.416 0.209   -5.486  1.00 22.18 ? 44  ASP A CG  1 
ATOM   340  O  OD1 . ASP A 1 44  ? -30.063 0.413   -6.661  1.00 24.09 ? 44  ASP A OD1 1 
ATOM   341  O  OD2 . ASP A 1 44  ? -31.508 -0.286  -5.165  1.00 24.81 ? 44  ASP A OD2 1 
ATOM   342  N  N   . GLN A 1 45  ? -26.171 -0.343  -3.008  1.00 13.38 ? 45  GLN A N   1 
ATOM   343  C  CA  . GLN A 1 45  ? -25.187 0.196   -2.083  1.00 12.16 ? 45  GLN A CA  1 
ATOM   344  C  C   . GLN A 1 45  ? -24.003 0.851   -2.799  1.00 12.67 ? 45  GLN A C   1 
ATOM   345  O  O   . GLN A 1 45  ? -23.667 0.522   -3.943  1.00 14.76 ? 45  GLN A O   1 
ATOM   346  C  CB  . GLN A 1 45  ? -24.663 -0.910  -1.172  1.00 11.31 ? 45  GLN A CB  1 
ATOM   347  C  CG  . GLN A 1 45  ? -25.742 -1.470  -0.254  1.00 12.80 ? 45  GLN A CG  1 
ATOM   348  C  CD  . GLN A 1 45  ? -26.439 -0.357  0.532   1.00 13.11 ? 45  GLN A CD  1 
ATOM   349  O  OE1 . GLN A 1 45  ? -27.569 0.072   0.220   1.00 14.54 ? 45  GLN A OE1 1 
ATOM   350  N  NE2 . GLN A 1 45  ? -25.770 0.121   1.536   1.00 12.78 ? 45  GLN A NE2 1 
ATOM   351  N  N   . LEU A 1 46  ? -23.379 1.808   -2.099  1.00 12.33 ? 46  LEU A N   1 
ATOM   352  C  CA  . LEU A 1 46  ? -22.159 2.497   -2.525  1.00 13.23 ? 46  LEU A CA  1 
ATOM   353  C  C   . LEU A 1 46  ? -20.979 1.675   -2.013  1.00 13.38 ? 46  LEU A C   1 
ATOM   354  O  O   . LEU A 1 46  ? -20.633 1.727   -0.825  1.00 13.51 ? 46  LEU A O   1 
ATOM   355  C  CB  . LEU A 1 46  ? -22.151 3.910   -1.960  1.00 14.18 ? 46  LEU A CB  1 
ATOM   356  C  CG  . LEU A 1 46  ? -20.955 4.800   -2.252  1.00 15.92 ? 46  LEU A CG  1 
ATOM   357  C  CD1 . LEU A 1 46  ? -20.739 4.998   -3.747  1.00 17.01 ? 46  LEU A CD1 1 
ATOM   358  C  CD2 . LEU A 1 46  ? -21.167 6.175   -1.596  1.00 17.84 ? 46  LEU A CD2 1 
ATOM   359  N  N   . MET A 1 47  ? -20.394 0.867   -2.901  1.00 13.41 ? 47  MET A N   1 
ATOM   360  C  CA  . MET A 1 47  ? -19.385 -0.106  -2.498  1.00 14.70 ? 47  MET A CA  1 
ATOM   361  C  C   . MET A 1 47  ? -18.325 -0.215  -3.571  1.00 14.21 ? 47  MET A C   1 
ATOM   362  O  O   . MET A 1 47  ? -18.593 0.040   -4.746  1.00 15.41 ? 47  MET A O   1 
ATOM   363  C  CB  . MET A 1 47  ? -19.941 -1.529  -2.378  1.00 17.37 ? 47  MET A CB  1 
ATOM   364  C  CG  . MET A 1 47  ? -21.273 -1.647  -1.694  1.00 20.15 ? 47  MET A CG  1 
ATOM   365  S  SD  . MET A 1 47  ? -21.899 -3.316  -1.610  1.00 21.68 ? 47  MET A SD  1 
ATOM   366  C  CE  . MET A 1 47  ? -20.408 -4.230  -1.765  1.00 22.79 ? 47  MET A CE  1 
ATOM   367  N  N   . ALA A 1 48  ? -17.134 -0.617  -3.153  1.00 13.78 ? 48  ALA A N   1 
ATOM   368  C  CA  . ALA A 1 48  ? -16.073 -0.992  -4.069  1.00 13.91 ? 48  ALA A CA  1 
ATOM   369  C  C   . ALA A 1 48  ? -15.430 -2.262  -3.547  1.00 13.95 ? 48  ALA A C   1 
ATOM   370  O  O   . ALA A 1 48  ? -15.423 -2.531  -2.343  1.00 14.09 ? 48  ALA A O   1 
ATOM   371  C  CB  . ALA A 1 48  ? -15.013 0.122   -4.176  1.00 14.86 ? 48  ALA A CB  1 
ATOM   372  N  N   . PHE A 1 49  ? -14.929 -3.064  -4.474  1.00 14.01 ? 49  PHE A N   1 
ATOM   373  C  CA  . PHE A 1 49  ? -14.220 -4.289  -4.142  1.00 14.61 ? 49  PHE A CA  1 
ATOM   374  C  C   . PHE A 1 49  ? -12.935 -4.278  -4.946  1.00 15.61 ? 49  PHE A C   1 
ATOM   375  O  O   . PHE A 1 49  ? -12.975 -4.195  -6.180  1.00 16.10 ? 49  PHE A O   1 
ATOM   376  C  CB  . PHE A 1 49  ? -15.075 -5.506  -4.502  1.00 15.20 ? 49  PHE A CB  1 
ATOM   377  C  CG  . PHE A 1 49  ? -14.567 -6.811  -3.939  1.00 16.27 ? 49  PHE A CG  1 
ATOM   378  C  CD1 . PHE A 1 49  ? -13.405 -7.400  -4.423  1.00 17.29 ? 49  PHE A CD1 1 
ATOM   379  C  CD2 . PHE A 1 49  ? -15.292 -7.484  -2.959  1.00 16.66 ? 49  PHE A CD2 1 
ATOM   380  C  CE1 . PHE A 1 49  ? -12.965 -8.605  -3.915  1.00 17.89 ? 49  PHE A CE1 1 
ATOM   381  C  CE2 . PHE A 1 49  ? -14.845 -8.706  -2.443  1.00 17.24 ? 49  PHE A CE2 1 
ATOM   382  C  CZ  . PHE A 1 49  ? -13.690 -9.253  -2.921  1.00 17.78 ? 49  PHE A CZ  1 
ATOM   383  N  N   . GLY A 1 50  ? -11.801 -4.334  -4.257  1.00 16.63 ? 50  GLY A N   1 
ATOM   384  C  CA  . GLY A 1 50  ? -10.519 -4.282  -4.942  1.00 18.04 ? 50  GLY A CA  1 
ATOM   385  C  C   . GLY A 1 50  ? -10.296 -3.014  -5.730  1.00 20.07 ? 50  GLY A C   1 
ATOM   386  O  O   . GLY A 1 50  ? -9.528  -3.018  -6.709  1.00 21.39 ? 50  GLY A O   1 
ATOM   387  N  N   . GLY A 1 51  ? -10.923 -1.914  -5.305  1.00 20.89 ? 51  GLY A N   1 
ATOM   388  C  CA  . GLY A 1 51  ? -10.801 -0.624  -5.946  1.00 22.10 ? 51  GLY A CA  1 
ATOM   389  C  C   . GLY A 1 51  ? -11.791 -0.308  -7.046  1.00 22.81 ? 51  GLY A C   1 
ATOM   390  O  O   . GLY A 1 51  ? -11.753 0.807   -7.566  1.00 25.64 ? 51  GLY A O   1 
ATOM   391  N  N   . SER A 1 52  ? -12.653 -1.239  -7.449  1.00 20.37 ? 52  SER A N   1 
ATOM   392  C  CA  . SER A 1 52  ? -13.579 -0.979  -8.540  1.00 19.52 ? 52  SER A CA  1 
ATOM   393  C  C   . SER A 1 52  ? -14.998 -1.268  -8.091  1.00 18.42 ? 52  SER A C   1 
ATOM   394  O  O   . SER A 1 52  ? -15.223 -1.962  -7.097  1.00 16.81 ? 52  SER A O   1 
ATOM   395  C  CB  . SER A 1 52  ? -13.213 -1.765  -9.805  1.00 20.23 ? 52  SER A CB  1 
ATOM   396  O  OG  . SER A 1 52  ? -13.345 -3.159  -9.567  1.00 21.69 ? 52  SER A OG  1 
ATOM   397  N  N   . SER A 1 53  ? -15.951 -0.747  -8.857  1.00 18.86 ? 53  SER A N   1 
ATOM   398  C  CA  . SER A 1 53  ? -17.355 -0.827  -8.490  1.00 19.35 ? 53  SER A CA  1 
ATOM   399  C  C   . SER A 1 53  ? -18.189 -1.628  -9.478  1.00 18.95 ? 53  SER A C   1 
ATOM   400  O  O   . SER A 1 53  ? -19.396 -1.409  -9.587  1.00 19.34 ? 53  SER A O   1 
ATOM   401  C  CB  . SER A 1 53  ? -17.942 0.549   -8.202  1.00 20.69 ? 53  SER A CB  1 
ATOM   402  O  OG  . SER A 1 53  ? -17.287 1.071   -7.063  1.00 22.45 ? 53  SER A OG  1 
ATOM   403  N  N   . GLU A 1 54  ? -17.576 -2.599  -10.168 1.00 18.87 ? 54  GLU A N   1 
ATOM   404  C  CA  . GLU A 1 54  ? -18.385 -3.612  -10.810 1.00 19.17 ? 54  GLU A CA  1 
ATOM   405  C  C   . GLU A 1 54  ? -19.188 -4.356  -9.738  1.00 17.26 ? 54  GLU A C   1 
ATOM   406  O  O   . GLU A 1 54  ? -18.921 -4.232  -8.534  1.00 15.93 ? 54  GLU A O   1 
ATOM   407  C  CB  . GLU A 1 54  ? -17.524 -4.595  -11.591 1.00 21.43 ? 54  GLU A CB  1 
ATOM   408  C  CG  . GLU A 1 54  ? -16.775 -3.976  -12.742 1.00 24.17 ? 54  GLU A CG  1 
ATOM   409  C  CD  . GLU A 1 54  ? -15.436 -3.536  -12.261 1.00 27.46 ? 54  GLU A CD  1 
ATOM   410  O  OE1 . GLU A 1 54  ? -15.120 -3.876  -11.094 1.00 28.04 ? 54  GLU A OE1 1 
ATOM   411  O  OE2 . GLU A 1 54  ? -14.717 -2.883  -13.024 1.00 29.38 ? 54  GLU A OE2 1 
ATOM   412  N  N   . PRO A 1 55  ? -20.220 -5.094  -10.133 1.00 17.17 ? 55  PRO A N   1 
ATOM   413  C  CA  . PRO A 1 55  ? -21.053 -5.755  -9.125  1.00 15.94 ? 55  PRO A CA  1 
ATOM   414  C  C   . PRO A 1 55  ? -20.228 -6.561  -8.130  1.00 14.84 ? 55  PRO A C   1 
ATOM   415  O  O   . PRO A 1 55  ? -19.288 -7.274  -8.497  1.00 15.62 ? 55  PRO A O   1 
ATOM   416  C  CB  . PRO A 1 55  ? -21.956 -6.659  -9.962  1.00 17.51 ? 55  PRO A CB  1 
ATOM   417  C  CG  . PRO A 1 55  ? -22.107 -5.902  -11.239 1.00 18.67 ? 55  PRO A CG  1 
ATOM   418  C  CD  . PRO A 1 55  ? -20.786 -5.262  -11.483 1.00 18.58 ? 55  PRO A CD  1 
ATOM   419  N  N   . CYS A 1 56  ? -20.578 -6.420  -6.855  1.00 14.09 ? 56  CYS A N   1 
ATOM   420  C  CA  . CYS A 1 56  ? -19.876 -7.115  -5.777  1.00 13.20 ? 56  CYS A CA  1 
ATOM   421  C  C   . CYS A 1 56  ? -20.847 -7.317  -4.622  1.00 12.43 ? 56  CYS A C   1 
ATOM   422  O  O   . CYS A 1 56  ? -21.940 -6.752  -4.616  1.00 13.65 ? 56  CYS A O   1 
ATOM   423  C  CB  . CYS A 1 56  ? -18.628 -6.327  -5.318  1.00 14.14 ? 56  CYS A CB  1 
ATOM   424  S  SG  . CYS A 1 56  ? -18.977 -4.682  -4.674  1.00 15.95 ? 56  CYS A SG  1 
ATOM   425  N  N   . ALA A 1 57  ? -20.446 -8.131  -3.640  1.00 12.79 ? 57  ALA A N   1 
ATOM   426  C  CA  . ALA A 1 57  ? -21.292 -8.333  -2.471  1.00 12.39 ? 57  ALA A CA  1 
ATOM   427  C  C   . ALA A 1 57  ? -20.432 -8.562  -1.236  1.00 12.28 ? 57  ALA A C   1 
ATOM   428  O  O   . ALA A 1 57  ? -19.399 -9.247  -1.292  1.00 13.13 ? 57  ALA A O   1 
ATOM   429  C  CB  . ALA A 1 57  ? -22.273 -9.501  -2.654  1.00 13.46 ? 57  ALA A CB  1 
ATOM   430  N  N   . LEU A 1 58  ? -20.878 -7.995  -0.118  1.00 12.12 ? 58  LEU A N   1 
ATOM   431  C  CA  . LEU A 1 58  ? -20.314 -8.259  1.201   1.00 11.68 ? 58  LEU A CA  1 
ATOM   432  C  C   . LEU A 1 58  ? -21.419 -8.868  2.044   1.00 11.65 ? 58  LEU A C   1 
ATOM   433  O  O   . LEU A 1 58  ? -22.479 -8.255  2.214   1.00 12.35 ? 58  LEU A O   1 
ATOM   434  C  CB  . LEU A 1 58  ? -19.811 -6.971  1.854   1.00 13.67 ? 58  LEU A CB  1 
ATOM   435  C  CG  . LEU A 1 58  ? -18.755 -6.187  1.065   1.00 15.28 ? 58  LEU A CG  1 
ATOM   436  C  CD1 . LEU A 1 58  ? -18.370 -4.905  1.815   1.00 16.33 ? 58  LEU A CD1 1 
ATOM   437  C  CD2 . LEU A 1 58  ? -17.525 -7.035  0.798   1.00 16.51 ? 58  LEU A CD2 1 
ATOM   438  N  N   . CYS A 1 59  ? -21.162 -10.051 2.582   1.00 11.65 ? 59  CYS A N   1 
ATOM   439  C  CA  . CYS A 1 59  ? -22.219 -10.839 3.188   1.00 11.11 ? 59  CYS A CA  1 
ATOM   440  C  C   . CYS A 1 59  ? -21.786 -11.359 4.538   1.00 11.43 ? 59  CYS A C   1 
ATOM   441  O  O   . CYS A 1 59  ? -20.594 -11.444 4.844   1.00 11.66 ? 59  CYS A O   1 
ATOM   442  C  CB  . CYS A 1 59  ? -22.549 -12.076 2.332   1.00 12.69 ? 59  CYS A CB  1 
ATOM   443  S  SG  . CYS A 1 59  ? -22.814 -11.753 0.592   1.00 13.92 ? 59  CYS A SG  1 
ATOM   444  N  N   . SER A 1 60  ? -22.770 -11.817 5.303   1.00 11.76 ? 60  SER A N   1 
ATOM   445  C  CA  . SER A 1 60  ? -22.440 -12.521 6.531   1.00 12.22 ? 60  SER A CA  1 
ATOM   446  C  C   . SER A 1 60  ? -23.463 -13.611 6.804   1.00 12.38 ? 60  SER A C   1 
ATOM   447  O  O   . SER A 1 60  ? -24.644 -13.485 6.461   1.00 13.89 ? 60  SER A O   1 
ATOM   448  C  CB  . SER A 1 60  ? -22.379 -11.610 7.751   1.00 14.21 ? 60  SER A CB  1 
ATOM   449  O  OG  . SER A 1 60  ? -23.610 -10.977 7.947   1.00 15.72 ? 60  SER A OG  1 
ATOM   450  N  N   . LEU A 1 61  ? -22.982 -14.695 7.419   1.00 11.49 ? 61  LEU A N   1 
ATOM   451  C  CA  . LEU A 1 61  ? -23.812 -15.794 7.900   1.00 12.23 ? 61  LEU A CA  1 
ATOM   452  C  C   . LEU A 1 61  ? -23.510 -15.978 9.377   1.00 11.81 ? 61  LEU A C   1 
ATOM   453  O  O   . LEU A 1 61  ? -22.363 -16.256 9.753   1.00 12.01 ? 61  LEU A O   1 
ATOM   454  C  CB  . LEU A 1 61  ? -23.537 -17.097 7.129   1.00 13.51 ? 61  LEU A CB  1 
ATOM   455  C  CG  . LEU A 1 61  ? -24.385 -18.311 7.546   1.00 14.83 ? 61  LEU A CG  1 
ATOM   456  C  CD1 . LEU A 1 61  ? -25.873 -18.079 7.273   1.00 15.61 ? 61  LEU A CD1 1 
ATOM   457  C  CD2 . LEU A 1 61  ? -23.947 -19.616 6.884   1.00 15.29 ? 61  LEU A CD2 1 
ATOM   458  N  N   . HIS A 1 62  ? -24.536 -15.798 10.208  1.00 11.72 ? 62  HIS A N   1 
ATOM   459  C  CA  . HIS A 1 62  ? -24.467 -16.064 11.643  1.00 12.65 ? 62  HIS A CA  1 
ATOM   460  C  C   . HIS A 1 62  ? -25.318 -17.290 11.929  1.00 12.92 ? 62  HIS A C   1 
ATOM   461  O  O   . HIS A 1 62  ? -26.477 -17.351 11.498  1.00 13.22 ? 62  HIS A O   1 
ATOM   462  C  CB  . HIS A 1 62  ? -25.072 -14.899 12.435  1.00 13.26 ? 62  HIS A CB  1 
ATOM   463  C  CG  . HIS A 1 62  ? -24.311 -13.618 12.327  1.00 14.73 ? 62  HIS A CG  1 
ATOM   464  N  ND1 . HIS A 1 62  ? -24.348 -12.821 11.207  1.00 15.78 ? 62  HIS A ND1 1 
ATOM   465  C  CD2 . HIS A 1 62  ? -23.518 -12.977 13.219  1.00 15.28 ? 62  HIS A CD2 1 
ATOM   466  C  CE1 . HIS A 1 62  ? -23.597 -11.749 11.406  1.00 15.55 ? 62  HIS A CE1 1 
ATOM   467  N  NE2 . HIS A 1 62  ? -23.084 -11.819 12.623  1.00 15.74 ? 62  HIS A NE2 1 
ATOM   468  N  N   . SER A 1 63  ? -24.771 -18.233 12.694  1.00 11.98 ? 63  SER A N   1 
ATOM   469  C  CA  . SER A 1 63  ? -25.516 -19.431 13.051  1.00 12.59 ? 63  SER A CA  1 
ATOM   470  C  C   . SER A 1 63  ? -25.042 -19.935 14.406  1.00 12.23 ? 63  SER A C   1 
ATOM   471  O  O   . SER A 1 63  ? -23.857 -19.837 14.733  1.00 12.28 ? 63  SER A O   1 
ATOM   472  C  CB  . SER A 1 63  ? -25.281 -20.530 12.006  1.00 14.43 ? 63  SER A CB  1 
ATOM   473  O  OG  . SER A 1 63  ? -26.012 -21.710 12.283  1.00 15.19 ? 63  SER A OG  1 
ATOM   474  N  N   . ILE A 1 64  ? -25.971 -20.491 15.183  1.00 12.24 ? 64  ILE A N   1 
ATOM   475  C  CA  . ILE A 1 64  ? -25.607 -21.168 16.424  1.00 12.31 ? 64  ILE A CA  1 
ATOM   476  C  C   . ILE A 1 64  ? -25.126 -22.569 16.041  1.00 13.07 ? 64  ILE A C   1 
ATOM   477  O  O   . ILE A 1 64  ? -25.923 -23.470 15.769  1.00 14.50 ? 64  ILE A O   1 
ATOM   478  C  CB  . ILE A 1 64  ? -26.768 -21.197 17.418  1.00 12.21 ? 64  ILE A CB  1 
ATOM   479  C  CG1 . ILE A 1 64  ? -27.164 -19.761 17.790  1.00 12.20 ? 64  ILE A CG1 1 
ATOM   480  C  CG2 . ILE A 1 64  ? -26.385 -22.012 18.624  1.00 12.65 ? 64  ILE A CG2 1 
ATOM   481  C  CD1 . ILE A 1 64  ? -28.494 -19.664 18.476  1.00 12.69 ? 64  ILE A CD1 1 
ATOM   482  N  N   . GLY A 1 65  ? -23.813 -22.745 15.979  1.00 12.79 ? 65  GLY A N   1 
ATOM   483  C  CA  . GLY A 1 65  ? -23.275 -23.983 15.451  1.00 13.92 ? 65  GLY A CA  1 
ATOM   484  C  C   . GLY A 1 65  ? -23.414 -24.047 13.924  1.00 14.09 ? 65  GLY A C   1 
ATOM   485  O  O   . GLY A 1 65  ? -23.848 -23.111 13.249  1.00 14.60 ? 65  GLY A O   1 
ATOM   486  N  N   . LYS A 1 66  ? -23.040 -25.207 13.387  1.00 13.77 ? 66  LYS A N   1 
ATOM   487  C  CA  . LYS A 1 66  ? -23.044 -25.453 11.939  1.00 14.02 ? 66  LYS A CA  1 
ATOM   488  C  C   . LYS A 1 66  ? -22.094 -24.526 11.185  1.00 13.95 ? 66  LYS A C   1 
ATOM   489  O  O   . LYS A 1 66  ? -22.322 -24.194 10.017  1.00 15.21 ? 66  LYS A O   1 
ATOM   490  C  CB  . LYS A 1 66  ? -24.457 -25.437 11.346  1.00 15.67 ? 66  LYS A CB  1 
ATOM   491  C  CG  . LYS A 1 66  ? -25.446 -26.339 12.092  1.00 17.36 ? 66  LYS A CG  1 
ATOM   492  C  CD  . LYS A 1 66  ? -24.942 -27.766 12.208  1.00 20.60 ? 66  LYS A CD  1 
ATOM   493  C  CE  . LYS A 1 66  ? -24.800 -28.429 10.865  1.00 23.69 ? 66  LYS A CE  1 
ATOM   494  N  NZ  . LYS A 1 66  ? -24.232 -29.812 10.995  1.00 25.78 ? 66  LYS A NZ  1 
ATOM   495  N  N   . ILE A 1 67  ? -21.009 -24.122 11.845  1.00 13.09 ? 67  ILE A N   1 
ATOM   496  C  CA  . ILE A 1 67  ? -19.971 -23.269 11.279  1.00 14.38 ? 67  ILE A CA  1 
ATOM   497  C  C   . ILE A 1 67  ? -18.637 -23.968 11.497  1.00 15.35 ? 67  ILE A C   1 
ATOM   498  O  O   . ILE A 1 67  ? -18.364 -24.484 12.586  1.00 16.70 ? 67  ILE A O   1 
ATOM   499  C  CB  . ILE A 1 67  ? -19.964 -21.892 11.970  1.00 14.56 ? 67  ILE A CB  1 
ATOM   500  C  CG1 . ILE A 1 67  ? -21.285 -21.140 11.734  1.00 14.53 ? 67  ILE A CG1 1 
ATOM   501  C  CG2 . ILE A 1 67  ? -18.718 -21.072 11.598  1.00 15.10 ? 67  ILE A CG2 1 
ATOM   502  C  CD1 . ILE A 1 67  ? -21.490 -20.642 10.307  1.00 14.83 ? 67  ILE A CD1 1 
ATOM   503  N  N   . GLY A 1 68  ? -17.815 -24.012 10.468  1.00 15.09 ? 68  GLY A N   1 
ATOM   504  C  CA  . GLY A 1 68  ? -16.518 -24.632 10.610  1.00 15.95 ? 68  GLY A CA  1 
ATOM   505  C  C   . GLY A 1 68  ? -15.817 -24.679 9.277   1.00 16.16 ? 68  GLY A C   1 
ATOM   506  O  O   . GLY A 1 68  ? -16.346 -24.236 8.255   1.00 16.40 ? 68  GLY A O   1 
ATOM   507  N  N   . GLY A 1 69  ? -14.604 -25.216 9.308   1.00 16.25 ? 69  GLY A N   1 
ATOM   508  C  CA  . GLY A 1 69  ? -13.741 -25.224 8.134   1.00 16.75 ? 69  GLY A CA  1 
ATOM   509  C  C   . GLY A 1 69  ? -14.409 -25.754 6.886   1.00 16.60 ? 69  GLY A C   1 
ATOM   510  O  O   . GLY A 1 69  ? -14.552 -25.041 5.871   1.00 16.55 ? 69  GLY A O   1 
ATOM   511  N  N   . ALA A 1 70  ? -14.840 -27.014 6.965   1.00 17.62 ? 70  ALA A N   1 
ATOM   512  C  CA  . ALA A 1 70  ? -15.432 -27.664 5.805   1.00 17.39 ? 70  ALA A CA  1 
ATOM   513  C  C   . ALA A 1 70  ? -16.817 -27.111 5.513   1.00 17.15 ? 70  ALA A C   1 
ATOM   514  O  O   . ALA A 1 70  ? -17.165 -26.879 4.354   1.00 16.73 ? 70  ALA A O   1 
ATOM   515  C  CB  . ALA A 1 70  ? -15.454 -29.176 6.018   1.00 18.01 ? 70  ALA A CB  1 
ATOM   516  N  N   . GLN A 1 71  ? -17.618 -26.880 6.550   1.00 16.37 ? 71  GLN A N   1 
ATOM   517  C  CA  . GLN A 1 71  ? -18.952 -26.352 6.319   1.00 15.03 ? 71  GLN A CA  1 
ATOM   518  C  C   . GLN A 1 71  ? -18.888 -24.999 5.640   1.00 15.01 ? 71  GLN A C   1 
ATOM   519  O  O   . GLN A 1 71  ? -19.697 -24.704 4.754   1.00 15.93 ? 71  GLN A O   1 
ATOM   520  C  CB  . GLN A 1 71  ? -19.717 -26.258 7.633   1.00 15.18 ? 71  GLN A CB  1 
ATOM   521  C  CG  . GLN A 1 71  ? -20.059 -27.638 8.165   1.00 15.95 ? 71  GLN A CG  1 
ATOM   522  C  CD  . GLN A 1 71  ? -20.678 -27.594 9.536   1.00 17.51 ? 71  GLN A CD  1 
ATOM   523  O  OE1 . GLN A 1 71  ? -21.896 -27.642 9.685   1.00 18.69 ? 71  GLN A OE1 1 
ATOM   524  N  NE2 . GLN A 1 71  ? -19.835 -27.485 10.548  1.00 17.88 ? 71  GLN A NE2 1 
ATOM   525  N  N   . ASN A 1 72  ? -17.939 -24.151 6.048   1.00 13.58 ? 72  ASN A N   1 
ATOM   526  C  CA  . ASN A 1 72  ? -17.891 -22.809 5.478   1.00 13.92 ? 72  ASN A CA  1 
ATOM   527  C  C   . ASN A 1 72  ? -17.449 -22.829 4.027   1.00 15.16 ? 72  ASN A C   1 
ATOM   528  O  O   . ASN A 1 72  ? -17.899 -21.999 3.228   1.00 15.68 ? 72  ASN A O   1 
ATOM   529  C  CB  . ASN A 1 72  ? -16.995 -21.890 6.299   1.00 13.13 ? 72  ASN A CB  1 
ATOM   530  C  CG  . ASN A 1 72  ? -17.484 -21.675 7.716   1.00 12.49 ? 72  ASN A CG  1 
ATOM   531  O  OD1 . ASN A 1 72  ? -18.603 -22.080 8.111   1.00 12.33 ? 72  ASN A OD1 1 
ATOM   532  N  ND2 . ASN A 1 72  ? -16.635 -21.016 8.498   1.00 12.61 ? 72  ASN A ND2 1 
ATOM   533  N  N   . ARG A 1 73  ? -16.562 -23.753 3.674   1.00 15.13 ? 73  ARG A N   1 
ATOM   534  C  CA  . ARG A 1 73  ? -16.235 -23.940 2.267   1.00 15.64 ? 73  ARG A CA  1 
ATOM   535  C  C   . ARG A 1 73  ? -17.476 -24.320 1.470   1.00 15.79 ? 73  ARG A C   1 
ATOM   536  O  O   . ARG A 1 73  ? -17.705 -23.793 0.376   1.00 16.20 ? 73  ARG A O   1 
ATOM   537  C  CB  . ARG A 1 73  ? -15.158 -25.010 2.138   1.00 16.65 ? 73  ARG A CB  1 
ATOM   538  C  CG  . ARG A 1 73  ? -13.779 -24.472 2.455   1.00 18.31 ? 73  ARG A CG  1 
ATOM   539  C  CD  . ARG A 1 73  ? -12.696 -25.495 2.146   1.00 20.27 ? 73  ARG A CD  1 
ATOM   540  N  NE  . ARG A 1 73  ? -12.636 -26.606 3.095   1.00 22.38 ? 73  ARG A NE  1 
ATOM   541  C  CZ  . ARG A 1 73  ? -11.984 -26.555 4.257   1.00 22.94 ? 73  ARG A CZ  1 
ATOM   542  N  NH1 . ARG A 1 73  ? -11.344 -25.445 4.615   1.00 23.20 ? 73  ARG A NH1 1 
ATOM   543  N  NH2 . ARG A 1 73  ? -11.976 -27.601 5.075   1.00 23.30 ? 73  ARG A NH2 1 
ATOM   544  N  N   . SER A 1 74  ? -18.307 -25.210 2.016   1.00 15.32 ? 74  SER A N   1 
ATOM   545  C  CA  . SER A 1 74  ? -19.522 -25.614 1.333   1.00 16.44 ? 74  SER A CA  1 
ATOM   546  C  C   . SER A 1 74  ? -20.512 -24.462 1.225   1.00 15.90 ? 74  SER A C   1 
ATOM   547  O  O   . SER A 1 74  ? -21.102 -24.235 0.154   1.00 17.06 ? 74  SER A O   1 
ATOM   548  C  CB  . SER A 1 74  ? -20.144 -26.771 2.102   1.00 17.55 ? 74  SER A CB  1 
ATOM   549  O  OG  . SER A 1 74  ? -21.220 -27.310 1.370   1.00 18.69 ? 74  SER A OG  1 
ATOM   550  N  N   . TYR A 1 75  ? -20.691 -23.709 2.310   1.00 15.52 ? 75  TYR A N   1 
ATOM   551  C  CA  . TYR A 1 75  ? -21.579 -22.557 2.243   1.00 14.98 ? 75  TYR A CA  1 
ATOM   552  C  C   . TYR A 1 75  ? -21.104 -21.566 1.192   1.00 15.43 ? 75  TYR A C   1 
ATOM   553  O  O   . TYR A 1 75  ? -21.917 -20.938 0.509   1.00 15.67 ? 75  TYR A O   1 
ATOM   554  C  CB  . TYR A 1 75  ? -21.627 -21.835 3.596   1.00 15.04 ? 75  TYR A CB  1 
ATOM   555  C  CG  . TYR A 1 75  ? -22.217 -22.613 4.751   1.00 16.16 ? 75  TYR A CG  1 
ATOM   556  C  CD1 . TYR A 1 75  ? -23.231 -23.528 4.541   1.00 17.53 ? 75  TYR A CD1 1 
ATOM   557  C  CD2 . TYR A 1 75  ? -21.764 -22.414 6.046   1.00 16.00 ? 75  TYR A CD2 1 
ATOM   558  C  CE1 . TYR A 1 75  ? -23.774 -24.234 5.592   1.00 18.49 ? 75  TYR A CE1 1 
ATOM   559  C  CE2 . TYR A 1 75  ? -22.300 -23.114 7.107   1.00 16.55 ? 75  TYR A CE2 1 
ATOM   560  C  CZ  . TYR A 1 75  ? -23.305 -24.015 6.879   1.00 17.89 ? 75  TYR A CZ  1 
ATOM   561  O  OH  . TYR A 1 75  ? -23.837 -24.714 7.933   1.00 19.58 ? 75  TYR A OH  1 
ATOM   562  N  N   . SER A 1 76  ? -19.792 -21.358 1.094   1.00 14.82 ? 76  SER A N   1 
ATOM   563  C  CA  . SER A 1 76  ? -19.299 -20.356 0.159   1.00 15.03 ? 76  SER A CA  1 
ATOM   564  C  C   . SER A 1 76  ? -19.579 -20.764 -1.281  1.00 15.18 ? 76  SER A C   1 
ATOM   565  O  O   . SER A 1 76  ? -19.933 -19.915 -2.115  1.00 15.93 ? 76  SER A O   1 
ATOM   566  C  CB  . SER A 1 76  ? -17.811 -20.141 0.379   1.00 15.91 ? 76  SER A CB  1 
ATOM   567  O  OG  . SER A 1 76  ? -17.603 -19.603 1.670   1.00 17.20 ? 76  SER A OG  1 
ATOM   568  N  N   . LYS A 1 77  ? -19.416 -22.056 -1.598  1.00 16.07 ? 77  LYS A N   1 
ATOM   569  C  CA  . LYS A 1 77  ? -19.739 -22.524 -2.940  1.00 17.11 ? 77  LYS A CA  1 
ATOM   570  C  C   . LYS A 1 77  ? -21.217 -22.329 -3.240  1.00 17.34 ? 77  LYS A C   1 
ATOM   571  O  O   . LYS A 1 77  ? -21.582 -21.852 -4.321  1.00 17.93 ? 77  LYS A O   1 
ATOM   572  C  CB  . LYS A 1 77  ? -19.355 -23.999 -3.065  1.00 18.91 ? 77  LYS A CB  1 
ATOM   573  C  CG  . LYS A 1 77  ? -19.603 -24.598 -4.435  1.00 21.20 ? 77  LYS A CG  1 
ATOM   574  C  CD  . LYS A 1 77  ? -19.156 -26.033 -4.501  1.00 23.66 ? 77  LYS A CD  1 
ATOM   575  C  CE  . LYS A 1 77  ? -19.275 -26.524 -5.930  1.00 25.74 ? 77  LYS A CE  1 
ATOM   576  N  NZ  . LYS A 1 77  ? -19.437 -27.988 -5.976  1.00 27.40 ? 77  LYS A NZ  1 
ATOM   577  N  N   . LEU A 1 78  ? -22.080 -22.673 -2.284  1.00 16.33 ? 78  LEU A N   1 
ATOM   578  C  CA  . LEU A 1 78  ? -23.519 -22.539 -2.485  1.00 16.74 ? 78  LEU A CA  1 
ATOM   579  C  C   . LEU A 1 78  ? -23.899 -21.084 -2.669  1.00 16.62 ? 78  LEU A C   1 
ATOM   580  O  O   . LEU A 1 78  ? -24.622 -20.716 -3.608  1.00 16.96 ? 78  LEU A O   1 
ATOM   581  C  CB  . LEU A 1 78  ? -24.240 -23.102 -1.260  1.00 17.39 ? 78  LEU A CB  1 
ATOM   582  C  CG  . LEU A 1 78  ? -25.725 -22.755 -1.136  1.00 18.28 ? 78  LEU A CG  1 
ATOM   583  C  CD1 . LEU A 1 78  ? -26.553 -23.578 -2.123  1.00 19.43 ? 78  LEU A CD1 1 
ATOM   584  C  CD2 . LEU A 1 78  ? -26.203 -22.987 0.297   1.00 18.58 ? 78  LEU A CD2 1 
ATOM   585  N  N   . LEU A 1 79  ? -23.395 -20.232 -1.784  1.00 16.31 ? 79  LEU A N   1 
ATOM   586  C  CA  . LEU A 1 79  ? -23.826 -18.840 -1.767  1.00 15.33 ? 79  LEU A CA  1 
ATOM   587  C  C   . LEU A 1 79  ? -23.219 -18.049 -2.911  1.00 15.19 ? 79  LEU A C   1 
ATOM   588  O  O   . LEU A 1 79  ? -23.915 -17.244 -3.531  1.00 14.91 ? 79  LEU A O   1 
ATOM   589  C  CB  . LEU A 1 79  ? -23.521 -18.209 -0.399  1.00 15.05 ? 79  LEU A CB  1 
ATOM   590  C  CG  . LEU A 1 79  ? -24.372 -18.772 0.745   1.00 16.77 ? 79  LEU A CG  1 
ATOM   591  C  CD1 . LEU A 1 79  ? -23.801 -18.385 2.086   1.00 17.20 ? 79  LEU A CD1 1 
ATOM   592  C  CD2 . LEU A 1 79  ? -25.789 -18.266 0.611   1.00 18.01 ? 79  LEU A CD2 1 
ATOM   593  N  N   . CYS A 1 80  ? -21.935 -18.254 -3.216  1.00 15.39 ? 80  CYS A N   1 
ATOM   594  C  CA  . CYS A 1 80  ? -21.385 -17.616 -4.408  1.00 15.94 ? 80  CYS A CA  1 
ATOM   595  C  C   . CYS A 1 80  ? -22.103 -18.087 -5.663  1.00 15.59 ? 80  CYS A C   1 
ATOM   596  O  O   . CYS A 1 80  ? -22.358 -17.292 -6.577  1.00 15.48 ? 80  CYS A O   1 
ATOM   597  C  CB  . CYS A 1 80  ? -19.884 -17.873 -4.534  1.00 16.44 ? 80  CYS A CB  1 
ATOM   598  S  SG  . CYS A 1 80  ? -18.886 -17.022 -3.313  1.00 17.81 ? 80  CYS A SG  1 
ATOM   599  N  N   . GLY A 1 81  ? -22.449 -19.377 -5.731  1.00 16.59 ? 81  GLY A N   1 
ATOM   600  C  CA  . GLY A 1 81  ? -23.193 -19.846 -6.889  1.00 18.40 ? 81  GLY A CA  1 
ATOM   601  C  C   . GLY A 1 81  ? -24.513 -19.117 -7.051  1.00 18.14 ? 81  GLY A C   1 
ATOM   602  O  O   . GLY A 1 81  ? -24.871 -18.695 -8.154  1.00 18.90 ? 81  GLY A O   1 
ATOM   603  N  N   . LEU A 1 82  ? -25.227 -18.917 -5.944  1.00 17.85 ? 82  LEU A N   1 
ATOM   604  C  CA  . LEU A 1 82  ? -26.508 -18.220 -5.984  1.00 17.62 ? 82  LEU A CA  1 
ATOM   605  C  C   . LEU A 1 82  ? -26.329 -16.756 -6.361  1.00 16.50 ? 82  LEU A C   1 
ATOM   606  O  O   . LEU A 1 82  ? -27.095 -16.227 -7.172  1.00 17.30 ? 82  LEU A O   1 
ATOM   607  C  CB  . LEU A 1 82  ? -27.182 -18.346 -4.620  1.00 18.93 ? 82  LEU A CB  1 
ATOM   608  C  CG  . LEU A 1 82  ? -27.839 -19.701 -4.350  1.00 19.48 ? 82  LEU A CG  1 
ATOM   609  C  CD1 . LEU A 1 82  ? -28.126 -19.882 -2.874  1.00 19.76 ? 82  LEU A CD1 1 
ATOM   610  C  CD2 . LEU A 1 82  ? -29.132 -19.835 -5.157  1.00 20.29 ? 82  LEU A CD2 1 
ATOM   611  N  N   . LEU A 1 83  ? -25.315 -16.084 -5.800  1.00 16.08 ? 83  LEU A N   1 
ATOM   612  C  CA  . LEU A 1 83  ? -25.080 -14.680 -6.147  1.00 14.85 ? 83  LEU A CA  1 
ATOM   613  C  C   . LEU A 1 83  ? -24.677 -14.535 -7.614  1.00 15.34 ? 83  LEU A C   1 
ATOM   614  O  O   . LEU A 1 83  ? -25.061 -13.560 -8.275  1.00 15.36 ? 83  LEU A O   1 
ATOM   615  C  CB  . LEU A 1 83  ? -24.020 -14.056 -5.231  1.00 15.01 ? 83  LEU A CB  1 
ATOM   616  C  CG  . LEU A 1 83  ? -24.448 -13.958 -3.758  1.00 16.00 ? 83  LEU A CG  1 
ATOM   617  C  CD1 . LEU A 1 83  ? -23.278 -13.602 -2.858  1.00 17.10 ? 83  LEU A CD1 1 
ATOM   618  C  CD2 . LEU A 1 83  ? -25.575 -12.926 -3.606  1.00 17.02 ? 83  LEU A CD2 1 
ATOM   619  N  N   . ALA A 1 84  ? -23.943 -15.510 -8.152  1.00 15.46 ? 84  ALA A N   1 
ATOM   620  C  CA  . ALA A 1 84  ? -23.568 -15.467 -9.558  1.00 16.41 ? 84  ALA A CA  1 
ATOM   621  C  C   . ALA A 1 84  ? -24.768 -15.715 -10.451 1.00 17.29 ? 84  ALA A C   1 
ATOM   622  O  O   . ALA A 1 84  ? -25.017 -14.953 -11.396 1.00 17.84 ? 84  ALA A O   1 
ATOM   623  C  CB  . ALA A 1 84  ? -22.463 -16.484 -9.830  1.00 16.42 ? 84  ALA A CB  1 
ATOM   624  N  N   . GLU A 1 85  ? -25.541 -16.761 -10.154 1.00 18.40 ? 85  GLU A N   1 
ATOM   625  C  CA  . GLU A 1 85  ? -26.623 -17.128 -11.060 1.00 21.19 ? 85  GLU A CA  1 
ATOM   626  C  C   . GLU A 1 85  ? -27.763 -16.127 -10.970 1.00 20.89 ? 85  GLU A C   1 
ATOM   627  O  O   . GLU A 1 85  ? -28.370 -15.771 -11.983 1.00 22.15 ? 85  GLU A O   1 
ATOM   628  C  CB  . GLU A 1 85  ? -27.098 -18.550 -10.764 1.00 24.96 ? 85  GLU A CB  1 
ATOM   629  C  CG  . GLU A 1 85  ? -26.164 -19.623 -11.304 1.00 28.87 ? 85  GLU A CG  1 
ATOM   630  C  CD  . GLU A 1 85  ? -25.592 -19.252 -12.668 1.00 32.07 ? 85  GLU A CD  1 
ATOM   631  O  OE1 . GLU A 1 85  ? -24.383 -18.930 -12.746 1.00 33.36 ? 85  GLU A OE1 1 
ATOM   632  O  OE2 . GLU A 1 85  ? -26.354 -19.263 -13.663 1.00 33.09 ? 85  GLU A OE2 1 
ATOM   633  N  N   . ARG A 1 86  ? -28.058 -15.641 -9.766  1.00 19.44 ? 86  ARG A N   1 
ATOM   634  C  CA  . ARG A 1 86  ? -29.244 -14.822 -9.569  1.00 18.85 ? 86  ARG A CA  1 
ATOM   635  C  C   . ARG A 1 86  ? -28.970 -13.327 -9.643  1.00 18.18 ? 86  ARG A C   1 
ATOM   636  O  O   . ARG A 1 86  ? -29.824 -12.583 -10.128 1.00 19.39 ? 86  ARG A O   1 
ATOM   637  C  CB  . ARG A 1 86  ? -29.913 -15.174 -8.238  1.00 19.03 ? 86  ARG A CB  1 
ATOM   638  C  CG  . ARG A 1 86  ? -30.072 -16.692 -7.973  1.00 20.34 ? 86  ARG A CG  1 
ATOM   639  C  CD  . ARG A 1 86  ? -30.874 -17.429 -9.046  1.00 21.00 ? 86  ARG A CD  1 
ATOM   640  N  NE  . ARG A 1 86  ? -32.256 -16.966 -9.062  1.00 21.53 ? 86  ARG A NE  1 
ATOM   641  C  CZ  . ARG A 1 86  ? -32.864 -16.450 -10.126 1.00 22.37 ? 86  ARG A CZ  1 
ATOM   642  N  NH1 . ARG A 1 86  ? -32.232 -16.362 -11.300 1.00 23.03 ? 86  ARG A NH1 1 
ATOM   643  N  NH2 . ARG A 1 86  ? -34.113 -16.031 -10.027 1.00 22.56 ? 86  ARG A NH2 1 
ATOM   644  N  N   . LEU A 1 87  ? -27.821 -12.855 -9.152  1.00 17.10 ? 87  LEU A N   1 
ATOM   645  C  CA  . LEU A 1 87  ? -27.503 -11.431 -9.167  1.00 17.39 ? 87  LEU A CA  1 
ATOM   646  C  C   . LEU A 1 87  ? -26.413 -11.078 -10.168 1.00 17.70 ? 87  LEU A C   1 
ATOM   647  O  O   . LEU A 1 87  ? -26.082 -9.890  -10.311 1.00 16.99 ? 87  LEU A O   1 
ATOM   648  C  CB  . LEU A 1 87  ? -27.107 -10.944 -7.767  1.00 17.42 ? 87  LEU A CB  1 
ATOM   649  C  CG  . LEU A 1 87  ? -28.159 -11.121 -6.671  1.00 18.53 ? 87  LEU A CG  1 
ATOM   650  C  CD1 . LEU A 1 87  ? -27.741 -10.395 -5.431  1.00 18.69 ? 87  LEU A CD1 1 
ATOM   651  C  CD2 . LEU A 1 87  ? -29.521 -10.661 -7.124  1.00 19.75 ? 87  LEU A CD2 1 
ATOM   652  N  N   . ARG A 1 88  ? -25.813 -12.076 -10.829 1.00 19.19 ? 88  ARG A N   1 
ATOM   653  C  CA  . ARG A 1 88  ? -24.778 -11.844 -11.835 1.00 20.48 ? 88  ARG A CA  1 
ATOM   654  C  C   . ARG A 1 88  ? -23.518 -11.235 -11.230 1.00 18.75 ? 88  ARG A C   1 
ATOM   655  O  O   . ARG A 1 88  ? -22.834 -10.421 -11.873 1.00 20.25 ? 88  ARG A O   1 
ATOM   656  C  CB  . ARG A 1 88  ? -25.293 -11.027 -13.037 1.00 24.28 ? 88  ARG A CB  1 
ATOM   657  C  CG  . ARG A 1 88  ? -26.659 -11.452 -13.567 1.00 29.16 ? 88  ARG A CG  1 
ATOM   658  C  CD  . ARG A 1 88  ? -26.686 -12.939 -13.886 1.00 33.17 ? 88  ARG A CD  1 
ATOM   659  N  NE  . ARG A 1 88  ? -25.638 -13.280 -14.850 1.00 36.44 ? 88  ARG A NE  1 
ATOM   660  C  CZ  . ARG A 1 88  ? -25.154 -14.504 -15.062 1.00 38.98 ? 88  ARG A CZ  1 
ATOM   661  N  NH1 . ARG A 1 88  ? -25.605 -15.538 -14.359 1.00 39.69 ? 88  ARG A NH1 1 
ATOM   662  N  NH2 . ARG A 1 88  ? -24.204 -14.690 -15.978 1.00 39.60 ? 88  ARG A NH2 1 
ATOM   663  N  N   . ILE A 1 89  ? -23.220 -11.619 -9.986  1.00 16.76 ? 89  ILE A N   1 
ATOM   664  C  CA  . ILE A 1 89  ? -22.032 -11.150 -9.276  1.00 15.73 ? 89  ILE A CA  1 
ATOM   665  C  C   . ILE A 1 89  ? -20.965 -12.227 -9.370  1.00 16.43 ? 89  ILE A C   1 
ATOM   666  O  O   . ILE A 1 89  ? -21.212 -13.391 -9.015  1.00 16.92 ? 89  ILE A O   1 
ATOM   667  C  CB  . ILE A 1 89  ? -22.340 -10.841 -7.798  1.00 15.42 ? 89  ILE A CB  1 
ATOM   668  C  CG1 . ILE A 1 89  ? -23.425 -9.782  -7.659  1.00 14.92 ? 89  ILE A CG1 1 
ATOM   669  C  CG2 . ILE A 1 89  ? -21.079 -10.355 -7.094  1.00 15.79 ? 89  ILE A CG2 1 
ATOM   670  C  CD1 . ILE A 1 89  ? -23.917 -9.641  -6.237  1.00 14.79 ? 89  ILE A CD1 1 
ATOM   671  N  N   A SER A 1 90  ? -19.781 -11.840 -9.820  0.46 16.74 ? 90  SER A N   1 
ATOM   672  N  N   B SER A 1 90  ? -19.780 -11.846 -9.827  0.54 16.75 ? 90  SER A N   1 
ATOM   673  C  CA  A SER A 1 90  ? -18.666 -12.771 -9.920  0.46 17.02 ? 90  SER A CA  1 
ATOM   674  C  CA  B SER A 1 90  ? -18.684 -12.801 -9.938  0.54 17.00 ? 90  SER A CA  1 
ATOM   675  C  C   A SER A 1 90  ? -18.279 -13.285 -8.534  0.46 16.00 ? 90  SER A C   1 
ATOM   676  C  C   B SER A 1 90  ? -18.266 -13.288 -8.553  0.54 16.00 ? 90  SER A C   1 
ATOM   677  O  O   A SER A 1 90  ? -18.163 -12.489 -7.593  0.46 15.96 ? 90  SER A O   1 
ATOM   678  O  O   B SER A 1 90  ? -18.105 -12.475 -7.639  0.54 15.95 ? 90  SER A O   1 
ATOM   679  C  CB  A SER A 1 90  ? -17.475 -12.045 -10.531 0.46 19.00 ? 90  SER A CB  1 
ATOM   680  C  CB  B SER A 1 90  ? -17.488 -12.144 -10.607 0.54 18.93 ? 90  SER A CB  1 
ATOM   681  O  OG  A SER A 1 90  ? -17.689 -11.824 -11.911 0.46 20.18 ? 90  SER A OG  1 
ATOM   682  O  OG  B SER A 1 90  ? -16.422 -13.077 -10.732 0.54 19.65 ? 90  SER A OG  1 
ATOM   683  N  N   . PRO A 1 91  ? -18.063 -14.594 -8.370  1.00 15.99 ? 91  PRO A N   1 
ATOM   684  C  CA  . PRO A 1 91  ? -17.633 -15.118 -7.059  1.00 15.96 ? 91  PRO A CA  1 
ATOM   685  C  C   . PRO A 1 91  ? -16.378 -14.477 -6.486  1.00 15.83 ? 91  PRO A C   1 
ATOM   686  O  O   . PRO A 1 91  ? -16.263 -14.360 -5.253  1.00 16.21 ? 91  PRO A O   1 
ATOM   687  C  CB  . PRO A 1 91  ? -17.421 -16.611 -7.349  1.00 16.18 ? 91  PRO A CB  1 
ATOM   688  C  CG  . PRO A 1 91  ? -18.345 -16.903 -8.477  1.00 17.05 ? 91  PRO A CG  1 
ATOM   689  C  CD  . PRO A 1 91  ? -18.326 -15.667 -9.349  1.00 17.03 ? 91  PRO A CD  1 
ATOM   690  N  N   . ASP A 1 92  ? -15.471 -13.995 -7.338  1.00 16.22 ? 92  ASP A N   1 
ATOM   691  C  CA  . ASP A 1 92  ? -14.253 -13.358 -6.842  1.00 15.63 ? 92  ASP A CA  1 
ATOM   692  C  C   . ASP A 1 92  ? -14.475 -11.923 -6.393  1.00 14.91 ? 92  ASP A C   1 
ATOM   693  O  O   . ASP A 1 92  ? -13.514 -11.259 -5.990  1.00 15.21 ? 92  ASP A O   1 
ATOM   694  C  CB  . ASP A 1 92  ? -13.064 -13.461 -7.822  1.00 16.47 ? 92  ASP A CB  1 
ATOM   695  C  CG  . ASP A 1 92  ? -13.267 -12.680 -9.109  1.00 18.17 ? 92  ASP A CG  1 
ATOM   696  O  OD1 . ASP A 1 92  ? -14.285 -11.992 -9.275  1.00 18.98 ? 92  ASP A OD1 1 
ATOM   697  O  OD2 . ASP A 1 92  ? -12.358 -12.730 -9.960  1.00 20.42 ? 92  ASP A OD2 1 
ATOM   698  N  N   . ARG A 1 93  ? -15.719 -11.454 -6.410  1.00 13.85 ? 93  ARG A N   1 
ATOM   699  C  CA  . ARG A 1 93  ? -16.083 -10.148 -5.878  1.00 13.71 ? 93  ARG A CA  1 
ATOM   700  C  C   . ARG A 1 93  ? -17.112 -10.289 -4.762  1.00 14.28 ? 93  ARG A C   1 
ATOM   701  O  O   . ARG A 1 93  ? -17.919 -9.384  -4.528  1.00 14.39 ? 93  ARG A O   1 
ATOM   702  C  CB  . ARG A 1 93  ? -16.579 -9.231  -6.998  1.00 13.74 ? 93  ARG A CB  1 
ATOM   703  C  CG  . ARG A 1 93  ? -15.481 -8.978  -8.015  1.00 13.65 ? 93  ARG A CG  1 
ATOM   704  C  CD  . ARG A 1 93  ? -15.948 -8.051  -9.146  1.00 14.71 ? 93  ARG A CD  1 
ATOM   705  N  NE  . ARG A 1 93  ? -16.450 -6.763  -8.659  1.00 15.14 ? 93  ARG A NE  1 
ATOM   706  C  CZ  . ARG A 1 93  ? -15.663 -5.760  -8.259  1.00 15.89 ? 93  ARG A CZ  1 
ATOM   707  N  NH1 . ARG A 1 93  ? -14.337 -5.886  -8.313  1.00 16.49 ? 93  ARG A NH1 1 
ATOM   708  N  NH2 . ARG A 1 93  ? -16.192 -4.626  -7.826  1.00 16.29 ? 93  ARG A NH2 1 
ATOM   709  N  N   . VAL A 1 94  ? -17.072 -11.416 -4.049  1.00 14.37 ? 94  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 94  ? -17.947 -11.684 -2.914  1.00 13.85 ? 94  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 94  ? -17.068 -12.000 -1.715  1.00 13.06 ? 94  VAL A C   1 
ATOM   712  O  O   . VAL A 1 94  ? -16.199 -12.873 -1.799  1.00 13.67 ? 94  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 94  ? -18.891 -12.872 -3.198  1.00 14.12 ? 94  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 94  ? -19.675 -13.237 -1.959  1.00 14.43 ? 94  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 94  ? -19.827 -12.561 -4.354  1.00 14.55 ? 94  VAL A CG2 1 
ATOM   716  N  N   . TYR A 1 95  ? -17.347 -11.358 -0.574  1.00 12.00 ? 95  TYR A N   1 
ATOM   717  C  CA  . TYR A 1 95  ? -16.862 -11.833 0.717   1.00 12.59 ? 95  TYR A CA  1 
ATOM   718  C  C   . TYR A 1 95  ? -18.047 -12.273 1.573   1.00 13.01 ? 95  TYR A C   1 
ATOM   719  O  O   . TYR A 1 95  ? -19.110 -11.636 1.557   1.00 13.91 ? 95  TYR A O   1 
ATOM   720  C  CB  . TYR A 1 95  ? -16.139 -10.720 1.469   1.00 12.81 ? 95  TYR A CB  1 
ATOM   721  C  CG  . TYR A 1 95  ? -14.722 -10.437 1.028   1.00 13.37 ? 95  TYR A CG  1 
ATOM   722  C  CD1 . TYR A 1 95  ? -13.910 -11.445 0.508   1.00 14.09 ? 95  TYR A CD1 1 
ATOM   723  C  CD2 . TYR A 1 95  ? -14.182 -9.176  1.175   1.00 13.22 ? 95  TYR A CD2 1 
ATOM   724  C  CE1 . TYR A 1 95  ? -12.617 -11.185 0.128   1.00 14.78 ? 95  TYR A CE1 1 
ATOM   725  C  CE2 . TYR A 1 95  ? -12.855 -8.910  0.827   1.00 14.54 ? 95  TYR A CE2 1 
ATOM   726  C  CZ  . TYR A 1 95  ? -12.089 -9.914  0.297   1.00 14.50 ? 95  TYR A CZ  1 
ATOM   727  O  OH  . TYR A 1 95  ? -10.786 -9.658  -0.060  1.00 16.17 ? 95  TYR A OH  1 
ATOM   728  N  N   . ILE A 1 96  ? -17.868 -13.365 2.318   1.00 12.49 ? 96  ILE A N   1 
ATOM   729  C  CA  . ILE A 1 96  ? -18.853 -13.841 3.281   1.00 12.44 ? 96  ILE A CA  1 
ATOM   730  C  C   . ILE A 1 96  ? -18.138 -14.073 4.609   1.00 12.31 ? 96  ILE A C   1 
ATOM   731  O  O   . ILE A 1 96  ? -17.276 -14.955 4.707   1.00 13.59 ? 96  ILE A O   1 
ATOM   732  C  CB  . ILE A 1 96  ? -19.529 -15.139 2.825   1.00 12.72 ? 96  ILE A CB  1 
ATOM   733  C  CG1 . ILE A 1 96  ? -20.151 -15.018 1.427   1.00 12.65 ? 96  ILE A CG1 1 
ATOM   734  C  CG2 . ILE A 1 96  ? -20.567 -15.557 3.832   1.00 13.50 ? 96  ILE A CG2 1 
ATOM   735  C  CD1 . ILE A 1 96  ? -20.424 -16.344 0.720   1.00 14.20 ? 96  ILE A CD1 1 
ATOM   736  N  N   . ASN A 1 97  ? -18.481 -13.293 5.637   1.00 11.01 ? 97  ASN A N   1 
ATOM   737  C  CA  . ASN A 1 97  ? -17.951 -13.553 6.973   1.00 10.81 ? 97  ASN A CA  1 
ATOM   738  C  C   . ASN A 1 97  ? -18.870 -14.507 7.719   1.00 11.57 ? 97  ASN A C   1 
ATOM   739  O  O   . ASN A 1 97  ? -20.086 -14.312 7.740   1.00 12.45 ? 97  ASN A O   1 
ATOM   740  C  CB  . ASN A 1 97  ? -17.821 -12.240 7.751   1.00 11.45 ? 97  ASN A CB  1 
ATOM   741  C  CG  . ASN A 1 97  ? -16.667 -11.405 7.273   1.00 13.92 ? 97  ASN A CG  1 
ATOM   742  O  OD1 . ASN A 1 97  ? -15.667 -11.925 6.771   1.00 15.66 ? 97  ASN A OD1 1 
ATOM   743  N  ND2 . ASN A 1 97  ? -16.790 -10.109 7.439   1.00 14.95 ? 97  ASN A ND2 1 
ATOM   744  N  N   . TYR A 1 98  ? -18.283 -15.531 8.324   1.00 11.77 ? 98  TYR A N   1 
ATOM   745  C  CA  . TYR A 1 98  ? -19.028 -16.549 9.052   1.00 11.77 ? 98  TYR A CA  1 
ATOM   746  C  C   . TYR A 1 98  ? -18.866 -16.344 10.551  1.00 11.82 ? 98  TYR A C   1 
ATOM   747  O  O   . TYR A 1 98  ? -17.758 -16.092 11.027  1.00 12.44 ? 98  TYR A O   1 
ATOM   748  C  CB  . TYR A 1 98  ? -18.534 -17.957 8.686   1.00 12.26 ? 98  TYR A CB  1 
ATOM   749  C  CG  . TYR A 1 98  ? -18.825 -18.272 7.246   1.00 12.39 ? 98  TYR A CG  1 
ATOM   750  C  CD1 . TYR A 1 98  ? -20.095 -18.680 6.846   1.00 12.53 ? 98  TYR A CD1 1 
ATOM   751  C  CD2 . TYR A 1 98  ? -17.862 -18.091 6.264   1.00 11.95 ? 98  TYR A CD2 1 
ATOM   752  C  CE1 . TYR A 1 98  ? -20.396 -18.951 5.522   1.00 12.68 ? 98  TYR A CE1 1 
ATOM   753  C  CE2 . TYR A 1 98  ? -18.150 -18.347 4.919   1.00 12.63 ? 98  TYR A CE2 1 
ATOM   754  C  CZ  . TYR A 1 98  ? -19.420 -18.786 4.565   1.00 13.25 ? 98  TYR A CZ  1 
ATOM   755  O  OH  . TYR A 1 98  ? -19.750 -19.008 3.244   1.00 14.39 ? 98  TYR A OH  1 
ATOM   756  N  N   . TYR A 1 99  ? -19.966 -16.479 11.287  1.00 11.08 ? 99  TYR A N   1 
ATOM   757  C  CA  . TYR A 1 99  ? -19.965 -16.290 12.736  1.00 11.07 ? 99  TYR A CA  1 
ATOM   758  C  C   . TYR A 1 99  ? -20.675 -17.461 13.382  1.00 11.81 ? 99  TYR A C   1 
ATOM   759  O  O   . TYR A 1 99  ? -21.870 -17.672 13.137  1.00 12.41 ? 99  TYR A O   1 
ATOM   760  C  CB  . TYR A 1 99  ? -20.694 -14.989 13.100  1.00 11.88 ? 99  TYR A CB  1 
ATOM   761  C  CG  . TYR A 1 99  ? -20.043 -13.759 12.509  1.00 12.06 ? 99  TYR A CG  1 
ATOM   762  C  CD1 . TYR A 1 99  ? -20.372 -13.315 11.223  1.00 13.33 ? 99  TYR A CD1 1 
ATOM   763  C  CD2 . TYR A 1 99  ? -19.084 -13.034 13.217  1.00 14.53 ? 99  TYR A CD2 1 
ATOM   764  C  CE1 . TYR A 1 99  ? -19.783 -12.210 10.667  1.00 14.85 ? 99  TYR A CE1 1 
ATOM   765  C  CE2 . TYR A 1 99  ? -18.474 -11.906 12.654  1.00 15.73 ? 99  TYR A CE2 1 
ATOM   766  C  CZ  . TYR A 1 99  ? -18.827 -11.506 11.377  1.00 16.52 ? 99  TYR A CZ  1 
ATOM   767  O  OH  . TYR A 1 99  ? -18.230 -10.407 10.825  1.00 19.48 ? 99  TYR A OH  1 
ATOM   768  N  N   . ASP A 1 100 ? -19.950 -18.178 14.245  1.00 12.13 ? 100 ASP A N   1 
ATOM   769  C  CA  . ASP A 1 100 ? -20.511 -19.244 15.078  1.00 12.34 ? 100 ASP A CA  1 
ATOM   770  C  C   . ASP A 1 100 ? -20.927 -18.595 16.394  1.00 13.02 ? 100 ASP A C   1 
ATOM   771  O  O   . ASP A 1 100 ? -20.081 -18.214 17.207  1.00 13.87 ? 100 ASP A O   1 
ATOM   772  C  CB  . ASP A 1 100 ? -19.462 -20.325 15.316  1.00 13.86 ? 100 ASP A CB  1 
ATOM   773  C  CG  . ASP A 1 100 ? -20.003 -21.558 16.048  1.00 16.47 ? 100 ASP A CG  1 
ATOM   774  O  OD1 . ASP A 1 100 ? -21.179 -21.580 16.436  1.00 16.70 ? 100 ASP A OD1 1 
ATOM   775  O  OD2 . ASP A 1 100 ? -19.206 -22.518 16.241  1.00 19.22 ? 100 ASP A OD2 1 
ATOM   776  N  N   . MET A 1 101 ? -22.221 -18.392 16.570  1.00 11.81 ? 101 MET A N   1 
ATOM   777  C  CA  . MET A 1 101 ? -22.733 -17.667 17.721  1.00 11.78 ? 101 MET A CA  1 
ATOM   778  C  C   . MET A 1 101 ? -23.013 -18.618 18.881  1.00 12.52 ? 101 MET A C   1 
ATOM   779  O  O   . MET A 1 101 ? -23.559 -19.708 18.681  1.00 13.50 ? 101 MET A O   1 
ATOM   780  C  CB  . MET A 1 101 ? -24.060 -16.988 17.379  1.00 12.45 ? 101 MET A CB  1 
ATOM   781  C  CG  . MET A 1 101 ? -23.998 -15.993 16.237  1.00 13.69 ? 101 MET A CG  1 
ATOM   782  S  SD  . MET A 1 101 ? -22.846 -14.613 16.543  1.00 15.57 ? 101 MET A SD  1 
ATOM   783  C  CE  . MET A 1 101 ? -23.690 -13.892 17.964  1.00 16.54 ? 101 MET A CE  1 
ATOM   784  N  N   . ASN A 1 102 ? -22.670 -18.185 20.093  1.00 12.32 ? 102 ASN A N   1 
ATOM   785  C  CA  . ASN A 1 102 ? -23.144 -18.876 21.287  1.00 12.82 ? 102 ASN A CA  1 
ATOM   786  C  C   . ASN A 1 102 ? -24.645 -18.616 21.456  1.00 13.07 ? 102 ASN A C   1 
ATOM   787  O  O   . ASN A 1 102 ? -25.122 -17.500 21.212  1.00 12.72 ? 102 ASN A O   1 
ATOM   788  C  CB  . ASN A 1 102 ? -22.425 -18.336 22.524  1.00 14.74 ? 102 ASN A CB  1 
ATOM   789  C  CG  . ASN A 1 102 ? -20.958 -18.666 22.553  1.00 18.92 ? 102 ASN A CG  1 
ATOM   790  O  OD1 . ASN A 1 102 ? -20.477 -19.498 21.792  1.00 21.39 ? 102 ASN A OD1 1 
ATOM   791  N  ND2 . ASN A 1 102 ? -20.232 -18.008 23.453  1.00 20.12 ? 102 ASN A ND2 1 
ATOM   792  N  N   . ALA A 1 103 ? -25.400 -19.650 21.874  1.00 13.14 ? 103 ALA A N   1 
ATOM   793  C  CA  . ALA A 1 103 ? -26.843 -19.497 22.055  1.00 13.04 ? 103 ALA A CA  1 
ATOM   794  C  C   . ALA A 1 103 ? -27.164 -18.368 23.031  1.00 12.06 ? 103 ALA A C   1 
ATOM   795  O  O   . ALA A 1 103 ? -28.173 -17.665 22.865  1.00 12.90 ? 103 ALA A O   1 
ATOM   796  C  CB  . ALA A 1 103 ? -27.438 -20.820 22.554  1.00 13.03 ? 103 ALA A CB  1 
ATOM   797  N  N   . ALA A 1 104 ? -26.311 -18.156 24.045  1.00 13.19 ? 104 ALA A N   1 
ATOM   798  C  CA  . ALA A 1 104 ? -26.551 -17.093 25.011  1.00 13.00 ? 104 ALA A CA  1 
ATOM   799  C  C   . ALA A 1 104 ? -26.419 -15.704 24.399  1.00 13.09 ? 104 ALA A C   1 
ATOM   800  O  O   . ALA A 1 104 ? -26.893 -14.729 25.000  1.00 13.23 ? 104 ALA A O   1 
ATOM   801  C  CB  . ALA A 1 104 ? -25.591 -17.242 26.187  1.00 14.04 ? 104 ALA A CB  1 
ATOM   802  N  N   . ASN A 1 105 ? -25.812 -15.591 23.218  1.00 12.47 ? 105 ASN A N   1 
ATOM   803  C  CA  . ASN A 1 105 ? -25.611 -14.315 22.551  1.00 12.06 ? 105 ASN A CA  1 
ATOM   804  C  C   . ASN A 1 105 ? -26.584 -14.101 21.399  1.00 11.94 ? 105 ASN A C   1 
ATOM   805  O  O   . ASN A 1 105 ? -26.376 -13.186 20.598  1.00 11.85 ? 105 ASN A O   1 
ATOM   806  C  CB  . ASN A 1 105 ? -24.152 -14.159 22.105  1.00 13.30 ? 105 ASN A CB  1 
ATOM   807  C  CG  . ASN A 1 105 ? -23.224 -14.003 23.287  1.00 13.46 ? 105 ASN A CG  1 
ATOM   808  O  OD1 . ASN A 1 105 ? -23.644 -13.527 24.361  1.00 14.41 ? 105 ASN A OD1 1 
ATOM   809  N  ND2 . ASN A 1 105 ? -21.969 -14.405 23.121  1.00 14.33 ? 105 ASN A ND2 1 
ATOM   810  N  N   . VAL A 1 106 ? -27.652 -14.898 21.306  1.00 11.84 ? 106 VAL A N   1 
ATOM   811  C  CA  . VAL A 1 106 ? -28.679 -14.697 20.277  1.00 11.72 ? 106 VAL A CA  1 
ATOM   812  C  C   . VAL A 1 106 ? -30.020 -14.509 20.973  1.00 12.42 ? 106 VAL A C   1 
ATOM   813  O  O   . VAL A 1 106 ? -30.563 -15.454 21.556  1.00 13.28 ? 106 VAL A O   1 
ATOM   814  C  CB  . VAL A 1 106 ? -28.744 -15.826 19.229  1.00 12.22 ? 106 VAL A CB  1 
ATOM   815  C  CG1 . VAL A 1 106 ? -29.797 -15.484 18.166  1.00 12.66 ? 106 VAL A CG1 1 
ATOM   816  C  CG2 . VAL A 1 106 ? -27.387 -16.055 18.552  1.00 12.54 ? 106 VAL A CG2 1 
ATOM   817  N  N   . GLY A 1 107 ? -30.552 -13.292 20.897  1.00 11.81 ? 107 GLY A N   1 
ATOM   818  C  CA  . GLY A 1 107 ? -31.864 -12.997 21.422  1.00 12.89 ? 107 GLY A CA  1 
ATOM   819  C  C   . GLY A 1 107 ? -32.968 -13.258 20.409  1.00 12.35 ? 107 GLY A C   1 
ATOM   820  O  O   . GLY A 1 107 ? -32.800 -13.092 19.198  1.00 12.60 ? 107 GLY A O   1 
ATOM   821  N  N   . TRP A 1 108 ? -34.117 -13.666 20.934  1.00 12.94 ? 108 TRP A N   1 
ATOM   822  C  CA  . TRP A 1 108 ? -35.283 -14.004 20.137  1.00 12.92 ? 108 TRP A CA  1 
ATOM   823  C  C   . TRP A 1 108 ? -36.458 -14.130 21.096  1.00 13.76 ? 108 TRP A C   1 
ATOM   824  O  O   . TRP A 1 108 ? -36.317 -14.705 22.179  1.00 14.28 ? 108 TRP A O   1 
ATOM   825  C  CB  . TRP A 1 108 ? -35.046 -15.323 19.371  1.00 13.88 ? 108 TRP A CB  1 
ATOM   826  C  CG  . TRP A 1 108 ? -36.286 -15.860 18.679  1.00 14.26 ? 108 TRP A CG  1 
ATOM   827  C  CD1 . TRP A 1 108 ? -36.881 -15.347 17.568  1.00 14.44 ? 108 TRP A CD1 1 
ATOM   828  C  CD2 . TRP A 1 108 ? -37.066 -17.016 19.055  1.00 15.68 ? 108 TRP A CD2 1 
ATOM   829  N  NE1 . TRP A 1 108 ? -37.987 -16.097 17.234  1.00 14.57 ? 108 TRP A NE1 1 
ATOM   830  C  CE2 . TRP A 1 108 ? -38.121 -17.131 18.123  1.00 15.38 ? 108 TRP A CE2 1 
ATOM   831  C  CE3 . TRP A 1 108 ? -36.985 -17.945 20.100  1.00 17.54 ? 108 TRP A CE3 1 
ATOM   832  C  CZ2 . TRP A 1 108 ? -39.079 -18.131 18.199  1.00 16.66 ? 108 TRP A CZ2 1 
ATOM   833  C  CZ3 . TRP A 1 108 ? -37.933 -18.946 20.168  1.00 18.68 ? 108 TRP A CZ3 1 
ATOM   834  C  CH2 . TRP A 1 108 ? -38.961 -19.031 19.221  1.00 17.94 ? 108 TRP A CH2 1 
ATOM   835  N  N   . ASN A 1 109 ? -37.597 -13.549 20.745  1.00 13.90 ? 109 ASN A N   1 
ATOM   836  C  CA  . ASN A 1 109 ? -38.841 -13.833 21.456  1.00 15.11 ? 109 ASN A CA  1 
ATOM   837  C  C   . ASN A 1 109 ? -38.724 -13.536 22.956  1.00 15.16 ? 109 ASN A C   1 
ATOM   838  O  O   . ASN A 1 109 ? -39.109 -14.339 23.801  1.00 16.33 ? 109 ASN A O   1 
ATOM   839  C  CB  . ASN A 1 109 ? -39.276 -15.278 21.189  1.00 16.22 ? 109 ASN A CB  1 
ATOM   840  C  CG  . ASN A 1 109 ? -40.747 -15.513 21.448  1.00 18.32 ? 109 ASN A CG  1 
ATOM   841  O  OD1 . ASN A 1 109 ? -41.528 -14.586 21.653  1.00 18.38 ? 109 ASN A OD1 1 
ATOM   842  N  ND2 . ASN A 1 109 ? -41.150 -16.768 21.356  1.00 20.59 ? 109 ASN A ND2 1 
ATOM   843  N  N   . ASN A 1 110 ? -38.181 -12.366 23.285  1.00 15.25 ? 110 ASN A N   1 
ATOM   844  C  CA  . ASN A 1 110 ? -38.084 -11.849 24.658  1.00 15.89 ? 110 ASN A CA  1 
ATOM   845  C  C   . ASN A 1 110 ? -37.055 -12.549 25.534  1.00 15.67 ? 110 ASN A C   1 
ATOM   846  O  O   . ASN A 1 110 ? -37.021 -12.297 26.737  1.00 16.84 ? 110 ASN A O   1 
ATOM   847  C  CB  . ASN A 1 110 ? -39.446 -11.777 25.371  1.00 17.55 ? 110 ASN A CB  1 
ATOM   848  C  CG  . ASN A 1 110 ? -40.308 -10.629 24.861  1.00 20.65 ? 110 ASN A CG  1 
ATOM   849  O  OD1 . ASN A 1 110 ? -39.859 -9.479  24.838  1.00 21.75 ? 110 ASN A OD1 1 
ATOM   850  N  ND2 . ASN A 1 110 ? -41.540 -10.927 24.452  1.00 22.56 ? 110 ASN A ND2 1 
ATOM   851  N  N   . SER A 1 111 ? -36.217 -13.412 24.973  1.00 14.74 ? 111 SER A N   1 
ATOM   852  C  CA  . SER A 1 111 ? -35.204 -14.140 25.730  1.00 14.58 ? 111 SER A CA  1 
ATOM   853  C  C   . SER A 1 111 ? -34.025 -14.420 24.801  1.00 13.70 ? 111 SER A C   1 
ATOM   854  O  O   . SER A 1 111 ? -33.838 -13.739 23.786  1.00 14.27 ? 111 SER A O   1 
ATOM   855  C  CB  . SER A 1 111 ? -35.816 -15.427 26.307  1.00 16.91 ? 111 SER A CB  1 
ATOM   856  O  OG  . SER A 1 111 ? -34.915 -16.103 27.156  1.00 19.44 ? 111 SER A OG  1 
ATOM   857  N  N   . THR A 1 112 ? -33.215 -15.415 25.149  1.00 14.34 ? 112 THR A N   1 
ATOM   858  C  CA  . THR A 1 112 ? -32.178 -15.902 24.258  1.00 14.22 ? 112 THR A CA  1 
ATOM   859  C  C   . THR A 1 112 ? -32.348 -17.399 24.078  1.00 14.73 ? 112 THR A C   1 
ATOM   860  O  O   . THR A 1 112 ? -33.173 -18.041 24.729  1.00 16.37 ? 112 THR A O   1 
ATOM   861  C  CB  . THR A 1 112 ? -30.762 -15.624 24.797  1.00 14.19 ? 112 THR A CB  1 
ATOM   862  O  OG1 . THR A 1 112 ? -30.520 -16.445 25.949  1.00 14.95 ? 112 THR A OG1 1 
ATOM   863  C  CG2 . THR A 1 112 ? -30.566 -14.146 25.136  1.00 13.74 ? 112 THR A CG2 1 
ATOM   864  N  N   . PHE A 1 113 ? -31.539 -17.958 23.190  1.00 13.97 ? 113 PHE A N   1 
ATOM   865  C  CA  . PHE A 1 113 ? -31.595 -19.384 22.942  1.00 15.22 ? 113 PHE A CA  1 
ATOM   866  C  C   . PHE A 1 113 ? -30.846 -20.206 23.980  1.00 15.62 ? 113 PHE A C   1 
ATOM   867  O  O   . PHE A 1 113 ? -30.926 -21.433 23.939  1.00 16.53 ? 113 PHE A O   1 
ATOM   868  C  CB  . PHE A 1 113 ? -31.049 -19.676 21.542  1.00 15.94 ? 113 PHE A CB  1 
ATOM   869  C  CG  . PHE A 1 113 ? -32.015 -19.333 20.441  1.00 16.16 ? 113 PHE A CG  1 
ATOM   870  C  CD1 . PHE A 1 113 ? -33.185 -20.054 20.297  1.00 17.29 ? 113 PHE A CD1 1 
ATOM   871  C  CD2 . PHE A 1 113 ? -31.762 -18.297 19.563  1.00 16.19 ? 113 PHE A CD2 1 
ATOM   872  C  CE1 . PHE A 1 113 ? -34.087 -19.752 19.286  1.00 17.72 ? 113 PHE A CE1 1 
ATOM   873  C  CE2 . PHE A 1 113 ? -32.655 -17.983 18.546  1.00 16.95 ? 113 PHE A CE2 1 
ATOM   874  C  CZ  . PHE A 1 113 ? -33.820 -18.708 18.400  1.00 17.92 ? 113 PHE A CZ  1 
ATOM   875  N  N   . ALA A 1 114 ? -30.110 -19.588 24.897  1.00 15.54 ? 114 ALA A N   1 
ATOM   876  C  CA  . ALA A 1 114 ? -29.366 -20.383 25.872  1.00 15.87 ? 114 ALA A CA  1 
ATOM   877  C  C   . ALA A 1 114 ? -30.268 -21.259 26.731  1.00 17.20 ? 114 ALA A C   1 
ATOM   878  O  O   . ALA A 1 114 ? -31.354 -20.831 27.159  1.00 18.32 ? 114 ALA A O   1 
ATOM   879  C  CB  . ALA A 1 114 ? -28.547 -19.515 26.751  1.00 15.80 ? 114 ALA A CB  1 
ATOM   880  O  OXT . ALA A 1 114 ? -29.879 -22.394 27.015  1.00 17.79 ? 114 ALA A OXT 1 
ATOM   881  N  N   . PRO B 1 1   ? -9.519  -7.369  3.403   1.00 14.67 ? 1   PRO B N   1 
ATOM   882  C  CA  . PRO B 1 1   ? -10.247 -6.729  4.497   1.00 14.21 ? 1   PRO B CA  1 
ATOM   883  C  C   . PRO B 1 1   ? -11.507 -6.055  4.000   1.00 14.15 ? 1   PRO B C   1 
ATOM   884  O  O   . PRO B 1 1   ? -11.730 -5.892  2.787   1.00 14.53 ? 1   PRO B O   1 
ATOM   885  C  CB  . PRO B 1 1   ? -9.250  -5.699  5.027   1.00 15.76 ? 1   PRO B CB  1 
ATOM   886  C  CG  . PRO B 1 1   ? -7.914  -6.322  4.741   1.00 16.34 ? 1   PRO B CG  1 
ATOM   887  C  CD  . PRO B 1 1   ? -8.082  -7.037  3.428   1.00 15.90 ? 1   PRO B CD  1 
ATOM   888  N  N   . MET B 1 2   ? -12.368 -5.713  4.946   1.00 14.09 ? 2   MET B N   1 
ATOM   889  C  CA  . MET B 1 2   ? -13.577 -4.985  4.594   1.00 15.17 ? 2   MET B CA  1 
ATOM   890  C  C   . MET B 1 2   ? -13.797 -3.856  5.581   1.00 13.51 ? 2   MET B C   1 
ATOM   891  O  O   . MET B 1 2   ? -13.644 -4.033  6.794   1.00 14.13 ? 2   MET B O   1 
ATOM   892  C  CB  . MET B 1 2   ? -14.814 -5.880  4.452   1.00 20.30 ? 2   MET B CB  1 
ATOM   893  C  CG  . MET B 1 2   ? -15.454 -6.351  5.706   1.00 24.22 ? 2   MET B CG  1 
ATOM   894  S  SD  . MET B 1 2   ? -16.951 -7.290  5.327   1.00 27.93 ? 2   MET B SD  1 
ATOM   895  C  CE  . MET B 1 2   ? -16.292 -8.568  4.286   1.00 26.63 ? 2   MET B CE  1 
ATOM   896  N  N   . PHE B 1 3   ? -14.109 -2.689  5.052   1.00 13.69 ? 3   PHE B N   1 
ATOM   897  C  CA  . PHE B 1 3   ? -14.376 -1.520  5.873   1.00 14.05 ? 3   PHE B CA  1 
ATOM   898  C  C   . PHE B 1 3   ? -15.752 -0.968  5.536   1.00 13.15 ? 3   PHE B C   1 
ATOM   899  O  O   . PHE B 1 3   ? -16.060 -0.723  4.363   1.00 13.97 ? 3   PHE B O   1 
ATOM   900  C  CB  . PHE B 1 3   ? -13.327 -0.433  5.649   1.00 15.36 ? 3   PHE B CB  1 
ATOM   901  C  CG  . PHE B 1 3   ? -13.571 0.788   6.489   1.00 16.36 ? 3   PHE B CG  1 
ATOM   902  C  CD1 . PHE B 1 3   ? -13.467 0.723   7.875   1.00 16.95 ? 3   PHE B CD1 1 
ATOM   903  C  CD2 . PHE B 1 3   ? -13.983 1.971   5.904   1.00 17.37 ? 3   PHE B CD2 1 
ATOM   904  C  CE1 . PHE B 1 3   ? -13.727 1.832   8.664   1.00 17.28 ? 3   PHE B CE1 1 
ATOM   905  C  CE2 . PHE B 1 3   ? -14.246 3.084   6.679   1.00 17.84 ? 3   PHE B CE2 1 
ATOM   906  C  CZ  . PHE B 1 3   ? -14.109 3.016   8.060   1.00 18.02 ? 3   PHE B CZ  1 
ATOM   907  N  N   . ILE B 1 4   ? -16.578 -0.771  6.558   1.00 12.07 ? 4   ILE B N   1 
ATOM   908  C  CA  . ILE B 1 4   ? -17.933 -0.271  6.370   1.00 12.31 ? 4   ILE B CA  1 
ATOM   909  C  C   . ILE B 1 4   ? -18.064 0.981   7.217   1.00 12.21 ? 4   ILE B C   1 
ATOM   910  O  O   . ILE B 1 4   ? -17.643 0.982   8.384   1.00 13.48 ? 4   ILE B O   1 
ATOM   911  C  CB  . ILE B 1 4   ? -18.998 -1.315  6.778   1.00 14.27 ? 4   ILE B CB  1 
ATOM   912  C  CG1 . ILE B 1 4   ? -18.759 -2.685  6.095   1.00 16.40 ? 4   ILE B CG1 1 
ATOM   913  C  CG2 . ILE B 1 4   ? -20.399 -0.781  6.490   1.00 15.26 ? 4   ILE B CG2 1 
ATOM   914  C  CD1 . ILE B 1 4   ? -19.467 -3.828  6.791   1.00 18.46 ? 4   ILE B CD1 1 
ATOM   915  N  N   . VAL B 1 5   ? -18.641 2.034   6.644   1.00 12.92 ? 5   VAL B N   1 
ATOM   916  C  CA  . VAL B 1 5   ? -19.004 3.216   7.417   1.00 13.29 ? 5   VAL B CA  1 
ATOM   917  C  C   . VAL B 1 5   ? -20.484 3.525   7.222   1.00 12.84 ? 5   VAL B C   1 
ATOM   918  O  O   . VAL B 1 5   ? -20.959 3.679   6.089   1.00 14.27 ? 5   VAL B O   1 
ATOM   919  C  CB  . VAL B 1 5   ? -18.117 4.437   7.110   1.00 15.99 ? 5   VAL B CB  1 
ATOM   920  C  CG1 . VAL B 1 5   ? -17.948 4.679   5.632   1.00 17.56 ? 5   VAL B CG1 1 
ATOM   921  C  CG2 . VAL B 1 5   ? -18.663 5.679   7.795   1.00 16.20 ? 5   VAL B CG2 1 
ATOM   922  N  N   . ASN B 1 6   ? -21.218 3.587   8.325   1.00 13.08 ? 6   ASN B N   1 
ATOM   923  C  CA  . ASN B 1 6   ? -22.614 3.997   8.323   1.00 14.14 ? 6   ASN B CA  1 
ATOM   924  C  C   . ASN B 1 6   ? -22.684 5.371   8.952   1.00 13.49 ? 6   ASN B C   1 
ATOM   925  O  O   . ASN B 1 6   ? -22.078 5.592   10.006  1.00 13.79 ? 6   ASN B O   1 
ATOM   926  C  CB  . ASN B 1 6   ? -23.432 3.038   9.176   1.00 16.41 ? 6   ASN B CB  1 
ATOM   927  C  CG  . ASN B 1 6   ? -23.623 1.738   8.509   1.00 20.45 ? 6   ASN B CG  1 
ATOM   928  O  OD1 . ASN B 1 6   ? -24.582 1.556   7.784   1.00 21.36 ? 6   ASN B OD1 1 
ATOM   929  N  ND2 . ASN B 1 6   ? -22.686 0.824   8.717   1.00 22.52 ? 6   ASN B ND2 1 
ATOM   930  N  N   . THR B 1 7   ? -23.390 6.300   8.303   1.00 12.60 ? 7   THR B N   1 
ATOM   931  C  CA  . THR B 1 7   ? -23.387 7.674   8.786   1.00 13.42 ? 7   THR B CA  1 
ATOM   932  C  C   . THR B 1 7   ? -24.718 8.344   8.464   1.00 13.42 ? 7   THR B C   1 
ATOM   933  O  O   . THR B 1 7   ? -25.408 7.960   7.504   1.00 12.90 ? 7   THR B O   1 
ATOM   934  C  CB  . THR B 1 7   ? -22.202 8.453   8.185   1.00 13.11 ? 7   THR B CB  1 
ATOM   935  O  OG1 . THR B 1 7   ? -22.212 9.804   8.661   1.00 13.81 ? 7   THR B OG1 1 
ATOM   936  C  CG2 . THR B 1 7   ? -22.250 8.480   6.662   1.00 13.34 ? 7   THR B CG2 1 
ATOM   937  N  N   . ASN B 1 8   ? -25.069 9.371   9.265   1.00 14.36 ? 8   ASN B N   1 
ATOM   938  C  CA  . ASN B 1 8   ? -26.230 10.210  8.976   1.00 15.16 ? 8   ASN B CA  1 
ATOM   939  C  C   . ASN B 1 8   ? -25.914 11.360  8.014   1.00 16.54 ? 8   ASN B C   1 
ATOM   940  O  O   . ASN B 1 8   ? -26.837 12.040  7.554   1.00 18.07 ? 8   ASN B O   1 
ATOM   941  C  CB  . ASN B 1 8   ? -26.872 10.721  10.277  1.00 15.86 ? 8   ASN B CB  1 
ATOM   942  C  CG  . ASN B 1 8   ? -25.887 11.415  11.187  1.00 16.37 ? 8   ASN B CG  1 
ATOM   943  O  OD1 . ASN B 1 8   ? -24.684 11.373  10.973  1.00 15.58 ? 8   ASN B OD1 1 
ATOM   944  N  ND2 . ASN B 1 8   ? -26.407 12.091  12.201  1.00 17.89 ? 8   ASN B ND2 1 
ATOM   945  N  N   . VAL B 1 9   ? -24.647 11.547  7.655   1.00 17.25 ? 9   VAL B N   1 
ATOM   946  C  CA  . VAL B 1 9   ? -24.266 12.589  6.693   1.00 19.29 ? 9   VAL B CA  1 
ATOM   947  C  C   . VAL B 1 9   ? -24.922 12.306  5.345   1.00 19.25 ? 9   VAL B C   1 
ATOM   948  O  O   . VAL B 1 9   ? -25.014 11.128  4.935   1.00 18.74 ? 9   VAL B O   1 
ATOM   949  C  CB  . VAL B 1 9   ? -22.733 12.646  6.573   1.00 22.28 ? 9   VAL B CB  1 
ATOM   950  C  CG1 . VAL B 1 9   ? -22.284 13.472  5.386   1.00 24.08 ? 9   VAL B CG1 1 
ATOM   951  C  CG2 . VAL B 1 9   ? -22.138 13.181  7.868   1.00 22.55 ? 9   VAL B CG2 1 
ATOM   952  N  N   . PRO B 1 10  ? -25.419 13.312  4.626   1.00 20.69 ? 10  PRO B N   1 
ATOM   953  C  CA  . PRO B 1 10  ? -26.102 13.030  3.362   1.00 21.28 ? 10  PRO B CA  1 
ATOM   954  C  C   . PRO B 1 10  ? -25.142 12.587  2.273   1.00 20.85 ? 10  PRO B C   1 
ATOM   955  O  O   . PRO B 1 10  ? -23.944 12.891  2.283   1.00 20.68 ? 10  PRO B O   1 
ATOM   956  C  CB  . PRO B 1 10  ? -26.775 14.355  2.995   1.00 22.08 ? 10  PRO B CB  1 
ATOM   957  C  CG  . PRO B 1 10  ? -26.061 15.386  3.764   1.00 22.00 ? 10  PRO B CG  1 
ATOM   958  C  CD  . PRO B 1 10  ? -25.503 14.732  5.003   1.00 21.09 ? 10  PRO B CD  1 
ATOM   959  N  N   . ARG B 1 11  ? -25.721 11.852  1.319   1.00 21.79 ? 11  ARG B N   1 
ATOM   960  C  CA  . ARG B 1 11  ? -24.956 11.287  0.213   1.00 23.47 ? 11  ARG B CA  1 
ATOM   961  C  C   . ARG B 1 11  ? -24.198 12.360  -0.555  1.00 23.46 ? 11  ARG B C   1 
ATOM   962  O  O   . ARG B 1 11  ? -23.065 12.129  -0.998  1.00 23.95 ? 11  ARG B O   1 
ATOM   963  C  CB  . ARG B 1 11  ? -25.898 10.525  -0.720  1.00 25.33 ? 11  ARG B CB  1 
ATOM   964  C  CG  . ARG B 1 11  ? -25.271 10.072  -2.031  1.00 28.03 ? 11  ARG B CG  1 
ATOM   965  C  CD  . ARG B 1 11  ? -24.087 9.140   -1.829  1.00 30.11 ? 11  ARG B CD  1 
ATOM   966  N  NE  . ARG B 1 11  ? -23.526 8.690   -3.107  1.00 31.89 ? 11  ARG B NE  1 
ATOM   967  C  CZ  . ARG B 1 11  ? -22.444 9.219   -3.670  1.00 33.35 ? 11  ARG B CZ  1 
ATOM   968  N  NH1 . ARG B 1 11  ? -21.802 10.215  -3.066  1.00 33.79 ? 11  ARG B NH1 1 
ATOM   969  N  NH2 . ARG B 1 11  ? -22.000 8.758   -4.834  1.00 34.15 ? 11  ARG B NH2 1 
ATOM   970  N  N   . ALA B 1 12  ? -24.810 13.534  -0.739  1.00 23.58 ? 12  ALA B N   1 
ATOM   971  C  CA  . ALA B 1 12  ? -24.151 14.587  -1.504  1.00 24.11 ? 12  ALA B CA  1 
ATOM   972  C  C   . ALA B 1 12  ? -22.862 15.069  -0.852  1.00 25.03 ? 12  ALA B C   1 
ATOM   973  O  O   . ALA B 1 12  ? -22.004 15.633  -1.547  1.00 26.33 ? 12  ALA B O   1 
ATOM   974  C  CB  . ALA B 1 12  ? -25.104 15.765  -1.727  1.00 23.92 ? 12  ALA B CB  1 
ATOM   975  N  N   . SER B 1 13  ? -22.708 14.862  0.456   1.00 24.91 ? 13  SER B N   1 
ATOM   976  C  CA  . SER B 1 13  ? -21.530 15.287  1.203   1.00 26.02 ? 13  SER B CA  1 
ATOM   977  C  C   . SER B 1 13  ? -20.395 14.268  1.182   1.00 25.34 ? 13  SER B C   1 
ATOM   978  O  O   . SER B 1 13  ? -19.300 14.560  1.686   1.00 25.46 ? 13  SER B O   1 
ATOM   979  C  CB  . SER B 1 13  ? -21.921 15.611  2.648   1.00 28.15 ? 13  SER B CB  1 
ATOM   980  O  OG  . SER B 1 13  ? -22.844 16.689  2.696   1.00 30.54 ? 13  SER B OG  1 
ATOM   981  N  N   . VAL B 1 14  ? -20.611 13.095  0.602   1.00 24.03 ? 14  VAL B N   1 
ATOM   982  C  CA  . VAL B 1 14  ? -19.534 12.124  0.432   1.00 24.06 ? 14  VAL B CA  1 
ATOM   983  C  C   . VAL B 1 14  ? -18.773 12.522  -0.823  1.00 25.33 ? 14  VAL B C   1 
ATOM   984  O  O   . VAL B 1 14  ? -19.353 12.485  -1.917  1.00 26.61 ? 14  VAL B O   1 
ATOM   985  C  CB  . VAL B 1 14  ? -20.070 10.691  0.292   1.00 23.61 ? 14  VAL B CB  1 
ATOM   986  C  CG1 . VAL B 1 14  ? -18.908 9.719   0.115   1.00 23.50 ? 14  VAL B CG1 1 
ATOM   987  C  CG2 . VAL B 1 14  ? -20.907 10.309  1.497   1.00 23.40 ? 14  VAL B CG2 1 
ATOM   988  N  N   . PRO B 1 15  ? -17.500 12.906  -0.735  1.00 25.46 ? 15  PRO B N   1 
ATOM   989  C  CA  . PRO B 1 15  ? -16.826 13.440  -1.921  1.00 25.82 ? 15  PRO B CA  1 
ATOM   990  C  C   . PRO B 1 15  ? -16.571 12.351  -2.951  1.00 26.77 ? 15  PRO B C   1 
ATOM   991  O  O   . PRO B 1 15  ? -16.500 11.161  -2.630  1.00 26.58 ? 15  PRO B O   1 
ATOM   992  C  CB  . PRO B 1 15  ? -15.508 13.995  -1.365  1.00 25.86 ? 15  PRO B CB  1 
ATOM   993  C  CG  . PRO B 1 15  ? -15.273 13.262  -0.130  1.00 26.06 ? 15  PRO B CG  1 
ATOM   994  C  CD  . PRO B 1 15  ? -16.627 12.918  0.451   1.00 25.72 ? 15  PRO B CD  1 
ATOM   995  N  N   . ASP B 1 16  ? -16.461 12.777  -4.210  1.00 28.31 ? 16  ASP B N   1 
ATOM   996  C  CA  . ASP B 1 16  ? -16.075 11.861  -5.269  1.00 30.37 ? 16  ASP B CA  1 
ATOM   997  C  C   . ASP B 1 16  ? -14.706 11.296  -4.937  1.00 29.70 ? 16  ASP B C   1 
ATOM   998  O  O   . ASP B 1 16  ? -13.834 11.995  -4.412  1.00 30.22 ? 16  ASP B O   1 
ATOM   999  C  CB  . ASP B 1 16  ? -16.059 12.584  -6.620  1.00 33.32 ? 16  ASP B CB  1 
ATOM   1000 C  CG  . ASP B 1 16  ? -17.432 13.092  -7.029  1.00 35.99 ? 16  ASP B CG  1 
ATOM   1001 O  OD1 . ASP B 1 16  ? -17.494 13.983  -7.894  1.00 37.06 ? 16  ASP B OD1 1 
ATOM   1002 O  OD2 . ASP B 1 16  ? -18.452 12.661  -6.440  1.00 37.24 ? 16  ASP B OD2 1 
ATOM   1003 N  N   . GLY B 1 17  ? -14.523 10.021  -5.243  1.00 27.87 ? 17  GLY B N   1 
ATOM   1004 C  CA  . GLY B 1 17  ? -13.265 9.369   -4.966  1.00 25.62 ? 17  GLY B CA  1 
ATOM   1005 C  C   . GLY B 1 17  ? -13.097 8.905   -3.537  1.00 23.37 ? 17  GLY B C   1 
ATOM   1006 O  O   . GLY B 1 17  ? -12.021 8.417   -3.182  1.00 22.82 ? 17  GLY B O   1 
ATOM   1007 N  N   . PHE B 1 18  ? -14.126 9.032   -2.703  1.00 21.49 ? 18  PHE B N   1 
ATOM   1008 C  CA  . PHE B 1 18  ? -13.981 8.643   -1.303  1.00 20.76 ? 18  PHE B CA  1 
ATOM   1009 C  C   . PHE B 1 18  ? -13.739 7.147   -1.159  1.00 19.94 ? 18  PHE B C   1 
ATOM   1010 O  O   . PHE B 1 18  ? -12.904 6.729   -0.347  1.00 18.50 ? 18  PHE B O   1 
ATOM   1011 C  CB  . PHE B 1 18  ? -15.221 9.073   -0.524  1.00 21.06 ? 18  PHE B CB  1 
ATOM   1012 C  CG  . PHE B 1 18  ? -15.113 8.878   0.967   1.00 21.35 ? 18  PHE B CG  1 
ATOM   1013 C  CD1 . PHE B 1 18  ? -14.062 9.431   1.687   1.00 21.77 ? 18  PHE B CD1 1 
ATOM   1014 C  CD2 . PHE B 1 18  ? -16.077 8.145   1.646   1.00 21.19 ? 18  PHE B CD2 1 
ATOM   1015 C  CE1 . PHE B 1 18  ? -13.981 9.266   3.052   1.00 22.19 ? 18  PHE B CE1 1 
ATOM   1016 C  CE2 . PHE B 1 18  ? -15.998 7.971   3.017   1.00 21.62 ? 18  PHE B CE2 1 
ATOM   1017 C  CZ  . PHE B 1 18  ? -14.951 8.531   3.717   1.00 22.06 ? 18  PHE B CZ  1 
ATOM   1018 N  N   . LEU B 1 19  ? -14.446 6.323   -1.941  1.00 20.02 ? 19  LEU B N   1 
ATOM   1019 C  CA  . LEU B 1 19  ? -14.211 4.882   -1.863  1.00 19.67 ? 19  LEU B CA  1 
ATOM   1020 C  C   . LEU B 1 19  ? -12.775 4.560   -2.239  1.00 19.18 ? 19  LEU B C   1 
ATOM   1021 O  O   . LEU B 1 19  ? -12.143 3.682   -1.631  1.00 18.62 ? 19  LEU B O   1 
ATOM   1022 C  CB  . LEU B 1 19  ? -15.156 4.129   -2.798  1.00 20.69 ? 19  LEU B CB  1 
ATOM   1023 C  CG  . LEU B 1 19  ? -16.645 4.203   -2.476  1.00 21.08 ? 19  LEU B CG  1 
ATOM   1024 C  CD1 . LEU B 1 19  ? -17.429 3.369   -3.466  1.00 21.93 ? 19  LEU B CD1 1 
ATOM   1025 C  CD2 . LEU B 1 19  ? -16.903 3.737   -1.059  1.00 21.72 ? 19  LEU B CD2 1 
ATOM   1026 N  N   . SER B 1 20  ? -12.248 5.254   -3.252  1.00 19.70 ? 20  SER B N   1 
ATOM   1027 C  CA  . SER B 1 20  ? -10.880 5.002   -3.678  1.00 21.14 ? 20  SER B CA  1 
ATOM   1028 C  C   . SER B 1 20  ? -9.875  5.433   -2.623  1.00 20.96 ? 20  SER B C   1 
ATOM   1029 O  O   . SER B 1 20  ? -8.881  4.741   -2.394  1.00 20.73 ? 20  SER B O   1 
ATOM   1030 C  CB  . SER B 1 20  ? -10.599 5.710   -4.999  1.00 23.95 ? 20  SER B CB  1 
ATOM   1031 O  OG  . SER B 1 20  ? -11.311 5.094   -6.049  1.00 26.62 ? 20  SER B OG  1 
ATOM   1032 N  N   . GLU B 1 21  ? -10.114 6.564   -1.958  1.00 21.33 ? 21  GLU B N   1 
ATOM   1033 C  CA  . GLU B 1 21  ? -9.202  6.977   -0.897  1.00 21.31 ? 21  GLU B CA  1 
ATOM   1034 C  C   . GLU B 1 21  ? -9.207  5.968   0.244   1.00 19.94 ? 21  GLU B C   1 
ATOM   1035 O  O   . GLU B 1 21  ? -8.143  5.603   0.760   1.00 20.86 ? 21  GLU B O   1 
ATOM   1036 C  CB  . GLU B 1 21  ? -9.578  8.357   -0.378  1.00 22.81 ? 21  GLU B CB  1 
ATOM   1037 C  CG  . GLU B 1 21  ? -8.479  8.976   0.466   1.00 24.71 ? 21  GLU B CG  1 
ATOM   1038 C  CD  . GLU B 1 21  ? -8.791  10.394  0.861   1.00 26.41 ? 21  GLU B CD  1 
ATOM   1039 O  OE1 . GLU B 1 21  ? -9.940  10.824  0.624   1.00 27.07 ? 21  GLU B OE1 1 
ATOM   1040 O  OE2 . GLU B 1 21  ? -7.874  11.078  1.371   1.00 27.07 ? 21  GLU B OE2 1 
ATOM   1041 N  N   . LEU B 1 22  ? -10.395 5.510   0.655   1.00 18.56 ? 22  LEU B N   1 
ATOM   1042 C  CA  . LEU B 1 22  ? -10.465 4.479   1.687   1.00 17.66 ? 22  LEU B CA  1 
ATOM   1043 C  C   . LEU B 1 22  ? -9.716  3.227   1.259   1.00 17.73 ? 22  LEU B C   1 
ATOM   1044 O  O   . LEU B 1 22  ? -8.998  2.617   2.064   1.00 18.37 ? 22  LEU B O   1 
ATOM   1045 C  CB  . LEU B 1 22  ? -11.929 4.119   1.982   1.00 18.00 ? 22  LEU B CB  1 
ATOM   1046 C  CG  . LEU B 1 22  ? -12.724 5.194   2.735   1.00 19.45 ? 22  LEU B CG  1 
ATOM   1047 C  CD1 . LEU B 1 22  ? -14.204 4.852   2.792   1.00 20.34 ? 22  LEU B CD1 1 
ATOM   1048 C  CD2 . LEU B 1 22  ? -12.160 5.391   4.125   1.00 20.22 ? 22  LEU B CD2 1 
ATOM   1049 N  N   . THR B 1 23  ? -9.893  2.810   0.002   1.00 17.45 ? 23  THR B N   1 
ATOM   1050 C  CA  . THR B 1 23  ? -9.240  1.593   -0.469  1.00 17.64 ? 23  THR B CA  1 
ATOM   1051 C  C   . THR B 1 23  ? -7.731  1.717   -0.364  1.00 17.47 ? 23  THR B C   1 
ATOM   1052 O  O   . THR B 1 23  ? -7.054  0.832   0.177   1.00 17.66 ? 23  THR B O   1 
ATOM   1053 C  CB  . THR B 1 23  ? -9.655  1.294   -1.918  1.00 17.65 ? 23  THR B CB  1 
ATOM   1054 O  OG1 . THR B 1 23  ? -11.060 1.057   -1.987  1.00 17.82 ? 23  THR B OG1 1 
ATOM   1055 C  CG2 . THR B 1 23  ? -8.960  0.050   -2.425  1.00 17.86 ? 23  THR B CG2 1 
ATOM   1056 N  N   . GLN B 1 24  ? -7.184  2.813   -0.890  1.00 18.54 ? 24  GLN B N   1 
ATOM   1057 C  CA  . GLN B 1 24  ? -5.736  2.985   -0.901  1.00 20.59 ? 24  GLN B CA  1 
ATOM   1058 C  C   . GLN B 1 24  ? -5.180  3.177   0.501   1.00 19.96 ? 24  GLN B C   1 
ATOM   1059 O  O   . GLN B 1 24  ? -4.167  2.566   0.859   1.00 20.08 ? 24  GLN B O   1 
ATOM   1060 C  CB  . GLN B 1 24  ? -5.346  4.117   -1.846  1.00 23.55 ? 24  GLN B CB  1 
ATOM   1061 C  CG  . GLN B 1 24  ? -5.610  3.792   -3.325  1.00 26.55 ? 24  GLN B CG  1 
ATOM   1062 C  CD  . GLN B 1 24  ? -5.099  2.404   -3.750  1.00 29.23 ? 24  GLN B CD  1 
ATOM   1063 O  OE1 . GLN B 1 24  ? -3.952  2.041   -3.486  1.00 31.16 ? 24  GLN B OE1 1 
ATOM   1064 N  NE2 . GLN B 1 24  ? -5.950  1.639   -4.424  1.00 29.79 ? 24  GLN B NE2 1 
ATOM   1065 N  N   . GLN B 1 25  ? -5.839  4.009   1.315   1.00 19.50 ? 25  GLN B N   1 
ATOM   1066 C  CA  . GLN B 1 25  ? -5.339  4.261   2.662   1.00 19.62 ? 25  GLN B CA  1 
ATOM   1067 C  C   . GLN B 1 25  ? -5.384  2.993   3.506   1.00 18.64 ? 25  GLN B C   1 
ATOM   1068 O  O   . GLN B 1 25  ? -4.476  2.745   4.310   1.00 18.30 ? 25  GLN B O   1 
ATOM   1069 C  CB  . GLN B 1 25  ? -6.149  5.378   3.316   1.00 20.94 ? 25  GLN B CB  1 
ATOM   1070 C  CG  . GLN B 1 25  ? -5.918  6.751   2.662   1.00 22.77 ? 25  GLN B CG  1 
ATOM   1071 C  CD  . GLN B 1 25  ? -4.508  7.269   2.894   1.00 25.79 ? 25  GLN B CD  1 
ATOM   1072 O  OE1 . GLN B 1 25  ? -3.907  7.016   3.941   1.00 27.14 ? 25  GLN B OE1 1 
ATOM   1073 N  NE2 . GLN B 1 25  ? -3.955  7.946   1.903   1.00 26.96 ? 25  GLN B NE2 1 
ATOM   1074 N  N   . LEU B 1 26  ? -6.428  2.172   3.333   1.00 18.11 ? 26  LEU B N   1 
ATOM   1075 C  CA  . LEU B 1 26  ? -6.495  0.930   4.096   1.00 17.07 ? 26  LEU B CA  1 
ATOM   1076 C  C   . LEU B 1 26  ? -5.481  -0.094  3.595   1.00 17.57 ? 26  LEU B C   1 
ATOM   1077 O  O   . LEU B 1 26  ? -4.921  -0.856  4.394   1.00 18.50 ? 26  LEU B O   1 
ATOM   1078 C  CB  . LEU B 1 26  ? -7.910  0.354   4.065   1.00 16.79 ? 26  LEU B CB  1 
ATOM   1079 C  CG  . LEU B 1 26  ? -8.837  1.145   4.985   1.00 17.43 ? 26  LEU B CG  1 
ATOM   1080 C  CD1 . LEU B 1 26  ? -10.282 0.855   4.659   1.00 18.52 ? 26  LEU B CD1 1 
ATOM   1081 C  CD2 . LEU B 1 26  ? -8.555  0.909   6.471   1.00 18.17 ? 26  LEU B CD2 1 
ATOM   1082 N  N   . ALA B 1 27  ? -5.252  -0.151  2.276   1.00 17.23 ? 27  ALA B N   1 
ATOM   1083 C  CA  . ALA B 1 27  ? -4.226  -1.046  1.754   1.00 18.78 ? 27  ALA B CA  1 
ATOM   1084 C  C   . ALA B 1 27  ? -2.880  -0.705  2.367   1.00 19.52 ? 27  ALA B C   1 
ATOM   1085 O  O   . ALA B 1 27  ? -2.159  -1.597  2.824   1.00 19.98 ? 27  ALA B O   1 
ATOM   1086 C  CB  . ALA B 1 27  ? -4.162  -0.975  0.221   1.00 18.63 ? 27  ALA B CB  1 
ATOM   1087 N  N   . GLN B 1 28  ? -2.556  0.593   2.457   1.00 20.48 ? 28  GLN B N   1 
ATOM   1088 C  CA  . GLN B 1 28  ? -1.272  0.985   3.038   1.00 22.85 ? 28  GLN B CA  1 
ATOM   1089 C  C   . GLN B 1 28  ? -1.221  0.670   4.525   1.00 22.04 ? 28  GLN B C   1 
ATOM   1090 O  O   . GLN B 1 28  ? -0.209  0.152   5.022   1.00 23.25 ? 28  GLN B O   1 
ATOM   1091 C  CB  . GLN B 1 28  ? -1.037  2.487   2.856   1.00 25.96 ? 28  GLN B CB  1 
ATOM   1092 C  CG  . GLN B 1 28  ? -0.940  2.982   1.438   1.00 29.01 ? 28  GLN B CG  1 
ATOM   1093 C  CD  . GLN B 1 28  ? -0.515  4.441   1.402   1.00 30.90 ? 28  GLN B CD  1 
ATOM   1094 O  OE1 . GLN B 1 28  ? 0.100   4.946   2.356   1.00 31.99 ? 28  GLN B OE1 1 
ATOM   1095 N  NE2 . GLN B 1 28  ? -0.845  5.131   0.313   1.00 31.37 ? 28  GLN B NE2 1 
ATOM   1096 N  N   . ALA B 1 29  ? -2.308  0.961   5.244   1.00 20.84 ? 29  ALA B N   1 
ATOM   1097 C  CA  . ALA B 1 29  ? -2.317  0.799   6.695   1.00 19.80 ? 29  ALA B CA  1 
ATOM   1098 C  C   . ALA B 1 29  ? -2.279  -0.666  7.099   1.00 19.95 ? 29  ALA B C   1 
ATOM   1099 O  O   . ALA B 1 29  ? -1.564  -1.029  8.039   1.00 19.85 ? 29  ALA B O   1 
ATOM   1100 C  CB  . ALA B 1 29  ? -3.530  1.496   7.298   1.00 19.67 ? 29  ALA B CB  1 
ATOM   1101 N  N   . THR B 1 30  ? -3.060  -1.516  6.425   1.00 20.00 ? 30  THR B N   1 
ATOM   1102 C  CA  . THR B 1 30  ? -3.099  -2.933  6.771   1.00 20.06 ? 30  THR B CA  1 
ATOM   1103 C  C   . THR B 1 30  ? -1.975  -3.720  6.116   1.00 20.28 ? 30  THR B C   1 
ATOM   1104 O  O   . THR B 1 30  ? -1.726  -4.862  6.510   1.00 21.36 ? 30  THR B O   1 
ATOM   1105 C  CB  . THR B 1 30  ? -4.436  -3.563  6.363   1.00 19.73 ? 30  THR B CB  1 
ATOM   1106 O  OG1 . THR B 1 30  ? -4.556  -3.551  4.934   1.00 18.73 ? 30  THR B OG1 1 
ATOM   1107 C  CG2 . THR B 1 30  ? -5.601  -2.824  6.984   1.00 20.64 ? 30  THR B CG2 1 
ATOM   1108 N  N   . GLY B 1 31  ? -1.304  -3.157  5.115   1.00 19.56 ? 31  GLY B N   1 
ATOM   1109 C  CA  . GLY B 1 31  ? -0.336  -3.911  4.360   1.00 18.60 ? 31  GLY B CA  1 
ATOM   1110 C  C   . GLY B 1 31  ? -0.925  -4.881  3.362   1.00 19.20 ? 31  GLY B C   1 
ATOM   1111 O  O   . GLY B 1 31  ? -0.170  -5.515  2.635   1.00 20.72 ? 31  GLY B O   1 
ATOM   1112 N  N   . LYS B 1 32  ? -2.235  -4.992  3.273   1.00 18.43 ? 32  LYS B N   1 
ATOM   1113 C  CA  . LYS B 1 32  ? -2.856  -5.943  2.357   1.00 17.86 ? 32  LYS B CA  1 
ATOM   1114 C  C   . LYS B 1 32  ? -2.940  -5.334  0.952   1.00 18.42 ? 32  LYS B C   1 
ATOM   1115 O  O   . LYS B 1 32  ? -2.967  -4.109  0.799   1.00 19.15 ? 32  LYS B O   1 
ATOM   1116 C  CB  . LYS B 1 32  ? -4.258  -6.276  2.850   1.00 18.19 ? 32  LYS B CB  1 
ATOM   1117 C  CG  . LYS B 1 32  ? -4.315  -6.853  4.266   1.00 19.15 ? 32  LYS B CG  1 
ATOM   1118 C  CD  . LYS B 1 32  ? -4.134  -8.353  4.260   1.00 19.12 ? 32  LYS B CD  1 
ATOM   1119 C  CE  . LYS B 1 32  ? -4.398  -8.939  5.647   1.00 18.50 ? 32  LYS B CE  1 
ATOM   1120 N  NZ  . LYS B 1 32  ? -4.318  -10.421 5.601   1.00 18.27 ? 32  LYS B NZ  1 
ATOM   1121 N  N   . PRO B 1 33  ? -2.986  -6.163  -0.089  1.00 18.18 ? 33  PRO B N   1 
ATOM   1122 C  CA  . PRO B 1 33  ? -3.096  -5.638  -1.465  1.00 17.78 ? 33  PRO B CA  1 
ATOM   1123 C  C   . PRO B 1 33  ? -4.426  -4.941  -1.667  1.00 16.14 ? 33  PRO B C   1 
ATOM   1124 O  O   . PRO B 1 33  ? -5.451  -5.395  -1.140  1.00 15.89 ? 33  PRO B O   1 
ATOM   1125 C  CB  . PRO B 1 33  ? -3.039  -6.899  -2.331  1.00 17.69 ? 33  PRO B CB  1 
ATOM   1126 C  CG  . PRO B 1 33  ? -2.481  -7.981  -1.436  1.00 18.30 ? 33  PRO B CG  1 
ATOM   1127 C  CD  . PRO B 1 33  ? -2.957  -7.636  -0.063  1.00 18.48 ? 33  PRO B CD  1 
ATOM   1128 N  N   . PRO B 1 34  ? -4.454  -3.833  -2.416  1.00 16.38 ? 34  PRO B N   1 
ATOM   1129 C  CA  . PRO B 1 34  ? -5.736  -3.150  -2.658  1.00 16.14 ? 34  PRO B CA  1 
ATOM   1130 C  C   . PRO B 1 34  ? -6.777  -4.055  -3.287  1.00 14.78 ? 34  PRO B C   1 
ATOM   1131 O  O   . PRO B 1 34  ? -7.977  -3.847  -3.063  1.00 15.21 ? 34  PRO B O   1 
ATOM   1132 C  CB  . PRO B 1 34  ? -5.372  -2.002  -3.614  1.00 17.41 ? 34  PRO B CB  1 
ATOM   1133 C  CG  . PRO B 1 34  ? -3.923  -2.100  -3.853  1.00 17.49 ? 34  PRO B CG  1 
ATOM   1134 C  CD  . PRO B 1 34  ? -3.295  -3.125  -2.981  1.00 16.64 ? 34  PRO B CD  1 
ATOM   1135 N  N   . GLN B 1 35  ? -6.344  -5.043  -4.087  1.00 13.62 ? 35  GLN B N   1 
ATOM   1136 C  CA  . GLN B 1 35  ? -7.271  -5.995  -4.687  1.00 14.91 ? 35  GLN B CA  1 
ATOM   1137 C  C   . GLN B 1 35  ? -8.107  -6.743  -3.664  1.00 15.37 ? 35  GLN B C   1 
ATOM   1138 O  O   . GLN B 1 35  ? -9.153  -7.288  -4.024  1.00 16.44 ? 35  GLN B O   1 
ATOM   1139 C  CB  . GLN B 1 35  ? -6.542  -6.992  -5.589  1.00 15.79 ? 35  GLN B CB  1 
ATOM   1140 C  CG  . GLN B 1 35  ? -5.885  -6.378  -6.838  1.00 18.32 ? 35  GLN B CG  1 
ATOM   1141 C  CD  . GLN B 1 35  ? -4.514  -5.761  -6.610  1.00 19.36 ? 35  GLN B CD  1 
ATOM   1142 O  OE1 . GLN B 1 35  ? -4.002  -5.710  -5.489  1.00 19.32 ? 35  GLN B OE1 1 
ATOM   1143 N  NE2 . GLN B 1 35  ? -3.872  -5.359  -7.704  1.00 20.75 ? 35  GLN B NE2 1 
ATOM   1144 N  N   . TYR B 1 36  ? -7.649  -6.831  -2.417  1.00 14.18 ? 36  TYR B N   1 
ATOM   1145 C  CA  . TYR B 1 36  ? -8.350  -7.565  -1.375  1.00 14.10 ? 36  TYR B CA  1 
ATOM   1146 C  C   . TYR B 1 36  ? -9.134  -6.657  -0.443  1.00 14.72 ? 36  TYR B C   1 
ATOM   1147 O  O   . TYR B 1 36  ? -9.739  -7.149  0.517   1.00 15.96 ? 36  TYR B O   1 
ATOM   1148 C  CB  . TYR B 1 36  ? -7.357  -8.404  -0.572  1.00 14.74 ? 36  TYR B CB  1 
ATOM   1149 C  CG  . TYR B 1 36  ? -6.856  -9.622  -1.312  1.00 15.29 ? 36  TYR B CG  1 
ATOM   1150 C  CD1 . TYR B 1 36  ? -5.794  -9.519  -2.212  1.00 15.85 ? 36  TYR B CD1 1 
ATOM   1151 C  CD2 . TYR B 1 36  ? -7.429  -10.865 -1.121  1.00 16.15 ? 36  TYR B CD2 1 
ATOM   1152 C  CE1 . TYR B 1 36  ? -5.311  -10.623 -2.888  1.00 17.52 ? 36  TYR B CE1 1 
ATOM   1153 C  CE2 . TYR B 1 36  ? -6.946  -11.979 -1.791  1.00 17.98 ? 36  TYR B CE2 1 
ATOM   1154 C  CZ  . TYR B 1 36  ? -5.901  -11.843 -2.688  1.00 19.00 ? 36  TYR B CZ  1 
ATOM   1155 O  OH  . TYR B 1 36  ? -5.410  -12.937 -3.347  1.00 20.97 ? 36  TYR B OH  1 
ATOM   1156 N  N   A ILE B 1 37  ? -9.166  -5.356  -0.699  0.60 15.25 ? 37  ILE B N   1 
ATOM   1157 N  N   B ILE B 1 37  ? -9.117  -5.346  -0.672  0.40 14.83 ? 37  ILE B N   1 
ATOM   1158 C  CA  A ILE B 1 37  ? -9.833  -4.414  0.190   0.60 17.44 ? 37  ILE B CA  1 
ATOM   1159 C  CA  B ILE B 1 37  ? -9.830  -4.406  0.192   0.40 17.08 ? 37  ILE B CA  1 
ATOM   1160 C  C   A ILE B 1 37  ? -11.201 -4.075  -0.381  0.60 14.56 ? 37  ILE B C   1 
ATOM   1161 C  C   B ILE B 1 37  ? -11.206 -4.138  -0.399  0.40 14.38 ? 37  ILE B C   1 
ATOM   1162 O  O   A ILE B 1 37  ? -11.311 -3.609  -1.522  0.60 13.84 ? 37  ILE B O   1 
ATOM   1163 O  O   B ILE B 1 37  ? -11.327 -3.728  -1.557  0.40 13.70 ? 37  ILE B O   1 
ATOM   1164 C  CB  A ILE B 1 37  ? -8.985  -3.154  0.414   0.60 23.43 ? 37  ILE B CB  1 
ATOM   1165 C  CB  B ILE B 1 37  ? -9.043  -3.090  0.321   0.40 23.00 ? 37  ILE B CB  1 
ATOM   1166 C  CG1 A ILE B 1 37  ? -7.705  -3.539  1.157   0.60 26.86 ? 37  ILE B CG1 1 
ATOM   1167 C  CG1 B ILE B 1 37  ? -7.646  -3.312  0.908   0.40 26.47 ? 37  ILE B CG1 1 
ATOM   1168 C  CG2 A ILE B 1 37  ? -9.791  -2.092  1.155   0.60 25.39 ? 37  ILE B CG2 1 
ATOM   1169 C  CG2 B ILE B 1 37  ? -9.829  -2.067  1.159   0.40 25.13 ? 37  ILE B CG2 1 
ATOM   1170 C  CD1 A ILE B 1 37  ? -7.361  -2.645  2.309   0.60 28.66 ? 37  ILE B CD1 1 
ATOM   1171 C  CD1 B ILE B 1 37  ? -7.616  -3.433  2.412   0.40 28.14 ? 37  ILE B CD1 1 
ATOM   1172 N  N   . ALA B 1 38  ? -12.246 -4.312  0.408   1.00 13.14 ? 38  ALA B N   1 
ATOM   1173 C  CA  . ALA B 1 38  ? -13.602 -3.919  0.045   1.00 13.05 ? 38  ALA B CA  1 
ATOM   1174 C  C   . ALA B 1 38  ? -14.071 -2.803  0.969   1.00 13.13 ? 38  ALA B C   1 
ATOM   1175 O  O   . ALA B 1 38  ? -13.785 -2.814  2.171   1.00 13.63 ? 38  ALA B O   1 
ATOM   1176 C  CB  . ALA B 1 38  ? -14.546 -5.118  0.095   1.00 13.83 ? 38  ALA B CB  1 
ATOM   1177 N  N   . VAL B 1 39  ? -14.771 -1.823  0.406   1.00 12.42 ? 39  VAL B N   1 
ATOM   1178 C  CA  . VAL B 1 39  ? -15.213 -0.653  1.159   1.00 12.65 ? 39  VAL B CA  1 
ATOM   1179 C  C   . VAL B 1 39  ? -16.680 -0.395  0.861   1.00 12.51 ? 39  VAL B C   1 
ATOM   1180 O  O   . VAL B 1 39  ? -17.157 -0.629  -0.253  1.00 13.65 ? 39  VAL B O   1 
ATOM   1181 C  CB  . VAL B 1 39  ? -14.337 0.602   0.865   1.00 14.30 ? 39  VAL B CB  1 
ATOM   1182 C  CG1 . VAL B 1 39  ? -12.868 0.403   1.262   1.00 14.62 ? 39  VAL B CG1 1 
ATOM   1183 C  CG2 . VAL B 1 39  ? -14.439 1.022   -0.596  1.00 16.29 ? 39  VAL B CG2 1 
ATOM   1184 N  N   . HIS B 1 40  ? -17.402 0.087   1.871   1.00 12.69 ? 40  HIS B N   1 
ATOM   1185 C  CA  . HIS B 1 40  ? -18.850 0.231   1.782   1.00 12.40 ? 40  HIS B CA  1 
ATOM   1186 C  C   . HIS B 1 40  ? -19.236 1.442   2.609   1.00 11.95 ? 40  HIS B C   1 
ATOM   1187 O  O   . HIS B 1 40  ? -18.940 1.487   3.806   1.00 13.53 ? 40  HIS B O   1 
ATOM   1188 C  CB  . HIS B 1 40  ? -19.488 -1.058  2.315   1.00 13.00 ? 40  HIS B CB  1 
ATOM   1189 C  CG  . HIS B 1 40  ? -20.982 -1.061  2.314   1.00 13.24 ? 40  HIS B CG  1 
ATOM   1190 N  ND1 . HIS B 1 40  ? -21.710 -2.016  2.995   1.00 14.02 ? 40  HIS B ND1 1 
ATOM   1191 C  CD2 . HIS B 1 40  ? -21.886 -0.261  1.705   1.00 13.25 ? 40  HIS B CD2 1 
ATOM   1192 C  CE1 . HIS B 1 40  ? -22.997 -1.769  2.853   1.00 13.77 ? 40  HIS B CE1 1 
ATOM   1193 N  NE2 . HIS B 1 40  ? -23.133 -0.733  2.043   1.00 13.20 ? 40  HIS B NE2 1 
ATOM   1194 N  N   . VAL B 1 41  ? -19.860 2.432   1.973   1.00 12.36 ? 41  VAL B N   1 
ATOM   1195 C  CA  . VAL B 1 41  ? -20.233 3.683   2.627   1.00 12.77 ? 41  VAL B CA  1 
ATOM   1196 C  C   . VAL B 1 41  ? -21.738 3.807   2.544   1.00 13.24 ? 41  VAL B C   1 
ATOM   1197 O  O   . VAL B 1 41  ? -22.313 3.681   1.454   1.00 13.28 ? 41  VAL B O   1 
ATOM   1198 C  CB  . VAL B 1 41  ? -19.542 4.906   1.995   1.00 14.60 ? 41  VAL B CB  1 
ATOM   1199 C  CG1 . VAL B 1 41  ? -19.998 6.181   2.670   1.00 16.11 ? 41  VAL B CG1 1 
ATOM   1200 C  CG2 . VAL B 1 41  ? -18.019 4.773   2.099   1.00 15.62 ? 41  VAL B CG2 1 
ATOM   1201 N  N   . VAL B 1 42  ? -22.369 4.057   3.688   1.00 13.02 ? 42  VAL B N   1 
ATOM   1202 C  CA  . VAL B 1 42  ? -23.830 4.076   3.783   1.00 13.34 ? 42  VAL B CA  1 
ATOM   1203 C  C   . VAL B 1 42  ? -24.245 5.416   4.365   1.00 13.32 ? 42  VAL B C   1 
ATOM   1204 O  O   . VAL B 1 42  ? -24.245 5.579   5.597   1.00 13.44 ? 42  VAL B O   1 
ATOM   1205 C  CB  . VAL B 1 42  ? -24.376 2.919   4.639   1.00 14.17 ? 42  VAL B CB  1 
ATOM   1206 C  CG1 . VAL B 1 42  ? -25.895 2.825   4.496   1.00 15.20 ? 42  VAL B CG1 1 
ATOM   1207 C  CG2 . VAL B 1 42  ? -23.688 1.589   4.291   1.00 14.50 ? 42  VAL B CG2 1 
ATOM   1208 N  N   . PRO B 1 43  ? -24.579 6.402   3.526   1.00 13.26 ? 43  PRO B N   1 
ATOM   1209 C  CA  . PRO B 1 43  ? -24.983 7.721   4.040   1.00 13.69 ? 43  PRO B CA  1 
ATOM   1210 C  C   . PRO B 1 43  ? -26.475 7.814   4.355   1.00 14.30 ? 43  PRO B C   1 
ATOM   1211 O  O   . PRO B 1 43  ? -27.222 6.838   4.183   1.00 14.76 ? 43  PRO B O   1 
ATOM   1212 C  CB  . PRO B 1 43  ? -24.592 8.659   2.887   1.00 13.99 ? 43  PRO B CB  1 
ATOM   1213 C  CG  . PRO B 1 43  ? -24.751 7.822   1.670   1.00 15.73 ? 43  PRO B CG  1 
ATOM   1214 C  CD  . PRO B 1 43  ? -24.476 6.385   2.056   1.00 14.25 ? 43  PRO B CD  1 
ATOM   1215 N  N   . ASP B 1 44  ? -26.918 8.976   4.847   1.00 15.03 ? 44  ASP B N   1 
ATOM   1216 C  CA  . ASP B 1 44  ? -28.345 9.267   5.027   1.00 16.36 ? 44  ASP B CA  1 
ATOM   1217 C  C   . ASP B 1 44  ? -29.021 8.356   6.047   1.00 15.41 ? 44  ASP B C   1 
ATOM   1218 O  O   . ASP B 1 44  ? -30.230 8.140   5.981   1.00 15.96 ? 44  ASP B O   1 
ATOM   1219 C  CB  . ASP B 1 44  ? -29.110 9.262   3.698   1.00 19.62 ? 44  ASP B CB  1 
ATOM   1220 C  CG  . ASP B 1 44  ? -28.747 10.429  2.822   1.00 23.44 ? 44  ASP B CG  1 
ATOM   1221 O  OD1 . ASP B 1 44  ? -29.066 11.575  3.211   1.00 24.56 ? 44  ASP B OD1 1 
ATOM   1222 O  OD2 . ASP B 1 44  ? -28.125 10.203  1.763   1.00 25.96 ? 44  ASP B OD2 1 
ATOM   1223 N  N   . GLN B 1 45  ? -28.266 7.823   7.003   1.00 13.65 ? 45  GLN B N   1 
ATOM   1224 C  CA  . GLN B 1 45  ? -28.819 6.888   7.961   1.00 13.34 ? 45  GLN B CA  1 
ATOM   1225 C  C   . GLN B 1 45  ? -29.512 7.608   9.114   1.00 13.58 ? 45  GLN B C   1 
ATOM   1226 O  O   . GLN B 1 45  ? -29.179 8.741   9.482   1.00 14.52 ? 45  GLN B O   1 
ATOM   1227 C  CB  . GLN B 1 45  ? -27.719 5.971   8.502   1.00 12.94 ? 45  GLN B CB  1 
ATOM   1228 C  CG  . GLN B 1 45  ? -27.151 5.043   7.419   1.00 12.79 ? 45  GLN B CG  1 
ATOM   1229 C  CD  . GLN B 1 45  ? -28.258 4.292   6.724   1.00 12.98 ? 45  GLN B CD  1 
ATOM   1230 O  OE1 . GLN B 1 45  ? -28.657 4.608   5.586   1.00 14.66 ? 45  GLN B OE1 1 
ATOM   1231 N  NE2 . GLN B 1 45  ? -28.797 3.329   7.410   1.00 12.76 ? 45  GLN B NE2 1 
ATOM   1232 N  N   . LEU B 1 46  ? -30.497 6.927   9.678   1.00 13.87 ? 46  LEU B N   1 
ATOM   1233 C  CA  . LEU B 1 46  ? -31.212 7.381   10.871  1.00 14.51 ? 46  LEU B CA  1 
ATOM   1234 C  C   . LEU B 1 46  ? -30.443 6.863   12.081  1.00 13.16 ? 46  LEU B C   1 
ATOM   1235 O  O   . LEU B 1 46  ? -30.554 5.688   12.453  1.00 13.00 ? 46  LEU B O   1 
ATOM   1236 C  CB  . LEU B 1 46  ? -32.637 6.840   10.840  1.00 19.76 ? 46  LEU B CB  1 
ATOM   1237 C  CG  . LEU B 1 46  ? -33.599 7.128   11.993  1.00 25.07 ? 46  LEU B CG  1 
ATOM   1238 C  CD1 . LEU B 1 46  ? -33.830 8.621   12.189  1.00 27.36 ? 46  LEU B CD1 1 
ATOM   1239 C  CD2 . LEU B 1 46  ? -34.930 6.400   11.783  1.00 27.07 ? 46  LEU B CD2 1 
ATOM   1240 N  N   . MET B 1 47  ? -29.638 7.737   12.678  1.00 14.30 ? 47  MET B N   1 
ATOM   1241 C  CA  . MET B 1 47  ? -28.686 7.364   13.715  1.00 15.39 ? 47  MET B CA  1 
ATOM   1242 C  C   . MET B 1 47  ? -28.575 8.472   14.742  1.00 14.83 ? 47  MET B C   1 
ATOM   1243 O  O   . MET B 1 47  ? -28.810 9.639   14.440  1.00 15.98 ? 47  MET B O   1 
ATOM   1244 C  CB  . MET B 1 47  ? -27.288 7.146   13.131  1.00 18.80 ? 47  MET B CB  1 
ATOM   1245 C  CG  . MET B 1 47  ? -27.236 6.299   11.911  1.00 21.40 ? 47  MET B CG  1 
ATOM   1246 S  SD  . MET B 1 47  ? -25.596 6.216   11.223  1.00 22.76 ? 47  MET B SD  1 
ATOM   1247 C  CE  . MET B 1 47  ? -24.678 6.790   12.513  1.00 15.49 ? 47  MET B CE  1 
ATOM   1248 N  N   . ALA B 1 48  ? -28.187 8.088   15.954  1.00 13.70 ? 48  ALA B N   1 
ATOM   1249 C  CA  . ALA B 1 48  ? -27.826 9.017   17.006  1.00 14.38 ? 48  ALA B CA  1 
ATOM   1250 C  C   . ALA B 1 48  ? -26.613 8.484   17.751  1.00 13.42 ? 48  ALA B C   1 
ATOM   1251 O  O   . ALA B 1 48  ? -26.348 7.272   17.763  1.00 14.14 ? 48  ALA B O   1 
ATOM   1252 C  CB  . ALA B 1 48  ? -28.996 9.186   17.958  1.00 15.64 ? 48  ALA B CB  1 
ATOM   1253 N  N   . PHE B 1 49  ? -25.832 9.411   18.289  1.00 14.26 ? 49  PHE B N   1 
ATOM   1254 C  CA  . PHE B 1 49  ? -24.659 9.104   19.098  1.00 14.06 ? 49  PHE B CA  1 
ATOM   1255 C  C   . PHE B 1 49  ? -24.789 9.956   20.349  1.00 14.63 ? 49  PHE B C   1 
ATOM   1256 O  O   . PHE B 1 49  ? -24.919 11.177  20.247  1.00 15.05 ? 49  PHE B O   1 
ATOM   1257 C  CB  . PHE B 1 49  ? -23.396 9.459   18.306  1.00 14.80 ? 49  PHE B CB  1 
ATOM   1258 C  CG  . PHE B 1 49  ? -22.125 8.935   18.899  1.00 16.78 ? 49  PHE B CG  1 
ATOM   1259 C  CD1 . PHE B 1 49  ? -21.632 9.446   20.090  1.00 18.35 ? 49  PHE B CD1 1 
ATOM   1260 C  CD2 . PHE B 1 49  ? -21.370 7.970   18.239  1.00 17.45 ? 49  PHE B CD2 1 
ATOM   1261 C  CE1 . PHE B 1 49  ? -20.439 8.957   20.632  1.00 19.22 ? 49  PHE B CE1 1 
ATOM   1262 C  CE2 . PHE B 1 49  ? -20.164 7.491   18.779  1.00 19.03 ? 49  PHE B CE2 1 
ATOM   1263 C  CZ  . PHE B 1 49  ? -19.712 7.982   19.968  1.00 19.80 ? 49  PHE B CZ  1 
ATOM   1264 N  N   . GLY B 1 50  ? -24.808 9.315   21.517  1.00 15.89 ? 50  GLY B N   1 
ATOM   1265 C  CA  . GLY B 1 50  ? -25.025 10.042  22.758  1.00 17.46 ? 50  GLY B CA  1 
ATOM   1266 C  C   . GLY B 1 50  ? -26.360 10.745  22.815  1.00 18.77 ? 50  GLY B C   1 
ATOM   1267 O  O   . GLY B 1 50  ? -26.508 11.761  23.511  1.00 20.34 ? 50  GLY B O   1 
ATOM   1268 N  N   . GLY B 1 51  ? -27.353 10.219  22.104  1.00 18.65 ? 51  GLY B N   1 
ATOM   1269 C  CA  . GLY B 1 51  ? -28.662 10.817  22.095  1.00 19.70 ? 51  GLY B CA  1 
ATOM   1270 C  C   . GLY B 1 51  ? -28.824 11.938  21.098  1.00 20.51 ? 51  GLY B C   1 
ATOM   1271 O  O   . GLY B 1 51  ? -29.942 12.443  20.944  1.00 22.28 ? 51  GLY B O   1 
ATOM   1272 N  N   . SER B 1 52  ? -27.757 12.318  20.397  1.00 20.12 ? 52  SER B N   1 
ATOM   1273 C  CA  . SER B 1 52  ? -27.742 13.467  19.507  1.00 20.34 ? 52  SER B CA  1 
ATOM   1274 C  C   . SER B 1 52  ? -27.630 13.022  18.051  1.00 19.81 ? 52  SER B C   1 
ATOM   1275 O  O   . SER B 1 52  ? -26.911 12.067  17.728  1.00 18.85 ? 52  SER B O   1 
ATOM   1276 C  CB  . SER B 1 52  ? -26.521 14.327  19.846  1.00 21.13 ? 52  SER B CB  1 
ATOM   1277 O  OG  . SER B 1 52  ? -26.093 15.122  18.760  1.00 22.21 ? 52  SER B OG  1 
ATOM   1278 N  N   A SER B 1 53  ? -28.349 13.732  17.178  0.58 21.60 ? 53  SER B N   1 
ATOM   1279 N  N   B SER B 1 53  ? -28.350 13.719  17.169  0.42 21.60 ? 53  SER B N   1 
ATOM   1280 C  CA  A SER B 1 53  ? -28.392 13.452  15.751  0.58 22.74 ? 53  SER B CA  1 
ATOM   1281 C  CA  B SER B 1 53  ? -28.345 13.405  15.748  0.42 22.74 ? 53  SER B CA  1 
ATOM   1282 C  C   A SER B 1 53  ? -27.425 14.311  14.943  0.58 21.68 ? 53  SER B C   1 
ATOM   1283 C  C   B SER B 1 53  ? -27.424 14.315  14.941  0.42 21.68 ? 53  SER B C   1 
ATOM   1284 O  O   A SER B 1 53  ? -27.525 14.342  13.709  0.58 21.90 ? 53  SER B O   1 
ATOM   1285 O  O   B SER B 1 53  ? -27.555 14.388  13.712  0.42 21.90 ? 53  SER B O   1 
ATOM   1286 C  CB  A SER B 1 53  ? -29.818 13.603  15.220  0.58 25.11 ? 53  SER B CB  1 
ATOM   1287 C  CB  B SER B 1 53  ? -29.763 13.388  15.179  0.42 25.11 ? 53  SER B CB  1 
ATOM   1288 O  OG  A SER B 1 53  ? -30.339 14.886  15.517  0.58 27.14 ? 53  SER B OG  1 
ATOM   1289 O  OG  B SER B 1 53  ? -30.139 12.061  14.846  0.42 27.14 ? 53  SER B OG  1 
ATOM   1290 N  N   . GLU B 1 54  ? -26.491 15.002  15.606  1.00 20.98 ? 54  GLU B N   1 
ATOM   1291 C  CA  . GLU B 1 54  ? -25.404 15.661  14.901  1.00 21.30 ? 54  GLU B CA  1 
ATOM   1292 C  C   . GLU B 1 54  ? -24.591 14.618  14.131  1.00 19.74 ? 54  GLU B C   1 
ATOM   1293 O  O   . GLU B 1 54  ? -24.695 13.422  14.403  1.00 18.66 ? 54  GLU B O   1 
ATOM   1294 C  CB  . GLU B 1 54  ? -24.518 16.383  15.917  1.00 23.85 ? 54  GLU B CB  1 
ATOM   1295 C  CG  . GLU B 1 54  ? -25.235 17.537  16.634  1.00 26.22 ? 54  GLU B CG  1 
ATOM   1296 C  CD  . GLU B 1 54  ? -25.350 18.814  15.789  1.00 29.42 ? 54  GLU B CD  1 
ATOM   1297 O  OE1 . GLU B 1 54  ? -25.414 18.720  14.542  1.00 30.62 ? 54  GLU B OE1 1 
ATOM   1298 O  OE2 . GLU B 1 54  ? -25.447 19.915  16.379  1.00 30.38 ? 54  GLU B OE2 1 
ATOM   1299 N  N   . PRO B 1 55  ? -23.789 15.036  13.151  1.00 19.33 ? 55  PRO B N   1 
ATOM   1300 C  CA  . PRO B 1 55  ? -23.065 14.045  12.337  1.00 19.33 ? 55  PRO B CA  1 
ATOM   1301 C  C   . PRO B 1 55  ? -22.283 13.043  13.182  1.00 18.19 ? 55  PRO B C   1 
ATOM   1302 O  O   . PRO B 1 55  ? -21.619 13.409  14.155  1.00 19.54 ? 55  PRO B O   1 
ATOM   1303 C  CB  . PRO B 1 55  ? -22.150 14.917  11.472  1.00 19.72 ? 55  PRO B CB  1 
ATOM   1304 C  CG  . PRO B 1 55  ? -22.929 16.188  11.297  1.00 20.18 ? 55  PRO B CG  1 
ATOM   1305 C  CD  . PRO B 1 55  ? -23.641 16.409  12.618  1.00 20.42 ? 55  PRO B CD  1 
ATOM   1306 N  N   . CYS B 1 56  ? -22.394 11.759  12.819  1.00 16.81 ? 56  CYS B N   1 
ATOM   1307 C  CA  . CYS B 1 56  ? -21.735 10.666  13.524  1.00 15.72 ? 56  CYS B CA  1 
ATOM   1308 C  C   . CYS B 1 56  ? -21.508 9.523   12.545  1.00 14.66 ? 56  CYS B C   1 
ATOM   1309 O  O   . CYS B 1 56  ? -22.035 9.521   11.430  1.00 14.68 ? 56  CYS B O   1 
ATOM   1310 C  CB  . CYS B 1 56  ? -22.541 10.208  14.759  1.00 15.70 ? 56  CYS B CB  1 
ATOM   1311 S  SG  . CYS B 1 56  ? -24.221 9.624   14.381  1.00 16.28 ? 56  CYS B SG  1 
ATOM   1312 N  N   . ALA B 1 57  ? -20.721 8.540   12.966  1.00 13.90 ? 57  ALA B N   1 
ATOM   1313 C  CA  . ALA B 1 57  ? -20.462 7.378   12.124  1.00 13.98 ? 57  ALA B CA  1 
ATOM   1314 C  C   . ALA B 1 57  ? -20.272 6.139   12.986  1.00 13.90 ? 57  ALA B C   1 
ATOM   1315 O  O   . ALA B 1 57  ? -19.628 6.187   14.042  1.00 14.12 ? 57  ALA B O   1 
ATOM   1316 C  CB  . ALA B 1 57  ? -19.204 7.617   11.282  1.00 13.93 ? 57  ALA B CB  1 
ATOM   1317 N  N   . LEU B 1 58  ? -20.810 5.025   12.511  1.00 13.39 ? 58  LEU B N   1 
ATOM   1318 C  CA  . LEU B 1 58  ? -20.554 3.713   13.079  1.00 12.96 ? 58  LEU B CA  1 
ATOM   1319 C  C   . LEU B 1 58  ? -19.879 2.895   11.992  1.00 12.68 ? 58  LEU B C   1 
ATOM   1320 O  O   . LEU B 1 58  ? -20.422 2.749   10.890  1.00 13.66 ? 58  LEU B O   1 
ATOM   1321 C  CB  . LEU B 1 58  ? -21.866 3.063   13.522  1.00 13.84 ? 58  LEU B CB  1 
ATOM   1322 C  CG  . LEU B 1 58  ? -22.684 3.890   14.527  1.00 16.04 ? 58  LEU B CG  1 
ATOM   1323 C  CD1 . LEU B 1 58  ? -23.983 3.185   14.870  1.00 16.80 ? 58  LEU B CD1 1 
ATOM   1324 C  CD2 . LEU B 1 58  ? -21.871 4.246   15.797  1.00 17.21 ? 58  LEU B CD2 1 
ATOM   1325 N  N   . CYS B 1 59  ? -18.706 2.364   12.305  1.00 12.50 ? 59  CYS B N   1 
ATOM   1326 C  CA  . CYS B 1 59  ? -17.851 1.718   11.319  1.00 13.24 ? 59  CYS B CA  1 
ATOM   1327 C  C   . CYS B 1 59  ? -17.353 0.374   11.819  1.00 12.85 ? 59  CYS B C   1 
ATOM   1328 O  O   . CYS B 1 59  ? -17.337 0.094   13.014  1.00 12.87 ? 59  CYS B O   1 
ATOM   1329 C  CB  . CYS B 1 59  ? -16.614 2.573   11.031  1.00 14.88 ? 59  CYS B CB  1 
ATOM   1330 S  SG  . CYS B 1 59  ? -16.938 4.299   10.674  1.00 15.99 ? 59  CYS B SG  1 
ATOM   1331 N  N   . SER B 1 60  ? -16.876 -0.435  10.885  1.00 12.65 ? 60  SER B N   1 
ATOM   1332 C  CA  . SER B 1 60  ? -16.232 -1.689  11.245  1.00 12.94 ? 60  SER B CA  1 
ATOM   1333 C  C   . SER B 1 60  ? -15.112 -1.977  10.264  1.00 12.50 ? 60  SER B C   1 
ATOM   1334 O  O   . SER B 1 60  ? -15.202 -1.650  9.078   1.00 13.57 ? 60  SER B O   1 
ATOM   1335 C  CB  . SER B 1 60  ? -17.194 -2.866  11.266  1.00 14.42 ? 60  SER B CB  1 
ATOM   1336 O  OG  . SER B 1 60  ? -17.794 -3.043  10.005  1.00 16.02 ? 60  SER B OG  1 
ATOM   1337 N  N   . LEU B 1 61  ? -14.044 -2.596  10.768  1.00 12.09 ? 61  LEU B N   1 
ATOM   1338 C  CA  . LEU B 1 61  ? -12.949 -3.095  9.943   1.00 13.00 ? 61  LEU B CA  1 
ATOM   1339 C  C   . LEU B 1 61  ? -12.760 -4.564  10.270  1.00 12.52 ? 61  LEU B C   1 
ATOM   1340 O  O   . LEU B 1 61  ? -12.473 -4.913  11.424  1.00 13.63 ? 61  LEU B O   1 
ATOM   1341 C  CB  . LEU B 1 61  ? -11.650 -2.335  10.229  1.00 13.91 ? 61  LEU B CB  1 
ATOM   1342 C  CG  . LEU B 1 61  ? -10.450 -2.770  9.392   1.00 14.80 ? 61  LEU B CG  1 
ATOM   1343 C  CD1 . LEU B 1 61  ? -10.663 -2.489  7.909   1.00 15.43 ? 61  LEU B CD1 1 
ATOM   1344 C  CD2 . LEU B 1 61  ? -9.187  -2.114  9.893   1.00 14.61 ? 61  LEU B CD2 1 
ATOM   1345 N  N   . HIS B 1 62  ? -12.939 -5.419  9.268   1.00 12.02 ? 62  HIS B N   1 
ATOM   1346 C  CA  . HIS B 1 62  ? -12.684 -6.846  9.392   1.00 11.97 ? 62  HIS B CA  1 
ATOM   1347 C  C   . HIS B 1 62  ? -11.433 -7.149  8.591   1.00 13.12 ? 62  HIS B C   1 
ATOM   1348 O  O   . HIS B 1 62  ? -11.323 -6.730  7.436   1.00 14.53 ? 62  HIS B O   1 
ATOM   1349 C  CB  . HIS B 1 62  ? -13.841 -7.678  8.819   1.00 13.44 ? 62  HIS B CB  1 
ATOM   1350 C  CG  . HIS B 1 62  ? -15.137 -7.552  9.563   1.00 15.29 ? 62  HIS B CG  1 
ATOM   1351 N  ND1 . HIS B 1 62  ? -15.955 -6.450  9.470   1.00 15.63 ? 62  HIS B ND1 1 
ATOM   1352 C  CD2 . HIS B 1 62  ? -15.774 -8.425  10.376  1.00 15.76 ? 62  HIS B CD2 1 
ATOM   1353 C  CE1 . HIS B 1 62  ? -17.023 -6.626  10.232  1.00 16.04 ? 62  HIS B CE1 1 
ATOM   1354 N  NE2 . HIS B 1 62  ? -16.930 -7.817  10.800  1.00 16.49 ? 62  HIS B NE2 1 
ATOM   1355 N  N   . SER B 1 63  ? -10.499 -7.893  9.184   1.00 12.15 ? 63  SER B N   1 
ATOM   1356 C  CA  . SER B 1 63  ? -9.281  -8.276  8.482   1.00 12.80 ? 63  SER B CA  1 
ATOM   1357 C  C   . SER B 1 63  ? -8.796  -9.617  9.008   1.00 12.99 ? 63  SER B C   1 
ATOM   1358 O  O   . SER B 1 63  ? -8.931  -9.905  10.205  1.00 13.48 ? 63  SER B O   1 
ATOM   1359 C  CB  . SER B 1 63  ? -8.187  -7.230  8.690   1.00 13.91 ? 63  SER B CB  1 
ATOM   1360 O  OG  . SER B 1 63  ? -7.015  -7.548  7.979   1.00 15.07 ? 63  SER B OG  1 
ATOM   1361 N  N   . ILE B 1 64  ? -8.235  -10.429 8.111   1.00 13.97 ? 64  ILE B N   1 
ATOM   1362 C  CA  . ILE B 1 64  ? -7.568  -11.673 8.508   1.00 14.33 ? 64  ILE B CA  1 
ATOM   1363 C  C   . ILE B 1 64  ? -6.172  -11.279 8.978   1.00 14.33 ? 64  ILE B C   1 
ATOM   1364 O  O   . ILE B 1 64  ? -5.265  -11.080 8.159   1.00 14.55 ? 64  ILE B O   1 
ATOM   1365 C  CB  . ILE B 1 64  ? -7.536  -12.705 7.378   1.00 14.02 ? 64  ILE B CB  1 
ATOM   1366 C  CG1 . ILE B 1 64  ? -8.953  -13.062 6.922   1.00 14.43 ? 64  ILE B CG1 1 
ATOM   1367 C  CG2 . ILE B 1 64  ? -6.778  -13.974 7.831   1.00 14.54 ? 64  ILE B CG2 1 
ATOM   1368 C  CD1 . ILE B 1 64  ? -9.003  -13.831 5.602   1.00 14.96 ? 64  ILE B CD1 1 
ATOM   1369 N  N   . GLY B 1 65  ? -6.004  -11.125 10.300  1.00 14.39 ? 65  GLY B N   1 
ATOM   1370 C  CA  . GLY B 1 65  ? -4.789  -10.562 10.842  1.00 15.02 ? 65  GLY B CA  1 
ATOM   1371 C  C   . GLY B 1 65  ? -4.707  -9.055  10.670  1.00 14.88 ? 65  GLY B C   1 
ATOM   1372 O  O   . GLY B 1 65  ? -5.648  -8.378  10.232  1.00 15.17 ? 65  GLY B O   1 
ATOM   1373 N  N   . LYS B 1 66  ? -3.553  -8.520  11.072  1.00 16.21 ? 66  LYS B N   1 
ATOM   1374 C  CA  . LYS B 1 66  ? -3.281  -7.076  11.043  1.00 16.72 ? 66  LYS B CA  1 
ATOM   1375 C  C   . LYS B 1 66  ? -4.234  -6.297  11.947  1.00 17.13 ? 66  LYS B C   1 
ATOM   1376 O  O   . LYS B 1 66  ? -4.561  -5.134  11.672  1.00 17.56 ? 66  LYS B O   1 
ATOM   1377 C  CB  . LYS B 1 66  ? -3.274  -6.523  9.608   1.00 18.18 ? 66  LYS B CB  1 
ATOM   1378 C  CG  . LYS B 1 66  ? -2.357  -7.288  8.672   1.00 20.24 ? 66  LYS B CG  1 
ATOM   1379 C  CD  . LYS B 1 66  ? -0.918  -7.330  9.194   1.00 22.96 ? 66  LYS B CD  1 
ATOM   1380 C  CE  . LYS B 1 66  ? 0.081   -7.590  8.082   1.00 26.09 ? 66  LYS B CE  1 
ATOM   1381 N  NZ  . LYS B 1 66  ? 0.135   -6.530  7.035   1.00 28.08 ? 66  LYS B NZ  1 
ATOM   1382 N  N   . ILE B 1 67  ? -4.688  -6.950  13.022  1.00 17.49 ? 67  ILE B N   1 
ATOM   1383 C  CA  . ILE B 1 67  ? -5.595  -6.373  14.017  1.00 16.68 ? 67  ILE B CA  1 
ATOM   1384 C  C   . ILE B 1 67  ? -4.963  -6.574  15.391  1.00 16.84 ? 67  ILE B C   1 
ATOM   1385 O  O   . ILE B 1 67  ? -4.491  -7.672  15.709  1.00 17.73 ? 67  ILE B O   1 
ATOM   1386 C  CB  . ILE B 1 67  ? -7.001  -7.023  13.951  1.00 14.94 ? 67  ILE B CB  1 
ATOM   1387 C  CG1 . ILE B 1 67  ? -7.688  -6.761  12.597  1.00 14.98 ? 67  ILE B CG1 1 
ATOM   1388 C  CG2 . ILE B 1 67  ? -7.907  -6.589  15.125  1.00 13.89 ? 67  ILE B CG2 1 
ATOM   1389 C  CD1 . ILE B 1 67  ? -8.165  -5.322  12.411  1.00 13.91 ? 67  ILE B CD1 1 
ATOM   1390 N  N   . GLY B 1 68  ? -4.930  -5.522  16.197  1.00 16.19 ? 68  GLY B N   1 
ATOM   1391 C  CA  . GLY B 1 68  ? -4.331  -5.632  17.519  1.00 16.17 ? 68  GLY B CA  1 
ATOM   1392 C  C   . GLY B 1 68  ? -4.307  -4.288  18.201  1.00 17.17 ? 68  GLY B C   1 
ATOM   1393 O  O   . GLY B 1 68  ? -4.750  -3.281  17.650  1.00 16.98 ? 68  GLY B O   1 
ATOM   1394 N  N   . GLY B 1 69  ? -3.783  -4.290  19.426  1.00 17.90 ? 69  GLY B N   1 
ATOM   1395 C  CA  . GLY B 1 69  ? -3.773  -3.099  20.260  1.00 18.93 ? 69  GLY B CA  1 
ATOM   1396 C  C   . GLY B 1 69  ? -3.208  -1.864  19.591  1.00 19.37 ? 69  GLY B C   1 
ATOM   1397 O  O   . GLY B 1 69  ? -3.907  -0.855  19.423  1.00 19.62 ? 69  GLY B O   1 
ATOM   1398 N  N   . ALA B 1 70  ? -1.934  -1.926  19.206  1.00 20.07 ? 70  ALA B N   1 
ATOM   1399 C  CA  . ALA B 1 70  ? -1.283  -0.773  18.596  1.00 20.02 ? 70  ALA B CA  1 
ATOM   1400 C  C   . ALA B 1 70  ? -1.809  -0.508  17.194  1.00 19.89 ? 70  ALA B C   1 
ATOM   1401 O  O   . ALA B 1 70  ? -1.973  0.649   16.796  1.00 20.59 ? 70  ALA B O   1 
ATOM   1402 C  CB  . ALA B 1 70  ? 0.228   -0.999  18.553  1.00 20.88 ? 70  ALA B CB  1 
ATOM   1403 N  N   . GLN B 1 71  ? -2.045  -1.567  16.415  1.00 18.87 ? 71  GLN B N   1 
ATOM   1404 C  CA  . GLN B 1 71  ? -2.533  -1.368  15.058  1.00 18.89 ? 71  GLN B CA  1 
ATOM   1405 C  C   . GLN B 1 71  ? -3.895  -0.688  15.050  1.00 18.73 ? 71  GLN B C   1 
ATOM   1406 O  O   . GLN B 1 71  ? -4.127  0.233   14.256  1.00 18.72 ? 71  GLN B O   1 
ATOM   1407 C  CB  . GLN B 1 71  ? -2.563  -2.705  14.321  1.00 18.68 ? 71  GLN B CB  1 
ATOM   1408 C  CG  . GLN B 1 71  ? -1.171  -3.267  14.029  1.00 19.07 ? 71  GLN B CG  1 
ATOM   1409 C  CD  . GLN B 1 71  ? -1.217  -4.648  13.412  1.00 19.63 ? 71  GLN B CD  1 
ATOM   1410 O  OE1 . GLN B 1 71  ? -1.153  -4.794  12.189  1.00 20.94 ? 71  GLN B OE1 1 
ATOM   1411 N  NE2 . GLN B 1 71  ? -1.329  -5.677  14.253  1.00 19.98 ? 71  GLN B NE2 1 
ATOM   1412 N  N   . ASN B 1 72  ? -4.793  -1.102  15.953  1.00 17.43 ? 72  ASN B N   1 
ATOM   1413 C  CA  . ASN B 1 72  ? -6.127  -0.513  15.991  1.00 17.17 ? 72  ASN B CA  1 
ATOM   1414 C  C   . ASN B 1 72  ? -6.080  0.941   16.436  1.00 17.34 ? 72  ASN B C   1 
ATOM   1415 O  O   . ASN B 1 72  ? -6.862  1.750   15.938  1.00 15.87 ? 72  ASN B O   1 
ATOM   1416 C  CB  . ASN B 1 72  ? -7.074  -1.317  16.895  1.00 16.57 ? 72  ASN B CB  1 
ATOM   1417 C  CG  . ASN B 1 72  ? -7.281  -2.749  16.416  1.00 15.65 ? 72  ASN B CG  1 
ATOM   1418 O  OD1 . ASN B 1 72  ? -6.836  -3.150  15.326  1.00 15.29 ? 72  ASN B OD1 1 
ATOM   1419 N  ND2 . ASN B 1 72  ? -7.952  -3.529  17.237  1.00 15.12 ? 72  ASN B ND2 1 
ATOM   1420 N  N   . ARG B 1 73  ? -5.162  1.297   17.341  1.00 19.03 ? 73  ARG B N   1 
ATOM   1421 C  CA  . ARG B 1 73  ? -4.999  2.713   17.673  1.00 20.09 ? 73  ARG B CA  1 
ATOM   1422 C  C   . ARG B 1 73  ? -4.594  3.506   16.440  1.00 20.16 ? 73  ARG B C   1 
ATOM   1423 O  O   . ARG B 1 73  ? -5.120  4.597   16.195  1.00 20.82 ? 73  ARG B O   1 
ATOM   1424 C  CB  . ARG B 1 73  ? -3.964  2.897   18.783  1.00 21.79 ? 73  ARG B CB  1 
ATOM   1425 C  CG  . ARG B 1 73  ? -4.485  2.627   20.183  1.00 23.34 ? 73  ARG B CG  1 
ATOM   1426 C  CD  . ARG B 1 73  ? -3.465  2.964   21.254  1.00 25.08 ? 73  ARG B CD  1 
ATOM   1427 N  NE  . ARG B 1 73  ? -2.368  1.998   21.286  1.00 26.63 ? 73  ARG B NE  1 
ATOM   1428 C  CZ  . ARG B 1 73  ? -2.429  0.821   21.905  1.00 28.24 ? 73  ARG B CZ  1 
ATOM   1429 N  NH1 . ARG B 1 73  ? -3.542  0.456   22.530  1.00 28.51 ? 73  ARG B NH1 1 
ATOM   1430 N  NH2 . ARG B 1 73  ? -1.386  0.001   21.889  1.00 29.04 ? 73  ARG B NH2 1 
ATOM   1431 N  N   . SER B 1 74  ? -3.680  2.951   15.634  1.00 19.97 ? 74  SER B N   1 
ATOM   1432 C  CA  . SER B 1 74  ? -3.230  3.632   14.425  1.00 19.45 ? 74  SER B CA  1 
ATOM   1433 C  C   . SER B 1 74  ? -4.350  3.726   13.392  1.00 17.85 ? 74  SER B C   1 
ATOM   1434 O  O   . SER B 1 74  ? -4.541  4.783   12.783  1.00 16.90 ? 74  SER B O   1 
ATOM   1435 C  CB  . SER B 1 74  ? -2.011  2.920   13.840  1.00 20.68 ? 74  SER B CB  1 
ATOM   1436 O  OG  . SER B 1 74  ? -1.456  3.686   12.792  1.00 22.35 ? 74  SER B OG  1 
ATOM   1437 N  N   . TYR B 1 75  ? -5.117  2.639   13.206  1.00 17.46 ? 75  TYR B N   1 
ATOM   1438 C  CA  . TYR B 1 75  ? -6.260  2.657   12.290  1.00 16.74 ? 75  TYR B CA  1 
ATOM   1439 C  C   . TYR B 1 75  ? -7.276  3.707   12.707  1.00 16.86 ? 75  TYR B C   1 
ATOM   1440 O  O   . TYR B 1 75  ? -7.860  4.389   11.856  1.00 17.52 ? 75  TYR B O   1 
ATOM   1441 C  CB  . TYR B 1 75  ? -6.958  1.290   12.260  1.00 17.12 ? 75  TYR B CB  1 
ATOM   1442 C  CG  . TYR B 1 75  ? -6.137  0.145   11.719  1.00 18.35 ? 75  TYR B CG  1 
ATOM   1443 C  CD1 . TYR B 1 75  ? -5.170  0.341   10.740  1.00 19.33 ? 75  TYR B CD1 1 
ATOM   1444 C  CD2 . TYR B 1 75  ? -6.339  -1.137  12.189  1.00 18.30 ? 75  TYR B CD2 1 
ATOM   1445 C  CE1 . TYR B 1 75  ? -4.429  -0.719  10.247  1.00 19.92 ? 75  TYR B CE1 1 
ATOM   1446 C  CE2 . TYR B 1 75  ? -5.617  -2.203  11.697  1.00 18.49 ? 75  TYR B CE2 1 
ATOM   1447 C  CZ  . TYR B 1 75  ? -4.661  -1.983  10.730  1.00 19.39 ? 75  TYR B CZ  1 
ATOM   1448 O  OH  . TYR B 1 75  ? -3.932  -3.022  10.235  1.00 19.32 ? 75  TYR B OH  1 
ATOM   1449 N  N   . SER B 1 76  ? -7.512  3.840   14.018  1.00 17.16 ? 76  SER B N   1 
ATOM   1450 C  CA  . SER B 1 76  ? -8.513  4.786   14.496  1.00 16.93 ? 76  SER B CA  1 
ATOM   1451 C  C   . SER B 1 76  ? -8.085  6.219   14.213  1.00 17.24 ? 76  SER B C   1 
ATOM   1452 O  O   . SER B 1 76  ? -8.908  7.047   13.804  1.00 17.18 ? 76  SER B O   1 
ATOM   1453 C  CB  . SER B 1 76  ? -8.755  4.555   15.987  1.00 16.79 ? 76  SER B CB  1 
ATOM   1454 O  OG  . SER B 1 76  ? -9.311  3.263   16.162  1.00 18.00 ? 76  SER B OG  1 
ATOM   1455 N  N   . LYS B 1 77  ? -6.799  6.531   14.402  1.00 18.34 ? 77  LYS B N   1 
ATOM   1456 C  CA  . LYS B 1 77  ? -6.325  7.871   14.067  1.00 19.43 ? 77  LYS B CA  1 
ATOM   1457 C  C   . LYS B 1 77  ? -6.481  8.134   12.571  1.00 19.11 ? 77  LYS B C   1 
ATOM   1458 O  O   . LYS B 1 77  ? -6.966  9.196   12.164  1.00 18.85 ? 77  LYS B O   1 
ATOM   1459 C  CB  . LYS B 1 77  ? -4.873  8.053   14.519  1.00 21.58 ? 77  LYS B CB  1 
ATOM   1460 C  CG  . LYS B 1 77  ? -4.324  9.450   14.298  1.00 23.99 ? 77  LYS B CG  1 
ATOM   1461 C  CD  . LYS B 1 77  ? -2.922  9.555   14.842  1.00 26.09 ? 77  LYS B CD  1 
ATOM   1462 C  CE  . LYS B 1 77  ? -2.239  10.825  14.367  1.00 27.78 ? 77  LYS B CE  1 
ATOM   1463 N  NZ  . LYS B 1 77  ? -0.783  10.786  14.672  1.00 29.08 ? 77  LYS B NZ  1 
ATOM   1464 N  N   . LEU B 1 78  ? -6.124  7.154   11.742  1.00 18.47 ? 78  LEU B N   1 
ATOM   1465 C  CA  . LEU B 1 78  ? -6.235  7.322   10.297  1.00 18.65 ? 78  LEU B CA  1 
ATOM   1466 C  C   . LEU B 1 78  ? -7.689  7.493   9.873   1.00 18.62 ? 78  LEU B C   1 
ATOM   1467 O  O   . LEU B 1 78  ? -8.036  8.414   9.118   1.00 19.27 ? 78  LEU B O   1 
ATOM   1468 C  CB  . LEU B 1 78  ? -5.631  6.094   9.627   1.00 19.42 ? 78  LEU B CB  1 
ATOM   1469 C  CG  . LEU B 1 78  ? -5.864  5.907   8.125   1.00 20.95 ? 78  LEU B CG  1 
ATOM   1470 C  CD1 . LEU B 1 78  ? -4.981  6.874   7.323   1.00 22.12 ? 78  LEU B CD1 1 
ATOM   1471 C  CD2 . LEU B 1 78  ? -5.569  4.456   7.742   1.00 21.25 ? 78  LEU B CD2 1 
ATOM   1472 N  N   . LEU B 1 79  ? -8.562  6.614   10.357  1.00 17.90 ? 79  LEU B N   1 
ATOM   1473 C  CA  . LEU B 1 79  ? -9.940  6.607   9.884   1.00 17.93 ? 79  LEU B CA  1 
ATOM   1474 C  C   . LEU B 1 79  ? -10.734 7.771   10.459  1.00 18.46 ? 79  LEU B C   1 
ATOM   1475 O  O   . LEU B 1 79  ? -11.526 8.392   9.743   1.00 18.53 ? 79  LEU B O   1 
ATOM   1476 C  CB  . LEU B 1 79  ? -10.600 5.267   10.195  1.00 18.70 ? 79  LEU B CB  1 
ATOM   1477 C  CG  . LEU B 1 79  ? -10.027 4.089   9.402   1.00 19.63 ? 79  LEU B CG  1 
ATOM   1478 C  CD1 . LEU B 1 79  ? -10.456 2.755   10.003  1.00 19.78 ? 79  LEU B CD1 1 
ATOM   1479 C  CD2 . LEU B 1 79  ? -10.451 4.185   7.941   1.00 20.37 ? 79  LEU B CD2 1 
ATOM   1480 N  N   . CYS B 1 80  ? -10.543 8.088   11.745  1.00 18.75 ? 80  CYS B N   1 
ATOM   1481 C  CA  . CYS B 1 80  ? -11.197 9.281   12.288  1.00 19.26 ? 80  CYS B CA  1 
ATOM   1482 C  C   . CYS B 1 80  ? -10.739 10.545  11.566  1.00 19.71 ? 80  CYS B C   1 
ATOM   1483 O  O   . CYS B 1 80  ? -11.549 11.428  11.274  1.00 19.53 ? 80  CYS B O   1 
ATOM   1484 C  CB  . CYS B 1 80  ? -10.974 9.425   13.793  1.00 19.33 ? 80  CYS B CB  1 
ATOM   1485 S  SG  . CYS B 1 80  ? -11.857 8.257   14.840  1.00 20.51 ? 80  CYS B SG  1 
ATOM   1486 N  N   . GLY B 1 81  ? -9.454  10.642  11.248  1.00 19.92 ? 81  GLY B N   1 
ATOM   1487 C  CA  . GLY B 1 81  ? -8.992  11.785  10.483  1.00 19.70 ? 81  GLY B CA  1 
ATOM   1488 C  C   . GLY B 1 81  ? -9.660  11.898  9.127   1.00 20.10 ? 81  GLY B C   1 
ATOM   1489 O  O   . GLY B 1 81  ? -10.045 12.993  8.702   1.00 21.26 ? 81  GLY B O   1 
ATOM   1490 N  N   . LEU B 1 82  ? -9.810  10.770  8.427   1.00 20.88 ? 82  LEU B N   1 
ATOM   1491 C  CA  . LEU B 1 82  ? -10.451 10.790  7.117   1.00 21.17 ? 82  LEU B CA  1 
ATOM   1492 C  C   . LEU B 1 82  ? -11.924 11.164  7.231   1.00 20.44 ? 82  LEU B C   1 
ATOM   1493 O  O   . LEU B 1 82  ? -12.450 11.916  6.401   1.00 21.77 ? 82  LEU B O   1 
ATOM   1494 C  CB  . LEU B 1 82  ? -10.298 9.422   6.443   1.00 21.57 ? 82  LEU B CB  1 
ATOM   1495 C  CG  . LEU B 1 82  ? -8.930  9.096   5.835   1.00 22.78 ? 82  LEU B CG  1 
ATOM   1496 C  CD1 . LEU B 1 82  ? -8.860  7.616   5.489   1.00 22.55 ? 82  LEU B CD1 1 
ATOM   1497 C  CD2 . LEU B 1 82  ? -8.683  9.952   4.601   1.00 24.38 ? 82  LEU B CD2 1 
ATOM   1498 N  N   . LEU B 1 83  ? -12.623 10.619  8.230   1.00 18.95 ? 83  LEU B N   1 
ATOM   1499 C  CA  . LEU B 1 83  ? -14.024 10.988  8.413   1.00 18.58 ? 83  LEU B CA  1 
ATOM   1500 C  C   . LEU B 1 83  ? -14.174 12.455  8.802   1.00 19.11 ? 83  LEU B C   1 
ATOM   1501 O  O   . LEU B 1 83  ? -15.132 13.112  8.384   1.00 19.13 ? 83  LEU B O   1 
ATOM   1502 C  CB  . LEU B 1 83  ? -14.661 10.075  9.447   1.00 18.23 ? 83  LEU B CB  1 
ATOM   1503 C  CG  . LEU B 1 83  ? -14.754 8.616   9.008   1.00 18.09 ? 83  LEU B CG  1 
ATOM   1504 C  CD1 . LEU B 1 83  ? -15.121 7.737   10.194  1.00 18.68 ? 83  LEU B CD1 1 
ATOM   1505 C  CD2 . LEU B 1 83  ? -15.805 8.475   7.903   1.00 19.12 ? 83  LEU B CD2 1 
ATOM   1506 N  N   . ALA B 1 84  ? -13.232 12.993  9.573   1.00 19.84 ? 84  ALA B N   1 
ATOM   1507 C  CA  . ALA B 1 84  ? -13.292 14.407  9.924   1.00 21.17 ? 84  ALA B CA  1 
ATOM   1508 C  C   . ALA B 1 84  ? -13.031 15.283  8.708   1.00 22.08 ? 84  ALA B C   1 
ATOM   1509 O  O   . ALA B 1 84  ? -13.777 16.237  8.443   1.00 22.82 ? 84  ALA B O   1 
ATOM   1510 C  CB  . ALA B 1 84  ? -12.296 14.714  11.043  1.00 21.78 ? 84  ALA B CB  1 
ATOM   1511 N  N   . GLU B 1 85  ? -11.986 14.959  7.941   1.00 23.23 ? 85  GLU B N   1 
ATOM   1512 C  CA  . GLU B 1 85  ? -11.586 15.821  6.834   1.00 24.45 ? 85  GLU B CA  1 
ATOM   1513 C  C   . GLU B 1 85  ? -12.578 15.748  5.678   1.00 24.67 ? 85  GLU B C   1 
ATOM   1514 O  O   . GLU B 1 85  ? -12.962 16.785  5.120   1.00 25.16 ? 85  GLU B O   1 
ATOM   1515 C  CB  . GLU B 1 85  ? -10.183 15.444  6.367   1.00 25.51 ? 85  GLU B CB  1 
ATOM   1516 N  N   . ARG B 1 86  ? -13.061 14.547  5.352   1.00 24.18 ? 86  ARG B N   1 
ATOM   1517 C  CA  . ARG B 1 86  ? -13.888 14.331  4.167   1.00 23.54 ? 86  ARG B CA  1 
ATOM   1518 C  C   . ARG B 1 86  ? -15.382 14.406  4.445   1.00 23.68 ? 86  ARG B C   1 
ATOM   1519 O  O   . ARG B 1 86  ? -16.126 14.940  3.619   1.00 24.47 ? 86  ARG B O   1 
ATOM   1520 C  CB  . ARG B 1 86  ? -13.562 12.975  3.522   1.00 23.84 ? 86  ARG B CB  1 
ATOM   1521 C  CG  . ARG B 1 86  ? -12.096 12.753  3.225   1.00 25.23 ? 86  ARG B CG  1 
ATOM   1522 C  CD  . ARG B 1 86  ? -11.621 13.819  2.263   1.00 26.44 ? 86  ARG B CD  1 
ATOM   1523 N  NE  . ARG B 1 86  ? -10.338 13.467  1.673   1.00 27.17 ? 86  ARG B NE  1 
ATOM   1524 C  CZ  . ARG B 1 86  ? -9.548  14.332  1.051   1.00 27.75 ? 86  ARG B CZ  1 
ATOM   1525 N  NH1 . ARG B 1 86  ? -9.911  15.606  0.966   1.00 27.71 ? 86  ARG B NH1 1 
ATOM   1526 N  NH2 . ARG B 1 86  ? -8.391  13.933  0.544   1.00 28.59 ? 86  ARG B NH2 1 
ATOM   1527 N  N   . LEU B 1 87  ? -15.844 13.893  5.585   1.00 22.96 ? 87  LEU B N   1 
ATOM   1528 C  CA  . LEU B 1 87  ? -17.266 13.893  5.903   1.00 22.42 ? 87  LEU B CA  1 
ATOM   1529 C  C   . LEU B 1 87  ? -17.639 14.914  6.970   1.00 22.39 ? 87  LEU B C   1 
ATOM   1530 O  O   . LEU B 1 87  ? -18.827 15.073  7.277   1.00 22.13 ? 87  LEU B O   1 
ATOM   1531 C  CB  . LEU B 1 87  ? -17.714 12.484  6.327   1.00 22.25 ? 87  LEU B CB  1 
ATOM   1532 C  CG  . LEU B 1 87  ? -17.547 11.349  5.307   1.00 22.99 ? 87  LEU B CG  1 
ATOM   1533 C  CD1 . LEU B 1 87  ? -18.248 10.116  5.810   1.00 22.52 ? 87  LEU B CD1 1 
ATOM   1534 C  CD2 . LEU B 1 87  ? -18.094 11.762  3.945   1.00 23.89 ? 87  LEU B CD2 1 
ATOM   1535 N  N   . ARG B 1 88  ? -16.656 15.597  7.548   1.00 22.87 ? 88  ARG B N   1 
ATOM   1536 C  CA  . ARG B 1 88  ? -16.875 16.626  8.566   1.00 24.01 ? 88  ARG B CA  1 
ATOM   1537 C  C   . ARG B 1 88  ? -17.482 16.052  9.847   1.00 22.08 ? 88  ARG B C   1 
ATOM   1538 O  O   . ARG B 1 88  ? -18.258 16.731  10.534  1.00 23.07 ? 88  ARG B O   1 
ATOM   1539 C  CB  . ARG B 1 88  ? -17.720 17.807  8.067   1.00 27.62 ? 88  ARG B CB  1 
ATOM   1540 C  CG  . ARG B 1 88  ? -17.542 18.239  6.610   1.00 31.46 ? 88  ARG B CG  1 
ATOM   1541 C  CD  . ARG B 1 88  ? -16.105 18.261  6.132   1.00 34.88 ? 88  ARG B CD  1 
ATOM   1542 N  NE  . ARG B 1 88  ? -15.202 19.004  6.998   1.00 38.02 ? 88  ARG B NE  1 
ATOM   1543 C  CZ  . ARG B 1 88  ? -14.063 19.554  6.587   1.00 40.16 ? 88  ARG B CZ  1 
ATOM   1544 N  NH1 . ARG B 1 88  ? -13.292 20.201  7.452   1.00 41.15 ? 88  ARG B NH1 1 
ATOM   1545 N  NH2 . ARG B 1 88  ? -13.699 19.474  5.310   1.00 40.63 ? 88  ARG B NH2 1 
ATOM   1546 N  N   . ILE B 1 89  ? -17.139 14.812  10.187  1.00 20.57 ? 89  ILE B N   1 
ATOM   1547 C  CA  . ILE B 1 89  ? -17.628 14.157  11.397  1.00 20.30 ? 89  ILE B CA  1 
ATOM   1548 C  C   . ILE B 1 89  ? -16.567 14.263  12.489  1.00 21.15 ? 89  ILE B C   1 
ATOM   1549 O  O   . ILE B 1 89  ? -15.391 13.925  12.271  1.00 21.35 ? 89  ILE B O   1 
ATOM   1550 C  CB  . ILE B 1 89  ? -17.981 12.685  11.127  1.00 19.91 ? 89  ILE B CB  1 
ATOM   1551 C  CG1 . ILE B 1 89  ? -19.066 12.563  10.048  1.00 19.46 ? 89  ILE B CG1 1 
ATOM   1552 C  CG2 . ILE B 1 89  ? -18.444 12.021  12.416  1.00 20.23 ? 89  ILE B CG2 1 
ATOM   1553 C  CD1 . ILE B 1 89  ? -19.264 11.150  9.528   1.00 19.17 ? 89  ILE B CD1 1 
ATOM   1554 N  N   A SER B 1 90  ? -16.981 14.726  13.661  0.57 22.49 ? 90  SER B N   1 
ATOM   1555 N  N   B SER B 1 90  ? -16.979 14.732  13.662  0.43 22.49 ? 90  SER B N   1 
ATOM   1556 C  CA  A SER B 1 90  ? -16.064 14.847  14.782  0.57 23.17 ? 90  SER B CA  1 
ATOM   1557 C  CA  B SER B 1 90  ? -16.058 14.849  14.782  0.43 23.17 ? 90  SER B CA  1 
ATOM   1558 C  C   A SER B 1 90  ? -15.586 13.465  15.229  0.57 21.13 ? 90  SER B C   1 
ATOM   1559 C  C   B SER B 1 90  ? -15.582 13.463  15.216  0.43 21.13 ? 90  SER B C   1 
ATOM   1560 O  O   A SER B 1 90  ? -16.395 12.536  15.352  0.57 20.02 ? 90  SER B O   1 
ATOM   1561 O  O   B SER B 1 90  ? -16.389 12.531  15.318  0.43 20.02 ? 90  SER B O   1 
ATOM   1562 C  CB  A SER B 1 90  ? -16.777 15.534  15.942  0.57 25.20 ? 90  SER B CB  1 
ATOM   1563 C  CB  B SER B 1 90  ? -16.754 15.528  15.960  0.43 25.20 ? 90  SER B CB  1 
ATOM   1564 O  OG  A SER B 1 90  ? -17.086 16.876  15.613  0.57 27.38 ? 90  SER B OG  1 
ATOM   1565 O  OG  B SER B 1 90  ? -15.929 15.519  17.117  0.43 27.38 ? 90  SER B OG  1 
ATOM   1566 N  N   . PRO B 1 91  ? -14.284 13.297  15.488  1.00 21.16 ? 91  PRO B N   1 
ATOM   1567 C  CA  . PRO B 1 91  ? -13.789 11.977  15.932  1.00 21.15 ? 91  PRO B CA  1 
ATOM   1568 C  C   . PRO B 1 91  ? -14.457 11.453  17.193  1.00 20.34 ? 91  PRO B C   1 
ATOM   1569 O  O   . PRO B 1 91  ? -14.519 10.234  17.389  1.00 20.60 ? 91  PRO B O   1 
ATOM   1570 C  CB  . PRO B 1 91  ? -12.288 12.225  16.154  1.00 21.44 ? 91  PRO B CB  1 
ATOM   1571 C  CG  . PRO B 1 91  ? -11.952 13.347  15.247  1.00 22.17 ? 91  PRO B CG  1 
ATOM   1572 C  CD  . PRO B 1 91  ? -13.180 14.251  15.259  1.00 21.83 ? 91  PRO B CD  1 
ATOM   1573 N  N   . ASP B 1 92  ? -14.940 12.334  18.073  1.00 20.42 ? 92  ASP B N   1 
ATOM   1574 C  CA  . ASP B 1 92  ? -15.619 11.871  19.275  1.00 20.35 ? 92  ASP B CA  1 
ATOM   1575 C  C   . ASP B 1 92  ? -17.052 11.440  19.013  1.00 18.33 ? 92  ASP B C   1 
ATOM   1576 O  O   . ASP B 1 92  ? -17.760 11.094  19.960  1.00 17.95 ? 92  ASP B O   1 
ATOM   1577 C  CB  . ASP B 1 92  ? -15.502 12.894  20.423  1.00 21.46 ? 92  ASP B CB  1 
ATOM   1578 C  CG  . ASP B 1 92  ? -16.205 14.230  20.137  1.00 22.83 ? 92  ASP B CG  1 
ATOM   1579 O  OD1 . ASP B 1 92  ? -16.867 14.377  19.092  1.00 22.64 ? 92  ASP B OD1 1 
ATOM   1580 O  OD2 . ASP B 1 92  ? -16.070 15.149  20.981  1.00 24.49 ? 92  ASP B OD2 1 
ATOM   1581 N  N   . ARG B 1 93  ? -17.483 11.435  17.750  1.00 16.98 ? 93  ARG B N   1 
ATOM   1582 C  CA  . ARG B 1 93  ? -18.776 10.897  17.356  1.00 16.68 ? 93  ARG B CA  1 
ATOM   1583 C  C   . ARG B 1 93  ? -18.618 9.763   16.343  1.00 15.96 ? 93  ARG B C   1 
ATOM   1584 O  O   . ARG B 1 93  ? -19.510 9.520   15.533  1.00 15.53 ? 93  ARG B O   1 
ATOM   1585 C  CB  . ARG B 1 93  ? -19.677 12.017  16.849  1.00 17.53 ? 93  ARG B CB  1 
ATOM   1586 C  CG  . ARG B 1 93  ? -19.955 13.044  17.955  1.00 17.73 ? 93  ARG B CG  1 
ATOM   1587 C  CD  . ARG B 1 93  ? -20.875 14.165  17.492  1.00 17.43 ? 93  ARG B CD  1 
ATOM   1588 N  NE  . ARG B 1 93  ? -22.112 13.638  16.927  1.00 17.12 ? 93  ARG B NE  1 
ATOM   1589 C  CZ  . ARG B 1 93  ? -23.126 13.157  17.645  1.00 17.93 ? 93  ARG B CZ  1 
ATOM   1590 N  NH1 . ARG B 1 93  ? -23.069 13.158  18.977  1.00 18.38 ? 93  ARG B NH1 1 
ATOM   1591 N  NH2 . ARG B 1 93  ? -24.195 12.677  17.033  1.00 18.48 ? 93  ARG B NH2 1 
ATOM   1592 N  N   . VAL B 1 94  ? -17.496 9.042   16.426  1.00 16.46 ? 94  VAL B N   1 
ATOM   1593 C  CA  . VAL B 1 94  ? -17.191 7.894   15.580  1.00 15.90 ? 94  VAL B CA  1 
ATOM   1594 C  C   . VAL B 1 94  ? -16.915 6.693   16.471  1.00 15.11 ? 94  VAL B C   1 
ATOM   1595 O  O   . VAL B 1 94  ? -16.094 6.777   17.393  1.00 15.67 ? 94  VAL B O   1 
ATOM   1596 C  CB  . VAL B 1 94  ? -15.939 8.147   14.713  1.00 16.12 ? 94  VAL B CB  1 
ATOM   1597 C  CG1 . VAL B 1 94  ? -15.539 6.864   13.933  1.00 16.93 ? 94  VAL B CG1 1 
ATOM   1598 C  CG2 . VAL B 1 94  ? -16.140 9.355   13.794  1.00 16.73 ? 94  VAL B CG2 1 
ATOM   1599 N  N   . TYR B 1 95  ? -17.546 5.558   16.155  1.00 14.15 ? 95  TYR B N   1 
ATOM   1600 C  CA  . TYR B 1 95  ? -17.101 4.257   16.648  1.00 14.40 ? 95  TYR B CA  1 
ATOM   1601 C  C   . TYR B 1 95  ? -16.581 3.417   15.495  1.00 14.28 ? 95  TYR B C   1 
ATOM   1602 O  O   . TYR B 1 95  ? -17.171 3.408   14.409  1.00 14.91 ? 95  TYR B O   1 
ATOM   1603 C  CB  . TYR B 1 95  ? -18.247 3.484   17.293  1.00 15.84 ? 95  TYR B CB  1 
ATOM   1604 C  CG  . TYR B 1 95  ? -18.562 3.872   18.724  1.00 16.40 ? 95  TYR B CG  1 
ATOM   1605 C  CD1 . TYR B 1 95  ? -17.553 4.287   19.600  1.00 17.45 ? 95  TYR B CD1 1 
ATOM   1606 C  CD2 . TYR B 1 95  ? -19.866 3.809   19.215  1.00 17.16 ? 95  TYR B CD2 1 
ATOM   1607 C  CE1 . TYR B 1 95  ? -17.839 4.621   20.898  1.00 19.20 ? 95  TYR B CE1 1 
ATOM   1608 C  CE2 . TYR B 1 95  ? -20.156 4.149   20.524  1.00 18.62 ? 95  TYR B CE2 1 
ATOM   1609 C  CZ  . TYR B 1 95  ? -19.132 4.552   21.350  1.00 19.37 ? 95  TYR B CZ  1 
ATOM   1610 O  OH  . TYR B 1 95  ? -19.367 4.888   22.656  1.00 20.65 ? 95  TYR B OH  1 
ATOM   1611 N  N   . ILE B 1 96  ? -15.496 2.685   15.742  1.00 13.66 ? 96  ILE B N   1 
ATOM   1612 C  CA  . ILE B 1 96  ? -14.966 1.709   14.784  1.00 13.42 ? 96  ILE B CA  1 
ATOM   1613 C  C   . ILE B 1 96  ? -14.781 0.390   15.531  1.00 13.55 ? 96  ILE B C   1 
ATOM   1614 O  O   . ILE B 1 96  ? -13.947 0.302   16.437  1.00 14.92 ? 96  ILE B O   1 
ATOM   1615 C  CB  . ILE B 1 96  ? -13.634 2.149   14.155  1.00 14.11 ? 96  ILE B CB  1 
ATOM   1616 C  CG1 . ILE B 1 96  ? -13.720 3.542   13.524  1.00 15.04 ? 96  ILE B CG1 1 
ATOM   1617 C  CG2 . ILE B 1 96  ? -13.206 1.118   13.116  1.00 14.63 ? 96  ILE B CG2 1 
ATOM   1618 C  CD1 . ILE B 1 96  ? -12.366 4.229   13.384  1.00 16.86 ? 96  ILE B CD1 1 
ATOM   1619 N  N   . ASN B 1 97  ? -15.543 -0.634  15.163  1.00 13.75 ? 97  ASN B N   1 
ATOM   1620 C  CA  . ASN B 1 97  ? -15.309 -1.963  15.729  1.00 12.78 ? 97  ASN B CA  1 
ATOM   1621 C  C   . ASN B 1 97  ? -14.334 -2.739  14.852  1.00 12.63 ? 97  ASN B C   1 
ATOM   1622 O  O   . ASN B 1 97  ? -14.486 -2.763  13.632  1.00 13.58 ? 97  ASN B O   1 
ATOM   1623 C  CB  . ASN B 1 97  ? -16.627 -2.724  15.838  1.00 14.35 ? 97  ASN B CB  1 
ATOM   1624 C  CG  . ASN B 1 97  ? -17.479 -2.238  16.983  1.00 17.56 ? 97  ASN B CG  1 
ATOM   1625 O  OD1 . ASN B 1 97  ? -16.959 -1.795  17.993  1.00 19.24 ? 97  ASN B OD1 1 
ATOM   1626 N  ND2 . ASN B 1 97  ? -18.786 -2.316  16.828  1.00 18.41 ? 97  ASN B ND2 1 
ATOM   1627 N  N   . TYR B 1 98  ? -13.345 -3.366  15.483  1.00 11.54 ? 98  TYR B N   1 
ATOM   1628 C  CA  . TYR B 1 98  ? -12.297 -4.118  14.805  1.00 10.77 ? 98  TYR B CA  1 
ATOM   1629 C  C   . TYR B 1 98  ? -12.502 -5.615  15.010  1.00 11.30 ? 98  TYR B C   1 
ATOM   1630 O  O   . TYR B 1 98  ? -12.803 -6.061  16.127  1.00 12.13 ? 98  TYR B O   1 
ATOM   1631 C  CB  . TYR B 1 98  ? -10.912 -3.721  15.341  1.00 12.43 ? 98  TYR B CB  1 
ATOM   1632 C  CG  . TYR B 1 98  ? -10.602 -2.288  15.007  1.00 13.00 ? 98  TYR B CG  1 
ATOM   1633 C  CD1 . TYR B 1 98  ? -10.186 -1.929  13.722  1.00 13.61 ? 98  TYR B CD1 1 
ATOM   1634 C  CD2 . TYR B 1 98  ? -10.778 -1.279  15.945  1.00 13.73 ? 98  TYR B CD2 1 
ATOM   1635 C  CE1 . TYR B 1 98  ? -9.944  -0.614  13.402  1.00 14.08 ? 98  TYR B CE1 1 
ATOM   1636 C  CE2 . TYR B 1 98  ? -10.528 0.035   15.635  1.00 13.05 ? 98  TYR B CE2 1 
ATOM   1637 C  CZ  . TYR B 1 98  ? -10.101 0.365   14.360  1.00 14.13 ? 98  TYR B CZ  1 
ATOM   1638 O  OH  . TYR B 1 98  ? -9.870  1.678   14.032  1.00 14.80 ? 98  TYR B OH  1 
ATOM   1639 N  N   . TYR B 1 99  ? -12.347 -6.382  13.925  1.00 11.35 ? 99  TYR B N   1 
ATOM   1640 C  CA  . TYR B 1 99  ? -12.555 -7.825  13.935  1.00 12.73 ? 99  TYR B CA  1 
ATOM   1641 C  C   . TYR B 1 99  ? -11.365 -8.502  13.277  1.00 12.71 ? 99  TYR B C   1 
ATOM   1642 O  O   . TYR B 1 99  ? -11.103 -8.303  12.082  1.00 12.91 ? 99  TYR B O   1 
ATOM   1643 C  CB  . TYR B 1 99  ? -13.836 -8.184  13.184  1.00 13.45 ? 99  TYR B CB  1 
ATOM   1644 C  CG  . TYR B 1 99  ? -15.037 -7.539  13.797  1.00 14.14 ? 99  TYR B CG  1 
ATOM   1645 C  CD1 . TYR B 1 99  ? -15.694 -8.135  14.863  1.00 16.20 ? 99  TYR B CD1 1 
ATOM   1646 C  CD2 . TYR B 1 99  ? -15.491 -6.298  13.337  1.00 14.37 ? 99  TYR B CD2 1 
ATOM   1647 C  CE1 . TYR B 1 99  ? -16.785 -7.535  15.443  1.00 17.12 ? 99  TYR B CE1 1 
ATOM   1648 C  CE2 . TYR B 1 99  ? -16.585 -5.694  13.916  1.00 15.55 ? 99  TYR B CE2 1 
ATOM   1649 C  CZ  . TYR B 1 99  ? -17.218 -6.306  14.978  1.00 16.29 ? 99  TYR B CZ  1 
ATOM   1650 O  OH  . TYR B 1 99  ? -18.309 -5.720  15.583  1.00 17.94 ? 99  TYR B OH  1 
ATOM   1651 N  N   . ASP B 1 100 ? -10.682 -9.338  14.047  1.00 13.90 ? 100 ASP B N   1 
ATOM   1652 C  CA  . ASP B 1 100 ? -9.600  -10.177 13.553  1.00 14.52 ? 100 ASP B CA  1 
ATOM   1653 C  C   . ASP B 1 100 ? -10.243 -11.502 13.148  1.00 14.62 ? 100 ASP B C   1 
ATOM   1654 O  O   . ASP B 1 100 ? -10.640 -12.306 14.001  1.00 15.32 ? 100 ASP B O   1 
ATOM   1655 C  CB  . ASP B 1 100 ? -8.564  -10.353 14.659  1.00 15.81 ? 100 ASP B CB  1 
ATOM   1656 C  CG  . ASP B 1 100 ? -7.312  -11.061 14.193  1.00 17.66 ? 100 ASP B CG  1 
ATOM   1657 O  OD1 . ASP B 1 100 ? -7.244  -11.495 13.020  1.00 17.27 ? 100 ASP B OD1 1 
ATOM   1658 O  OD2 . ASP B 1 100 ? -6.387  -11.162 15.024  1.00 19.82 ? 100 ASP B OD2 1 
ATOM   1659 N  N   . MET B 1 101 ? -10.396 -11.709 11.850  1.00 14.37 ? 101 MET B N   1 
ATOM   1660 C  CA  . MET B 1 101 ? -11.108 -12.871 11.329  1.00 13.50 ? 101 MET B CA  1 
ATOM   1661 C  C   . MET B 1 101 ? -10.165 -14.045 11.107  1.00 13.32 ? 101 MET B C   1 
ATOM   1662 O  O   . MET B 1 101 ? -9.062  -13.887 10.575  1.00 13.66 ? 101 MET B O   1 
ATOM   1663 C  CB  . MET B 1 101 ? -11.782 -12.533 10.001  1.00 14.25 ? 101 MET B CB  1 
ATOM   1664 C  CG  . MET B 1 101 ? -12.807 -11.423 10.067  1.00 14.92 ? 101 MET B CG  1 
ATOM   1665 S  SD  . MET B 1 101 ? -14.205 -11.752 11.145  1.00 16.30 ? 101 MET B SD  1 
ATOM   1666 C  CE  . MET B 1 101 ? -14.971 -13.164 10.362  1.00 16.61 ? 101 MET B CE  1 
ATOM   1667 N  N   . ASN B 1 102 ? -10.624 -15.233 11.470  1.00 13.44 ? 102 ASN B N   1 
ATOM   1668 C  CA  . ASN B 1 102 ? -9.932  -16.452 11.053  1.00 13.61 ? 102 ASN B CA  1 
ATOM   1669 C  C   . ASN B 1 102 ? -10.168 -16.696 9.568   1.00 13.12 ? 102 ASN B C   1 
ATOM   1670 O  O   . ASN B 1 102 ? -11.277 -16.475 9.064   1.00 13.32 ? 102 ASN B O   1 
ATOM   1671 C  CB  . ASN B 1 102 ? -10.499 -17.639 11.827  1.00 15.89 ? 102 ASN B CB  1 
ATOM   1672 C  CG  . ASN B 1 102 ? -10.162 -17.585 13.295  1.00 19.78 ? 102 ASN B CG  1 
ATOM   1673 O  OD1 . ASN B 1 102 ? -9.289  -16.831 13.711  1.00 22.85 ? 102 ASN B OD1 1 
ATOM   1674 N  ND2 . ASN B 1 102 ? -10.869 -18.365 14.092  1.00 21.04 ? 102 ASN B ND2 1 
ATOM   1675 N  N   . ALA B 1 103 ? -9.121  -17.155 8.865   1.00 13.38 ? 103 ALA B N   1 
ATOM   1676 C  CA  . ALA B 1 103 ? -9.247  -17.377 7.432   1.00 13.94 ? 103 ALA B CA  1 
ATOM   1677 C  C   . ALA B 1 103 ? -10.355 -18.375 7.134   1.00 13.72 ? 103 ALA B C   1 
ATOM   1678 O  O   . ALA B 1 103 ? -11.025 -18.277 6.100   1.00 14.21 ? 103 ALA B O   1 
ATOM   1679 C  CB  . ALA B 1 103 ? -7.913  -17.850 6.867   1.00 13.73 ? 103 ALA B CB  1 
ATOM   1680 N  N   . ALA B 1 104 ? -10.567 -19.345 8.026   1.00 13.50 ? 104 ALA B N   1 
ATOM   1681 C  CA  . ALA B 1 104 ? -11.606 -20.337 7.807   1.00 13.84 ? 104 ALA B CA  1 
ATOM   1682 C  C   . ALA B 1 104 ? -12.998 -19.739 7.881   1.00 13.47 ? 104 ALA B C   1 
ATOM   1683 O  O   . ALA B 1 104 ? -13.960 -20.395 7.448   1.00 13.97 ? 104 ALA B O   1 
ATOM   1684 C  CB  . ALA B 1 104 ? -11.495 -21.445 8.849   1.00 14.18 ? 104 ALA B CB  1 
ATOM   1685 N  N   . ASN B 1 105 ? -13.128 -18.524 8.435   1.00 12.89 ? 105 ASN B N   1 
ATOM   1686 C  CA  . ASN B 1 105 ? -14.413 -17.852 8.593   1.00 12.55 ? 105 ASN B CA  1 
ATOM   1687 C  C   . ASN B 1 105 ? -14.601 -16.717 7.589   1.00 11.88 ? 105 ASN B C   1 
ATOM   1688 O  O   . ASN B 1 105 ? -15.505 -15.900 7.751   1.00 12.41 ? 105 ASN B O   1 
ATOM   1689 C  CB  . ASN B 1 105 ? -14.619 -17.380 10.032  1.00 13.00 ? 105 ASN B CB  1 
ATOM   1690 C  CG  . ASN B 1 105 ? -14.799 -18.523 10.967  1.00 14.15 ? 105 ASN B CG  1 
ATOM   1691 O  OD1 . ASN B 1 105 ? -15.281 -19.582 10.564  1.00 14.95 ? 105 ASN B OD1 1 
ATOM   1692 N  ND2 . ASN B 1 105 ? -14.415 -18.330 12.223  1.00 14.49 ? 105 ASN B ND2 1 
ATOM   1693 N  N   . VAL B 1 106 ? -13.786 -16.669 6.536   1.00 12.62 ? 106 VAL B N   1 
ATOM   1694 C  CA  . VAL B 1 106 ? -13.964 -15.680 5.471   1.00 12.32 ? 106 VAL B CA  1 
ATOM   1695 C  C   . VAL B 1 106 ? -14.096 -16.402 4.140   1.00 12.04 ? 106 VAL B C   1 
ATOM   1696 O  O   . VAL B 1 106 ? -13.121 -16.987 3.628   1.00 12.51 ? 106 VAL B O   1 
ATOM   1697 C  CB  . VAL B 1 106 ? -12.841 -14.648 5.436   1.00 13.25 ? 106 VAL B CB  1 
ATOM   1698 C  CG1 . VAL B 1 106 ? -13.106 -13.625 4.339   1.00 13.70 ? 106 VAL B CG1 1 
ATOM   1699 C  CG2 . VAL B 1 106 ? -12.727 -13.976 6.788   1.00 13.26 ? 106 VAL B CG2 1 
ATOM   1700 N  N   . GLY B 1 107 ? -15.294 -16.351 3.572   1.00 13.30 ? 107 GLY B N   1 
ATOM   1701 C  CA  . GLY B 1 107 ? -15.550 -16.926 2.266   1.00 14.35 ? 107 GLY B CA  1 
ATOM   1702 C  C   . GLY B 1 107 ? -15.294 -15.942 1.141   1.00 14.36 ? 107 GLY B C   1 
ATOM   1703 O  O   . GLY B 1 107 ? -15.465 -14.734 1.293   1.00 13.91 ? 107 GLY B O   1 
ATOM   1704 N  N   . TRP B 1 108 ? -14.884 -16.491 0.003   1.00 14.64 ? 108 TRP B N   1 
ATOM   1705 C  CA  . TRP B 1 108 ? -14.551 -15.696 -1.171  1.00 14.92 ? 108 TRP B CA  1 
ATOM   1706 C  C   . TRP B 1 108 ? -14.411 -16.657 -2.332  1.00 16.06 ? 108 TRP B C   1 
ATOM   1707 O  O   . TRP B 1 108 ? -13.798 -17.726 -2.186  1.00 16.74 ? 108 TRP B O   1 
ATOM   1708 C  CB  . TRP B 1 108 ? -13.214 -14.965 -0.944  1.00 14.67 ? 108 TRP B CB  1 
ATOM   1709 C  CG  . TRP B 1 108 ? -12.679 -14.297 -2.173  1.00 14.78 ? 108 TRP B CG  1 
ATOM   1710 C  CD1 . TRP B 1 108 ? -13.167 -13.163 -2.767  1.00 14.94 ? 108 TRP B CD1 1 
ATOM   1711 C  CD2 . TRP B 1 108 ? -11.537 -14.707 -2.946  1.00 15.97 ? 108 TRP B CD2 1 
ATOM   1712 N  NE1 . TRP B 1 108 ? -12.397 -12.848 -3.876  1.00 15.52 ? 108 TRP B NE1 1 
ATOM   1713 C  CE2 . TRP B 1 108 ? -11.388 -13.779 -4.005  1.00 16.05 ? 108 TRP B CE2 1 
ATOM   1714 C  CE3 . TRP B 1 108 ? -10.626 -15.772 -2.844  1.00 17.68 ? 108 TRP B CE3 1 
ATOM   1715 C  CZ2 . TRP B 1 108 ? -10.360 -13.897 -4.971  1.00 16.66 ? 108 TRP B CZ2 1 
ATOM   1716 C  CZ3 . TRP B 1 108 ? -9.611  -15.890 -3.788  1.00 18.25 ? 108 TRP B CZ3 1 
ATOM   1717 C  CH2 . TRP B 1 108 ? -9.485  -14.962 -4.842  1.00 17.68 ? 108 TRP B CH2 1 
ATOM   1718 N  N   . ASN B 1 109 ? -15.010 -16.326 -3.473  1.00 15.98 ? 109 ASN B N   1 
ATOM   1719 C  CA  . ASN B 1 109 ? -14.688 -17.031 -4.711  1.00 17.69 ? 109 ASN B CA  1 
ATOM   1720 C  C   . ASN B 1 109 ? -14.885 -18.547 -4.577  1.00 18.39 ? 109 ASN B C   1 
ATOM   1721 O  O   . ASN B 1 109 ? -14.005 -19.356 -4.899  1.00 19.35 ? 109 ASN B O   1 
ATOM   1722 C  CB  . ASN B 1 109 ? -13.274 -16.659 -5.138  1.00 18.09 ? 109 ASN B CB  1 
ATOM   1723 C  CG  . ASN B 1 109 ? -12.990 -16.977 -6.586  1.00 19.12 ? 109 ASN B CG  1 
ATOM   1724 O  OD1 . ASN B 1 109 ? -13.876 -17.359 -7.349  1.00 19.97 ? 109 ASN B OD1 1 
ATOM   1725 N  ND2 . ASN B 1 109 ? -11.769 -16.730 -6.991  1.00 20.18 ? 109 ASN B ND2 1 
ATOM   1726 N  N   . ASN B 1 110 ? -16.057 -18.923 -4.078  1.00 18.23 ? 110 ASN B N   1 
ATOM   1727 C  CA  . ASN B 1 110 ? -16.541 -20.296 -3.973  1.00 19.03 ? 110 ASN B CA  1 
ATOM   1728 C  C   . ASN B 1 110 ? -15.873 -21.117 -2.875  1.00 18.04 ? 110 ASN B C   1 
ATOM   1729 O  O   . ASN B 1 110 ? -16.130 -22.321 -2.782  1.00 18.50 ? 110 ASN B O   1 
ATOM   1730 C  CB  . ASN B 1 110 ? -16.514 -21.049 -5.311  1.00 21.08 ? 110 ASN B CB  1 
ATOM   1731 C  CG  . ASN B 1 110 ? -17.577 -20.556 -6.264  1.00 23.39 ? 110 ASN B CG  1 
ATOM   1732 O  OD1 . ASN B 1 110 ? -18.750 -20.452 -5.889  1.00 25.00 ? 110 ASN B OD1 1 
ATOM   1733 N  ND2 . ASN B 1 110 ? -17.189 -20.297 -7.512  1.00 24.53 ? 110 ASN B ND2 1 
ATOM   1734 N  N   . SER B 1 111 ? -15.062 -20.509 -2.021  1.00 17.79 ? 111 SER B N   1 
ATOM   1735 C  CA  . SER B 1 111 ? -14.384 -21.260 -0.969  1.00 17.36 ? 111 SER B CA  1 
ATOM   1736 C  C   . SER B 1 111 ? -14.147 -20.331 0.215   1.00 16.17 ? 111 SER B C   1 
ATOM   1737 O  O   . SER B 1 111 ? -14.834 -19.320 0.364   1.00 16.39 ? 111 SER B O   1 
ATOM   1738 C  CB  . SER B 1 111 ? -13.100 -21.883 -1.541  1.00 18.14 ? 111 SER B CB  1 
ATOM   1739 O  OG  . SER B 1 111 ? -12.484 -22.698 -0.575  1.00 19.34 ? 111 SER B OG  1 
ATOM   1740 N  N   . THR B 1 112 ? -13.209 -20.687 1.087   1.00 15.10 ? 112 THR B N   1 
ATOM   1741 C  CA  . THR B 1 112 ? -12.748 -19.772 2.130   1.00 14.78 ? 112 THR B CA  1 
ATOM   1742 C  C   . THR B 1 112 ? -11.240 -19.653 1.988   1.00 15.75 ? 112 THR B C   1 
ATOM   1743 O  O   . THR B 1 112 ? -10.602 -20.404 1.242   1.00 18.25 ? 112 THR B O   1 
ATOM   1744 C  CB  . THR B 1 112 ? -13.093 -20.263 3.545   1.00 13.88 ? 112 THR B CB  1 
ATOM   1745 O  OG1 . THR B 1 112 ? -12.304 -21.419 3.836   1.00 15.30 ? 112 THR B OG1 1 
ATOM   1746 C  CG2 . THR B 1 112 ? -14.574 -20.589 3.691   1.00 13.54 ? 112 THR B CG2 1 
ATOM   1747 N  N   . PHE B 1 113 ? -10.664 -18.721 2.744   1.00 14.72 ? 113 PHE B N   1 
ATOM   1748 C  CA  . PHE B 1 113 ? -9.237  -18.481 2.655   1.00 15.26 ? 113 PHE B CA  1 
ATOM   1749 C  C   . PHE B 1 113 ? -8.401  -19.491 3.427   1.00 15.76 ? 113 PHE B C   1 
ATOM   1750 O  O   . PHE B 1 113 ? -7.182  -19.515 3.219   1.00 16.99 ? 113 PHE B O   1 
ATOM   1751 C  CB  . PHE B 1 113 ? -8.912  -17.063 3.140   1.00 15.72 ? 113 PHE B CB  1 
ATOM   1752 C  CG  . PHE B 1 113 ? -9.264  -16.000 2.149   1.00 15.71 ? 113 PHE B CG  1 
ATOM   1753 C  CD1 . PHE B 1 113 ? -8.607  -15.962 0.916   1.00 16.04 ? 113 PHE B CD1 1 
ATOM   1754 C  CD2 . PHE B 1 113 ? -10.224 -15.044 2.423   1.00 15.68 ? 113 PHE B CD2 1 
ATOM   1755 C  CE1 . PHE B 1 113 ? -8.915  -14.994 -0.032  1.00 16.72 ? 113 PHE B CE1 1 
ATOM   1756 C  CE2 . PHE B 1 113 ? -10.532 -14.046 1.485   1.00 15.90 ? 113 PHE B CE2 1 
ATOM   1757 C  CZ  . PHE B 1 113 ? -9.874  -14.024 0.255   1.00 16.42 ? 113 PHE B CZ  1 
ATOM   1758 N  N   . ALA B 1 114 ? -9.013  -20.365 4.237   1.00 15.74 ? 114 ALA B N   1 
ATOM   1759 C  CA  . ALA B 1 114 ? -8.235  -21.287 5.062   1.00 16.65 ? 114 ALA B CA  1 
ATOM   1760 C  C   . ALA B 1 114 ? -7.371  -22.196 4.203   1.00 18.23 ? 114 ALA B C   1 
ATOM   1761 O  O   . ALA B 1 114 ? -7.819  -22.689 3.162   1.00 19.51 ? 114 ALA B O   1 
ATOM   1762 C  CB  . ALA B 1 114 ? -9.134  -22.120 5.979   1.00 16.17 ? 114 ALA B CB  1 
ATOM   1763 O  OXT . ALA B 1 114 ? -6.227  -22.449 4.558   1.00 19.12 ? 114 ALA B OXT 1 
ATOM   1764 N  N   . PRO C 1 1   ? -21.821 1.654   23.913  1.00 18.95 ? 1   PRO C N   1 
ATOM   1765 C  CA  . PRO C 1 1   ? -22.421 0.533   23.208  1.00 18.03 ? 1   PRO C CA  1 
ATOM   1766 C  C   . PRO C 1 1   ? -23.058 1.019   21.933  1.00 16.73 ? 1   PRO C C   1 
ATOM   1767 O  O   . PRO C 1 1   ? -23.288 2.218   21.750  1.00 17.61 ? 1   PRO C O   1 
ATOM   1768 C  CB  . PRO C 1 1   ? -23.503 0.051   24.181  1.00 19.25 ? 1   PRO C CB  1 
ATOM   1769 C  CG  . PRO C 1 1   ? -23.000 0.416   25.498  1.00 20.34 ? 1   PRO C CG  1 
ATOM   1770 C  CD  . PRO C 1 1   ? -22.272 1.723   25.312  1.00 19.45 ? 1   PRO C CD  1 
ATOM   1771 N  N   . MET C 1 2   ? -23.380 0.079   21.064  1.00 15.09 ? 2   MET C N   1 
ATOM   1772 C  CA  . MET C 1 2   ? -23.981 0.376   19.778  1.00 15.33 ? 2   MET C CA  1 
ATOM   1773 C  C   . MET C 1 2   ? -25.130 -0.592  19.579  1.00 14.20 ? 2   MET C C   1 
ATOM   1774 O  O   . MET C 1 2   ? -24.954 -1.803  19.731  1.00 15.47 ? 2   MET C O   1 
ATOM   1775 C  CB  . MET C 1 2   ? -22.916 0.104   18.731  1.00 18.79 ? 2   MET C CB  1 
ATOM   1776 C  CG  . MET C 1 2   ? -23.301 0.378   17.319  1.00 22.69 ? 2   MET C CG  1 
ATOM   1777 S  SD  . MET C 1 2   ? -21.917 -0.127  16.294  1.00 26.49 ? 2   MET C SD  1 
ATOM   1778 C  CE  . MET C 1 2   ? -20.515 0.587   17.160  1.00 26.71 ? 2   MET C CE  1 
ATOM   1779 N  N   . PHE C 1 3   ? -26.286 -0.070  19.199  1.00 12.76 ? 3   PHE C N   1 
ATOM   1780 C  CA  . PHE C 1 3   ? -27.451 -0.900  18.938  1.00 12.56 ? 3   PHE C CA  1 
ATOM   1781 C  C   . PHE C 1 3   ? -27.970 -0.583  17.547  1.00 11.73 ? 3   PHE C C   1 
ATOM   1782 O  O   . PHE C 1 3   ? -28.229 0.584   17.239  1.00 12.83 ? 3   PHE C O   1 
ATOM   1783 C  CB  . PHE C 1 3   ? -28.546 -0.676  19.996  1.00 12.92 ? 3   PHE C CB  1 
ATOM   1784 C  CG  . PHE C 1 3   ? -29.776 -1.491  19.756  1.00 12.75 ? 3   PHE C CG  1 
ATOM   1785 C  CD1 . PHE C 1 3   ? -29.731 -2.889  19.830  1.00 13.47 ? 3   PHE C CD1 1 
ATOM   1786 C  CD2 . PHE C 1 3   ? -30.971 -0.881  19.395  1.00 14.13 ? 3   PHE C CD2 1 
ATOM   1787 C  CE1 . PHE C 1 3   ? -30.851 -3.657  19.579  1.00 14.13 ? 3   PHE C CE1 1 
ATOM   1788 C  CE2 . PHE C 1 3   ? -32.105 -1.656  19.129  1.00 15.44 ? 3   PHE C CE2 1 
ATOM   1789 C  CZ  . PHE C 1 3   ? -32.035 -3.048  19.212  1.00 15.20 ? 3   PHE C CZ  1 
ATOM   1790 N  N   . ILE C 1 4   ? -28.130 -1.612  16.713  1.00 11.41 ? 4   ILE C N   1 
ATOM   1791 C  CA  . ILE C 1 4   ? -28.581 -1.449  15.333  1.00 11.45 ? 4   ILE C CA  1 
ATOM   1792 C  C   . ILE C 1 4   ? -29.839 -2.293  15.158  1.00 11.54 ? 4   ILE C C   1 
ATOM   1793 O  O   . ILE C 1 4   ? -29.877 -3.448  15.596  1.00 11.77 ? 4   ILE C O   1 
ATOM   1794 C  CB  . ILE C 1 4   ? -27.506 -1.865  14.304  1.00 13.07 ? 4   ILE C CB  1 
ATOM   1795 C  CG1 . ILE C 1 4   ? -26.164 -1.184  14.588  1.00 15.38 ? 4   ILE C CG1 1 
ATOM   1796 C  CG2 . ILE C 1 4   ? -27.980 -1.565  12.867  1.00 13.66 ? 4   ILE C CG2 1 
ATOM   1797 C  CD1 . ILE C 1 4   ? -24.977 -1.841  13.949  1.00 17.36 ? 4   ILE C CD1 1 
ATOM   1798 N  N   . VAL C 1 5   ? -30.869 -1.720  14.538  1.00 12.12 ? 5   VAL C N   1 
ATOM   1799 C  CA  . VAL C 1 5   ? -32.076 -2.461  14.183  1.00 12.92 ? 5   VAL C CA  1 
ATOM   1800 C  C   . VAL C 1 5   ? -32.292 -2.317  12.689  1.00 12.06 ? 5   VAL C C   1 
ATOM   1801 O  O   . VAL C 1 5   ? -32.363 -1.199  12.159  1.00 13.25 ? 5   VAL C O   1 
ATOM   1802 C  CB  . VAL C 1 5   ? -33.323 -2.030  14.977  1.00 16.40 ? 5   VAL C CB  1 
ATOM   1803 C  CG1 . VAL C 1 5   ? -33.476 -0.589  14.972  1.00 19.45 ? 5   VAL C CG1 1 
ATOM   1804 C  CG2 . VAL C 1 5   ? -34.554 -2.674  14.422  1.00 16.64 ? 5   VAL C CG2 1 
ATOM   1805 N  N   . ASN C 1 6   ? -32.354 -3.444  12.008  1.00 11.90 ? 6   ASN C N   1 
ATOM   1806 C  CA  . ASN C 1 6   ? -32.738 -3.495  10.602  1.00 12.16 ? 6   ASN C CA  1 
ATOM   1807 C  C   . ASN C 1 6   ? -34.125 -4.095  10.512  1.00 11.69 ? 6   ASN C C   1 
ATOM   1808 O  O   . ASN C 1 6   ? -34.378 -5.146  11.107  1.00 11.60 ? 6   ASN C O   1 
ATOM   1809 C  CB  . ASN C 1 6   ? -31.762 -4.356  9.809   1.00 14.36 ? 6   ASN C CB  1 
ATOM   1810 C  CG  . ASN C 1 6   ? -30.486 -3.651  9.583   1.00 18.33 ? 6   ASN C CG  1 
ATOM   1811 O  OD1 . ASN C 1 6   ? -30.341 -2.948  8.595   1.00 19.62 ? 6   ASN C OD1 1 
ATOM   1812 N  ND2 . ASN C 1 6   ? -29.546 -3.832  10.487  1.00 20.53 ? 6   ASN C ND2 1 
ATOM   1813 N  N   . THR C 1 7   ? -35.019 -3.437  9.775   1.00 11.88 ? 7   THR C N   1 
ATOM   1814 C  CA  . THR C 1 7   ? -36.406 -3.896  9.756   1.00 11.79 ? 7   THR C CA  1 
ATOM   1815 C  C   . THR C 1 7   ? -37.044 -3.583  8.407   1.00 11.41 ? 7   THR C C   1 
ATOM   1816 O  O   . THR C 1 7   ? -36.666 -2.624  7.714   1.00 11.30 ? 7   THR C O   1 
ATOM   1817 C  CB  . THR C 1 7   ? -37.236 -3.277  10.905  1.00 12.21 ? 7   THR C CB  1 
ATOM   1818 O  OG1 . THR C 1 7   ? -38.586 -3.756  10.836  1.00 13.16 ? 7   THR C OG1 1 
ATOM   1819 C  CG2 . THR C 1 7   ? -37.235 -1.736  10.823  1.00 12.59 ? 7   THR C CG2 1 
ATOM   1820 N  N   . ASN C 1 8   ? -38.036 -4.398  8.046   1.00 11.35 ? 8   ASN C N   1 
ATOM   1821 C  CA  . ASN C 1 8   ? -38.841 -4.153  6.860   1.00 11.96 ? 8   ASN C CA  1 
ATOM   1822 C  C   . ASN C 1 8   ? -40.004 -3.214  7.133   1.00 13.67 ? 8   ASN C C   1 
ATOM   1823 O  O   . ASN C 1 8   ? -40.718 -2.849  6.197   1.00 15.46 ? 8   ASN C O   1 
ATOM   1824 C  CB  . ASN C 1 8   ? -39.338 -5.475  6.232   1.00 12.40 ? 8   ASN C CB  1 
ATOM   1825 C  CG  . ASN C 1 8   ? -40.073 -6.379  7.209   1.00 13.37 ? 8   ASN C CG  1 
ATOM   1826 O  OD1 . ASN C 1 8   ? -40.054 -6.157  8.414   1.00 13.19 ? 8   ASN C OD1 1 
ATOM   1827 N  ND2 . ASN C 1 8   ? -40.697 -7.420  6.684   1.00 14.68 ? 8   ASN C ND2 1 
ATOM   1828 N  N   . VAL C 1 9   ? -40.219 -2.823  8.387   1.00 13.27 ? 9   VAL C N   1 
ATOM   1829 C  CA  . VAL C 1 9   ? -41.268 -1.841  8.688   1.00 15.46 ? 9   VAL C CA  1 
ATOM   1830 C  C   . VAL C 1 9   ? -40.931 -0.547  7.953   1.00 16.37 ? 9   VAL C C   1 
ATOM   1831 O  O   . VAL C 1 9   ? -39.741 -0.169  7.870   1.00 16.81 ? 9   VAL C O   1 
ATOM   1832 C  CB  . VAL C 1 9   ? -41.358 -1.629  10.216  1.00 16.77 ? 9   VAL C CB  1 
ATOM   1833 C  CG1 . VAL C 1 9   ? -42.193 -0.434  10.593  1.00 18.30 ? 9   VAL C CG1 1 
ATOM   1834 C  CG2 . VAL C 1 9   ? -41.915 -2.889  10.866  1.00 16.69 ? 9   VAL C CG2 1 
ATOM   1835 N  N   . PRO C 1 10  ? -41.899 0.128   7.341   1.00 17.22 ? 10  PRO C N   1 
ATOM   1836 C  CA  . PRO C 1 10  ? -41.583 1.348   6.587   1.00 18.16 ? 10  PRO C CA  1 
ATOM   1837 C  C   . PRO C 1 10  ? -41.221 2.518   7.498   1.00 17.68 ? 10  PRO C C   1 
ATOM   1838 O  O   . PRO C 1 10  ? -41.613 2.582   8.668   1.00 17.89 ? 10  PRO C O   1 
ATOM   1839 C  CB  . PRO C 1 10  ? -42.856 1.623   5.776   1.00 19.15 ? 10  PRO C CB  1 
ATOM   1840 C  CG  . PRO C 1 10  ? -43.942 0.871   6.466   1.00 19.15 ? 10  PRO C CG  1 
ATOM   1841 C  CD  . PRO C 1 10  ? -43.298 -0.301  7.187   1.00 18.09 ? 10  PRO C CD  1 
ATOM   1842 N  N   . ARG C 1 11  ? -40.466 3.468   6.928   1.00 18.00 ? 11  ARG C N   1 
ATOM   1843 C  CA  . ARG C 1 11  ? -39.978 4.609   7.705   1.00 19.23 ? 11  ARG C CA  1 
ATOM   1844 C  C   . ARG C 1 11  ? -41.115 5.385   8.361   1.00 18.14 ? 11  ARG C C   1 
ATOM   1845 O  O   . ARG C 1 11  ? -40.981 5.840   9.504   1.00 17.92 ? 11  ARG C O   1 
ATOM   1846 C  CB  . ARG C 1 11  ? -39.114 5.530   6.834   1.00 22.87 ? 11  ARG C CB  1 
ATOM   1847 C  CG  . ARG C 1 11  ? -38.684 6.849   7.508   1.00 26.94 ? 11  ARG C CG  1 
ATOM   1848 C  CD  . ARG C 1 11  ? -37.845 6.633   8.771   1.00 30.50 ? 11  ARG C CD  1 
ATOM   1849 N  NE  . ARG C 1 11  ? -37.397 7.889   9.382   1.00 33.48 ? 11  ARG C NE  1 
ATOM   1850 C  CZ  . ARG C 1 11  ? -37.973 8.455   10.442  1.00 35.15 ? 11  ARG C CZ  1 
ATOM   1851 N  NH1 . ARG C 1 11  ? -39.020 7.878   11.022  1.00 35.58 ? 11  ARG C NH1 1 
ATOM   1852 N  NH2 . ARG C 1 11  ? -37.496 9.597   10.935  1.00 35.78 ? 11  ARG C NH2 1 
ATOM   1853 N  N   . ALA C 1 12  ? -42.241 5.557   7.660   1.00 18.08 ? 12  ALA C N   1 
ATOM   1854 C  CA  . ALA C 1 12  ? -43.358 6.316   8.225   1.00 19.84 ? 12  ALA C CA  1 
ATOM   1855 C  C   . ALA C 1 12  ? -43.949 5.661   9.469   1.00 19.97 ? 12  ALA C C   1 
ATOM   1856 O  O   . ALA C 1 12  ? -44.650 6.334   10.239  1.00 21.32 ? 12  ALA C O   1 
ATOM   1857 C  CB  . ALA C 1 12  ? -44.456 6.533   7.182   1.00 20.80 ? 12  ALA C CB  1 
ATOM   1858 N  N   A SER C 1 13  ? -43.673 4.368   9.683   0.81 19.59 ? 13  SER C N   1 
ATOM   1859 N  N   B SER C 1 13  ? -43.693 4.375   9.692   0.19 19.90 ? 13  SER C N   1 
ATOM   1860 C  CA  A SER C 1 13  ? -44.166 3.634   10.837  0.81 19.87 ? 13  SER C CA  1 
ATOM   1861 C  CA  B SER C 1 13  ? -44.206 3.710   10.880  0.19 20.24 ? 13  SER C CA  1 
ATOM   1862 C  C   A SER C 1 13  ? -43.203 3.654   12.018  0.81 19.76 ? 13  SER C C   1 
ATOM   1863 C  C   B SER C 1 13  ? -43.250 3.773   12.063  0.19 19.68 ? 13  SER C C   1 
ATOM   1864 O  O   A SER C 1 13  ? -43.545 3.125   13.083  0.81 21.22 ? 13  SER C O   1 
ATOM   1865 O  O   B SER C 1 13  ? -43.640 3.394   13.173  0.19 20.34 ? 13  SER C O   1 
ATOM   1866 C  CB  A SER C 1 13  ? -44.497 2.187   10.460  0.81 21.35 ? 13  SER C CB  1 
ATOM   1867 C  CB  B SER C 1 13  ? -44.568 2.259   10.569  0.19 21.37 ? 13  SER C CB  1 
ATOM   1868 O  OG  A SER C 1 13  ? -45.596 2.124   9.560   0.81 22.82 ? 13  SER C OG  1 
ATOM   1869 O  OG  B SER C 1 13  ? -43.920 1.841   9.388   0.19 22.18 ? 13  SER C OG  1 
ATOM   1870 N  N   . VAL C 1 14  ? -42.021 4.238   11.861  1.00 18.44 ? 14  VAL C N   1 
ATOM   1871 C  CA  . VAL C 1 14  ? -41.095 4.446   12.977  1.00 17.39 ? 14  VAL C CA  1 
ATOM   1872 C  C   . VAL C 1 14  ? -41.508 5.726   13.695  1.00 17.50 ? 14  VAL C C   1 
ATOM   1873 O  O   . VAL C 1 14  ? -41.436 6.815   13.108  1.00 18.11 ? 14  VAL C O   1 
ATOM   1874 C  CB  . VAL C 1 14  ? -39.640 4.537   12.489  1.00 16.43 ? 14  VAL C CB  1 
ATOM   1875 C  CG1 . VAL C 1 14  ? -38.676 4.722   13.682  1.00 17.21 ? 14  VAL C CG1 1 
ATOM   1876 C  CG2 . VAL C 1 14  ? -39.259 3.311   11.679  1.00 16.79 ? 14  VAL C CG2 1 
ATOM   1877 N  N   . PRO C 1 15  ? -41.953 5.655   14.943  1.00 16.85 ? 15  PRO C N   1 
ATOM   1878 C  CA  . PRO C 1 15  ? -42.512 6.846   15.588  1.00 16.48 ? 15  PRO C CA  1 
ATOM   1879 C  C   . PRO C 1 15  ? -41.454 7.870   15.946  1.00 15.59 ? 15  PRO C C   1 
ATOM   1880 O  O   . PRO C 1 15  ? -40.267 7.557   16.088  1.00 15.11 ? 15  PRO C O   1 
ATOM   1881 C  CB  . PRO C 1 15  ? -43.171 6.295   16.850  1.00 17.27 ? 15  PRO C CB  1 
ATOM   1882 C  CG  . PRO C 1 15  ? -42.461 5.024   17.131  1.00 17.91 ? 15  PRO C CG  1 
ATOM   1883 C  CD  . PRO C 1 15  ? -42.041 4.464   15.806  1.00 17.16 ? 15  PRO C CD  1 
ATOM   1884 N  N   . ASP C 1 16  ? -41.909 9.115   16.089  1.00 15.49 ? 16  ASP C N   1 
ATOM   1885 C  CA  . ASP C 1 16  ? -41.019 10.166  16.561  1.00 14.89 ? 16  ASP C CA  1 
ATOM   1886 C  C   . ASP C 1 16  ? -40.403 9.780   17.895  1.00 14.72 ? 16  ASP C C   1 
ATOM   1887 O  O   . ASP C 1 16  ? -41.055 9.183   18.758  1.00 16.63 ? 16  ASP C O   1 
ATOM   1888 C  CB  . ASP C 1 16  ? -41.771 11.478  16.786  1.00 15.75 ? 16  ASP C CB  1 
ATOM   1889 C  CG  . ASP C 1 16  ? -42.245 12.104  15.518  1.00 17.08 ? 16  ASP C CG  1 
ATOM   1890 O  OD1 . ASP C 1 16  ? -41.840 11.635  14.430  1.00 19.26 ? 16  ASP C OD1 1 
ATOM   1891 O  OD2 . ASP C 1 16  ? -42.953 13.126  15.596  1.00 18.45 ? 16  ASP C OD2 1 
ATOM   1892 N  N   . GLY C 1 17  ? -39.144 10.170  18.077  1.00 13.35 ? 17  GLY C N   1 
ATOM   1893 C  CA  . GLY C 1 17  ? -38.461 9.936   19.333  1.00 14.59 ? 17  GLY C CA  1 
ATOM   1894 C  C   . GLY C 1 17  ? -37.937 8.541   19.539  1.00 14.71 ? 17  GLY C C   1 
ATOM   1895 O  O   . GLY C 1 17  ? -37.407 8.266   20.625  1.00 15.47 ? 17  GLY C O   1 
ATOM   1896 N  N   . PHE C 1 18  ? -38.025 7.671   18.529  1.00 14.34 ? 18  PHE C N   1 
ATOM   1897 C  CA  . PHE C 1 18  ? -37.627 6.277   18.720  1.00 14.01 ? 18  PHE C CA  1 
ATOM   1898 C  C   . PHE C 1 18  ? -36.134 6.141   19.025  1.00 14.35 ? 18  PHE C C   1 
ATOM   1899 O  O   . PHE C 1 18  ? -35.749 5.335   19.880  1.00 14.53 ? 18  PHE C O   1 
ATOM   1900 C  CB  . PHE C 1 18  ? -38.016 5.453   17.488  1.00 14.34 ? 18  PHE C CB  1 
ATOM   1901 C  CG  . PHE C 1 18  ? -37.851 3.973   17.665  1.00 15.24 ? 18  PHE C CG  1 
ATOM   1902 C  CD1 . PHE C 1 18  ? -38.473 3.311   18.710  1.00 16.40 ? 18  PHE C CD1 1 
ATOM   1903 C  CD2 . PHE C 1 18  ? -37.102 3.229   16.756  1.00 15.59 ? 18  PHE C CD2 1 
ATOM   1904 C  CE1 . PHE C 1 18  ? -38.336 1.919   18.851  1.00 16.88 ? 18  PHE C CE1 1 
ATOM   1905 C  CE2 . PHE C 1 18  ? -36.950 1.867   16.914  1.00 16.36 ? 18  PHE C CE2 1 
ATOM   1906 C  CZ  . PHE C 1 18  ? -37.591 1.209   17.944  1.00 17.41 ? 18  PHE C CZ  1 
ATOM   1907 N  N   . LEU C 1 19  ? -35.273 6.908   18.335  1.00 13.50 ? 19  LEU C N   1 
ATOM   1908 C  CA  . LEU C 1 19  ? -33.839 6.852   18.641  1.00 14.63 ? 19  LEU C CA  1 
ATOM   1909 C  C   . LEU C 1 19  ? -33.566 7.293   20.083  1.00 14.17 ? 19  LEU C C   1 
ATOM   1910 O  O   . LEU C 1 19  ? -32.724 6.709   20.773  1.00 13.63 ? 19  LEU C O   1 
ATOM   1911 C  CB  . LEU C 1 19  ? -33.039 7.710   17.656  1.00 16.17 ? 19  LEU C CB  1 
ATOM   1912 C  CG  . LEU C 1 19  ? -32.931 7.361   16.180  1.00 18.55 ? 19  LEU C CG  1 
ATOM   1913 C  CD1 . LEU C 1 19  ? -32.046 8.395   15.476  1.00 19.88 ? 19  LEU C CD1 1 
ATOM   1914 C  CD2 . LEU C 1 19  ? -32.334 5.996   16.039  1.00 19.10 ? 19  LEU C CD2 1 
ATOM   1915 N  N   A SER C 1 20  ? -34.255 8.337   20.548  0.33 14.62 ? 20  SER C N   1 
ATOM   1916 N  N   B SER C 1 20  ? -34.249 8.341   20.541  0.67 14.45 ? 20  SER C N   1 
ATOM   1917 C  CA  A SER C 1 20  ? -34.067 8.790   21.926  0.33 15.13 ? 20  SER C CA  1 
ATOM   1918 C  CA  B SER C 1 20  ? -34.077 8.800   21.918  0.67 14.61 ? 20  SER C CA  1 
ATOM   1919 C  C   A SER C 1 20  ? -34.554 7.748   22.926  0.33 14.41 ? 20  SER C C   1 
ATOM   1920 C  C   B SER C 1 20  ? -34.551 7.747   22.917  0.67 14.21 ? 20  SER C C   1 
ATOM   1921 O  O   A SER C 1 20  ? -33.890 7.490   23.939  0.33 13.98 ? 20  SER C O   1 
ATOM   1922 O  O   B SER C 1 20  ? -33.868 7.464   23.914  0.67 13.71 ? 20  SER C O   1 
ATOM   1923 C  CB  A SER C 1 20  ? -34.772 10.126  22.150  0.33 16.85 ? 20  SER C CB  1 
ATOM   1924 C  CB  B SER C 1 20  ? -34.820 10.119  22.125  0.67 16.25 ? 20  SER C CB  1 
ATOM   1925 O  OG  A SER C 1 20  ? -33.941 11.193  21.742  0.33 18.14 ? 20  SER C OG  1 
ATOM   1926 O  OG  B SER C 1 20  ? -34.550 10.627  23.410  0.67 17.97 ? 20  SER C OG  1 
ATOM   1927 N  N   . GLU C 1 21  ? -35.706 7.136   22.656  1.00 14.27 ? 21  GLU C N   1 
ATOM   1928 C  CA  . GLU C 1 21  ? -36.228 6.098   23.541  1.00 14.10 ? 21  GLU C CA  1 
ATOM   1929 C  C   . GLU C 1 21  ? -35.255 4.937   23.643  1.00 12.96 ? 21  GLU C C   1 
ATOM   1930 O  O   . GLU C 1 21  ? -34.995 4.433   24.744  1.00 13.72 ? 21  GLU C O   1 
ATOM   1931 C  CB  . GLU C 1 21  ? -37.578 5.620   23.009  1.00 15.50 ? 21  GLU C CB  1 
ATOM   1932 C  CG  . GLU C 1 21  ? -38.338 4.729   23.961  1.00 18.75 ? 21  GLU C CG  1 
ATOM   1933 C  CD  . GLU C 1 21  ? -39.733 4.424   23.446  1.00 21.51 ? 21  GLU C CD  1 
ATOM   1934 O  OE1 . GLU C 1 21  ? -40.026 4.777   22.281  1.00 22.34 ? 21  GLU C OE1 1 
ATOM   1935 O  OE2 . GLU C 1 21  ? -40.548 3.878   24.221  1.00 23.62 ? 21  GLU C OE2 1 
ATOM   1936 N  N   . LEU C 1 22  ? -34.712 4.491   22.498  1.00 13.19 ? 22  LEU C N   1 
ATOM   1937 C  CA  . LEU C 1 22  ? -33.712 3.425   22.527  1.00 13.01 ? 22  LEU C CA  1 
ATOM   1938 C  C   . LEU C 1 22  ? -32.485 3.840   23.329  1.00 13.30 ? 22  LEU C C   1 
ATOM   1939 O  O   . LEU C 1 22  ? -31.979 3.066   24.142  1.00 14.71 ? 22  LEU C O   1 
ATOM   1940 C  CB  . LEU C 1 22  ? -33.311 3.040   21.105  1.00 13.80 ? 22  LEU C CB  1 
ATOM   1941 C  CG  . LEU C 1 22  ? -34.345 2.256   20.300  1.00 15.45 ? 22  LEU C CG  1 
ATOM   1942 C  CD1 . LEU C 1 22  ? -33.893 2.166   18.856  1.00 15.86 ? 22  LEU C CD1 1 
ATOM   1943 C  CD2 . LEU C 1 22  ? -34.520 0.880   20.913  1.00 16.56 ? 22  LEU C CD2 1 
ATOM   1944 N  N   . THR C 1 23  ? -32.003 5.066   23.116  1.00 12.83 ? 23  THR C N   1 
ATOM   1945 C  CA  . THR C 1 23  ? -30.827 5.557   23.838  1.00 13.94 ? 23  THR C CA  1 
ATOM   1946 C  C   . THR C 1 23  ? -31.046 5.531   25.344  1.00 14.35 ? 23  THR C C   1 
ATOM   1947 O  O   . THR C 1 23  ? -30.213 5.008   26.097  1.00 14.26 ? 23  THR C O   1 
ATOM   1948 C  CB  . THR C 1 23  ? -30.475 6.971   23.373  1.00 13.69 ? 23  THR C CB  1 
ATOM   1949 O  OG1 . THR C 1 23  ? -30.182 6.933   21.971  1.00 13.91 ? 23  THR C OG1 1 
ATOM   1950 C  CG2 . THR C 1 23  ? -29.242 7.523   24.114  1.00 13.88 ? 23  THR C CG2 1 
ATOM   1951 N  N   . GLN C 1 24  ? -32.179 6.068   25.797  1.00 14.16 ? 24  GLN C N   1 
ATOM   1952 C  CA  . GLN C 1 24  ? -32.480 6.139   27.218  1.00 14.69 ? 24  GLN C CA  1 
ATOM   1953 C  C   . GLN C 1 24  ? -32.664 4.757   27.823  1.00 15.02 ? 24  GLN C C   1 
ATOM   1954 O  O   . GLN C 1 24  ? -32.173 4.486   28.924  1.00 16.73 ? 24  GLN C O   1 
ATOM   1955 C  CB  . GLN C 1 24  ? -33.745 6.944   27.426  1.00 16.10 ? 24  GLN C CB  1 
ATOM   1956 C  CG  . GLN C 1 24  ? -33.599 8.372   27.062  1.00 17.56 ? 24  GLN C CG  1 
ATOM   1957 C  CD  . GLN C 1 24  ? -34.891 9.123   27.204  1.00 19.97 ? 24  GLN C CD  1 
ATOM   1958 O  OE1 . GLN C 1 24  ? -35.998 8.552   27.153  1.00 20.95 ? 24  GLN C OE1 1 
ATOM   1959 N  NE2 . GLN C 1 24  ? -34.769 10.416  27.359  1.00 21.07 ? 24  GLN C NE2 1 
ATOM   1960 N  N   . GLN C 1 25  ? -33.414 3.888   27.145  1.00 15.31 ? 25  GLN C N   1 
ATOM   1961 C  CA  . GLN C 1 25  ? -33.675 2.557   27.679  1.00 16.83 ? 25  GLN C CA  1 
ATOM   1962 C  C   . GLN C 1 25  ? -32.395 1.725   27.727  1.00 15.87 ? 25  GLN C C   1 
ATOM   1963 O  O   . GLN C 1 25  ? -32.174 0.962   28.681  1.00 15.75 ? 25  GLN C O   1 
ATOM   1964 C  CB  . GLN C 1 25  ? -34.748 1.865   26.841  1.00 18.52 ? 25  GLN C CB  1 
ATOM   1965 C  CG  . GLN C 1 25  ? -36.156 2.498   26.946  1.00 20.80 ? 25  GLN C CG  1 
ATOM   1966 C  CD  . GLN C 1 25  ? -36.792 2.356   28.324  1.00 23.38 ? 25  GLN C CD  1 
ATOM   1967 O  OE1 . GLN C 1 25  ? -36.527 1.396   29.057  1.00 24.37 ? 25  GLN C OE1 1 
ATOM   1968 N  NE2 . GLN C 1 25  ? -37.668 3.283   28.663  1.00 24.63 ? 25  GLN C NE2 1 
ATOM   1969 N  N   . LEU C 1 26  ? -31.529 1.864   26.719  1.00 15.96 ? 26  LEU C N   1 
ATOM   1970 C  CA  . LEU C 1 26  ? -30.285 1.098   26.713  1.00 16.43 ? 26  LEU C CA  1 
ATOM   1971 C  C   . LEU C 1 26  ? -29.312 1.608   27.764  1.00 17.39 ? 26  LEU C C   1 
ATOM   1972 O  O   . LEU C 1 26  ? -28.572 0.817   28.365  1.00 18.44 ? 26  LEU C O   1 
ATOM   1973 C  CB  . LEU C 1 26  ? -29.634 1.184   25.341  1.00 16.89 ? 26  LEU C CB  1 
ATOM   1974 C  CG  . LEU C 1 26  ? -30.328 0.293   24.316  1.00 17.03 ? 26  LEU C CG  1 
ATOM   1975 C  CD1 . LEU C 1 26  ? -29.892 0.704   22.930  1.00 17.72 ? 26  LEU C CD1 1 
ATOM   1976 C  CD2 . LEU C 1 26  ? -29.973 -1.183  24.609  1.00 16.20 ? 26  LEU C CD2 1 
ATOM   1977 N  N   . ALA C 1 27  ? -29.279 2.922   27.995  1.00 17.59 ? 27  ALA C N   1 
ATOM   1978 C  CA  . ALA C 1 27  ? -28.424 3.435   29.064  1.00 19.47 ? 27  ALA C CA  1 
ATOM   1979 C  C   . ALA C 1 27  ? -28.793 2.815   30.395  1.00 20.80 ? 27  ALA C C   1 
ATOM   1980 O  O   . ALA C 1 27  ? -27.917 2.392   31.158  1.00 21.82 ? 27  ALA C O   1 
ATOM   1981 C  CB  . ALA C 1 27  ? -28.549 4.962   29.149  1.00 19.76 ? 27  ALA C CB  1 
ATOM   1982 N  N   . GLN C 1 28  ? -30.090 2.729   30.679  1.00 20.73 ? 28  GLN C N   1 
ATOM   1983 C  CA  . GLN C 1 28  ? -30.511 2.174   31.957  1.00 21.97 ? 28  GLN C CA  1 
ATOM   1984 C  C   . GLN C 1 28  ? -30.258 0.676   32.019  1.00 20.83 ? 28  GLN C C   1 
ATOM   1985 O  O   . GLN C 1 28  ? -29.794 0.153   33.045  1.00 20.40 ? 28  GLN C O   1 
ATOM   1986 C  CB  . GLN C 1 28  ? -31.950 2.563   32.244  1.00 24.79 ? 28  GLN C CB  1 
ATOM   1987 C  CG  . GLN C 1 28  ? -32.030 4.082   32.308  1.00 28.15 ? 28  GLN C CG  1 
ATOM   1988 C  CD  . GLN C 1 28  ? -33.311 4.601   32.914  1.00 31.47 ? 28  GLN C CD  1 
ATOM   1989 O  OE1 . GLN C 1 28  ? -33.265 5.339   33.885  1.00 32.51 ? 28  GLN C OE1 1 
ATOM   1990 N  NE2 . GLN C 1 28  ? -34.455 4.233   32.341  1.00 32.81 ? 28  GLN C NE2 1 
ATOM   1991 N  N   . ALA C 1 29  ? -30.505 -0.021  30.915  1.00 19.69 ? 29  ALA C N   1 
ATOM   1992 C  CA  . ALA C 1 29  ? -30.369 -1.470  30.914  1.00 19.44 ? 29  ALA C CA  1 
ATOM   1993 C  C   . ALA C 1 29  ? -28.913 -1.895  31.024  1.00 19.63 ? 29  ALA C C   1 
ATOM   1994 O  O   . ALA C 1 29  ? -28.592 -2.822  31.768  1.00 20.58 ? 29  ALA C O   1 
ATOM   1995 C  CB  . ALA C 1 29  ? -30.971 -2.035  29.633  1.00 19.43 ? 29  ALA C CB  1 
ATOM   1996 N  N   . THR C 1 30  ? -28.024 -1.246  30.270  1.00 19.63 ? 30  THR C N   1 
ATOM   1997 C  CA  . THR C 1 30  ? -26.619 -1.626  30.261  1.00 19.60 ? 30  THR C CA  1 
ATOM   1998 C  C   . THR C 1 30  ? -25.832 -0.977  31.384  1.00 20.24 ? 30  THR C C   1 
ATOM   1999 O  O   . THR C 1 30  ? -24.760 -1.480  31.730  1.00 20.32 ? 30  THR C O   1 
ATOM   2000 C  CB  . THR C 1 30  ? -25.958 -1.222  28.937  1.00 19.92 ? 30  THR C CB  1 
ATOM   2001 O  OG1 . THR C 1 30  ? -25.986 0.209   28.806  1.00 20.43 ? 30  THR C OG1 1 
ATOM   2002 C  CG2 . THR C 1 30  ? -26.666 -1.857  27.770  1.00 20.24 ? 30  THR C CG2 1 
ATOM   2003 N  N   . GLY C 1 31  ? -26.357 0.097   31.980  1.00 20.49 ? 31  GLY C N   1 
ATOM   2004 C  CA  . GLY C 1 31  ? -25.631 0.895   32.947  1.00 20.18 ? 31  GLY C CA  1 
ATOM   2005 C  C   . GLY C 1 31  ? -24.590 1.833   32.360  1.00 20.80 ? 31  GLY C C   1 
ATOM   2006 O  O   . GLY C 1 31  ? -23.939 2.564   33.120  1.00 22.42 ? 31  GLY C O   1 
ATOM   2007 N  N   . LYS C 1 32  ? -24.441 1.875   31.040  1.00 20.60 ? 32  LYS C N   1 
ATOM   2008 C  CA  . LYS C 1 32  ? -23.419 2.689   30.407  1.00 19.91 ? 32  LYS C CA  1 
ATOM   2009 C  C   . LYS C 1 32  ? -23.882 4.134   30.329  1.00 20.35 ? 32  LYS C C   1 
ATOM   2010 O  O   . LYS C 1 32  ? -25.086 4.412   30.349  1.00 21.37 ? 32  LYS C O   1 
ATOM   2011 C  CB  . LYS C 1 32  ? -23.140 2.164   29.003  1.00 19.99 ? 32  LYS C CB  1 
ATOM   2012 C  CG  . LYS C 1 32  ? -22.682 0.722   28.972  1.00 20.24 ? 32  LYS C CG  1 
ATOM   2013 C  CD  . LYS C 1 32  ? -21.206 0.667   29.174  1.00 19.56 ? 32  LYS C CD  1 
ATOM   2014 C  CE  . LYS C 1 32  ? -20.629 -0.723  28.945  1.00 19.62 ? 32  LYS C CE  1 
ATOM   2015 N  NZ  . LYS C 1 32  ? -19.161 -0.644  29.065  1.00 20.09 ? 32  LYS C NZ  1 
ATOM   2016 N  N   . PRO C 1 33  ? -22.945 5.072   30.252  1.00 20.68 ? 33  PRO C N   1 
ATOM   2017 C  CA  . PRO C 1 33  ? -23.314 6.470   30.143  1.00 21.87 ? 33  PRO C CA  1 
ATOM   2018 C  C   . PRO C 1 33  ? -24.060 6.729   28.849  1.00 21.83 ? 33  PRO C C   1 
ATOM   2019 O  O   . PRO C 1 33  ? -23.648 6.256   27.779  1.00 21.87 ? 33  PRO C O   1 
ATOM   2020 C  CB  . PRO C 1 33  ? -21.955 7.193   30.148  1.00 21.95 ? 33  PRO C CB  1 
ATOM   2021 C  CG  . PRO C 1 33  ? -20.987 6.243   30.737  1.00 21.75 ? 33  PRO C CG  1 
ATOM   2022 C  CD  . PRO C 1 33  ? -21.486 4.889   30.325  1.00 20.58 ? 33  PRO C CD  1 
ATOM   2023 N  N   . PRO C 1 34  ? -25.150 7.502   28.895  1.00 21.49 ? 34  PRO C N   1 
ATOM   2024 C  CA  . PRO C 1 34  ? -25.875 7.784   27.646  1.00 22.12 ? 34  PRO C CA  1 
ATOM   2025 C  C   . PRO C 1 34  ? -24.998 8.402   26.576  1.00 23.02 ? 34  PRO C C   1 
ATOM   2026 O  O   . PRO C 1 34  ? -25.264 8.211   25.384  1.00 22.59 ? 34  PRO C O   1 
ATOM   2027 C  CB  . PRO C 1 34  ? -27.023 8.708   28.075  1.00 22.59 ? 34  PRO C CB  1 
ATOM   2028 C  CG  . PRO C 1 34  ? -26.947 8.832   29.536  1.00 22.64 ? 34  PRO C CG  1 
ATOM   2029 C  CD  . PRO C 1 34  ? -25.890 7.946   30.088  1.00 22.00 ? 34  PRO C CD  1 
ATOM   2030 N  N   . GLN C 1 35  ? -23.951 9.128   26.974  1.00 24.66 ? 35  GLN C N   1 
ATOM   2031 C  CA  . GLN C 1 35  ? -23.026 9.737   26.023  1.00 27.15 ? 35  GLN C CA  1 
ATOM   2032 C  C   . GLN C 1 35  ? -22.326 8.703   25.143  1.00 27.80 ? 35  GLN C C   1 
ATOM   2033 O  O   . GLN C 1 35  ? -21.893 9.028   24.029  1.00 29.52 ? 35  GLN C O   1 
ATOM   2034 C  CB  . GLN C 1 35  ? -21.983 10.542  26.794  1.00 28.98 ? 35  GLN C CB  1 
ATOM   2035 C  CG  . GLN C 1 35  ? -22.586 11.539  27.775  1.00 30.39 ? 35  GLN C CG  1 
ATOM   2036 C  CD  . GLN C 1 35  ? -22.915 10.893  29.133  1.00 31.13 ? 35  GLN C CD  1 
ATOM   2037 O  OE1 . GLN C 1 35  ? -22.028 10.371  29.788  1.00 32.05 ? 35  GLN C OE1 1 
ATOM   2038 N  NE2 . GLN C 1 35  ? -24.183 10.928  29.543  1.00 30.91 ? 35  GLN C NE2 1 
ATOM   2039 N  N   . TYR C 1 36  ? -22.196 7.464   25.609  1.00 26.61 ? 36  TYR C N   1 
ATOM   2040 C  CA  . TYR C 1 36  ? -21.489 6.438   24.852  1.00 26.23 ? 36  TYR C CA  1 
ATOM   2041 C  C   . TYR C 1 36  ? -22.428 5.528   24.089  1.00 21.58 ? 36  TYR C C   1 
ATOM   2042 O  O   . TYR C 1 36  ? -21.970 4.572   23.462  1.00 22.18 ? 36  TYR C O   1 
ATOM   2043 C  CB  . TYR C 1 36  ? -20.623 5.573   25.777  1.00 29.67 ? 36  TYR C CB  1 
ATOM   2044 C  CG  . TYR C 1 36  ? -19.371 6.245   26.283  1.00 33.17 ? 36  TYR C CG  1 
ATOM   2045 C  CD1 . TYR C 1 36  ? -18.298 6.491   25.432  1.00 34.54 ? 36  TYR C CD1 1 
ATOM   2046 C  CD2 . TYR C 1 36  ? -19.259 6.623   27.612  1.00 34.91 ? 36  TYR C CD2 1 
ATOM   2047 C  CE1 . TYR C 1 36  ? -17.149 7.103   25.892  1.00 35.68 ? 36  TYR C CE1 1 
ATOM   2048 C  CE2 . TYR C 1 36  ? -18.120 7.233   28.082  1.00 35.79 ? 36  TYR C CE2 1 
ATOM   2049 C  CZ  . TYR C 1 36  ? -17.069 7.470   27.219  1.00 36.15 ? 36  TYR C CZ  1 
ATOM   2050 O  OH  . TYR C 1 36  ? -15.932 8.081   27.685  1.00 36.74 ? 36  TYR C OH  1 
ATOM   2051 N  N   A ILE C 1 37  ? -23.731 5.778   24.140  0.39 19.28 ? 37  ILE C N   1 
ATOM   2052 N  N   B ILE C 1 37  ? -23.724 5.794   24.103  0.61 19.20 ? 37  ILE C N   1 
ATOM   2053 C  CA  A ILE C 1 37  ? -24.711 4.914   23.491  0.39 17.06 ? 37  ILE C CA  1 
ATOM   2054 C  CA  B ILE C 1 37  ? -24.686 4.909   23.464  0.61 16.82 ? 37  ILE C CA  1 
ATOM   2055 C  C   A ILE C 1 37  ? -24.974 5.442   22.088  0.39 15.68 ? 37  ILE C C   1 
ATOM   2056 C  C   B ILE C 1 37  ? -25.012 5.430   22.082  0.61 15.65 ? 37  ILE C C   1 
ATOM   2057 O  O   A ILE C 1 37  ? -25.350 6.605   21.914  0.39 16.13 ? 37  ILE C O   1 
ATOM   2058 O  O   B ILE C 1 37  ? -25.485 6.561   21.923  0.61 16.36 ? 37  ILE C O   1 
ATOM   2059 C  CB  A ILE C 1 37  ? -26.010 4.842   24.310  0.39 17.16 ? 37  ILE C CB  1 
ATOM   2060 C  CB  B ILE C 1 37  ? -25.947 4.749   24.316  0.61 16.96 ? 37  ILE C CB  1 
ATOM   2061 C  CG1 A ILE C 1 37  ? -25.711 4.321   25.721  0.39 18.25 ? 37  ILE C CG1 1 
ATOM   2062 C  CG1 B ILE C 1 37  ? -25.530 4.054   25.594  0.61 18.09 ? 37  ILE C CG1 1 
ATOM   2063 C  CG2 A ILE C 1 37  ? -27.053 3.975   23.595  0.39 16.97 ? 37  ILE C CG2 1 
ATOM   2064 C  CG2 B ILE C 1 37  ? -27.011 3.945   23.558  0.61 16.91 ? 37  ILE C CG2 1 
ATOM   2065 C  CD1 A ILE C 1 37  ? -25.695 2.808   25.835  0.39 19.03 ? 37  ILE C CD1 1 
ATOM   2066 C  CD1 B ILE C 1 37  ? -26.466 4.253   26.621  0.61 19.07 ? 37  ILE C CD1 1 
ATOM   2067 N  N   . ALA C 1 38  ? -24.771 4.589   21.086  1.00 14.17 ? 38  ALA C N   1 
ATOM   2068 C  CA  . ALA C 1 38  ? -25.081 4.910   19.706  1.00 12.80 ? 38  ALA C CA  1 
ATOM   2069 C  C   . ALA C 1 38  ? -26.209 3.994   19.253  1.00 12.65 ? 38  ALA C C   1 
ATOM   2070 O  O   . ALA C 1 38  ? -26.208 2.798   19.569  1.00 13.12 ? 38  ALA C O   1 
ATOM   2071 C  CB  . ALA C 1 38  ? -23.862 4.717   18.819  1.00 13.55 ? 38  ALA C CB  1 
ATOM   2072 N  N   . VAL C 1 39  ? -27.157 4.551   18.490  1.00 12.47 ? 39  VAL C N   1 
ATOM   2073 C  CA  . VAL C 1 39  ? -28.317 3.807   18.008  1.00 12.85 ? 39  VAL C CA  1 
ATOM   2074 C  C   . VAL C 1 39  ? -28.496 4.081   16.521  1.00 12.70 ? 39  VAL C C   1 
ATOM   2075 O  O   . VAL C 1 39  ? -28.246 5.193   16.038  1.00 13.53 ? 39  VAL C O   1 
ATOM   2076 C  CB  . VAL C 1 39  ? -29.595 4.146   18.821  1.00 13.86 ? 39  VAL C CB  1 
ATOM   2077 C  CG1 . VAL C 1 39  ? -29.407 3.758   20.286  1.00 14.46 ? 39  VAL C CG1 1 
ATOM   2078 C  CG2 . VAL C 1 39  ? -29.947 5.631   18.724  1.00 16.66 ? 39  VAL C CG2 1 
ATOM   2079 N  N   . HIS C 1 40  ? -28.948 3.065   15.794  1.00 11.09 ? 40  HIS C N   1 
ATOM   2080 C  CA  . HIS C 1 40  ? -29.061 3.145   14.342  1.00 11.15 ? 40  HIS C CA  1 
ATOM   2081 C  C   . HIS C 1 40  ? -30.265 2.306   13.940  1.00 11.43 ? 40  HIS C C   1 
ATOM   2082 O  O   . HIS C 1 40  ? -30.349 1.126   14.298  1.00 11.49 ? 40  HIS C O   1 
ATOM   2083 C  CB  . HIS C 1 40  ? -27.767 2.601   13.747  1.00 11.69 ? 40  HIS C CB  1 
ATOM   2084 C  CG  . HIS C 1 40  ? -27.719 2.577   12.254  1.00 12.53 ? 40  HIS C CG  1 
ATOM   2085 N  ND1 . HIS C 1 40  ? -26.750 1.869   11.568  1.00 12.79 ? 40  HIS C ND1 1 
ATOM   2086 C  CD2 . HIS C 1 40  ? -28.486 3.183   11.322  1.00 13.49 ? 40  HIS C CD2 1 
ATOM   2087 C  CE1 . HIS C 1 40  ? -26.932 2.047   10.272  1.00 13.33 ? 40  HIS C CE1 1 
ATOM   2088 N  NE2 . HIS C 1 40  ? -27.984 2.825   10.098  1.00 13.17 ? 40  HIS C NE2 1 
ATOM   2089 N  N   . VAL C 1 41  ? -31.245 2.928   13.282  1.00 11.05 ? 41  VAL C N   1 
ATOM   2090 C  CA  . VAL C 1 41  ? -32.468 2.247   12.866  1.00 11.35 ? 41  VAL C CA  1 
ATOM   2091 C  C   . VAL C 1 41  ? -32.547 2.317   11.353  1.00 11.28 ? 41  VAL C C   1 
ATOM   2092 O  O   . VAL C 1 41  ? -32.401 3.400   10.767  1.00 12.49 ? 41  VAL C O   1 
ATOM   2093 C  CB  . VAL C 1 41  ? -33.723 2.853   13.526  1.00 13.00 ? 41  VAL C CB  1 
ATOM   2094 C  CG1 . VAL C 1 41  ? -34.967 2.154   13.006  1.00 14.31 ? 41  VAL C CG1 1 
ATOM   2095 C  CG2 . VAL C 1 41  ? -33.635 2.765   15.058  1.00 14.29 ? 41  VAL C CG2 1 
ATOM   2096 N  N   . VAL C 1 42  ? -32.762 1.164   10.725  1.00 11.78 ? 42  VAL C N   1 
ATOM   2097 C  CA  . VAL C 1 42  ? -32.758 1.038   9.274   1.00 12.32 ? 42  VAL C CA  1 
ATOM   2098 C  C   . VAL C 1 42  ? -34.081 0.445   8.825   1.00 11.00 ? 42  VAL C C   1 
ATOM   2099 O  O   . VAL C 1 42  ? -34.260 -0.775  8.833   1.00 11.36 ? 42  VAL C O   1 
ATOM   2100 C  CB  . VAL C 1 42  ? -31.593 0.171   8.765   1.00 13.65 ? 42  VAL C CB  1 
ATOM   2101 C  CG1 . VAL C 1 42  ? -31.504 0.290   7.245   1.00 14.17 ? 42  VAL C CG1 1 
ATOM   2102 C  CG2 . VAL C 1 42  ? -30.284 0.523   9.421   1.00 13.67 ? 42  VAL C CG2 1 
ATOM   2103 N  N   . PRO C 1 43  ? -35.037 1.288   8.406   1.00 11.94 ? 43  PRO C N   1 
ATOM   2104 C  CA  . PRO C 1 43  ? -36.348 0.787   7.969   1.00 12.49 ? 43  PRO C CA  1 
ATOM   2105 C  C   . PRO C 1 43  ? -36.383 0.415   6.500   1.00 12.46 ? 43  PRO C C   1 
ATOM   2106 O  O   . PRO C 1 43  ? -35.381 0.557   5.784   1.00 12.77 ? 43  PRO C O   1 
ATOM   2107 C  CB  . PRO C 1 43  ? -37.273 1.987   8.233   1.00 13.66 ? 43  PRO C CB  1 
ATOM   2108 C  CG  . PRO C 1 43  ? -36.375 3.197   8.050   1.00 14.68 ? 43  PRO C CG  1 
ATOM   2109 C  CD  . PRO C 1 43  ? -34.981 2.766   8.469   1.00 12.71 ? 43  PRO C CD  1 
ATOM   2110 N  N   . ASP C 1 44  ? -37.541 -0.053  6.041   1.00 13.24 ? 44  ASP C N   1 
ATOM   2111 C  CA  . ASP C 1 44  ? -37.796 -0.267  4.607   1.00 14.19 ? 44  ASP C CA  1 
ATOM   2112 C  C   . ASP C 1 44  ? -36.903 -1.335  3.998   1.00 13.70 ? 44  ASP C C   1 
ATOM   2113 O  O   . ASP C 1 44  ? -36.642 -1.310  2.793   1.00 15.22 ? 44  ASP C O   1 
ATOM   2114 C  CB  . ASP C 1 44  ? -37.695 1.027   3.791   1.00 17.18 ? 44  ASP C CB  1 
ATOM   2115 C  CG  . ASP C 1 44  ? -38.788 2.004   4.128   1.00 22.04 ? 44  ASP C CG  1 
ATOM   2116 O  OD1 . ASP C 1 44  ? -39.966 1.697   3.874   1.00 24.20 ? 44  ASP C OD1 1 
ATOM   2117 O  OD2 . ASP C 1 44  ? -38.473 3.073   4.673   1.00 24.96 ? 44  ASP C OD2 1 
ATOM   2118 N  N   . GLN C 1 45  ? -36.428 -2.287  4.795   1.00 12.67 ? 45  GLN C N   1 
ATOM   2119 C  CA  . GLN C 1 45  ? -35.474 -3.267  4.300   1.00 11.37 ? 45  GLN C CA  1 
ATOM   2120 C  C   . GLN C 1 45  ? -36.181 -4.439  3.626   1.00 11.71 ? 45  GLN C C   1 
ATOM   2121 O  O   . GLN C 1 45  ? -37.314 -4.805  3.983   1.00 12.89 ? 45  GLN C O   1 
ATOM   2122 C  CB  . GLN C 1 45  ? -34.599 -3.786  5.439   1.00 11.66 ? 45  GLN C CB  1 
ATOM   2123 C  CG  . GLN C 1 45  ? -33.657 -2.735  6.035   1.00 13.51 ? 45  GLN C CG  1 
ATOM   2124 C  CD  . GLN C 1 45  ? -32.782 -2.151  4.953   1.00 14.14 ? 45  GLN C CD  1 
ATOM   2125 O  OE1 . GLN C 1 45  ? -31.834 -2.795  4.512   1.00 14.67 ? 45  GLN C OE1 1 
ATOM   2126 N  NE2 . GLN C 1 45  ? -33.119 -0.958  4.488   1.00 13.88 ? 45  GLN C NE2 1 
ATOM   2127 N  N   . LEU C 1 46  ? -35.467 -5.057  2.683   1.00 11.68 ? 46  LEU C N   1 
ATOM   2128 C  CA  . LEU C 1 46  ? -35.890 -6.270  1.985   1.00 11.89 ? 46  LEU C CA  1 
ATOM   2129 C  C   . LEU C 1 46  ? -35.417 -7.460  2.829   1.00 11.28 ? 46  LEU C C   1 
ATOM   2130 O  O   . LEU C 1 46  ? -34.238 -7.828  2.814   1.00 12.27 ? 46  LEU C O   1 
ATOM   2131 C  CB  . LEU C 1 46  ? -35.291 -6.279  0.580   1.00 13.13 ? 46  LEU C CB  1 
ATOM   2132 C  CG  . LEU C 1 46  ? -35.631 -7.488  -0.295  1.00 15.19 ? 46  LEU C CG  1 
ATOM   2133 C  CD1 . LEU C 1 46  ? -37.139 -7.623  -0.509  1.00 16.76 ? 46  LEU C CD1 1 
ATOM   2134 C  CD2 . LEU C 1 46  ? -34.890 -7.389  -1.620  1.00 15.72 ? 46  LEU C CD2 1 
ATOM   2135 N  N   . MET C 1 47  ? -36.322 -8.023  3.626   1.00 11.59 ? 47  MET C N   1 
ATOM   2136 C  CA  . MET C 1 47  ? -35.956 -9.018  4.623   1.00 13.70 ? 47  MET C CA  1 
ATOM   2137 C  C   . MET C 1 47  ? -37.060 -10.046 4.751   1.00 13.81 ? 47  MET C C   1 
ATOM   2138 O  O   . MET C 1 47  ? -38.226 -9.759  4.485   1.00 15.30 ? 47  MET C O   1 
ATOM   2139 C  CB  . MET C 1 47  ? -35.778 -8.393  6.029   1.00 17.54 ? 47  MET C CB  1 
ATOM   2140 C  CG  . MET C 1 47  ? -34.948 -7.165  6.142   1.00 21.28 ? 47  MET C CG  1 
ATOM   2141 S  SD  . MET C 1 47  ? -34.990 -6.494  7.799   1.00 22.58 ? 47  MET C SD  1 
ATOM   2142 C  CE  . MET C 1 47  ? -35.593 -7.788  8.682   1.00 18.94 ? 47  MET C CE  1 
ATOM   2143 N  N   . ALA C 1 48  ? -36.678 -11.243 5.201   1.00 14.02 ? 48  ALA C N   1 
ATOM   2144 C  CA  . ALA C 1 48  ? -37.622 -12.283 5.559   1.00 15.00 ? 48  ALA C CA  1 
ATOM   2145 C  C   . ALA C 1 48  ? -37.133 -12.962 6.822   1.00 14.07 ? 48  ALA C C   1 
ATOM   2146 O  O   . ALA C 1 48  ? -35.929 -13.003 7.117   1.00 14.61 ? 48  ALA C O   1 
ATOM   2147 C  CB  . ALA C 1 48  ? -37.790 -13.326 4.447   1.00 14.70 ? 48  ALA C CB  1 
ATOM   2148 N  N   . PHE C 1 49  ? -38.095 -13.469 7.584   1.00 13.47 ? 49  PHE C N   1 
ATOM   2149 C  CA  . PHE C 1 49  ? -37.836 -14.219 8.802   1.00 13.18 ? 49  PHE C CA  1 
ATOM   2150 C  C   . PHE C 1 49  ? -38.689 -15.474 8.714   1.00 13.17 ? 49  PHE C C   1 
ATOM   2151 O  O   . PHE C 1 49  ? -39.912 -15.385 8.569   1.00 13.39 ? 49  PHE C O   1 
ATOM   2152 C  CB  . PHE C 1 49  ? -38.191 -13.372 10.031  1.00 13.51 ? 49  PHE C CB  1 
ATOM   2153 C  CG  . PHE C 1 49  ? -37.753 -13.969 11.343  1.00 14.16 ? 49  PHE C CG  1 
ATOM   2154 C  CD1 . PHE C 1 49  ? -38.391 -15.107 11.851  1.00 15.05 ? 49  PHE C CD1 1 
ATOM   2155 C  CD2 . PHE C 1 49  ? -36.731 -13.388 12.086  1.00 15.07 ? 49  PHE C CD2 1 
ATOM   2156 C  CE1 . PHE C 1 49  ? -38.012 -15.663 13.061  1.00 16.12 ? 49  PHE C CE1 1 
ATOM   2157 C  CE2 . PHE C 1 49  ? -36.353 -13.937 13.317  1.00 15.21 ? 49  PHE C CE2 1 
ATOM   2158 C  CZ  . PHE C 1 49  ? -37.006 -15.082 13.800  1.00 15.60 ? 49  PHE C CZ  1 
ATOM   2159 N  N   . GLY C 1 50  ? -38.053 -16.636 8.761   1.00 13.35 ? 50  GLY C N   1 
ATOM   2160 C  CA  . GLY C 1 50  ? -38.796 -17.876 8.574   1.00 13.82 ? 50  GLY C CA  1 
ATOM   2161 C  C   . GLY C 1 50  ? -39.456 -17.991 7.218   1.00 15.43 ? 50  GLY C C   1 
ATOM   2162 O  O   . GLY C 1 50  ? -40.495 -18.665 7.077   1.00 16.22 ? 50  GLY C O   1 
ATOM   2163 N  N   . GLY C 1 51  ? -38.875 -17.341 6.204   1.00 16.62 ? 51  GLY C N   1 
ATOM   2164 C  CA  . GLY C 1 51  ? -39.379 -17.390 4.848   1.00 18.25 ? 51  GLY C CA  1 
ATOM   2165 C  C   . GLY C 1 51  ? -40.455 -16.380 4.548   1.00 19.44 ? 51  GLY C C   1 
ATOM   2166 O  O   . GLY C 1 51  ? -40.851 -16.255 3.382   1.00 21.07 ? 51  GLY C O   1 
ATOM   2167 N  N   . SER C 1 52  ? -40.894 -15.612 5.541   1.00 20.57 ? 52  SER C N   1 
ATOM   2168 C  CA  . SER C 1 52  ? -42.042 -14.720 5.433   1.00 20.81 ? 52  SER C CA  1 
ATOM   2169 C  C   . SER C 1 52  ? -41.585 -13.274 5.545   1.00 20.07 ? 52  SER C C   1 
ATOM   2170 O  O   . SER C 1 52  ? -40.663 -12.954 6.304   1.00 17.88 ? 52  SER C O   1 
ATOM   2171 C  CB  . SER C 1 52  ? -43.017 -15.001 6.583   1.00 23.05 ? 52  SER C CB  1 
ATOM   2172 O  OG  . SER C 1 52  ? -43.833 -13.884 6.905   1.00 24.83 ? 52  SER C OG  1 
ATOM   2173 N  N   A SER C 1 53  ? -42.227 -12.395 4.782   0.47 20.95 ? 53  SER C N   1 
ATOM   2174 N  N   B SER C 1 53  ? -42.251 -12.407 4.783   0.53 20.95 ? 53  SER C N   1 
ATOM   2175 C  CA  A SER C 1 53  ? -41.886 -10.982 4.826   0.47 21.25 ? 53  SER C CA  1 
ATOM   2176 C  CA  B SER C 1 53  ? -41.952 -10.984 4.745   0.53 21.19 ? 53  SER C CA  1 
ATOM   2177 C  C   A SER C 1 53  ? -42.867 -10.162 5.654   0.47 20.66 ? 53  SER C C   1 
ATOM   2178 C  C   B SER C 1 53  ? -42.851 -10.160 5.662   0.53 20.63 ? 53  SER C C   1 
ATOM   2179 O  O   A SER C 1 53  ? -42.959 -8.944  5.466   0.47 20.89 ? 53  SER C O   1 
ATOM   2180 O  O   B SER C 1 53  ? -42.867 -8.929  5.546   0.53 20.85 ? 53  SER C O   1 
ATOM   2181 C  CB  A SER C 1 53  ? -41.683 -10.415 3.422   0.47 22.75 ? 53  SER C CB  1 
ATOM   2182 C  CB  B SER C 1 53  ? -42.006 -10.457 3.305   0.53 22.69 ? 53  SER C CB  1 
ATOM   2183 O  OG  A SER C 1 53  ? -40.403 -10.789 2.948   0.47 23.32 ? 53  SER C OG  1 
ATOM   2184 O  OG  B SER C 1 53  ? -43.141 -10.948 2.618   0.53 23.16 ? 53  SER C OG  1 
ATOM   2185 N  N   . GLU C 1 54  ? -43.590 -10.804 6.580   1.00 20.46 ? 54  GLU C N   1 
ATOM   2186 C  CA  . GLU C 1 54  ? -44.328 -10.057 7.590   1.00 21.22 ? 54  GLU C CA  1 
ATOM   2187 C  C   . GLU C 1 54  ? -43.317 -9.266  8.433   1.00 18.89 ? 54  GLU C C   1 
ATOM   2188 O  O   . GLU C 1 54  ? -42.120 -9.567  8.412   1.00 18.63 ? 54  GLU C O   1 
ATOM   2189 C  CB  . GLU C 1 54  ? -45.139 -11.011 8.473   1.00 24.80 ? 54  GLU C CB  1 
ATOM   2190 C  CG  . GLU C 1 54  ? -46.275 -11.790 7.789   1.00 28.05 ? 54  GLU C CG  1 
ATOM   2191 C  CD  . GLU C 1 54  ? -47.513 -10.949 7.480   1.00 30.73 ? 54  GLU C CD  1 
ATOM   2192 O  OE1 . GLU C 1 54  ? -48.623 -11.476 7.676   1.00 31.61 ? 54  GLU C OE1 1 
ATOM   2193 O  OE2 . GLU C 1 54  ? -47.396 -9.760  7.102   1.00 32.01 ? 54  GLU C OE2 1 
ATOM   2194 N  N   . PRO C 1 55  ? -43.758 -8.245  9.169   1.00 17.43 ? 55  PRO C N   1 
ATOM   2195 C  CA  . PRO C 1 55  ? -42.794 -7.411  9.910   1.00 16.26 ? 55  PRO C CA  1 
ATOM   2196 C  C   . PRO C 1 55  ? -41.844 -8.236  10.775  1.00 13.81 ? 55  PRO C C   1 
ATOM   2197 O  O   . PRO C 1 55  ? -42.259 -9.161  11.496  1.00 15.22 ? 55  PRO C O   1 
ATOM   2198 C  CB  . PRO C 1 55  ? -43.689 -6.490  10.745  1.00 17.48 ? 55  PRO C CB  1 
ATOM   2199 C  CG  . PRO C 1 55  ? -44.952 -6.356  9.882   1.00 17.99 ? 55  PRO C CG  1 
ATOM   2200 C  CD  . PRO C 1 55  ? -45.136 -7.717  9.246   1.00 18.17 ? 55  PRO C CD  1 
ATOM   2201 N  N   . CYS C 1 56  ? -40.556 -7.893  10.695  1.00 11.99 ? 56  CYS C N   1 
ATOM   2202 C  CA  . CYS C 1 56  ? -39.507 -8.586  11.430  1.00 11.99 ? 56  CYS C CA  1 
ATOM   2203 C  C   . CYS C 1 56  ? -38.351 -7.615  11.665  1.00 12.34 ? 56  CYS C C   1 
ATOM   2204 O  O   . CYS C 1 56  ? -38.330 -6.497  11.137  1.00 13.00 ? 56  CYS C O   1 
ATOM   2205 C  CB  . CYS C 1 56  ? -39.044 -9.829  10.666  1.00 12.98 ? 56  CYS C CB  1 
ATOM   2206 S  SG  . CYS C 1 56  ? -38.360 -9.503  9.024   1.00 14.92 ? 56  CYS C SG  1 
ATOM   2207 N  N   . ALA C 1 57  ? -37.403 -8.028  12.506  1.00 12.90 ? 57  ALA C N   1 
ATOM   2208 C  CA  . ALA C 1 57  ? -36.234 -7.199  12.756  1.00 13.06 ? 57  ALA C CA  1 
ATOM   2209 C  C   . ALA C 1 57  ? -35.027 -8.069  13.036  1.00 12.33 ? 57  ALA C C   1 
ATOM   2210 O  O   . ALA C 1 57  ? -35.124 -9.087  13.730  1.00 12.85 ? 57  ALA C O   1 
ATOM   2211 C  CB  . ALA C 1 57  ? -36.423 -6.240  13.941  1.00 13.99 ? 57  ALA C CB  1 
ATOM   2212 N  N   . LEU C 1 58  ? -33.884 -7.640  12.516  1.00 11.99 ? 58  LEU C N   1 
ATOM   2213 C  CA  . LEU C 1 58  ? -32.587 -8.233  12.813  1.00 11.80 ? 58  LEU C CA  1 
ATOM   2214 C  C   . LEU C 1 58  ? -31.744 -7.143  13.446  1.00 10.72 ? 58  LEU C C   1 
ATOM   2215 O  O   . LEU C 1 58  ? -31.590 -6.072  12.858  1.00 12.37 ? 58  LEU C O   1 
ATOM   2216 C  CB  . LEU C 1 58  ? -31.915 -8.729  11.529  1.00 12.98 ? 58  LEU C CB  1 
ATOM   2217 C  CG  . LEU C 1 58  ? -32.740 -9.757  10.738  1.00 14.64 ? 58  LEU C CG  1 
ATOM   2218 C  CD1 . LEU C 1 58  ? -32.009 -10.121 9.447   1.00 15.79 ? 58  LEU C CD1 1 
ATOM   2219 C  CD2 . LEU C 1 58  ? -32.977 -10.974 11.596  1.00 15.99 ? 58  LEU C CD2 1 
ATOM   2220 N  N   . CYS C 1 59  ? -31.221 -7.405  14.645  1.00 10.50 ? 59  CYS C N   1 
ATOM   2221 C  CA  . CYS C 1 59  ? -30.599 -6.369  15.455  1.00 11.13 ? 59  CYS C CA  1 
ATOM   2222 C  C   . CYS C 1 59  ? -29.270 -6.839  16.000  1.00 11.04 ? 59  CYS C C   1 
ATOM   2223 O  O   . CYS C 1 59  ? -28.979 -8.038  16.042  1.00 11.62 ? 59  CYS C O   1 
ATOM   2224 C  CB  . CYS C 1 59  ? -31.481 -6.012  16.660  1.00 11.70 ? 59  CYS C CB  1 
ATOM   2225 S  SG  . CYS C 1 59  ? -33.193 -5.703  16.288  1.00 13.36 ? 59  CYS C SG  1 
ATOM   2226 N  N   . SER C 1 60  ? -28.476 -5.871  16.463  1.00 10.17 ? 60  SER C N   1 
ATOM   2227 C  CA  . SER C 1 60  ? -27.247 -6.221  17.153  1.00 11.08 ? 60  SER C CA  1 
ATOM   2228 C  C   . SER C 1 60  ? -26.982 -5.221  18.258  1.00 10.94 ? 60  SER C C   1 
ATOM   2229 O  O   . SER C 1 60  ? -27.357 -4.054  18.154  1.00 12.32 ? 60  SER C O   1 
ATOM   2230 C  CB  . SER C 1 60  ? -26.029 -6.292  16.222  1.00 13.61 ? 60  SER C CB  1 
ATOM   2231 O  OG  . SER C 1 60  ? -25.754 -5.059  15.597  1.00 15.93 ? 60  SER C OG  1 
ATOM   2232 N  N   . LEU C 1 61  ? -26.384 -5.722  19.338  1.00 10.85 ? 61  LEU C N   1 
ATOM   2233 C  CA  . LEU C 1 61  ? -25.900 -4.899  20.441  1.00 11.26 ? 61  LEU C CA  1 
ATOM   2234 C  C   . LEU C 1 61  ? -24.429 -5.224  20.658  1.00 11.57 ? 61  LEU C C   1 
ATOM   2235 O  O   . LEU C 1 61  ? -24.083 -6.367  20.970  1.00 12.42 ? 61  LEU C O   1 
ATOM   2236 C  CB  . LEU C 1 61  ? -26.703 -5.177  21.725  1.00 12.26 ? 61  LEU C CB  1 
ATOM   2237 C  CG  . LEU C 1 61  ? -26.308 -4.316  22.941  1.00 12.98 ? 61  LEU C CG  1 
ATOM   2238 C  CD1 . LEU C 1 61  ? -26.575 -2.831  22.666  1.00 14.40 ? 61  LEU C CD1 1 
ATOM   2239 C  CD2 . LEU C 1 61  ? -27.019 -4.720  24.222  1.00 13.79 ? 61  LEU C CD2 1 
ATOM   2240 N  N   . HIS C 1 62  ? -23.573 -4.230  20.491  1.00 12.45 ? 62  HIS C N   1 
ATOM   2241 C  CA  . HIS C 1 62  ? -22.150 -4.374  20.778  1.00 12.75 ? 62  HIS C CA  1 
ATOM   2242 C  C   . HIS C 1 62  ? -21.841 -3.544  22.013  1.00 14.03 ? 62  HIS C C   1 
ATOM   2243 O  O   . HIS C 1 62  ? -22.256 -2.384  22.090  1.00 14.42 ? 62  HIS C O   1 
ATOM   2244 C  CB  . HIS C 1 62  ? -21.302 -3.829  19.624  1.00 12.91 ? 62  HIS C CB  1 
ATOM   2245 C  CG  . HIS C 1 62  ? -21.376 -4.630  18.369  1.00 14.22 ? 62  HIS C CG  1 
ATOM   2246 N  ND1 . HIS C 1 62  ? -22.478 -4.617  17.547  1.00 14.63 ? 62  HIS C ND1 1 
ATOM   2247 C  CD2 . HIS C 1 62  ? -20.471 -5.444  17.775  1.00 15.05 ? 62  HIS C CD2 1 
ATOM   2248 C  CE1 . HIS C 1 62  ? -22.256 -5.392  16.499  1.00 15.24 ? 62  HIS C CE1 1 
ATOM   2249 N  NE2 . HIS C 1 62  ? -21.046 -5.910  16.617  1.00 16.13 ? 62  HIS C NE2 1 
ATOM   2250 N  N   . SER C 1 63  ? -21.103 -4.116  22.962  1.00 13.58 ? 63  SER C N   1 
ATOM   2251 C  CA  . SER C 1 63  ? -20.791 -3.408  24.195  1.00 13.30 ? 63  SER C CA  1 
ATOM   2252 C  C   . SER C 1 63  ? -19.452 -3.912  24.729  1.00 13.41 ? 63  SER C C   1 
ATOM   2253 O  O   . SER C 1 63  ? -19.117 -5.092  24.586  1.00 13.90 ? 63  SER C O   1 
ATOM   2254 C  CB  . SER C 1 63  ? -21.889 -3.637  25.246  1.00 13.74 ? 63  SER C CB  1 
ATOM   2255 O  OG  . SER C 1 63  ? -21.598 -2.919  26.428  1.00 14.02 ? 63  SER C OG  1 
ATOM   2256 N  N   . ILE C 1 64  ? -18.680 -3.014  25.341  1.00 14.13 ? 64  ILE C N   1 
ATOM   2257 C  CA  . ILE C 1 64  ? -17.472 -3.416  26.064  1.00 14.72 ? 64  ILE C CA  1 
ATOM   2258 C  C   . ILE C 1 64  ? -17.922 -3.891  27.442  1.00 16.02 ? 64  ILE C C   1 
ATOM   2259 O  O   . ILE C 1 64  ? -18.143 -3.086  28.347  1.00 17.49 ? 64  ILE C O   1 
ATOM   2260 C  CB  . ILE C 1 64  ? -16.444 -2.287  26.152  1.00 14.41 ? 64  ILE C CB  1 
ATOM   2261 C  CG1 . ILE C 1 64  ? -16.016 -1.855  24.741  1.00 15.00 ? 64  ILE C CG1 1 
ATOM   2262 C  CG2 . ILE C 1 64  ? -15.258 -2.757  26.971  1.00 14.43 ? 64  ILE C CG2 1 
ATOM   2263 C  CD1 . ILE C 1 64  ? -15.246 -0.566  24.750  1.00 15.10 ? 64  ILE C CD1 1 
ATOM   2264 N  N   . GLY C 1 65  ? -18.071 -5.188  27.602  1.00 16.38 ? 65  GLY C N   1 
ATOM   2265 C  CA  . GLY C 1 65  ? -18.660 -5.720  28.806  1.00 16.89 ? 65  GLY C CA  1 
ATOM   2266 C  C   . GLY C 1 65  ? -20.169 -5.538  28.850  1.00 16.87 ? 65  GLY C C   1 
ATOM   2267 O  O   . GLY C 1 65  ? -20.816 -5.061  27.907  1.00 16.39 ? 65  GLY C O   1 
ATOM   2268 N  N   . LYS C 1 66  ? -20.733 -5.918  30.001  1.00 17.29 ? 66  LYS C N   1 
ATOM   2269 C  CA  . LYS C 1 66  ? -22.178 -5.893  30.232  1.00 17.06 ? 66  LYS C CA  1 
ATOM   2270 C  C   . LYS C 1 66  ? -22.926 -6.805  29.271  1.00 16.21 ? 66  LYS C C   1 
ATOM   2271 O  O   . LYS C 1 66  ? -24.075 -6.524  28.921  1.00 16.51 ? 66  LYS C O   1 
ATOM   2272 C  CB  . LYS C 1 66  ? -22.782 -4.477  30.244  1.00 18.59 ? 66  LYS C CB  1 
ATOM   2273 C  CG  . LYS C 1 66  ? -22.125 -3.491  31.216  1.00 20.88 ? 66  LYS C CG  1 
ATOM   2274 C  CD  . LYS C 1 66  ? -22.106 -4.105  32.611  1.00 23.35 ? 66  LYS C CD  1 
ATOM   2275 C  CE  . LYS C 1 66  ? -22.060 -3.123  33.739  1.00 25.95 ? 66  LYS C CE  1 
ATOM   2276 N  NZ  . LYS C 1 66  ? -23.312 -2.312  33.833  1.00 27.23 ? 66  LYS C NZ  1 
ATOM   2277 N  N   . ILE C 1 67  ? -22.280 -7.890  28.851  1.00 15.76 ? 67  ILE C N   1 
ATOM   2278 C  CA  . ILE C 1 67  ? -22.868 -8.903  27.984  1.00 15.06 ? 67  ILE C CA  1 
ATOM   2279 C  C   . ILE C 1 67  ? -22.720 -10.234 28.707  1.00 15.65 ? 67  ILE C C   1 
ATOM   2280 O  O   . ILE C 1 67  ? -21.651 -10.536 29.249  1.00 17.35 ? 67  ILE C O   1 
ATOM   2281 C  CB  . ILE C 1 67  ? -22.162 -8.920  26.612  1.00 14.51 ? 67  ILE C CB  1 
ATOM   2282 C  CG1 . ILE C 1 67  ? -22.383 -7.564  25.896  1.00 14.93 ? 67  ILE C CG1 1 
ATOM   2283 C  CG2 . ILE C 1 67  ? -22.585 -10.148 25.767  1.00 13.58 ? 67  ILE C CG2 1 
ATOM   2284 C  CD1 . ILE C 1 67  ? -23.783 -7.339  25.373  1.00 15.25 ? 67  ILE C CD1 1 
ATOM   2285 N  N   . GLY C 1 68  ? -23.795 -11.008 28.752  1.00 15.04 ? 68  GLY C N   1 
ATOM   2286 C  CA  . GLY C 1 68  ? -23.713 -12.303 29.401  1.00 15.04 ? 68  GLY C CA  1 
ATOM   2287 C  C   . GLY C 1 68  ? -25.063 -12.971 29.387  1.00 15.09 ? 68  GLY C C   1 
ATOM   2288 O  O   . GLY C 1 68  ? -26.051 -12.412 28.913  1.00 14.97 ? 68  GLY C O   1 
ATOM   2289 N  N   . GLY C 1 69  ? -25.088 -14.193 29.916  1.00 15.14 ? 69  GLY C N   1 
ATOM   2290 C  CA  . GLY C 1 69  ? -26.291 -15.009 29.889  1.00 15.19 ? 69  GLY C CA  1 
ATOM   2291 C  C   . GLY C 1 69  ? -27.530 -14.292 30.402  1.00 15.71 ? 69  GLY C C   1 
ATOM   2292 O  O   . GLY C 1 69  ? -28.513 -14.111 29.674  1.00 15.30 ? 69  GLY C O   1 
ATOM   2293 N  N   . ALA C 1 70  ? -27.487 -13.864 31.665  1.00 16.41 ? 70  ALA C N   1 
ATOM   2294 C  CA  . ALA C 1 70  ? -28.647 -13.224 32.280  1.00 16.47 ? 70  ALA C CA  1 
ATOM   2295 C  C   . ALA C 1 70  ? -28.880 -11.836 31.713  1.00 15.41 ? 70  ALA C C   1 
ATOM   2296 O  O   . ALA C 1 70  ? -30.025 -11.456 31.455  1.00 15.72 ? 70  ALA C O   1 
ATOM   2297 C  CB  . ALA C 1 70  ? -28.461 -13.142 33.796  1.00 17.46 ? 70  ALA C CB  1 
ATOM   2298 N  N   . GLN C 1 71  ? -27.810 -11.068 31.504  1.00 14.38 ? 71  GLN C N   1 
ATOM   2299 C  CA  . GLN C 1 71  ? -27.982 -9.714  30.991  1.00 14.14 ? 71  GLN C CA  1 
ATOM   2300 C  C   . GLN C 1 71  ? -28.630 -9.750  29.620  1.00 13.47 ? 71  GLN C C   1 
ATOM   2301 O  O   . GLN C 1 71  ? -29.519 -8.941  29.327  1.00 13.16 ? 71  GLN C O   1 
ATOM   2302 C  CB  . GLN C 1 71  ? -26.626 -9.011  30.935  1.00 15.47 ? 71  GLN C CB  1 
ATOM   2303 C  CG  . GLN C 1 71  ? -26.081 -8.758  32.320  1.00 16.64 ? 71  GLN C CG  1 
ATOM   2304 C  CD  . GLN C 1 71  ? -24.693 -8.216  32.275  1.00 18.01 ? 71  GLN C CD  1 
ATOM   2305 O  OE1 . GLN C 1 71  ? -24.497 -6.994  32.339  1.00 20.38 ? 71  GLN C OE1 1 
ATOM   2306 N  NE2 . GLN C 1 71  ? -23.703 -9.109  32.183  1.00 18.43 ? 71  GLN C NE2 1 
ATOM   2307 N  N   . ASN C 1 72  ? -28.212 -10.703 28.774  1.00 12.59 ? 72  ASN C N   1 
ATOM   2308 C  CA  . ASN C 1 72  ? -28.750 -10.752 27.417  1.00 13.02 ? 72  ASN C CA  1 
ATOM   2309 C  C   . ASN C 1 72  ? -30.212 -11.169 27.407  1.00 13.05 ? 72  ASN C C   1 
ATOM   2310 O  O   . ASN C 1 72  ? -30.971 -10.702 26.548  1.00 13.36 ? 72  ASN C O   1 
ATOM   2311 C  CB  . ASN C 1 72  ? -27.938 -11.680 26.495  1.00 12.09 ? 72  ASN C CB  1 
ATOM   2312 C  CG  . ASN C 1 72  ? -26.493 -11.249 26.327  1.00 12.67 ? 72  ASN C CG  1 
ATOM   2313 O  OD1 . ASN C 1 72  ? -26.088 -10.170 26.751  1.00 12.71 ? 72  ASN C OD1 1 
ATOM   2314 N  ND2 . ASN C 1 72  ? -25.698 -12.117 25.716  1.00 12.75 ? 72  ASN C ND2 1 
ATOM   2315 N  N   . ARG C 1 73  ? -30.626 -12.038 28.337  1.00 13.06 ? 73  ARG C N   1 
ATOM   2316 C  CA  . ARG C 1 73  ? -32.051 -12.323 28.463  1.00 14.06 ? 73  ARG C CA  1 
ATOM   2317 C  C   . ARG C 1 73  ? -32.832 -11.064 28.805  1.00 14.45 ? 73  ARG C C   1 
ATOM   2318 O  O   . ARG C 1 73  ? -33.896 -10.809 28.231  1.00 14.67 ? 73  ARG C O   1 
ATOM   2319 C  CB  . ARG C 1 73  ? -32.291 -13.387 29.533  1.00 15.49 ? 73  ARG C CB  1 
ATOM   2320 C  CG  . ARG C 1 73  ? -32.041 -14.804 29.008  1.00 17.86 ? 73  ARG C CG  1 
ATOM   2321 C  CD  . ARG C 1 73  ? -32.421 -15.846 30.050  1.00 19.58 ? 73  ARG C CD  1 
ATOM   2322 N  NE  . ARG C 1 73  ? -31.445 -15.909 31.128  1.00 20.93 ? 73  ARG C NE  1 
ATOM   2323 C  CZ  . ARG C 1 73  ? -30.311 -16.602 31.041  1.00 22.18 ? 73  ARG C CZ  1 
ATOM   2324 N  NH1 . ARG C 1 73  ? -30.027 -17.264 29.912  1.00 22.79 ? 73  ARG C NH1 1 
ATOM   2325 N  NH2 . ARG C 1 73  ? -29.464 -16.626 32.063  1.00 22.61 ? 73  ARG C NH2 1 
ATOM   2326 N  N   . SER C 1 74  ? -32.307 -10.258 29.734  1.00 15.15 ? 74  SER C N   1 
ATOM   2327 C  CA  . SER C 1 74  ? -32.983 -9.025  30.121  1.00 15.94 ? 74  SER C CA  1 
ATOM   2328 C  C   . SER C 1 74  ? -33.016 -8.027  28.968  1.00 14.80 ? 74  SER C C   1 
ATOM   2329 O  O   . SER C 1 74  ? -34.052 -7.392  28.730  1.00 14.73 ? 74  SER C O   1 
ATOM   2330 C  CB  . SER C 1 74  ? -32.283 -8.416  31.338  1.00 17.89 ? 74  SER C CB  1 
ATOM   2331 O  OG  . SER C 1 74  ? -33.025 -7.344  31.871  1.00 20.37 ? 74  SER C OG  1 
ATOM   2332 N  N   . TYR C 1 75  ? -31.900 -7.874  28.238  1.00 14.49 ? 75  TYR C N   1 
ATOM   2333 C  CA  . TYR C 1 75  ? -31.909 -6.968  27.091  1.00 13.44 ? 75  TYR C CA  1 
ATOM   2334 C  C   . TYR C 1 75  ? -32.928 -7.416  26.056  1.00 13.20 ? 75  TYR C C   1 
ATOM   2335 O  O   . TYR C 1 75  ? -33.576 -6.586  25.411  1.00 13.71 ? 75  TYR C O   1 
ATOM   2336 C  CB  . TYR C 1 75  ? -30.540 -6.925  26.414  1.00 13.52 ? 75  TYR C CB  1 
ATOM   2337 C  CG  . TYR C 1 75  ? -29.404 -6.442  27.286  1.00 14.42 ? 75  TYR C CG  1 
ATOM   2338 C  CD1 . TYR C 1 75  ? -29.619 -5.534  28.316  1.00 16.57 ? 75  TYR C CD1 1 
ATOM   2339 C  CD2 . TYR C 1 75  ? -28.104 -6.895  27.077  1.00 14.15 ? 75  TYR C CD2 1 
ATOM   2340 C  CE1 . TYR C 1 75  ? -28.571 -5.105  29.118  1.00 17.82 ? 75  TYR C CE1 1 
ATOM   2341 C  CE2 . TYR C 1 75  ? -27.048 -6.468  27.856  1.00 14.44 ? 75  TYR C CE2 1 
ATOM   2342 C  CZ  . TYR C 1 75  ? -27.283 -5.574  28.882  1.00 16.94 ? 75  TYR C CZ  1 
ATOM   2343 O  OH  . TYR C 1 75  ? -26.234 -5.159  29.667  1.00 18.14 ? 75  TYR C OH  1 
ATOM   2344 N  N   . SER C 1 76  ? -33.043 -8.729  25.846  1.00 12.95 ? 76  SER C N   1 
ATOM   2345 C  CA  . SER C 1 76  ? -33.948 -9.218  24.809  1.00 13.60 ? 76  SER C CA  1 
ATOM   2346 C  C   . SER C 1 76  ? -35.393 -8.913  25.165  1.00 13.46 ? 76  SER C C   1 
ATOM   2347 O  O   . SER C 1 76  ? -36.191 -8.519  24.300  1.00 13.34 ? 76  SER C O   1 
ATOM   2348 C  CB  . SER C 1 76  ? -33.757 -10.719 24.597  1.00 14.49 ? 76  SER C CB  1 
ATOM   2349 O  OG  . SER C 1 76  ? -32.460 -10.981 24.108  1.00 15.13 ? 76  SER C OG  1 
ATOM   2350 N  N   . LYS C 1 77  ? -35.743 -9.074  26.447  1.00 13.94 ? 77  LYS C N   1 
ATOM   2351 C  CA  . LYS C 1 77  ? -37.095 -8.742  26.898  1.00 14.57 ? 77  LYS C CA  1 
ATOM   2352 C  C   . LYS C 1 77  ? -37.375 -7.252  26.714  1.00 14.97 ? 77  LYS C C   1 
ATOM   2353 O  O   . LYS C 1 77  ? -38.419 -6.866  26.171  1.00 15.43 ? 77  LYS C O   1 
ATOM   2354 C  CB  . LYS C 1 77  ? -37.287 -9.186  28.358  1.00 15.70 ? 77  LYS C CB  1 
ATOM   2355 C  CG  . LYS C 1 77  ? -38.651 -8.905  28.944  1.00 16.90 ? 77  LYS C CG  1 
ATOM   2356 C  CD  . LYS C 1 77  ? -38.643 -9.325  30.391  1.00 17.62 ? 77  LYS C CD  1 
ATOM   2357 N  N   . LEU C 1 78  ? -36.412 -6.405  27.081  1.00 14.37 ? 78  LEU C N   1 
ATOM   2358 C  CA  . LEU C 1 78  ? -36.578 -4.961  26.926  1.00 15.14 ? 78  LEU C CA  1 
ATOM   2359 C  C   . LEU C 1 78  ? -36.713 -4.572  25.455  1.00 14.98 ? 78  LEU C C   1 
ATOM   2360 O  O   . LEU C 1 78  ? -37.625 -3.826  25.073  1.00 14.43 ? 78  LEU C O   1 
ATOM   2361 C  CB  . LEU C 1 78  ? -35.368 -4.246  27.536  1.00 16.26 ? 78  LEU C CB  1 
ATOM   2362 C  CG  . LEU C 1 78  ? -35.187 -2.779  27.177  1.00 18.07 ? 78  LEU C CG  1 
ATOM   2363 C  CD1 . LEU C 1 78  ? -36.191 -1.947  27.922  1.00 19.27 ? 78  LEU C CD1 1 
ATOM   2364 C  CD2 . LEU C 1 78  ? -33.759 -2.344  27.501  1.00 18.36 ? 78  LEU C CD2 1 
ATOM   2365 N  N   . LEU C 1 79  ? -35.804 -5.076  24.616  1.00 14.37 ? 79  LEU C N   1 
ATOM   2366 C  CA  . LEU C 1 79  ? -35.754 -4.627  23.232  1.00 14.06 ? 79  LEU C CA  1 
ATOM   2367 C  C   . LEU C 1 79  ? -36.891 -5.220  22.403  1.00 14.23 ? 79  LEU C C   1 
ATOM   2368 O  O   . LEU C 1 79  ? -37.496 -4.521  21.585  1.00 14.24 ? 79  LEU C O   1 
ATOM   2369 C  CB  . LEU C 1 79  ? -34.374 -4.934  22.636  1.00 13.98 ? 79  LEU C CB  1 
ATOM   2370 C  CG  . LEU C 1 79  ? -33.213 -4.156  23.280  1.00 15.01 ? 79  LEU C CG  1 
ATOM   2371 C  CD1 . LEU C 1 79  ? -31.830 -4.718  22.882  1.00 15.42 ? 79  LEU C CD1 1 
ATOM   2372 C  CD2 . LEU C 1 79  ? -33.294 -2.674  22.952  1.00 15.59 ? 79  LEU C CD2 1 
ATOM   2373 N  N   . CYS C 1 80  ? -37.212 -6.498  22.594  1.00 13.77 ? 80  CYS C N   1 
ATOM   2374 C  CA  . CYS C 1 80  ? -38.390 -7.039  21.916  1.00 14.33 ? 80  CYS C CA  1 
ATOM   2375 C  C   . CYS C 1 80  ? -39.655 -6.299  22.356  1.00 15.06 ? 80  CYS C C   1 
ATOM   2376 O  O   . CYS C 1 80  ? -40.564 -6.073  21.548  1.00 15.02 ? 80  CYS C O   1 
ATOM   2377 C  CB  . CYS C 1 80  ? -38.517 -8.544  22.161  1.00 15.43 ? 80  CYS C CB  1 
ATOM   2378 S  SG  . CYS C 1 80  ? -37.267 -9.586  21.372  1.00 16.84 ? 80  CYS C SG  1 
ATOM   2379 N  N   . GLY C 1 81  ? -39.745 -5.930  23.642  1.00 16.47 ? 81  GLY C N   1 
ATOM   2380 C  CA  . GLY C 1 81  ? -40.892 -5.159  24.085  1.00 16.69 ? 81  GLY C CA  1 
ATOM   2381 C  C   . GLY C 1 81  ? -41.007 -3.836  23.356  1.00 16.37 ? 81  GLY C C   1 
ATOM   2382 O  O   . GLY C 1 81  ? -42.090 -3.447  22.916  1.00 16.56 ? 81  GLY C O   1 
ATOM   2383 N  N   . LEU C 1 82  ? -39.886 -3.139  23.189  1.00 16.09 ? 82  LEU C N   1 
ATOM   2384 C  CA  . LEU C 1 82  ? -39.928 -1.869  22.478  1.00 16.26 ? 82  LEU C CA  1 
ATOM   2385 C  C   . LEU C 1 82  ? -40.262 -2.068  21.008  1.00 15.42 ? 82  LEU C C   1 
ATOM   2386 O  O   . LEU C 1 82  ? -41.021 -1.283  20.425  1.00 16.44 ? 82  LEU C O   1 
ATOM   2387 C  CB  . LEU C 1 82  ? -38.581 -1.168  22.598  1.00 17.35 ? 82  LEU C CB  1 
ATOM   2388 C  CG  . LEU C 1 82  ? -38.326 -0.540  23.967  1.00 18.50 ? 82  LEU C CG  1 
ATOM   2389 C  CD1 . LEU C 1 82  ? -36.863 -0.127  24.107  1.00 19.55 ? 82  LEU C CD1 1 
ATOM   2390 C  CD2 . LEU C 1 82  ? -39.280 0.621   24.243  1.00 18.96 ? 82  LEU C CD2 1 
ATOM   2391 N  N   . LEU C 1 83  ? -39.666 -3.077  20.366  1.00 15.00 ? 83  LEU C N   1 
ATOM   2392 C  CA  . LEU C 1 83  ? -40.000 -3.293  18.955  1.00 15.20 ? 83  LEU C CA  1 
ATOM   2393 C  C   . LEU C 1 83  ? -41.464 -3.675  18.765  1.00 15.85 ? 83  LEU C C   1 
ATOM   2394 O  O   . LEU C 1 83  ? -42.093 -3.282  17.772  1.00 16.12 ? 83  LEU C O   1 
ATOM   2395 C  CB  . LEU C 1 83  ? -39.087 -4.357  18.358  1.00 15.75 ? 83  LEU C CB  1 
ATOM   2396 C  CG  . LEU C 1 83  ? -37.607 -3.966  18.321  1.00 16.41 ? 83  LEU C CG  1 
ATOM   2397 C  CD1 . LEU C 1 83  ? -36.767 -5.194  17.949  1.00 17.59 ? 83  LEU C CD1 1 
ATOM   2398 C  CD2 . LEU C 1 83  ? -37.388 -2.804  17.346  1.00 17.25 ? 83  LEU C CD2 1 
ATOM   2399 N  N   . ALA C 1 84  ? -42.029 -4.427  19.709  1.00 15.79 ? 84  ALA C N   1 
ATOM   2400 C  CA  . ALA C 1 84  ? -43.447 -4.765  19.642  1.00 16.12 ? 84  ALA C CA  1 
ATOM   2401 C  C   . ALA C 1 84  ? -44.322 -3.541  19.891  1.00 17.77 ? 84  ALA C C   1 
ATOM   2402 O  O   . ALA C 1 84  ? -45.272 -3.282  19.144  1.00 18.91 ? 84  ALA C O   1 
ATOM   2403 C  CB  . ALA C 1 84  ? -43.762 -5.863  20.655  1.00 16.64 ? 84  ALA C CB  1 
ATOM   2404 N  N   . GLU C 1 85  ? -44.015 -2.765  20.933  1.00 18.59 ? 85  GLU C N   1 
ATOM   2405 C  CA  . GLU C 1 85  ? -44.884 -1.641  21.268  1.00 19.89 ? 85  GLU C CA  1 
ATOM   2406 C  C   . GLU C 1 85  ? -44.756 -0.514  20.249  1.00 19.24 ? 85  GLU C C   1 
ATOM   2407 O  O   . GLU C 1 85  ? -45.763 0.096   19.867  1.00 20.93 ? 85  GLU C O   1 
ATOM   2408 C  CB  . GLU C 1 85  ? -44.575 -1.137  22.675  1.00 23.15 ? 85  GLU C CB  1 
ATOM   2409 C  CG  . GLU C 1 85  ? -44.944 -2.130  23.783  1.00 27.26 ? 85  GLU C CG  1 
ATOM   2410 C  CD  . GLU C 1 85  ? -46.374 -2.636  23.659  1.00 31.22 ? 85  GLU C CD  1 
ATOM   2411 O  OE1 . GLU C 1 85  ? -46.564 -3.871  23.559  1.00 32.62 ? 85  GLU C OE1 1 
ATOM   2412 O  OE2 . GLU C 1 85  ? -47.303 -1.800  23.651  1.00 33.01 ? 85  GLU C OE2 1 
ATOM   2413 N  N   . ARG C 1 86  ? -43.540 -0.235  19.782  1.00 17.75 ? 86  ARG C N   1 
ATOM   2414 C  CA  . ARG C 1 86  ? -43.310 0.949   18.962  1.00 17.61 ? 86  ARG C CA  1 
ATOM   2415 C  C   . ARG C 1 86  ? -43.357 0.660   17.463  1.00 17.05 ? 86  ARG C C   1 
ATOM   2416 O  O   . ARG C 1 86  ? -43.819 1.508   16.696  1.00 18.01 ? 86  ARG C O   1 
ATOM   2417 C  CB  . ARG C 1 86  ? -41.968 1.590   19.330  1.00 18.65 ? 86  ARG C CB  1 
ATOM   2418 C  CG  . ARG C 1 86  ? -41.752 1.715   20.861  1.00 20.04 ? 86  ARG C CG  1 
ATOM   2419 C  CD  . ARG C 1 86  ? -42.839 2.492   21.599  1.00 21.80 ? 86  ARG C CD  1 
ATOM   2420 N  NE  . ARG C 1 86  ? -42.818 3.868   21.157  1.00 22.91 ? 86  ARG C NE  1 
ATOM   2421 C  CZ  . ARG C 1 86  ? -43.845 4.491   20.598  1.00 24.91 ? 86  ARG C CZ  1 
ATOM   2422 N  NH1 . ARG C 1 86  ? -45.016 3.869   20.449  1.00 25.87 ? 86  ARG C NH1 1 
ATOM   2423 N  NH2 . ARG C 1 86  ? -43.695 5.753   20.207  1.00 25.06 ? 86  ARG C NH2 1 
ATOM   2424 N  N   . LEU C 1 87  ? -42.874 -0.503  17.019  1.00 16.40 ? 87  LEU C N   1 
ATOM   2425 C  CA  . LEU C 1 87  ? -42.855 -0.845  15.598  1.00 15.52 ? 87  LEU C CA  1 
ATOM   2426 C  C   . LEU C 1 87  ? -43.885 -1.899  15.228  1.00 15.54 ? 87  LEU C C   1 
ATOM   2427 O  O   . LEU C 1 87  ? -44.012 -2.240  14.044  1.00 15.59 ? 87  LEU C O   1 
ATOM   2428 C  CB  . LEU C 1 87  ? -41.460 -1.309  15.155  1.00 15.54 ? 87  LEU C CB  1 
ATOM   2429 C  CG  . LEU C 1 87  ? -40.329 -0.299  15.340  1.00 16.05 ? 87  LEU C CG  1 
ATOM   2430 C  CD1 . LEU C 1 87  ? -39.082 -0.740  14.607  1.00 15.96 ? 87  LEU C CD1 1 
ATOM   2431 C  CD2 . LEU C 1 87  ? -40.746 1.083   14.863  1.00 17.42 ? 87  LEU C CD2 1 
ATOM   2432 N  N   . ARG C 1 88  ? -44.596 -2.457  16.209  1.00 16.24 ? 88  ARG C N   1 
ATOM   2433 C  CA  . ARG C 1 88  ? -45.620 -3.470  15.957  1.00 17.31 ? 88  ARG C CA  1 
ATOM   2434 C  C   . ARG C 1 88  ? -45.022 -4.756  15.378  1.00 16.57 ? 88  ARG C C   1 
ATOM   2435 O  O   . ARG C 1 88  ? -45.647 -5.421  14.539  1.00 17.53 ? 88  ARG C O   1 
ATOM   2436 C  CB  . ARG C 1 88  ? -46.775 -2.939  15.093  1.00 20.24 ? 88  ARG C CB  1 
ATOM   2437 C  CG  . ARG C 1 88  ? -47.218 -1.508  15.416  1.00 24.32 ? 88  ARG C CG  1 
ATOM   2438 C  CD  . ARG C 1 88  ? -47.478 -1.273  16.891  1.00 28.42 ? 88  ARG C CD  1 
ATOM   2439 N  NE  . ARG C 1 88  ? -48.470 -2.205  17.423  1.00 31.87 ? 88  ARG C NE  1 
ATOM   2440 C  CZ  . ARG C 1 88  ? -48.925 -2.177  18.673  1.00 34.50 ? 88  ARG C CZ  1 
ATOM   2441 N  NH1 . ARG C 1 88  ? -49.834 -3.061  19.072  1.00 35.75 ? 88  ARG C NH1 1 
ATOM   2442 N  NH2 . ARG C 1 88  ? -48.469 -1.267  19.530  1.00 35.12 ? 88  ARG C NH2 1 
ATOM   2443 N  N   . ILE C 1 89  ? -43.802 -5.100  15.799  1.00 14.62 ? 89  ILE C N   1 
ATOM   2444 C  CA  . ILE C 1 89  ? -43.132 -6.331  15.372  1.00 14.16 ? 89  ILE C CA  1 
ATOM   2445 C  C   . ILE C 1 89  ? -43.298 -7.395  16.453  1.00 14.96 ? 89  ILE C C   1 
ATOM   2446 O  O   . ILE C 1 89  ? -42.947 -7.163  17.618  1.00 15.57 ? 89  ILE C O   1 
ATOM   2447 C  CB  . ILE C 1 89  ? -41.639 -6.096  15.083  1.00 13.57 ? 89  ILE C CB  1 
ATOM   2448 C  CG1 . ILE C 1 89  ? -41.444 -5.066  13.963  1.00 13.93 ? 89  ILE C CG1 1 
ATOM   2449 C  CG2 . ILE C 1 89  ? -40.993 -7.402  14.673  1.00 13.70 ? 89  ILE C CG2 1 
ATOM   2450 C  CD1 . ILE C 1 89  ? -39.984 -4.582  13.861  1.00 14.20 ? 89  ILE C CD1 1 
ATOM   2451 N  N   . SER C 1 90  ? -43.755 -8.588  16.060  1.00 15.03 ? 90  SER C N   1 
ATOM   2452 C  CA  . SER C 1 90  ? -43.906 -9.682  17.016  1.00 16.07 ? 90  SER C CA  1 
ATOM   2453 C  C   . SER C 1 90  ? -42.538 -10.125 17.536  1.00 15.42 ? 90  SER C C   1 
ATOM   2454 O  O   . SER C 1 90  ? -41.598 -10.277 16.757  1.00 15.52 ? 90  SER C O   1 
ATOM   2455 C  CB  . SER C 1 90  ? -44.566 -10.863 16.320  1.00 18.33 ? 90  SER C CB  1 
ATOM   2456 O  OG  . SER C 1 90  ? -45.911 -10.574 16.003  1.00 21.81 ? 90  SER C OG  1 
ATOM   2457 N  N   . PRO C 1 91  ? -42.399 -10.352 18.846  1.00 15.28 ? 91  PRO C N   1 
ATOM   2458 C  CA  . PRO C 1 91  ? -41.095 -10.758 19.393  1.00 15.23 ? 91  PRO C CA  1 
ATOM   2459 C  C   . PRO C 1 91  ? -40.543 -12.039 18.800  1.00 14.87 ? 91  PRO C C   1 
ATOM   2460 O  O   . PRO C 1 91  ? -39.316 -12.202 18.750  1.00 15.81 ? 91  PRO C O   1 
ATOM   2461 C  CB  . PRO C 1 91  ? -41.361 -10.883 20.902  1.00 15.91 ? 91  PRO C CB  1 
ATOM   2462 C  CG  . PRO C 1 91  ? -42.453 -9.934  21.153  1.00 17.00 ? 91  PRO C CG  1 
ATOM   2463 C  CD  . PRO C 1 91  ? -43.345 -10.015 19.919  1.00 16.19 ? 91  PRO C CD  1 
ATOM   2464 N  N   . ASP C 1 92  ? -41.400 -12.949 18.325  1.00 15.44 ? 92  ASP C N   1 
ATOM   2465 C  CA  . ASP C 1 92  ? -40.894 -14.177 17.729  1.00 15.83 ? 92  ASP C CA  1 
ATOM   2466 C  C   . ASP C 1 92  ? -40.409 -13.974 16.296  1.00 14.51 ? 92  ASP C C   1 
ATOM   2467 O  O   . ASP C 1 92  ? -40.044 -14.942 15.622  1.00 15.49 ? 92  ASP C O   1 
ATOM   2468 C  CB  . ASP C 1 92  ? -41.888 -15.347 17.883  1.00 17.39 ? 92  ASP C CB  1 
ATOM   2469 C  CG  . ASP C 1 92  ? -43.189 -15.144 17.111  1.00 18.28 ? 92  ASP C CG  1 
ATOM   2470 O  OD1 . ASP C 1 92  ? -43.291 -14.139 16.376  1.00 18.77 ? 92  ASP C OD1 1 
ATOM   2471 O  OD2 . ASP C 1 92  ? -44.107 -15.993 17.239  1.00 21.09 ? 92  ASP C OD2 1 
ATOM   2472 N  N   . ARG C 1 93  ? -40.395 -12.725 15.818  1.00 13.59 ? 93  ARG C N   1 
ATOM   2473 C  CA  . ARG C 1 93  ? -39.835 -12.365 14.520  1.00 13.88 ? 93  ARG C CA  1 
ATOM   2474 C  C   . ARG C 1 93  ? -38.706 -11.357 14.667  1.00 13.17 ? 93  ARG C C   1 
ATOM   2475 O  O   . ARG C 1 93  ? -38.443 -10.559 13.755  1.00 13.84 ? 93  ARG C O   1 
ATOM   2476 C  CB  . ARG C 1 93  ? -40.916 -11.851 13.578  1.00 14.90 ? 93  ARG C CB  1 
ATOM   2477 C  CG  . ARG C 1 93  ? -41.940 -12.931 13.259  1.00 15.35 ? 93  ARG C CG  1 
ATOM   2478 C  CD  . ARG C 1 93  ? -43.030 -12.496 12.252  1.00 15.99 ? 93  ARG C CD  1 
ATOM   2479 N  NE  . ARG C 1 93  ? -42.484 -11.991 10.992  1.00 16.47 ? 93  ARG C NE  1 
ATOM   2480 C  CZ  . ARG C 1 93  ? -41.967 -12.761 10.052  1.00 16.52 ? 93  ARG C CZ  1 
ATOM   2481 N  NH1 . ARG C 1 93  ? -41.947 -14.085 10.212  1.00 16.94 ? 93  ARG C NH1 1 
ATOM   2482 N  NH2 . ARG C 1 93  ? -41.465 -12.209 8.966   1.00 16.66 ? 93  ARG C NH2 1 
ATOM   2483 N  N   . VAL C 1 94  ? -38.007 -11.413 15.802  1.00 12.42 ? 94  VAL C N   1 
ATOM   2484 C  CA  . VAL C 1 94  ? -36.862 -10.559 16.071  1.00 13.19 ? 94  VAL C CA  1 
ATOM   2485 C  C   . VAL C 1 94  ? -35.684 -11.443 16.431  1.00 12.83 ? 94  VAL C C   1 
ATOM   2486 O  O   . VAL C 1 94  ? -35.810 -12.323 17.291  1.00 12.70 ? 94  VAL C O   1 
ATOM   2487 C  CB  . VAL C 1 94  ? -37.151 -9.619  17.257  1.00 12.98 ? 94  VAL C CB  1 
ATOM   2488 C  CG1 . VAL C 1 94  ? -35.908 -8.816  17.666  1.00 13.60 ? 94  VAL C CG1 1 
ATOM   2489 C  CG2 . VAL C 1 94  ? -38.354 -8.710  16.971  1.00 13.91 ? 94  VAL C CG2 1 
ATOM   2490 N  N   . TYR C 1 95  ? -34.529 -11.194 15.812  1.00 12.08 ? 95  TYR C N   1 
ATOM   2491 C  CA  . TYR C 1 95  ? -33.266 -11.692 16.344  1.00 11.52 ? 95  TYR C CA  1 
ATOM   2492 C  C   . TYR C 1 95  ? -32.407 -10.519 16.800  1.00 11.29 ? 95  TYR C C   1 
ATOM   2493 O  O   . TYR C 1 95  ? -32.378 -9.485  16.125  1.00 11.47 ? 95  TYR C O   1 
ATOM   2494 C  CB  . TYR C 1 95  ? -32.470 -12.438 15.283  1.00 12.14 ? 95  TYR C CB  1 
ATOM   2495 C  CG  . TYR C 1 95  ? -32.913 -13.847 14.978  1.00 12.23 ? 95  TYR C CG  1 
ATOM   2496 C  CD1 . TYR C 1 95  ? -33.485 -14.660 15.960  1.00 12.69 ? 95  TYR C CD1 1 
ATOM   2497 C  CD2 . TYR C 1 95  ? -32.744 -14.378 13.702  1.00 12.62 ? 95  TYR C CD2 1 
ATOM   2498 C  CE1 . TYR C 1 95  ? -33.855 -15.971 15.662  1.00 13.32 ? 95  TYR C CE1 1 
ATOM   2499 C  CE2 . TYR C 1 95  ? -33.131 -15.684 13.392  1.00 12.33 ? 95  TYR C CE2 1 
ATOM   2500 C  CZ  . TYR C 1 95  ? -33.679 -16.475 14.372  1.00 12.53 ? 95  TYR C CZ  1 
ATOM   2501 O  OH  . TYR C 1 95  ? -34.061 -17.769 14.127  1.00 14.04 ? 95  TYR C OH  1 
ATOM   2502 N  N   . ILE C 1 96  ? -31.678 -10.700 17.915  1.00 11.29 ? 96  ILE C N   1 
ATOM   2503 C  CA  . ILE C 1 96  ? -30.702 -9.726  18.414  1.00 11.76 ? 96  ILE C CA  1 
ATOM   2504 C  C   . ILE C 1 96  ? -29.402 -10.473 18.663  1.00 12.44 ? 96  ILE C C   1 
ATOM   2505 O  O   . ILE C 1 96  ? -29.348 -11.344 19.538  1.00 13.73 ? 96  ILE C O   1 
ATOM   2506 C  CB  . ILE C 1 96  ? -31.154 -9.052  19.714  1.00 12.58 ? 96  ILE C CB  1 
ATOM   2507 C  CG1 . ILE C 1 96  ? -32.555 -8.452  19.556  1.00 13.42 ? 96  ILE C CG1 1 
ATOM   2508 C  CG2 . ILE C 1 96  ? -30.110 -8.007  20.110  1.00 13.29 ? 96  ILE C CG2 1 
ATOM   2509 C  CD1 . ILE C 1 96  ? -33.255 -8.177  20.860  1.00 14.73 ? 96  ILE C CD1 1 
ATOM   2510 N  N   . ASN C 1 97  ? -28.356 -10.148 17.905  1.00 11.52 ? 97  ASN C N   1 
ATOM   2511 C  CA  . ASN C 1 97  ? -27.036 -10.713 18.188  1.00 11.55 ? 97  ASN C CA  1 
ATOM   2512 C  C   . ASN C 1 97  ? -26.271 -9.822  19.165  1.00 11.71 ? 97  ASN C C   1 
ATOM   2513 O  O   . ASN C 1 97  ? -26.196 -8.598  18.973  1.00 12.23 ? 97  ASN C O   1 
ATOM   2514 C  CB  . ASN C 1 97  ? -26.213 -10.869 16.904  1.00 13.25 ? 97  ASN C CB  1 
ATOM   2515 C  CG  . ASN C 1 97  ? -26.683 -12.020 16.056  1.00 15.24 ? 97  ASN C CG  1 
ATOM   2516 O  OD1 . ASN C 1 97  ? -27.214 -13.016 16.572  1.00 17.62 ? 97  ASN C OD1 1 
ATOM   2517 N  ND2 . ASN C 1 97  ? -26.498 -11.900 14.760  1.00 15.50 ? 97  ASN C ND2 1 
ATOM   2518 N  N   . TYR C 1 98  ? -25.686 -10.436 20.192  1.00 11.52 ? 98  TYR C N   1 
ATOM   2519 C  CA  . TYR C 1 98  ? -24.944 -9.741  21.237  1.00 11.70 ? 98  TYR C CA  1 
ATOM   2520 C  C   . TYR C 1 98  ? -23.446 -9.972  21.086  1.00 12.20 ? 98  TYR C C   1 
ATOM   2521 O  O   . TYR C 1 98  ? -23.003 -11.106 20.866  1.00 12.82 ? 98  TYR C O   1 
ATOM   2522 C  CB  . TYR C 1 98  ? -25.400 -10.254 22.610  1.00 12.38 ? 98  TYR C CB  1 
ATOM   2523 C  CG  . TYR C 1 98  ? -26.844 -9.897  22.887  1.00 12.04 ? 98  TYR C CG  1 
ATOM   2524 C  CD1 . TYR C 1 98  ? -27.188 -8.607  23.302  1.00 12.31 ? 98  TYR C CD1 1 
ATOM   2525 C  CD2 . TYR C 1 98  ? -27.874 -10.831 22.725  1.00 12.22 ? 98  TYR C CD2 1 
ATOM   2526 C  CE1 . TYR C 1 98  ? -28.533 -8.247  23.542  1.00 12.00 ? 98  TYR C CE1 1 
ATOM   2527 C  CE2 . TYR C 1 98  ? -29.209 -10.483 22.963  1.00 12.01 ? 98  TYR C CE2 1 
ATOM   2528 C  CZ  . TYR C 1 98  ? -29.526 -9.187  23.370  1.00 12.10 ? 98  TYR C CZ  1 
ATOM   2529 O  OH  . TYR C 1 98  ? -30.831 -8.827  23.549  1.00 13.09 ? 98  TYR C OH  1 
ATOM   2530 N  N   . TYR C 1 99  ? -22.669 -8.897  21.251  1.00 12.20 ? 99  TYR C N   1 
ATOM   2531 C  CA  . TYR C 1 99  ? -21.216 -8.923  21.078  1.00 11.91 ? 99  TYR C CA  1 
ATOM   2532 C  C   . TYR C 1 99  ? -20.560 -8.246  22.269  1.00 13.07 ? 99  TYR C C   1 
ATOM   2533 O  O   . TYR C 1 99  ? -20.775 -7.050  22.514  1.00 12.95 ? 99  TYR C O   1 
ATOM   2534 C  CB  . TYR C 1 99  ? -20.804 -8.208  19.781  1.00 13.11 ? 99  TYR C CB  1 
ATOM   2535 C  CG  . TYR C 1 99  ? -21.421 -8.826  18.558  1.00 13.72 ? 99  TYR C CG  1 
ATOM   2536 C  CD1 . TYR C 1 99  ? -22.677 -8.420  18.124  1.00 14.38 ? 99  TYR C CD1 1 
ATOM   2537 C  CD2 . TYR C 1 99  ? -20.777 -9.862  17.870  1.00 15.57 ? 99  TYR C CD2 1 
ATOM   2538 C  CE1 . TYR C 1 99  ? -23.270 -8.998  17.035  1.00 15.04 ? 99  TYR C CE1 1 
ATOM   2539 C  CE2 . TYR C 1 99  ? -21.357 -10.452 16.746  1.00 16.41 ? 99  TYR C CE2 1 
ATOM   2540 C  CZ  . TYR C 1 99  ? -22.605 -10.017 16.336  1.00 16.14 ? 99  TYR C CZ  1 
ATOM   2541 O  OH  . TYR C 1 99  ? -23.176 -10.630 15.233  1.00 17.87 ? 99  TYR C OH  1 
ATOM   2542 N  N   . ASP C 1 100 ? -19.740 -8.999  22.994  1.00 13.62 ? 100 ASP C N   1 
ATOM   2543 C  CA  . ASP C 1 100 ? -18.923 -8.468  24.081  1.00 13.64 ? 100 ASP C CA  1 
ATOM   2544 C  C   . ASP C 1 100 ? -17.587 -8.098  23.459  1.00 12.92 ? 100 ASP C C   1 
ATOM   2545 O  O   . ASP C 1 100 ? -16.780 -8.975  23.128  1.00 14.19 ? 100 ASP C O   1 
ATOM   2546 C  CB  . ASP C 1 100 ? -18.760 -9.537  25.151  1.00 14.76 ? 100 ASP C CB  1 
ATOM   2547 C  CG  . ASP C 1 100 ? -18.044 -9.042  26.379  1.00 17.34 ? 100 ASP C CG  1 
ATOM   2548 O  OD1 . ASP C 1 100 ? -17.629 -7.857  26.424  1.00 17.14 ? 100 ASP C OD1 1 
ATOM   2549 O  OD2 . ASP C 1 100 ? -17.877 -9.873  27.299  1.00 19.16 ? 100 ASP C OD2 1 
ATOM   2550 N  N   . MET C 1 101 ? -17.361 -6.799  23.265  1.00 12.46 ? 101 MET C N   1 
ATOM   2551 C  CA  . MET C 1 101 ? -16.171 -6.324  22.568  1.00 13.64 ? 101 MET C CA  1 
ATOM   2552 C  C   . MET C 1 101 ? -15.010 -6.120  23.532  1.00 13.84 ? 101 MET C C   1 
ATOM   2553 O  O   . MET C 1 101 ? -15.188 -5.590  24.638  1.00 15.06 ? 101 MET C O   1 
ATOM   2554 C  CB  . MET C 1 101 ? -16.453 -4.991  21.883  1.00 14.98 ? 101 MET C CB  1 
ATOM   2555 C  CG  . MET C 1 101 ? -17.551 -5.053  20.824  1.00 15.74 ? 101 MET C CG  1 
ATOM   2556 S  SD  . MET C 1 101 ? -17.199 -6.191  19.453  1.00 16.71 ? 101 MET C SD  1 
ATOM   2557 C  CE  . MET C 1 101 ? -15.785 -5.370  18.732  1.00 17.24 ? 101 MET C CE  1 
ATOM   2558 N  N   . ASN C 1 102 ? -13.812 -6.521  23.100  1.00 14.56 ? 102 ASN C N   1 
ATOM   2559 C  CA  . ASN C 1 102 ? -12.602 -6.140  23.827  1.00 15.90 ? 102 ASN C CA  1 
ATOM   2560 C  C   . ASN C 1 102 ? -12.328 -4.655  23.600  1.00 16.01 ? 102 ASN C C   1 
ATOM   2561 O  O   . ASN C 1 102 ? -12.455 -4.152  22.475  1.00 16.43 ? 102 ASN C O   1 
ATOM   2562 C  CB  . ASN C 1 102 ? -11.382 -6.936  23.331  1.00 17.74 ? 102 ASN C CB  1 
ATOM   2563 C  CG  . ASN C 1 102 ? -11.465 -8.418  23.656  1.00 21.67 ? 102 ASN C CG  1 
ATOM   2564 O  OD1 . ASN C 1 102 ? -12.339 -8.863  24.405  1.00 23.71 ? 102 ASN C OD1 1 
ATOM   2565 N  ND2 . ASN C 1 102 ? -10.513 -9.185  23.123  1.00 22.97 ? 102 ASN C ND2 1 
ATOM   2566 N  N   . ALA C 1 103 ? -11.896 -3.962  24.665  1.00 16.56 ? 103 ALA C N   1 
ATOM   2567 C  CA  . ALA C 1 103 ? -11.657 -2.521  24.586  1.00 16.41 ? 103 ALA C CA  1 
ATOM   2568 C  C   . ALA C 1 103 ? -10.655 -2.175  23.500  1.00 16.53 ? 103 ALA C C   1 
ATOM   2569 O  O   . ALA C 1 103 ? -10.784 -1.129  22.852  1.00 16.93 ? 103 ALA C O   1 
ATOM   2570 C  CB  . ALA C 1 103 ? -11.168 -1.993  25.939  1.00 16.65 ? 103 ALA C CB  1 
ATOM   2571 N  N   . ALA C 1 104 ? -9.663  -3.047  23.280  1.00 15.79 ? 104 ALA C N   1 
ATOM   2572 C  CA  . ALA C 1 104 ? -8.650  -2.828  22.258  1.00 16.10 ? 104 ALA C CA  1 
ATOM   2573 C  C   . ALA C 1 104 ? -9.232  -2.861  20.858  1.00 15.53 ? 104 ALA C C   1 
ATOM   2574 O  O   . ALA C 1 104 ? -8.590  -2.352  19.929  1.00 15.63 ? 104 ALA C O   1 
ATOM   2575 C  CB  . ALA C 1 104 ? -7.563  -3.907  22.348  1.00 16.18 ? 104 ALA C CB  1 
ATOM   2576 N  N   . ASN C 1 105 ? -10.443 -3.403  20.698  1.00 14.75 ? 105 ASN C N   1 
ATOM   2577 C  CA  . ASN C 1 105 ? -11.087 -3.568  19.399  1.00 13.99 ? 105 ASN C CA  1 
ATOM   2578 C  C   . ASN C 1 105 ? -12.201 -2.561  19.162  1.00 13.66 ? 105 ASN C C   1 
ATOM   2579 O  O   . ASN C 1 105 ? -12.978 -2.718  18.222  1.00 13.82 ? 105 ASN C O   1 
ATOM   2580 C  CB  . ASN C 1 105 ? -11.579 -4.999  19.200  1.00 14.14 ? 105 ASN C CB  1 
ATOM   2581 C  CG  . ASN C 1 105 ? -10.439 -5.978  19.014  1.00 14.95 ? 105 ASN C CG  1 
ATOM   2582 O  OD1 . ASN C 1 105 ? -9.348  -5.621  18.541  1.00 16.23 ? 105 ASN C OD1 1 
ATOM   2583 N  ND2 . ASN C 1 105 ? -10.684 -7.225  19.371  1.00 15.98 ? 105 ASN C ND2 1 
ATOM   2584 N  N   . VAL C 1 106 ? -12.272 -1.496  19.961  1.00 14.31 ? 106 VAL C N   1 
ATOM   2585 C  CA  . VAL C 1 106 ? -13.253 -0.434  19.744  1.00 14.98 ? 106 VAL C CA  1 
ATOM   2586 C  C   . VAL C 1 106 ? -12.522 0.895   19.606  1.00 15.87 ? 106 VAL C C   1 
ATOM   2587 O  O   . VAL C 1 106 ? -11.931 1.398   20.574  1.00 17.10 ? 106 VAL C O   1 
ATOM   2588 C  CB  . VAL C 1 106 ? -14.327 -0.374  20.842  1.00 14.84 ? 106 VAL C CB  1 
ATOM   2589 C  CG1 . VAL C 1 106 ? -15.321 0.730   20.510  1.00 15.38 ? 106 VAL C CG1 1 
ATOM   2590 C  CG2 . VAL C 1 106 ? -15.035 -1.715  20.977  1.00 14.99 ? 106 VAL C CG2 1 
ATOM   2591 N  N   . GLY C 1 107 ? -12.564 1.458   18.402  1.00 14.88 ? 107 GLY C N   1 
ATOM   2592 C  CA  . GLY C 1 107 ? -12.036 2.777   18.155  1.00 15.24 ? 107 GLY C CA  1 
ATOM   2593 C  C   . GLY C 1 107 ? -13.059 3.877   18.404  1.00 15.76 ? 107 GLY C C   1 
ATOM   2594 O  O   . GLY C 1 107 ? -14.261 3.719   18.176  1.00 15.95 ? 107 GLY C O   1 
ATOM   2595 N  N   . TRP C 1 108 ? -12.553 5.013   18.872  1.00 16.29 ? 108 TRP C N   1 
ATOM   2596 C  CA  . TRP C 1 108 ? -13.354 6.191   19.183  1.00 17.15 ? 108 TRP C CA  1 
ATOM   2597 C  C   . TRP C 1 108 ? -12.380 7.325   19.434  1.00 18.34 ? 108 TRP C C   1 
ATOM   2598 O  O   . TRP C 1 108 ? -11.351 7.117   20.084  1.00 18.99 ? 108 TRP C O   1 
ATOM   2599 C  CB  . TRP C 1 108 ? -14.223 5.957   20.430  1.00 18.86 ? 108 TRP C CB  1 
ATOM   2600 C  CG  . TRP C 1 108 ? -14.935 7.194   20.932  1.00 20.62 ? 108 TRP C CG  1 
ATOM   2601 C  CD1 . TRP C 1 108 ? -16.029 7.801   20.376  1.00 21.19 ? 108 TRP C CD1 1 
ATOM   2602 C  CD2 . TRP C 1 108 ? -14.585 7.983   22.077  1.00 21.87 ? 108 TRP C CD2 1 
ATOM   2603 N  NE1 . TRP C 1 108 ? -16.388 8.909   21.112  1.00 21.98 ? 108 TRP C NE1 1 
ATOM   2604 C  CE2 . TRP C 1 108 ? -15.518 9.040   22.159  1.00 22.00 ? 108 TRP C CE2 1 
ATOM   2605 C  CE3 . TRP C 1 108 ? -13.577 7.895   23.041  1.00 22.46 ? 108 TRP C CE3 1 
ATOM   2606 C  CZ2 . TRP C 1 108 ? -15.472 10.002  23.166  1.00 22.30 ? 108 TRP C CZ2 1 
ATOM   2607 C  CZ3 . TRP C 1 108 ? -13.536 8.853   24.048  1.00 23.14 ? 108 TRP C CZ3 1 
ATOM   2608 C  CH2 . TRP C 1 108 ? -14.474 9.892   24.095  1.00 23.27 ? 108 TRP C CH2 1 
ATOM   2609 N  N   . ASN C 1 109 ? -12.683 8.499   18.878  1.00 19.37 ? 109 ASN C N   1 
ATOM   2610 C  CA  . ASN C 1 109 ? -11.952 9.726   19.215  1.00 21.28 ? 109 ASN C CA  1 
ATOM   2611 C  C   . ASN C 1 109 ? -10.455 9.568   18.955  1.00 21.72 ? 109 ASN C C   1 
ATOM   2612 O  O   . ASN C 1 109 ? -9.622  9.834   19.823  1.00 22.52 ? 109 ASN C O   1 
ATOM   2613 C  CB  . ASN C 1 109 ? -12.182 10.143  20.670  1.00 23.79 ? 109 ASN C CB  1 
ATOM   2614 C  CG  . ASN C 1 109 ? -11.787 11.600  20.937  1.00 26.33 ? 109 ASN C CG  1 
ATOM   2615 O  OD1 . ASN C 1 109 ? -11.600 12.401  20.015  1.00 26.72 ? 109 ASN C OD1 1 
ATOM   2616 N  ND2 . ASN C 1 109 ? -11.568 11.911  22.200  1.00 27.63 ? 109 ASN C ND2 1 
ATOM   2617 N  N   . ASN C 1 110 ? -10.117 9.069   17.769  1.00 21.57 ? 110 ASN C N   1 
ATOM   2618 C  CA  . ASN C 1 110 ? -8.734  8.942   17.305  1.00 21.22 ? 110 ASN C CA  1 
ATOM   2619 C  C   . ASN C 1 110 ? -7.937  7.874   18.039  1.00 21.17 ? 110 ASN C C   1 
ATOM   2620 O  O   . ASN C 1 110 ? -6.710  7.779   17.848  1.00 22.75 ? 110 ASN C O   1 
ATOM   2621 C  CB  . ASN C 1 110 ? -7.967  10.272  17.310  1.00 22.88 ? 110 ASN C CB  1 
ATOM   2622 C  CG  . ASN C 1 110 ? -8.429  11.186  16.217  1.00 24.79 ? 110 ASN C CG  1 
ATOM   2623 O  OD1 . ASN C 1 110 ? -8.497  10.779  15.055  1.00 26.06 ? 110 ASN C OD1 1 
ATOM   2624 N  ND2 . ASN C 1 110 ? -8.760  12.421  16.569  1.00 25.52 ? 110 ASN C ND2 1 
ATOM   2625 N  N   . SER C 1 111 ? -8.578  7.059   18.866  1.00 20.04 ? 111 SER C N   1 
ATOM   2626 C  CA  . SER C 1 111 ? -7.829  6.055   19.613  1.00 21.04 ? 111 SER C CA  1 
ATOM   2627 C  C   . SER C 1 111 ? -8.741  4.852   19.834  1.00 19.57 ? 111 SER C C   1 
ATOM   2628 O  O   . SER C 1 111 ? -9.745  4.686   19.133  1.00 19.43 ? 111 SER C O   1 
ATOM   2629 C  CB  . SER C 1 111 ? -7.281  6.685   20.907  1.00 22.93 ? 111 SER C CB  1 
ATOM   2630 O  OG  . SER C 1 111 ? -6.449  5.773   21.585  1.00 24.80 ? 111 SER C OG  1 
ATOM   2631 N  N   . THR C 1 112 ? -8.373  3.989   20.783  1.00 19.95 ? 112 THR C N   1 
ATOM   2632 C  CA  . THR C 1 112 ? -9.237  2.904   21.229  1.00 20.23 ? 112 THR C CA  1 
ATOM   2633 C  C   . THR C 1 112 ? -9.380  2.983   22.743  1.00 21.18 ? 112 THR C C   1 
ATOM   2634 O  O   . THR C 1 112 ? -8.725  3.788   23.415  1.00 21.53 ? 112 THR C O   1 
ATOM   2635 C  CB  . THR C 1 112 ? -8.714  1.513   20.830  1.00 19.73 ? 112 THR C CB  1 
ATOM   2636 O  OG1 . THR C 1 112 ? -7.576  1.191   21.636  1.00 19.88 ? 112 THR C OG1 1 
ATOM   2637 C  CG2 . THR C 1 112 ? -8.325  1.480   19.337  1.00 19.13 ? 112 THR C CG2 1 
ATOM   2638 N  N   . PHE C 1 113 ? -10.260 2.141   23.273  1.00 22.01 ? 113 PHE C N   1 
ATOM   2639 C  CA  . PHE C 1 113 ? -10.543 2.137   24.702  1.00 23.30 ? 113 PHE C CA  1 
ATOM   2640 C  C   . PHE C 1 113 ? -9.549  1.323   25.525  1.00 24.52 ? 113 PHE C C   1 
ATOM   2641 O  O   . PHE C 1 113 ? -9.648  1.331   26.761  1.00 25.38 ? 113 PHE C O   1 
ATOM   2642 C  CB  . PHE C 1 113 ? -11.976 1.674   24.926  1.00 23.29 ? 113 PHE C CB  1 
ATOM   2643 C  CG  . PHE C 1 113 ? -12.987 2.702   24.529  1.00 23.22 ? 113 PHE C CG  1 
ATOM   2644 C  CD1 . PHE C 1 113 ? -13.116 3.898   25.237  1.00 23.32 ? 113 PHE C CD1 1 
ATOM   2645 C  CD2 . PHE C 1 113 ? -13.750 2.515   23.395  1.00 23.48 ? 113 PHE C CD2 1 
ATOM   2646 C  CE1 . PHE C 1 113 ? -14.044 4.844   24.845  1.00 24.01 ? 113 PHE C CE1 1 
ATOM   2647 C  CE2 . PHE C 1 113 ? -14.676 3.447   22.998  1.00 23.54 ? 113 PHE C CE2 1 
ATOM   2648 C  CZ  . PHE C 1 113 ? -14.826 4.615   23.713  1.00 23.71 ? 113 PHE C CZ  1 
ATOM   2649 N  N   . ALA C 1 114 ? -8.618  0.618   24.886  1.00 25.34 ? 114 ALA C N   1 
ATOM   2650 C  CA  . ALA C 1 114 ? -7.624  -0.191  25.591  1.00 27.03 ? 114 ALA C CA  1 
ATOM   2651 C  C   . ALA C 1 114 ? -6.751  0.663   26.506  1.00 29.32 ? 114 ALA C C   1 
ATOM   2652 O  O   . ALA C 1 114 ? -6.375  1.791   26.165  1.00 29.39 ? 114 ALA C O   1 
ATOM   2653 C  CB  . ALA C 1 114 ? -6.754  -0.957  24.601  1.00 26.82 ? 114 ALA C CB  1 
ATOM   2654 O  OXT . ALA C 1 114 ? -6.402  0.228   27.609  1.00 30.72 ? 114 ALA C OXT 1 
HETATM 2655 CL CL  . CL  D 2 .   ? -15.087 1.452   -10.921 1.00 26.23 ? 201 CL  A CL  1 
HETATM 2656 CL CL  . CL  E 2 .   ? -16.817 -28.066 9.638   1.00 24.75 ? 202 CL  A CL  1 
HETATM 2657 CL CL  . CL  F 2 .   ? -20.956 -15.556 20.315  1.00 16.09 ? 203 CL  A CL  1 
HETATM 2658 C  C1  . 7Y8 G 3 .   ? -23.468 -25.701 20.872  1.00 26.30 ? 204 7Y8 A C1  1 
HETATM 2659 C  C2  . 7Y8 G 3 .   ? -24.651 -25.219 20.057  1.00 26.91 ? 204 7Y8 A C2  1 
HETATM 2660 C  C11 . 7Y8 G 3 .   ? -27.163 -25.708 19.559  1.00 26.68 ? 204 7Y8 A C11 1 
HETATM 2661 C  C12 . 7Y8 G 3 .   ? -27.795 -26.250 18.444  1.00 26.09 ? 204 7Y8 A C12 1 
HETATM 2662 C  C13 . 7Y8 G 3 .   ? -29.011 -25.740 17.995  1.00 24.83 ? 204 7Y8 A C13 1 
HETATM 2663 C  C14 . 7Y8 G 3 .   ? -29.604 -24.657 18.664  1.00 26.14 ? 204 7Y8 A C14 1 
HETATM 2664 C  C15 . 7Y8 G 3 .   ? -28.940 -24.130 19.783  1.00 26.17 ? 204 7Y8 A C15 1 
HETATM 2665 C  C17 . 7Y8 G 3 .   ? -27.731 -24.640 20.241  1.00 26.85 ? 204 7Y8 A C17 1 
HETATM 2666 C  C8  . 7Y8 G 3 .   ? -25.836 -26.260 19.986  1.00 27.82 ? 204 7Y8 A C8  1 
HETATM 2667 N  N4  . 7Y8 G 3 .   ? -24.156 -25.041 18.686  1.00 27.04 ? 204 7Y8 A N4  1 
HETATM 2668 O  O10 . 7Y8 G 3 .   ? -25.670 -27.447 20.180  1.00 29.19 ? 204 7Y8 A O10 1 
HETATM 2669 O  O16 . 7Y8 G 3 .   ? -29.474 -23.064 20.450  1.00 27.17 ? 204 7Y8 A O16 1 
HETATM 2670 CL CL  . CL  H 2 .   ? -0.878  -4.629  17.298  1.00 29.50 ? 201 CL  B CL  1 
HETATM 2671 CL CL  . CL  I 2 .   ? -16.614 7.369   -4.184  1.00 34.18 ? 202 CL  B CL  1 
HETATM 2672 CL CL  . CL  J 2 .   ? -13.321 -15.434 13.128  1.00 16.05 ? 203 CL  B CL  1 
HETATM 2673 C  C1  . J23 K 4 .   ? -2.773  -16.047 10.726  1.00 25.70 ? 204 J23 B C1  1 
HETATM 2674 C  C2  . J23 K 4 .   ? -3.253  -15.104 9.654   1.00 26.81 ? 204 J23 B C2  1 
HETATM 2675 C  C11 . J23 K 4 .   ? -3.033  -14.962 7.004   1.00 22.14 ? 204 J23 B C11 1 
HETATM 2676 C  C12 . J23 K 4 .   ? -2.463  -13.870 6.337   1.00 20.70 ? 204 J23 B C12 1 
HETATM 2677 C  C13 . J23 K 4 .   ? -2.979  -13.430 5.116   1.00 20.09 ? 204 J23 B C13 1 
HETATM 2678 C  C14 . J23 K 4 .   ? -4.060  -14.069 4.544   1.00 20.25 ? 204 J23 B C14 1 
HETATM 2679 C  C15 . J23 K 4 .   ? -4.612  -15.165 5.208   1.00 20.40 ? 204 J23 B C15 1 
HETATM 2680 C  C17 . J23 K 4 .   ? -4.122  -15.638 6.431   1.00 21.28 ? 204 J23 B C17 1 
HETATM 2681 C  C8  . J23 K 4 .   ? -2.421  -15.299 8.346   1.00 25.13 ? 204 J23 B C8  1 
HETATM 2682 N  N4  . J23 K 4 .   ? -4.643  -15.354 9.464   1.00 30.79 ? 204 J23 B N4  1 
HETATM 2683 O  O10 . J23 K 4 .   ? -1.264  -15.567 8.504   1.00 25.93 ? 204 J23 B O10 1 
HETATM 2684 O  O16 . J23 K 4 .   ? -5.703  -15.754 4.639   1.00 20.64 ? 204 J23 B O16 1 
HETATM 2685 CL CL  . CL  L 2 .   ? -13.518 -8.202  20.526  1.00 18.42 ? 201 CL  C CL  1 
HETATM 2686 CL CL  . CL  M 2 .   ? -19.304 0.079   25.045  1.00 28.04 ? 202 CL  C CL  1 
HETATM 2687 CL CL  . CL  N 2 .   ? -32.170 -14.839 33.904  1.00 29.88 ? 203 CL  C CL  1 
HETATM 2688 O  O   . HOH O 5 .   ? -16.819 -22.635 16.053  1.00 39.50 ? 301 HOH A O   1 
HETATM 2689 O  O   . HOH O 5 .   ? -18.980 -29.355 -4.049  1.00 40.30 ? 302 HOH A O   1 
HETATM 2690 O  O   . HOH O 5 .   ? -17.975 -16.929 17.252  1.00 20.53 ? 303 HOH A O   1 
HETATM 2691 O  O   . HOH O 5 .   ? -25.574 -12.541 9.023   1.00 22.60 ? 304 HOH A O   1 
HETATM 2692 O  O   . HOH O 5 .   ? -15.093 -15.188 -10.354 1.00 30.07 ? 305 HOH A O   1 
HETATM 2693 O  O   . HOH O 5 .   ? -11.313 -4.520  -8.803  1.00 31.84 ? 306 HOH A O   1 
HETATM 2694 O  O   . HOH O 5 .   ? -16.682 -25.804 14.016  1.00 38.11 ? 307 HOH A O   1 
HETATM 2695 O  O   . HOH O 5 .   ? -31.386 -3.294  -13.349 1.00 45.39 ? 308 HOH A O   1 
HETATM 2696 O  O   . HOH O 5 .   ? -34.268 -25.593 -2.286  1.00 22.01 ? 309 HOH A O   1 
HETATM 2697 O  O   . HOH O 5 .   ? -32.193 -22.407 -6.127  1.00 28.46 ? 310 HOH A O   1 
HETATM 2698 O  O   . HOH O 5 .   ? -21.817 -30.224 11.914  1.00 43.00 ? 311 HOH A O   1 
HETATM 2699 O  O   . HOH O 5 .   ? -35.978 -23.089 19.506  1.00 15.68 ? 312 HOH A O   1 
HETATM 2700 O  O   . HOH O 5 .   ? -37.132 -15.239 -9.932  1.00 23.11 ? 313 HOH A O   1 
HETATM 2701 O  O   . HOH O 5 .   ? -34.919 -16.933 22.600  1.00 40.32 ? 314 HOH A O   1 
HETATM 2702 O  O   . HOH O 5 .   ? -7.091  -3.237  -7.766  1.00 28.71 ? 315 HOH A O   1 
HETATM 2703 O  O   . HOH O 5 .   ? -28.460 -15.486 27.354  1.00 17.36 ? 316 HOH A O   1 
HETATM 2704 O  O   . HOH O 5 .   ? -34.524 -23.088 -3.373  1.00 24.77 ? 317 HOH A O   1 
HETATM 2705 O  O   . HOH O 5 .   ? -40.684 -19.990 -2.718  1.00 18.96 ? 318 HOH A O   1 
HETATM 2706 O  O   . HOH O 5 .   ? -37.948 -8.801  -7.572  1.00 46.27 ? 319 HOH A O   1 
HETATM 2707 O  O   . HOH O 5 .   ? -9.793  -10.369 2.338   1.00 32.77 ? 320 HOH A O   1 
HETATM 2708 O  O   . HOH O 5 .   ? -39.594 -18.906 1.837   1.00 13.99 ? 321 HOH A O   1 
HETATM 2709 O  O   . HOH O 5 .   ? -31.767 -18.223 27.705  1.00 19.85 ? 322 HOH A O   1 
HETATM 2710 O  O   . HOH O 5 .   ? -19.872 -11.181 -13.363 1.00 42.37 ? 323 HOH A O   1 
HETATM 2711 O  O   . HOH O 5 .   ? -23.461 -27.445 7.492   1.00 28.40 ? 324 HOH A O   1 
HETATM 2712 O  O   . HOH O 5 .   ? -27.365 -30.010 6.053   1.00 39.39 ? 325 HOH A O   1 
HETATM 2713 O  O   . HOH O 5 .   ? -19.837 -24.830 14.834  1.00 20.25 ? 326 HOH A O   1 
HETATM 2714 O  O   . HOH O 5 .   ? -32.922 -3.933  2.102   1.00 15.12 ? 327 HOH A O   1 
HETATM 2715 O  O   . HOH O 5 .   ? -29.457 -23.144 29.595  1.00 34.05 ? 328 HOH A O   1 
HETATM 2716 O  O   . HOH O 5 .   ? -35.789 -15.483 29.662  1.00 22.04 ? 329 HOH A O   1 
HETATM 2717 O  O   . HOH O 5 .   ? -34.607 -18.955 26.875  1.00 39.26 ? 330 HOH A O   1 
HETATM 2718 O  O   . HOH O 5 .   ? -19.116 -9.112  -10.521 1.00 18.03 ? 331 HOH A O   1 
HETATM 2719 O  O   . HOH O 5 .   ? -13.743 -10.052 -11.147 1.00 23.04 ? 332 HOH A O   1 
HETATM 2720 O  O   . HOH O 5 .   ? -40.143 -22.701 16.900  1.00 35.66 ? 333 HOH A O   1 
HETATM 2721 O  O   . HOH O 5 .   ? -19.474 -8.982  5.370   1.00 33.16 ? 334 HOH A O   1 
HETATM 2722 O  O   . HOH O 5 .   ? -22.642 -14.247 26.825  1.00 26.11 ? 335 HOH A O   1 
HETATM 2723 O  O   . HOH O 5 .   ? -19.242 -19.865 19.354  1.00 32.26 ? 336 HOH A O   1 
HETATM 2724 O  O   . HOH O 5 .   ? -23.087 -8.416  7.065   1.00 28.41 ? 337 HOH A O   1 
HETATM 2725 O  O   . HOH O 5 .   ? -42.536 -13.940 -10.133 1.00 15.33 ? 338 HOH A O   1 
HETATM 2726 O  O   . HOH O 5 .   ? -25.783 3.967   -4.129  1.00 40.10 ? 339 HOH A O   1 
HETATM 2727 O  O   . HOH O 5 .   ? -36.319 -16.116 5.839   1.00 14.10 ? 340 HOH A O   1 
HETATM 2728 O  O   . HOH O 5 .   ? -16.342 -15.289 13.279  1.00 15.95 ? 341 HOH A O   1 
HETATM 2729 O  O   . HOH O 5 .   ? -23.628 -26.120 2.087   1.00 23.22 ? 342 HOH A O   1 
HETATM 2730 O  O   . HOH O 5 .   ? -20.739 -29.863 0.380   1.00 30.05 ? 343 HOH A O   1 
HETATM 2731 O  O   . HOH O 5 .   ? -41.253 -7.719  26.480  1.00 25.07 ? 344 HOH A O   1 
HETATM 2732 O  O   . HOH O 5 .   ? -21.677 -1.864  -11.116 1.00 29.28 ? 345 HOH A O   1 
HETATM 2733 O  O   . HOH O 5 .   ? -22.128 -22.062 19.100  1.00 28.90 ? 346 HOH A O   1 
HETATM 2734 O  O   . HOH O 5 .   ? -19.987 -24.259 18.282  1.00 29.61 ? 347 HOH A O   1 
HETATM 2735 O  O   . HOH O 5 .   ? -16.598 -9.311  -12.464 1.00 28.54 ? 348 HOH A O   1 
HETATM 2736 O  O   . HOH O 5 .   ? -36.184 -12.678 29.378  1.00 23.87 ? 349 HOH A O   1 
HETATM 2737 O  O   . HOH O 5 .   ? -33.051 -20.259 -9.438  1.00 26.67 ? 350 HOH A O   1 
HETATM 2738 O  O   . HOH O 5 .   ? -16.581 -28.542 2.175   1.00 24.83 ? 351 HOH A O   1 
HETATM 2739 O  O   . HOH O 5 .   ? -34.732 -15.642 -7.147  1.00 19.26 ? 352 HOH A O   1 
HETATM 2740 O  O   . HOH O 5 .   ? -29.193 -6.895  9.202   1.00 24.59 ? 353 HOH A O   1 
HETATM 2741 O  O   . HOH O 5 .   ? -32.512 -23.701 24.480  1.00 22.43 ? 354 HOH A O   1 
HETATM 2742 O  O   . HOH O 5 .   ? -25.618 -22.444 -5.602  1.00 20.45 ? 355 HOH A O   1 
HETATM 2743 O  O   . HOH O 5 .   ? -28.713 3.276   -1.678  1.00 29.11 ? 356 HOH A O   1 
HETATM 2744 O  O   . HOH O 5 .   ? -31.214 -0.536  -0.360  1.00 21.23 ? 357 HOH A O   1 
HETATM 2745 O  O   . HOH O 5 .   ? -40.506 -18.051 11.677  1.00 24.26 ? 358 HOH A O   1 
HETATM 2746 O  O   . HOH O 5 .   ? -20.814 -14.908 -6.618  1.00 16.87 ? 359 HOH A O   1 
HETATM 2747 O  O   . HOH O 5 .   ? -13.754 -9.898  6.218   1.00 21.64 ? 360 HOH A O   1 
HETATM 2748 O  O   . HOH O 5 .   ? -33.211 -22.858 27.887  1.00 25.33 ? 361 HOH A O   1 
HETATM 2749 O  O   . HOH O 5 .   ? -25.312 0.845   -6.323  1.00 32.14 ? 362 HOH A O   1 
HETATM 2750 O  O   . HOH O 5 .   ? -28.579 -28.082 11.979  1.00 25.71 ? 363 HOH A O   1 
HETATM 2751 O  O   . HOH O 5 .   ? -21.956 -26.461 4.932   1.00 30.00 ? 364 HOH A O   1 
HETATM 2752 O  O   . HOH O 5 .   ? -17.307 -17.327 14.975  1.00 16.39 ? 365 HOH A O   1 
HETATM 2753 O  O   . HOH O 5 .   ? -11.482 -9.676  -7.262  1.00 22.07 ? 366 HOH A O   1 
HETATM 2754 O  O   . HOH O 5 .   ? -21.779 -26.425 -1.580  1.00 22.99 ? 367 HOH A O   1 
HETATM 2755 O  O   . HOH O 5 .   ? -20.780 -22.283 -7.056  1.00 26.94 ? 368 HOH A O   1 
HETATM 2756 O  O   . HOH O 5 .   ? -43.670 -9.559  -9.601  1.00 35.35 ? 369 HOH A O   1 
HETATM 2757 O  O   . HOH O 5 .   ? -40.683 -7.805  -10.224 1.00 52.92 ? 370 HOH A O   1 
HETATM 2758 O  O   . HOH O 5 .   ? -28.568 -26.149 -0.038  1.00 23.94 ? 371 HOH A O   1 
HETATM 2759 O  O   . HOH O 5 .   ? -27.940 -4.570  -13.388 1.00 38.03 ? 372 HOH A O   1 
HETATM 2760 O  O   . HOH O 5 .   ? -22.520 -20.422 -10.954 1.00 38.39 ? 373 HOH A O   1 
HETATM 2761 O  O   . HOH O 5 .   ? -40.649 -22.897 -3.645  1.00 13.42 ? 374 HOH A O   1 
HETATM 2762 O  O   . HOH O 5 .   ? -22.788 -15.332 -13.376 1.00 43.64 ? 375 HOH A O   1 
HETATM 2763 O  O   . HOH O 5 .   ? -30.647 -18.456 -12.741 1.00 43.27 ? 376 HOH A O   1 
HETATM 2764 O  O   . HOH O 5 .   ? -19.617 -9.095  8.508   1.00 9.10  ? 377 HOH A O   1 
HETATM 2765 O  O   . HOH O 5 .   ? -22.633 -27.428 15.367  1.00 27.24 ? 378 HOH A O   1 
HETATM 2766 O  O   . HOH O 5 .   ? -26.180 -1.148  4.241   1.00 28.24 ? 379 HOH A O   1 
HETATM 2767 O  O   . HOH O 5 .   ? -33.500 -0.472  -9.427  1.00 22.16 ? 380 HOH A O   1 
HETATM 2768 O  O   . HOH O 5 .   ? -20.892 1.543   -6.026  1.00 25.38 ? 381 HOH A O   1 
HETATM 2769 O  O   . HOH O 5 .   ? -31.541 -28.171 13.215  1.00 28.08 ? 382 HOH A O   1 
HETATM 2770 O  O   . HOH O 5 .   ? -29.023 -19.863 14.584  1.00 12.85 ? 383 HOH A O   1 
HETATM 2771 O  O   . HOH O 5 .   ? -13.799 -29.423 2.539   1.00 31.03 ? 384 HOH A O   1 
HETATM 2772 O  O   . HOH O 5 .   ? -28.793 2.246   2.071   1.00 23.66 ? 385 HOH A O   1 
HETATM 2773 O  O   . HOH O 5 .   ? -27.882 -27.305 14.733  1.00 18.71 ? 386 HOH A O   1 
HETATM 2774 O  O   . HOH O 5 .   ? -43.454 -27.235 9.287   1.00 21.96 ? 387 HOH A O   1 
HETATM 2775 O  O   . HOH O 5 .   ? -23.804 -22.248 22.554  1.00 13.87 ? 388 HOH A O   1 
HETATM 2776 O  O   . HOH O 5 .   ? -13.288 -28.526 9.221   1.00 36.93 ? 389 HOH A O   1 
HETATM 2777 O  O   . HOH O 5 .   ? -33.822 -9.382  -11.797 1.00 40.67 ? 390 HOH A O   1 
HETATM 2778 O  O   . HOH O 5 .   ? -12.365 -8.095  -9.377  1.00 18.76 ? 391 HOH A O   1 
HETATM 2779 O  O   . HOH O 5 .   ? -26.377 -30.263 8.735   1.00 29.18 ? 392 HOH A O   1 
HETATM 2780 O  O   . HOH O 5 .   ? -39.051 -13.071 29.039  1.00 37.76 ? 393 HOH A O   1 
HETATM 2781 O  O   . HOH O 5 .   ? -38.115 -11.282 -11.479 1.00 25.77 ? 394 HOH A O   1 
HETATM 2782 O  O   . HOH O 5 .   ? -9.968  -25.949 7.439   1.00 24.18 ? 395 HOH A O   1 
HETATM 2783 O  O   . HOH O 5 .   ? -13.298 -26.315 12.008  1.00 30.84 ? 396 HOH A O   1 
HETATM 2784 O  O   . HOH O 5 .   ? -19.355 -15.123 16.720  1.00 20.41 ? 397 HOH A O   1 
HETATM 2785 O  O   . HOH O 5 .   ? -21.889 -18.510 26.164  1.00 31.16 ? 398 HOH A O   1 
HETATM 2786 O  O   . HOH O 5 .   ? -26.852 -4.020  6.234   1.00 19.53 ? 399 HOH A O   1 
HETATM 2787 O  O   . HOH O 5 .   ? -20.985 -27.941 13.529  1.00 20.94 ? 400 HOH A O   1 
HETATM 2788 O  O   . HOH O 5 .   ? -19.946 -28.330 -1.444  1.00 31.38 ? 401 HOH A O   1 
HETATM 2789 O  O   . HOH O 5 .   ? -37.482 -11.562 -2.625  1.00 23.94 ? 402 HOH A O   1 
HETATM 2790 O  O   . HOH O 5 .   ? -19.199 -13.512 24.616  1.00 20.47 ? 403 HOH A O   1 
HETATM 2791 O  O   . HOH O 5 .   ? -26.051 -21.749 -8.201  1.00 30.83 ? 404 HOH A O   1 
HETATM 2792 O  O   . HOH O 5 .   ? -21.933 0.589   -8.270  1.00 19.98 ? 405 HOH A O   1 
HETATM 2793 O  O   . HOH O 5 .   ? -29.760 -16.839 14.268  1.00 24.31 ? 406 HOH A O   1 
HETATM 2794 O  O   . HOH O 5 .   ? -44.808 -11.203 23.831  1.00 33.90 ? 407 HOH A O   1 
HETATM 2795 O  O   . HOH O 5 .   ? -42.309 -23.041 6.740   1.00 29.88 ? 408 HOH A O   1 
HETATM 2796 O  O   . HOH O 5 .   ? -24.452 -6.151  7.404   1.00 33.18 ? 409 HOH A O   1 
HETATM 2797 O  O   . HOH O 5 .   ? -24.155 -2.930  -10.098 1.00 26.52 ? 410 HOH A O   1 
HETATM 2798 O  O   . HOH O 5 .   ? -21.445 -14.054 -12.325 1.00 37.74 ? 411 HOH A O   1 
HETATM 2799 O  O   . HOH O 5 .   ? -31.398 -30.092 6.064   1.00 37.49 ? 412 HOH A O   1 
HETATM 2800 O  O   . HOH O 5 .   ? -22.719 -28.484 -5.124  1.00 38.88 ? 413 HOH A O   1 
HETATM 2801 O  O   . HOH O 5 .   ? -23.202 -24.198 -6.346  1.00 29.88 ? 414 HOH A O   1 
HETATM 2802 O  O   . HOH O 5 .   ? -34.280 -19.139 -11.943 1.00 21.30 ? 415 HOH A O   1 
HETATM 2803 O  O   . HOH O 5 .   ? -43.404 -7.988  23.975  1.00 26.98 ? 416 HOH A O   1 
HETATM 2804 O  O   . HOH O 5 .   ? -28.143 -23.807 -5.223  1.00 36.48 ? 417 HOH A O   1 
HETATM 2805 O  O   . HOH O 5 .   ? -21.964 -9.052  10.684  1.00 33.84 ? 418 HOH A O   1 
HETATM 2806 O  O   . HOH O 5 .   ? -22.188 -28.166 19.642  1.00 28.34 ? 419 HOH A O   1 
HETATM 2807 O  O   . HOH O 5 .   ? -22.216 -21.835 23.994  1.00 33.65 ? 420 HOH A O   1 
HETATM 2808 O  O   . HOH O 5 .   ? -21.121 -26.737 17.557  1.00 29.88 ? 421 HOH A O   1 
HETATM 2809 O  O   . HOH O 5 .   ? -17.074 -27.409 -0.658  1.00 20.80 ? 422 HOH A O   1 
HETATM 2810 O  O   . HOH O 5 .   ? -11.927 -23.807 11.423  1.00 39.89 ? 423 HOH A O   1 
HETATM 2811 O  O   . HOH O 5 .   ? -23.154 -3.773  6.750   1.00 22.89 ? 424 HOH A O   1 
HETATM 2812 O  O   . HOH O 5 .   ? -42.464 -9.859  27.894  1.00 24.57 ? 425 HOH A O   1 
HETATM 2813 O  O   . HOH O 5 .   ? -19.737 -29.583 4.888   1.00 28.54 ? 426 HOH A O   1 
HETATM 2814 O  O   . HOH O 5 .   ? -24.309 -22.194 -9.641  1.00 40.58 ? 427 HOH A O   1 
HETATM 2815 O  O   . HOH O 5 .   ? -20.980 -6.729  5.407   1.00 26.26 ? 428 HOH A O   1 
HETATM 2816 O  O   . HOH O 5 .   ? -23.222 -25.875 -4.106  1.00 22.22 ? 429 HOH A O   1 
HETATM 2817 O  O   . HOH O 5 .   ? -30.849 2.175   -0.462  1.00 29.84 ? 430 HOH A O   1 
HETATM 2818 O  O   . HOH O 5 .   ? -21.824 -28.959 4.919   1.00 45.64 ? 431 HOH A O   1 
HETATM 2819 O  O   . HOH O 5 .   ? -19.834 4.128   -6.832  1.00 34.62 ? 432 HOH A O   1 
HETATM 2820 O  O   . HOH O 5 .   ? -17.694 4.999   -6.482  1.00 38.23 ? 433 HOH A O   1 
HETATM 2821 O  O   . HOH O 5 .   ? -19.680 -15.216 -12.686 1.00 35.37 ? 434 HOH A O   1 
HETATM 2822 O  O   . HOH O 5 .   ? -12.757 -27.854 -0.823  1.00 41.26 ? 435 HOH A O   1 
HETATM 2823 O  O   . HOH O 5 .   ? -28.718 -20.613 -8.601  1.00 35.63 ? 436 HOH A O   1 
HETATM 2824 O  O   . HOH O 5 .   ? -26.626 4.189   -0.146  1.00 30.31 ? 437 HOH A O   1 
HETATM 2825 O  O   . HOH O 5 .   ? -30.152 -31.660 7.780   1.00 31.64 ? 438 HOH A O   1 
HETATM 2826 O  O   . HOH O 5 .   ? -29.754 -23.171 -7.329  1.00 39.28 ? 439 HOH A O   1 
HETATM 2827 O  O   . HOH O 5 .   ? -34.302 -22.968 -8.931  1.00 26.52 ? 440 HOH A O   1 
HETATM 2828 O  O   . HOH O 5 .   ? -19.203 4.067   -9.763  1.00 43.47 ? 441 HOH A O   1 
HETATM 2829 O  O   . HOH O 5 .   ? -31.059 2.415   1.945   1.00 29.69 ? 442 HOH A O   1 
HETATM 2830 O  O   . HOH O 5 .   ? -30.121 -20.654 -10.686 1.00 41.67 ? 443 HOH A O   1 
HETATM 2831 O  O   . HOH O 5 .   ? -13.830 -25.359 13.986  1.00 50.25 ? 444 HOH A O   1 
HETATM 2832 O  O   . HOH O 5 .   ? -25.579 -5.003  -11.713 1.00 26.26 ? 445 HOH A O   1 
HETATM 2833 O  O   . HOH O 5 .   ? -19.506 -17.870 -11.899 1.00 32.62 ? 446 HOH A O   1 
HETATM 2834 O  O   . HOH O 5 .   ? -25.487 -27.238 -3.349  1.00 62.32 ? 447 HOH A O   1 
HETATM 2835 O  O   . HOH O 5 .   ? -16.081 -13.307 15.229  1.00 18.34 ? 448 HOH A O   1 
HETATM 2836 O  O   . HOH O 5 .   ? -17.828 -11.122 16.130  1.00 16.32 ? 449 HOH A O   1 
HETATM 2837 O  O   . HOH O 5 .   ? -15.261 -14.932 17.321  1.00 40.07 ? 450 HOH A O   1 
HETATM 2838 O  O   . HOH P 5 .   ? -30.374 15.976  17.260  1.00 32.88 ? 301 HOH B O   1 
HETATM 2839 O  O   . HOH P 5 .   ? -0.736  -7.511  5.126   1.00 21.50 ? 302 HOH B O   1 
HETATM 2840 O  O   . HOH P 5 .   ? -30.659 12.194  4.914   1.00 38.25 ? 303 HOH B O   1 
HETATM 2841 O  O   . HOH P 5 .   ? -15.349 17.472  20.426  1.00 53.55 ? 304 HOH B O   1 
HETATM 2842 O  O   . HOH P 5 .   ? -14.873 -19.785 -8.286  1.00 41.77 ? 305 HOH B O   1 
HETATM 2843 O  O   . HOH P 5 .   ? -11.951 -12.304 16.132  1.00 17.92 ? 306 HOH B O   1 
HETATM 2844 O  O   . HOH P 5 .   ? -25.461 20.540  18.856  1.00 29.26 ? 307 HOH B O   1 
HETATM 2845 O  O   . HOH P 5 .   ? -13.140 -22.667 5.919   1.00 16.38 ? 308 HOH B O   1 
HETATM 2846 O  O   . HOH P 5 .   ? -13.740 15.325  18.498  1.00 32.06 ? 309 HOH B O   1 
HETATM 2847 O  O   . HOH P 5 .   ? -24.838 17.716  1.325   1.00 46.62 ? 310 HOH B O   1 
HETATM 2848 O  O   . HOH P 5 .   ? -18.442 16.744  2.874   1.00 37.59 ? 311 HOH B O   1 
HETATM 2849 O  O   . HOH P 5 .   ? -8.546  -14.427 14.523  1.00 29.88 ? 312 HOH B O   1 
HETATM 2850 O  O   . HOH P 5 .   ? -5.059  -19.874 1.673   1.00 24.15 ? 313 HOH B O   1 
HETATM 2851 O  O   . HOH P 5 .   ? -16.172 -4.220  8.035   1.00 21.01 ? 314 HOH B O   1 
HETATM 2852 O  O   . HOH P 5 .   ? -20.258 -2.054  10.313  1.00 31.24 ? 315 HOH B O   1 
HETATM 2853 O  O   . HOH P 5 .   ? -21.760 -4.269  4.436   1.00 21.48 ? 316 HOH B O   1 
HETATM 2854 O  O   . HOH P 5 .   ? -29.682 13.107  1.100   1.00 35.37 ? 317 HOH B O   1 
HETATM 2855 O  O   . HOH P 5 .   ? -19.800 15.399  14.233  1.00 25.01 ? 318 HOH B O   1 
HETATM 2856 O  O   . HOH P 5 .   ? -1.032  -2.742  10.421  1.00 29.40 ? 319 HOH B O   1 
HETATM 2857 O  O   . HOH P 5 .   ? -20.888 16.202  5.908   1.00 37.14 ? 320 HOH B O   1 
HETATM 2858 O  O   . HOH P 5 .   ? -0.386  2.794   17.357  1.00 29.12 ? 321 HOH B O   1 
HETATM 2859 O  O   . HOH P 5 .   ? -12.195 -1.352  -2.771  1.00 16.78 ? 322 HOH B O   1 
HETATM 2860 O  O   . HOH P 5 .   ? -2.461  6.433   12.141  1.00 29.52 ? 323 HOH B O   1 
HETATM 2861 O  O   . HOH P 5 .   ? -14.852 -21.920 11.916  1.00 26.44 ? 324 HOH B O   1 
HETATM 2862 O  O   . HOH P 5 .   ? -10.486 -23.217 2.760   1.00 20.21 ? 325 HOH B O   1 
HETATM 2863 O  O   . HOH P 5 .   ? -2.664  4.668   5.084   1.00 26.83 ? 326 HOH B O   1 
HETATM 2864 O  O   . HOH P 5 .   ? -12.076 11.531  -0.972  1.00 30.08 ? 327 HOH B O   1 
HETATM 2865 O  O   . HOH P 5 .   ? -10.520 -7.257  -6.420  1.00 23.97 ? 328 HOH B O   1 
HETATM 2866 O  O   . HOH P 5 .   ? -13.909 11.624  12.692  1.00 26.02 ? 329 HOH B O   1 
HETATM 2867 O  O   . HOH P 5 .   ? -20.301 18.549  10.158  1.00 36.00 ? 330 HOH B O   1 
HETATM 2868 O  O   . HOH P 5 .   ? -18.792 16.315  19.508  1.00 32.54 ? 331 HOH B O   1 
HETATM 2869 O  O   . HOH P 5 .   ? -6.328  10.375  8.174   1.00 24.58 ? 332 HOH B O   1 
HETATM 2870 O  O   . HOH P 5 .   ? -24.606 2.536   0.407   1.00 15.55 ? 333 HOH B O   1 
HETATM 2871 O  O   . HOH P 5 .   ? -26.943 15.818  11.419  1.00 36.72 ? 334 HOH B O   1 
HETATM 2872 O  O   . HOH P 5 .   ? -13.156 -25.270 -1.359  1.00 20.03 ? 335 HOH B O   1 
HETATM 2873 O  O   . HOH P 5 .   ? -19.252 17.860  17.037  1.00 29.88 ? 336 HOH B O   1 
HETATM 2874 O  O   . HOH P 5 .   ? -19.245 12.371  21.925  1.00 22.40 ? 337 HOH B O   1 
HETATM 2875 O  O   . HOH P 5 .   ? -3.546  -9.235  17.808  1.00 34.03 ? 338 HOH B O   1 
HETATM 2876 O  O   . HOH P 5 .   ? -6.794  -14.248 12.150  1.00 28.45 ? 339 HOH B O   1 
HETATM 2877 O  O   . HOH P 5 .   ? -5.878  -23.436 1.306   1.00 35.73 ? 340 HOH B O   1 
HETATM 2878 O  O   . HOH P 5 .   ? -26.524 21.746  14.566  1.00 28.74 ? 341 HOH B O   1 
HETATM 2879 O  O   . HOH P 5 .   ? -13.693 -8.323  17.506  1.00 15.64 ? 342 HOH B O   1 
HETATM 2880 O  O   . HOH P 5 .   ? -15.961 -24.925 -1.781  1.00 25.30 ? 343 HOH B O   1 
HETATM 2881 O  O   . HOH P 5 .   ? -28.124 5.265   2.045   1.00 24.31 ? 344 HOH B O   1 
HETATM 2882 O  O   . HOH P 5 .   ? -9.589  9.298   -4.275  1.00 26.87 ? 345 HOH B O   1 
HETATM 2883 O  O   . HOH P 5 .   ? -19.949 -0.447  13.894  1.00 34.28 ? 346 HOH B O   1 
HETATM 2884 O  O   . HOH P 5 .   ? 2.483   -7.249  5.661   1.00 33.82 ? 347 HOH B O   1 
HETATM 2885 O  O   . HOH P 5 .   ? 2.537   -6.222  2.977   1.00 29.48 ? 348 HOH B O   1 
HETATM 2886 O  O   . HOH P 5 .   ? -3.893  -9.962  14.158  1.00 21.75 ? 349 HOH B O   1 
HETATM 2887 O  O   . HOH P 5 .   ? -0.536  -2.632  0.510   1.00 25.44 ? 350 HOH B O   1 
HETATM 2888 O  O   . HOH P 5 .   ? -23.810 16.573  19.707  1.00 26.37 ? 351 HOH B O   1 
HETATM 2889 O  O   . HOH P 5 .   ? -19.175 -1.157  19.713  1.00 28.94 ? 352 HOH B O   1 
HETATM 2890 O  O   . HOH P 5 .   ? -31.809 6.322   4.381   1.00 27.33 ? 353 HOH B O   1 
HETATM 2891 O  O   . HOH P 5 .   ? -6.691  11.954  13.020  1.00 33.56 ? 354 HOH B O   1 
HETATM 2892 O  O   . HOH P 5 .   ? -11.577 -10.011 16.745  1.00 17.24 ? 355 HOH B O   1 
HETATM 2893 O  O   . HOH P 5 .   ? -2.661  2.918   10.241  1.00 31.91 ? 356 HOH B O   1 
HETATM 2894 O  O   . HOH P 5 .   ? -11.211 -19.839 -4.177  1.00 29.54 ? 357 HOH B O   1 
HETATM 2895 O  O   . HOH P 5 .   ? -14.209 14.806  23.217  1.00 52.88 ? 358 HOH B O   1 
HETATM 2896 O  O   . HOH P 5 .   ? -13.420 3.053   -5.968  1.00 26.04 ? 359 HOH B O   1 
HETATM 2897 O  O   . HOH P 5 .   ? -29.651 11.230  7.905   1.00 37.30 ? 360 HOH B O   1 
HETATM 2898 O  O   . HOH P 5 .   ? -17.615 18.346  12.917  1.00 47.24 ? 361 HOH B O   1 
HETATM 2899 O  O   . HOH P 5 .   ? -30.460 10.825  12.175  1.00 27.37 ? 362 HOH B O   1 
HETATM 2900 O  O   . HOH P 5 .   ? -1.107  -6.215  -5.108  1.00 22.24 ? 363 HOH B O   1 
HETATM 2901 O  O   . HOH P 5 .   ? -6.460  -9.730  17.623  1.00 31.01 ? 364 HOH B O   1 
HETATM 2902 O  O   . HOH P 5 .   ? -1.463  -10.576 11.600  1.00 23.68 ? 365 HOH B O   1 
HETATM 2903 O  O   . HOH P 5 .   ? -27.742 14.086  -0.610  1.00 25.62 ? 366 HOH B O   1 
HETATM 2904 O  O   . HOH P 5 .   ? -19.741 -3.597  14.039  1.00 11.66 ? 367 HOH B O   1 
HETATM 2905 O  O   . HOH P 5 .   ? -8.847  15.446  9.950   1.00 35.75 ? 368 HOH B O   1 
HETATM 2906 O  O   . HOH P 5 .   ? 0.486   2.409   20.440  1.00 36.16 ? 369 HOH B O   1 
HETATM 2907 O  O   . HOH P 5 .   ? -27.351 0.598   7.080   1.00 24.64 ? 370 HOH B O   1 
HETATM 2908 O  O   . HOH P 5 .   ? -14.000 6.347   -5.475  1.00 30.19 ? 371 HOH B O   1 
HETATM 2909 O  O   . HOH P 5 .   ? -12.833 6.708   -8.143  1.00 33.87 ? 372 HOH B O   1 
HETATM 2910 O  O   . HOH P 5 .   ? -8.893  -9.905  4.995   1.00 13.32 ? 373 HOH B O   1 
HETATM 2911 O  O   . HOH P 5 .   ? -30.887 2.919   4.343   1.00 24.91 ? 374 HOH B O   1 
HETATM 2912 O  O   . HOH P 5 .   ? -0.890  -8.574  13.331  1.00 25.40 ? 375 HOH B O   1 
HETATM 2913 O  O   . HOH P 5 .   ? -19.392 -7.906  12.637  1.00 29.88 ? 376 HOH B O   1 
HETATM 2914 O  O   . HOH P 5 .   ? -7.611  -22.041 0.163   1.00 38.90 ? 377 HOH B O   1 
HETATM 2915 O  O   . HOH P 5 .   ? -3.381  -2.250  23.984  1.00 35.71 ? 378 HOH B O   1 
HETATM 2916 O  O   . HOH P 5 .   ? -29.185 17.427  14.222  1.00 26.35 ? 379 HOH B O   1 
HETATM 2917 O  O   . HOH P 5 .   ? -16.812 15.784  -4.813  1.00 36.21 ? 380 HOH B O   1 
HETATM 2918 O  O   . HOH P 5 .   ? -21.053 14.320  21.027  1.00 21.36 ? 381 HOH B O   1 
HETATM 2919 O  O   . HOH P 5 .   ? -1.294  -10.223 6.296   1.00 13.18 ? 382 HOH B O   1 
HETATM 2920 O  O   . HOH P 5 .   ? -22.563 19.908  14.158  1.00 39.90 ? 383 HOH B O   1 
HETATM 2921 O  O   . HOH P 5 .   ? -6.440  -17.787 10.374  1.00 13.09 ? 384 HOH B O   1 
HETATM 2922 O  O   . HOH P 5 .   ? -10.763 -16.958 -9.963  1.00 30.35 ? 385 HOH B O   1 
HETATM 2923 O  O   . HOH P 5 .   ? -5.105  -6.383  -10.449 1.00 20.71 ? 386 HOH B O   1 
HETATM 2924 O  O   . HOH P 5 .   ? -2.522  -7.028  20.453  1.00 31.06 ? 387 HOH B O   1 
HETATM 2925 O  O   . HOH P 5 .   ? -13.752 -11.865 14.588  1.00 22.90 ? 388 HOH B O   1 
HETATM 2926 O  O   . HOH P 5 .   ? -7.847  15.885  3.432   1.00 37.42 ? 389 HOH B O   1 
HETATM 2927 O  O   . HOH P 5 .   ? -29.089 16.307  18.992  1.00 29.17 ? 390 HOH B O   1 
HETATM 2928 O  O   . HOH P 5 .   ? -14.087 9.672   -8.429  1.00 51.09 ? 391 HOH B O   1 
HETATM 2929 O  O   . HOH P 5 .   ? -1.854  -2.899  -7.092  1.00 31.64 ? 392 HOH B O   1 
HETATM 2930 O  O   . HOH P 5 .   ? -12.082 -14.661 15.736  1.00 35.55 ? 393 HOH B O   1 
HETATM 2931 O  O   . HOH P 5 .   ? -29.355 13.052  11.188  1.00 25.46 ? 394 HOH B O   1 
HETATM 2932 O  O   . HOH P 5 .   ? -32.738 14.777  13.308  1.00 31.64 ? 395 HOH B O   1 
HETATM 2933 O  O   . HOH P 5 .   ? -8.835  2.473   -5.764  1.00 28.06 ? 396 HOH B O   1 
HETATM 2934 O  O   . HOH P 5 .   ? -11.809 -9.577  4.237   1.00 25.08 ? 397 HOH B O   1 
HETATM 2935 O  O   . HOH P 5 .   ? -15.308 -19.732 15.061  1.00 17.82 ? 398 HOH B O   1 
HETATM 2936 O  O   . HOH P 5 .   ? 1.236   -7.088  12.239  1.00 34.30 ? 399 HOH B O   1 
HETATM 2937 O  O   . HOH P 5 .   ? -12.168 -21.171 12.861  1.00 32.58 ? 400 HOH B O   1 
HETATM 2938 O  O   . HOH P 5 .   ? -24.559 -1.561  6.613   1.00 20.37 ? 401 HOH B O   1 
HETATM 2939 O  O   . HOH P 5 .   ? -32.982 11.791  13.126  1.00 36.35 ? 402 HOH B O   1 
HETATM 2940 O  O   . HOH P 5 .   ? -7.146  12.818  7.031   1.00 29.18 ? 403 HOH B O   1 
HETATM 2941 O  O   . HOH P 5 .   ? -0.417  6.606   14.105  1.00 39.99 ? 404 HOH B O   1 
HETATM 2942 O  O   . HOH P 5 .   ? -26.010 15.032  8.910   1.00 30.51 ? 405 HOH B O   1 
HETATM 2943 O  O   . HOH P 5 .   ? -5.291  7.753   -1.262  1.00 27.15 ? 406 HOH B O   1 
HETATM 2944 O  O   . HOH P 5 .   ? -22.302 -2.638  9.159   1.00 28.26 ? 407 HOH B O   1 
HETATM 2945 O  O   . HOH P 5 .   ? -5.039  10.019  5.382   1.00 39.03 ? 408 HOH B O   1 
HETATM 2946 O  O   . HOH P 5 .   ? -10.997 13.146  -6.166  1.00 56.77 ? 409 HOH B O   1 
HETATM 2947 O  O   . HOH P 5 .   ? -12.302 11.254  -7.720  1.00 45.00 ? 410 HOH B O   1 
HETATM 2948 O  O   . HOH P 5 .   ? -30.571 15.281  11.975  1.00 38.19 ? 411 HOH B O   1 
HETATM 2949 O  O   . HOH P 5 .   ? -9.955  -21.392 12.381  1.00 33.12 ? 412 HOH B O   1 
HETATM 2950 O  O   . HOH P 5 .   ? -9.850  -12.808 17.502  1.00 33.73 ? 413 HOH B O   1 
HETATM 2951 O  O   . HOH P 5 .   ? -1.437  5.580   16.833  1.00 25.65 ? 414 HOH B O   1 
HETATM 2952 O  O   . HOH P 5 .   ? -17.210 13.380  23.976  1.00 32.23 ? 415 HOH B O   1 
HETATM 2953 O  O   . HOH P 5 .   ? -19.783 -5.748  11.876  1.00 34.26 ? 416 HOH B O   1 
HETATM 2954 O  O   . HOH P 5 .   ? -24.896 -1.836  10.064  1.00 23.69 ? 417 HOH B O   1 
HETATM 2955 O  O   . HOH P 5 .   ? -20.453 18.426  4.984   1.00 40.33 ? 418 HOH B O   1 
HETATM 2956 O  O   . HOH P 5 .   ? -10.155 17.766  9.668   1.00 39.38 ? 419 HOH B O   1 
HETATM 2957 O  O   . HOH P 5 .   ? 0.809   0.122   14.275  1.00 29.64 ? 420 HOH B O   1 
HETATM 2958 O  O   . HOH P 5 .   ? -20.437 -19.971 -9.511  1.00 29.85 ? 421 HOH B O   1 
HETATM 2959 O  O   . HOH P 5 .   ? -18.672 -23.814 -8.141  1.00 35.75 ? 422 HOH B O   1 
HETATM 2960 O  O   . HOH P 5 .   ? -2.804  9.065   10.990  1.00 30.03 ? 423 HOH B O   1 
HETATM 2961 O  O   . HOH P 5 .   ? -22.146 -0.373  12.481  1.00 28.80 ? 424 HOH B O   1 
HETATM 2962 O  O   . HOH P 5 .   ? -4.022  -5.176  23.242  1.00 45.64 ? 425 HOH B O   1 
HETATM 2963 O  O   . HOH P 5 .   ? 1.731   -1.903  2.025   1.00 36.45 ? 426 HOH B O   1 
HETATM 2964 O  O   . HOH P 5 .   ? -30.869 5.016   2.274   1.00 31.96 ? 427 HOH B O   1 
HETATM 2965 O  O   . HOH P 5 .   ? -1.372  4.124   7.556   1.00 47.04 ? 428 HOH B O   1 
HETATM 2966 O  O   . HOH P 5 .   ? -20.985 17.929  15.430  1.00 24.30 ? 429 HOH B O   1 
HETATM 2967 O  O   . HOH P 5 .   ? -7.991  13.371  5.047   1.00 34.31 ? 430 HOH B O   1 
HETATM 2968 O  O   . HOH P 5 .   ? -28.737 0.320   4.587   1.00 30.73 ? 431 HOH B O   1 
HETATM 2969 O  O   . HOH P 5 .   ? -32.720 4.754   6.354   1.00 28.14 ? 432 HOH B O   1 
HETATM 2970 O  O   . HOH P 5 .   ? -13.237 17.457  13.821  1.00 32.29 ? 433 HOH B O   1 
HETATM 2971 O  O   . HOH P 5 .   ? -0.868  -0.444  -1.389  1.00 30.39 ? 434 HOH B O   1 
HETATM 2972 O  O   . HOH P 5 .   ? 2.008   -3.175  16.000  1.00 33.82 ? 435 HOH B O   1 
HETATM 2973 O  O   . HOH P 5 .   ? -2.333  -12.655 13.233  1.00 29.29 ? 436 HOH B O   1 
HETATM 2974 O  O   . HOH P 5 .   ? -24.079 16.607  7.789   1.00 33.49 ? 437 HOH B O   1 
HETATM 2975 O  O   . HOH P 5 .   ? -11.084 16.853  14.061  1.00 34.15 ? 438 HOH B O   1 
HETATM 2976 O  O   . HOH P 5 .   ? -15.744 -10.233 17.766  1.00 19.17 ? 439 HOH B O   1 
HETATM 2977 O  O   . HOH P 5 .   ? -13.936 -12.245 18.301  1.00 34.76 ? 440 HOH B O   1 
HETATM 2978 O  O   . HOH Q 5 .   ? -34.438 5.959   35.776  1.00 20.41 ? 301 HOH C O   1 
HETATM 2979 O  O   . HOH Q 5 .   ? -7.413  5.412   24.410  1.00 34.47 ? 302 HOH C O   1 
HETATM 2980 O  O   . HOH Q 5 .   ? -40.943 -0.067  2.713   1.00 41.97 ? 303 HOH C O   1 
HETATM 2981 O  O   . HOH Q 5 .   ? -43.576 -12.024 0.549   1.00 21.81 ? 304 HOH C O   1 
HETATM 2982 O  O   . HOH Q 5 .   ? -39.882 3.674   26.576  1.00 29.05 ? 305 HOH C O   1 
HETATM 2983 O  O   . HOH Q 5 .   ? -50.405 -9.848  7.185   1.00 34.19 ? 306 HOH C O   1 
HETATM 2984 O  O   . HOH Q 5 .   ? -36.389 12.043  24.411  1.00 21.55 ? 307 HOH C O   1 
HETATM 2985 O  O   . HOH Q 5 .   ? -36.742 3.139   32.224  1.00 35.46 ? 308 HOH C O   1 
HETATM 2986 O  O   . HOH Q 5 .   ? -46.373 3.275   7.411   1.00 32.60 ? 309 HOH C O   1 
HETATM 2987 O  O   . HOH Q 5 .   ? -45.362 1.648   14.167  1.00 35.60 ? 310 HOH C O   1 
HETATM 2988 O  O   . HOH Q 5 .   ? -9.351  13.281  19.052  1.00 34.81 ? 311 HOH C O   1 
HETATM 2989 O  O   . HOH Q 5 .   ? -24.619 -3.177  17.172  1.00 18.51 ? 312 HOH C O   1 
HETATM 2990 O  O   . HOH Q 5 .   ? -16.749 -11.170 21.705  1.00 21.17 ? 313 HOH C O   1 
HETATM 2991 O  O   . HOH Q 5 .   ? -27.640 7.676   20.897  1.00 14.61 ? 314 HOH C O   1 
HETATM 2992 O  O   . HOH Q 5 .   ? -6.318  -0.917  20.659  1.00 21.19 ? 315 HOH C O   1 
HETATM 2993 O  O   . HOH Q 5 .   ? -43.608 8.811   19.352  1.00 26.21 ? 316 HOH C O   1 
HETATM 2994 O  O   . HOH Q 5 .   ? -43.111 4.480   24.522  1.00 27.14 ? 317 HOH C O   1 
HETATM 2995 O  O   . HOH Q 5 .   ? -3.965  6.504   20.999  1.00 34.59 ? 318 HOH C O   1 
HETATM 2996 O  O   . HOH Q 5 .   ? -26.425 4.887   32.614  1.00 26.75 ? 319 HOH C O   1 
HETATM 2997 O  O   . HOH Q 5 .   ? -5.797  2.316   23.602  1.00 26.54 ? 320 HOH C O   1 
HETATM 2998 O  O   . HOH Q 5 .   ? -7.180  4.336   26.481  1.00 44.48 ? 321 HOH C O   1 
HETATM 2999 O  O   . HOH Q 5 .   ? -31.164 4.367   8.579   1.00 15.43 ? 322 HOH C O   1 
HETATM 3000 O  O   . HOH Q 5 .   ? -28.542 -9.297  13.698  1.00 36.90 ? 323 HOH C O   1 
HETATM 3001 O  O   . HOH Q 5 .   ? -14.329 5.942   28.088  1.00 29.88 ? 324 HOH C O   1 
HETATM 3002 O  O   . HOH Q 5 .   ? -44.288 -6.670  6.077   1.00 35.72 ? 325 HOH C O   1 
HETATM 3003 O  O   . HOH Q 5 .   ? -7.118  -7.121  18.865  1.00 26.91 ? 326 HOH C O   1 
HETATM 3004 O  O   . HOH Q 5 .   ? -20.810 -12.535 20.162  1.00 15.40 ? 327 HOH C O   1 
HETATM 3005 O  O   . HOH Q 5 .   ? -45.318 -3.330  11.931  1.00 47.60 ? 328 HOH C O   1 
HETATM 3006 O  O   . HOH Q 5 .   ? -26.643 -5.242  32.350  1.00 30.65 ? 329 HOH C O   1 
HETATM 3007 O  O   . HOH Q 5 .   ? -31.674 -18.871 14.838  1.00 30.52 ? 330 HOH C O   1 
HETATM 3008 O  O   . HOH Q 5 .   ? -27.721 -14.846 14.601  1.00 21.98 ? 331 HOH C O   1 
HETATM 3009 O  O   . HOH Q 5 .   ? -44.388 -9.189  13.217  1.00 16.37 ? 332 HOH C O   1 
HETATM 3010 O  O   . HOH Q 5 .   ? -45.209 -0.911  11.970  1.00 46.33 ? 333 HOH C O   1 
HETATM 3011 O  O   . HOH Q 5 .   ? -39.285 -4.550  2.087   1.00 31.16 ? 334 HOH C O   1 
HETATM 3012 O  O   . HOH Q 5 .   ? -33.805 2.698   5.063   1.00 21.29 ? 335 HOH C O   1 
HETATM 3013 O  O   . HOH Q 5 .   ? -24.389 0.449   11.495  1.00 20.82 ? 336 HOH C O   1 
HETATM 3014 O  O   . HOH Q 5 .   ? -26.943 -5.466  13.139  1.00 26.22 ? 337 HOH C O   1 
HETATM 3015 O  O   . HOH Q 5 .   ? -43.535 14.086  18.119  1.00 17.54 ? 338 HOH C O   1 
HETATM 3016 O  O   . HOH Q 5 .   ? -4.103  6.874   18.039  1.00 32.41 ? 339 HOH C O   1 
HETATM 3017 O  O   . HOH Q 5 .   ? -42.845 15.163  13.725  1.00 28.24 ? 340 HOH C O   1 
HETATM 3018 O  O   . HOH Q 5 .   ? -40.193 -2.723  3.482   1.00 34.54 ? 341 HOH C O   1 
HETATM 3019 O  O   . HOH Q 5 .   ? -39.650 -3.042  26.793  1.00 20.56 ? 342 HOH C O   1 
HETATM 3020 O  O   . HOH Q 5 .   ? -19.351 -9.013  29.602  1.00 23.68 ? 343 HOH C O   1 
HETATM 3021 O  O   . HOH Q 5 .   ? -47.441 -5.230  12.416  1.00 31.33 ? 344 HOH C O   1 
HETATM 3022 O  O   . HOH Q 5 .   ? -15.819 -9.597  29.164  1.00 45.12 ? 345 HOH C O   1 
HETATM 3023 O  O   . HOH Q 5 .   ? -40.596 -7.643  19.239  1.00 16.95 ? 346 HOH C O   1 
HETATM 3024 O  O   . HOH Q 5 .   ? -35.801 -6.702  30.799  1.00 23.51 ? 347 HOH C O   1 
HETATM 3025 O  O   . HOH Q 5 .   ? -21.732 11.633  22.996  1.00 30.99 ? 348 HOH C O   1 
HETATM 3026 O  O   . HOH Q 5 .   ? -34.096 -0.016  30.488  1.00 23.56 ? 349 HOH C O   1 
HETATM 3027 O  O   . HOH Q 5 .   ? -36.094 4.528   4.291   1.00 33.63 ? 350 HOH C O   1 
HETATM 3028 O  O   . HOH Q 5 .   ? -15.079 -6.849  27.160  1.00 21.77 ? 351 HOH C O   1 
HETATM 3029 O  O   . HOH Q 5 .   ? -41.388 -16.962 14.177  1.00 21.68 ? 352 HOH C O   1 
HETATM 3030 O  O   . HOH Q 5 .   ? -37.839 -2.389  0.467   1.00 33.70 ? 353 HOH C O   1 
HETATM 3031 O  O   . HOH Q 5 .   ? -32.363 -11.908 33.009  1.00 23.24 ? 354 HOH C O   1 
HETATM 3032 O  O   . HOH Q 5 .   ? -23.362 10.480  32.299  1.00 31.83 ? 355 HOH C O   1 
HETATM 3033 O  O   . HOH Q 5 .   ? -37.198 5.989   27.462  1.00 27.22 ? 356 HOH C O   1 
HETATM 3034 O  O   . HOH Q 5 .   ? -45.207 -14.336 14.279  1.00 30.02 ? 357 HOH C O   1 
HETATM 3035 O  O   . HOH Q 5 .   ? -43.071 12.280  11.944  1.00 35.49 ? 358 HOH C O   1 
HETATM 3036 O  O   . HOH Q 5 .   ? -28.925 1.712   35.265  1.00 28.74 ? 359 HOH C O   1 
HETATM 3037 O  O   . HOH Q 5 .   ? -38.092 -0.400  30.646  1.00 35.97 ? 360 HOH C O   1 
HETATM 3038 O  O   . HOH Q 5 .   ? -32.203 -4.898  30.618  1.00 33.44 ? 361 HOH C O   1 
HETATM 3039 O  O   . HOH Q 5 .   ? -47.150 -8.019  15.578  1.00 36.35 ? 362 HOH C O   1 
HETATM 3040 O  O   . HOH Q 5 .   ? -43.240 -4.225  6.358   1.00 41.48 ? 363 HOH C O   1 
HETATM 3041 O  O   . HOH Q 5 .   ? -34.796 0.309   1.287   1.00 28.08 ? 364 HOH C O   1 
HETATM 3042 O  O   . HOH Q 5 .   ? -40.753 6.280   19.925  1.00 23.05 ? 365 HOH C O   1 
HETATM 3043 O  O   . HOH Q 5 .   ? -19.171 -11.725 22.211  1.00 17.87 ? 366 HOH C O   1 
HETATM 3044 O  O   . HOH Q 5 .   ? -25.643 -15.437 33.267  1.00 37.56 ? 367 HOH C O   1 
HETATM 3045 O  O   . HOH Q 5 .   ? -38.237 8.350   14.141  1.00 37.49 ? 368 HOH C O   1 
HETATM 3046 O  O   . HOH Q 5 .   ? -25.265 -9.153  13.810  1.00 8.16  ? 369 HOH C O   1 
HETATM 3047 O  O   . HOH Q 5 .   ? -42.592 5.139   4.742   1.00 25.61 ? 370 HOH C O   1 
HETATM 3048 O  O   . HOH Q 5 .   ? -43.246 -15.851 12.255  1.00 22.75 ? 371 HOH C O   1 
HETATM 3049 O  O   . HOH Q 5 .   ? -29.199 -2.286  5.900   1.00 25.80 ? 372 HOH C O   1 
HETATM 3050 O  O   . HOH Q 5 .   ? -49.270 -9.300  4.784   1.00 53.45 ? 373 HOH C O   1 
HETATM 3051 O  O   . HOH Q 5 .   ? -18.920 -6.157  32.400  1.00 25.76 ? 374 HOH C O   1 
HETATM 3052 O  O   . HOH Q 5 .   ? -37.228 12.212  27.362  1.00 13.24 ? 375 HOH C O   1 
HETATM 3053 O  O   . HOH Q 5 .   ? -31.140 0.265   2.473   1.00 22.87 ? 376 HOH C O   1 
HETATM 3054 O  O   . HOH Q 5 .   ? -45.614 -9.482  3.792   1.00 31.25 ? 377 HOH C O   1 
HETATM 3055 O  O   . HOH Q 5 .   ? -11.932 -5.388  27.427  1.00 21.03 ? 378 HOH C O   1 
HETATM 3056 O  O   . HOH Q 5 .   ? -30.876 -4.701  32.767  1.00 36.34 ? 379 HOH C O   1 
HETATM 3057 O  O   . HOH Q 5 .   ? -45.185 -14.593 9.629   1.00 29.11 ? 380 HOH C O   1 
HETATM 3058 O  O   . HOH Q 5 .   ? -36.086 8.819   16.000  1.00 21.90 ? 381 HOH C O   1 
HETATM 3059 O  O   . HOH Q 5 .   ? -39.409 -7.384  2.830   1.00 25.96 ? 382 HOH C O   1 
HETATM 3060 O  O   . HOH Q 5 .   ? -44.928 9.699   15.513  1.00 25.04 ? 383 HOH C O   1 
HETATM 3061 O  O   . HOH Q 5 .   ? -46.321 2.354   22.863  1.00 37.51 ? 384 HOH C O   1 
HETATM 3062 O  O   . HOH Q 5 .   ? -24.833 -11.991 32.682  1.00 14.96 ? 385 HOH C O   1 
HETATM 3063 O  O   . HOH Q 5 .   ? -43.443 -14.029 1.968   1.00 25.97 ? 386 HOH C O   1 
HETATM 3064 O  O   . HOH Q 5 .   ? -7.937  -7.832  21.856  1.00 43.61 ? 387 HOH C O   1 
HETATM 3065 O  O   . HOH Q 5 .   ? -8.617  -5.196  25.370  1.00 23.12 ? 388 HOH C O   1 
HETATM 3066 O  O   . HOH Q 5 .   ? -46.775 -12.091 18.673  1.00 46.64 ? 389 HOH C O   1 
HETATM 3067 O  O   . HOH Q 5 .   ? -22.410 -15.291 31.259  1.00 32.00 ? 390 HOH C O   1 
HETATM 3068 O  O   . HOH Q 5 .   ? -27.205 -18.631 30.596  1.00 26.56 ? 391 HOH C O   1 
HETATM 3069 O  O   . HOH Q 5 .   ? -17.275 -9.649  20.004  1.00 23.02 ? 392 HOH C O   1 
HETATM 3070 O  O   . HOH Q 5 .   ? -9.137  -10.030 18.705  1.00 18.59 ? 393 HOH C O   1 
HETATM 3071 O  O   . HOH Q 5 .   ? -44.413 -13.441 19.522  1.00 32.08 ? 394 HOH C O   1 
HETATM 3072 O  O   . HOH Q 5 .   ? -20.629 -7.859  32.663  1.00 33.22 ? 395 HOH C O   1 
HETATM 3073 O  O   . HOH Q 5 .   ? -27.259 -1.755  8.726   1.00 19.25 ? 396 HOH C O   1 
HETATM 3074 O  O   . HOH Q 5 .   ? -42.260 -2.246  25.993  1.00 28.48 ? 397 HOH C O   1 
HETATM 3075 O  O   . HOH Q 5 .   ? -41.583 -6.414  3.610   1.00 23.96 ? 398 HOH C O   1 
HETATM 3076 O  O   . HOH Q 5 .   ? -18.865 0.757   22.570  1.00 48.27 ? 399 HOH C O   1 
HETATM 3077 O  O   . HOH Q 5 .   ? -35.923 -8.886  32.658  1.00 28.51 ? 400 HOH C O   1 
HETATM 3078 O  O   . HOH Q 5 .   ? -43.265 -8.348  0.450   1.00 44.12 ? 401 HOH C O   1 
HETATM 3079 O  O   . HOH Q 5 .   ? -39.740 3.013   31.341  1.00 27.18 ? 402 HOH C O   1 
HETATM 3080 O  O   . HOH Q 5 .   ? -40.267 -5.203  28.514  1.00 38.53 ? 403 HOH C O   1 
HETATM 3081 O  O   . HOH Q 5 .   ? -29.595 -12.391 13.366  1.00 34.28 ? 404 HOH C O   1 
HETATM 3082 O  O   . HOH Q 5 .   ? -40.507 -8.637  0.248   1.00 30.08 ? 405 HOH C O   1 
HETATM 3083 O  O   . HOH Q 5 .   ? -20.000 -12.579 26.963  1.00 46.98 ? 406 HOH C O   1 
HETATM 3084 O  O   . HOH Q 5 .   ? -26.116 -4.215  10.915  1.00 27.94 ? 407 HOH C O   1 
HETATM 3085 O  O   . HOH Q 5 .   ? -23.154 -16.858 28.564  1.00 27.32 ? 408 HOH C O   1 
HETATM 3086 O  O   . HOH Q 5 .   ? -16.446 -12.532 23.819  1.00 31.61 ? 409 HOH C O   1 
HETATM 3087 O  O   . HOH Q 5 .   ? -15.209 -5.464  29.861  1.00 24.67 ? 410 HOH C O   1 
HETATM 3088 O  O   . HOH Q 5 .   ? -24.638 -8.202  35.795  1.00 36.43 ? 411 HOH C O   1 
HETATM 3089 O  O   . HOH Q 5 .   ? -35.058 -11.462 31.842  1.00 18.98 ? 412 HOH C O   1 
HETATM 3090 O  O   . HOH Q 5 .   ? -29.451 -9.110  34.258  1.00 29.73 ? 413 HOH C O   1 
HETATM 3091 O  O   . HOH Q 5 .   ? -26.778 -5.477  8.538   1.00 29.69 ? 414 HOH C O   1 
HETATM 3092 O  O   . HOH Q 5 .   ? -38.313 -5.303  30.189  1.00 19.91 ? 415 HOH C O   1 
HETATM 3093 O  O   . HOH Q 5 .   ? -28.352 -7.647  11.538  1.00 30.82 ? 416 HOH C O   1 
HETATM 3094 O  O   . HOH Q 5 .   ? -9.104  14.373  13.276  1.00 30.05 ? 417 HOH C O   1 
HETATM 3095 O  O   . HOH Q 5 .   ? -33.107 -1.780  0.681   1.00 32.60 ? 418 HOH C O   1 
HETATM 3096 O  O   . HOH Q 5 .   ? -23.179 -9.734  36.008  1.00 38.56 ? 419 HOH C O   1 
HETATM 3097 O  O   . HOH Q 5 .   ? -41.173 1.341   27.140  1.00 29.88 ? 420 HOH C O   1 
HETATM 3098 O  O   . HOH Q 5 .   ? -18.065 -8.497  31.404  1.00 60.86 ? 421 HOH C O   1 
HETATM 3099 O  O   . HOH Q 5 .   ? -27.112 13.173  28.013  1.00 29.88 ? 422 HOH C O   1 
HETATM 3100 O  O   . HOH Q 5 .   ? -9.952  9.069   24.515  1.00 29.88 ? 423 HOH C O   1 
HETATM 3101 O  O   . HOH Q 5 .   ? -33.691 2.342   2.285   1.00 31.44 ? 424 HOH C O   1 
HETATM 3102 O  O   . HOH Q 5 .   ? -46.676 -10.504 12.058  1.00 32.22 ? 425 HOH C O   1 
HETATM 3103 O  O   . HOH Q 5 .   ? -10.060 16.105  17.765  1.00 46.16 ? 426 HOH C O   1 
HETATM 3104 O  O   . HOH Q 5 .   ? -42.330 5.847   27.330  1.00 19.77 ? 427 HOH C O   1 
HETATM 3105 O  O   . HOH Q 5 .   ? -42.559 0.041   25.034  1.00 44.45 ? 428 HOH C O   1 
HETATM 3106 O  O   . HOH Q 5 .   ? -4.654  11.961  17.306  1.00 33.40 ? 429 HOH C O   1 
HETATM 3107 O  O   . HOH Q 5 .   ? -25.802 -10.874 35.379  1.00 33.43 ? 430 HOH C O   1 
HETATM 3108 O  O   . HOH Q 5 .   ? -45.019 -3.556  7.271   1.00 30.11 ? 431 HOH C O   1 
HETATM 3109 O  O   . HOH Q 5 .   ? -6.722  -6.833  23.921  1.00 39.67 ? 432 HOH C O   1 
HETATM 3110 O  O   . HOH Q 5 .   ? -44.701 1.864   24.992  1.00 36.77 ? 433 HOH C O   1 
HETATM 3111 O  O   . HOH Q 5 .   ? -45.235 -2.680  9.141   1.00 32.79 ? 434 HOH C O   1 
HETATM 3112 O  O   . HOH Q 5 .   ? -46.007 -8.936  21.912  1.00 31.84 ? 435 HOH C O   1 
HETATM 3113 O  O   . HOH Q 5 .   ? -25.586 -7.543  11.268  1.00 35.56 ? 436 HOH C O   1 
HETATM 3114 O  O   . HOH Q 5 .   ? -16.780 -13.113 20.144  1.00 31.38 ? 437 HOH C O   1 
HETATM 3115 O  O   . HOH Q 5 .   ? -18.915 -12.844 18.070  1.00 19.64 ? 438 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   ? 0.2272 0.1686 0.1636 -0.0789 0.0251  0.0207  1   PRO A N   
2    C  CA  . PRO A 1   ? 0.2256 0.1745 0.1651 -0.0484 0.0217  0.0314  1   PRO A CA  
3    C  C   . PRO A 1   ? 0.2186 0.1865 0.1587 -0.0382 0.0026  0.0377  1   PRO A C   
4    O  O   . PRO A 1   ? 0.2035 0.1952 0.1380 -0.0279 0.0028  0.0455  1   PRO A O   
5    C  CB  . PRO A 1   ? 0.2360 0.1791 0.1808 -0.0364 0.0178  0.0176  1   PRO A CB  
6    C  CG  . PRO A 1   ? 0.2217 0.1808 0.1810 -0.0700 0.0298  0.0227  1   PRO A CG  
7    C  CD  . PRO A 1   ? 0.2174 0.1655 0.1750 -0.0784 0.0410  0.0161  1   PRO A CD  
8    N  N   . MET A 2   ? 0.1954 0.1636 0.1697 -0.0387 0.0154  0.0374  2   MET A N   
9    C  CA  . MET A 2   ? 0.2021 0.1754 0.1915 -0.0397 0.0320  0.0450  2   MET A CA  
10   C  C   . MET A 2   ? 0.1856 0.1650 0.1649 -0.0339 0.0157  0.0250  2   MET A C   
11   O  O   . MET A 2   ? 0.1812 0.1740 0.1606 -0.0195 0.0116  0.0296  2   MET A O   
12   C  CB  . MET A 2   ? 0.2506 0.2228 0.2694 -0.0234 0.0554  0.0239  2   MET A CB  
13   C  CG  . MET A 2   ? 0.2958 0.2820 0.3425 -0.0190 0.0671  -0.0177 2   MET A CG  
14   S  SD  . MET A 2   ? 0.3341 0.3287 0.4062 -0.0166 0.0835  -0.0553 2   MET A SD  
15   C  CE  . MET A 2   ? 0.3342 0.3382 0.4190 -0.0155 0.0812  -0.0676 2   MET A CE  
16   N  N   . PHE A 3   ? 0.1791 0.1610 0.1334 -0.0286 0.0087  0.0088  3   PHE A N   
17   C  CA  . PHE A 3   ? 0.1883 0.1448 0.1309 -0.0342 0.0146  0.0014  3   PHE A CA  
18   C  C   . PHE A 3   ? 0.1873 0.1409 0.1368 -0.0362 0.0254  0.0081  3   PHE A C   
19   O  O   . PHE A 3   ? 0.1882 0.1488 0.1475 -0.0300 0.0178  0.0200  3   PHE A O   
20   C  CB  . PHE A 3   ? 0.1990 0.1543 0.1440 -0.0413 0.0157  -0.0166 3   PHE A CB  
21   C  CG  . PHE A 3   ? 0.2173 0.1757 0.1526 -0.0462 0.0064  -0.0239 3   PHE A CG  
22   C  CD1 . PHE A 3   ? 0.2379 0.1632 0.1670 -0.0545 0.0080  -0.0275 3   PHE A CD1 
23   C  CD2 . PHE A 3   ? 0.2124 0.2167 0.1574 -0.0675 -0.0024 -0.0119 3   PHE A CD2 
24   C  CE1 . PHE A 3   ? 0.2476 0.1977 0.1796 -0.0580 0.0059  -0.0258 3   PHE A CE1 
25   C  CE2 . PHE A 3   ? 0.2199 0.2423 0.1721 -0.0735 -0.0013 -0.0094 3   PHE A CE2 
26   C  CZ  . PHE A 3   ? 0.2426 0.2365 0.1842 -0.0733 0.0073  -0.0049 3   PHE A CZ  
27   N  N   . ILE A 4   ? 0.2038 0.1232 0.1027 -0.0472 0.0447  0.0125  4   ILE A N   
28   C  CA  . ILE A 4   ? 0.2147 0.1402 0.1008 -0.0340 0.0366  0.0134  4   ILE A CA  
29   C  C   . ILE A 4   ? 0.2038 0.1420 0.1156 -0.0365 0.0400  0.0187  4   ILE A C   
30   O  O   . ILE A 4   ? 0.1826 0.1383 0.1299 -0.0322 0.0322  0.0188  4   ILE A O   
31   C  CB  . ILE A 4   ? 0.2420 0.1565 0.1181 -0.0464 0.0357  -0.0102 4   ILE A CB  
32   C  CG1 . ILE A 4   ? 0.2817 0.1888 0.1268 -0.0327 0.0243  -0.0456 4   ILE A CG1 
33   C  CG2 . ILE A 4   ? 0.2412 0.1651 0.1497 -0.0346 0.0215  0.0030  4   ILE A CG2 
34   C  CD1 . ILE A 4   ? 0.3088 0.2273 0.1501 -0.0160 0.0093  -0.0510 4   ILE A CD1 
35   N  N   A VAL A 5   ? 0.2074 0.1436 0.1139 -0.0269 0.0533  0.0246  5   VAL A N   
36   N  N   B VAL A 5   ? 0.2071 0.1415 0.1093 -0.0265 0.0562  0.0269  5   VAL A N   
37   C  CA  A VAL A 5   ? 0.2178 0.1560 0.1271 -0.0227 0.0565  0.0203  5   VAL A CA  
38   C  CA  B VAL A 5   ? 0.2174 0.1535 0.1229 -0.0218 0.0588  0.0236  5   VAL A CA  
39   C  C   A VAL A 5   ? 0.1932 0.1245 0.1322 -0.0160 0.0389  0.0122  5   VAL A C   
40   C  C   B VAL A 5   ? 0.1913 0.1211 0.1280 -0.0127 0.0398  0.0133  5   VAL A C   
41   O  O   A VAL A 5   ? 0.1919 0.1267 0.1435 -0.0170 0.0262  0.0004  5   VAL A O   
42   O  O   B VAL A 5   ? 0.1974 0.1312 0.1459 -0.0222 0.0208  0.0061  5   VAL A O   
43   C  CB  A VAL A 5   ? 0.2524 0.2073 0.1421 -0.0267 0.0727  0.0012  5   VAL A CB  
44   C  CB  B VAL A 5   ? 0.2508 0.2021 0.1417 -0.0269 0.0706  -0.0009 5   VAL A CB  
45   C  CG1 A VAL A 5   ? 0.2697 0.2435 0.1453 -0.0243 0.0792  -0.0045 5   VAL A CG1 
46   C  CG1 B VAL A 5   ? 0.2713 0.2394 0.1550 -0.0257 0.0724  -0.0047 5   VAL A CG1 
47   C  CG2 A VAL A 5   ? 0.2634 0.2187 0.1522 -0.0264 0.0777  -0.0027 5   VAL A CG2 
48   C  CG2 B VAL A 5   ? 0.2582 0.2166 0.1465 -0.0311 0.0711  -0.0065 5   VAL A CG2 
49   N  N   . ASN A 6   ? 0.1756 0.1134 0.1272 -0.0214 0.0384  0.0038  6   ASN A N   
50   C  CA  . ASN A 6   ? 0.1760 0.1394 0.1317 -0.0331 0.0481  0.0078  6   ASN A CA  
51   C  C   . ASN A 6   ? 0.1784 0.1452 0.1223 -0.0063 0.0344  0.0225  6   ASN A C   
52   O  O   . ASN A 6   ? 0.1730 0.1554 0.1243 -0.0084 0.0297  0.0162  6   ASN A O   
53   C  CB  . ASN A 6   ? 0.1954 0.2044 0.1671 -0.0591 0.0611  -0.0131 6   ASN A CB  
54   C  CG  . ASN A 6   ? 0.2530 0.3010 0.2228 -0.0645 0.0316  -0.0561 6   ASN A CG  
55   O  OD1 . ASN A 6   ? 0.2354 0.3573 0.2577 -0.0597 0.0265  -0.0931 6   ASN A OD1 
56   N  ND2 . ASN A 6   ? 0.3087 0.3308 0.2224 -0.0937 0.0199  -0.0585 6   ASN A ND2 
57   N  N   . THR A 7   ? 0.1790 0.1404 0.1229 0.0104  0.0191  0.0197  7   THR A N   
58   C  CA  . THR A 7   ? 0.1986 0.1549 0.1339 0.0128  0.0171  0.0032  7   THR A CA  
59   C  C   . THR A 7   ? 0.2045 0.1474 0.1371 0.0035  0.0210  0.0123  7   THR A C   
60   O  O   . THR A 7   ? 0.2107 0.1231 0.1364 0.0056  0.0333  0.0215  7   THR A O   
61   C  CB  . THR A 7   ? 0.2046 0.1560 0.1297 0.0073  0.0204  -0.0086 7   THR A CB  
62   O  OG1 . THR A 7   ? 0.2099 0.1471 0.1128 0.0010  -0.0078 0.0065  7   THR A OG1 
63   C  CG2 . THR A 7   ? 0.1994 0.1742 0.1372 0.0134  0.0171  -0.0153 7   THR A CG2 
64   N  N   . ASN A 8   ? 0.2003 0.1373 0.1394 -0.0089 0.0153  0.0215  8   ASN A N   
65   C  CA  . ASN A 8   ? 0.2076 0.1545 0.1596 -0.0093 0.0187  0.0404  8   ASN A CA  
66   C  C   . ASN A 8   ? 0.2130 0.1746 0.1769 -0.0127 -0.0011 0.0345  8   ASN A C   
67   O  O   . ASN A 8   ? 0.2212 0.2004 0.2006 -0.0097 -0.0428 0.0405  8   ASN A O   
68   C  CB  . ASN A 8   ? 0.2040 0.1584 0.1617 0.0043  0.0453  0.0395  8   ASN A CB  
69   C  CG  . ASN A 8   ? 0.2205 0.1760 0.1798 0.0209  0.0401  0.0409  8   ASN A CG  
70   O  OD1 . ASN A 8   ? 0.2189 0.1741 0.1678 0.0163  0.0396  0.0347  8   ASN A OD1 
71   N  ND2 . ASN A 8   ? 0.2144 0.1836 0.2109 0.0270  0.0481  0.0409  8   ASN A ND2 
72   N  N   . VAL A 9   ? 0.1768 0.1696 0.1654 -0.0143 0.0132  0.0134  9   VAL A N   
73   C  CA  . VAL A 9   ? 0.1819 0.1957 0.1813 -0.0015 0.0043  -0.0087 9   VAL A CA  
74   C  C   . VAL A 9   ? 0.2019 0.2135 0.1701 0.0006  0.0194  -0.0009 9   VAL A C   
75   O  O   . VAL A 9   ? 0.2219 0.2240 0.1665 -0.0022 0.0265  -0.0197 9   VAL A O   
76   C  CB  . VAL A 9   ? 0.1591 0.2129 0.2054 0.0100  -0.0258 -0.0320 9   VAL A CB  
77   C  CG1 . VAL A 9   ? 0.1716 0.2619 0.2295 0.0137  -0.0229 -0.0320 9   VAL A CG1 
78   C  CG2 . VAL A 9   ? 0.1738 0.2139 0.2080 0.0147  -0.0237 -0.0494 9   VAL A CG2 
79   N  N   . PRO A 10  ? 0.2361 0.2324 0.1734 0.0183  0.0079  0.0289  10  PRO A N   
80   C  CA  . PRO A 10  ? 0.2494 0.2343 0.1922 0.0430  -0.0083 0.0400  10  PRO A CA  
81   C  C   . PRO A 10  ? 0.2483 0.2301 0.1993 0.0375  -0.0019 0.0285  10  PRO A C   
82   O  O   . PRO A 10  ? 0.2460 0.2396 0.1883 0.0048  0.0024  0.0036  10  PRO A O   
83   C  CB  . PRO A 10  ? 0.2734 0.2486 0.1951 0.0466  -0.0127 0.0500  10  PRO A CB  
84   C  CG  . PRO A 10  ? 0.2856 0.2658 0.1924 0.0383  -0.0128 0.0474  10  PRO A CG  
85   C  CD  . PRO A 10  ? 0.2610 0.2500 0.1725 0.0224  -0.0048 0.0411  10  PRO A CD  
86   N  N   . ARG A 11  ? 0.2582 0.2294 0.2144 0.0428  -0.0161 0.0213  11  ARG A N   
87   C  CA  . ARG A 11  ? 0.2686 0.2422 0.2413 0.0138  -0.0165 0.0177  11  ARG A CA  
88   C  C   . ARG A 11  ? 0.2819 0.2625 0.2559 0.0068  -0.0361 0.0206  11  ARG A C   
89   O  O   . ARG A 11  ? 0.2646 0.2576 0.2668 0.0027  -0.0354 0.0187  11  ARG A O   
90   C  CB  . ARG A 11  ? 0.2828 0.2590 0.2695 -0.0169 0.0022  0.0092  11  ARG A CB  
91   C  CG  . ARG A 11  ? 0.3082 0.2930 0.3037 -0.0349 0.0038  0.0091  11  ARG A CG  
92   C  CD  . ARG A 11  ? 0.3395 0.3297 0.3398 -0.0457 -0.0008 0.0025  11  ARG A CD  
93   N  NE  . ARG A 11  ? 0.3765 0.3731 0.3713 -0.0411 -0.0092 0.0036  11  ARG A NE  
94   C  CZ  . ARG A 11  ? 0.3960 0.4004 0.3893 -0.0439 -0.0070 0.0007  11  ARG A CZ  
95   N  NH1 . ARG A 11  ? 0.4101 0.4139 0.4004 -0.0324 -0.0032 -0.0004 11  ARG A NH1 
96   N  NH2 . ARG A 11  ? 0.3955 0.4051 0.3931 -0.0558 -0.0125 0.0027  11  ARG A NH2 
97   N  N   . ALA A 12  ? 0.2996 0.2792 0.2480 0.0063  -0.0436 0.0196  12  ALA A N   
98   C  CA  . ALA A 12  ? 0.3203 0.3042 0.2537 0.0044  -0.0510 0.0120  12  ALA A CA  
99   C  C   . ALA A 12  ? 0.3280 0.3082 0.2516 -0.0181 -0.0519 0.0047  12  ALA A C   
100  O  O   . ALA A 12  ? 0.3405 0.3315 0.2717 -0.0334 -0.0533 -0.0073 12  ALA A O   
101  C  CB  . ALA A 12  ? 0.3246 0.3093 0.2553 0.0182  -0.0505 0.0098  12  ALA A CB  
102  N  N   . SER A 13  ? 0.3168 0.2900 0.2376 -0.0184 -0.0362 0.0190  13  SER A N   
103  C  CA  . SER A 13  ? 0.3275 0.2811 0.2401 -0.0271 -0.0218 0.0151  13  SER A CA  
104  C  C   . SER A 13  ? 0.3327 0.2548 0.2413 -0.0287 0.0033  0.0074  13  SER A C   
105  O  O   . SER A 13  ? 0.3658 0.2474 0.2530 -0.0183 0.0217  0.0080  13  SER A O   
106  C  CB  . SER A 13  ? 0.3450 0.3022 0.2534 -0.0349 -0.0154 0.0135  13  SER A CB  
107  O  OG  . SER A 13  ? 0.3599 0.3327 0.2792 -0.0391 -0.0135 0.0165  13  SER A OG  
108  N  N   . VAL A 14  ? 0.3011 0.2328 0.2248 -0.0454 -0.0027 0.0010  14  VAL A N   
109  C  CA  . VAL A 14  ? 0.2891 0.2221 0.2163 -0.0521 -0.0112 -0.0074 14  VAL A CA  
110  C  C   . VAL A 14  ? 0.2786 0.2356 0.2170 -0.0581 -0.0061 -0.0182 14  VAL A C   
111  O  O   . VAL A 14  ? 0.2680 0.2536 0.2239 -0.0708 -0.0094 -0.0099 14  VAL A O   
112  C  CB  . VAL A 14  ? 0.2868 0.2068 0.2236 -0.0540 -0.0239 -0.0083 14  VAL A CB  
113  C  CG1 . VAL A 14  ? 0.2876 0.1940 0.2271 -0.0501 -0.0355 -0.0023 14  VAL A CG1 
114  C  CG2 . VAL A 14  ? 0.2946 0.2250 0.2315 -0.0457 -0.0245 -0.0049 14  VAL A CG2 
115  N  N   . PRO A 15  ? 0.2725 0.2380 0.2157 -0.0466 -0.0120 -0.0224 15  PRO A N   
116  C  CA  . PRO A 15  ? 0.2592 0.2265 0.2107 -0.0478 -0.0163 -0.0208 15  PRO A CA  
117  C  C   . PRO A 15  ? 0.2389 0.2111 0.2003 -0.0571 -0.0225 0.0025  15  PRO A C   
118  O  O   . PRO A 15  ? 0.2378 0.2221 0.2001 -0.0381 -0.0468 0.0001  15  PRO A O   
119  C  CB  . PRO A 15  ? 0.2780 0.2395 0.2155 -0.0316 -0.0303 -0.0300 15  PRO A CB  
120  C  CG  . PRO A 15  ? 0.2828 0.2434 0.2254 -0.0387 -0.0331 -0.0312 15  PRO A CG  
121  C  CD  . PRO A 15  ? 0.2788 0.2386 0.2170 -0.0419 -0.0255 -0.0293 15  PRO A CD  
122  N  N   . ASP A 16  ? 0.2372 0.1980 0.2009 -0.0644 -0.0228 0.0205  16  ASP A N   
123  C  CA  . ASP A 16  ? 0.2493 0.1853 0.2151 -0.0760 -0.0368 0.0258  16  ASP A CA  
124  C  C   . ASP A 16  ? 0.2526 0.1860 0.2227 -0.0516 -0.0314 0.0141  16  ASP A C   
125  O  O   . ASP A 16  ? 0.2598 0.2020 0.2403 -0.0605 -0.0315 -0.0004 16  ASP A O   
126  C  CB  . ASP A 16  ? 0.2716 0.1922 0.2270 -0.0677 -0.0504 0.0356  16  ASP A CB  
127  C  CG  . ASP A 16  ? 0.2943 0.1929 0.2350 -0.0614 -0.0696 0.0246  16  ASP A CG  
128  O  OD1 . ASP A 16  ? 0.3123 0.2076 0.2558 -0.0521 -0.0785 0.0236  16  ASP A OD1 
129  O  OD2 . ASP A 16  ? 0.3070 0.2001 0.2308 -0.0644 -0.0561 0.0362  16  ASP A OD2 
130  N  N   . GLY A 17  ? 0.2445 0.1723 0.2028 -0.0242 -0.0230 0.0196  17  GLY A N   
131  C  CA  . GLY A 17  ? 0.2373 0.1577 0.1953 -0.0241 -0.0401 0.0207  17  GLY A CA  
132  C  C   . GLY A 17  ? 0.2367 0.1686 0.1794 -0.0285 -0.0444 0.0233  17  GLY A C   
133  O  O   . GLY A 17  ? 0.2598 0.1672 0.1866 -0.0350 -0.0516 0.0256  17  GLY A O   
134  N  N   . PHE A 18  ? 0.2243 0.1915 0.1617 -0.0350 -0.0290 0.0101  18  PHE A N   
135  C  CA  . PHE A 18  ? 0.2183 0.2043 0.1622 -0.0430 -0.0324 0.0117  18  PHE A CA  
136  C  C   . PHE A 18  ? 0.2292 0.1842 0.1737 -0.0445 -0.0327 0.0123  18  PHE A C   
137  O  O   . PHE A 18  ? 0.2335 0.1878 0.1790 -0.0306 -0.0266 0.0095  18  PHE A O   
138  C  CB  . PHE A 18  ? 0.2123 0.2357 0.1603 -0.0471 -0.0232 0.0100  18  PHE A CB  
139  C  CG  . PHE A 18  ? 0.2127 0.2584 0.1571 -0.0464 -0.0197 0.0154  18  PHE A CG  
140  C  CD1 . PHE A 18  ? 0.2297 0.2918 0.1619 -0.0424 -0.0101 0.0266  18  PHE A CD1 
141  C  CD2 . PHE A 18  ? 0.2358 0.2647 0.1729 -0.0525 -0.0038 0.0200  18  PHE A CD2 
142  C  CE1 . PHE A 18  ? 0.2445 0.3036 0.1695 -0.0335 0.0026  0.0256  18  PHE A CE1 
143  C  CE2 . PHE A 18  ? 0.2377 0.2687 0.1720 -0.0390 -0.0064 0.0230  18  PHE A CE2 
144  C  CZ  . PHE A 18  ? 0.2432 0.2894 0.1705 -0.0360 0.0068  0.0247  18  PHE A CZ  
145  N  N   . LEU A 19  ? 0.2392 0.1725 0.1653 -0.0595 -0.0246 0.0086  19  LEU A N   
146  C  CA  . LEU A 19  ? 0.2466 0.1663 0.1701 -0.0564 -0.0307 0.0064  19  LEU A CA  
147  C  C   . LEU A 19  ? 0.2239 0.1652 0.1809 -0.0518 -0.0339 0.0001  19  LEU A C   
148  O  O   . LEU A 19  ? 0.2222 0.1705 0.1850 -0.0388 -0.0342 -0.0120 19  LEU A O   
149  C  CB  . LEU A 19  ? 0.2838 0.1689 0.1865 -0.0616 -0.0244 -0.0052 19  LEU A CB  
150  C  CG  . LEU A 19  ? 0.3081 0.1824 0.2050 -0.0667 -0.0305 -0.0253 19  LEU A CG  
151  C  CD1 . LEU A 19  ? 0.3243 0.1927 0.2081 -0.0534 -0.0163 -0.0441 19  LEU A CD1 
152  C  CD2 . LEU A 19  ? 0.3186 0.2063 0.2243 -0.0826 -0.0400 -0.0065 19  LEU A CD2 
153  N  N   . SER A 20  ? 0.2155 0.1650 0.1886 -0.0670 -0.0363 -0.0044 20  SER A N   
154  C  CA  . SER A 20  ? 0.2235 0.1644 0.1961 -0.0652 -0.0496 -0.0024 20  SER A CA  
155  C  C   . SER A 20  ? 0.2356 0.1602 0.1707 -0.0538 -0.0530 0.0058  20  SER A C   
156  O  O   . SER A 20  ? 0.2611 0.1567 0.1844 -0.0595 -0.0437 0.0057  20  SER A O   
157  C  CB  . SER A 20  ? 0.2256 0.1604 0.2127 -0.0716 -0.0445 -0.0013 20  SER A CB  
158  O  OG  . SER A 20  ? 0.2559 0.1814 0.2292 -0.0642 -0.0366 0.0102  20  SER A OG  
159  N  N   . GLU A 21  ? 0.2390 0.1668 0.1557 -0.0466 -0.0412 -0.0058 21  GLU A N   
160  C  CA  . GLU A 21  ? 0.2435 0.1580 0.1386 -0.0334 -0.0357 -0.0005 21  GLU A CA  
161  C  C   . GLU A 21  ? 0.2450 0.1509 0.1334 -0.0339 -0.0391 -0.0014 21  GLU A C   
162  O  O   . GLU A 21  ? 0.2547 0.1466 0.1398 -0.0285 -0.0448 -0.0063 21  GLU A O   
163  C  CB  . GLU A 21  ? 0.2549 0.1809 0.1375 -0.0221 -0.0188 0.0001  21  GLU A CB  
164  C  CG  . GLU A 21  ? 0.2664 0.2385 0.1524 -0.0243 -0.0010 -0.0063 21  GLU A CG  
165  C  CD  . GLU A 21  ? 0.2771 0.2764 0.1661 -0.0410 -0.0147 -0.0219 21  GLU A CD  
166  O  OE1 . GLU A 21  ? 0.2911 0.3043 0.1759 -0.0578 -0.0001 -0.0344 21  GLU A OE1 
167  O  OE2 . GLU A 21  ? 0.2884 0.3130 0.1834 -0.0392 -0.0259 -0.0329 21  GLU A OE2 
168  N  N   . LEU A 22  ? 0.2422 0.1543 0.1215 -0.0448 -0.0319 -0.0116 22  LEU A N   
169  C  CA  . LEU A 22  ? 0.2333 0.1659 0.1263 -0.0526 -0.0211 0.0033  22  LEU A CA  
170  C  C   . LEU A 22  ? 0.2468 0.1674 0.1252 -0.0640 -0.0155 -0.0058 22  LEU A C   
171  O  O   . LEU A 22  ? 0.2548 0.1742 0.1353 -0.0583 -0.0247 -0.0095 22  LEU A O   
172  C  CB  . LEU A 22  ? 0.2129 0.1935 0.1401 -0.0550 -0.0122 0.0087  22  LEU A CB  
173  C  CG  . LEU A 22  ? 0.1872 0.2155 0.1624 -0.0717 -0.0008 0.0312  22  LEU A CG  
174  C  CD1 . LEU A 22  ? 0.2066 0.2071 0.1714 -0.0762 -0.0103 0.0430  22  LEU A CD1 
175  C  CD2 . LEU A 22  ? 0.1893 0.2579 0.1758 -0.0714 0.0169  0.0359  22  LEU A CD2 
176  N  N   . THR A 23  ? 0.2507 0.1599 0.1184 -0.0715 -0.0124 -0.0081 23  THR A N   
177  C  CA  . THR A 23  ? 0.2631 0.1577 0.1248 -0.0897 -0.0114 0.0117  23  THR A CA  
178  C  C   . THR A 23  ? 0.2857 0.1750 0.1307 -0.0788 -0.0184 0.0278  23  THR A C   
179  O  O   . THR A 23  ? 0.2957 0.1869 0.1274 -0.0817 -0.0112 0.0390  23  THR A O   
180  C  CB  . THR A 23  ? 0.2655 0.1873 0.1291 -0.0739 -0.0149 0.0017  23  THR A CB  
181  O  OG1 . THR A 23  ? 0.2421 0.1864 0.1261 -0.0544 -0.0120 -0.0114 23  THR A OG1 
182  C  CG2 . THR A 23  ? 0.2838 0.2092 0.1407 -0.0675 -0.0083 0.0151  23  THR A CG2 
183  N  N   . GLN A 24  ? 0.2955 0.1945 0.1518 -0.0693 -0.0251 0.0245  24  GLN A N   
184  C  CA  . GLN A 24  ? 0.3134 0.2140 0.1798 -0.0515 -0.0428 0.0135  24  GLN A CA  
185  C  C   . GLN A 24  ? 0.3058 0.1910 0.1647 -0.0571 -0.0463 0.0032  24  GLN A C   
186  O  O   . GLN A 24  ? 0.3095 0.1781 0.1626 -0.0581 -0.0459 0.0125  24  GLN A O   
187  C  CB  . GLN A 24  ? 0.3392 0.2605 0.2281 -0.0375 -0.0361 0.0044  24  GLN A CB  
188  C  CG  . GLN A 24  ? 0.3543 0.3129 0.2800 -0.0184 -0.0239 0.0027  24  GLN A CG  
189  C  CD  . GLN A 24  ? 0.3632 0.3331 0.3233 -0.0028 -0.0216 0.0032  24  GLN A CD  
190  O  OE1 . GLN A 24  ? 0.3584 0.3240 0.3316 0.0002  -0.0324 -0.0058 24  GLN A OE1 
191  N  NE2 . GLN A 24  ? 0.3675 0.3386 0.3348 -0.0076 -0.0163 0.0104  24  GLN A NE2 
192  N  N   . GLN A 25  ? 0.2891 0.1851 0.1505 -0.0482 -0.0625 -0.0004 25  GLN A N   
193  C  CA  . GLN A 25  ? 0.2945 0.1949 0.1511 -0.0330 -0.0539 -0.0023 25  GLN A CA  
194  C  C   . GLN A 25  ? 0.2815 0.1765 0.1599 -0.0426 -0.0361 0.0163  25  GLN A C   
195  O  O   . GLN A 25  ? 0.2733 0.1631 0.1700 -0.0414 -0.0147 0.0272  25  GLN A O   
196  C  CB  . GLN A 25  ? 0.3120 0.2376 0.1549 -0.0093 -0.0678 -0.0175 25  GLN A CB  
197  C  CG  . GLN A 25  ? 0.3401 0.2667 0.1715 0.0134  -0.0735 -0.0391 25  GLN A CG  
198  C  CD  . GLN A 25  ? 0.3678 0.3081 0.2020 0.0486  -0.0776 -0.0358 25  GLN A CD  
199  O  OE1 . GLN A 25  ? 0.3916 0.3333 0.2171 0.0546  -0.0682 -0.0285 25  GLN A OE1 
200  N  NE2 . GLN A 25  ? 0.3656 0.3161 0.2092 0.0642  -0.0891 -0.0368 25  GLN A NE2 
201  N  N   . LEU A 26  ? 0.2688 0.1715 0.1550 -0.0445 -0.0452 0.0083  26  LEU A N   
202  C  CA  . LEU A 26  ? 0.2555 0.1638 0.1456 -0.0609 -0.0411 0.0132  26  LEU A CA  
203  C  C   . LEU A 26  ? 0.2679 0.1884 0.1631 -0.0714 -0.0397 0.0259  26  LEU A C   
204  O  O   . LEU A 26  ? 0.2800 0.1896 0.1683 -0.0820 -0.0404 0.0343  26  LEU A O   
205  C  CB  . LEU A 26  ? 0.2456 0.1678 0.1412 -0.0691 -0.0303 0.0080  26  LEU A CB  
206  C  CG  . LEU A 26  ? 0.2596 0.1829 0.1599 -0.0733 -0.0212 0.0029  26  LEU A CG  
207  C  CD1 . LEU A 26  ? 0.2838 0.1812 0.1705 -0.0724 -0.0182 -0.0123 26  LEU A CD1 
208  C  CD2 . LEU A 26  ? 0.2664 0.2198 0.1627 -0.0710 -0.0169 0.0109  26  LEU A CD2 
209  N  N   . ALA A 27  ? 0.2800 0.2038 0.1778 -0.0843 -0.0365 0.0332  27  ALA A N   
210  C  CA  . ALA A 27  ? 0.2907 0.2125 0.1850 -0.0776 -0.0441 0.0504  27  ALA A CA  
211  C  C   . ALA A 27  ? 0.3226 0.2069 0.1903 -0.0903 -0.0575 0.0403  27  ALA A C   
212  O  O   . ALA A 27  ? 0.3366 0.2083 0.2035 -0.0856 -0.0615 0.0626  27  ALA A O   
213  C  CB  . ALA A 27  ? 0.2789 0.2081 0.1972 -0.0668 -0.0426 0.0564  27  ALA A CB  
214  N  N   . GLN A 28  ? 0.3542 0.2161 0.1988 -0.0828 -0.0478 0.0171  28  GLN A N   
215  C  CA  . GLN A 28  ? 0.3818 0.2260 0.2109 -0.0703 -0.0489 -0.0041 28  GLN A CA  
216  C  C   . GLN A 28  ? 0.3940 0.1989 0.1895 -0.0678 -0.0557 -0.0087 28  GLN A C   
217  O  O   . GLN A 28  ? 0.4168 0.1896 0.2035 -0.0647 -0.0531 -0.0114 28  GLN A O   
218  C  CB  . GLN A 28  ? 0.3961 0.2617 0.2530 -0.0602 -0.0496 -0.0263 28  GLN A CB  
219  C  CG  . GLN A 28  ? 0.4227 0.3001 0.2964 -0.0360 -0.0468 -0.0347 28  GLN A CG  
220  C  CD  . GLN A 28  ? 0.4465 0.3357 0.3348 -0.0215 -0.0378 -0.0423 28  GLN A CD  
221  O  OE1 . GLN A 28  ? 0.4711 0.3531 0.3599 -0.0276 -0.0323 -0.0308 28  GLN A OE1 
222  N  NE2 . GLN A 28  ? 0.4273 0.3270 0.3339 -0.0101 -0.0468 -0.0710 28  GLN A NE2 
223  N  N   . ALA A 29  ? 0.3754 0.1828 0.1630 -0.0801 -0.0602 -0.0033 29  ALA A N   
224  C  CA  . ALA A 29  ? 0.3763 0.1921 0.1633 -0.0683 -0.0519 0.0145  29  ALA A CA  
225  C  C   . ALA A 29  ? 0.3533 0.1926 0.1693 -0.0636 -0.0557 0.0237  29  ALA A C   
226  O  O   . ALA A 29  ? 0.3451 0.1938 0.1876 -0.0465 -0.0533 0.0290  29  ALA A O   
227  C  CB  . ALA A 29  ? 0.3913 0.1965 0.1622 -0.0735 -0.0511 0.0219  29  ALA A CB  
228  N  N   . THR A 30  ? 0.3495 0.1986 0.1519 -0.0728 -0.0706 0.0160  30  THR A N   
229  C  CA  . THR A 30  ? 0.3407 0.1943 0.1542 -0.0576 -0.0856 0.0177  30  THR A CA  
230  C  C   . THR A 30  ? 0.3315 0.2007 0.1559 -0.0439 -0.0890 0.0212  30  THR A C   
231  O  O   . THR A 30  ? 0.3406 0.2113 0.1482 -0.0277 -0.0886 0.0368  30  THR A O   
232  C  CB  . THR A 30  ? 0.3452 0.1967 0.1740 -0.0577 -0.0763 0.0202  30  THR A CB  
233  O  OG1 . THR A 30  ? 0.3297 0.1838 0.1629 -0.0494 -0.0633 0.0340  30  THR A OG1 
234  C  CG2 . THR A 30  ? 0.3440 0.2065 0.1839 -0.0625 -0.0794 0.0169  30  THR A CG2 
235  N  N   . GLY A 31  ? 0.3182 0.1960 0.1746 -0.0417 -0.0609 0.0216  31  GLY A N   
236  C  CA  . GLY A 31  ? 0.3119 0.1935 0.1756 -0.0517 -0.0401 0.0253  31  GLY A CA  
237  C  C   . GLY A 31  ? 0.3241 0.2212 0.1837 -0.0365 -0.0382 0.0191  31  GLY A C   
238  O  O   . GLY A 31  ? 0.3476 0.2426 0.2055 -0.0286 -0.0213 0.0256  31  GLY A O   
239  N  N   . LYS A 32  ? 0.3026 0.2194 0.1777 -0.0259 -0.0422 0.0171  32  LYS A N   
240  C  CA  . LYS A 32  ? 0.2970 0.2128 0.1697 -0.0254 -0.0551 0.0123  32  LYS A CA  
241  C  C   . LYS A 32  ? 0.3011 0.1851 0.1534 -0.0330 -0.0617 0.0211  32  LYS A C   
242  O  O   . LYS A 32  ? 0.3065 0.1736 0.1353 -0.0379 -0.0644 0.0072  32  LYS A O   
243  C  CB  . LYS A 32  ? 0.2791 0.2404 0.1796 -0.0208 -0.0675 0.0075  32  LYS A CB  
244  C  CG  . LYS A 32  ? 0.2737 0.2795 0.1881 -0.0041 -0.0563 0.0146  32  LYS A CG  
245  C  CD  . LYS A 32  ? 0.2784 0.3096 0.1886 -0.0013 -0.0391 0.0245  32  LYS A CD  
246  C  CE  . LYS A 32  ? 0.2832 0.3290 0.1906 -0.0041 -0.0243 0.0354  32  LYS A CE  
247  N  NZ  . LYS A 32  ? 0.2769 0.3306 0.1880 -0.0080 -0.0100 0.0465  32  LYS A NZ  
248  N  N   . PRO A 33  ? 0.3056 0.1746 0.1465 -0.0346 -0.0534 0.0307  33  PRO A N   
249  C  CA  . PRO A 33  ? 0.3108 0.1778 0.1532 -0.0579 -0.0416 0.0152  33  PRO A CA  
250  C  C   . PRO A 33  ? 0.2985 0.1647 0.1430 -0.0605 -0.0444 0.0158  33  PRO A C   
251  O  O   . PRO A 33  ? 0.2957 0.1631 0.1277 -0.0367 -0.0277 0.0136  33  PRO A O   
252  C  CB  . PRO A 33  ? 0.3247 0.2002 0.1626 -0.0503 -0.0367 0.0217  33  PRO A CB  
253  C  CG  . PRO A 33  ? 0.3254 0.2055 0.1775 -0.0471 -0.0314 0.0392  33  PRO A CG  
254  C  CD  . PRO A 33  ? 0.3175 0.1935 0.1622 -0.0404 -0.0383 0.0477  33  PRO A CD  
255  N  N   . PRO A 34  ? 0.2878 0.1517 0.1566 -0.0742 -0.0821 0.0061  34  PRO A N   
256  C  CA  . PRO A 34  ? 0.2805 0.1497 0.1605 -0.0557 -0.0766 0.0066  34  PRO A CA  
257  C  C   . PRO A 34  ? 0.2645 0.1476 0.1634 -0.0757 -0.0533 0.0171  34  PRO A C   
258  O  O   . PRO A 34  ? 0.2658 0.1280 0.1539 -0.0910 -0.0524 0.0272  34  PRO A O   
259  C  CB  . PRO A 34  ? 0.3043 0.1722 0.1806 -0.0614 -0.0768 -0.0021 34  PRO A CB  
260  C  CG  . PRO A 34  ? 0.3033 0.1861 0.1862 -0.0644 -0.0825 0.0023  34  PRO A CG  
261  C  CD  . PRO A 34  ? 0.2786 0.1685 0.1724 -0.0750 -0.0964 -0.0028 34  PRO A CD  
262  N  N   . GLN A 35  ? 0.2555 0.1805 0.1720 -0.0770 -0.0352 0.0188  35  GLN A N   
263  C  CA  . GLN A 35  ? 0.2618 0.2110 0.1798 -0.1030 -0.0262 0.0191  35  GLN A CA  
264  C  C   . GLN A 35  ? 0.2580 0.2047 0.1594 -0.1102 -0.0087 0.0289  35  GLN A C   
265  O  O   . GLN A 35  ? 0.2811 0.2199 0.1695 -0.0868 -0.0241 0.0138  35  GLN A O   
266  C  CB  . GLN A 35  ? 0.2771 0.2465 0.2017 -0.1023 -0.0396 0.0318  35  GLN A CB  
267  C  CG  . GLN A 35  ? 0.2888 0.2809 0.2287 -0.0979 -0.0607 0.0409  35  GLN A CG  
268  C  CD  . GLN A 35  ? 0.2921 0.2806 0.2480 -0.1275 -0.0646 0.0591  35  GLN A CD  
269  O  OE1 . GLN A 35  ? 0.2716 0.2620 0.2381 -0.1367 -0.0622 0.0761  35  GLN A OE1 
270  N  NE2 . GLN A 35  ? 0.3126 0.2972 0.2743 -0.1276 -0.0562 0.0540  35  GLN A NE2 
271  N  N   . TYR A 36  ? 0.2442 0.1917 0.1381 -0.1154 0.0063  0.0313  36  TYR A N   
272  C  CA  . TYR A 36  ? 0.2348 0.1942 0.1313 -0.1059 0.0083  0.0249  36  TYR A CA  
273  C  C   . TYR A 36  ? 0.2265 0.1790 0.1066 -0.0922 0.0130  0.0036  36  TYR A C   
274  O  O   . TYR A 36  ? 0.2348 0.2056 0.1020 -0.0968 -0.0038 -0.0055 36  TYR A O   
275  C  CB  . TYR A 36  ? 0.2421 0.2080 0.1383 -0.1069 0.0132  0.0410  36  TYR A CB  
276  C  CG  . TYR A 36  ? 0.2569 0.2334 0.1619 -0.1130 0.0243  0.0511  36  TYR A CG  
277  C  CD1 . TYR A 36  ? 0.2718 0.2413 0.1783 -0.1133 0.0302  0.0591  36  TYR A CD1 
278  C  CD2 . TYR A 36  ? 0.2709 0.2558 0.1699 -0.1172 0.0364  0.0430  36  TYR A CD2 
279  C  CE1 . TYR A 36  ? 0.2831 0.2553 0.1931 -0.1252 0.0362  0.0543  36  TYR A CE1 
280  C  CE2 . TYR A 36  ? 0.2961 0.2645 0.1894 -0.1235 0.0491  0.0485  36  TYR A CE2 
281  C  CZ  . TYR A 36  ? 0.2942 0.2738 0.2080 -0.1228 0.0581  0.0540  36  TYR A CZ  
282  O  OH  . TYR A 36  ? 0.3121 0.3125 0.2401 -0.1208 0.0709  0.0535  36  TYR A OH  
283  N  N   . ILE A 37  ? 0.2226 0.1570 0.0919 -0.0498 0.0192  0.0044  37  ILE A N   
284  C  CA  . ILE A 37  ? 0.2295 0.1542 0.0907 -0.0382 0.0300  -0.0019 37  ILE A CA  
285  C  C   . ILE A 37  ? 0.1939 0.1609 0.1101 -0.0426 0.0034  0.0052  37  ILE A C   
286  O  O   . ILE A 37  ? 0.2197 0.1789 0.1300 -0.0360 0.0001  -0.0134 37  ILE A O   
287  C  CB  . ILE A 37  ? 0.2775 0.1470 0.0964 -0.0499 0.0257  0.0027  37  ILE A CB  
288  C  CG1 . ILE A 37  ? 0.3101 0.1645 0.1411 -0.0551 0.0351  0.0250  37  ILE A CG1 
289  C  CG2 . ILE A 37  ? 0.2841 0.1572 0.0995 -0.0508 0.0276  0.0106  37  ILE A CG2 
290  C  CD1 . ILE A 37  ? 0.3334 0.1843 0.1588 -0.0450 0.0344  0.0322  37  ILE A CD1 
291  N  N   . ALA A 38  ? 0.1766 0.1532 0.1047 -0.0521 -0.0023 0.0107  38  ALA A N   
292  C  CA  . ALA A 38  ? 0.1857 0.1573 0.0998 -0.0395 0.0181  0.0091  38  ALA A CA  
293  C  C   . ALA A 38  ? 0.1855 0.1639 0.1143 -0.0335 0.0053  0.0114  38  ALA A C   
294  O  O   . ALA A 38  ? 0.1803 0.1729 0.1233 -0.0485 0.0151  -0.0022 38  ALA A O   
295  C  CB  . ALA A 38  ? 0.1944 0.1712 0.0957 -0.0369 0.0040  -0.0036 38  ALA A CB  
296  N  N   . VAL A 39  ? 0.1963 0.1367 0.1133 -0.0316 -0.0073 0.0239  39  VAL A N   
297  C  CA  . VAL A 39  ? 0.2051 0.1372 0.1220 -0.0273 -0.0028 0.0152  39  VAL A CA  
298  C  C   . VAL A 39  ? 0.1789 0.1516 0.1301 -0.0317 0.0064  0.0096  39  VAL A C   
299  O  O   . VAL A 39  ? 0.1872 0.1642 0.1291 -0.0312 0.0061  0.0119  39  VAL A O   
300  C  CB  . VAL A 39  ? 0.2218 0.1620 0.1431 -0.0301 0.0056  0.0163  39  VAL A CB  
301  C  CG1 . VAL A 39  ? 0.2222 0.1409 0.1469 -0.0521 0.0037  0.0191  39  VAL A CG1 
302  C  CG2 . VAL A 39  ? 0.2514 0.2001 0.1822 -0.0265 0.0166  0.0415  39  VAL A CG2 
303  N  N   . HIS A 40  ? 0.1866 0.1547 0.1334 -0.0367 0.0132  0.0157  40  HIS A N   
304  C  CA  . HIS A 40  ? 0.1634 0.1399 0.1203 -0.0527 0.0156  0.0182  40  HIS A CA  
305  C  C   . HIS A 40  ? 0.1656 0.1378 0.1259 -0.0667 0.0136  0.0235  40  HIS A C   
306  O  O   . HIS A 40  ? 0.1858 0.1723 0.1408 -0.0407 0.0048  0.0344  40  HIS A O   
307  C  CB  . HIS A 40  ? 0.1929 0.1508 0.1318 -0.0480 0.0196  0.0048  40  HIS A CB  
308  C  CG  . HIS A 40  ? 0.1806 0.1636 0.1444 -0.0213 0.0427  -0.0034 40  HIS A CG  
309  N  ND1 . HIS A 40  ? 0.1861 0.1840 0.1552 -0.0165 0.0454  -0.0052 40  HIS A ND1 
310  C  CD2 . HIS A 40  ? 0.1740 0.1583 0.1536 -0.0224 0.0554  0.0036  40  HIS A CD2 
311  C  CE1 . HIS A 40  ? 0.1752 0.1688 0.1554 -0.0011 0.0506  0.0128  40  HIS A CE1 
312  N  NE2 . HIS A 40  ? 0.1828 0.1605 0.1531 -0.0090 0.0442  0.0093  40  HIS A NE2 
313  N  N   . VAL A 41  ? 0.1761 0.1415 0.1153 -0.0563 0.0376  0.0047  41  VAL A N   
314  C  CA  . VAL A 41  ? 0.1887 0.1496 0.1195 -0.0466 0.0348  -0.0009 41  VAL A CA  
315  C  C   . VAL A 41  ? 0.1816 0.1463 0.1188 -0.0299 0.0402  0.0001  41  VAL A C   
316  O  O   . VAL A 41  ? 0.1916 0.1627 0.1434 -0.0403 0.0422  0.0055  41  VAL A O   
317  C  CB  . VAL A 41  ? 0.2082 0.1517 0.1376 -0.0378 0.0141  -0.0181 41  VAL A CB  
318  C  CG1 . VAL A 41  ? 0.2202 0.1627 0.1476 -0.0356 0.0134  -0.0012 41  VAL A CG1 
319  C  CG2 . VAL A 41  ? 0.2259 0.1765 0.1584 -0.0262 0.0121  -0.0333 41  VAL A CG2 
320  N  N   . VAL A 42  ? 0.1780 0.1268 0.1203 -0.0319 0.0231  -0.0047 42  VAL A N   
321  C  CA  . VAL A 42  ? 0.1891 0.1356 0.1325 -0.0334 0.0122  -0.0004 42  VAL A CA  
322  C  C   . VAL A 42  ? 0.1802 0.1499 0.1377 -0.0241 0.0142  0.0084  42  VAL A C   
323  O  O   . VAL A 42  ? 0.1690 0.1450 0.1458 -0.0118 0.0303  0.0108  42  VAL A O   
324  C  CB  . VAL A 42  ? 0.1993 0.1536 0.1383 -0.0351 0.0113  0.0049  42  VAL A CB  
325  C  CG1 . VAL A 42  ? 0.2010 0.1717 0.1585 -0.0292 0.0140  0.0016  42  VAL A CG1 
326  C  CG2 . VAL A 42  ? 0.2064 0.1566 0.1429 -0.0384 0.0183  0.0205  42  VAL A CG2 
327  N  N   . PRO A 43  ? 0.1793 0.1630 0.1238 0.0016  0.0109  0.0109  43  PRO A N   
328  C  CA  . PRO A 43  ? 0.1923 0.1855 0.1278 -0.0003 0.0070  0.0205  43  PRO A CA  
329  C  C   . PRO A 43  ? 0.1893 0.1698 0.1341 -0.0208 0.0044  0.0123  43  PRO A C   
330  O  O   . PRO A 43  ? 0.1952 0.1581 0.1446 -0.0048 0.0182  0.0052  43  PRO A O   
331  C  CB  . PRO A 43  ? 0.1848 0.2106 0.1398 -0.0021 0.0113  0.0176  43  PRO A CB  
332  C  CG  . PRO A 43  ? 0.1881 0.2301 0.1515 0.0060  -0.0075 0.0153  43  PRO A CG  
333  C  CD  . PRO A 43  ? 0.1873 0.2015 0.1398 0.0000  -0.0075 0.0100  43  PRO A CD  
334  N  N   . ASP A 44  ? 0.1674 0.1618 0.1595 -0.0240 0.0118  0.0333  44  ASP A N   
335  C  CA  . ASP A 44  ? 0.1952 0.1685 0.1803 -0.0143 -0.0117 0.0214  44  ASP A CA  
336  C  C   . ASP A 44  ? 0.2059 0.1601 0.1677 -0.0115 0.0012  0.0124  44  ASP A C   
337  O  O   . ASP A 44  ? 0.2387 0.1725 0.1836 -0.0225 -0.0010 0.0066  44  ASP A O   
338  C  CB  . ASP A 44  ? 0.2328 0.2093 0.2164 0.0010  -0.0292 0.0287  44  ASP A CB  
339  C  CG  . ASP A 44  ? 0.2976 0.2755 0.2695 0.0206  -0.0287 0.0189  44  ASP A CG  
340  O  OD1 . ASP A 44  ? 0.3342 0.2974 0.2837 0.0384  -0.0470 0.0048  44  ASP A OD1 
341  O  OD2 . ASP A 44  ? 0.3265 0.3123 0.3037 0.0238  -0.0292 0.0115  44  ASP A OD2 
342  N  N   . GLN A 45  ? 0.1842 0.1582 0.1659 -0.0079 0.0236  0.0108  45  GLN A N   
343  C  CA  . GLN A 45  ? 0.1672 0.1387 0.1562 -0.0004 0.0328  0.0090  45  GLN A CA  
344  C  C   . GLN A 45  ? 0.1829 0.1373 0.1611 -0.0272 0.0403  0.0134  45  GLN A C   
345  O  O   . GLN A 45  ? 0.2033 0.1736 0.1840 -0.0285 0.0342  0.0118  45  GLN A O   
346  C  CB  . GLN A 45  ? 0.1599 0.1141 0.1558 0.0052  0.0342  0.0155  45  GLN A CB  
347  C  CG  . GLN A 45  ? 0.1790 0.1313 0.1759 0.0007  0.0262  0.0067  45  GLN A CG  
348  C  CD  . GLN A 45  ? 0.1737 0.1449 0.1793 0.0065  0.0166  -0.0027 45  GLN A CD  
349  O  OE1 . GLN A 45  ? 0.1992 0.1596 0.1935 0.0346  0.0378  -0.0008 45  GLN A OE1 
350  N  NE2 . GLN A 45  ? 0.1689 0.1478 0.1687 -0.0110 0.0024  -0.0208 45  GLN A NE2 
351  N  N   . LEU A 46  ? 0.1923 0.1046 0.1714 -0.0239 0.0359  0.0301  46  LEU A N   
352  C  CA  . LEU A 46  ? 0.1921 0.1248 0.1857 -0.0120 0.0252  0.0325  46  LEU A CA  
353  C  C   . LEU A 46  ? 0.1770 0.1468 0.1845 0.0026  0.0232  0.0335  46  LEU A C   
354  O  O   . LEU A 46  ? 0.1686 0.1680 0.1768 0.0146  0.0165  0.0156  46  LEU A O   
355  C  CB  . LEU A 46  ? 0.2019 0.1338 0.2028 -0.0145 0.0342  0.0356  46  LEU A CB  
356  C  CG  . LEU A 46  ? 0.2271 0.1548 0.2230 -0.0020 0.0497  0.0316  46  LEU A CG  
357  C  CD1 . LEU A 46  ? 0.2554 0.1674 0.2236 0.0097  0.0417  0.0250  46  LEU A CD1 
358  C  CD2 . LEU A 46  ? 0.2603 0.1708 0.2468 -0.0077 0.0335  0.0301  46  LEU A CD2 
359  N  N   . MET A 47  ? 0.1750 0.1363 0.1981 0.0154  0.0334  0.0341  47  MET A N   
360  C  CA  . MET A 47  ? 0.1996 0.1533 0.2055 0.0256  0.0456  0.0617  47  MET A CA  
361  C  C   . MET A 47  ? 0.2036 0.1501 0.1862 0.0459  0.0519  0.0501  47  MET A C   
362  O  O   . MET A 47  ? 0.2239 0.1741 0.1875 0.0493  0.0460  0.0357  47  MET A O   
363  C  CB  . MET A 47  ? 0.2475 0.1646 0.2478 0.0181  0.0298  0.0648  47  MET A CB  
364  C  CG  . MET A 47  ? 0.2869 0.1859 0.2927 -0.0149 -0.0161 0.0618  47  MET A CG  
365  S  SD  . MET A 47  ? 0.3270 0.1929 0.3036 -0.0512 -0.0576 0.0739  47  MET A SD  
366  C  CE  . MET A 47  ? 0.3341 0.2103 0.3215 -0.0694 -0.0515 0.0361  47  MET A CE  
367  N  N   . ALA A 48  ? 0.1943 0.1617 0.1675 0.0520  0.0558  0.0447  48  ALA A N   
368  C  CA  . ALA A 48  ? 0.1891 0.1601 0.1792 0.0493  0.0590  0.0359  48  ALA A CA  
369  C  C   . ALA A 48  ? 0.1949 0.1680 0.1672 0.0395  0.0561  0.0279  48  ALA A C   
370  O  O   . ALA A 48  ? 0.2199 0.1630 0.1522 0.0465  0.0525  0.0162  48  ALA A O   
371  C  CB  . ALA A 48  ? 0.1968 0.1682 0.1995 0.0334  0.0761  0.0345  48  ALA A CB  
372  N  N   . PHE A 49  ? 0.1826 0.1735 0.1761 0.0348  0.0488  0.0345  49  PHE A N   
373  C  CA  . PHE A 49  ? 0.1922 0.1834 0.1795 0.0349  0.0455  0.0366  49  PHE A CA  
374  C  C   . PHE A 49  ? 0.2041 0.2081 0.1807 0.0333  0.0487  0.0269  49  PHE A C   
375  O  O   . PHE A 49  ? 0.2145 0.2238 0.1732 0.0214  0.0424  0.0211  49  PHE A O   
376  C  CB  . PHE A 49  ? 0.1987 0.1916 0.1873 0.0091  0.0618  0.0315  49  PHE A CB  
377  C  CG  . PHE A 49  ? 0.2234 0.1876 0.2071 0.0063  0.0564  0.0304  49  PHE A CG  
378  C  CD1 . PHE A 49  ? 0.2460 0.1917 0.2190 0.0280  0.0453  0.0299  49  PHE A CD1 
379  C  CD2 . PHE A 49  ? 0.2456 0.1787 0.2088 -0.0052 0.0372  0.0391  49  PHE A CD2 
380  C  CE1 . PHE A 49  ? 0.2616 0.1907 0.2272 0.0309  0.0433  0.0206  49  PHE A CE1 
381  C  CE2 . PHE A 49  ? 0.2569 0.1836 0.2144 0.0062  0.0278  0.0298  49  PHE A CE2 
382  C  CZ  . PHE A 49  ? 0.2640 0.1885 0.2229 0.0153  0.0332  0.0260  49  PHE A CZ  
383  N  N   . GLY A 50  ? 0.2027 0.2378 0.1914 0.0254  0.0582  0.0186  50  GLY A N   
384  C  CA  . GLY A 50  ? 0.2024 0.2820 0.2009 -0.0032 0.0674  0.0316  50  GLY A CA  
385  C  C   . GLY A 50  ? 0.2202 0.3303 0.2118 -0.0357 0.0592  0.0334  50  GLY A C   
386  O  O   . GLY A 50  ? 0.2300 0.3678 0.2150 -0.0409 0.0698  0.0040  50  GLY A O   
387  N  N   . GLY A 51  ? 0.2421 0.3258 0.2257 -0.0669 0.0245  0.0631  51  GLY A N   
388  C  CA  . GLY A 51  ? 0.2765 0.3264 0.2369 -0.0768 0.0048  0.0809  51  GLY A CA  
389  C  C   . GLY A 51  ? 0.3131 0.3210 0.2324 -0.0651 0.0109  0.0873  51  GLY A C   
390  O  O   . GLY A 51  ? 0.3548 0.3509 0.2685 -0.0845 -0.0072 0.0966  51  GLY A O   
391  N  N   . SER A 52  ? 0.2886 0.2912 0.1942 -0.0254 0.0354  0.0777  52  SER A N   
392  C  CA  . SER A 52  ? 0.2828 0.2727 0.1860 0.0103  0.0506  0.0578  52  SER A CA  
393  C  C   . SER A 52  ? 0.2567 0.2571 0.1860 0.0204  0.0483  0.0587  52  SER A C   
394  O  O   . SER A 52  ? 0.2425 0.2362 0.1598 0.0337  0.0583  0.0420  52  SER A O   
395  C  CB  . SER A 52  ? 0.3190 0.2704 0.1790 0.0292  0.0524  0.0368  52  SER A CB  
396  O  OG  . SER A 52  ? 0.3572 0.2866 0.1802 0.0225  0.0602  0.0348  52  SER A OG  
397  N  N   . SER A 53  ? 0.2405 0.2680 0.2079 0.0043  0.0586  0.0694  53  SER A N   
398  C  CA  . SER A 53  ? 0.2476 0.2711 0.2166 0.0312  0.0726  0.0739  53  SER A CA  
399  C  C   . SER A 53  ? 0.2467 0.2526 0.2208 0.0309  0.0800  0.0895  53  SER A C   
400  O  O   . SER A 53  ? 0.2449 0.2510 0.2387 0.0322  0.0561  0.0926  53  SER A O   
401  C  CB  . SER A 53  ? 0.2661 0.2894 0.2306 0.0244  0.0641  0.0654  53  SER A CB  
402  O  OG  . SER A 53  ? 0.2903 0.3188 0.2439 0.0137  0.0468  0.0760  53  SER A OG  
403  N  N   . GLU A 54  ? 0.2590 0.2558 0.2020 0.0213  0.1027  0.0901  54  GLU A N   
404  C  CA  . GLU A 54  ? 0.2817 0.2603 0.1863 0.0423  0.0910  0.0737  54  GLU A CA  
405  C  C   . GLU A 54  ? 0.2679 0.2338 0.1540 0.0528  0.0977  0.0499  54  GLU A C   
406  O  O   . GLU A 54  ? 0.2484 0.2024 0.1542 0.0482  0.0961  0.0614  54  GLU A O   
407  C  CB  . GLU A 54  ? 0.3122 0.3042 0.1977 0.0345  0.0965  0.0864  54  GLU A CB  
408  C  CG  . GLU A 54  ? 0.3378 0.3594 0.2209 0.0302  0.0914  0.0668  54  GLU A CG  
409  C  CD  . GLU A 54  ? 0.3758 0.4064 0.2609 0.0370  0.0804  0.0505  54  GLU A CD  
410  O  OE1 . GLU A 54  ? 0.3807 0.4168 0.2677 0.0503  0.0790  0.0439  54  GLU A OE1 
411  O  OE2 . GLU A 54  ? 0.3994 0.4243 0.2927 0.0338  0.0593  0.0417  54  GLU A OE2 
412  N  N   . PRO A 55  ? 0.2798 0.2397 0.1328 0.0469  0.0842  0.0371  55  PRO A N   
413  C  CA  . PRO A 55  ? 0.2708 0.2168 0.1180 0.0394  0.0645  0.0523  55  PRO A CA  
414  C  C   . PRO A 55  ? 0.2513 0.1921 0.1205 0.0436  0.0486  0.0365  55  PRO A C   
415  O  O   . PRO A 55  ? 0.2728 0.1909 0.1297 0.0403  0.0438  0.0414  55  PRO A O   
416  C  CB  . PRO A 55  ? 0.2972 0.2439 0.1240 0.0439  0.0511  0.0486  55  PRO A CB  
417  C  CG  . PRO A 55  ? 0.3131 0.2623 0.1337 0.0368  0.0518  0.0520  55  PRO A CG  
418  C  CD  . PRO A 55  ? 0.3114 0.2602 0.1343 0.0330  0.0622  0.0474  55  PRO A CD  
419  N  N   . CYS A 56  ? 0.2287 0.1874 0.1191 0.0230  0.0352  0.0367  56  CYS A N   
420  C  CA  . CYS A 56  ? 0.2015 0.1659 0.1339 0.0212  0.0426  0.0357  56  CYS A CA  
421  C  C   . CYS A 56  ? 0.1994 0.1538 0.1189 0.0234  0.0499  0.0359  56  CYS A C   
422  O  O   . CYS A 56  ? 0.2203 0.1749 0.1234 0.0390  0.0602  0.0265  56  CYS A O   
423  C  CB  . CYS A 56  ? 0.2037 0.1567 0.1766 0.0257  0.0455  0.0272  56  CYS A CB  
424  S  SG  . CYS A 56  ? 0.2260 0.1703 0.2096 0.0229  0.0460  -0.0032 56  CYS A SG  
425  N  N   . ALA A 57  ? 0.2014 0.1732 0.1114 0.0257  0.0512  0.0193  57  ALA A N   
426  C  CA  . ALA A 57  ? 0.1916 0.1628 0.1164 0.0265  0.0597  0.0196  57  ALA A CA  
427  C  C   . ALA A 57  ? 0.1886 0.1595 0.1185 0.0342  0.0593  0.0213  57  ALA A C   
428  O  O   . ALA A 57  ? 0.1876 0.1860 0.1253 0.0360  0.0450  0.0363  57  ALA A O   
429  C  CB  . ALA A 57  ? 0.2204 0.1658 0.1252 0.0295  0.0549  0.0209  57  ALA A CB  
430  N  N   . LEU A 58  ? 0.1915 0.1530 0.1159 0.0120  0.0606  0.0122  58  LEU A N   
431  C  CA  . LEU A 58  ? 0.1795 0.1392 0.1251 0.0112  0.0510  -0.0052 58  LEU A CA  
432  C  C   . LEU A 58  ? 0.1924 0.1326 0.1177 0.0217  0.0414  0.0080  58  LEU A C   
433  O  O   . LEU A 58  ? 0.1885 0.1459 0.1349 0.0067  0.0522  0.0267  58  LEU A O   
434  C  CB  . LEU A 58  ? 0.1921 0.1636 0.1637 -0.0133 0.0505  -0.0041 58  LEU A CB  
435  C  CG  . LEU A 58  ? 0.2038 0.1718 0.2050 -0.0199 0.0731  -0.0019 58  LEU A CG  
436  C  CD1 . LEU A 58  ? 0.2103 0.1835 0.2266 -0.0311 0.0623  -0.0062 58  LEU A CD1 
437  C  CD2 . LEU A 58  ? 0.2088 0.2000 0.2184 -0.0256 0.0934  0.0035  58  LEU A CD2 
438  N  N   . CYS A 59  ? 0.1953 0.1311 0.1162 0.0015  0.0313  0.0146  59  CYS A N   
439  C  CA  . CYS A 59  ? 0.1804 0.1293 0.1123 -0.0163 0.0117  0.0162  59  CYS A CA  
440  C  C   . CYS A 59  ? 0.1746 0.1447 0.1150 -0.0165 0.0232  0.0211  59  CYS A C   
441  O  O   . CYS A 59  ? 0.1619 0.1679 0.1132 0.0114  0.0289  0.0258  59  CYS A O   
442  C  CB  . CYS A 59  ? 0.2130 0.1514 0.1177 -0.0230 0.0047  -0.0074 59  CYS A CB  
443  S  SG  . CYS A 59  ? 0.2380 0.1670 0.1238 -0.0041 0.0184  -0.0098 59  CYS A SG  
444  N  N   . SER A 60  ? 0.1786 0.1410 0.1272 -0.0311 0.0238  0.0138  60  SER A N   
445  C  CA  . SER A 60  ? 0.1865 0.1445 0.1331 -0.0199 0.0125  0.0134  60  SER A CA  
446  C  C   . SER A 60  ? 0.1881 0.1551 0.1270 -0.0246 0.0195  0.0247  60  SER A C   
447  O  O   . SER A 60  ? 0.2076 0.1658 0.1541 -0.0397 0.0077  0.0315  60  SER A O   
448  C  CB  . SER A 60  ? 0.2182 0.1535 0.1683 -0.0389 0.0210  -0.0039 60  SER A CB  
449  O  OG  . SER A 60  ? 0.2456 0.1748 0.1768 -0.0140 0.0256  -0.0111 60  SER A OG  
450  N  N   . LEU A 61  ? 0.1905 0.1453 0.1006 -0.0144 0.0311  0.0139  61  LEU A N   
451  C  CA  . LEU A 61  ? 0.1975 0.1511 0.1159 -0.0265 0.0190  0.0087  61  LEU A CA  
452  C  C   . LEU A 61  ? 0.1847 0.1543 0.1095 -0.0367 0.0184  0.0167  61  LEU A C   
453  O  O   . LEU A 61  ? 0.1845 0.1635 0.1083 -0.0319 0.0199  0.0029  61  LEU A O   
454  C  CB  . LEU A 61  ? 0.2158 0.1563 0.1410 -0.0268 0.0203  0.0017  61  LEU A CB  
455  C  CG  . LEU A 61  ? 0.2423 0.1596 0.1614 0.0068  0.0040  0.0006  61  LEU A CG  
456  C  CD1 . LEU A 61  ? 0.2516 0.1739 0.1675 -0.0001 0.0049  -0.0095 61  LEU A CD1 
457  C  CD2 . LEU A 61  ? 0.2478 0.1621 0.1709 0.0241  -0.0096 -0.0141 61  LEU A CD2 
458  N  N   . HIS A 62  ? 0.1872 0.1592 0.0987 -0.0261 0.0274  0.0178  62  HIS A N   
459  C  CA  . HIS A 62  ? 0.2081 0.1643 0.1083 -0.0280 0.0194  0.0154  62  HIS A CA  
460  C  C   . HIS A 62  ? 0.2077 0.1682 0.1149 -0.0308 0.0037  0.0214  62  HIS A C   
461  O  O   . HIS A 62  ? 0.1965 0.1836 0.1220 -0.0373 -0.0006 0.0363  62  HIS A O   
462  C  CB  . HIS A 62  ? 0.2057 0.1725 0.1255 -0.0166 0.0311  -0.0096 62  HIS A CB  
463  C  CG  . HIS A 62  ? 0.2318 0.1751 0.1525 -0.0136 0.0395  -0.0178 62  HIS A CG  
464  N  ND1 . HIS A 62  ? 0.2515 0.1692 0.1789 -0.0355 0.0481  -0.0180 62  HIS A ND1 
465  C  CD2 . HIS A 62  ? 0.2428 0.1708 0.1669 -0.0124 0.0364  -0.0230 62  HIS A CD2 
466  C  CE1 . HIS A 62  ? 0.2546 0.1569 0.1794 -0.0332 0.0400  -0.0290 62  HIS A CE1 
467  N  NE2 . HIS A 62  ? 0.2519 0.1616 0.1844 -0.0193 0.0286  -0.0306 62  HIS A NE2 
468  N  N   . SER A 63  ? 0.2095 0.1429 0.1028 -0.0459 0.0152  0.0285  63  SER A N   
469  C  CA  . SER A 63  ? 0.2252 0.1401 0.1129 -0.0351 0.0034  0.0149  63  SER A CA  
470  C  C   . SER A 63  ? 0.2014 0.1624 0.1007 -0.0282 0.0192  0.0083  63  SER A C   
471  O  O   . SER A 63  ? 0.1896 0.1645 0.1124 -0.0116 0.0243  0.0273  63  SER A O   
472  C  CB  . SER A 63  ? 0.2616 0.1528 0.1336 -0.0281 -0.0035 -0.0028 63  SER A CB  
473  O  OG  . SER A 63  ? 0.2595 0.1702 0.1475 -0.0386 0.0101  0.0066  63  SER A OG  
474  N  N   . ILE A 64  ? 0.1977 0.1748 0.0924 -0.0199 0.0183  0.0200  64  ILE A N   
475  C  CA  . ILE A 64  ? 0.1894 0.1754 0.1030 -0.0145 0.0109  0.0139  64  ILE A CA  
476  C  C   . ILE A 64  ? 0.2097 0.1698 0.1172 -0.0202 -0.0037 0.0273  64  ILE A C   
477  O  O   . ILE A 64  ? 0.2245 0.1883 0.1380 -0.0345 -0.0024 0.0313  64  ILE A O   
478  C  CB  . ILE A 64  ? 0.1896 0.1707 0.1037 -0.0259 0.0373  0.0242  64  ILE A CB  
479  C  CG1 . ILE A 64  ? 0.1780 0.1686 0.1167 -0.0343 0.0374  0.0163  64  ILE A CG1 
480  C  CG2 . ILE A 64  ? 0.1781 0.1947 0.1078 -0.0409 0.0348  0.0522  64  ILE A CG2 
481  C  CD1 . ILE A 64  ? 0.1806 0.1797 0.1216 -0.0420 0.0340  -0.0095 64  ILE A CD1 
482  N  N   . GLY A 65  ? 0.2105 0.1665 0.1089 -0.0244 0.0113  0.0172  65  GLY A N   
483  C  CA  . GLY A 65  ? 0.2339 0.1805 0.1146 -0.0231 0.0137  -0.0039 65  GLY A CA  
484  C  C   . GLY A 65  ? 0.2471 0.1695 0.1186 -0.0165 0.0106  -0.0001 65  GLY A C   
485  O  O   . GLY A 65  ? 0.2413 0.1829 0.1303 -0.0289 0.0217  0.0129  65  GLY A O   
486  N  N   . LYS A 66  ? 0.2562 0.1482 0.1188 -0.0180 0.0119  -0.0098 66  LYS A N   
487  C  CA  . LYS A 66  ? 0.2633 0.1516 0.1176 -0.0225 0.0138  0.0012  66  LYS A CA  
488  C  C   . LYS A 66  ? 0.2584 0.1509 0.1208 -0.0248 0.0187  -0.0069 66  LYS A C   
489  O  O   . LYS A 66  ? 0.2758 0.1705 0.1315 -0.0373 0.0050  0.0126  66  LYS A O   
490  C  CB  . LYS A 66  ? 0.2870 0.1660 0.1423 -0.0487 0.0035  0.0086  66  LYS A CB  
491  C  CG  . LYS A 66  ? 0.3195 0.1585 0.1814 -0.0727 -0.0213 0.0293  66  LYS A CG  
492  C  CD  . LYS A 66  ? 0.3520 0.2015 0.2290 -0.0617 -0.0153 0.0412  66  LYS A CD  
493  C  CE  . LYS A 66  ? 0.3850 0.2416 0.2736 -0.0438 -0.0210 0.0387  66  LYS A CE  
494  N  NZ  . LYS A 66  ? 0.4061 0.2742 0.2993 -0.0363 -0.0197 0.0440  66  LYS A NZ  
495  N  N   . ILE A 67  ? 0.2378 0.1340 0.1254 -0.0047 0.0156  -0.0019 67  ILE A N   
496  C  CA  . ILE A 67  ? 0.2511 0.1537 0.1413 0.0091  0.0270  -0.0025 67  ILE A CA  
497  C  C   . ILE A 67  ? 0.2608 0.1678 0.1544 0.0166  0.0314  -0.0018 67  ILE A C   
498  O  O   . ILE A 67  ? 0.2705 0.2117 0.1521 0.0133  0.0149  0.0171  67  ILE A O   
499  C  CB  . ILE A 67  ? 0.2563 0.1541 0.1429 -0.0011 0.0358  -0.0009 67  ILE A CB  
500  C  CG1 . ILE A 67  ? 0.2668 0.1550 0.1300 0.0057  0.0230  0.0099  67  ILE A CG1 
501  C  CG2 . ILE A 67  ? 0.2531 0.1600 0.1606 -0.0144 0.0366  -0.0158 67  ILE A CG2 
502  C  CD1 . ILE A 67  ? 0.2704 0.1663 0.1265 0.0118  0.0183  0.0142  67  ILE A CD1 
503  N  N   . GLY A 68  ? 0.2540 0.1451 0.1742 0.0221  0.0510  -0.0057 68  GLY A N   
504  C  CA  . GLY A 68  ? 0.2623 0.1599 0.1837 0.0291  0.0482  0.0179  68  GLY A CA  
505  C  C   . GLY A 68  ? 0.2637 0.1732 0.1772 0.0210  0.0490  0.0105  68  GLY A C   
506  O  O   . GLY A 68  ? 0.2667 0.1802 0.1760 0.0130  0.0498  0.0175  68  GLY A O   
507  N  N   . GLY A 69  ? 0.2717 0.1707 0.1749 0.0346  0.0477  -0.0002 69  GLY A N   
508  C  CA  . GLY A 69  ? 0.2816 0.1795 0.1751 0.0317  0.0427  -0.0050 69  GLY A CA  
509  C  C   . GLY A 69  ? 0.2956 0.1586 0.1765 0.0347  0.0522  -0.0104 69  GLY A C   
510  O  O   . GLY A 69  ? 0.3011 0.1630 0.1647 0.0377  0.0577  -0.0137 69  GLY A O   
511  N  N   . ALA A 70  ? 0.3054 0.1695 0.1944 0.0183  0.0470  -0.0005 70  ALA A N   
512  C  CA  . ALA A 70  ? 0.3137 0.1426 0.2044 0.0039  0.0437  0.0071  70  ALA A CA  
513  C  C   . ALA A 70  ? 0.3221 0.1333 0.1963 -0.0156 0.0478  -0.0056 70  ALA A C   
514  O  O   . ALA A 70  ? 0.3244 0.1198 0.1914 -0.0219 0.0496  -0.0105 70  ALA A O   
515  C  CB  . ALA A 70  ? 0.3234 0.1344 0.2265 0.0107  0.0337  0.0217  70  ALA A CB  
516  N  N   . GLN A 71  ? 0.3114 0.1310 0.1796 -0.0158 0.0451  -0.0130 71  GLN A N   
517  C  CA  . GLN A 71  ? 0.2897 0.1256 0.1556 -0.0274 0.0469  -0.0199 71  GLN A CA  
518  C  C   . GLN A 71  ? 0.2889 0.1364 0.1448 -0.0386 0.0373  -0.0160 71  GLN A C   
519  O  O   . GLN A 71  ? 0.3006 0.1545 0.1499 -0.0271 0.0294  -0.0071 71  GLN A O   
520  C  CB  . GLN A 71  ? 0.2952 0.1249 0.1564 -0.0203 0.0496  0.0035  71  GLN A CB  
521  C  CG  . GLN A 71  ? 0.3140 0.1317 0.1604 -0.0385 0.0525  0.0184  71  GLN A CG  
522  C  CD  . GLN A 71  ? 0.3292 0.1634 0.1728 -0.0375 0.0538  0.0168  71  GLN A CD  
523  O  OE1 . GLN A 71  ? 0.3393 0.1900 0.1806 -0.0404 0.0724  0.0210  71  GLN A OE1 
524  N  NE2 . GLN A 71  ? 0.3385 0.1659 0.1749 -0.0292 0.0446  0.0257  71  GLN A NE2 
525  N  N   . ASN A 72  ? 0.2651 0.1174 0.1333 -0.0574 0.0577  -0.0127 72  ASN A N   
526  C  CA  . ASN A 72  ? 0.2606 0.1358 0.1326 -0.0452 0.0525  -0.0164 72  ASN A CA  
527  C  C   . ASN A 72  ? 0.2821 0.1479 0.1458 -0.0291 0.0347  -0.0368 72  ASN A C   
528  O  O   . ASN A 72  ? 0.3006 0.1490 0.1459 -0.0115 0.0173  -0.0432 72  ASN A O   
529  C  CB  . ASN A 72  ? 0.2377 0.1332 0.1279 -0.0237 0.0426  -0.0229 72  ASN A CB  
530  C  CG  . ASN A 72  ? 0.2092 0.1361 0.1290 -0.0086 0.0409  -0.0045 72  ASN A CG  
531  O  OD1 . ASN A 72  ? 0.2072 0.1407 0.1205 -0.0031 0.0193  -0.0036 72  ASN A OD1 
532  N  ND2 . ASN A 72  ? 0.1997 0.1375 0.1418 0.0052  0.0431  -0.0065 72  ASN A ND2 
533  N  N   . ARG A 73  ? 0.2697 0.1557 0.1493 -0.0135 0.0497  -0.0347 73  ARG A N   
534  C  CA  . ARG A 73  ? 0.2792 0.1609 0.1540 -0.0002 0.0463  -0.0345 73  ARG A CA  
535  C  C   . ARG A 73  ? 0.2932 0.1623 0.1445 -0.0038 0.0273  -0.0214 73  ARG A C   
536  O  O   . ARG A 73  ? 0.3050 0.1752 0.1351 -0.0032 0.0314  -0.0106 73  ARG A O   
537  C  CB  . ARG A 73  ? 0.2788 0.1750 0.1787 0.0084  0.0613  -0.0347 73  ARG A CB  
538  C  CG  . ARG A 73  ? 0.2932 0.2004 0.2019 0.0269  0.0474  -0.0328 73  ARG A CG  
539  C  CD  . ARG A 73  ? 0.3119 0.2288 0.2293 0.0454  0.0425  -0.0154 73  ARG A CD  
540  N  NE  . ARG A 73  ? 0.3362 0.2549 0.2592 0.0577  0.0464  -0.0112 73  ARG A NE  
541  C  CZ  . ARG A 73  ? 0.3415 0.2676 0.2624 0.0625  0.0636  -0.0047 73  ARG A CZ  
542  N  NH1 . ARG A 73  ? 0.3421 0.2754 0.2639 0.0466  0.0741  0.0020  73  ARG A NH1 
543  N  NH2 . ARG A 73  ? 0.3409 0.2745 0.2698 0.0751  0.0712  0.0039  73  ARG A NH2 
544  N  N   . SER A 74  ? 0.2916 0.1519 0.1385 -0.0006 0.0064  -0.0308 74  SER A N   
545  C  CA  . SER A 74  ? 0.3113 0.1569 0.1565 -0.0187 -0.0070 -0.0168 74  SER A CA  
546  C  C   . SER A 74  ? 0.3287 0.1368 0.1386 -0.0248 -0.0214 -0.0215 74  SER A C   
547  O  O   . SER A 74  ? 0.3656 0.1385 0.1439 -0.0141 -0.0278 -0.0065 74  SER A O   
548  C  CB  . SER A 74  ? 0.3154 0.1824 0.1690 -0.0326 0.0060  -0.0020 74  SER A CB  
549  O  OG  . SER A 74  ? 0.3244 0.1967 0.1888 -0.0354 0.0125  0.0032  74  SER A OG  
550  N  N   . TYR A 75  ? 0.3122 0.1427 0.1348 -0.0238 0.0008  -0.0218 75  TYR A N   
551  C  CA  . TYR A 75  ? 0.3069 0.1407 0.1215 -0.0111 0.0150  -0.0089 75  TYR A CA  
552  C  C   . TYR A 75  ? 0.3028 0.1547 0.1287 -0.0123 0.0164  -0.0103 75  TYR A C   
553  O  O   . TYR A 75  ? 0.3033 0.1629 0.1290 -0.0223 0.0008  -0.0059 75  TYR A O   
554  C  CB  . TYR A 75  ? 0.3062 0.1629 0.1024 -0.0277 0.0264  0.0055  75  TYR A CB  
555  C  CG  . TYR A 75  ? 0.3148 0.1889 0.1101 -0.0541 0.0120  0.0201  75  TYR A CG  
556  C  CD1 . TYR A 75  ? 0.3223 0.2201 0.1237 -0.0861 0.0095  0.0160  75  TYR A CD1 
557  C  CD2 . TYR A 75  ? 0.3173 0.1858 0.1047 -0.0408 0.0220  0.0217  75  TYR A CD2 
558  C  CE1 . TYR A 75  ? 0.3373 0.2354 0.1298 -0.0855 0.0077  0.0179  75  TYR A CE1 
559  C  CE2 . TYR A 75  ? 0.3275 0.1916 0.1098 -0.0459 0.0312  0.0167  75  TYR A CE2 
560  C  CZ  . TYR A 75  ? 0.3295 0.2328 0.1172 -0.0791 0.0220  0.0106  75  TYR A CZ  
561  O  OH  . TYR A 75  ? 0.3460 0.2640 0.1340 -0.1032 0.0149  0.0111  75  TYR A OH  
562  N  N   . SER A 76  ? 0.2985 0.1386 0.1260 -0.0247 0.0263  -0.0067 76  SER A N   
563  C  CA  . SER A 76  ? 0.2999 0.1530 0.1180 -0.0172 0.0330  -0.0167 76  SER A CA  
564  C  C   . SER A 76  ? 0.3068 0.1483 0.1215 0.0092  0.0310  -0.0212 76  SER A C   
565  O  O   . SER A 76  ? 0.3114 0.1675 0.1264 -0.0055 0.0514  -0.0018 76  SER A O   
566  C  CB  . SER A 76  ? 0.3052 0.1709 0.1283 -0.0339 0.0291  -0.0250 76  SER A CB  
567  O  OG  . SER A 76  ? 0.3019 0.1979 0.1535 -0.0188 0.0482  -0.0385 76  SER A OG  
568  N  N   . LYS A 77  ? 0.3206 0.1529 0.1371 -0.0010 0.0226  -0.0346 77  LYS A N   
569  C  CA  . LYS A 77  ? 0.3493 0.1459 0.1547 -0.0048 0.0149  -0.0387 77  LYS A CA  
570  C  C   . LYS A 77  ? 0.3505 0.1567 0.1516 -0.0130 0.0261  -0.0180 77  LYS A C   
571  O  O   . LYS A 77  ? 0.3684 0.1616 0.1510 0.0007  0.0049  -0.0047 77  LYS A O   
572  C  CB  . LYS A 77  ? 0.3789 0.1605 0.1791 0.0005  0.0115  -0.0653 77  LYS A CB  
573  C  CG  . LYS A 77  ? 0.4106 0.1925 0.2022 -0.0001 0.0051  -0.0674 77  LYS A CG  
574  C  CD  . LYS A 77  ? 0.4462 0.2265 0.2260 -0.0137 -0.0054 -0.0766 77  LYS A CD  
575  C  CE  . LYS A 77  ? 0.4757 0.2539 0.2483 -0.0060 -0.0072 -0.0811 77  LYS A CE  
576  N  NZ  . LYS A 77  ? 0.4941 0.2748 0.2719 0.0007  -0.0062 -0.0680 77  LYS A NZ  
577  N  N   . LEU A 78  ? 0.3196 0.1578 0.1428 -0.0291 0.0413  -0.0114 78  LEU A N   
578  C  CA  . LEU A 78  ? 0.2999 0.1856 0.1506 -0.0374 0.0317  0.0013  78  LEU A CA  
579  C  C   . LEU A 78  ? 0.3033 0.1879 0.1401 -0.0413 0.0204  -0.0040 78  LEU A C   
580  O  O   . LEU A 78  ? 0.3068 0.1947 0.1427 -0.0528 0.0141  0.0024  78  LEU A O   
581  C  CB  . LEU A 78  ? 0.2833 0.2155 0.1620 -0.0422 0.0244  0.0026  78  LEU A CB  
582  C  CG  . LEU A 78  ? 0.2728 0.2443 0.1774 -0.0463 0.0078  0.0072  78  LEU A CG  
583  C  CD1 . LEU A 78  ? 0.2793 0.2613 0.1974 -0.0621 -0.0042 0.0128  78  LEU A CD1 
584  C  CD2 . LEU A 78  ? 0.2722 0.2559 0.1779 -0.0297 0.0106  0.0106  78  LEU A CD2 
585  N  N   . LEU A 79  ? 0.3094 0.1756 0.1347 -0.0393 0.0185  -0.0156 79  LEU A N   
586  C  CA  . LEU A 79  ? 0.2977 0.1673 0.1174 -0.0346 0.0217  -0.0020 79  LEU A CA  
587  C  C   . LEU A 79  ? 0.2700 0.1720 0.1350 -0.0327 0.0130  -0.0004 79  LEU A C   
588  O  O   . LEU A 79  ? 0.2543 0.1744 0.1377 -0.0280 -0.0267 0.0084  79  LEU A O   
589  C  CB  . LEU A 79  ? 0.2978 0.1785 0.0955 -0.0353 0.0270  -0.0025 79  LEU A CB  
590  C  CG  . LEU A 79  ? 0.3072 0.2196 0.1103 -0.0206 0.0147  -0.0021 79  LEU A CG  
591  C  CD1 . LEU A 79  ? 0.3138 0.2274 0.1121 -0.0172 0.0063  -0.0187 79  LEU A CD1 
592  C  CD2 . LEU A 79  ? 0.3098 0.2505 0.1240 -0.0243 0.0059  -0.0030 79  LEU A CD2 
593  N  N   . CYS A 80  ? 0.2629 0.1819 0.1398 -0.0313 0.0173  0.0117  80  CYS A N   
594  C  CA  . CYS A 80  ? 0.2764 0.1857 0.1435 -0.0298 0.0185  0.0163  80  CYS A CA  
595  C  C   . CYS A 80  ? 0.2746 0.1743 0.1435 -0.0493 0.0103  0.0103  80  CYS A C   
596  O  O   . CYS A 80  ? 0.2652 0.1879 0.1351 -0.0424 0.0140  0.0312  80  CYS A O   
597  C  CB  . CYS A 80  ? 0.2806 0.1852 0.1589 -0.0350 0.0203  0.0139  80  CYS A CB  
598  S  SG  . CYS A 80  ? 0.3091 0.1821 0.1853 -0.0262 0.0268  -0.0001 80  CYS A SG  
599  N  N   . GLY A 81  ? 0.3075 0.1765 0.1464 -0.0452 0.0042  -0.0075 81  GLY A N   
600  C  CA  . GLY A 81  ? 0.3307 0.2126 0.1556 -0.0399 0.0015  -0.0086 81  GLY A CA  
601  C  C   . GLY A 81  ? 0.3379 0.2055 0.1459 -0.0537 0.0051  -0.0005 81  GLY A C   
602  O  O   . GLY A 81  ? 0.3649 0.2086 0.1446 -0.0407 0.0183  0.0069  81  GLY A O   
603  N  N   . LEU A 82  ? 0.3239 0.2170 0.1372 -0.0715 0.0029  -0.0026 82  LEU A N   
604  C  CA  . LEU A 82  ? 0.3220 0.2179 0.1296 -0.0570 0.0104  0.0011  82  LEU A CA  
605  C  C   . LEU A 82  ? 0.3045 0.1996 0.1229 -0.0423 0.0033  0.0072  82  LEU A C   
606  O  O   . LEU A 82  ? 0.3106 0.2100 0.1367 -0.0205 0.0088  0.0036  82  LEU A O   
607  C  CB  . LEU A 82  ? 0.3306 0.2495 0.1389 -0.0651 0.0168  -0.0029 82  LEU A CB  
608  C  CG  . LEU A 82  ? 0.3299 0.2707 0.1395 -0.0848 0.0107  -0.0011 82  LEU A CG  
609  C  CD1 . LEU A 82  ? 0.3367 0.2778 0.1362 -0.0824 0.0253  -0.0106 82  LEU A CD1 
610  C  CD2 . LEU A 82  ? 0.3288 0.2873 0.1547 -0.0787 0.0078  0.0078  82  LEU A CD2 
611  N  N   . LEU A 83  ? 0.2969 0.1905 0.1234 -0.0391 0.0047  0.0078  83  LEU A N   
612  C  CA  . LEU A 83  ? 0.2770 0.1746 0.1126 -0.0332 0.0134  0.0044  83  LEU A CA  
613  C  C   . LEU A 83  ? 0.2960 0.1751 0.1117 -0.0126 0.0298  -0.0011 83  LEU A C   
614  O  O   . LEU A 83  ? 0.2888 0.1915 0.1031 -0.0095 0.0389  0.0191  83  LEU A O   
615  C  CB  . LEU A 83  ? 0.2707 0.1960 0.1037 -0.0286 0.0170  -0.0120 83  LEU A CB  
616  C  CG  . LEU A 83  ? 0.2595 0.2233 0.1252 -0.0222 0.0073  -0.0240 83  LEU A CG  
617  C  CD1 . LEU A 83  ? 0.2792 0.2434 0.1269 -0.0306 -0.0049 -0.0293 83  LEU A CD1 
618  C  CD2 . LEU A 83  ? 0.2501 0.2494 0.1472 -0.0052 0.0033  -0.0203 83  LEU A CD2 
619  N  N   . ALA A 84  ? 0.3192 0.1622 0.1059 -0.0111 0.0327  -0.0165 84  ALA A N   
620  C  CA  . ALA A 84  ? 0.3367 0.1708 0.1160 -0.0098 0.0262  -0.0127 84  ALA A CA  
621  C  C   . ALA A 84  ? 0.3419 0.1861 0.1288 -0.0192 0.0124  0.0021  84  ALA A C   
622  O  O   . ALA A 84  ? 0.3458 0.2051 0.1270 -0.0095 -0.0244 0.0109  84  ALA A O   
623  C  CB  . ALA A 84  ? 0.3428 0.1669 0.1140 -0.0023 0.0206  -0.0099 84  ALA A CB  
624  N  N   . GLU A 85  ? 0.3570 0.2013 0.1407 -0.0274 0.0032  -0.0282 85  GLU A N   
625  C  CA  . GLU A 85  ? 0.3857 0.2515 0.1677 -0.0316 -0.0008 -0.0261 85  GLU A CA  
626  C  C   . GLU A 85  ? 0.3768 0.2590 0.1577 -0.0336 0.0061  -0.0252 85  GLU A C   
627  O  O   . GLU A 85  ? 0.3894 0.2888 0.1632 -0.0164 0.0044  -0.0295 85  GLU A O   
628  C  CB  . GLU A 85  ? 0.4310 0.3008 0.2165 -0.0116 -0.0004 -0.0233 85  GLU A CB  
629  C  CG  . GLU A 85  ? 0.4739 0.3595 0.2635 -0.0020 -0.0047 -0.0233 85  GLU A CG  
630  C  CD  . GLU A 85  ? 0.5088 0.4091 0.3004 0.0108  -0.0065 -0.0333 85  GLU A CD  
631  O  OE1 . GLU A 85  ? 0.5179 0.4343 0.3151 0.0200  -0.0033 -0.0415 85  GLU A OE1 
632  O  OE2 . GLU A 85  ? 0.5248 0.4193 0.3130 0.0139  -0.0106 -0.0387 85  GLU A OE2 
633  N  N   . ARG A 86  ? 0.3485 0.2382 0.1517 -0.0485 0.0225  -0.0280 86  ARG A N   
634  C  CA  . ARG A 86  ? 0.3352 0.2259 0.1549 -0.0520 0.0096  -0.0140 86  ARG A CA  
635  C  C   . ARG A 86  ? 0.3122 0.2143 0.1641 -0.0372 0.0032  -0.0208 86  ARG A C   
636  O  O   . ARG A 86  ? 0.3244 0.2303 0.1819 -0.0403 0.0006  -0.0172 86  ARG A O   
637  C  CB  . ARG A 86  ? 0.3415 0.2301 0.1514 -0.0684 0.0102  0.0060  86  ARG A CB  
638  C  CG  . ARG A 86  ? 0.3560 0.2512 0.1656 -0.0661 0.0015  -0.0024 86  ARG A CG  
639  C  CD  . ARG A 86  ? 0.3568 0.2685 0.1724 -0.0502 -0.0078 -0.0058 86  ARG A CD  
640  N  NE  . ARG A 86  ? 0.3624 0.2732 0.1822 -0.0420 -0.0051 -0.0066 86  ARG A NE  
641  C  CZ  . ARG A 86  ? 0.3733 0.2862 0.1904 -0.0465 0.0075  -0.0084 86  ARG A CZ  
642  N  NH1 . ARG A 86  ? 0.3775 0.3033 0.1942 -0.0407 0.0142  -0.0138 86  ARG A NH1 
643  N  NH2 . ARG A 86  ? 0.3745 0.2821 0.2005 -0.0478 0.0131  -0.0003 86  ARG A NH2 
644  N  N   . LEU A 87  ? 0.2900 0.1968 0.1630 -0.0271 0.0087  -0.0327 87  LEU A N   
645  C  CA  . LEU A 87  ? 0.2814 0.2129 0.1665 -0.0234 0.0094  -0.0160 87  LEU A CA  
646  C  C   . LEU A 87  ? 0.3005 0.2061 0.1657 -0.0267 0.0186  -0.0088 87  LEU A C   
647  O  O   . LEU A 87  ? 0.2921 0.1860 0.1673 -0.0413 0.0277  -0.0171 87  LEU A O   
648  C  CB  . LEU A 87  ? 0.2629 0.2326 0.1664 -0.0350 0.0121  -0.0011 87  LEU A CB  
649  C  CG  . LEU A 87  ? 0.2553 0.2639 0.1846 -0.0228 0.0165  -0.0079 87  LEU A CG  
650  C  CD1 . LEU A 87  ? 0.2547 0.2647 0.1906 -0.0286 0.0241  -0.0238 87  LEU A CD1 
651  C  CD2 . LEU A 87  ? 0.2642 0.2909 0.1953 -0.0136 0.0195  0.0124  87  LEU A CD2 
652  N  N   . ARG A 88  ? 0.3234 0.2331 0.1725 -0.0117 0.0170  0.0029  88  ARG A N   
653  C  CA  . ARG A 88  ? 0.3492 0.2600 0.1690 -0.0072 0.0282  0.0232  88  ARG A CA  
654  C  C   . ARG A 88  ? 0.3350 0.2404 0.1368 -0.0120 0.0289  0.0306  88  ARG A C   
655  O  O   . ARG A 88  ? 0.3456 0.2795 0.1442 -0.0303 0.0156  0.0371  88  ARG A O   
656  C  CB  . ARG A 88  ? 0.4025 0.3137 0.2062 -0.0001 0.0230  0.0167  88  ARG A CB  
657  C  CG  . ARG A 88  ? 0.4668 0.3748 0.2663 0.0093  0.0253  0.0146  88  ARG A CG  
658  C  CD  . ARG A 88  ? 0.5176 0.4208 0.3217 0.0147  0.0319  0.0102  88  ARG A CD  
659  N  NE  . ARG A 88  ? 0.5586 0.4591 0.3668 0.0158  0.0407  -0.0015 88  ARG A NE  
660  C  CZ  . ARG A 88  ? 0.5845 0.4940 0.4025 0.0102  0.0461  -0.0060 88  ARG A CZ  
661  N  NH1 . ARG A 88  ? 0.5936 0.5035 0.4110 0.0042  0.0468  -0.0084 88  ARG A NH1 
662  N  NH2 . ARG A 88  ? 0.5893 0.5025 0.4126 0.0090  0.0482  -0.0141 88  ARG A NH2 
663  N  N   . ILE A 89  ? 0.3082 0.2029 0.1258 0.0072  0.0221  0.0065  89  ILE A N   
664  C  CA  . ILE A 89  ? 0.2866 0.1852 0.1258 0.0211  0.0302  0.0058  89  ILE A CA  
665  C  C   . ILE A 89  ? 0.3013 0.1857 0.1372 0.0247  0.0230  0.0105  89  ILE A C   
666  O  O   . ILE A 89  ? 0.3173 0.1738 0.1516 0.0168  0.0281  0.0070  89  ILE A O   
667  C  CB  . ILE A 89  ? 0.2766 0.1759 0.1334 0.0172  0.0344  -0.0048 89  ILE A CB  
668  C  CG1 . ILE A 89  ? 0.2635 0.1698 0.1334 0.0105  0.0509  -0.0106 89  ILE A CG1 
669  C  CG2 . ILE A 89  ? 0.2873 0.1687 0.1439 -0.0114 0.0324  0.0024  89  ILE A CG2 
670  C  CD1 . ILE A 89  ? 0.2628 0.1676 0.1316 -0.0013 0.0406  0.0035  89  ILE A CD1 
671  N  N   A SER A 90  ? 0.3040 0.1938 0.1380 0.0308  0.0280  0.0136  90  SER A N   
672  N  N   B SER A 90  ? 0.3039 0.1937 0.1386 0.0303  0.0280  0.0144  90  SER A N   
673  C  CA  A SER A 90  ? 0.3052 0.2022 0.1393 0.0292  0.0307  0.0090  90  SER A CA  
674  C  CA  B SER A 90  ? 0.3045 0.2009 0.1405 0.0286  0.0309  0.0117  90  SER A CA  
675  C  C   A SER A 90  ? 0.2972 0.1781 0.1327 0.0235  0.0278  0.0075  90  SER A C   
676  C  C   B SER A 90  ? 0.2969 0.1781 0.1327 0.0232  0.0285  0.0082  90  SER A C   
677  O  O   A SER A 90  ? 0.2934 0.1678 0.1452 0.0201  0.0233  0.0030  90  SER A O   
678  O  O   B SER A 90  ? 0.2927 0.1688 0.1444 0.0199  0.0259  0.0035  90  SER A O   
679  C  CB  A SER A 90  ? 0.3223 0.2432 0.1565 0.0266  0.0345  0.0043  90  SER A CB  
680  C  CB  B SER A 90  ? 0.3202 0.2377 0.1614 0.0251  0.0350  0.0143  90  SER A CB  
681  O  OG  A SER A 90  ? 0.3370 0.2670 0.1626 0.0238  0.0291  -0.0005 90  SER A OG  
682  O  OG  B SER A 90  ? 0.3298 0.2473 0.1693 0.0270  0.0346  0.0213  90  SER A OG  
683  N  N   . PRO A 91  ? 0.2987 0.1764 0.1322 0.0306  0.0239  0.0118  91  PRO A N   
684  C  CA  . PRO A 91  ? 0.2937 0.1692 0.1433 0.0482  0.0347  0.0260  91  PRO A CA  
685  C  C   . PRO A 91  ? 0.2790 0.1700 0.1525 0.0658  0.0394  0.0296  91  PRO A C   
686  O  O   . PRO A 91  ? 0.2798 0.1784 0.1577 0.0555  0.0343  0.0271  91  PRO A O   
687  C  CB  . PRO A 91  ? 0.3084 0.1698 0.1364 0.0435  0.0328  0.0500  91  PRO A CB  
688  C  CG  . PRO A 91  ? 0.3138 0.1905 0.1436 0.0520  0.0215  0.0451  91  PRO A CG  
689  C  CD  . PRO A 91  ? 0.3164 0.1894 0.1413 0.0477  0.0170  0.0203  91  PRO A CD  
690  N  N   . ASP A 92  ? 0.2604 0.1867 0.1691 0.0812  0.0541  0.0252  92  ASP A N   
691  C  CA  . ASP A 92  ? 0.2341 0.1962 0.1634 0.0453  0.0729  0.0269  92  ASP A CA  
692  C  C   . ASP A 92  ? 0.2281 0.1947 0.1436 0.0445  0.0724  0.0392  92  ASP A C   
693  O  O   . ASP A 92  ? 0.2311 0.2100 0.1368 0.0407  0.0592  0.0538  92  ASP A O   
694  C  CB  . ASP A 92  ? 0.2266 0.2271 0.1719 0.0344  0.0935  0.0268  92  ASP A CB  
695  C  CG  . ASP A 92  ? 0.2423 0.2584 0.1896 0.0455  0.1072  0.0245  92  ASP A CG  
696  O  OD1 . ASP A 92  ? 0.2532 0.2778 0.1899 0.0468  0.1157  0.0201  92  ASP A OD1 
697  O  OD2 . ASP A 92  ? 0.2764 0.2884 0.2110 0.0600  0.0977  0.0288  92  ASP A OD2 
698  N  N   . ARG A 93  ? 0.2169 0.1847 0.1245 0.0469  0.0835  0.0377  93  ARG A N   
699  C  CA  . ARG A 93  ? 0.2243 0.1808 0.1159 0.0402  0.0544  0.0463  93  ARG A CA  
700  C  C   . ARG A 93  ? 0.2267 0.1891 0.1267 0.0328  0.0416  0.0409  93  ARG A C   
701  O  O   . ARG A 93  ? 0.2346 0.1738 0.1384 0.0271  0.0529  0.0489  93  ARG A O   
702  C  CB  . ARG A 93  ? 0.2203 0.1973 0.1043 0.0359  0.0608  0.0482  93  ARG A CB  
703  C  CG  . ARG A 93  ? 0.2153 0.1947 0.1087 0.0347  0.0697  0.0417  93  ARG A CG  
704  C  CD  . ARG A 93  ? 0.2386 0.1964 0.1240 0.0388  0.0561  0.0404  93  ARG A CD  
705  N  NE  . ARG A 93  ? 0.2360 0.1935 0.1456 0.0341  0.0600  0.0427  93  ARG A NE  
706  C  CZ  . ARG A 93  ? 0.2521 0.2051 0.1464 0.0202  0.0483  0.0324  93  ARG A CZ  
707  N  NH1 . ARG A 93  ? 0.2652 0.2144 0.1468 0.0096  0.0470  0.0290  93  ARG A NH1 
708  N  NH2 . ARG A 93  ? 0.2663 0.2083 0.1443 0.0172  0.0297  0.0329  93  ARG A NH2 
709  N  N   . VAL A 94  ? 0.2197 0.2015 0.1246 0.0237  0.0364  0.0371  94  VAL A N   
710  C  CA  . VAL A 94  ? 0.2025 0.2003 0.1233 0.0129  0.0415  0.0415  94  VAL A CA  
711  C  C   . VAL A 94  ? 0.1988 0.1747 0.1228 0.0255  0.0398  0.0305  94  VAL A C   
712  O  O   . VAL A 94  ? 0.2147 0.1677 0.1368 0.0267  0.0488  0.0276  94  VAL A O   
713  C  CB  . VAL A 94  ? 0.1881 0.2242 0.1242 0.0044  0.0703  0.0258  94  VAL A CB  
714  C  CG1 . VAL A 94  ? 0.1863 0.2316 0.1303 0.0114  0.0878  0.0114  94  VAL A CG1 
715  C  CG2 . VAL A 94  ? 0.2062 0.2231 0.1233 0.0016  0.0560  0.0277  94  VAL A CG2 
716  N  N   . TYR A 95  ? 0.1869 0.1552 0.1136 0.0139  0.0388  0.0292  95  TYR A N   
717  C  CA  . TYR A 95  ? 0.1866 0.1591 0.1326 -0.0029 0.0388  0.0210  95  TYR A CA  
718  C  C   . TYR A 95  ? 0.2059 0.1558 0.1327 0.0122  0.0385  0.0192  95  TYR A C   
719  O  O   . TYR A 95  ? 0.2061 0.1794 0.1428 -0.0070 0.0380  0.0146  95  TYR A O   
720  C  CB  . TYR A 95  ? 0.1714 0.1622 0.1530 -0.0131 0.0536  0.0102  95  TYR A CB  
721  C  CG  . TYR A 95  ? 0.1733 0.1646 0.1701 0.0028  0.0643  0.0131  95  TYR A CG  
722  C  CD1 . TYR A 95  ? 0.1866 0.1666 0.1819 0.0123  0.0603  0.0130  95  TYR A CD1 
723  C  CD2 . TYR A 95  ? 0.1755 0.1650 0.1619 0.0063  0.0657  0.0109  95  TYR A CD2 
724  C  CE1 . TYR A 95  ? 0.2026 0.1719 0.1868 0.0070  0.0702  0.0148  95  TYR A CE1 
725  C  CE2 . TYR A 95  ? 0.1955 0.1770 0.1798 0.0218  0.0658  0.0114  95  TYR A CE2 
726  C  CZ  . TYR A 95  ? 0.1959 0.1741 0.1808 0.0150  0.0660  0.0011  95  TYR A CZ  
727  O  OH  . TYR A 95  ? 0.2248 0.1969 0.1926 -0.0007 0.0597  -0.0020 95  TYR A OH  
728  N  N   . ILE A 96  ? 0.2057 0.1489 0.1198 0.0074  0.0388  0.0242  96  ILE A N   
729  C  CA  . ILE A 96  ? 0.2059 0.1475 0.1190 0.0020  0.0273  0.0214  96  ILE A CA  
730  C  C   . ILE A 96  ? 0.2087 0.1499 0.1091 0.0129  0.0347  0.0149  96  ILE A C   
731  O  O   . ILE A 96  ? 0.2249 0.1690 0.1225 0.0231  0.0340  0.0239  96  ILE A O   
732  C  CB  . ILE A 96  ? 0.2127 0.1517 0.1190 -0.0042 0.0097  0.0150  96  ILE A CB  
733  C  CG1 . ILE A 96  ? 0.2085 0.1591 0.1131 -0.0054 0.0123  -0.0069 96  ILE A CG1 
734  C  CG2 . ILE A 96  ? 0.2089 0.1744 0.1297 -0.0014 0.0080  0.0162  96  ILE A CG2 
735  C  CD1 . ILE A 96  ? 0.2360 0.1753 0.1280 -0.0285 0.0138  -0.0092 96  ILE A CD1 
736  N  N   . ASN A 97  ? 0.1871 0.1367 0.0944 -0.0033 0.0296  0.0145  97  ASN A N   
737  C  CA  . ASN A 97  ? 0.1701 0.1299 0.1107 -0.0274 0.0251  0.0198  97  ASN A CA  
738  C  C   . ASN A 97  ? 0.1882 0.1295 0.1220 -0.0303 0.0288  -0.0072 97  ASN A C   
739  O  O   . ASN A 97  ? 0.2059 0.1244 0.1428 -0.0280 0.0397  0.0027  97  ASN A O   
740  C  CB  . ASN A 97  ? 0.1584 0.1412 0.1353 -0.0496 0.0400  0.0069  97  ASN A CB  
741  C  CG  . ASN A 97  ? 0.2009 0.1526 0.1752 -0.0415 0.0284  0.0019  97  ASN A CG  
742  O  OD1 . ASN A 97  ? 0.2070 0.1883 0.1996 -0.0535 0.0203  0.0091  97  ASN A OD1 
743  N  ND2 . ASN A 97  ? 0.2377 0.1426 0.1876 -0.0403 0.0171  -0.0127 97  ASN A ND2 
744  N  N   . TYR A 98  ? 0.2040 0.1339 0.1091 -0.0345 0.0169  0.0007  98  TYR A N   
745  C  CA  . TYR A 98  ? 0.2077 0.1371 0.1022 -0.0038 0.0293  0.0008  98  TYR A CA  
746  C  C   . TYR A 98  ? 0.2061 0.1462 0.0966 -0.0017 0.0241  -0.0001 98  TYR A C   
747  O  O   . TYR A 98  ? 0.2015 0.1619 0.1090 -0.0044 0.0201  -0.0035 98  TYR A O   
748  C  CB  . TYR A 98  ? 0.2245 0.1363 0.1051 -0.0008 0.0183  -0.0048 98  TYR A CB  
749  C  CG  . TYR A 98  ? 0.2271 0.1396 0.1038 -0.0009 0.0125  -0.0039 98  TYR A CG  
750  C  CD1 . TYR A 98  ? 0.2319 0.1399 0.1041 -0.0061 0.0064  -0.0024 98  TYR A CD1 
751  C  CD2 . TYR A 98  ? 0.2263 0.1216 0.1062 -0.0019 0.0118  -0.0064 98  TYR A CD2 
752  C  CE1 . TYR A 98  ? 0.2388 0.1432 0.0996 0.0134  0.0119  -0.0052 98  TYR A CE1 
753  C  CE2 . TYR A 98  ? 0.2460 0.1207 0.1130 -0.0053 0.0016  -0.0078 98  TYR A CE2 
754  C  CZ  . TYR A 98  ? 0.2561 0.1339 0.1133 -0.0003 0.0038  -0.0107 98  TYR A CZ  
755  O  OH  . TYR A 98  ? 0.2778 0.1491 0.1197 -0.0172 0.0019  -0.0232 98  TYR A OH  
756  N  N   . TYR A 99  ? 0.1984 0.1404 0.0822 -0.0070 0.0237  -0.0027 99  TYR A N   
757  C  CA  . TYR A 99  ? 0.1873 0.1392 0.0941 0.0003  0.0113  0.0040  99  TYR A CA  
758  C  C   . TYR A 99  ? 0.1769 0.1699 0.1020 0.0063  0.0200  0.0134  99  TYR A C   
759  O  O   . TYR A 99  ? 0.1657 0.1885 0.1174 0.0106  0.0228  0.0283  99  TYR A O   
760  C  CB  . TYR A 99  ? 0.2091 0.1315 0.1108 -0.0160 0.0090  -0.0021 99  TYR A CB  
761  C  CG  . TYR A 99  ? 0.1969 0.1244 0.1369 -0.0606 -0.0026 0.0168  99  TYR A CG  
762  C  CD1 . TYR A 99  ? 0.2102 0.1361 0.1602 -0.0454 0.0075  0.0360  99  TYR A CD1 
763  C  CD2 . TYR A 99  ? 0.2280 0.1629 0.1610 -0.0716 -0.0329 0.0168  99  TYR A CD2 
764  C  CE1 . TYR A 99  ? 0.2346 0.1514 0.1781 -0.0621 -0.0117 0.0447  99  TYR A CE1 
765  C  CE2 . TYR A 99  ? 0.2567 0.1695 0.1715 -0.0734 -0.0437 0.0312  99  TYR A CE2 
766  C  CZ  . TYR A 99  ? 0.2727 0.1670 0.1880 -0.0805 -0.0207 0.0482  99  TYR A CZ  
767  O  OH  . TYR A 99  ? 0.3227 0.2018 0.2154 -0.1024 -0.0143 0.0416  99  TYR A OH  
768  N  N   . ASP A 100 ? 0.1991 0.1599 0.1018 0.0064  0.0235  0.0116  100 ASP A N   
769  C  CA  . ASP A 100 ? 0.2068 0.1458 0.1161 -0.0065 0.0247  0.0136  100 ASP A CA  
770  C  C   . ASP A 100 ? 0.2040 0.1726 0.1179 -0.0241 0.0215  0.0076  100 ASP A C   
771  O  O   . ASP A 100 ? 0.1888 0.2138 0.1243 -0.0122 0.0145  -0.0016 100 ASP A O   
772  C  CB  . ASP A 100 ? 0.2113 0.1688 0.1463 -0.0019 0.0031  0.0359  100 ASP A CB  
773  C  CG  . ASP A 100 ? 0.2367 0.1935 0.1955 0.0023  -0.0255 0.0276  100 ASP A CG  
774  O  OD1 . ASP A 100 ? 0.2405 0.1965 0.1976 -0.0245 -0.0463 0.0200  100 ASP A OD1 
775  O  OD2 . ASP A 100 ? 0.2667 0.2217 0.2417 0.0176  -0.0235 0.0200  100 ASP A OD2 
776  N  N   . MET A 101 ? 0.1879 0.1434 0.1173 -0.0356 0.0223  0.0156  101 MET A N   
777  C  CA  . MET A 101 ? 0.1756 0.1593 0.1127 -0.0223 0.0313  0.0158  101 MET A CA  
778  C  C   . MET A 101 ? 0.1885 0.1771 0.1102 -0.0280 0.0126  0.0102  101 MET A C   
779  O  O   . MET A 101 ? 0.2113 0.1911 0.1103 -0.0438 0.0024  -0.0025 101 MET A O   
780  C  CB  . MET A 101 ? 0.1802 0.1630 0.1298 -0.0187 -0.0035 0.0182  101 MET A CB  
781  C  CG  . MET A 101 ? 0.2040 0.1662 0.1499 -0.0121 0.0208  0.0140  101 MET A CG  
782  S  SD  . MET A 101 ? 0.2228 0.1795 0.1892 0.0019  0.0400  0.0272  101 MET A SD  
783  C  CE  . MET A 101 ? 0.2230 0.1976 0.2078 -0.0068 0.0407  0.0064  101 MET A CE  
784  N  N   . ASN A 102 ? 0.1862 0.1767 0.1051 -0.0123 0.0159  0.0079  102 ASN A N   
785  C  CA  . ASN A 102 ? 0.1851 0.1959 0.1059 -0.0137 0.0152  0.0139  102 ASN A CA  
786  C  C   . ASN A 102 ? 0.1890 0.1944 0.1133 -0.0222 0.0141  0.0190  102 ASN A C   
787  O  O   . ASN A 102 ? 0.1963 0.1851 0.1019 -0.0086 0.0111  0.0062  102 ASN A O   
788  C  CB  . ASN A 102 ? 0.2128 0.2267 0.1203 -0.0049 0.0142  -0.0075 102 ASN A CB  
789  C  CG  . ASN A 102 ? 0.2684 0.2875 0.1629 -0.0028 -0.0055 -0.0189 102 ASN A CG  
790  O  OD1 . ASN A 102 ? 0.3013 0.3160 0.1953 0.0103  -0.0086 -0.0240 102 ASN A OD1 
791  N  ND2 . ASN A 102 ? 0.2636 0.3126 0.1883 -0.0191 -0.0176 -0.0224 102 ASN A ND2 
792  N  N   . ALA A 103 ? 0.1841 0.1900 0.1250 -0.0372 0.0086  0.0124  103 ALA A N   
793  C  CA  . ALA A 103 ? 0.1887 0.1687 0.1379 -0.0383 0.0088  0.0089  103 ALA A CA  
794  C  C   . ALA A 103 ? 0.1655 0.1628 0.1299 -0.0224 0.0102  0.0054  103 ALA A C   
795  O  O   . ALA A 103 ? 0.1713 0.1741 0.1445 -0.0158 0.0193  0.0209  103 ALA A O   
796  C  CB  . ALA A 103 ? 0.1863 0.1621 0.1465 -0.0587 -0.0112 0.0131  103 ALA A CB  
797  N  N   . ALA A 104 ? 0.1894 0.1876 0.1242 -0.0099 0.0231  -0.0071 104 ALA A N   
798  C  CA  . ALA A 104 ? 0.1840 0.1783 0.1314 -0.0164 0.0096  -0.0267 104 ALA A CA  
799  C  C   . ALA A 104 ? 0.1881 0.1713 0.1378 -0.0155 0.0159  -0.0122 104 ALA A C   
800  O  O   . ALA A 104 ? 0.1944 0.1719 0.1362 -0.0211 0.0193  0.0003  104 ALA A O   
801  C  CB  . ALA A 104 ? 0.1982 0.1983 0.1370 -0.0112 -0.0105 -0.0334 104 ALA A CB  
802  N  N   . ASN A 105 ? 0.1752 0.1579 0.1405 -0.0062 0.0230  0.0044  105 ASN A N   
803  C  CA  . ASN A 105 ? 0.1506 0.1645 0.1429 -0.0144 0.0366  0.0021  105 ASN A CA  
804  C  C   . ASN A 105 ? 0.1521 0.1632 0.1384 -0.0097 0.0249  0.0069  105 ASN A C   
805  O  O   . ASN A 105 ? 0.1466 0.1578 0.1456 -0.0047 0.0232  0.0136  105 ASN A O   
806  C  CB  . ASN A 105 ? 0.1592 0.1985 0.1477 -0.0001 0.0378  0.0014  105 ASN A CB  
807  C  CG  . ASN A 105 ? 0.1580 0.2127 0.1406 -0.0003 0.0183  -0.0085 105 ASN A CG  
808  O  OD1 . ASN A 105 ? 0.1617 0.2381 0.1475 -0.0096 -0.0091 -0.0198 105 ASN A OD1 
809  N  ND2 . ASN A 105 ? 0.1781 0.2220 0.1442 -0.0044 -0.0043 -0.0089 105 ASN A ND2 
810  N  N   . VAL A 106 ? 0.1536 0.1639 0.1321 -0.0098 0.0112  0.0106  106 VAL A N   
811  C  CA  . VAL A 106 ? 0.1564 0.1669 0.1219 -0.0226 0.0122  0.0079  106 VAL A CA  
812  C  C   . VAL A 106 ? 0.1738 0.1818 0.1163 -0.0217 0.0155  0.0034  106 VAL A C   
813  O  O   . VAL A 106 ? 0.2030 0.1808 0.1207 -0.0314 0.0247  0.0016  106 VAL A O   
814  C  CB  . VAL A 106 ? 0.1601 0.1763 0.1279 -0.0176 0.0022  0.0074  106 VAL A CB  
815  C  CG1 . VAL A 106 ? 0.1641 0.1826 0.1343 -0.0358 -0.0093 0.0043  106 VAL A CG1 
816  C  CG2 . VAL A 106 ? 0.1668 0.1768 0.1327 -0.0040 0.0192  0.0212  106 VAL A CG2 
817  N  N   . GLY A 107 ? 0.1413 0.1887 0.1185 0.0028  0.0128  0.0084  107 GLY A N   
818  C  CA  . GLY A 107 ? 0.1487 0.2046 0.1364 -0.0184 0.0032  0.0022  107 GLY A CA  
819  C  C   . GLY A 107 ? 0.1432 0.1905 0.1355 -0.0104 -0.0015 0.0096  107 GLY A C   
820  O  O   . GLY A 107 ? 0.1538 0.1961 0.1288 -0.0088 0.0053  0.0087  107 GLY A O   
821  N  N   . TRP A 108 ? 0.1487 0.2007 0.1420 -0.0049 -0.0014 -0.0051 108 TRP A N   
822  C  CA  . TRP A 108 ? 0.1419 0.1952 0.1536 -0.0126 0.0032  -0.0093 108 TRP A CA  
823  C  C   . TRP A 108 ? 0.1631 0.2085 0.1512 -0.0230 0.0185  0.0086  108 TRP A C   
824  O  O   . TRP A 108 ? 0.1745 0.2084 0.1595 -0.0123 0.0196  0.0227  108 TRP A O   
825  C  CB  . TRP A 108 ? 0.1713 0.1913 0.1646 -0.0239 -0.0031 0.0037  108 TRP A CB  
826  C  CG  . TRP A 108 ? 0.1894 0.1770 0.1755 -0.0330 -0.0145 0.0199  108 TRP A CG  
827  C  CD1 . TRP A 108 ? 0.2110 0.1717 0.1657 -0.0220 -0.0107 0.0109  108 TRP A CD1 
828  C  CD2 . TRP A 108 ? 0.2026 0.1965 0.1965 -0.0533 -0.0253 0.0323  108 TRP A CD2 
829  N  NE1 . TRP A 108 ? 0.2117 0.1710 0.1708 -0.0371 -0.0166 0.0288  108 TRP A NE1 
830  C  CE2 . TRP A 108 ? 0.1980 0.1923 0.1941 -0.0784 -0.0192 0.0418  108 TRP A CE2 
831  C  CE3 . TRP A 108 ? 0.2207 0.2251 0.2207 -0.0728 -0.0372 0.0422  108 TRP A CE3 
832  C  CZ2 . TRP A 108 ? 0.2134 0.2081 0.2116 -0.0933 -0.0407 0.0607  108 TRP A CZ2 
833  C  CZ3 . TRP A 108 ? 0.2369 0.2441 0.2288 -0.0851 -0.0411 0.0513  108 TRP A CZ3 
834  C  CH2 . TRP A 108 ? 0.2272 0.2320 0.2224 -0.0990 -0.0406 0.0642  108 TRP A CH2 
835  N  N   . ASN A 109 ? 0.1732 0.1968 0.1579 -0.0470 0.0245  0.0014  109 ASN A N   
836  C  CA  . ASN A 109 ? 0.1816 0.2033 0.1893 -0.0521 0.0160  0.0195  109 ASN A CA  
837  C  C   . ASN A 109 ? 0.1864 0.2144 0.1751 -0.0295 0.0178  0.0270  109 ASN A C   
838  O  O   . ASN A 109 ? 0.2144 0.2233 0.1826 -0.0097 0.0264  0.0473  109 ASN A O   
839  C  CB  . ASN A 109 ? 0.1879 0.1951 0.2331 -0.0504 0.0166  0.0386  109 ASN A CB  
840  C  CG  . ASN A 109 ? 0.2002 0.2109 0.2849 -0.0572 -0.0051 0.0496  109 ASN A CG  
841  O  OD1 . ASN A 109 ? 0.1844 0.2281 0.2858 -0.0683 0.0086  0.0510  109 ASN A OD1 
842  N  ND2 . ASN A 109 ? 0.2228 0.2341 0.3253 -0.0531 -0.0207 0.0529  109 ASN A ND2 
843  N  N   . ASN A 110 ? 0.1918 0.2273 0.1601 -0.0162 0.0122  -0.0012 110 ASN A N   
844  C  CA  . ASN A 110 ? 0.1865 0.2591 0.1581 0.0015  0.0211  0.0033  110 ASN A CA  
845  C  C   . ASN A 110 ? 0.1810 0.2556 0.1587 -0.0131 0.0360  -0.0040 110 ASN A C   
846  O  O   . ASN A 110 ? 0.1978 0.2726 0.1693 0.0006  0.0505  -0.0315 110 ASN A O   
847  C  CB  . ASN A 110 ? 0.1997 0.2914 0.1758 0.0088  0.0211  0.0183  110 ASN A CB  
848  C  CG  . ASN A 110 ? 0.2353 0.3366 0.2126 0.0107  0.0166  0.0206  110 ASN A CG  
849  O  OD1 . ASN A 110 ? 0.2565 0.3436 0.2262 0.0184  0.0148  0.0408  110 ASN A OD1 
850  N  ND2 . ASN A 110 ? 0.2642 0.3673 0.2256 0.0128  0.0030  0.0065  110 ASN A ND2 
851  N  N   . SER A 111 ? 0.1659 0.2381 0.1561 0.0032  0.0289  0.0012  111 SER A N   
852  C  CA  . SER A 111 ? 0.1550 0.2457 0.1531 0.0179  0.0357  0.0154  111 SER A CA  
853  C  C   . SER A 111 ? 0.1688 0.2150 0.1365 0.0264  0.0331  0.0188  111 SER A C   
854  O  O   . SER A 111 ? 0.1888 0.2199 0.1333 0.0174  0.0191  0.0118  111 SER A O   
855  C  CB  . SER A 111 ? 0.1705 0.2857 0.1863 0.0162  0.0260  0.0325  111 SER A CB  
856  O  OG  . SER A 111 ? 0.1930 0.3258 0.2196 -0.0014 0.0206  0.0454  111 SER A OG  
857  N  N   . THR A 112 ? 0.1905 0.2148 0.1395 -0.0003 0.0195  0.0253  112 THR A N   
858  C  CA  . THR A 112 ? 0.2050 0.1989 0.1364 -0.0077 0.0122  0.0281  112 THR A CA  
859  C  C   . THR A 112 ? 0.2068 0.1952 0.1577 -0.0125 0.0179  0.0270  112 THR A C   
860  O  O   . THR A 112 ? 0.2120 0.2178 0.1921 -0.0287 0.0293  0.0220  112 THR A O   
861  C  CB  . THR A 112 ? 0.2095 0.1944 0.1351 -0.0105 0.0050  0.0214  112 THR A CB  
862  O  OG1 . THR A 112 ? 0.2242 0.2096 0.1342 -0.0043 0.0073  0.0184  112 THR A OG1 
863  C  CG2 . THR A 112 ? 0.2041 0.1836 0.1341 -0.0212 -0.0070 -0.0045 112 THR A CG2 
864  N  N   . PHE A 113 ? 0.2014 0.1707 0.1585 -0.0099 0.0115  0.0096  113 PHE A N   
865  C  CA  . PHE A 113 ? 0.2145 0.1831 0.1807 -0.0233 0.0098  0.0031  113 PHE A CA  
866  C  C   . PHE A 113 ? 0.2193 0.1750 0.1991 -0.0226 0.0106  0.0044  113 PHE A C   
867  O  O   . PHE A 113 ? 0.2405 0.1727 0.2147 -0.0475 -0.0077 -0.0054 113 PHE A O   
868  C  CB  . PHE A 113 ? 0.2210 0.2020 0.1826 -0.0332 -0.0211 -0.0114 113 PHE A CB  
869  C  CG  . PHE A 113 ? 0.2235 0.1940 0.1964 -0.0382 -0.0534 0.0093  113 PHE A CG  
870  C  CD1 . PHE A 113 ? 0.2451 0.1986 0.2133 -0.0476 -0.0675 0.0202  113 PHE A CD1 
871  C  CD2 . PHE A 113 ? 0.2234 0.1965 0.1953 -0.0240 -0.0594 0.0086  113 PHE A CD2 
872  C  CE1 . PHE A 113 ? 0.2587 0.2016 0.2128 -0.0515 -0.0752 0.0417  113 PHE A CE1 
873  C  CE2 . PHE A 113 ? 0.2376 0.2004 0.2058 -0.0234 -0.0734 0.0156  113 PHE A CE2 
874  C  CZ  . PHE A 113 ? 0.2591 0.2065 0.2151 -0.0304 -0.0745 0.0345  113 PHE A CZ  
875  N  N   . ALA A 114 ? 0.2235 0.1720 0.1948 -0.0174 0.0245  0.0190  114 ALA A N   
876  C  CA  . ALA A 114 ? 0.2106 0.1830 0.2092 -0.0235 0.0356  0.0315  114 ALA A CA  
877  C  C   . ALA A 114 ? 0.2380 0.1977 0.2179 -0.0177 0.0541  0.0382  114 ALA A C   
878  O  O   . ALA A 114 ? 0.2541 0.2051 0.2367 -0.0220 0.0566  0.0533  114 ALA A O   
879  C  CB  . ALA A 114 ? 0.2014 0.1817 0.2170 -0.0401 0.0282  0.0279  114 ALA A CB  
880  O  OXT . ALA A 114 ? 0.2567 0.2050 0.2140 -0.0236 0.0527  0.0346  114 ALA A OXT 
881  N  N   . PRO B 1   ? 0.1675 0.2156 0.1742 0.0261  0.0674  -0.0068 1   PRO B N   
882  C  CA  . PRO B 1   ? 0.1665 0.2025 0.1710 0.0291  0.0623  -0.0063 1   PRO B CA  
883  C  C   . PRO B 1   ? 0.1969 0.1807 0.1600 0.0225  0.0456  0.0085  1   PRO B C   
884  O  O   . PRO B 1   ? 0.2202 0.1796 0.1523 0.0232  0.0453  0.0077  1   PRO B O   
885  C  CB  . PRO B 1   ? 0.1846 0.2286 0.1857 0.0258  0.0531  -0.0030 1   PRO B CB  
886  C  CG  . PRO B 1   ? 0.1835 0.2439 0.1933 0.0285  0.0517  -0.0022 1   PRO B CG  
887  C  CD  . PRO B 1   ? 0.1742 0.2395 0.1903 0.0187  0.0494  -0.0012 1   PRO B CD  
888  N  N   . MET B 2   ? 0.2019 0.1661 0.1674 0.0255  0.0438  0.0161  2   MET B N   
889  C  CA  . MET B 2   ? 0.2242 0.1699 0.1821 0.0298  0.0436  0.0024  2   MET B CA  
890  C  C   . MET B 2   ? 0.2033 0.1503 0.1598 0.0281  0.0236  0.0012  2   MET B C   
891  O  O   . MET B 2   ? 0.2117 0.1748 0.1504 0.0238  -0.0139 0.0031  2   MET B O   
892  C  CB  . MET B 2   ? 0.3034 0.2292 0.2385 -0.0024 0.0478  -0.0103 2   MET B CB  
893  C  CG  . MET B 2   ? 0.3769 0.2646 0.2788 -0.0335 0.0578  -0.0317 2   MET B CG  
894  S  SD  . MET B 2   ? 0.4493 0.3012 0.3108 -0.0646 0.0706  -0.0452 2   MET B SD  
895  C  CE  . MET B 2   ? 0.4408 0.2765 0.2946 -0.0901 0.0875  -0.0404 2   MET B CE  
896  N  N   . PHE B 3   ? 0.2116 0.1387 0.1699 0.0147  0.0369  -0.0094 3   PHE B N   
897  C  CA  . PHE B 3   ? 0.2153 0.1448 0.1738 0.0090  0.0363  -0.0136 3   PHE B CA  
898  C  C   . PHE B 3   ? 0.1912 0.1442 0.1642 0.0084  0.0332  -0.0122 3   PHE B C   
899  O  O   . PHE B 3   ? 0.2082 0.1543 0.1681 0.0108  0.0340  -0.0028 3   PHE B O   
900  C  CB  . PHE B 3   ? 0.2255 0.1762 0.1820 -0.0130 0.0498  -0.0173 3   PHE B CB  
901  C  CG  . PHE B 3   ? 0.2512 0.1757 0.1946 -0.0001 0.0586  -0.0133 3   PHE B CG  
902  C  CD1 . PHE B 3   ? 0.2512 0.1856 0.2070 -0.0149 0.0608  -0.0230 3   PHE B CD1 
903  C  CD2 . PHE B 3   ? 0.2754 0.1870 0.1976 0.0182  0.0616  -0.0127 3   PHE B CD2 
904  C  CE1 . PHE B 3   ? 0.2607 0.1846 0.2113 -0.0229 0.0643  -0.0181 3   PHE B CE1 
905  C  CE2 . PHE B 3   ? 0.2871 0.1867 0.2039 0.0036  0.0677  -0.0161 3   PHE B CE2 
906  C  CZ  . PHE B 3   ? 0.2749 0.1969 0.2129 -0.0177 0.0713  -0.0126 3   PHE B CZ  
907  N  N   . ILE B 4   ? 0.1637 0.1273 0.1676 0.0083  0.0316  -0.0125 4   ILE B N   
908  C  CA  . ILE B 4   ? 0.1800 0.1137 0.1738 0.0113  0.0324  -0.0151 4   ILE B CA  
909  C  C   . ILE B 4   ? 0.1780 0.1227 0.1632 0.0152  0.0299  -0.0159 4   ILE B C   
910  O  O   . ILE B 4   ? 0.2069 0.1501 0.1550 0.0143  0.0193  -0.0014 4   ILE B O   
911  C  CB  . ILE B 4   ? 0.1959 0.1560 0.1903 -0.0117 0.0262  -0.0180 4   ILE B CB  
912  C  CG1 . ILE B 4   ? 0.2283 0.1815 0.2132 -0.0191 0.0217  -0.0178 4   ILE B CG1 
913  C  CG2 . ILE B 4   ? 0.1861 0.1970 0.1968 -0.0031 0.0378  -0.0187 4   ILE B CG2 
914  C  CD1 . ILE B 4   ? 0.2692 0.2100 0.2222 -0.0099 0.0208  -0.0171 4   ILE B CD1 
915  N  N   . VAL B 5   ? 0.1713 0.1333 0.1861 0.0228  0.0533  -0.0180 5   VAL B N   
916  C  CA  . VAL B 5   ? 0.1793 0.1266 0.1989 0.0356  0.0478  -0.0100 5   VAL B CA  
917  C  C   . VAL B 5   ? 0.1768 0.1271 0.1837 0.0252  0.0343  -0.0063 5   VAL B C   
918  O  O   . VAL B 5   ? 0.2009 0.1555 0.1856 0.0392  0.0294  -0.0215 5   VAL B O   
919  C  CB  . VAL B 5   ? 0.2253 0.1396 0.2427 0.0183  0.0408  -0.0189 5   VAL B CB  
920  C  CG1 . VAL B 5   ? 0.2493 0.1603 0.2576 0.0025  0.0437  -0.0224 5   VAL B CG1 
921  C  CG2 . VAL B 5   ? 0.2252 0.1323 0.2578 0.0190  0.0153  -0.0282 5   VAL B CG2 
922  N  N   . ASN B 6   ? 0.1888 0.1178 0.1902 0.0093  0.0520  -0.0146 6   ASN B N   
923  C  CA  . ASN B 6   ? 0.2108 0.1274 0.1988 -0.0065 0.0469  -0.0146 6   ASN B CA  
924  C  C   . ASN B 6   ? 0.1940 0.1255 0.1929 0.0191  0.0207  -0.0268 6   ASN B C   
925  O  O   . ASN B 6   ? 0.1978 0.1432 0.1827 0.0433  0.0189  -0.0251 6   ASN B O   
926  C  CB  . ASN B 6   ? 0.2572 0.1499 0.2162 -0.0314 0.0626  -0.0125 6   ASN B CB  
927  C  CG  . ASN B 6   ? 0.3306 0.1995 0.2468 -0.0657 0.0768  -0.0068 6   ASN B CG  
928  O  OD1 . ASN B 6   ? 0.3672 0.2199 0.2243 -0.1336 0.0675  -0.0359 6   ASN B OD1 
929  N  ND2 . ASN B 6   ? 0.3643 0.2057 0.2854 -0.0474 0.1016  -0.0030 6   ASN B ND2 
930  N  N   . THR B 7   ? 0.1679 0.1137 0.1969 0.0030  0.0104  -0.0236 7   THR B N   
931  C  CA  . THR B 7   ? 0.1728 0.1199 0.2170 -0.0045 0.0254  -0.0238 7   THR B CA  
932  C  C   . THR B 7   ? 0.1738 0.1196 0.2164 -0.0086 0.0111  -0.0203 7   THR B C   
933  O  O   . THR B 7   ? 0.1730 0.0983 0.2188 -0.0155 0.0039  0.0031  7   THR B O   
934  C  CB  . THR B 7   ? 0.1660 0.1197 0.2122 -0.0116 0.0178  -0.0090 7   THR B CB  
935  O  OG1 . THR B 7   ? 0.1707 0.1243 0.2298 -0.0135 0.0041  0.0019  7   THR B OG1 
936  C  CG2 . THR B 7   ? 0.1619 0.1368 0.2079 0.0053  0.0242  -0.0190 7   THR B CG2 
937  N  N   . ASN B 8   ? 0.1768 0.1453 0.2234 0.0128  0.0160  -0.0182 8   ASN B N   
938  C  CA  . ASN B 8   ? 0.2010 0.1424 0.2324 0.0131  0.0199  -0.0312 8   ASN B CA  
939  C  C   . ASN B 8   ? 0.2240 0.1544 0.2499 0.0102  0.0222  -0.0115 8   ASN B C   
940  O  O   . ASN B 8   ? 0.2456 0.1683 0.2727 0.0036  0.0209  -0.0006 8   ASN B O   
941  C  CB  . ASN B 8   ? 0.2146 0.1603 0.2276 0.0138  0.0149  -0.0461 8   ASN B CB  
942  C  CG  . ASN B 8   ? 0.2220 0.1714 0.2284 0.0269  0.0239  -0.0443 8   ASN B CG  
943  O  OD1 . ASN B 8   ? 0.2151 0.1526 0.2242 0.0365  0.0193  -0.0389 8   ASN B OD1 
944  N  ND2 . ASN B 8   ? 0.2412 0.2040 0.2345 0.0189  0.0380  -0.0561 8   ASN B ND2 
945  N  N   . VAL B 9   ? 0.2470 0.1520 0.2563 0.0077  0.0286  -0.0044 9   VAL B N   
946  C  CA  . VAL B 9   ? 0.2695 0.1851 0.2784 -0.0007 0.0209  0.0055  9   VAL B CA  
947  C  C   . VAL B 9   ? 0.2629 0.1755 0.2928 0.0072  0.0217  0.0107  9   VAL B C   
948  O  O   . VAL B 9   ? 0.2564 0.1709 0.2848 -0.0135 0.0253  0.0016  9   VAL B O   
949  C  CB  . VAL B 9   ? 0.3076 0.2401 0.2986 -0.0264 0.0018  0.0096  9   VAL B CB  
950  C  CG1 . VAL B 9   ? 0.3315 0.2679 0.3154 -0.0171 0.0008  0.0051  9   VAL B CG1 
951  C  CG2 . VAL B 9   ? 0.3253 0.2315 0.3000 -0.0248 -0.0041 -0.0043 9   VAL B CG2 
952  N  N   . PRO B 10  ? 0.2807 0.1902 0.3151 0.0183  0.0190  0.0124  10  PRO B N   
953  C  CA  . PRO B 10  ? 0.2836 0.2050 0.3198 0.0364  0.0219  0.0233  10  PRO B CA  
954  C  C   . PRO B 10  ? 0.2757 0.2024 0.3142 0.0352  0.0443  0.0350  10  PRO B C   
955  O  O   . PRO B 10  ? 0.2860 0.1936 0.3060 0.0294  0.0620  0.0280  10  PRO B O   
956  C  CB  . PRO B 10  ? 0.2959 0.2120 0.3309 0.0352  0.0054  0.0254  10  PRO B CB  
957  C  CG  . PRO B 10  ? 0.3028 0.1965 0.3366 0.0227  0.0020  0.0236  10  PRO B CG  
958  C  CD  . PRO B 10  ? 0.2934 0.1813 0.3267 0.0302  0.0128  0.0209  10  PRO B CD  
959  N  N   . ARG B 11  ? 0.2886 0.2104 0.3288 0.0343  0.0504  0.0450  11  ARG B N   
960  C  CA  . ARG B 11  ? 0.3127 0.2391 0.3398 0.0395  0.0451  0.0521  11  ARG B CA  
961  C  C   . ARG B 11  ? 0.3186 0.2337 0.3390 0.0450  0.0395  0.0710  11  ARG B C   
962  O  O   . ARG B 11  ? 0.3319 0.2486 0.3293 0.0327  0.0557  0.0689  11  ARG B O   
963  C  CB  . ARG B 11  ? 0.3352 0.2683 0.3589 0.0429  0.0377  0.0415  11  ARG B CB  
964  C  CG  . ARG B 11  ? 0.3672 0.3131 0.3846 0.0429  0.0359  0.0418  11  ARG B CG  
965  C  CD  . ARG B 11  ? 0.3952 0.3412 0.4075 0.0451  0.0401  0.0395  11  ARG B CD  
966  N  NE  . ARG B 11  ? 0.4178 0.3643 0.4296 0.0517  0.0391  0.0359  11  ARG B NE  
967  C  CZ  . ARG B 11  ? 0.4339 0.3841 0.4492 0.0475  0.0402  0.0296  11  ARG B CZ  
968  N  NH1 . ARG B 11  ? 0.4369 0.3885 0.4583 0.0428  0.0403  0.0275  11  ARG B NH1 
969  N  NH2 . ARG B 11  ? 0.4476 0.3932 0.4566 0.0452  0.0391  0.0301  11  ARG B NH2 
970  N  N   . ALA B 12  ? 0.3235 0.2213 0.3510 0.0377  0.0394  0.0832  12  ALA B N   
971  C  CA  . ALA B 12  ? 0.3229 0.2223 0.3708 0.0293  0.0320  0.0892  12  ALA B CA  
972  C  C   . ALA B 12  ? 0.3238 0.2363 0.3908 0.0155  0.0395  0.0708  12  ALA B C   
973  O  O   . ALA B 12  ? 0.3403 0.2601 0.3998 0.0102  0.0376  0.0632  12  ALA B O   
974  C  CB  . ALA B 12  ? 0.3234 0.2133 0.3722 0.0379  0.0225  0.1047  12  ALA B CB  
975  N  N   . SER B 13  ? 0.3162 0.2291 0.4011 0.0202  0.0388  0.0552  13  SER B N   
976  C  CA  . SER B 13  ? 0.3232 0.2462 0.4192 -0.0032 0.0385  0.0397  13  SER B CA  
977  C  C   . SER B 13  ? 0.3003 0.2430 0.4194 -0.0117 0.0330  0.0381  13  SER B C   
978  O  O   . SER B 13  ? 0.2858 0.2575 0.4239 -0.0072 0.0382  0.0305  13  SER B O   
979  C  CB  . SER B 13  ? 0.3524 0.2798 0.4371 0.0040  0.0352  0.0217  13  SER B CB  
980  O  OG  . SER B 13  ? 0.3802 0.3261 0.4539 -0.0032 0.0351  0.0185  13  SER B OG  
981  N  N   . VAL B 14  ? 0.2842 0.2154 0.4133 -0.0106 0.0296  0.0462  14  VAL B N   
982  C  CA  . VAL B 14  ? 0.2765 0.2284 0.4090 0.0016  0.0278  0.0389  14  VAL B CA  
983  C  C   . VAL B 14  ? 0.2944 0.2571 0.4110 -0.0057 0.0262  0.0550  14  VAL B C   
984  O  O   . VAL B 14  ? 0.3174 0.2796 0.4140 -0.0221 0.0280  0.0465  14  VAL B O   
985  C  CB  . VAL B 14  ? 0.2708 0.2209 0.4052 0.0078  0.0275  0.0186  14  VAL B CB  
986  C  CG1 . VAL B 14  ? 0.2724 0.2142 0.4061 0.0204  0.0199  0.0135  14  VAL B CG1 
987  C  CG2 . VAL B 14  ? 0.2678 0.2229 0.3984 0.0056  0.0311  0.0096  14  VAL B CG2 
988  N  N   . PRO B 15  ? 0.2913 0.2659 0.4099 -0.0211 0.0348  0.0785  15  PRO B N   
989  C  CA  . PRO B 15  ? 0.2940 0.2782 0.4087 -0.0318 0.0375  0.0928  15  PRO B CA  
990  C  C   . PRO B 15  ? 0.3248 0.2900 0.4022 -0.0119 0.0419  0.0958  15  PRO B C   
991  O  O   . PRO B 15  ? 0.3248 0.2907 0.3942 -0.0075 0.0344  0.0970  15  PRO B O   
992  C  CB  . PRO B 15  ? 0.2794 0.2875 0.4154 -0.0387 0.0368  0.0974  15  PRO B CB  
993  C  CG  . PRO B 15  ? 0.2824 0.2878 0.4199 -0.0471 0.0387  0.0974  15  PRO B CG  
994  C  CD  . PRO B 15  ? 0.2839 0.2763 0.4169 -0.0379 0.0406  0.0837  15  PRO B CD  
995  N  N   . ASP B 16  ? 0.3568 0.3092 0.4097 0.0025  0.0415  0.0985  16  ASP B N   
996  C  CA  . ASP B 16  ? 0.3863 0.3416 0.4260 0.0075  0.0412  0.0957  16  ASP B CA  
997  C  C   . ASP B 16  ? 0.3822 0.3305 0.4157 -0.0032 0.0456  0.0828  16  ASP B C   
998  O  O   . ASP B 16  ? 0.3885 0.3353 0.4245 -0.0181 0.0427  0.0799  16  ASP B O   
999  C  CB  . ASP B 16  ? 0.4206 0.3899 0.4556 0.0120  0.0336  0.0970  16  ASP B CB  
1000 C  CG  . ASP B 16  ? 0.4530 0.4318 0.4827 0.0149  0.0261  0.1002  16  ASP B CG  
1001 O  OD1 . ASP B 16  ? 0.4659 0.4502 0.4921 0.0129  0.0203  0.0975  16  ASP B OD1 
1002 O  OD2 . ASP B 16  ? 0.4689 0.4478 0.4983 0.0211  0.0192  0.0986  16  ASP B OD2 
1003 N  N   . GLY B 17  ? 0.3616 0.3027 0.3946 -0.0009 0.0585  0.0871  17  GLY B N   
1004 C  CA  . GLY B 17  ? 0.3210 0.2819 0.3704 -0.0082 0.0779  0.0900  17  GLY B CA  
1005 C  C   . GLY B 17  ? 0.2934 0.2432 0.3511 -0.0220 0.0786  0.0886  17  GLY B C   
1006 O  O   . GLY B 17  ? 0.2661 0.2468 0.3540 -0.0236 0.0911  0.0872  17  GLY B O   
1007 N  N   . PHE B 18  ? 0.2789 0.2095 0.3279 -0.0206 0.0762  0.0725  18  PHE B N   
1008 C  CA  . PHE B 18  ? 0.2784 0.1978 0.3124 -0.0147 0.0746  0.0537  18  PHE B CA  
1009 C  C   . PHE B 18  ? 0.2685 0.1914 0.2975 -0.0155 0.0797  0.0496  18  PHE B C   
1010 O  O   . PHE B 18  ? 0.2594 0.1657 0.2779 0.0091  0.0856  0.0394  18  PHE B O   
1011 C  CB  . PHE B 18  ? 0.2834 0.2040 0.3128 -0.0022 0.0742  0.0536  18  PHE B CB  
1012 C  CG  . PHE B 18  ? 0.2940 0.1995 0.3178 0.0081  0.0673  0.0473  18  PHE B CG  
1013 C  CD1 . PHE B 18  ? 0.3048 0.2000 0.3224 0.0169  0.0590  0.0441  18  PHE B CD1 
1014 C  CD2 . PHE B 18  ? 0.2896 0.1984 0.3172 0.0163  0.0749  0.0455  18  PHE B CD2 
1015 C  CE1 . PHE B 18  ? 0.3142 0.2031 0.3257 0.0216  0.0589  0.0346  18  PHE B CE1 
1016 C  CE2 . PHE B 18  ? 0.2987 0.2030 0.3198 0.0325  0.0730  0.0396  18  PHE B CE2 
1017 C  CZ  . PHE B 18  ? 0.3088 0.2088 0.3206 0.0341  0.0676  0.0372  18  PHE B CZ  
1018 N  N   . LEU B 19  ? 0.2656 0.1990 0.2960 -0.0128 0.0793  0.0498  19  LEU B N   
1019 C  CA  . LEU B 19  ? 0.2566 0.1964 0.2943 -0.0142 0.0894  0.0458  19  LEU B CA  
1020 C  C   . LEU B 19  ? 0.2575 0.1917 0.2796 0.0167  0.1035  0.0361  19  LEU B C   
1021 O  O   . LEU B 19  ? 0.2641 0.1734 0.2700 0.0413  0.1036  0.0247  19  LEU B O   
1022 C  CB  . LEU B 19  ? 0.2583 0.2150 0.3129 -0.0265 0.0883  0.0433  19  LEU B CB  
1023 C  CG  . LEU B 19  ? 0.2468 0.2271 0.3269 -0.0420 0.0931  0.0389  19  LEU B CG  
1024 C  CD1 . LEU B 19  ? 0.2500 0.2469 0.3362 -0.0390 0.0808  0.0285  19  LEU B CD1 
1025 C  CD2 . LEU B 19  ? 0.2492 0.2454 0.3307 -0.0364 0.0950  0.0450  19  LEU B CD2 
1026 N  N   . SER B 20  ? 0.2474 0.2158 0.2853 0.0041  0.1082  0.0288  20  SER B N   
1027 C  CA  . SER B 20  ? 0.2595 0.2443 0.2995 0.0070  0.1146  0.0230  20  SER B CA  
1028 C  C   . SER B 20  ? 0.2546 0.2293 0.3124 -0.0055 0.1101  0.0270  20  SER B C   
1029 O  O   . SER B 20  ? 0.2396 0.2359 0.3119 -0.0005 0.1225  0.0212  20  SER B O   
1030 C  CB  . SER B 20  ? 0.2975 0.2984 0.3139 0.0024  0.1122  0.0162  20  SER B CB  
1031 O  OG  . SER B 20  ? 0.3227 0.3472 0.3414 0.0086  0.1014  0.0148  20  SER B OG  
1032 N  N   . GLU B 21  ? 0.2647 0.2192 0.3266 -0.0268 0.0916  0.0311  21  GLU B N   
1033 C  CA  . GLU B 21  ? 0.2609 0.2133 0.3354 -0.0391 0.0804  0.0381  21  GLU B CA  
1034 C  C   . GLU B 21  ? 0.2456 0.1975 0.3145 -0.0351 0.0683  0.0355  21  GLU B C   
1035 O  O   . GLU B 21  ? 0.2605 0.2156 0.3165 -0.0378 0.0476  0.0248  21  GLU B O   
1036 C  CB  . GLU B 21  ? 0.2754 0.2160 0.3750 -0.0795 0.0716  0.0299  21  GLU B CB  
1037 C  CG  . GLU B 21  ? 0.2973 0.2296 0.4118 -0.0769 0.0507  0.0199  21  GLU B CG  
1038 C  CD  . GLU B 21  ? 0.3092 0.2493 0.4447 -0.0740 0.0415  0.0220  21  GLU B CD  
1039 O  OE1 . GLU B 21  ? 0.3188 0.2519 0.4576 -0.0718 0.0471  0.0282  21  GLU B OE1 
1040 O  OE2 . GLU B 21  ? 0.3103 0.2608 0.4572 -0.0684 0.0289  0.0245  21  GLU B OE2 
1041 N  N   . LEU B 22  ? 0.2241 0.1872 0.2938 -0.0109 0.0768  0.0330  22  LEU B N   
1042 C  CA  . LEU B 22  ? 0.2018 0.1818 0.2875 -0.0048 0.0883  0.0302  22  LEU B CA  
1043 C  C   . LEU B 22  ? 0.1995 0.1839 0.2901 0.0157  0.0834  0.0165  22  LEU B C   
1044 O  O   . LEU B 22  ? 0.2178 0.1955 0.2846 0.0112  0.0851  0.0193  22  LEU B O   
1045 C  CB  . LEU B 22  ? 0.1990 0.1899 0.2949 -0.0118 0.0991  0.0261  22  LEU B CB  
1046 C  CG  . LEU B 22  ? 0.2181 0.2138 0.3070 0.0077  0.0930  0.0228  22  LEU B CG  
1047 C  CD1 . LEU B 22  ? 0.2298 0.2266 0.3164 0.0245  0.0900  0.0258  22  LEU B CD1 
1048 C  CD2 . LEU B 22  ? 0.2257 0.2314 0.3111 0.0236  0.0878  0.0212  22  LEU B CD2 
1049 N  N   . THR B 23  ? 0.1993 0.1694 0.2941 0.0118  0.0844  0.0109  23  THR B N   
1050 C  CA  . THR B 23  ? 0.2094 0.1678 0.2931 0.0189  0.0751  0.0111  23  THR B CA  
1051 C  C   . THR B 23  ? 0.2152 0.1692 0.2793 0.0055  0.0910  0.0231  23  THR B C   
1052 O  O   . THR B 23  ? 0.2230 0.1760 0.2718 0.0209  0.0781  0.0189  23  THR B O   
1053 C  CB  . THR B 23  ? 0.2199 0.1531 0.2974 0.0272  0.0647  0.0085  23  THR B CB  
1054 O  OG1 . THR B 23  ? 0.2217 0.1514 0.3039 0.0229  0.0596  -0.0033 23  THR B OG1 
1055 C  CG2 . THR B 23  ? 0.2275 0.1512 0.3000 0.0393  0.0567  0.0022  23  THR B CG2 
1056 N  N   . GLN B 24  ? 0.2429 0.1762 0.2852 -0.0181 0.0808  0.0449  24  GLN B N   
1057 C  CA  . GLN B 24  ? 0.2618 0.2207 0.2999 -0.0032 0.0783  0.0539  24  GLN B CA  
1058 C  C   . GLN B 24  ? 0.2510 0.2146 0.2927 0.0097  0.0799  0.0412  24  GLN B C   
1059 O  O   . GLN B 24  ? 0.2540 0.2269 0.2818 0.0130  0.0746  0.0397  24  GLN B O   
1060 C  CB  . GLN B 24  ? 0.3001 0.2644 0.3302 -0.0060 0.0778  0.0630  24  GLN B CB  
1061 C  CG  . GLN B 24  ? 0.3357 0.3109 0.3620 -0.0018 0.0805  0.0570  24  GLN B CG  
1062 C  CD  . GLN B 24  ? 0.3679 0.3571 0.3855 -0.0025 0.0894  0.0625  24  GLN B CD  
1063 O  OE1 . GLN B 24  ? 0.3930 0.3906 0.4001 0.0005  0.0943  0.0623  24  GLN B OE1 
1064 N  NE2 . GLN B 24  ? 0.3846 0.3588 0.3884 0.0021  0.0914  0.0569  24  GLN B NE2 
1065 N  N   . GLN B 25  ? 0.2460 0.1999 0.2948 0.0025  0.0791  0.0339  25  GLN B N   
1066 C  CA  . GLN B 25  ? 0.2439 0.1945 0.3070 -0.0031 0.0542  0.0325  25  GLN B CA  
1067 C  C   . GLN B 25  ? 0.2188 0.1926 0.2966 0.0000  0.0596  0.0292  25  GLN B C   
1068 O  O   . GLN B 25  ? 0.1983 0.1857 0.3112 0.0156  0.0624  0.0230  25  GLN B O   
1069 C  CB  . GLN B 25  ? 0.2678 0.2016 0.3262 -0.0153 0.0322  0.0415  25  GLN B CB  
1070 C  CG  . GLN B 25  ? 0.2937 0.2246 0.3467 -0.0442 0.0188  0.0437  25  GLN B CG  
1071 C  CD  . GLN B 25  ? 0.3323 0.2756 0.3720 -0.0673 0.0057  0.0548  25  GLN B CD  
1072 O  OE1 . GLN B 25  ? 0.3451 0.3000 0.3860 -0.0754 -0.0027 0.0501  25  GLN B OE1 
1073 N  NE2 . GLN B 25  ? 0.3445 0.2987 0.3810 -0.0646 0.0001  0.0578  25  GLN B NE2 
1074 N  N   . LEU B 26  ? 0.2210 0.1892 0.2777 -0.0041 0.0750  0.0190  26  LEU B N   
1075 C  CA  . LEU B 26  ? 0.1998 0.1851 0.2636 -0.0047 0.0712  0.0171  26  LEU B CA  
1076 C  C   . LEU B 26  ? 0.2146 0.2037 0.2493 0.0094  0.0796  0.0182  26  LEU B C   
1077 O  O   . LEU B 26  ? 0.2383 0.2141 0.2506 0.0095  0.0699  0.0118  26  LEU B O   
1078 C  CB  . LEU B 26  ? 0.1916 0.1945 0.2516 -0.0177 0.0806  0.0049  26  LEU B CB  
1079 C  CG  . LEU B 26  ? 0.2042 0.2139 0.2440 -0.0103 0.0814  -0.0035 26  LEU B CG  
1080 C  CD1 . LEU B 26  ? 0.2136 0.2211 0.2688 -0.0268 0.0867  -0.0097 26  LEU B CD1 
1081 C  CD2 . LEU B 26  ? 0.2214 0.2436 0.2254 -0.0014 0.0937  -0.0052 26  LEU B CD2 
1082 N  N   . ALA B 27  ? 0.2107 0.2113 0.2325 0.0245  0.0924  0.0239  27  ALA B N   
1083 C  CA  . ALA B 27  ? 0.2400 0.2420 0.2314 0.0217  0.0912  0.0291  27  ALA B CA  
1084 C  C   . ALA B 27  ? 0.2331 0.2653 0.2433 0.0194  0.0833  0.0379  27  ALA B C   
1085 O  O   . ALA B 27  ? 0.2468 0.2763 0.2361 0.0196  0.0690  0.0439  27  ALA B O   
1086 C  CB  . ALA B 27  ? 0.2476 0.2366 0.2235 0.0212  0.1007  0.0341  27  ALA B CB  
1087 N  N   . GLN B 28  ? 0.2399 0.2749 0.2632 0.0289  0.0719  0.0351  28  GLN B N   
1088 C  CA  . GLN B 28  ? 0.2678 0.3026 0.2976 0.0181  0.0508  0.0347  28  GLN B CA  
1089 C  C   . GLN B 28  ? 0.2425 0.3000 0.2950 0.0286  0.0595  0.0351  28  GLN B C   
1090 O  O   . GLN B 28  ? 0.2559 0.3248 0.3027 0.0370  0.0608  0.0482  28  GLN B O   
1091 C  CB  . GLN B 28  ? 0.3209 0.3354 0.3298 0.0102  0.0295  0.0256  28  GLN B CB  
1092 C  CG  . GLN B 28  ? 0.3637 0.3722 0.3664 0.0039  0.0104  0.0104  28  GLN B CG  
1093 C  CD  . GLN B 28  ? 0.3920 0.3935 0.3885 -0.0034 -0.0037 0.0041  28  GLN B CD  
1094 O  OE1 . GLN B 28  ? 0.4087 0.4028 0.4037 -0.0045 -0.0156 -0.0067 28  GLN B OE1 
1095 N  NE2 . GLN B 28  ? 0.3943 0.4015 0.3960 0.0012  0.0014  0.0087  28  GLN B NE2 
1096 N  N   . ALA B 29  ? 0.2286 0.2769 0.2863 0.0200  0.0723  0.0243  29  ALA B N   
1097 C  CA  . ALA B 29  ? 0.2132 0.2604 0.2787 0.0322  0.0781  0.0167  29  ALA B CA  
1098 C  C   . ALA B 29  ? 0.2237 0.2587 0.2757 0.0123  0.0679  0.0230  29  ALA B C   
1099 O  O   . ALA B 29  ? 0.2244 0.2569 0.2727 0.0038  0.0685  0.0323  29  ALA B O   
1100 C  CB  . ALA B 29  ? 0.2164 0.2495 0.2812 0.0611  0.0813  0.0011  29  ALA B CB  
1101 N  N   . THR B 30  ? 0.2285 0.2561 0.2754 0.0254  0.0453  0.0207  30  THR B N   
1102 C  CA  . THR B 30  ? 0.2385 0.2556 0.2679 0.0268  0.0416  0.0222  30  THR B CA  
1103 C  C   . THR B 30  ? 0.2487 0.2549 0.2669 0.0339  0.0467  0.0336  30  THR B C   
1104 O  O   . THR B 30  ? 0.2750 0.2649 0.2716 0.0612  0.0528  0.0481  30  THR B O   
1105 C  CB  . THR B 30  ? 0.2391 0.2514 0.2589 0.0326  0.0321  0.0201  30  THR B CB  
1106 O  OG1 . THR B 30  ? 0.2297 0.2346 0.2471 0.0631  0.0385  0.0286  30  THR B OG1 
1107 C  CG2 . THR B 30  ? 0.2463 0.2697 0.2680 0.0210  0.0344  0.0140  30  THR B CG2 
1108 N  N   . GLY B 31  ? 0.2413 0.2426 0.2593 0.0173  0.0383  0.0182  31  GLY B N   
1109 C  CA  . GLY B 31  ? 0.2159 0.2291 0.2617 0.0300  0.0343  0.0139  31  GLY B CA  
1110 C  C   . GLY B 31  ? 0.2236 0.2380 0.2678 0.0397  0.0506  0.0040  31  GLY B C   
1111 O  O   . GLY B 31  ? 0.2382 0.2766 0.2723 0.0500  0.0699  -0.0191 31  GLY B O   
1112 N  N   . LYS B 32  ? 0.2133 0.2175 0.2695 0.0179  0.0552  0.0142  32  LYS B N   
1113 C  CA  . LYS B 32  ? 0.2166 0.1986 0.2632 0.0088  0.0580  0.0254  32  LYS B CA  
1114 C  C   . LYS B 32  ? 0.2376 0.1801 0.2819 0.0215  0.0608  0.0355  32  LYS B C   
1115 O  O   . LYS B 32  ? 0.2613 0.1795 0.2866 0.0359  0.0784  0.0494  32  LYS B O   
1116 C  CB  . LYS B 32  ? 0.2399 0.2003 0.2508 -0.0041 0.0498  0.0286  32  LYS B CB  
1117 C  CG  . LYS B 32  ? 0.2811 0.2060 0.2403 0.0002  0.0321  0.0208  32  LYS B CG  
1118 C  CD  . LYS B 32  ? 0.3015 0.1981 0.2267 0.0134  0.0252  0.0235  32  LYS B CD  
1119 C  CE  . LYS B 32  ? 0.3057 0.1844 0.2128 0.0342  0.0254  0.0233  32  LYS B CE  
1120 N  NZ  . LYS B 32  ? 0.3075 0.1757 0.2110 0.0490  0.0231  0.0147  32  LYS B NZ  
1121 N  N   . PRO B 33  ? 0.2336 0.1643 0.2926 0.0251  0.0439  0.0289  33  PRO B N   
1122 C  CA  . PRO B 33  ? 0.2248 0.1603 0.2904 0.0245  0.0510  0.0282  33  PRO B CA  
1123 C  C   . PRO B 33  ? 0.2062 0.1396 0.2673 0.0118  0.0597  0.0257  33  PRO B C   
1124 O  O   . PRO B 33  ? 0.1942 0.1504 0.2591 -0.0009 0.0651  0.0083  33  PRO B O   
1125 C  CB  . PRO B 33  ? 0.2203 0.1497 0.3019 0.0514  0.0390  0.0244  33  PRO B CB  
1126 C  CG  . PRO B 33  ? 0.2279 0.1601 0.3074 0.0459  0.0281  0.0212  33  PRO B CG  
1127 C  CD  . PRO B 33  ? 0.2367 0.1607 0.3047 0.0324  0.0302  0.0226  33  PRO B CD  
1128 N  N   . PRO B 34  ? 0.2146 0.1465 0.2613 0.0254  0.0668  0.0308  34  PRO B N   
1129 C  CA  . PRO B 34  ? 0.2130 0.1452 0.2551 0.0265  0.0688  0.0366  34  PRO B CA  
1130 C  C   . PRO B 34  ? 0.1926 0.1450 0.2239 0.0393  0.0873  0.0347  34  PRO B C   
1131 O  O   . PRO B 34  ? 0.1920 0.1709 0.2148 0.0555  0.0898  0.0364  34  PRO B O   
1132 C  CB  . PRO B 34  ? 0.2253 0.1640 0.2720 0.0196  0.0671  0.0416  34  PRO B CB  
1133 C  CG  . PRO B 34  ? 0.2185 0.1765 0.2696 0.0360  0.0739  0.0353  34  PRO B CG  
1134 C  CD  . PRO B 34  ? 0.2140 0.1558 0.2625 0.0368  0.0734  0.0225  34  PRO B CD  
1135 N  N   . GLN B 35  ? 0.2023 0.1216 0.1935 0.0184  0.0966  0.0302  35  GLN B N   
1136 C  CA  . GLN B 35  ? 0.2225 0.1566 0.1872 0.0248  0.0829  0.0276  35  GLN B CA  
1137 C  C   . GLN B 35  ? 0.2269 0.1821 0.1750 0.0147  0.0669  0.0317  35  GLN B C   
1138 O  O   . GLN B 35  ? 0.2568 0.1972 0.1705 -0.0096 0.0534  0.0308  35  GLN B O   
1139 C  CB  . GLN B 35  ? 0.2348 0.1800 0.1852 0.0402  0.1009  0.0315  35  GLN B CB  
1140 C  CG  . GLN B 35  ? 0.2775 0.2129 0.2055 0.0499  0.1097  0.0444  35  GLN B CG  
1141 C  CD  . GLN B 35  ? 0.2980 0.2116 0.2260 0.0589  0.1172  0.0481  35  GLN B CD  
1142 O  OE1 . GLN B 35  ? 0.2989 0.2011 0.2340 0.0581  0.1136  0.0264  35  GLN B OE1 
1143 N  NE2 . GLN B 35  ? 0.3211 0.2295 0.2379 0.0493  0.1198  0.0481  35  GLN B NE2 
1144 N  N   . TYR B 36  ? 0.2093 0.1657 0.1636 0.0122  0.0629  0.0352  36  TYR B N   
1145 C  CA  . TYR B 36  ? 0.2073 0.1557 0.1728 0.0194  0.0716  0.0295  36  TYR B CA  
1146 C  C   . TYR B 36  ? 0.2148 0.1546 0.1898 0.0270  0.0880  0.0231  36  TYR B C   
1147 O  O   . TYR B 36  ? 0.2456 0.1706 0.1901 0.0056  0.0964  0.0205  36  TYR B O   
1148 C  CB  . TYR B 36  ? 0.2090 0.1622 0.1886 0.0253  0.0831  0.0240  36  TYR B CB  
1149 C  CG  . TYR B 36  ? 0.2250 0.1755 0.1803 0.0381  0.0995  0.0138  36  TYR B CG  
1150 C  CD1 . TYR B 36  ? 0.2374 0.1864 0.1784 0.0630  0.1087  0.0354  36  TYR B CD1 
1151 C  CD2 . TYR B 36  ? 0.2469 0.1798 0.1868 0.0591  0.1053  -0.0092 36  TYR B CD2 
1152 C  CE1 . TYR B 36  ? 0.2702 0.1992 0.1962 0.0721  0.1037  0.0336  36  TYR B CE1 
1153 C  CE2 . TYR B 36  ? 0.2784 0.1974 0.2073 0.0756  0.1086  -0.0161 36  TYR B CE2 
1154 C  CZ  . TYR B 36  ? 0.2964 0.2101 0.2153 0.0825  0.1083  -0.0029 36  TYR B CZ  
1155 O  OH  . TYR B 36  ? 0.3187 0.2368 0.2412 0.0985  0.1130  -0.0125 36  TYR B OH  
1156 N  N   A ILE B 37  ? 0.2052 0.1681 0.2062 0.0465  0.0775  0.0164  37  ILE B N   
1157 N  N   B ILE B 37  ? 0.1987 0.1639 0.2008 0.0559  0.0828  0.0169  37  ILE B N   
1158 C  CA  A ILE B 37  ? 0.2255 0.2044 0.2327 0.0346  0.0612  0.0055  37  ILE B CA  
1159 C  CA  B ILE B 37  ? 0.2203 0.1996 0.2291 0.0387  0.0657  0.0044  37  ILE B CA  
1160 C  C   A ILE B 37  ? 0.1916 0.1702 0.1912 0.0268  0.0658  0.0036  37  ILE B C   
1161 C  C   B ILE B 37  ? 0.1911 0.1669 0.1881 0.0250  0.0670  0.0043  37  ILE B C   
1162 O  O   A ILE B 37  ? 0.1910 0.1639 0.1707 0.0252  0.0600  0.0059  37  ILE B O   
1163 O  O   B ILE B 37  ? 0.1927 0.1629 0.1648 0.0263  0.0566  0.0054  37  ILE B O   
1164 C  CB  A ILE B 37  ? 0.3009 0.2892 0.2999 0.0210  0.0315  -0.0034 37  ILE B CB  
1165 C  CB  B ILE B 37  ? 0.2965 0.2825 0.2948 0.0208  0.0331  -0.0043 37  ILE B CB  
1166 C  CG1 A ILE B 37  ? 0.3432 0.3397 0.3377 0.0137  0.0157  -0.0050 37  ILE B CG1 
1167 C  CG1 B ILE B 37  ? 0.3407 0.3338 0.3311 0.0111  0.0191  -0.0027 37  ILE B CG1 
1168 C  CG2 A ILE B 37  ? 0.3270 0.3187 0.3188 0.0129  0.0249  -0.0073 37  ILE B CG2 
1169 C  CG2 B ILE B 37  ? 0.3244 0.3145 0.3159 0.0124  0.0271  -0.0104 37  ILE B CG2 
1170 C  CD1 A ILE B 37  ? 0.3666 0.3648 0.3573 0.0093  0.0064  -0.0050 37  ILE B CD1 
1171 C  CD1 B ILE B 37  ? 0.3617 0.3583 0.3491 0.0037  0.0092  -0.0026 37  ILE B CD1 
1172 N  N   . ALA B 38  ? 0.1694 0.1542 0.1754 0.0302  0.0764  -0.0058 38  ALA B N   
1173 C  CA  . ALA B 38  ? 0.1582 0.1561 0.1814 0.0282  0.0699  -0.0027 38  ALA B CA  
1174 C  C   . ALA B 38  ? 0.1631 0.1727 0.1631 0.0244  0.0678  0.0029  38  ALA B C   
1175 O  O   . ALA B 38  ? 0.1755 0.1817 0.1606 0.0389  0.0608  0.0021  38  ALA B O   
1176 C  CB  . ALA B 38  ? 0.1665 0.1670 0.1920 0.0212  0.0630  0.0085  38  ALA B CB  
1177 N  N   . VAL B 39  ? 0.1690 0.1498 0.1530 0.0346  0.0681  -0.0034 39  VAL B N   
1178 C  CA  . VAL B 39  ? 0.1580 0.1670 0.1557 0.0300  0.0593  0.0058  39  VAL B CA  
1179 C  C   . VAL B 39  ? 0.1531 0.1765 0.1457 0.0367  0.0431  0.0101  39  VAL B C   
1180 O  O   . VAL B 39  ? 0.1602 0.2034 0.1548 0.0264  0.0453  -0.0010 39  VAL B O   
1181 C  CB  . VAL B 39  ? 0.1924 0.1729 0.1779 0.0034  0.0304  0.0017  39  VAL B CB  
1182 C  CG1 . VAL B 39  ? 0.1842 0.1876 0.1837 0.0057  0.0312  -0.0099 39  VAL B CG1 
1183 C  CG2 . VAL B 39  ? 0.2315 0.1927 0.1946 -0.0235 0.0161  0.0102  39  VAL B CG2 
1184 N  N   . HIS B 40  ? 0.1549 0.1644 0.1629 0.0230  0.0420  0.0006  40  HIS B N   
1185 C  CA  . HIS B 40  ? 0.1658 0.1412 0.1641 0.0018  0.0268  -0.0143 40  HIS B CA  
1186 C  C   . HIS B 40  ? 0.1588 0.1292 0.1658 0.0111  0.0167  -0.0040 40  HIS B C   
1187 O  O   . HIS B 40  ? 0.1934 0.1471 0.1736 0.0168  0.0078  -0.0001 40  HIS B O   
1188 C  CB  . HIS B 40  ? 0.1741 0.1520 0.1678 -0.0074 0.0331  -0.0117 40  HIS B CB  
1189 C  CG  . HIS B 40  ? 0.1740 0.1624 0.1666 -0.0137 0.0327  -0.0252 40  HIS B CG  
1190 N  ND1 . HIS B 40  ? 0.1831 0.1703 0.1791 -0.0193 0.0429  -0.0286 40  HIS B ND1 
1191 C  CD2 . HIS B 40  ? 0.1701 0.1714 0.1618 0.0018  0.0301  -0.0396 40  HIS B CD2 
1192 C  CE1 . HIS B 40  ? 0.1689 0.1713 0.1829 -0.0135 0.0373  -0.0421 40  HIS B CE1 
1193 N  NE2 . HIS B 40  ? 0.1577 0.1692 0.1745 0.0070  0.0303  -0.0379 40  HIS B NE2 
1194 N  N   . VAL B 41  ? 0.1614 0.1309 0.1774 0.0169  0.0298  0.0053  41  VAL B N   
1195 C  CA  . VAL B 41  ? 0.1716 0.1284 0.1851 -0.0026 0.0506  0.0111  41  VAL B CA  
1196 C  C   . VAL B 41  ? 0.1831 0.1342 0.1858 0.0088  0.0336  0.0014  41  VAL B C   
1197 O  O   . VAL B 41  ? 0.1817 0.1435 0.1792 -0.0029 0.0272  -0.0124 41  VAL B O   
1198 C  CB  . VAL B 41  ? 0.1784 0.1522 0.2241 -0.0007 0.0593  0.0074  41  VAL B CB  
1199 C  CG1 . VAL B 41  ? 0.2079 0.1647 0.2396 0.0171  0.0601  0.0042  41  VAL B CG1 
1200 C  CG2 . VAL B 41  ? 0.1745 0.1730 0.2459 -0.0103 0.0388  -0.0019 41  VAL B CG2 
1201 N  N   . VAL B 42  ? 0.1653 0.1506 0.1789 0.0142  0.0414  0.0151  42  VAL B N   
1202 C  CA  . VAL B 42  ? 0.1756 0.1521 0.1790 0.0109  0.0341  0.0047  42  VAL B CA  
1203 C  C   . VAL B 42  ? 0.1858 0.1348 0.1855 0.0193  0.0313  -0.0087 42  VAL B C   
1204 O  O   . VAL B 42  ? 0.1995 0.1194 0.1915 0.0092  0.0149  -0.0296 42  VAL B O   
1205 C  CB  . VAL B 42  ? 0.1957 0.1541 0.1886 0.0159  0.0481  0.0066  42  VAL B CB  
1206 C  CG1 . VAL B 42  ? 0.2067 0.1702 0.2006 0.0173  0.0383  0.0039  42  VAL B CG1 
1207 C  CG2 . VAL B 42  ? 0.2137 0.1448 0.1922 0.0033  0.0469  0.0108  42  VAL B CG2 
1208 N  N   . PRO B 43  ? 0.1849 0.1280 0.1909 0.0232  0.0383  0.0008  43  PRO B N   
1209 C  CA  . PRO B 43  ? 0.1952 0.1301 0.1947 0.0206  0.0383  0.0132  43  PRO B CA  
1210 C  C   . PRO B 43  ? 0.2115 0.1416 0.1903 0.0014  0.0315  0.0237  43  PRO B C   
1211 O  O   . PRO B 43  ? 0.2252 0.1430 0.1925 -0.0223 0.0408  0.0122  43  PRO B O   
1212 C  CB  . PRO B 43  ? 0.2012 0.1274 0.2028 0.0186  0.0562  0.0059  43  PRO B CB  
1213 C  CG  . PRO B 43  ? 0.2286 0.1575 0.2115 0.0356  0.0414  0.0052  43  PRO B CG  
1214 C  CD  . PRO B 43  ? 0.2034 0.1371 0.2009 0.0277  0.0362  -0.0126 43  PRO B CD  
1215 N  N   . ASP B 44  ? 0.2140 0.1612 0.1958 0.0223  0.0276  0.0232  44  ASP B N   
1216 C  CA  . ASP B 44  ? 0.2299 0.1702 0.2214 0.0199  0.0139  0.0104  44  ASP B CA  
1217 C  C   . ASP B 44  ? 0.2180 0.1562 0.2112 0.0132  0.0041  0.0055  44  ASP B C   
1218 O  O   . ASP B 44  ? 0.2066 0.1735 0.2262 0.0219  0.0129  0.0365  44  ASP B O   
1219 C  CB  . ASP B 44  ? 0.2758 0.2168 0.2529 0.0311  0.0252  0.0139  44  ASP B CB  
1220 C  CG  . ASP B 44  ? 0.3331 0.2655 0.2920 0.0371  0.0363  0.0093  44  ASP B CG  
1221 O  OD1 . ASP B 44  ? 0.3602 0.2619 0.3108 0.0355  0.0270  0.0127  44  ASP B OD1 
1222 O  OD2 . ASP B 44  ? 0.3616 0.3147 0.3101 0.0220  0.0492  0.0267  44  ASP B OD2 
1223 N  N   . GLN B 45  ? 0.2112 0.1264 0.1808 -0.0010 0.0020  -0.0152 45  GLN B N   
1224 C  CA  . GLN B 45  ? 0.1937 0.1436 0.1693 -0.0003 0.0109  -0.0135 45  GLN B CA  
1225 C  C   . GLN B 45  ? 0.1910 0.1420 0.1828 -0.0103 0.0075  -0.0465 45  GLN B C   
1226 O  O   . GLN B 45  ? 0.1970 0.1545 0.2001 -0.0181 0.0148  -0.0505 45  GLN B O   
1227 C  CB  . GLN B 45  ? 0.1956 0.1562 0.1398 -0.0077 0.0203  -0.0026 45  GLN B CB  
1228 C  CG  . GLN B 45  ? 0.2122 0.1421 0.1314 -0.0177 0.0094  -0.0116 45  GLN B CG  
1229 C  CD  . GLN B 45  ? 0.2222 0.1420 0.1290 -0.0086 0.0058  -0.0004 45  GLN B CD  
1230 O  OE1 . GLN B 45  ? 0.2479 0.1703 0.1388 0.0097  0.0220  0.0112  45  GLN B OE1 
1231 N  NE2 . GLN B 45  ? 0.2302 0.1342 0.1202 -0.0161 -0.0055 0.0090  45  GLN B NE2 
1232 N  N   . LEU B 46  ? 0.1897 0.1610 0.1762 0.0005  0.0232  -0.0411 46  LEU B N   
1233 C  CA  . LEU B 46  ? 0.1903 0.1627 0.1984 0.0143  0.0234  -0.0390 46  LEU B CA  
1234 C  C   . LEU B 46  ? 0.1669 0.1443 0.1886 0.0252  0.0243  -0.0364 46  LEU B C   
1235 O  O   . LEU B 46  ? 0.1739 0.1347 0.1853 0.0113  0.0089  -0.0318 46  LEU B O   
1236 C  CB  . LEU B 46  ? 0.2529 0.2432 0.2546 -0.0014 0.0269  -0.0196 46  LEU B CB  
1237 C  CG  . LEU B 46  ? 0.3223 0.3179 0.3121 0.0047  0.0125  -0.0106 46  LEU B CG  
1238 C  CD1 . LEU B 46  ? 0.3506 0.3493 0.3397 0.0024  0.0112  0.0018  46  LEU B CD1 
1239 C  CD2 . LEU B 46  ? 0.3460 0.3448 0.3375 0.0074  0.0073  -0.0103 46  LEU B CD2 
1240 N  N   . MET B 47  ? 0.1869 0.1626 0.1938 0.0352  0.0100  -0.0343 47  MET B N   
1241 C  CA  . MET B 47  ? 0.1947 0.1812 0.2086 0.0507  -0.0026 -0.0482 47  MET B CA  
1242 C  C   . MET B 47  ? 0.1989 0.1705 0.1938 0.0213  -0.0169 -0.0511 47  MET B C   
1243 O  O   . MET B 47  ? 0.2228 0.1833 0.2010 0.0133  -0.0395 -0.0395 47  MET B O   
1244 C  CB  . MET B 47  ? 0.2108 0.2604 0.2432 0.0528  0.0104  -0.0457 47  MET B CB  
1245 C  CG  . MET B 47  ? 0.2317 0.3129 0.2683 0.0210  0.0569  -0.0257 47  MET B CG  
1246 S  SD  . MET B 47  ? 0.2481 0.3352 0.2815 0.0042  0.0929  -0.0107 47  MET B SD  
1247 C  CE  . MET B 47  ? 0.1898 0.1586 0.2400 -0.0285 0.1069  -0.0781 47  MET B CE  
1248 N  N   . ALA B 48  ? 0.1838 0.1559 0.1808 0.0185  -0.0138 -0.0492 48  ALA B N   
1249 C  CA  . ALA B 48  ? 0.1851 0.1812 0.1798 0.0136  -0.0093 -0.0629 48  ALA B CA  
1250 C  C   . ALA B 48  ? 0.1701 0.1634 0.1763 -0.0009 -0.0071 -0.0693 48  ALA B C   
1251 O  O   . ALA B 48  ? 0.1810 0.1705 0.1858 0.0103  0.0008  -0.0424 48  ALA B O   
1252 C  CB  . ALA B 48  ? 0.1991 0.2106 0.1845 0.0207  -0.0049 -0.0843 48  ALA B CB  
1253 N  N   . PHE B 49  ? 0.1702 0.1871 0.1844 -0.0049 -0.0125 -0.0592 49  PHE B N   
1254 C  CA  . PHE B 49  ? 0.1669 0.1801 0.1871 -0.0007 0.0094  -0.0707 49  PHE B CA  
1255 C  C   . PHE B 49  ? 0.1814 0.1829 0.1913 -0.0160 0.0080  -0.0802 49  PHE B C   
1256 O  O   . PHE B 49  ? 0.1895 0.1800 0.2024 -0.0106 0.0136  -0.0776 49  PHE B O   
1257 C  CB  . PHE B 49  ? 0.1649 0.1957 0.2018 0.0032  0.0287  -0.0635 49  PHE B CB  
1258 C  CG  . PHE B 49  ? 0.1752 0.2254 0.2368 0.0168  0.0246  -0.0409 49  PHE B CG  
1259 C  CD1 . PHE B 49  ? 0.1908 0.2550 0.2512 0.0128  0.0259  -0.0312 49  PHE B CD1 
1260 C  CD2 . PHE B 49  ? 0.1677 0.2412 0.2542 0.0395  0.0296  -0.0227 49  PHE B CD2 
1261 C  CE1 . PHE B 49  ? 0.1930 0.2731 0.2641 0.0194  0.0356  -0.0058 49  PHE B CE1 
1262 C  CE2 . PHE B 49  ? 0.1911 0.2620 0.2697 0.0334  0.0299  -0.0080 49  PHE B CE2 
1263 C  CZ  . PHE B 49  ? 0.2039 0.2767 0.2718 0.0292  0.0282  0.0096  49  PHE B CZ  
1264 N  N   . GLY B 50  ? 0.2038 0.2022 0.1977 -0.0282 0.0343  -0.0882 50  GLY B N   
1265 C  CA  . GLY B 50  ? 0.2217 0.2271 0.2146 -0.0275 0.0363  -0.0943 50  GLY B CA  
1266 C  C   . GLY B 50  ? 0.2304 0.2420 0.2405 -0.0188 0.0458  -0.1104 50  GLY B C   
1267 O  O   . GLY B 50  ? 0.2569 0.2599 0.2559 -0.0021 0.0429  -0.1259 50  GLY B O   
1268 N  N   . GLY B 51  ? 0.2037 0.2438 0.2612 -0.0267 0.0471  -0.1049 51  GLY B N   
1269 C  CA  . GLY B 51  ? 0.2204 0.2410 0.2870 0.0036  0.0443  -0.1098 51  GLY B CA  
1270 C  C   . GLY B 51  ? 0.2401 0.2384 0.3008 0.0212  0.0481  -0.1207 51  GLY B C   
1271 O  O   . GLY B 51  ? 0.2588 0.2714 0.3163 0.0391  0.0651  -0.1161 51  GLY B O   
1272 N  N   . SER B 52  ? 0.2537 0.2213 0.2896 0.0267  0.0370  -0.1389 52  SER B N   
1273 C  CA  . SER B 52  ? 0.2558 0.2268 0.2902 0.0207  0.0188  -0.1365 52  SER B CA  
1274 C  C   . SER B 52  ? 0.2389 0.2178 0.2959 0.0393  -0.0079 -0.1067 52  SER B C   
1275 O  O   . SER B 52  ? 0.2324 0.2107 0.2729 0.0349  -0.0151 -0.1160 52  SER B O   
1276 C  CB  . SER B 52  ? 0.2713 0.2436 0.2878 0.0024  0.0311  -0.1472 52  SER B CB  
1277 O  OG  . SER B 52  ? 0.2847 0.2701 0.2891 -0.0016 0.0376  -0.1605 52  SER B OG  
1278 N  N   A SER B 53  ? 0.2586 0.2313 0.3307 0.0415  -0.0247 -0.0764 53  SER B N   
1279 N  N   B SER B 53  ? 0.2586 0.2313 0.3307 0.0415  -0.0247 -0.0764 53  SER B N   
1280 C  CA  A SER B 53  ? 0.2723 0.2323 0.3592 0.0527  -0.0249 -0.0604 53  SER B CA  
1281 C  CA  B SER B 53  ? 0.2723 0.2323 0.3592 0.0527  -0.0249 -0.0604 53  SER B CA  
1282 C  C   A SER B 53  ? 0.2592 0.2040 0.3605 0.0669  -0.0082 -0.0742 53  SER B C   
1283 C  C   B SER B 53  ? 0.2592 0.2040 0.3605 0.0669  -0.0082 -0.0742 53  SER B C   
1284 O  O   A SER B 53  ? 0.2579 0.2130 0.3613 0.0814  0.0051  -0.0783 53  SER B O   
1285 O  O   B SER B 53  ? 0.2579 0.2130 0.3613 0.0814  0.0051  -0.0783 53  SER B O   
1286 C  CB  A SER B 53  ? 0.3061 0.2660 0.3817 0.0466  -0.0244 -0.0483 53  SER B CB  
1287 C  CB  B SER B 53  ? 0.3061 0.2660 0.3817 0.0466  -0.0244 -0.0483 53  SER B CB  
1288 O  OG  A SER B 53  ? 0.3371 0.2971 0.3970 0.0500  -0.0174 -0.0450 53  SER B OG  
1289 O  OG  B SER B 53  ? 0.3371 0.2971 0.3970 0.0500  -0.0174 -0.0450 53  SER B OG  
1290 N  N   . GLU B 54  ? 0.2540 0.1781 0.3648 0.0544  0.0049  -0.0817 54  GLU B N   
1291 C  CA  . GLU B 54  ? 0.2699 0.1709 0.3683 0.0418  0.0085  -0.0841 54  GLU B CA  
1292 C  C   . GLU B 54  ? 0.2598 0.1416 0.3484 0.0320  0.0051  -0.0849 54  GLU B C   
1293 O  O   . GLU B 54  ? 0.2464 0.1377 0.3248 0.0140  0.0044  -0.1010 54  GLU B O   
1294 C  CB  . GLU B 54  ? 0.3167 0.1979 0.3915 0.0454  0.0166  -0.0911 54  GLU B CB  
1295 C  CG  . GLU B 54  ? 0.3600 0.2263 0.4100 0.0613  0.0204  -0.0824 54  GLU B CG  
1296 C  CD  . GLU B 54  ? 0.4132 0.2797 0.4248 0.0671  0.0253  -0.0860 54  GLU B CD  
1297 O  OE1 . GLU B 54  ? 0.4344 0.3042 0.4246 0.0657  0.0379  -0.0966 54  GLU B OE1 
1298 O  OE2 . GLU B 54  ? 0.4303 0.2917 0.4323 0.0796  0.0235  -0.0832 54  GLU B OE2 
1299 N  N   . PRO B 55  ? 0.2695 0.1124 0.3525 0.0273  0.0058  -0.0638 55  PRO B N   
1300 C  CA  . PRO B 55  ? 0.2654 0.1256 0.3433 0.0248  0.0059  -0.0553 55  PRO B CA  
1301 C  C   . PRO B 55  ? 0.2495 0.1249 0.3165 0.0060  0.0103  -0.0665 55  PRO B C   
1302 O  O   . PRO B 55  ? 0.2702 0.1491 0.3230 -0.0181 0.0078  -0.0680 55  PRO B O   
1303 C  CB  . PRO B 55  ? 0.2748 0.1188 0.3554 0.0397  0.0054  -0.0336 55  PRO B CB  
1304 C  CG  . PRO B 55  ? 0.2836 0.1224 0.3606 0.0503  0.0050  -0.0328 55  PRO B CG  
1305 C  CD  . PRO B 55  ? 0.2847 0.1263 0.3647 0.0352  0.0095  -0.0398 55  PRO B CD  
1306 N  N   . CYS B 56  ? 0.2367 0.1191 0.2827 0.0208  0.0180  -0.0537 56  CYS B N   
1307 C  CA  . CYS B 56  ? 0.2193 0.1320 0.2460 0.0231  0.0227  -0.0509 56  CYS B CA  
1308 C  C   . CYS B 56  ? 0.2079 0.1241 0.2248 0.0173  0.0259  -0.0336 56  CYS B C   
1309 O  O   . CYS B 56  ? 0.2229 0.1273 0.2075 0.0065  0.0167  -0.0192 56  CYS B O   
1310 C  CB  . CYS B 56  ? 0.2030 0.1578 0.2358 0.0020  0.0108  -0.0553 56  CYS B CB  
1311 S  SG  . CYS B 56  ? 0.2085 0.1898 0.2202 -0.0078 0.0088  -0.0425 56  CYS B SG  
1312 N  N   . ALA B 57  ? 0.2076 0.1032 0.2171 -0.0003 0.0364  -0.0207 57  ALA B N   
1313 C  CA  . ALA B 57  ? 0.2003 0.1264 0.2044 0.0086  0.0421  -0.0296 57  ALA B CA  
1314 C  C   . ALA B 57  ? 0.1963 0.1381 0.1938 0.0100  0.0378  -0.0397 57  ALA B C   
1315 O  O   . ALA B 57  ? 0.1965 0.1486 0.1913 -0.0034 0.0256  -0.0442 57  ALA B O   
1316 C  CB  . ALA B 57  ? 0.1958 0.1296 0.2038 -0.0176 0.0456  -0.0347 57  ALA B CB  
1317 N  N   . LEU B 58  ? 0.1737 0.1543 0.1807 0.0095  0.0334  -0.0367 58  LEU B N   
1318 C  CA  . LEU B 58  ? 0.1626 0.1628 0.1668 0.0119  0.0499  -0.0475 58  LEU B CA  
1319 C  C   . LEU B 58  ? 0.1620 0.1510 0.1687 0.0063  0.0346  -0.0402 58  LEU B C   
1320 O  O   . LEU B 58  ? 0.1850 0.1661 0.1677 0.0099  0.0273  -0.0119 58  LEU B O   
1321 C  CB  . LEU B 58  ? 0.1692 0.1920 0.1646 0.0212  0.0669  -0.0558 58  LEU B CB  
1322 C  CG  . LEU B 58  ? 0.1776 0.2510 0.1808 -0.0121 0.0639  -0.0554 58  LEU B CG  
1323 C  CD1 . LEU B 58  ? 0.1673 0.2704 0.2005 -0.0245 0.0525  -0.0403 58  LEU B CD1 
1324 C  CD2 . LEU B 58  ? 0.1916 0.2779 0.1845 -0.0051 0.0512  -0.0716 58  LEU B CD2 
1325 N  N   . CYS B 59  ? 0.1523 0.1555 0.1672 0.0236  0.0298  -0.0444 59  CYS B N   
1326 C  CA  . CYS B 59  ? 0.1566 0.1624 0.1838 0.0189  0.0393  -0.0352 59  CYS B CA  
1327 C  C   . CYS B 59  ? 0.1570 0.1566 0.1745 0.0003  0.0328  -0.0320 59  CYS B C   
1328 O  O   . CYS B 59  ? 0.1725 0.1522 0.1642 -0.0029 0.0221  -0.0225 59  CYS B O   
1329 C  CB  . CYS B 59  ? 0.1927 0.1590 0.2135 0.0029  0.0389  -0.0224 59  CYS B CB  
1330 S  SG  . CYS B 59  ? 0.2173 0.1617 0.2286 -0.0060 0.0426  -0.0293 59  CYS B SG  
1331 N  N   . SER B 60  ? 0.1650 0.1464 0.1691 0.0164  0.0278  -0.0251 60  SER B N   
1332 C  CA  . SER B 60  ? 0.1716 0.1481 0.1718 0.0221  0.0391  -0.0138 60  SER B CA  
1333 C  C   . SER B 60  ? 0.1722 0.1447 0.1578 0.0271  0.0446  -0.0120 60  SER B C   
1334 O  O   . SER B 60  ? 0.2028 0.1519 0.1609 0.0389  0.0451  0.0157  60  SER B O   
1335 C  CB  . SER B 60  ? 0.1987 0.1741 0.1750 0.0035  0.0465  -0.0232 60  SER B CB  
1336 O  OG  . SER B 60  ? 0.2175 0.2005 0.1905 -0.0160 0.0548  -0.0394 60  SER B OG  
1337 N  N   . LEU B 61  ? 0.1511 0.1489 0.1593 0.0248  0.0404  -0.0183 61  LEU B N   
1338 C  CA  . LEU B 61  ? 0.1807 0.1506 0.1625 0.0211  0.0451  -0.0257 61  LEU B CA  
1339 C  C   . LEU B 61  ? 0.1872 0.1356 0.1527 0.0208  0.0375  -0.0028 61  LEU B C   
1340 O  O   . LEU B 61  ? 0.2154 0.1508 0.1517 0.0110  0.0357  0.0139  61  LEU B O   
1341 C  CB  . LEU B 61  ? 0.1715 0.1890 0.1679 0.0196  0.0495  -0.0196 61  LEU B CB  
1342 C  CG  . LEU B 61  ? 0.1707 0.2138 0.1776 0.0297  0.0216  -0.0109 61  LEU B CG  
1343 C  CD1 . LEU B 61  ? 0.1827 0.2323 0.1711 0.0304  0.0189  -0.0049 61  LEU B CD1 
1344 C  CD2 . LEU B 61  ? 0.1539 0.2089 0.1922 0.0268  0.0210  -0.0122 61  LEU B CD2 
1345 N  N   . HIS B 62  ? 0.1711 0.1247 0.1607 0.0256  0.0327  -0.0046 62  HIS B N   
1346 C  CA  . HIS B 62  ? 0.1442 0.1372 0.1733 0.0329  0.0243  -0.0101 62  HIS B CA  
1347 C  C   . HIS B 62  ? 0.1746 0.1550 0.1689 0.0355  0.0386  -0.0010 62  HIS B C   
1348 O  O   . HIS B 62  ? 0.2103 0.1654 0.1761 0.0455  0.0472  0.0060  62  HIS B O   
1349 C  CB  . HIS B 62  ? 0.1556 0.1684 0.1864 -0.0008 0.0198  -0.0276 62  HIS B CB  
1350 C  CG  . HIS B 62  ? 0.1848 0.1958 0.2002 0.0014  0.0209  -0.0428 62  HIS B CG  
1351 N  ND1 . HIS B 62  ? 0.1862 0.2031 0.2046 -0.0057 0.0327  -0.0447 62  HIS B ND1 
1352 C  CD2 . HIS B 62  ? 0.1835 0.2112 0.2042 -0.0011 0.0210  -0.0419 62  HIS B CD2 
1353 C  CE1 . HIS B 62  ? 0.1922 0.2087 0.2084 -0.0138 0.0249  -0.0356 62  HIS B CE1 
1354 N  NE2 . HIS B 62  ? 0.2021 0.2168 0.2077 0.0014  0.0289  -0.0408 62  HIS B NE2 
1355 N  N   . SER B 63  ? 0.1569 0.1429 0.1616 0.0447  0.0417  0.0061  63  SER B N   
1356 C  CA  . SER B 63  ? 0.1710 0.1391 0.1760 0.0535  0.0402  -0.0064 63  SER B CA  
1357 C  C   . SER B 63  ? 0.1916 0.1252 0.1765 0.0225  0.0277  0.0009  63  SER B C   
1358 O  O   . SER B 63  ? 0.1956 0.1327 0.1839 0.0155  0.0127  0.0094  63  SER B O   
1359 C  CB  . SER B 63  ? 0.1866 0.1615 0.1803 0.0591  0.0434  -0.0118 63  SER B CB  
1360 O  OG  . SER B 63  ? 0.2037 0.1855 0.1832 0.0514  0.0376  -0.0071 63  SER B OG  
1361 N  N   . ILE B 64  ? 0.2220 0.1390 0.1696 0.0248  0.0220  -0.0004 64  ILE B N   
1362 C  CA  . ILE B 64  ? 0.2251 0.1503 0.1688 0.0122  0.0342  -0.0030 64  ILE B CA  
1363 C  C   . ILE B 64  ? 0.2165 0.1608 0.1672 0.0242  0.0370  -0.0032 64  ILE B C   
1364 O  O   . ILE B 64  ? 0.2133 0.1606 0.1788 0.0335  0.0331  -0.0006 64  ILE B O   
1365 C  CB  . ILE B 64  ? 0.2134 0.1526 0.1667 0.0225  0.0436  0.0019  64  ILE B CB  
1366 C  CG1 . ILE B 64  ? 0.2171 0.1719 0.1591 0.0287  0.0552  -0.0086 64  ILE B CG1 
1367 C  CG2 . ILE B 64  ? 0.2153 0.1618 0.1752 0.0270  0.0307  0.0069  64  ILE B CG2 
1368 C  CD1 . ILE B 64  ? 0.2302 0.1855 0.1527 0.0044  0.0530  -0.0181 64  ILE B CD1 
1369 N  N   . GLY B 65  ? 0.2096 0.1594 0.1777 0.0277  0.0206  -0.0040 65  GLY B N   
1370 C  CA  . GLY B 65  ? 0.2080 0.1730 0.1895 0.0343  0.0180  -0.0218 65  GLY B CA  
1371 C  C   . GLY B 65  ? 0.1829 0.1901 0.1924 0.0453  0.0201  -0.0249 65  GLY B C   
1372 O  O   . GLY B 65  ? 0.1830 0.2106 0.1828 0.0446  0.0072  -0.0322 65  GLY B O   
1373 N  N   . LYS B 66  ? 0.1903 0.2045 0.2210 0.0423  0.0206  -0.0197 66  LYS B N   
1374 C  CA  . LYS B 66  ? 0.1913 0.2056 0.2384 0.0301  0.0264  -0.0317 66  LYS B CA  
1375 C  C   . LYS B 66  ? 0.2038 0.2075 0.2395 0.0158  0.0162  -0.0431 66  LYS B C   
1376 O  O   . LYS B 66  ? 0.2104 0.2117 0.2452 0.0081  0.0217  -0.0386 66  LYS B O   
1377 C  CB  . LYS B 66  ? 0.2044 0.2256 0.2608 0.0357  0.0399  -0.0308 66  LYS B CB  
1378 C  CG  . LYS B 66  ? 0.2237 0.2631 0.2821 0.0346  0.0469  -0.0346 66  LYS B CG  
1379 C  CD  . LYS B 66  ? 0.2462 0.3181 0.3080 0.0349  0.0630  -0.0292 66  LYS B CD  
1380 C  CE  . LYS B 66  ? 0.2856 0.3638 0.3420 0.0303  0.0601  -0.0228 66  LYS B CE  
1381 N  NZ  . LYS B 66  ? 0.3057 0.3965 0.3645 0.0284  0.0531  -0.0177 66  LYS B NZ  
1382 N  N   . ILE B 67  ? 0.2104 0.2181 0.2358 0.0149  0.0072  -0.0308 67  ILE B N   
1383 C  CA  . ILE B 67  ? 0.1913 0.2228 0.2194 0.0048  0.0062  -0.0239 67  ILE B CA  
1384 C  C   . ILE B 67  ? 0.1932 0.2315 0.2151 0.0148  -0.0089 -0.0092 67  ILE B C   
1385 O  O   . ILE B 67  ? 0.2219 0.2314 0.2201 0.0274  -0.0249 -0.0066 67  ILE B O   
1386 C  CB  . ILE B 67  ? 0.1642 0.1958 0.2077 0.0093  0.0251  -0.0237 67  ILE B CB  
1387 C  CG1 . ILE B 67  ? 0.1629 0.1916 0.2147 0.0211  0.0331  -0.0235 67  ILE B CG1 
1388 C  CG2 . ILE B 67  ? 0.1570 0.1633 0.2075 0.0064  0.0374  -0.0337 67  ILE B CG2 
1389 C  CD1 . ILE B 67  ? 0.1397 0.1771 0.2118 0.0149  0.0424  -0.0165 67  ILE B CD1 
1390 N  N   . GLY B 68  ? 0.1684 0.2432 0.2033 -0.0038 -0.0234 -0.0174 68  GLY B N   
1391 C  CA  . GLY B 68  ? 0.1622 0.2449 0.2073 0.0146  -0.0358 -0.0294 68  GLY B CA  
1392 C  C   . GLY B 68  ? 0.1789 0.2582 0.2153 0.0113  -0.0355 -0.0350 68  GLY B C   
1393 O  O   . GLY B 68  ? 0.1874 0.2467 0.2109 -0.0070 -0.0172 -0.0231 68  GLY B O   
1394 N  N   . GLY B 69  ? 0.1880 0.2678 0.2242 0.0232  -0.0514 -0.0469 69  GLY B N   
1395 C  CA  . GLY B 69  ? 0.1912 0.2864 0.2416 0.0391  -0.0449 -0.0585 69  GLY B CA  
1396 C  C   . GLY B 69  ? 0.1794 0.3033 0.2531 0.0235  -0.0284 -0.0631 69  GLY B C   
1397 O  O   . GLY B 69  ? 0.1901 0.3063 0.2490 0.0271  -0.0156 -0.0712 69  GLY B O   
1398 N  N   . ALA B 70  ? 0.1756 0.3112 0.2757 0.0040  -0.0178 -0.0643 70  ALA B N   
1399 C  CA  . ALA B 70  ? 0.1629 0.3039 0.2939 -0.0170 -0.0116 -0.0657 70  ALA B CA  
1400 C  C   . ALA B 70  ? 0.1735 0.2882 0.2938 -0.0093 0.0102  -0.0731 70  ALA B C   
1401 O  O   . ALA B 70  ? 0.1867 0.2893 0.3063 -0.0000 0.0096  -0.0816 70  ALA B O   
1402 C  CB  . ALA B 70  ? 0.1648 0.3187 0.3096 -0.0064 -0.0121 -0.0686 70  ALA B CB  
1403 N  N   . GLN B 71  ? 0.1674 0.2715 0.2781 -0.0238 0.0036  -0.0669 71  GLN B N   
1404 C  CA  . GLN B 71  ? 0.1754 0.2660 0.2761 -0.0044 0.0119  -0.0565 71  GLN B CA  
1405 C  C   . GLN B 71  ? 0.1797 0.2584 0.2734 -0.0008 0.0151  -0.0460 71  GLN B C   
1406 O  O   . GLN B 71  ? 0.1761 0.2598 0.2754 -0.0092 0.0166  -0.0381 71  GLN B O   
1407 C  CB  . GLN B 71  ? 0.1772 0.2546 0.2780 0.0245  0.0207  -0.0494 71  GLN B CB  
1408 C  CG  . GLN B 71  ? 0.1876 0.2554 0.2813 0.0341  0.0158  -0.0378 71  GLN B CG  
1409 C  CD  . GLN B 71  ? 0.2168 0.2484 0.2805 0.0343  0.0062  -0.0232 71  GLN B CD  
1410 O  OE1 . GLN B 71  ? 0.2606 0.2494 0.2854 0.0358  0.0059  -0.0217 71  GLN B OE1 
1411 N  NE2 . GLN B 71  ? 0.2172 0.2545 0.2875 0.0177  -0.0032 -0.0084 71  GLN B NE2 
1412 N  N   . ASN B 72  ? 0.1693 0.2308 0.2619 -0.0162 0.0146  -0.0450 72  ASN B N   
1413 C  CA  . ASN B 72  ? 0.1805 0.2122 0.2595 -0.0171 0.0153  -0.0393 72  ASN B CA  
1414 C  C   . ASN B 72  ? 0.1812 0.1983 0.2793 -0.0260 0.0086  -0.0484 72  ASN B C   
1415 O  O   . ASN B 72  ? 0.1694 0.1631 0.2705 -0.0222 0.0296  -0.0383 72  ASN B O   
1416 C  CB  . ASN B 72  ? 0.1796 0.2115 0.2384 -0.0227 0.0188  -0.0225 72  ASN B CB  
1417 C  CG  . ASN B 72  ? 0.1703 0.2018 0.2224 -0.0149 0.0240  -0.0181 72  ASN B CG  
1418 O  OD1 . ASN B 72  ? 0.1692 0.1859 0.2258 -0.0058 0.0394  -0.0191 72  ASN B OD1 
1419 N  ND2 . ASN B 72  ? 0.1605 0.1989 0.2149 -0.0152 0.0124  -0.0101 72  ASN B ND2 
1420 N  N   . ARG B 73  ? 0.2024 0.2180 0.3027 -0.0269 -0.0025 -0.0605 73  ARG B N   
1421 C  CA  . ARG B 73  ? 0.2075 0.2423 0.3133 -0.0392 -0.0119 -0.0683 73  ARG B CA  
1422 C  C   . ARG B 73  ? 0.1998 0.2503 0.3159 -0.0369 0.0097  -0.0517 73  ARG B C   
1423 O  O   . ARG B 73  ? 0.2125 0.2584 0.3202 -0.0447 0.0247  -0.0514 73  ARG B O   
1424 C  CB  . ARG B 73  ? 0.2325 0.2694 0.3261 -0.0387 -0.0375 -0.0830 73  ARG B CB  
1425 C  CG  . ARG B 73  ? 0.2482 0.3003 0.3382 -0.0473 -0.0503 -0.0906 73  ARG B CG  
1426 C  CD  . ARG B 73  ? 0.2728 0.3340 0.3462 -0.0419 -0.0600 -0.0913 73  ARG B CD  
1427 N  NE  . ARG B 73  ? 0.2921 0.3646 0.3549 -0.0318 -0.0723 -0.0866 73  ARG B NE  
1428 C  CZ  . ARG B 73  ? 0.3081 0.4003 0.3645 -0.0137 -0.0812 -0.0824 73  ARG B CZ  
1429 N  NH1 . ARG B 73  ? 0.3058 0.4177 0.3598 -0.0183 -0.0898 -0.0862 73  ARG B NH1 
1430 N  NH2 . ARG B 73  ? 0.3243 0.4065 0.3726 -0.0016 -0.0794 -0.0799 73  ARG B NH2 
1431 N  N   . SER B 74  ? 0.1925 0.2556 0.3105 -0.0404 0.0199  -0.0496 74  SER B N   
1432 C  CA  . SER B 74  ? 0.1842 0.2413 0.3133 -0.0342 0.0332  -0.0421 74  SER B CA  
1433 C  C   . SER B 74  ? 0.1693 0.2125 0.2962 -0.0317 0.0325  -0.0483 74  SER B C   
1434 O  O   . SER B 74  ? 0.1561 0.1811 0.3049 -0.0397 0.0414  -0.0509 74  SER B O   
1435 C  CB  . SER B 74  ? 0.1997 0.2556 0.3303 -0.0377 0.0545  -0.0224 74  SER B CB  
1436 O  OG  . SER B 74  ? 0.2161 0.2882 0.3447 -0.0354 0.0620  -0.0100 74  SER B OG  
1437 N  N   . TYR B 75  ? 0.1811 0.2029 0.2793 -0.0391 0.0325  -0.0493 75  TYR B N   
1438 C  CA  . TYR B 75  ? 0.1872 0.1797 0.2690 -0.0305 0.0404  -0.0549 75  TYR B CA  
1439 C  C   . TYR B 75  ? 0.1852 0.1869 0.2686 -0.0292 0.0502  -0.0467 75  TYR B C   
1440 O  O   . TYR B 75  ? 0.2060 0.1807 0.2790 -0.0394 0.0563  -0.0213 75  TYR B O   
1441 C  CB  . TYR B 75  ? 0.2101 0.1744 0.2659 -0.0233 0.0330  -0.0498 75  TYR B CB  
1442 C  CG  . TYR B 75  ? 0.2288 0.2011 0.2673 -0.0049 0.0400  -0.0426 75  TYR B CG  
1443 C  CD1 . TYR B 75  ? 0.2544 0.2055 0.2744 0.0173  0.0490  -0.0276 75  TYR B CD1 
1444 C  CD2 . TYR B 75  ? 0.2274 0.2004 0.2674 -0.0120 0.0370  -0.0440 75  TYR B CD2 
1445 C  CE1 . TYR B 75  ? 0.2664 0.2147 0.2758 0.0245  0.0554  -0.0218 75  TYR B CE1 
1446 C  CE2 . TYR B 75  ? 0.2276 0.2071 0.2678 -0.0040 0.0461  -0.0400 75  TYR B CE2 
1447 C  CZ  . TYR B 75  ? 0.2503 0.2108 0.2757 0.0119  0.0628  -0.0327 75  TYR B CZ  
1448 O  OH  . TYR B 75  ? 0.2482 0.2015 0.2842 0.0186  0.0840  -0.0316 75  TYR B OH  
1449 N  N   . SER B 76  ? 0.1934 0.1913 0.2671 -0.0220 0.0413  -0.0592 76  SER B N   
1450 C  CA  . SER B 76  ? 0.1851 0.1843 0.2737 -0.0239 0.0303  -0.0608 76  SER B CA  
1451 C  C   . SER B 76  ? 0.1791 0.1812 0.2948 -0.0331 0.0202  -0.0584 76  SER B C   
1452 O  O   . SER B 76  ? 0.1787 0.1816 0.2922 -0.0244 0.0228  -0.0817 76  SER B O   
1453 C  CB  . SER B 76  ? 0.1800 0.1888 0.2691 -0.0472 0.0272  -0.0586 76  SER B CB  
1454 O  OG  . SER B 76  ? 0.2041 0.2079 0.2719 -0.0513 0.0211  -0.0396 76  SER B OG  
1455 N  N   . LYS B 77  ? 0.1914 0.1856 0.3197 -0.0684 0.0010  -0.0486 77  LYS B N   
1456 C  CA  . LYS B 77  ? 0.1830 0.2135 0.3416 -0.0794 -0.0006 -0.0317 77  LYS B CA  
1457 C  C   . LYS B 77  ? 0.1946 0.2118 0.3196 -0.0581 0.0213  -0.0265 77  LYS B C   
1458 O  O   . LYS B 77  ? 0.1888 0.2094 0.3179 -0.0492 0.0269  -0.0197 77  LYS B O   
1459 C  CB  . LYS B 77  ? 0.1887 0.2440 0.3872 -0.0736 -0.0057 -0.0251 77  LYS B CB  
1460 C  CG  . LYS B 77  ? 0.2087 0.2775 0.4251 -0.0647 0.0008  -0.0109 77  LYS B CG  
1461 C  CD  . LYS B 77  ? 0.2306 0.3041 0.4566 -0.0703 0.0122  -0.0009 77  LYS B CD  
1462 C  CE  . LYS B 77  ? 0.2489 0.3269 0.4796 -0.0696 0.0240  0.0040  77  LYS B CE  
1463 N  NZ  . LYS B 77  ? 0.2628 0.3525 0.4896 -0.0636 0.0322  0.0125  77  LYS B NZ  
1464 N  N   . LEU B 78  ? 0.1929 0.2100 0.2988 -0.0506 0.0342  -0.0330 78  LEU B N   
1465 C  CA  . LEU B 78  ? 0.2136 0.1958 0.2991 -0.0349 0.0440  -0.0301 78  LEU B CA  
1466 C  C   . LEU B 78  ? 0.2128 0.1858 0.3087 -0.0148 0.0432  -0.0347 78  LEU B C   
1467 O  O   . LEU B 78  ? 0.2211 0.1996 0.3113 -0.0145 0.0457  -0.0190 78  LEU B O   
1468 C  CB  . LEU B 78  ? 0.2519 0.1877 0.2982 -0.0378 0.0454  -0.0303 78  LEU B CB  
1469 C  CG  . LEU B 78  ? 0.2870 0.2063 0.3028 -0.0308 0.0467  -0.0139 78  LEU B CG  
1470 C  CD1 . LEU B 78  ? 0.3034 0.2267 0.3101 -0.0302 0.0466  -0.0133 78  LEU B CD1 
1471 C  CD2 . LEU B 78  ? 0.2920 0.2080 0.3074 -0.0239 0.0468  -0.0111 78  LEU B CD2 
1472 N  N   . LEU B 79  ? 0.2029 0.1608 0.3162 -0.0161 0.0343  -0.0445 79  LEU B N   
1473 C  CA  . LEU B 79  ? 0.1984 0.1571 0.3257 0.0044  0.0432  -0.0393 79  LEU B CA  
1474 C  C   . LEU B 79  ? 0.2057 0.1705 0.3252 0.0082  0.0458  -0.0426 79  LEU B C   
1475 O  O   . LEU B 79  ? 0.2038 0.1797 0.3206 0.0039  0.0578  -0.0291 79  LEU B O   
1476 C  CB  . LEU B 79  ? 0.2136 0.1602 0.3366 -0.0099 0.0425  -0.0344 79  LEU B CB  
1477 C  CG  . LEU B 79  ? 0.2297 0.1786 0.3374 -0.0202 0.0433  -0.0205 79  LEU B CG  
1478 C  CD1 . LEU B 79  ? 0.2260 0.1870 0.3385 -0.0380 0.0429  -0.0197 79  LEU B CD1 
1479 C  CD2 . LEU B 79  ? 0.2452 0.1876 0.3411 -0.0172 0.0379  -0.0136 79  LEU B CD2 
1480 N  N   . CYS B 80  ? 0.2102 0.1759 0.3263 -0.0036 0.0309  -0.0419 80  CYS B N   
1481 C  CA  . CYS B 80  ? 0.2148 0.1856 0.3312 -0.0066 0.0196  -0.0352 80  CYS B CA  
1482 C  C   . CYS B 80  ? 0.2176 0.1881 0.3430 -0.0190 0.0159  -0.0277 80  CYS B C   
1483 O  O   . CYS B 80  ? 0.2229 0.1758 0.3432 -0.0118 0.0064  -0.0265 80  CYS B O   
1484 C  CB  . CYS B 80  ? 0.2105 0.1980 0.3259 -0.0300 0.0049  -0.0335 80  CYS B CB  
1485 S  SG  . CYS B 80  ? 0.2236 0.2324 0.3233 -0.0312 0.0155  -0.0311 80  CYS B SG  
1486 N  N   . GLY B 81  ? 0.2137 0.1879 0.3551 -0.0220 0.0143  -0.0220 81  GLY B N   
1487 C  CA  . GLY B 81  ? 0.2017 0.1800 0.3667 -0.0341 0.0350  -0.0104 81  GLY B CA  
1488 C  C   . GLY B 81  ? 0.2089 0.1745 0.3804 -0.0394 0.0576  -0.0152 81  GLY B C   
1489 O  O   . GLY B 81  ? 0.2185 0.1886 0.4006 -0.0255 0.0645  -0.0124 81  GLY B O   
1490 N  N   . LEU B 82  ? 0.2317 0.1902 0.3714 -0.0303 0.0680  -0.0245 82  LEU B N   
1491 C  CA  . LEU B 82  ? 0.2495 0.1883 0.3664 -0.0152 0.0675  -0.0111 82  LEU B CA  
1492 C  C   . LEU B 82  ? 0.2449 0.1777 0.3541 -0.0322 0.0495  -0.0088 82  LEU B C   
1493 O  O   . LEU B 82  ? 0.2779 0.1841 0.3652 -0.0271 0.0480  -0.0203 82  LEU B O   
1494 C  CB  . LEU B 82  ? 0.2593 0.1860 0.3742 0.0095  0.0898  -0.0075 82  LEU B CB  
1495 C  CG  . LEU B 82  ? 0.2897 0.1967 0.3790 -0.0100 0.1107  0.0137  82  LEU B CG  
1496 C  CD1 . LEU B 82  ? 0.2944 0.1843 0.3782 0.0015  0.1149  0.0043  82  LEU B CD1 
1497 C  CD2 . LEU B 82  ? 0.3139 0.2265 0.3859 -0.0199 0.1128  0.0263  82  LEU B CD2 
1498 N  N   . LEU B 83  ? 0.2175 0.1603 0.3420 -0.0512 0.0444  -0.0018 83  LEU B N   
1499 C  CA  . LEU B 83  ? 0.2208 0.1512 0.3339 -0.0286 0.0296  0.0057  83  LEU B CA  
1500 C  C   . LEU B 83  ? 0.2229 0.1506 0.3525 -0.0231 0.0249  0.0034  83  LEU B C   
1501 O  O   . LEU B 83  ? 0.2326 0.1406 0.3535 -0.0122 0.0077  0.0030  83  LEU B O   
1502 C  CB  . LEU B 83  ? 0.2374 0.1461 0.3091 -0.0154 0.0227  0.0156  83  LEU B CB  
1503 C  CG  . LEU B 83  ? 0.2401 0.1498 0.2974 -0.0250 0.0198  0.0213  83  LEU B CG  
1504 C  CD1 . LEU B 83  ? 0.2511 0.1688 0.2897 -0.0234 0.0469  0.0316  83  LEU B CD1 
1505 C  CD2 . LEU B 83  ? 0.2619 0.1674 0.2971 -0.0133 0.0076  0.0241  83  LEU B CD2 
1506 N  N   . ALA B 84  ? 0.2311 0.1522 0.3706 -0.0317 0.0296  -0.0099 84  ALA B N   
1507 C  CA  . ALA B 84  ? 0.2451 0.1650 0.3942 -0.0128 0.0418  -0.0194 84  ALA B CA  
1508 C  C   . ALA B 84  ? 0.2567 0.1684 0.4138 -0.0005 0.0612  -0.0141 84  ALA B C   
1509 O  O   . ALA B 84  ? 0.2616 0.1800 0.4253 0.0056  0.0533  -0.0108 84  ALA B O   
1510 C  CB  . ALA B 84  ? 0.2537 0.1728 0.4009 -0.0217 0.0323  -0.0231 84  ALA B CB  
1511 N  N   . GLU B 85  ? 0.2797 0.1820 0.4207 -0.0193 0.0782  0.0026  85  GLU B N   
1512 C  CA  . GLU B 85  ? 0.3050 0.1911 0.4328 -0.0304 0.0709  0.0251  85  GLU B CA  
1513 C  C   . GLU B 85  ? 0.3143 0.1857 0.4371 -0.0327 0.0669  0.0314  85  GLU B C   
1514 O  O   . GLU B 85  ? 0.3335 0.1775 0.4450 -0.0527 0.0650  0.0220  85  GLU B O   
1515 C  CB  . GLU B 85  ? 0.3219 0.2076 0.4398 -0.0329 0.0634  0.0260  85  GLU B CB  
1516 N  N   . ARG B 86  ? 0.2979 0.1864 0.4343 -0.0145 0.0723  0.0326  86  ARG B N   
1517 C  CA  . ARG B 86  ? 0.2788 0.1847 0.4307 -0.0055 0.0792  0.0398  86  ARG B CA  
1518 C  C   . ARG B 86  ? 0.2781 0.1988 0.4229 0.0093  0.0646  0.0448  86  ARG B C   
1519 O  O   . ARG B 86  ? 0.2849 0.2188 0.4259 0.0231  0.0581  0.0643  86  ARG B O   
1520 C  CB  . ARG B 86  ? 0.2757 0.1937 0.4364 -0.0109 0.0971  0.0456  86  ARG B CB  
1521 C  CG  . ARG B 86  ? 0.2851 0.2238 0.4497 -0.0082 0.0990  0.0456  86  ARG B CG  
1522 C  CD  . ARG B 86  ? 0.2880 0.2526 0.4638 -0.0118 0.1107  0.0494  86  ARG B CD  
1523 N  NE  . ARG B 86  ? 0.2882 0.2673 0.4768 -0.0430 0.1298  0.0523  86  ARG B NE  
1524 C  CZ  . ARG B 86  ? 0.2895 0.2698 0.4951 -0.0562 0.1240  0.0390  86  ARG B CZ  
1525 N  NH1 . ARG B 86  ? 0.2904 0.2638 0.4986 -0.0584 0.1090  0.0412  86  ARG B NH1 
1526 N  NH2 . ARG B 86  ? 0.3011 0.2799 0.5051 -0.0497 0.1272  0.0308  86  ARG B NH2 
1527 N  N   . LEU B 87  ? 0.2707 0.1879 0.4135 -0.0030 0.0596  0.0285  87  LEU B N   
1528 C  CA  . LEU B 87  ? 0.2723 0.1752 0.4042 -0.0147 0.0520  0.0125  87  LEU B CA  
1529 C  C   . LEU B 87  ? 0.2591 0.1778 0.4139 -0.0060 0.0436  0.0110  87  LEU B C   
1530 O  O   . LEU B 87  ? 0.2427 0.1869 0.4113 0.0057  0.0465  0.0176  87  LEU B O   
1531 C  CB  . LEU B 87  ? 0.2983 0.1618 0.3854 -0.0292 0.0398  0.0077  87  LEU B CB  
1532 C  CG  . LEU B 87  ? 0.3200 0.1818 0.3716 -0.0433 0.0317  0.0028  87  LEU B CG  
1533 C  CD1 . LEU B 87  ? 0.3266 0.1669 0.3620 -0.0504 0.0339  -0.0055 87  LEU B CD1 
1534 C  CD2 . LEU B 87  ? 0.3331 0.2020 0.3725 -0.0373 0.0262  -0.0063 87  LEU B CD2 
1535 N  N   . ARG B 88  ? 0.2645 0.1785 0.4260 -0.0013 0.0421  0.0093  88  ARG B N   
1536 C  CA  . ARG B 88  ? 0.2820 0.1881 0.4421 0.0042  0.0376  -0.0075 88  ARG B CA  
1537 C  C   . ARG B 88  ? 0.2563 0.1547 0.4278 -0.0097 0.0306  -0.0156 88  ARG B C   
1538 O  O   . ARG B 88  ? 0.2609 0.1731 0.4424 -0.0055 0.0341  -0.0262 88  ARG B O   
1539 C  CB  . ARG B 88  ? 0.3304 0.2385 0.4804 0.0048  0.0373  -0.0139 88  ARG B CB  
1540 C  CG  . ARG B 88  ? 0.3821 0.2949 0.5183 -0.0052 0.0332  -0.0176 88  ARG B CG  
1541 C  CD  . ARG B 88  ? 0.4276 0.3477 0.5499 -0.0147 0.0267  -0.0207 88  ARG B CD  
1542 N  NE  . ARG B 88  ? 0.4693 0.4002 0.5750 -0.0258 0.0234  -0.0223 88  ARG B NE  
1543 C  CZ  . ARG B 88  ? 0.5003 0.4329 0.5926 -0.0399 0.0185  -0.0242 88  ARG B CZ  
1544 N  NH1 . ARG B 88  ? 0.5122 0.4525 0.5986 -0.0399 0.0158  -0.0257 88  ARG B NH1 
1545 N  NH2 . ARG B 88  ? 0.5105 0.4366 0.5965 -0.0471 0.0188  -0.0229 88  ARG B NH2 
1546 N  N   . ILE B 89  ? 0.2494 0.1309 0.4012 -0.0313 0.0198  0.0074  89  ILE B N   
1547 C  CA  . ILE B 89  ? 0.2437 0.1460 0.3814 -0.0148 0.0248  -0.0040 89  ILE B CA  
1548 C  C   . ILE B 89  ? 0.2360 0.1767 0.3907 -0.0190 0.0259  -0.0326 89  ILE B C   
1549 O  O   . ILE B 89  ? 0.2246 0.1909 0.3956 -0.0263 0.0184  -0.0364 89  ILE B O   
1550 C  CB  . ILE B 89  ? 0.2532 0.1450 0.3582 0.0049  0.0221  0.0133  89  ILE B CB  
1551 C  CG1 . ILE B 89  ? 0.2555 0.1366 0.3473 0.0024  0.0253  0.0217  89  ILE B CG1 
1552 C  CG2 . ILE B 89  ? 0.2551 0.1652 0.3483 0.0133  0.0264  0.0178  89  ILE B CG2 
1553 C  CD1 . ILE B 89  ? 0.2627 0.1321 0.3333 -0.0025 0.0335  0.0357  89  ILE B CD1 
1554 N  N   A SER B 90  ? 0.2540 0.2019 0.3984 -0.0139 0.0267  -0.0490 90  SER B N   
1555 N  N   B SER B 90  ? 0.2540 0.2019 0.3984 -0.0139 0.0267  -0.0490 90  SER B N   
1556 C  CA  A SER B 90  ? 0.2590 0.2154 0.4057 -0.0165 0.0278  -0.0622 90  SER B CA  
1557 C  CA  B SER B 90  ? 0.2590 0.2154 0.4057 -0.0165 0.0278  -0.0622 90  SER B CA  
1558 C  C   A SER B 90  ? 0.2289 0.1848 0.3891 -0.0396 0.0252  -0.0725 90  SER B C   
1559 C  C   B SER B 90  ? 0.2289 0.1848 0.3891 -0.0396 0.0252  -0.0725 90  SER B C   
1560 O  O   A SER B 90  ? 0.2079 0.1698 0.3827 -0.0520 0.0096  -0.0772 90  SER B O   
1561 O  O   B SER B 90  ? 0.2079 0.1698 0.3827 -0.0520 0.0096  -0.0772 90  SER B O   
1562 C  CB  A SER B 90  ? 0.2929 0.2424 0.4220 -0.0116 0.0412  -0.0548 90  SER B CB  
1563 C  CB  B SER B 90  ? 0.2929 0.2424 0.4220 -0.0116 0.0412  -0.0548 90  SER B CB  
1564 O  OG  A SER B 90  ? 0.3297 0.2761 0.4345 -0.0209 0.0416  -0.0458 90  SER B OG  
1565 O  OG  B SER B 90  ? 0.3297 0.2761 0.4345 -0.0209 0.0416  -0.0458 90  SER B OG  
1566 N  N   . PRO B 91  ? 0.2330 0.1908 0.3800 -0.0422 0.0292  -0.0733 91  PRO B N   
1567 C  CA  . PRO B 91  ? 0.2389 0.1982 0.3663 -0.0332 0.0263  -0.0661 91  PRO B CA  
1568 C  C   . PRO B 91  ? 0.2411 0.1893 0.3423 -0.0239 0.0180  -0.0814 91  PRO B C   
1569 O  O   . PRO B 91  ? 0.2470 0.1945 0.3413 -0.0240 0.0188  -0.0789 91  PRO B O   
1570 C  CB  . PRO B 91  ? 0.2372 0.1995 0.3777 -0.0402 0.0308  -0.0520 91  PRO B CB  
1571 C  CG  . PRO B 91  ? 0.2435 0.2113 0.3874 -0.0255 0.0333  -0.0463 91  PRO B CG  
1572 C  CD  . PRO B 91  ? 0.2342 0.2055 0.3895 -0.0275 0.0346  -0.0596 91  PRO B CD  
1573 N  N   . ASP B 92  ? 0.2478 0.2047 0.3234 -0.0026 0.0120  -0.0906 92  ASP B N   
1574 C  CA  . ASP B 92  ? 0.2509 0.2031 0.3192 -0.0101 -0.0161 -0.1062 92  ASP B CA  
1575 C  C   . ASP B 92  ? 0.2248 0.1740 0.2977 -0.0029 -0.0286 -0.1012 92  ASP B C   
1576 O  O   . ASP B 92  ? 0.2218 0.1690 0.2910 0.0132  -0.0320 -0.1022 92  ASP B O   
1577 C  CB  . ASP B 92  ? 0.2802 0.2039 0.3313 0.0014  -0.0241 -0.1261 92  ASP B CB  
1578 C  CG  . ASP B 92  ? 0.3113 0.2140 0.3422 -0.0031 -0.0287 -0.1311 92  ASP B CG  
1579 O  OD1 . ASP B 92  ? 0.3078 0.2071 0.3451 -0.0013 -0.0205 -0.1175 92  ASP B OD1 
1580 O  OD2 . ASP B 92  ? 0.3339 0.2478 0.3486 0.0018  -0.0359 -0.1364 92  ASP B OD2 
1581 N  N   . ARG B 93  ? 0.2102 0.1541 0.2809 -0.0166 -0.0306 -0.0969 93  ARG B N   
1582 C  CA  . ARG B 93  ? 0.2058 0.1513 0.2765 0.0082  -0.0242 -0.0920 93  ARG B CA  
1583 C  C   . ARG B 93  ? 0.1963 0.1537 0.2565 0.0060  -0.0343 -0.0937 93  ARG B C   
1584 O  O   . ARG B 93  ? 0.1897 0.1483 0.2518 0.0098  -0.0346 -0.0824 93  ARG B O   
1585 C  CB  . ARG B 93  ? 0.2046 0.1694 0.2919 0.0226  -0.0227 -0.0814 93  ARG B CB  
1586 C  CG  . ARG B 93  ? 0.2089 0.1633 0.3012 0.0106  -0.0274 -0.0770 93  ARG B CG  
1587 C  CD  . ARG B 93  ? 0.1984 0.1526 0.3112 0.0098  -0.0204 -0.0756 93  ARG B CD  
1588 N  NE  . ARG B 93  ? 0.1954 0.1415 0.3136 -0.0007 -0.0114 -0.0667 93  ARG B NE  
1589 C  CZ  . ARG B 93  ? 0.2018 0.1582 0.3210 0.0054  0.0012  -0.0632 93  ARG B CZ  
1590 N  NH1 . ARG B 93  ? 0.2050 0.1664 0.3269 0.0202  0.0122  -0.0596 93  ARG B NH1 
1591 N  NH2 . ARG B 93  ? 0.2132 0.1620 0.3267 -0.0059 0.0031  -0.0499 93  ARG B NH2 
1592 N  N   . VAL B 94  ? 0.1975 0.1771 0.2508 0.0023  -0.0214 -0.0868 94  VAL B N   
1593 C  CA  . VAL B 94  ? 0.1864 0.1657 0.2518 0.0105  -0.0042 -0.0678 94  VAL B CA  
1594 C  C   . VAL B 94  ? 0.1758 0.1583 0.2398 0.0025  -0.0146 -0.0653 94  VAL B C   
1595 O  O   . VAL B 94  ? 0.1862 0.1787 0.2305 0.0168  -0.0285 -0.0541 94  VAL B O   
1596 C  CB  . VAL B 94  ? 0.1781 0.1685 0.2658 0.0109  -0.0127 -0.0499 94  VAL B CB  
1597 C  CG1 . VAL B 94  ? 0.1974 0.1701 0.2758 0.0099  -0.0201 -0.0508 94  VAL B CG1 
1598 C  CG2 . VAL B 94  ? 0.1850 0.1817 0.2688 0.0341  -0.0033 -0.0415 94  VAL B CG2 
1599 N  N   . TYR B 95  ? 0.1619 0.1413 0.2342 -0.0087 0.0032  -0.0728 95  TYR B N   
1600 C  CA  . TYR B 95  ? 0.1601 0.1605 0.2264 0.0006  0.0197  -0.0705 95  TYR B CA  
1601 C  C   . TYR B 95  ? 0.1656 0.1576 0.2191 -0.0041 0.0195  -0.0571 95  TYR B C   
1602 O  O   . TYR B 95  ? 0.1822 0.1647 0.2195 -0.0054 0.0006  -0.0606 95  TYR B O   
1603 C  CB  . TYR B 95  ? 0.1675 0.2117 0.2226 -0.0189 0.0190  -0.0705 95  TYR B CB  
1604 C  CG  . TYR B 95  ? 0.1654 0.2517 0.2059 -0.0183 0.0143  -0.0887 95  TYR B CG  
1605 C  CD1 . TYR B 95  ? 0.1774 0.2818 0.2038 -0.0251 0.0053  -0.0870 95  TYR B CD1 
1606 C  CD2 . TYR B 95  ? 0.1744 0.2750 0.2024 0.0057  0.0391  -0.0982 95  TYR B CD2 
1607 C  CE1 . TYR B 95  ? 0.2041 0.3120 0.2133 -0.0289 0.0073  -0.0907 95  TYR B CE1 
1608 C  CE2 . TYR B 95  ? 0.1937 0.3054 0.2082 -0.0170 0.0290  -0.0939 95  TYR B CE2 
1609 C  CZ  . TYR B 95  ? 0.2063 0.3276 0.2021 -0.0251 0.0163  -0.0970 95  TYR B CZ  
1610 O  OH  . TYR B 95  ? 0.2203 0.3673 0.1970 -0.0256 0.0229  -0.0929 95  TYR B OH  
1611 N  N   . ILE B 96  ? 0.1571 0.1419 0.2198 0.0018  0.0274  -0.0325 96  ILE B N   
1612 C  CA  . ILE B 96  ? 0.1516 0.1361 0.2223 0.0193  0.0265  -0.0312 96  ILE B CA  
1613 C  C   . ILE B 96  ? 0.1645 0.1407 0.2095 0.0226  0.0026  -0.0380 96  ILE B C   
1614 O  O   . ILE B 96  ? 0.1890 0.1619 0.2158 0.0324  -0.0271 -0.0408 96  ILE B O   
1615 C  CB  . ILE B 96  ? 0.1603 0.1451 0.2306 0.0076  0.0400  -0.0358 96  ILE B CB  
1616 C  CG1 . ILE B 96  ? 0.1681 0.1590 0.2443 0.0059  0.0340  -0.0182 96  ILE B CG1 
1617 C  CG2 . ILE B 96  ? 0.1628 0.1552 0.2378 0.0248  0.0357  -0.0392 96  ILE B CG2 
1618 C  CD1 . ILE B 96  ? 0.1973 0.1846 0.2586 -0.0166 0.0341  -0.0041 96  ILE B CD1 
1619 N  N   . ASN B 97  ? 0.1885 0.1408 0.1929 0.0200  0.0131  -0.0461 97  ASN B N   
1620 C  CA  . ASN B 97  ? 0.1606 0.1425 0.1823 -0.0031 0.0066  -0.0527 97  ASN B CA  
1621 C  C   . ASN B 97  ? 0.1563 0.1644 0.1591 -0.0067 0.0024  -0.0386 97  ASN B C   
1622 O  O   . ASN B 97  ? 0.1909 0.1801 0.1450 0.0035  0.0223  -0.0345 97  ASN B O   
1623 C  CB  . ASN B 97  ? 0.1572 0.1729 0.2152 -0.0136 0.0321  -0.0580 97  ASN B CB  
1624 C  CG  . ASN B 97  ? 0.1991 0.2135 0.2547 0.0030  0.0481  -0.0715 97  ASN B CG  
1625 O  OD1 . ASN B 97  ? 0.2194 0.2466 0.2648 -0.0071 0.0519  -0.0800 97  ASN B OD1 
1626 N  ND2 . ASN B 97  ? 0.2126 0.2088 0.2779 0.0150  0.0622  -0.0651 97  ASN B ND2 
1627 N  N   . TYR B 98  ? 0.1336 0.1491 0.1555 0.0080  0.0192  -0.0195 98  TYR B N   
1628 C  CA  . TYR B 98  ? 0.1303 0.1331 0.1458 0.0045  0.0155  -0.0292 98  TYR B CA  
1629 C  C   . TYR B 98  ? 0.1543 0.1427 0.1321 0.0049  0.0236  -0.0109 98  TYR B C   
1630 O  O   . TYR B 98  ? 0.1696 0.1648 0.1265 0.0079  0.0334  -0.0277 98  TYR B O   
1631 C  CB  . TYR B 98  ? 0.1575 0.1421 0.1726 -0.0155 0.0110  -0.0264 98  TYR B CB  
1632 C  CG  . TYR B 98  ? 0.1600 0.1534 0.1803 -0.0136 0.0315  -0.0114 98  TYR B CG  
1633 C  CD1 . TYR B 98  ? 0.1639 0.1694 0.1838 0.0072  0.0357  -0.0014 98  TYR B CD1 
1634 C  CD2 . TYR B 98  ? 0.1673 0.1639 0.1904 -0.0312 0.0388  -0.0168 98  TYR B CD2 
1635 C  CE1 . TYR B 98  ? 0.1595 0.1764 0.1990 -0.0034 0.0192  -0.0001 98  TYR B CE1 
1636 C  CE2 . TYR B 98  ? 0.1437 0.1615 0.1904 -0.0280 0.0282  -0.0097 98  TYR B CE2 
1637 C  CZ  . TYR B 98  ? 0.1560 0.1721 0.2085 -0.0092 0.0259  0.0043  98  TYR B CZ  
1638 O  OH  . TYR B 98  ? 0.1557 0.1740 0.2324 -0.0038 0.0258  -0.0013 98  TYR B OH  
1639 N  N   . TYR B 99  ? 0.1555 0.1381 0.1377 0.0003  0.0293  -0.0058 99  TYR B N   
1640 C  CA  . TYR B 99  ? 0.1722 0.1625 0.1489 0.0059  0.0312  -0.0156 99  TYR B CA  
1641 C  C   . TYR B 99  ? 0.1727 0.1604 0.1499 0.0040  0.0360  -0.0147 99  TYR B C   
1642 O  O   . TYR B 99  ? 0.1886 0.1572 0.1447 0.0061  0.0225  -0.0231 99  TYR B O   
1643 C  CB  . TYR B 99  ? 0.1698 0.1835 0.1576 -0.0136 0.0230  -0.0016 99  TYR B CB  
1644 C  CG  . TYR B 99  ? 0.1756 0.1926 0.1690 -0.0060 0.0391  0.0066  99  TYR B CG  
1645 C  CD1 . TYR B 99  ? 0.1907 0.2290 0.1959 0.0071  0.0553  0.0057  99  TYR B CD1 
1646 C  CD2 . TYR B 99  ? 0.1772 0.1928 0.1759 -0.0096 0.0308  -0.0116 99  TYR B CD2 
1647 C  CE1 . TYR B 99  ? 0.1976 0.2418 0.2110 0.0245  0.0608  0.0095  99  TYR B CE1 
1648 C  CE2 . TYR B 99  ? 0.1746 0.2262 0.1900 -0.0057 0.0339  -0.0073 99  TYR B CE2 
1649 C  CZ  . TYR B 99  ? 0.1759 0.2379 0.2050 0.0122  0.0510  0.0042  99  TYR B CZ  
1650 O  OH  . TYR B 99  ? 0.1839 0.2743 0.2234 0.0310  0.0530  0.0042  99  TYR B OH  
1651 N  N   . ASP B 100 ? 0.1907 0.1709 0.1664 0.0108  0.0302  -0.0067 100 ASP B N   
1652 C  CA  . ASP B 100 ? 0.1996 0.1763 0.1757 0.0186  0.0129  -0.0077 100 ASP B CA  
1653 C  C   . ASP B 100 ? 0.2233 0.1729 0.1592 0.0087  0.0166  -0.0047 100 ASP B C   
1654 O  O   . ASP B 100 ? 0.2404 0.1924 0.1491 -0.0023 0.0200  0.0104  100 ASP B O   
1655 C  CB  . ASP B 100 ? 0.1895 0.2096 0.2016 0.0211  0.0114  -0.0206 100 ASP B CB  
1656 C  CG  . ASP B 100 ? 0.2048 0.2419 0.2243 0.0399  0.0046  -0.0031 100 ASP B CG  
1657 O  OD1 . ASP B 100 ? 0.2038 0.2282 0.2240 0.0589  0.0222  0.0044  100 ASP B OD1 
1658 O  OD2 . ASP B 100 ? 0.2184 0.2827 0.2517 0.0405  -0.0073 0.0145  100 ASP B OD2 
1659 N  N   . MET B 101 ? 0.2247 0.1609 0.1602 0.0119  0.0336  -0.0008 101 MET B N   
1660 C  CA  . MET B 101 ? 0.1985 0.1513 0.1632 0.0185  0.0259  0.0100  101 MET B CA  
1661 C  C   . MET B 101 ? 0.1915 0.1432 0.1715 0.0215  0.0298  0.0108  101 MET B C   
1662 O  O   . MET B 101 ? 0.2028 0.1406 0.1755 0.0136  0.0456  0.0143  101 MET B O   
1663 C  CB  . MET B 101 ? 0.1966 0.1794 0.1654 0.0317  0.0215  0.0091  101 MET B CB  
1664 C  CG  . MET B 101 ? 0.2086 0.1859 0.1724 0.0293  0.0150  0.0024  101 MET B CG  
1665 S  SD  . MET B 101 ? 0.2126 0.2255 0.1810 0.0328  0.0016  -0.0328 101 MET B SD  
1666 C  CE  . MET B 101 ? 0.2025 0.2337 0.1950 0.0034  -0.0095 -0.0290 101 MET B CE  
1667 N  N   . ASN B 102 ? 0.1898 0.1511 0.1697 0.0255  0.0228  0.0209  102 ASN B N   
1668 C  CA  . ASN B 102 ? 0.1869 0.1527 0.1776 0.0234  0.0415  0.0047  102 ASN B CA  
1669 C  C   . ASN B 102 ? 0.1732 0.1507 0.1747 0.0377  0.0511  0.0020  102 ASN B C   
1670 O  O   . ASN B 102 ? 0.1771 0.1577 0.1711 0.0198  0.0260  -0.0059 102 ASN B O   
1671 C  CB  . ASN B 102 ? 0.2228 0.1803 0.2005 0.0003  0.0200  0.0248  102 ASN B CB  
1672 C  CG  . ASN B 102 ? 0.2857 0.2280 0.2378 -0.0085 0.0051  0.0449  102 ASN B CG  
1673 O  OD1 . ASN B 102 ? 0.3445 0.2635 0.2600 0.0050  -0.0149 0.0357  102 ASN B OD1 
1674 N  ND2 . ASN B 102 ? 0.2882 0.2557 0.2555 -0.0138 0.0154  0.0486  102 ASN B ND2 
1675 N  N   . ALA B 103 ? 0.1880 0.1535 0.1668 0.0386  0.0577  -0.0074 103 ALA B N   
1676 C  CA  . ALA B 103 ? 0.1962 0.1719 0.1614 0.0318  0.0563  -0.0110 103 ALA B CA  
1677 C  C   . ALA B 103 ? 0.1915 0.1813 0.1485 0.0159  0.0594  -0.0125 103 ALA B C   
1678 O  O   . ALA B 103 ? 0.2002 0.2038 0.1359 -0.0010 0.0483  -0.0198 103 ALA B O   
1679 C  CB  . ALA B 103 ? 0.1984 0.1648 0.1583 0.0219  0.0516  -0.0079 103 ALA B CB  
1680 N  N   . ALA B 104 ? 0.1868 0.1797 0.1465 0.0148  0.0564  -0.0017 104 ALA B N   
1681 C  CA  . ALA B 104 ? 0.1813 0.1911 0.1532 0.0032  0.0724  -0.0011 104 ALA B CA  
1682 C  C   . ALA B 104 ? 0.1900 0.1795 0.1422 0.0168  0.0730  -0.0186 104 ALA B C   
1683 O  O   . ALA B 104 ? 0.2182 0.1726 0.1400 0.0238  0.0582  -0.0283 104 ALA B O   
1684 C  CB  . ALA B 104 ? 0.1904 0.1795 0.1689 -0.0088 0.0777  0.0047  104 ALA B CB  
1685 N  N   . ASN B 105 ? 0.1875 0.1730 0.1293 0.0197  0.0675  -0.0070 105 ASN B N   
1686 C  CA  . ASN B 105 ? 0.1827 0.1749 0.1193 0.0162  0.0620  -0.0007 105 ASN B CA  
1687 C  C   . ASN B 105 ? 0.1652 0.1648 0.1213 0.0155  0.0510  -0.0116 105 ASN B C   
1688 O  O   . ASN B 105 ? 0.1561 0.1817 0.1338 0.0141  0.0455  0.0005  105 ASN B O   
1689 C  CB  . ASN B 105 ? 0.1911 0.1800 0.1229 0.0122  0.0512  0.0060  105 ASN B CB  
1690 C  CG  . ASN B 105 ? 0.2126 0.1885 0.1365 -0.0131 0.0349  -0.0027 105 ASN B CG  
1691 O  OD1 . ASN B 105 ? 0.2171 0.1998 0.1509 -0.0475 0.0457  0.0118  105 ASN B OD1 
1692 N  ND2 . ASN B 105 ? 0.2197 0.1979 0.1328 -0.0191 0.0175  0.0155  105 ASN B ND2 
1693 N  N   . VAL B 106 ? 0.1920 0.1614 0.1259 0.0209  0.0634  -0.0088 106 VAL B N   
1694 C  CA  . VAL B 106 ? 0.1913 0.1576 0.1191 0.0245  0.0506  0.0029  106 VAL B CA  
1695 C  C   . VAL B 106 ? 0.1925 0.1473 0.1174 0.0248  0.0544  0.0038  106 VAL B C   
1696 O  O   . VAL B 106 ? 0.1913 0.1572 0.1266 0.0330  0.0547  -0.0089 106 VAL B O   
1697 C  CB  . VAL B 106 ? 0.2038 0.1772 0.1222 0.0059  0.0268  0.0017  106 VAL B CB  
1698 C  CG1 . VAL B 106 ? 0.2134 0.1822 0.1248 -0.0030 0.0055  -0.0021 106 VAL B CG1 
1699 C  CG2 . VAL B 106 ? 0.2082 0.1771 0.1184 -0.0058 0.0333  0.0004  106 VAL B CG2 
1700 N  N   . GLY B 107 ? 0.2332 0.1558 0.1161 0.0187  0.0469  0.0160  107 GLY B N   
1701 C  CA  . GLY B 107 ? 0.2551 0.1742 0.1157 0.0141  0.0446  0.0210  107 GLY B CA  
1702 C  C   . GLY B 107 ? 0.2565 0.1787 0.1103 0.0195  0.0463  0.0191  107 GLY B C   
1703 O  O   . GLY B 107 ? 0.2468 0.1739 0.1079 0.0271  0.0386  0.0154  107 GLY B O   
1704 N  N   . TRP B 108 ? 0.2496 0.1927 0.1138 0.0125  0.0630  0.0258  108 TRP B N   
1705 C  CA  . TRP B 108 ? 0.2606 0.1893 0.1168 0.0244  0.0478  0.0193  108 TRP B CA  
1706 C  C   . TRP B 108 ? 0.3001 0.1844 0.1255 0.0482  0.0288  0.0129  108 TRP B C   
1707 O  O   . TRP B 108 ? 0.3019 0.1930 0.1412 0.0590  0.0371  -0.0047 108 TRP B O   
1708 C  CB  . TRP B 108 ? 0.2348 0.1961 0.1264 0.0253  0.0716  0.0307  108 TRP B CB  
1709 C  CG  . TRP B 108 ? 0.2084 0.2101 0.1429 0.0305  0.0710  0.0212  108 TRP B CG  
1710 C  CD1 . TRP B 108 ? 0.1919 0.2220 0.1538 0.0346  0.0652  0.0217  108 TRP B CD1 
1711 C  CD2 . TRP B 108 ? 0.2151 0.2343 0.1572 0.0377  0.0700  0.0191  108 TRP B CD2 
1712 N  NE1 . TRP B 108 ? 0.1997 0.2308 0.1592 0.0471  0.0778  0.0146  108 TRP B NE1 
1713 C  CE2 . TRP B 108 ? 0.2098 0.2305 0.1696 0.0516  0.0692  0.0179  108 TRP B CE2 
1714 C  CE3 . TRP B 108 ? 0.2403 0.2573 0.1742 0.0489  0.0694  0.0137  108 TRP B CE3 
1715 C  CZ2 . TRP B 108 ? 0.2179 0.2370 0.1782 0.0807  0.0633  0.0167  108 TRP B CZ2 
1716 C  CZ3 . TRP B 108 ? 0.2454 0.2691 0.1790 0.0754  0.0677  0.0209  108 TRP B CZ3 
1717 C  CH2 . TRP B 108 ? 0.2319 0.2614 0.1782 0.0800  0.0611  0.0292  108 TRP B CH2 
1718 N  N   . ASN B 109 ? 0.3114 0.1797 0.1159 0.0427  0.0349  0.0159  109 ASN B N   
1719 C  CA  . ASN B 109 ? 0.3286 0.2024 0.1410 0.0457  0.0420  -0.0157 109 ASN B CA  
1720 C  C   . ASN B 109 ? 0.3493 0.1991 0.1503 0.0501  0.0374  -0.0086 109 ASN B C   
1721 O  O   . ASN B 109 ? 0.3589 0.2142 0.1620 0.0522  0.0299  0.0075  109 ASN B O   
1722 C  CB  . ASN B 109 ? 0.3148 0.2199 0.1525 0.0525  0.0598  -0.0158 109 ASN B CB  
1723 C  CG  . ASN B 109 ? 0.3094 0.2445 0.1725 0.0637  0.0649  -0.0080 109 ASN B CG  
1724 O  OD1 . ASN B 109 ? 0.3148 0.2677 0.1761 0.0592  0.0606  -0.0114 109 ASN B OD1 
1725 N  ND2 . ASN B 109 ? 0.3188 0.2533 0.1945 0.0593  0.0649  0.0214  109 ASN B ND2 
1726 N  N   . ASN B 110 ? 0.3655 0.1838 0.1431 0.0269  0.0316  -0.0133 110 ASN B N   
1727 C  CA  . ASN B 110 ? 0.3819 0.1943 0.1468 0.0180  0.0304  -0.0269 110 ASN B CA  
1728 C  C   . ASN B 110 ? 0.3556 0.1745 0.1554 0.0003  0.0243  -0.0232 110 ASN B C   
1729 O  O   . ASN B 110 ? 0.3631 0.1681 0.1718 -0.0340 0.0141  -0.0203 110 ASN B O   
1730 C  CB  . ASN B 110 ? 0.4068 0.2386 0.1556 0.0400  0.0291  -0.0409 110 ASN B CB  
1731 C  CG  . ASN B 110 ? 0.4434 0.2825 0.1627 0.0464  0.0295  -0.0440 110 ASN B CG  
1732 O  OD1 . ASN B 110 ? 0.4684 0.3011 0.1803 0.0607  -0.0003 -0.0564 110 ASN B OD1 
1733 N  ND2 . ASN B 110 ? 0.4659 0.2941 0.1718 0.0316  0.0382  -0.0197 110 ASN B ND2 
1734 N  N   . SER B 111 ? 0.3344 0.1819 0.1594 0.0226  0.0206  -0.0309 111 SER B N   
1735 C  CA  . SER B 111 ? 0.3185 0.1840 0.1572 0.0207  0.0209  -0.0161 111 SER B CA  
1736 C  C   . SER B 111 ? 0.2914 0.1805 0.1423 0.0163  0.0356  0.0027  111 SER B C   
1737 O  O   . SER B 111 ? 0.3003 0.1752 0.1471 0.0170  0.0151  0.0051  111 SER B O   
1738 C  CB  . SER B 111 ? 0.3342 0.1840 0.1711 0.0533  0.0207  -0.0198 111 SER B CB  
1739 O  OG  . SER B 111 ? 0.3377 0.2116 0.1856 0.0412  0.0272  -0.0046 111 SER B OG  
1740 N  N   . THR B 112 ? 0.2598 0.1739 0.1401 -0.0027 0.0493  -0.0029 112 THR B N   
1741 C  CA  . THR B 112 ? 0.2534 0.1665 0.1417 0.0021  0.0524  0.0070  112 THR B CA  
1742 C  C   . THR B 112 ? 0.2570 0.1834 0.1579 0.0122  0.0612  -0.0014 112 THR B C   
1743 O  O   . THR B 112 ? 0.2924 0.2164 0.1846 0.0099  0.0588  -0.0203 112 THR B O   
1744 C  CB  . THR B 112 ? 0.2414 0.1379 0.1480 0.0167  0.0438  0.0189  112 THR B CB  
1745 O  OG1 . THR B 112 ? 0.2580 0.1596 0.1637 0.0244  0.0346  0.0091  112 THR B OG1 
1746 C  CG2 . THR B 112 ? 0.2206 0.1424 0.1514 0.0299  0.0378  0.0216  112 THR B CG2 
1747 N  N   . PHE B 113 ? 0.2280 0.1700 0.1613 0.0088  0.0542  0.0099  113 PHE B N   
1748 C  CA  . PHE B 113 ? 0.2163 0.1840 0.1794 0.0176  0.0409  0.0174  113 PHE B CA  
1749 C  C   . PHE B 113 ? 0.2132 0.2005 0.1849 0.0015  0.0438  0.0290  113 PHE B C   
1750 O  O   . PHE B 113 ? 0.2210 0.2231 0.2012 0.0139  0.0476  0.0299  113 PHE B O   
1751 C  CB  . PHE B 113 ? 0.2125 0.2007 0.1841 0.0101  0.0444  0.0349  113 PHE B CB  
1752 C  CG  . PHE B 113 ? 0.2067 0.2088 0.1813 0.0222  0.0460  0.0444  113 PHE B CG  
1753 C  CD1 . PHE B 113 ? 0.2068 0.2233 0.1793 0.0404  0.0457  0.0382  113 PHE B CD1 
1754 C  CD2 . PHE B 113 ? 0.2137 0.2019 0.1799 0.0121  0.0495  0.0386  113 PHE B CD2 
1755 C  CE1 . PHE B 113 ? 0.2256 0.2228 0.1868 0.0454  0.0437  0.0347  113 PHE B CE1 
1756 C  CE2 . PHE B 113 ? 0.2089 0.2120 0.1832 0.0255  0.0531  0.0350  113 PHE B CE2 
1757 C  CZ  . PHE B 113 ? 0.2188 0.2198 0.1853 0.0476  0.0554  0.0393  113 PHE B CZ  
1758 N  N   . ALA B 114 ? 0.2204 0.1930 0.1845 0.0031  0.0454  0.0251  114 ALA B N   
1759 C  CA  . ALA B 114 ? 0.2481 0.1863 0.1983 0.0375  0.0604  0.0127  114 ALA B CA  
1760 C  C   . ALA B 114 ? 0.2608 0.2130 0.2188 0.0429  0.0523  -0.0091 114 ALA B C   
1761 O  O   . ALA B 114 ? 0.2627 0.2443 0.2342 0.0447  0.0476  -0.0193 114 ALA B O   
1762 C  CB  . ALA B 114 ? 0.2473 0.1734 0.1936 0.0475  0.0598  0.0272  114 ALA B CB  
1763 O  OXT . ALA B 114 ? 0.2829 0.2210 0.2224 0.0414  0.0414  -0.0075 114 ALA B OXT 
1764 N  N   . PRO C 1   ? 0.2406 0.2575 0.2217 0.0193  -0.0359 -0.1207 1   PRO C N   
1765 C  CA  . PRO C 1   ? 0.2263 0.2510 0.2075 0.0259  -0.0297 -0.1034 1   PRO C CA  
1766 C  C   . PRO C 1   ? 0.2188 0.2240 0.1929 0.0307  -0.0246 -0.0884 1   PRO C C   
1767 O  O   . PRO C 1   ? 0.2470 0.2112 0.2110 0.0290  -0.0484 -0.0748 1   PRO C O   
1768 C  CB  . PRO C 1   ? 0.2517 0.2774 0.2022 0.0327  -0.0171 -0.1139 1   PRO C CB  
1769 C  CG  . PRO C 1   ? 0.2679 0.2880 0.2168 0.0267  -0.0223 -0.1226 1   PRO C CG  
1770 C  CD  . PRO C 1   ? 0.2505 0.2723 0.2161 0.0243  -0.0381 -0.1234 1   PRO C CD  
1771 N  N   . MET C 2   ? 0.1871 0.2232 0.1630 0.0185  -0.0121 -0.0736 2   MET C N   
1772 C  CA  . MET C 2   ? 0.1900 0.2274 0.1651 -0.0146 -0.0088 -0.0543 2   MET C CA  
1773 C  C   . MET C 2   ? 0.1836 0.2011 0.1547 0.0035  -0.0195 -0.0225 2   MET C C   
1774 O  O   . MET C 2   ? 0.1989 0.2130 0.1757 0.0079  -0.0210 -0.0080 2   MET C O   
1775 C  CB  . MET C 2   ? 0.2249 0.2877 0.2013 -0.0557 0.0246  -0.0448 2   MET C CB  
1776 C  CG  . MET C 2   ? 0.2820 0.3235 0.2564 -0.0589 0.0583  -0.0434 2   MET C CG  
1777 S  SD  . MET C 2   ? 0.3399 0.3536 0.3129 -0.0652 0.0937  -0.0395 2   MET C SD  
1778 C  CE  . MET C 2   ? 0.3414 0.3526 0.3208 -0.0537 0.0966  -0.0511 2   MET C CE  
1779 N  N   . PHE C 3   ? 0.1707 0.1768 0.1372 0.0182  -0.0361 -0.0230 3   PHE C N   
1780 C  CA  . PHE C 3   ? 0.1728 0.1684 0.1360 0.0166  -0.0304 -0.0221 3   PHE C CA  
1781 C  C   . PHE C 3   ? 0.1630 0.1525 0.1300 -0.0002 -0.0196 -0.0276 3   PHE C C   
1782 O  O   . PHE C 3   ? 0.1844 0.1695 0.1336 0.0036  -0.0083 -0.0322 3   PHE C O   
1783 C  CB  . PHE C 3   ? 0.1898 0.1694 0.1315 0.0041  -0.0011 -0.0313 3   PHE C CB  
1784 C  CG  . PHE C 3   ? 0.1839 0.1605 0.1399 -0.0041 0.0229  -0.0535 3   PHE C CG  
1785 C  CD1 . PHE C 3   ? 0.2026 0.1680 0.1411 -0.0091 0.0331  -0.0526 3   PHE C CD1 
1786 C  CD2 . PHE C 3   ? 0.1942 0.1584 0.1841 -0.0114 0.0041  -0.0641 3   PHE C CD2 
1787 C  CE1 . PHE C 3   ? 0.2014 0.1698 0.1657 0.0046  0.0214  -0.0687 3   PHE C CE1 
1788 C  CE2 . PHE C 3   ? 0.2012 0.1701 0.2151 -0.0076 -0.0020 -0.0655 3   PHE C CE2 
1789 C  CZ  . PHE C 3   ? 0.1998 0.1773 0.2005 -0.0005 0.0104  -0.0588 3   PHE C CZ  
1790 N  N   . ILE C 4   ? 0.1426 0.1620 0.1290 -0.0137 -0.0033 -0.0360 4   ILE C N   
1791 C  CA  . ILE C 4   ? 0.1360 0.1675 0.1315 -0.0201 0.0025  -0.0271 4   ILE C CA  
1792 C  C   . ILE C 4   ? 0.1515 0.1546 0.1324 -0.0113 -0.0039 -0.0221 4   ILE C C   
1793 O  O   . ILE C 4   ? 0.1585 0.1554 0.1333 -0.0023 0.0036  -0.0208 4   ILE C O   
1794 C  CB  . ILE C 4   ? 0.1424 0.1997 0.1546 -0.0064 0.0282  -0.0308 4   ILE C CB  
1795 C  CG1 . ILE C 4   ? 0.1588 0.2497 0.1756 0.0054  0.0490  -0.0356 4   ILE C CG1 
1796 C  CG2 . ILE C 4   ? 0.1599 0.2050 0.1539 -0.0184 0.0357  -0.0286 4   ILE C CG2 
1797 C  CD1 . ILE C 4   ? 0.1954 0.2707 0.1933 0.0254  0.0498  -0.0292 4   ILE C CD1 
1798 N  N   . VAL C 5   ? 0.1615 0.1678 0.1313 -0.0164 -0.0267 -0.0190 5   VAL C N   
1799 C  CA  . VAL C 5   ? 0.1671 0.1806 0.1433 -0.0122 -0.0176 -0.0074 5   VAL C CA  
1800 C  C   . VAL C 5   ? 0.1793 0.1526 0.1261 -0.0130 -0.0204 -0.0033 5   VAL C C   
1801 O  O   . VAL C 5   ? 0.2120 0.1533 0.1379 -0.0059 -0.0262 -0.0136 5   VAL C O   
1802 C  CB  . VAL C 5   ? 0.1980 0.2383 0.1866 -0.0246 -0.0096 -0.0034 5   VAL C CB  
1803 C  CG1 . VAL C 5   ? 0.2467 0.2711 0.2210 -0.0321 -0.0151 0.0103  5   VAL C CG1 
1804 C  CG2 . VAL C 5   ? 0.1917 0.2452 0.1952 -0.0342 -0.0071 -0.0009 5   VAL C CG2 
1805 N  N   . ASN C 6   ? 0.1764 0.1556 0.1200 -0.0260 -0.0156 -0.0160 6   ASN C N   
1806 C  CA  . ASN C 6   ? 0.1562 0.1674 0.1382 -0.0130 -0.0033 -0.0304 6   ASN C CA  
1807 C  C   . ASN C 6   ? 0.1469 0.1664 0.1307 -0.0120 0.0081  -0.0197 6   ASN C C   
1808 O  O   . ASN C 6   ? 0.1494 0.1690 0.1224 -0.0290 -0.0080 -0.0123 6   ASN C O   
1809 C  CB  . ASN C 6   ? 0.1769 0.1857 0.1828 -0.0147 0.0377  -0.0450 6   ASN C CB  
1810 C  CG  . ASN C 6   ? 0.2160 0.2220 0.2584 0.0022  0.0537  -0.0695 6   ASN C CG  
1811 O  OD1 . ASN C 6   ? 0.2346 0.1996 0.3112 -0.0368 0.1023  -0.0607 6   ASN C OD1 
1812 N  ND2 . ASN C 6   ? 0.2244 0.2724 0.2831 -0.0006 0.0307  -0.1040 6   ASN C ND2 
1813 N  N   . THR C 7   ? 0.1519 0.1747 0.1248 0.0032  0.0170  -0.0162 7   THR C N   
1814 C  CA  . THR C 7   ? 0.1486 0.1714 0.1279 0.0109  0.0071  -0.0184 7   THR C CA  
1815 C  C   . THR C 7   ? 0.1518 0.1623 0.1195 -0.0074 -0.0049 -0.0156 7   THR C C   
1816 O  O   . THR C 7   ? 0.1454 0.1705 0.1132 -0.0247 0.0169  -0.0160 7   THR C O   
1817 C  CB  . THR C 7   ? 0.1514 0.1682 0.1441 0.0075  0.0207  -0.0054 7   THR C CB  
1818 O  OG1 . THR C 7   ? 0.1567 0.2017 0.1415 -0.0131 0.0122  -0.0122 7   THR C OG1 
1819 C  CG2 . THR C 7   ? 0.1616 0.1516 0.1649 -0.0004 0.0278  0.0097  7   THR C CG2 
1820 N  N   . ASN C 8   ? 0.1520 0.1629 0.1162 -0.0163 -0.0197 -0.0164 8   ASN C N   
1821 C  CA  . ASN C 8   ? 0.1575 0.1709 0.1261 -0.0265 -0.0445 -0.0099 8   ASN C CA  
1822 C  C   . ASN C 8   ? 0.1738 0.1931 0.1523 -0.0133 -0.0176 0.0001  8   ASN C C   
1823 O  O   . ASN C 8   ? 0.2074 0.2158 0.1642 0.0198  -0.0270 -0.0009 8   ASN C O   
1824 C  CB  . ASN C 8   ? 0.1841 0.1518 0.1351 -0.0365 -0.0307 0.0018  8   ASN C CB  
1825 C  CG  . ASN C 8   ? 0.2130 0.1473 0.1478 -0.0632 -0.0310 -0.0162 8   ASN C CG  
1826 O  OD1 . ASN C 8   ? 0.2038 0.1550 0.1422 -0.0588 -0.0136 -0.0115 8   ASN C OD1 
1827 N  ND2 . ASN C 8   ? 0.2469 0.1517 0.1592 -0.0808 -0.0461 0.0006  8   ASN C ND2 
1828 N  N   . VAL C 9   ? 0.1676 0.1719 0.1648 -0.0017 0.0019  -0.0240 9   VAL C N   
1829 C  CA  . VAL C 9   ? 0.2063 0.1974 0.1836 0.0128  0.0445  -0.0049 9   VAL C CA  
1830 C  C   . VAL C 9   ? 0.2196 0.2013 0.2009 0.0124  0.0548  0.0063  9   VAL C C   
1831 O  O   . VAL C 9   ? 0.2403 0.1852 0.2130 -0.0120 0.0548  0.0178  9   VAL C O   
1832 C  CB  . VAL C 9   ? 0.2203 0.2227 0.1942 0.0241  0.0674  0.0195  9   VAL C CB  
1833 C  CG1 . VAL C 9   ? 0.2402 0.2498 0.2054 0.0246  0.0596  0.0043  9   VAL C CG1 
1834 C  CG2 . VAL C 9   ? 0.2024 0.2316 0.2001 0.0116  0.0645  0.0322  9   VAL C CG2 
1835 N  N   . PRO C 10  ? 0.2323 0.2152 0.2068 0.0227  0.0193  0.0214  10  PRO C N   
1836 C  CA  . PRO C 10  ? 0.2400 0.2275 0.2224 0.0247  -0.0006 0.0191  10  PRO C CA  
1837 C  C   . PRO C 10  ? 0.2267 0.2226 0.2223 0.0266  -0.0031 0.0124  10  PRO C C   
1838 O  O   . PRO C 10  ? 0.2229 0.2374 0.2195 0.0437  0.0092  0.0128  10  PRO C O   
1839 C  CB  . PRO C 10  ? 0.2487 0.2470 0.2317 0.0321  -0.0170 0.0279  10  PRO C CB  
1840 C  CG  . PRO C 10  ? 0.2388 0.2614 0.2274 0.0462  -0.0165 0.0402  10  PRO C CG  
1841 C  CD  . PRO C 10  ? 0.2365 0.2350 0.2156 0.0378  -0.0006 0.0328  10  PRO C CD  
1842 N  N   . ARG C 11  ? 0.2281 0.2191 0.2368 0.0043  -0.0177 0.0017  11  ARG C N   
1843 C  CA  . ARG C 11  ? 0.2492 0.2219 0.2594 0.0004  -0.0183 -0.0094 11  ARG C CA  
1844 C  C   . ARG C 11  ? 0.2399 0.2031 0.2462 0.0110  -0.0272 0.0033  11  ARG C C   
1845 O  O   . ARG C 11  ? 0.2597 0.1888 0.2323 0.0047  -0.0284 -0.0033 11  ARG C O   
1846 C  CB  . ARG C 11  ? 0.2908 0.2746 0.3035 -0.0018 -0.0245 -0.0222 11  ARG C CB  
1847 C  CG  . ARG C 11  ? 0.3423 0.3316 0.3497 0.0007  -0.0259 -0.0360 11  ARG C CG  
1848 C  CD  . ARG C 11  ? 0.3866 0.3764 0.3956 0.0082  -0.0183 -0.0559 11  ARG C CD  
1849 N  NE  . ARG C 11  ? 0.4241 0.4142 0.4336 0.0155  -0.0061 -0.0652 11  ARG C NE  
1850 C  CZ  . ARG C 11  ? 0.4416 0.4329 0.4610 0.0122  0.0093  -0.0739 11  ARG C CZ  
1851 N  NH1 . ARG C 11  ? 0.4473 0.4371 0.4673 0.0101  0.0184  -0.0726 11  ARG C NH1 
1852 N  NH2 . ARG C 11  ? 0.4475 0.4379 0.4741 0.0103  0.0125  -0.0777 11  ARG C NH2 
1853 N  N   . ALA C 12  ? 0.2335 0.2053 0.2480 0.0458  -0.0301 0.0167  12  ALA C N   
1854 C  CA  . ALA C 12  ? 0.2526 0.2424 0.2588 0.0618  -0.0154 0.0001  12  ALA C CA  
1855 C  C   . ALA C 12  ? 0.2525 0.2487 0.2573 0.0727  0.0017  -0.0233 12  ALA C C   
1856 O  O   . ALA C 12  ? 0.2525 0.2830 0.2745 0.0989  0.0064  -0.0256 12  ALA C O   
1857 C  CB  . ALA C 12  ? 0.2627 0.2619 0.2655 0.0619  -0.0163 0.0073  12  ALA C CB  
1858 N  N   A SER C 13  ? 0.2533 0.2404 0.2507 0.0515  -0.0070 -0.0242 13  SER C N   
1859 N  N   B SER C 13  ? 0.2534 0.2498 0.2529 0.0440  0.0012  -0.0257 13  SER C N   
1860 C  CA  A SER C 13  ? 0.2577 0.2554 0.2417 0.0055  0.0079  -0.0311 13  SER C CA  
1861 C  CA  B SER C 13  ? 0.2608 0.2610 0.2470 0.0048  0.0066  -0.0301 13  SER C CA  
1862 C  C   A SER C 13  ? 0.2592 0.2693 0.2222 -0.0081 0.0168  -0.0288 13  SER C C   
1863 C  C   B SER C 13  ? 0.2568 0.2642 0.2267 -0.0068 0.0132  -0.0332 13  SER C C   
1864 O  O   A SER C 13  ? 0.2829 0.3031 0.2201 -0.0295 0.0213  -0.0175 13  SER C O   
1865 O  O   B SER C 13  ? 0.2669 0.2827 0.2232 -0.0195 0.0173  -0.0268 13  SER C O   
1866 C  CB  A SER C 13  ? 0.2805 0.2699 0.2608 -0.0329 0.0033  -0.0299 13  SER C CB  
1867 C  CB  B SER C 13  ? 0.2777 0.2726 0.2614 -0.0220 0.0037  -0.0309 13  SER C CB  
1868 O  OG  A SER C 13  ? 0.2968 0.2883 0.2817 -0.0461 -0.0017 -0.0353 13  SER C OG  
1869 O  OG  B SER C 13  ? 0.2894 0.2817 0.2714 -0.0366 0.0021  -0.0325 13  SER C OG  
1870 N  N   . VAL C 14  ? 0.2445 0.2434 0.2125 -0.0004 0.0144  -0.0470 14  VAL C N   
1871 C  CA  . VAL C 14  ? 0.2393 0.2242 0.1970 0.0003  0.0184  -0.0510 14  VAL C CA  
1872 C  C   . VAL C 14  ? 0.2448 0.2188 0.2011 -0.0026 0.0203  -0.0495 14  VAL C C   
1873 O  O   . VAL C 14  ? 0.2616 0.2195 0.2069 -0.0159 0.0173  -0.0565 14  VAL C O   
1874 C  CB  . VAL C 14  ? 0.2314 0.2054 0.1875 -0.0100 0.0133  -0.0366 14  VAL C CB  
1875 C  CG1 . VAL C 14  ? 0.2500 0.2181 0.1858 -0.0111 0.0051  -0.0465 14  VAL C CG1 
1876 C  CG2 . VAL C 14  ? 0.2459 0.2019 0.1901 -0.0056 0.0141  -0.0232 14  VAL C CG2 
1877 N  N   . PRO C 15  ? 0.2327 0.2147 0.1929 0.0089  0.0313  -0.0484 15  PRO C N   
1878 C  CA  . PRO C 15  ? 0.2246 0.2142 0.1871 0.0149  0.0384  -0.0480 15  PRO C CA  
1879 C  C   . PRO C 15  ? 0.2208 0.1986 0.1729 0.0222  0.0265  -0.0392 15  PRO C C   
1880 O  O   . PRO C 15  ? 0.2090 0.1986 0.1663 0.0443  0.0125  -0.0317 15  PRO C O   
1881 C  CB  . PRO C 15  ? 0.2294 0.2295 0.1973 0.0199  0.0535  -0.0395 15  PRO C CB  
1882 C  CG  . PRO C 15  ? 0.2421 0.2342 0.2041 0.0196  0.0490  -0.0440 15  PRO C CG  
1883 C  CD  . PRO C 15  ? 0.2471 0.2072 0.1975 0.0089  0.0404  -0.0583 15  PRO C CD  
1884 N  N   . ASP C 16  ? 0.2328 0.1859 0.1699 0.0129  0.0123  -0.0342 16  ASP C N   
1885 C  CA  . ASP C 16  ? 0.2220 0.1733 0.1704 0.0248  -0.0085 -0.0385 16  ASP C CA  
1886 C  C   . ASP C 16  ? 0.2123 0.1796 0.1674 0.0073  -0.0007 -0.0153 16  ASP C C   
1887 O  O   . ASP C 16  ? 0.2493 0.2169 0.1654 0.0110  0.0272  -0.0240 16  ASP C O   
1888 C  CB  . ASP C 16  ? 0.2444 0.1734 0.1806 0.0574  -0.0400 -0.0310 16  ASP C CB  
1889 C  CG  . ASP C 16  ? 0.2743 0.1878 0.1866 0.0776  -0.0610 -0.0325 16  ASP C CG  
1890 O  OD1 . ASP C 16  ? 0.3075 0.2308 0.1935 0.0758  -0.0424 -0.0298 16  ASP C OD1 
1891 O  OD2 . ASP C 16  ? 0.3004 0.2035 0.1971 0.0860  -0.0713 -0.0282 16  ASP C OD2 
1892 N  N   . GLY C 17  ? 0.1747 0.1676 0.1650 -0.0064 -0.0213 -0.0089 17  GLY C N   
1893 C  CA  . GLY C 17  ? 0.2117 0.1730 0.1697 0.0076  -0.0262 -0.0191 17  GLY C CA  
1894 C  C   . GLY C 17  ? 0.2159 0.1825 0.1605 0.0210  -0.0052 -0.0322 17  GLY C C   
1895 O  O   . GLY C 17  ? 0.2321 0.2063 0.1493 0.0326  0.0013  -0.0346 17  GLY C O   
1896 N  N   . PHE C 18  ? 0.2047 0.1672 0.1729 0.0045  0.0209  -0.0365 18  PHE C N   
1897 C  CA  . PHE C 18  ? 0.1925 0.1597 0.1799 -0.0060 0.0010  -0.0538 18  PHE C CA  
1898 C  C   . PHE C 18  ? 0.1977 0.1740 0.1733 -0.0073 0.0058  -0.0432 18  PHE C C   
1899 O  O   . PHE C 18  ? 0.2088 0.1794 0.1638 0.0121  -0.0152 -0.0426 18  PHE C O   
1900 C  CB  . PHE C 18  ? 0.1787 0.1685 0.1976 -0.0087 -0.0083 -0.0624 18  PHE C CB  
1901 C  CG  . PHE C 18  ? 0.1733 0.1693 0.2362 0.0222  -0.0061 -0.0590 18  PHE C CG  
1902 C  CD1 . PHE C 18  ? 0.1977 0.1618 0.2636 0.0026  -0.0148 -0.0546 18  PHE C CD1 
1903 C  CD2 . PHE C 18  ? 0.1912 0.1557 0.2455 0.0431  -0.0222 -0.0693 18  PHE C CD2 
1904 C  CE1 . PHE C 18  ? 0.2045 0.1612 0.2756 -0.0007 -0.0185 -0.0528 18  PHE C CE1 
1905 C  CE2 . PHE C 18  ? 0.2029 0.1649 0.2536 0.0187  -0.0224 -0.0730 18  PHE C CE2 
1906 C  CZ  . PHE C 18  ? 0.2057 0.1840 0.2719 0.0006  -0.0270 -0.0589 18  PHE C CZ  
1907 N  N   . LEU C 19  ? 0.1775 0.1741 0.1614 -0.0106 0.0180  -0.0418 19  LEU C N   
1908 C  CA  . LEU C 19  ? 0.1870 0.2106 0.1580 0.0032  0.0187  -0.0371 19  LEU C CA  
1909 C  C   . LEU C 19  ? 0.1820 0.1995 0.1569 0.0240  0.0133  -0.0323 19  LEU C C   
1910 O  O   . LEU C 19  ? 0.1783 0.1775 0.1619 0.0160  0.0107  -0.0367 19  LEU C O   
1911 C  CB  . LEU C 19  ? 0.2118 0.2448 0.1577 0.0215  0.0307  -0.0486 19  LEU C CB  
1912 C  CG  . LEU C 19  ? 0.2464 0.2839 0.1746 0.0220  0.0338  -0.0341 19  LEU C CG  
1913 C  CD1 . LEU C 19  ? 0.2554 0.3079 0.1921 -0.0004 0.0449  -0.0229 19  LEU C CD1 
1914 C  CD2 . LEU C 19  ? 0.2573 0.2874 0.1809 0.0370  0.0161  -0.0467 19  LEU C CD2 
1915 N  N   A SER C 20  ? 0.1865 0.2104 0.1584 0.0415  0.0144  -0.0298 20  SER C N   
1916 N  N   B SER C 20  ? 0.1872 0.2099 0.1517 0.0422  0.0134  -0.0362 20  SER C N   
1917 C  CA  A SER C 20  ? 0.1942 0.2187 0.1619 0.0609  0.0179  -0.0213 20  SER C CA  
1918 C  CA  B SER C 20  ? 0.1943 0.2118 0.1490 0.0670  0.0170  -0.0283 20  SER C CA  
1919 C  C   A SER C 20  ? 0.1847 0.2131 0.1497 0.0417  0.0106  -0.0253 20  SER C C   
1920 C  C   B SER C 20  ? 0.1875 0.2100 0.1422 0.0421  0.0063  -0.0313 20  SER C C   
1921 O  O   A SER C 20  ? 0.1851 0.2091 0.1369 0.0397  -0.0002 -0.0364 20  SER C O   
1922 O  O   B SER C 20  ? 0.1882 0.2067 0.1260 0.0408  -0.0087 -0.0468 20  SER C O   
1923 C  CB  A SER C 20  ? 0.2130 0.2414 0.1859 0.0865  0.0238  -0.0076 20  SER C CB  
1924 C  CB  B SER C 20  ? 0.2148 0.2318 0.1706 0.0909  0.0187  -0.0150 20  SER C CB  
1925 O  OG  A SER C 20  ? 0.2254 0.2602 0.2035 0.0982  0.0284  -0.0018 20  SER C OG  
1926 O  OG  B SER C 20  ? 0.2435 0.2526 0.1865 0.0837  0.0154  -0.0162 20  SER C OG  
1927 N  N   . GLU C 21  ? 0.1726 0.2158 0.1536 0.0284  0.0196  -0.0149 21  GLU C N   
1928 C  CA  . GLU C 21  ? 0.1512 0.2217 0.1627 0.0206  0.0199  -0.0168 21  GLU C CA  
1929 C  C   . GLU C 21  ? 0.1577 0.1895 0.1450 0.0378  0.0118  -0.0154 21  GLU C C   
1930 O  O   . GLU C 21  ? 0.1743 0.1882 0.1587 0.0299  -0.0031 -0.0119 21  GLU C O   
1931 C  CB  . GLU C 21  ? 0.1548 0.2496 0.1844 0.0166  0.0347  -0.0136 21  GLU C CB  
1932 C  CG  . GLU C 21  ? 0.1974 0.2825 0.2323 0.0050  0.0441  -0.0045 21  GLU C CG  
1933 C  CD  . GLU C 21  ? 0.2327 0.3144 0.2700 0.0052  0.0510  -0.0061 21  GLU C CD  
1934 O  OE1 . GLU C 21  ? 0.2425 0.3218 0.2843 -0.0047 0.0435  -0.0329 21  GLU C OE1 
1935 O  OE2 . GLU C 21  ? 0.2660 0.3373 0.2939 0.0221  0.0565  0.0021  21  GLU C OE2 
1936 N  N   . LEU C 22  ? 0.1690 0.1822 0.1497 0.0327  -0.0006 -0.0305 22  LEU C N   
1937 C  CA  . LEU C 22  ? 0.1698 0.1774 0.1471 0.0305  -0.0050 -0.0514 22  LEU C CA  
1938 C  C   . LEU C 22  ? 0.1828 0.1795 0.1430 0.0284  -0.0004 -0.0607 22  LEU C C   
1939 O  O   . LEU C 22  ? 0.2345 0.1714 0.1528 0.0244  -0.0092 -0.0497 22  LEU C O   
1940 C  CB  . LEU C 22  ? 0.1872 0.1799 0.1572 0.0108  -0.0019 -0.0612 22  LEU C CB  
1941 C  CG  . LEU C 22  ? 0.2138 0.1971 0.1760 0.0063  -0.0166 -0.0490 22  LEU C CG  
1942 C  CD1 . LEU C 22  ? 0.2251 0.2050 0.1725 0.0170  -0.0335 -0.0473 22  LEU C CD1 
1943 C  CD2 . LEU C 22  ? 0.2341 0.2081 0.1871 -0.0150 -0.0317 -0.0427 22  LEU C CD2 
1944 N  N   . THR C 23  ? 0.1659 0.1746 0.1469 0.0361  0.0180  -0.0598 23  THR C N   
1945 C  CA  . THR C 23  ? 0.1763 0.2061 0.1471 0.0028  0.0022  -0.0754 23  THR C CA  
1946 C  C   . THR C 23  ? 0.1791 0.2209 0.1452 0.0177  -0.0259 -0.0739 23  THR C C   
1947 O  O   . THR C 23  ? 0.1681 0.2189 0.1547 0.0319  -0.0421 -0.0675 23  THR C O   
1948 C  CB  . THR C 23  ? 0.1555 0.2050 0.1596 -0.0080 0.0089  -0.0728 23  THR C CB  
1949 O  OG1 . THR C 23  ? 0.1624 0.2085 0.1574 0.0023  0.0205  -0.0618 23  THR C OG1 
1950 C  CG2 . THR C 23  ? 0.1570 0.2003 0.1700 -0.0105 0.0043  -0.0841 23  THR C CG2 
1951 N  N   . GLN C 24  ? 0.1841 0.2172 0.1368 0.0209  -0.0083 -0.0798 24  GLN C N   
1952 C  CA  . GLN C 24  ? 0.1946 0.2169 0.1466 0.0507  -0.0164 -0.0849 24  GLN C CA  
1953 C  C   . GLN C 24  ? 0.1996 0.2314 0.1395 0.0511  -0.0098 -0.0606 24  GLN C C   
1954 O  O   . GLN C 24  ? 0.2377 0.2633 0.1347 0.0432  -0.0247 -0.0555 24  GLN C O   
1955 C  CB  . GLN C 24  ? 0.1965 0.2260 0.1893 0.0460  -0.0172 -0.0861 24  GLN C CB  
1956 C  CG  . GLN C 24  ? 0.2117 0.2401 0.2154 0.0485  -0.0248 -0.0964 24  GLN C CG  
1957 C  CD  . GLN C 24  ? 0.2235 0.2916 0.2434 0.0537  -0.0383 -0.0755 24  GLN C CD  
1958 O  OE1 . GLN C 24  ? 0.2414 0.3044 0.2501 0.0702  -0.0107 -0.0601 24  GLN C OE1 
1959 N  NE2 . GLN C 24  ? 0.2294 0.3126 0.2583 0.0572  -0.0594 -0.0808 24  GLN C NE2 
1960 N  N   . GLN C 25  ? 0.1984 0.2263 0.1569 0.0634  0.0104  -0.0499 25  GLN C N   
1961 C  CA  . GLN C 25  ? 0.2195 0.2456 0.1743 0.0685  -0.0112 -0.0317 25  GLN C CA  
1962 C  C   . GLN C 25  ? 0.1956 0.2473 0.1600 0.0487  -0.0253 -0.0425 25  GLN C C   
1963 O  O   . GLN C 25  ? 0.1991 0.2390 0.1602 0.0689  -0.0515 -0.0287 25  GLN C O   
1964 C  CB  . GLN C 25  ? 0.2401 0.2554 0.2082 0.0880  -0.0136 -0.0006 25  GLN C CB  
1965 C  CG  . GLN C 25  ? 0.2655 0.2819 0.2428 0.0866  -0.0018 0.0213  25  GLN C CG  
1966 C  CD  . GLN C 25  ? 0.3040 0.3128 0.2714 0.0973  0.0208  0.0424  25  GLN C CD  
1967 O  OE1 . GLN C 25  ? 0.3257 0.3179 0.2822 0.1073  0.0275  0.0603  25  GLN C OE1 
1968 N  NE2 . GLN C 25  ? 0.3188 0.3378 0.2793 0.0923  0.0460  0.0311  25  GLN C NE2 
1969 N  N   . LEU C 26  ? 0.1905 0.2545 0.1612 0.0431  -0.0056 -0.0577 26  LEU C N   
1970 C  CA  . LEU C 26  ? 0.2054 0.2541 0.1648 0.0413  -0.0175 -0.0617 26  LEU C CA  
1971 C  C   . LEU C 26  ? 0.2303 0.2519 0.1785 0.0389  -0.0469 -0.0582 26  LEU C C   
1972 O  O   . LEU C 26  ? 0.2364 0.2776 0.1867 0.0474  -0.0377 -0.0425 26  LEU C O   
1973 C  CB  . LEU C 26  ? 0.2156 0.2643 0.1618 0.0233  -0.0057 -0.0715 26  LEU C CB  
1974 C  CG  . LEU C 26  ? 0.2110 0.2682 0.1678 0.0215  -0.0053 -0.0794 26  LEU C CG  
1975 C  CD1 . LEU C 26  ? 0.2098 0.2990 0.1644 0.0152  -0.0098 -0.0586 26  LEU C CD1 
1976 C  CD2 . LEU C 26  ? 0.1988 0.2382 0.1783 0.0243  0.0052  -0.0999 26  LEU C CD2 
1977 N  N   . ALA C 27  ? 0.2558 0.2305 0.1821 0.0121  -0.0753 -0.0669 27  ALA C N   
1978 C  CA  . ALA C 27  ? 0.2956 0.2437 0.2003 0.0091  -0.0844 -0.0617 27  ALA C CA  
1979 C  C   . ALA C 27  ? 0.3237 0.2529 0.2135 0.0111  -0.0703 -0.0636 27  ALA C C   
1980 O  O   . ALA C 27  ? 0.3338 0.2767 0.2186 -0.0006 -0.0839 -0.0567 27  ALA C O   
1981 C  CB  . ALA C 27  ? 0.2987 0.2462 0.2059 0.0093  -0.0907 -0.0603 27  ALA C CB  
1982 N  N   . GLN C 28  ? 0.3284 0.2481 0.2109 0.0300  -0.0420 -0.0695 28  GLN C N   
1983 C  CA  . GLN C 28  ? 0.3414 0.2763 0.2168 0.0470  -0.0307 -0.0559 28  GLN C CA  
1984 C  C   . GLN C 28  ? 0.3286 0.2637 0.1990 0.0523  -0.0304 -0.0552 28  GLN C C   
1985 O  O   . GLN C 28  ? 0.3341 0.2582 0.1827 0.0598  -0.0233 -0.0359 28  GLN C O   
1986 C  CB  . GLN C 28  ? 0.3716 0.3210 0.2492 0.0554  -0.0185 -0.0488 28  GLN C CB  
1987 C  CG  . GLN C 28  ? 0.4024 0.3757 0.2912 0.0570  -0.0079 -0.0389 28  GLN C CG  
1988 C  CD  . GLN C 28  ? 0.4304 0.4319 0.3332 0.0599  -0.0034 -0.0295 28  GLN C CD  
1989 O  OE1 . GLN C 28  ? 0.4510 0.4421 0.3420 0.0609  -0.0050 -0.0225 28  GLN C OE1 
1990 N  NE2 . GLN C 28  ? 0.4309 0.4605 0.3550 0.0649  0.0037  -0.0285 28  GLN C NE2 
1991 N  N   . ALA C 29  ? 0.2945 0.2644 0.1892 0.0589  -0.0323 -0.0773 29  ALA C N   
1992 C  CA  . ALA C 29  ? 0.2776 0.2720 0.1888 0.0643  -0.0375 -0.0835 29  ALA C CA  
1993 C  C   . ALA C 29  ? 0.2618 0.2861 0.1977 0.0725  -0.0435 -0.0882 29  ALA C C   
1994 O  O   . ALA C 29  ? 0.2638 0.3002 0.2177 0.0772  -0.0422 -0.0881 29  ALA C O   
1995 C  CB  . ALA C 29  ? 0.2816 0.2760 0.1806 0.0565  -0.0389 -0.0940 29  ALA C CB  
1996 N  N   . THR C 30  ? 0.2470 0.2984 0.2004 0.0707  -0.0458 -0.0848 30  THR C N   
1997 C  CA  . THR C 30  ? 0.2356 0.3173 0.1918 0.0687  -0.0474 -0.0808 30  THR C CA  
1998 C  C   . THR C 30  ? 0.2426 0.3313 0.1949 0.0701  -0.0555 -0.0795 30  THR C C   
1999 O  O   . THR C 30  ? 0.2347 0.3398 0.1973 0.0819  -0.0490 -0.0775 30  THR C O   
2000 C  CB  . THR C 30  ? 0.2406 0.3269 0.1892 0.0556  -0.0462 -0.0915 30  THR C CB  
2001 O  OG1 . THR C 30  ? 0.2520 0.3396 0.1847 0.0559  -0.0228 -0.0834 30  THR C OG1 
2002 C  CG2 . THR C 30  ? 0.2454 0.3328 0.1906 0.0576  -0.0496 -0.0956 30  THR C CG2 
2003 N  N   . GLY C 31  ? 0.2521 0.3359 0.1905 0.0523  -0.0604 -0.0930 31  GLY C N   
2004 C  CA  . GLY C 31  ? 0.2505 0.3302 0.1859 0.0399  -0.0674 -0.0933 31  GLY C CA  
2005 C  C   . GLY C 31  ? 0.2658 0.3278 0.1967 0.0466  -0.0560 -0.0935 31  GLY C C   
2006 O  O   . GLY C 31  ? 0.2826 0.3591 0.2100 0.0437  -0.0446 -0.0888 31  GLY C O   
2007 N  N   . LYS C 32  ? 0.2776 0.2989 0.2060 0.0621  -0.0509 -0.0829 32  LYS C N   
2008 C  CA  . LYS C 32  ? 0.2797 0.2701 0.2065 0.0657  -0.0520 -0.0800 32  LYS C CA  
2009 C  C   . LYS C 32  ? 0.2996 0.2786 0.1950 0.0621  -0.0548 -0.0723 32  LYS C C   
2010 O  O   . LYS C 32  ? 0.3160 0.2972 0.1987 0.0720  -0.0388 -0.0725 32  LYS C O   
2011 C  CB  . LYS C 32  ? 0.2768 0.2518 0.2307 0.0702  -0.0451 -0.0605 32  LYS C CB  
2012 C  CG  . LYS C 32  ? 0.2794 0.2406 0.2491 0.0671  -0.0601 -0.0497 32  LYS C CG  
2013 C  CD  . LYS C 32  ? 0.2565 0.2242 0.2624 0.0830  -0.0617 -0.0453 32  LYS C CD  
2014 C  CE  . LYS C 32  ? 0.2480 0.2263 0.2709 0.0714  -0.0595 -0.0504 32  LYS C CE  
2015 N  NZ  . LYS C 32  ? 0.2580 0.2247 0.2806 0.0424  -0.0654 -0.0586 32  LYS C NZ  
2016 N  N   . PRO C 33  ? 0.3169 0.2711 0.1975 0.0496  -0.0636 -0.0714 33  PRO C N   
2017 C  CA  . PRO C 33  ? 0.3339 0.2817 0.2152 0.0445  -0.0600 -0.0658 33  PRO C CA  
2018 C  C   . PRO C 33  ? 0.3411 0.2822 0.2062 0.0443  -0.0427 -0.0809 33  PRO C C   
2019 O  O   . PRO C 33  ? 0.3441 0.2888 0.1981 0.0213  -0.0551 -0.0925 33  PRO C O   
2020 C  CB  . PRO C 33  ? 0.3318 0.2797 0.2224 0.0411  -0.0676 -0.0595 33  PRO C CB  
2021 C  CG  . PRO C 33  ? 0.3324 0.2737 0.2202 0.0415  -0.0613 -0.0660 33  PRO C CG  
2022 C  CD  . PRO C 33  ? 0.3154 0.2612 0.2051 0.0369  -0.0711 -0.0732 33  PRO C CD  
2023 N  N   . PRO C 34  ? 0.3413 0.2705 0.2046 0.0721  -0.0155 -0.0881 34  PRO C N   
2024 C  CA  . PRO C 34  ? 0.3509 0.2709 0.2184 0.0508  -0.0109 -0.0775 34  PRO C CA  
2025 C  C   . PRO C 34  ? 0.3595 0.2822 0.2329 0.0091  -0.0136 -0.0829 34  PRO C C   
2026 O  O   . PRO C 34  ? 0.3648 0.2720 0.2215 -0.0076 -0.0255 -0.0802 34  PRO C O   
2027 C  CB  . PRO C 34  ? 0.3586 0.2814 0.2182 0.0604  -0.0035 -0.0736 34  PRO C CB  
2028 C  CG  . PRO C 34  ? 0.3579 0.2846 0.2177 0.0688  -0.0036 -0.0723 34  PRO C CG  
2029 C  CD  . PRO C 34  ? 0.3436 0.2791 0.2132 0.0793  -0.0026 -0.0810 34  PRO C CD  
2030 N  N   . GLN C 35  ? 0.3652 0.3180 0.2535 -0.0247 -0.0155 -0.0997 35  GLN C N   
2031 C  CA  . GLN C 35  ? 0.3691 0.3677 0.2946 -0.0358 -0.0207 -0.0907 35  GLN C CA  
2032 C  C   . GLN C 35  ? 0.3601 0.4089 0.2873 -0.0428 -0.0324 -0.1094 35  GLN C C   
2033 O  O   . GLN C 35  ? 0.3723 0.4486 0.3007 -0.0540 -0.0296 -0.0950 35  GLN C O   
2034 C  CB  . GLN C 35  ? 0.3834 0.3817 0.3361 -0.0200 -0.0131 -0.0591 35  GLN C CB  
2035 C  CG  . GLN C 35  ? 0.3926 0.3939 0.3681 -0.0049 -0.0061 -0.0315 35  GLN C CG  
2036 C  CD  . GLN C 35  ? 0.3982 0.3979 0.3868 -0.0011 -0.0025 -0.0172 35  GLN C CD  
2037 O  OE1 . GLN C 35  ? 0.4133 0.4096 0.3948 -0.0006 -0.0101 -0.0044 35  GLN C OE1 
2038 N  NE2 . GLN C 35  ? 0.3991 0.3917 0.3837 -0.0091 0.0100  -0.0265 35  GLN C NE2 
2039 N  N   . TYR C 36  ? 0.3333 0.3999 0.2778 -0.0417 -0.0464 -0.1433 36  TYR C N   
2040 C  CA  . TYR C 36  ? 0.3045 0.4008 0.2914 -0.0199 -0.0440 -0.1298 36  TYR C CA  
2041 C  C   . TYR C 36  ? 0.2377 0.3446 0.2374 -0.0019 -0.0231 -0.1165 36  TYR C C   
2042 O  O   . TYR C 36  ? 0.2225 0.3768 0.2433 0.0106  0.0076  -0.1205 36  TYR C O   
2043 C  CB  . TYR C 36  ? 0.3375 0.4402 0.3494 -0.0287 -0.0734 -0.1389 36  TYR C CB  
2044 C  CG  . TYR C 36  ? 0.3782 0.4741 0.4080 -0.0346 -0.0874 -0.1351 36  TYR C CG  
2045 C  CD1 . TYR C 36  ? 0.3922 0.4866 0.4335 -0.0397 -0.0974 -0.1346 36  TYR C CD1 
2046 C  CD2 . TYR C 36  ? 0.3996 0.4928 0.4339 -0.0342 -0.0911 -0.1277 36  TYR C CD2 
2047 C  CE1 . TYR C 36  ? 0.4031 0.4991 0.4533 -0.0407 -0.1054 -0.1266 36  TYR C CE1 
2048 C  CE2 . TYR C 36  ? 0.4093 0.5008 0.4498 -0.0406 -0.1056 -0.1247 36  TYR C CE2 
2049 C  CZ  . TYR C 36  ? 0.4093 0.5045 0.4597 -0.0483 -0.1157 -0.1216 36  TYR C CZ  
2050 O  OH  . TYR C 36  ? 0.4143 0.5111 0.4705 -0.0627 -0.1328 -0.1130 36  TYR C OH  
2051 N  N   A ILE C 37  ? 0.2177 0.3052 0.2094 -0.0038 -0.0245 -0.1051 37  ILE C N   
2052 N  N   B ILE C 37  ? 0.2166 0.3062 0.2067 -0.0062 -0.0240 -0.1047 37  ILE C N   
2053 C  CA  A ILE C 37  ? 0.2050 0.2571 0.1862 0.0051  -0.0294 -0.0968 37  ILE C CA  
2054 C  CA  B ILE C 37  ? 0.2022 0.2549 0.1818 0.0045  -0.0305 -0.0987 37  ILE C CA  
2055 C  C   A ILE C 37  ? 0.2042 0.2212 0.1703 0.0030  -0.0152 -0.0902 37  ILE C C   
2056 C  C   B ILE C 37  ? 0.2055 0.2192 0.1700 0.0052  -0.0146 -0.0914 37  ILE C C   
2057 O  O   A ILE C 37  ? 0.2254 0.2146 0.1726 -0.0089 -0.0103 -0.0890 37  ILE C O   
2058 O  O   B ILE C 37  ? 0.2337 0.2148 0.1732 -0.0124 -0.0086 -0.0906 37  ILE C O   
2059 C  CB  A ILE C 37  ? 0.2094 0.2561 0.1864 0.0229  -0.0383 -0.0928 37  ILE C CB  
2060 C  CB  B ILE C 37  ? 0.2078 0.2554 0.1812 0.0250  -0.0381 -0.0947 37  ILE C CB  
2061 C  CG1 A ILE C 37  ? 0.2334 0.2632 0.1966 0.0283  -0.0521 -0.0824 37  ILE C CG1 
2062 C  CG1 B ILE C 37  ? 0.2328 0.2651 0.1895 0.0339  -0.0495 -0.0848 37  ILE C CG1 
2063 C  CG2 A ILE C 37  ? 0.2026 0.2560 0.1860 0.0236  -0.0309 -0.0931 37  ILE C CG2 
2064 C  CG2 B ILE C 37  ? 0.2021 0.2568 0.1837 0.0224  -0.0290 -0.0939 37  ILE C CG2 
2065 C  CD1 A ILE C 37  ? 0.2502 0.2688 0.2038 0.0282  -0.0609 -0.0721 37  ILE C CD1 
2066 C  CD1 B ILE C 37  ? 0.2493 0.2767 0.1984 0.0427  -0.0539 -0.0670 37  ILE C CD1 
2067 N  N   . ALA C 38  ? 0.1852 0.2061 0.1469 -0.0027 -0.0096 -0.0829 38  ALA C N   
2068 C  CA  . ALA C 38  ? 0.1614 0.1828 0.1421 0.0063  -0.0122 -0.0610 38  ALA C CA  
2069 C  C   . ALA C 38  ? 0.1692 0.1647 0.1466 0.0019  -0.0066 -0.0509 38  ALA C C   
2070 O  O   . ALA C 38  ? 0.1850 0.1589 0.1547 -0.0083 -0.0030 -0.0438 38  ALA C O   
2071 C  CB  . ALA C 38  ? 0.1586 0.1943 0.1618 0.0124  -0.0018 -0.0451 38  ALA C CB  
2072 N  N   . VAL C 39  ? 0.1689 0.1737 0.1313 -0.0008 0.0026  -0.0595 39  VAL C N   
2073 C  CA  . VAL C 39  ? 0.1788 0.1792 0.1303 -0.0012 -0.0051 -0.0498 39  VAL C CA  
2074 C  C   . VAL C 39  ? 0.1761 0.1653 0.1411 -0.0145 -0.0143 -0.0657 39  VAL C C   
2075 O  O   . VAL C 39  ? 0.1887 0.1652 0.1602 -0.0206 -0.0148 -0.0680 39  VAL C O   
2076 C  CB  . VAL C 39  ? 0.1947 0.1951 0.1367 0.0080  -0.0034 -0.0397 39  VAL C CB  
2077 C  CG1 . VAL C 39  ? 0.1985 0.2246 0.1264 -0.0046 -0.0163 -0.0401 39  VAL C CG1 
2078 C  CG2 . VAL C 39  ? 0.2346 0.2251 0.1731 0.0131  -0.0019 -0.0286 39  VAL C CG2 
2079 N  N   . HIS C 40  ? 0.1405 0.1506 0.1300 -0.0212 -0.0167 -0.0527 40  HIS C N   
2080 C  CA  . HIS C 40  ? 0.1415 0.1518 0.1303 -0.0079 0.0007  -0.0335 40  HIS C CA  
2081 C  C   . HIS C 40  ? 0.1573 0.1459 0.1310 -0.0158 -0.0081 -0.0300 40  HIS C C   
2082 O  O   . HIS C 40  ? 0.1704 0.1496 0.1165 -0.0439 -0.0115 -0.0154 40  HIS C O   
2083 C  CB  . HIS C 40  ? 0.1544 0.1574 0.1323 -0.0190 0.0127  -0.0194 40  HIS C CB  
2084 C  CG  . HIS C 40  ? 0.1737 0.1555 0.1468 -0.0182 0.0071  -0.0304 40  HIS C CG  
2085 N  ND1 . HIS C 40  ? 0.1873 0.1416 0.1570 -0.0184 0.0062  -0.0266 40  HIS C ND1 
2086 C  CD2 . HIS C 40  ? 0.1826 0.1664 0.1634 -0.0305 0.0163  -0.0252 40  HIS C CD2 
2087 C  CE1 . HIS C 40  ? 0.1940 0.1514 0.1609 -0.0175 0.0266  -0.0206 40  HIS C CE1 
2088 N  NE2 . HIS C 40  ? 0.1857 0.1500 0.1646 -0.0206 0.0245  -0.0204 40  HIS C NE2 
2089 N  N   . VAL C 41  ? 0.1461 0.1389 0.1349 -0.0067 0.0062  -0.0224 41  VAL C N   
2090 C  CA  . VAL C 41  ? 0.1415 0.1555 0.1343 -0.0002 0.0201  -0.0268 41  VAL C CA  
2091 C  C   . VAL C 41  ? 0.1607 0.1248 0.1430 -0.0157 0.0128  -0.0116 41  VAL C C   
2092 O  O   . VAL C 41  ? 0.2034 0.1193 0.1518 -0.0052 -0.0051 -0.0139 41  VAL C O   
2093 C  CB  . VAL C 41  ? 0.1451 0.2038 0.1450 0.0030  0.0277  -0.0172 41  VAL C CB  
2094 C  CG1 . VAL C 41  ? 0.1552 0.2205 0.1680 -0.0072 0.0325  -0.0126 41  VAL C CG1 
2095 C  CG2 . VAL C 41  ? 0.1665 0.2219 0.1546 0.0030  0.0197  -0.0022 41  VAL C CG2 
2096 N  N   . VAL C 42  ? 0.1702 0.1352 0.1420 -0.0090 0.0330  -0.0243 42  VAL C N   
2097 C  CA  . VAL C 42  ? 0.1867 0.1416 0.1399 -0.0030 0.0335  -0.0222 42  VAL C CA  
2098 C  C   . VAL C 42  ? 0.1624 0.1143 0.1411 0.0067  0.0150  -0.0157 42  VAL C C   
2099 O  O   . VAL C 42  ? 0.1637 0.1279 0.1398 0.0023  -0.0097 -0.0081 42  VAL C O   
2100 C  CB  . VAL C 42  ? 0.1933 0.1761 0.1492 -0.0125 0.0524  -0.0354 42  VAL C CB  
2101 C  CG1 . VAL C 42  ? 0.1974 0.2041 0.1368 -0.0376 0.0681  -0.0456 42  VAL C CG1 
2102 C  CG2 . VAL C 42  ? 0.1805 0.1754 0.1635 -0.0025 0.0555  -0.0434 42  VAL C CG2 
2103 N  N   . PRO C 43  ? 0.1527 0.1313 0.1696 0.0084  -0.0059 -0.0219 43  PRO C N   
2104 C  CA  . PRO C 43  ? 0.1613 0.1422 0.1708 0.0046  -0.0001 -0.0257 43  PRO C CA  
2105 C  C   . PRO C 43  ? 0.1733 0.1513 0.1486 0.0106  0.0035  -0.0033 43  PRO C C   
2106 O  O   . PRO C 43  ? 0.1769 0.1622 0.1459 0.0083  0.0121  -0.0058 43  PRO C O   
2107 C  CB  . PRO C 43  ? 0.1766 0.1459 0.1964 0.0053  -0.0097 -0.0215 43  PRO C CB  
2108 C  CG  . PRO C 43  ? 0.1839 0.1580 0.2157 0.0089  -0.0319 -0.0111 43  PRO C CG  
2109 C  CD  . PRO C 43  ? 0.1619 0.1311 0.1900 0.0128  -0.0250 -0.0067 43  PRO C CD  
2110 N  N   . ASP C 44  ? 0.1961 0.1696 0.1371 0.0212  -0.0027 -0.0098 44  ASP C N   
2111 C  CA  . ASP C 44  ? 0.2077 0.1880 0.1434 0.0338  -0.0042 0.0007  44  ASP C CA  
2112 C  C   . ASP C 44  ? 0.2034 0.1848 0.1324 0.0129  -0.0039 -0.0031 44  ASP C C   
2113 O  O   . ASP C 44  ? 0.2365 0.2038 0.1379 0.0155  0.0008  -0.0045 44  ASP C O   
2114 C  CB  . ASP C 44  ? 0.2509 0.2212 0.1805 0.0602  0.0053  0.0016  44  ASP C CB  
2115 C  CG  . ASP C 44  ? 0.3111 0.3009 0.2254 0.0551  0.0007  0.0095  44  ASP C CG  
2116 O  OD1 . ASP C 44  ? 0.3267 0.3460 0.2467 0.0539  0.0218  0.0202  44  ASP C OD1 
2117 O  OD2 . ASP C 44  ? 0.3595 0.3382 0.2504 0.0599  -0.0049 -0.0024 44  ASP C OD2 
2118 N  N   . GLN C 45  ? 0.1883 0.1653 0.1279 0.0114  -0.0006 -0.0089 45  GLN C N   
2119 C  CA  . GLN C 45  ? 0.1621 0.1606 0.1093 0.0063  0.0018  -0.0129 45  GLN C CA  
2120 C  C   . GLN C 45  ? 0.1750 0.1623 0.1074 -0.0089 -0.0015 -0.0204 45  GLN C C   
2121 O  O   . GLN C 45  ? 0.1910 0.1851 0.1137 -0.0413 -0.0140 -0.0175 45  GLN C O   
2122 C  CB  . GLN C 45  ? 0.1713 0.1517 0.1200 0.0098  -0.0004 -0.0087 45  GLN C CB  
2123 C  CG  . GLN C 45  ? 0.1960 0.1744 0.1428 -0.0048 0.0201  -0.0106 45  GLN C CG  
2124 C  CD  . GLN C 45  ? 0.1862 0.1853 0.1657 0.0141  0.0116  -0.0057 45  GLN C CD  
2125 O  OE1 . GLN C 45  ? 0.1941 0.1863 0.1768 0.0132  0.0381  0.0052  45  GLN C OE1 
2126 N  NE2 . GLN C 45  ? 0.1598 0.1889 0.1786 0.0379  -0.0214 0.0002  45  GLN C NE2 
2127 N  N   . LEU C 46  ? 0.1882 0.1518 0.1038 -0.0027 -0.0228 -0.0412 46  LEU C N   
2128 C  CA  . LEU C 46  ? 0.1922 0.1401 0.1192 -0.0092 -0.0089 -0.0377 46  LEU C CA  
2129 C  C   . LEU C 46  ? 0.1679 0.1431 0.1175 0.0010  -0.0054 -0.0103 46  LEU C C   
2130 O  O   . LEU C 46  ? 0.1877 0.1467 0.1319 0.0007  0.0006  0.0026  46  LEU C O   
2131 C  CB  . LEU C 46  ? 0.2027 0.1615 0.1346 -0.0335 -0.0023 -0.0270 46  LEU C CB  
2132 C  CG  . LEU C 46  ? 0.2174 0.1977 0.1619 -0.0489 0.0035  -0.0259 46  LEU C CG  
2133 C  CD1 . LEU C 46  ? 0.2321 0.2231 0.1814 -0.0667 -0.0180 -0.0358 46  LEU C CD1 
2134 C  CD2 . LEU C 46  ? 0.2211 0.2074 0.1687 -0.0335 0.0062  -0.0159 46  LEU C CD2 
2135 N  N   . MET C 47  ? 0.1594 0.1615 0.1194 -0.0162 -0.0044 -0.0016 47  MET C N   
2136 C  CA  . MET C 47  ? 0.1866 0.1969 0.1368 -0.0569 -0.0224 0.0134  47  MET C CA  
2137 C  C   . MET C 47  ? 0.1946 0.1959 0.1343 -0.0651 -0.0160 0.0411  47  MET C C   
2138 O  O   . MET C 47  ? 0.1901 0.2178 0.1732 -0.0537 -0.0146 0.0372  47  MET C O   
2139 C  CB  . MET C 47  ? 0.2449 0.2499 0.1716 -0.0531 -0.0479 -0.0004 47  MET C CB  
2140 C  CG  . MET C 47  ? 0.3111 0.2890 0.2085 -0.0161 -0.0387 -0.0367 47  MET C CG  
2141 S  SD  . MET C 47  ? 0.3415 0.3013 0.2149 0.0076  -0.0354 -0.0843 47  MET C SD  
2142 C  CE  . MET C 47  ? 0.2862 0.2432 0.1904 -0.0480 -0.0191 -0.1165 47  MET C CE  
2143 N  N   . ALA C 48  ? 0.2266 0.1770 0.1289 -0.0784 -0.0002 0.0311  48  ALA C N   
2144 C  CA  . ALA C 48  ? 0.2515 0.1823 0.1359 -0.0752 -0.0012 0.0285  48  ALA C CA  
2145 C  C   . ALA C 48  ? 0.2376 0.1658 0.1311 -0.0748 -0.0006 0.0236  48  ALA C C   
2146 O  O   . ALA C 48  ? 0.2618 0.1696 0.1238 -0.0700 0.0049  0.0143  48  ALA C O   
2147 C  CB  . ALA C 48  ? 0.2538 0.1650 0.1395 -0.0851 -0.0009 0.0325  48  ALA C CB  
2148 N  N   . PHE C 49  ? 0.2191 0.1672 0.1255 -0.0772 0.0037  0.0305  49  PHE C N   
2149 C  CA  . PHE C 49  ? 0.1952 0.1695 0.1359 -0.0658 0.0116  0.0275  49  PHE C CA  
2150 C  C   . PHE C 49  ? 0.1925 0.1635 0.1445 -0.0581 -0.0040 0.0192  49  PHE C C   
2151 O  O   . PHE C 49  ? 0.1828 0.1769 0.1489 -0.0636 -0.0237 0.0120  49  PHE C O   
2152 C  CB  . PHE C 49  ? 0.1747 0.1854 0.1532 -0.0505 0.0241  0.0113  49  PHE C CB  
2153 C  CG  . PHE C 49  ? 0.1677 0.2074 0.1629 -0.0471 0.0257  0.0134  49  PHE C CG  
2154 C  CD1 . PHE C 49  ? 0.1887 0.2198 0.1631 -0.0394 0.0245  0.0197  49  PHE C CD1 
2155 C  CD2 . PHE C 49  ? 0.1646 0.2395 0.1683 -0.0385 0.0346  0.0065  49  PHE C CD2 
2156 C  CE1 . PHE C 49  ? 0.1940 0.2468 0.1715 -0.0280 0.0219  0.0079  49  PHE C CE1 
2157 C  CE2 . PHE C 49  ? 0.1638 0.2420 0.1719 -0.0493 0.0181  0.0064  49  PHE C CE2 
2158 C  CZ  . PHE C 49  ? 0.1677 0.2545 0.1705 -0.0463 0.0256  0.0097  49  PHE C CZ  
2159 N  N   . GLY C 50  ? 0.2121 0.1452 0.1498 -0.0494 -0.0133 -0.0029 50  GLY C N   
2160 C  CA  . GLY C 50  ? 0.2187 0.1532 0.1532 -0.0670 -0.0127 -0.0121 50  GLY C CA  
2161 C  C   . GLY C 50  ? 0.2430 0.1765 0.1665 -0.0882 -0.0186 -0.0061 50  GLY C C   
2162 O  O   . GLY C 50  ? 0.2475 0.1786 0.1900 -0.0781 -0.0094 -0.0046 50  GLY C O   
2163 N  N   . GLY C 51  ? 0.2880 0.1960 0.1474 -0.0900 -0.0440 -0.0066 51  GLY C N   
2164 C  CA  . GLY C 51  ? 0.3105 0.2237 0.1593 -0.1088 -0.0482 0.0037  51  GLY C CA  
2165 C  C   . GLY C 51  ? 0.3171 0.2334 0.1879 -0.1167 -0.0677 0.0226  51  GLY C C   
2166 O  O   . GLY C 51  ? 0.3437 0.2595 0.1972 -0.1080 -0.0790 0.0195  51  GLY C O   
2167 N  N   . SER C 52  ? 0.3231 0.2350 0.2232 -0.1069 -0.0692 0.0338  52  SER C N   
2168 C  CA  . SER C 52  ? 0.3084 0.2310 0.2511 -0.1223 -0.0712 0.0287  52  SER C CA  
2169 C  C   . SER C 52  ? 0.3026 0.2221 0.2378 -0.1063 -0.0784 0.0246  52  SER C C   
2170 O  O   . SER C 52  ? 0.2762 0.2054 0.1978 -0.1062 -0.0552 0.0165  52  SER C O   
2171 C  CB  . SER C 52  ? 0.3242 0.2518 0.2998 -0.1380 -0.0531 0.0189  52  SER C CB  
2172 O  OG  . SER C 52  ? 0.3336 0.2854 0.3242 -0.1526 -0.0523 0.0056  52  SER C OG  
2173 N  N   A SER C 53  ? 0.3174 0.2237 0.2547 -0.0983 -0.0728 0.0311  53  SER C N   
2174 N  N   B SER C 53  ? 0.3177 0.2235 0.2549 -0.0977 -0.0726 0.0313  53  SER C N   
2175 C  CA  A SER C 53  ? 0.3105 0.2326 0.2641 -0.0937 -0.0700 0.0373  53  SER C CA  
2176 C  CA  B SER C 53  ? 0.3098 0.2319 0.2635 -0.0931 -0.0703 0.0380  53  SER C CA  
2177 C  C   A SER C 53  ? 0.2862 0.2429 0.2558 -0.1099 -0.0859 0.0317  53  SER C C   
2178 C  C   B SER C 53  ? 0.2854 0.2426 0.2556 -0.1104 -0.0866 0.0322  53  SER C C   
2179 O  O   A SER C 53  ? 0.2891 0.2498 0.2547 -0.1003 -0.0918 0.0202  53  SER C O   
2180 O  O   B SER C 53  ? 0.2879 0.2487 0.2554 -0.1011 -0.0933 0.0209  53  SER C O   
2181 C  CB  A SER C 53  ? 0.3314 0.2481 0.2847 -0.0622 -0.0474 0.0410  53  SER C CB  
2182 C  CB  B SER C 53  ? 0.3316 0.2461 0.2845 -0.0599 -0.0473 0.0415  53  SER C CB  
2183 O  OG  A SER C 53  ? 0.3359 0.2573 0.2928 -0.0424 -0.0404 0.0440  53  SER C OG  
2184 O  OG  B SER C 53  ? 0.3380 0.2501 0.2916 -0.0395 -0.0361 0.0428  53  SER C OG  
2185 N  N   . GLU C 54  ? 0.2710 0.2499 0.2563 -0.1176 -0.0858 0.0359  54  GLU C N   
2186 C  CA  . GLU C 54  ? 0.2491 0.2893 0.2679 -0.0903 -0.0699 0.0538  54  GLU C CA  
2187 C  C   . GLU C 54  ? 0.2182 0.2677 0.2319 -0.0619 -0.0560 0.0495  54  GLU C C   
2188 O  O   . GLU C 54  ? 0.2250 0.2640 0.2187 -0.0756 -0.0521 0.0543  54  GLU C O   
2189 C  CB  . GLU C 54  ? 0.2719 0.3505 0.3197 -0.0920 -0.0734 0.0452  54  GLU C CB  
2190 C  CG  . GLU C 54  ? 0.3046 0.3990 0.3621 -0.0819 -0.0748 0.0505  54  GLU C CG  
2191 C  CD  . GLU C 54  ? 0.3386 0.4315 0.3973 -0.0830 -0.0667 0.0540  54  GLU C CD  
2192 O  OE1 . GLU C 54  ? 0.3463 0.4495 0.4053 -0.0812 -0.0742 0.0468  54  GLU C OE1 
2193 O  OE2 . GLU C 54  ? 0.3567 0.4439 0.4155 -0.0780 -0.0544 0.0594  54  GLU C OE2 
2194 N  N   . PRO C 55  ? 0.1764 0.2660 0.2197 -0.0373 -0.0404 0.0384  55  PRO C N   
2195 C  CA  . PRO C 55  ? 0.1697 0.2538 0.1941 -0.0287 -0.0315 0.0268  55  PRO C CA  
2196 C  C   . PRO C 55  ? 0.1408 0.2231 0.1608 -0.0337 -0.0182 0.0374  55  PRO C C   
2197 O  O   . PRO C 55  ? 0.1743 0.2356 0.1683 -0.0261 -0.0272 0.0420  55  PRO C O   
2198 C  CB  . PRO C 55  ? 0.1770 0.2779 0.2091 -0.0316 -0.0239 0.0096  55  PRO C CB  
2199 C  CG  . PRO C 55  ? 0.1849 0.2799 0.2188 -0.0296 -0.0262 0.0157  55  PRO C CG  
2200 C  CD  . PRO C 55  ? 0.1777 0.2848 0.2277 -0.0298 -0.0360 0.0174  55  PRO C CD  
2201 N  N   . CYS C 56  ? 0.1284 0.1958 0.1312 -0.0348 -0.0195 0.0220  56  CYS C N   
2202 C  CA  . CYS C 56  ? 0.1562 0.1751 0.1243 -0.0285 -0.0091 0.0098  56  CYS C CA  
2203 C  C   . CYS C 56  ? 0.1629 0.1779 0.1278 -0.0285 -0.0117 0.0151  56  CYS C C   
2204 O  O   . CYS C 56  ? 0.1694 0.1730 0.1516 -0.0317 -0.0094 0.0114  56  CYS C O   
2205 C  CB  . CYS C 56  ? 0.1913 0.1698 0.1320 -0.0271 -0.0001 -0.0131 56  CYS C CB  
2206 S  SG  . CYS C 56  ? 0.2347 0.1770 0.1552 -0.0355 0.0156  -0.0032 56  CYS C SG  
2207 N  N   . ALA C 57  ? 0.1495 0.1920 0.1487 -0.0110 -0.0202 -0.0129 57  ALA C N   
2208 C  CA  . ALA C 57  ? 0.1600 0.1813 0.1549 -0.0250 -0.0253 -0.0123 57  ALA C CA  
2209 C  C   . ALA C 57  ? 0.1680 0.1573 0.1431 -0.0332 -0.0336 -0.0104 57  ALA C C   
2210 O  O   . ALA C 57  ? 0.1792 0.1464 0.1627 -0.0330 -0.0160 0.0085  57  ALA C O   
2211 C  CB  . ALA C 57  ? 0.1750 0.1903 0.1660 -0.0155 -0.0213 -0.0196 57  ALA C CB  
2212 N  N   . LEU C 58  ? 0.1668 0.1709 0.1179 -0.0096 -0.0148 -0.0047 58  LEU C N   
2213 C  CA  . LEU C 58  ? 0.1654 0.1702 0.1126 -0.0320 -0.0179 -0.0105 58  LEU C CA  
2214 C  C   . LEU C 58  ? 0.1452 0.1516 0.1106 -0.0312 -0.0218 -0.0072 58  LEU C C   
2215 O  O   . LEU C 58  ? 0.1745 0.1834 0.1119 -0.0217 -0.0241 0.0016  58  LEU C O   
2216 C  CB  . LEU C 58  ? 0.2077 0.1751 0.1102 -0.0482 0.0130  -0.0220 58  LEU C CB  
2217 C  CG  . LEU C 58  ? 0.2436 0.2009 0.1117 -0.0645 0.0372  -0.0170 58  LEU C CG  
2218 C  CD1 . LEU C 58  ? 0.2740 0.2254 0.1006 -0.0586 0.0358  -0.0398 58  LEU C CD1 
2219 C  CD2 . LEU C 58  ? 0.2664 0.2048 0.1364 -0.0441 0.0492  -0.0151 58  LEU C CD2 
2220 N  N   . CYS C 59  ? 0.1416 0.1407 0.1164 -0.0132 -0.0128 -0.0214 59  CYS C N   
2221 C  CA  . CYS C 59  ? 0.1569 0.1538 0.1122 0.0114  -0.0070 -0.0193 59  CYS C CA  
2222 C  C   . CYS C 59  ? 0.1460 0.1586 0.1146 -0.0053 -0.0081 -0.0102 59  CYS C C   
2223 O  O   . CYS C 59  ? 0.1622 0.1532 0.1261 0.0040  -0.0067 -0.0267 59  CYS C O   
2224 C  CB  . CYS C 59  ? 0.1524 0.1544 0.1378 0.0264  0.0096  -0.0161 59  CYS C CB  
2225 S  SG  . CYS C 59  ? 0.1517 0.1863 0.1697 -0.0113 0.0070  -0.0039 59  CYS C SG  
2226 N  N   . SER C 60  ? 0.1182 0.1630 0.1053 -0.0146 -0.0273 -0.0069 60  SER C N   
2227 C  CA  . SER C 60  ? 0.1318 0.1675 0.1217 -0.0203 -0.0178 -0.0078 60  SER C CA  
2228 C  C   . SER C 60  ? 0.1383 0.1544 0.1230 -0.0025 0.0019  -0.0151 60  SER C C   
2229 O  O   . SER C 60  ? 0.1728 0.1568 0.1385 -0.0081 0.0020  -0.0226 60  SER C O   
2230 C  CB  . SER C 60  ? 0.1625 0.2091 0.1455 -0.0094 -0.0101 -0.0212 60  SER C CB  
2231 O  OG  . SER C 60  ? 0.2015 0.2455 0.1582 0.0008  0.0130  -0.0274 60  SER C OG  
2232 N  N   . LEU C 61  ? 0.1397 0.1549 0.1174 -0.0017 -0.0098 -0.0182 61  LEU C N   
2233 C  CA  . LEU C 61  ? 0.1412 0.1738 0.1129 -0.0090 -0.0017 -0.0242 61  LEU C CA  
2234 C  C   . LEU C 61  ? 0.1419 0.1747 0.1229 -0.0030 -0.0043 -0.0335 61  LEU C C   
2235 O  O   . LEU C 61  ? 0.1538 0.1798 0.1382 0.0134  -0.0099 -0.0183 61  LEU C O   
2236 C  CB  . LEU C 61  ? 0.1800 0.1834 0.1025 0.0086  0.0208  -0.0346 61  LEU C CB  
2237 C  CG  . LEU C 61  ? 0.2121 0.1742 0.1068 -0.0119 0.0282  -0.0272 61  LEU C CG  
2238 C  CD1 . LEU C 61  ? 0.2369 0.1726 0.1376 -0.0224 0.0213  -0.0500 61  LEU C CD1 
2239 C  CD2 . LEU C 61  ? 0.2265 0.1811 0.1164 -0.0244 0.0412  -0.0186 61  LEU C CD2 
2240 N  N   . HIS C 62  ? 0.1340 0.2109 0.1280 -0.0069 -0.0182 -0.0180 62  HIS C N   
2241 C  CA  . HIS C 62  ? 0.1376 0.2253 0.1215 -0.0056 -0.0258 -0.0284 62  HIS C CA  
2242 C  C   . HIS C 62  ? 0.1760 0.2208 0.1362 0.0057  -0.0215 -0.0301 62  HIS C C   
2243 O  O   . HIS C 62  ? 0.1967 0.2021 0.1489 0.0158  -0.0189 -0.0326 62  HIS C O   
2244 C  CB  . HIS C 62  ? 0.1416 0.2277 0.1212 -0.0167 -0.0005 -0.0241 62  HIS C CB  
2245 C  CG  . HIS C 62  ? 0.1612 0.2505 0.1284 -0.0412 0.0121  -0.0149 62  HIS C CG  
2246 N  ND1 . HIS C 62  ? 0.1619 0.2718 0.1222 -0.0465 0.0200  -0.0249 62  HIS C ND1 
2247 C  CD2 . HIS C 62  ? 0.1843 0.2577 0.1298 -0.0489 0.0217  -0.0071 62  HIS C CD2 
2248 C  CE1 . HIS C 62  ? 0.1770 0.2718 0.1300 -0.0458 0.0287  -0.0211 62  HIS C CE1 
2249 N  NE2 . HIS C 62  ? 0.1965 0.2774 0.1389 -0.0482 0.0215  -0.0083 62  HIS C NE2 
2250 N  N   . SER C 63  ? 0.1575 0.2239 0.1346 0.0066  -0.0221 -0.0205 63  SER C N   
2251 C  CA  . SER C 63  ? 0.1405 0.2250 0.1396 0.0054  -0.0375 -0.0266 63  SER C CA  
2252 C  C   . SER C 63  ? 0.1411 0.2268 0.1417 0.0159  -0.0310 -0.0164 63  SER C C   
2253 O  O   . SER C 63  ? 0.1543 0.2260 0.1478 0.0282  -0.0219 -0.0365 63  SER C O   
2254 C  CB  . SER C 63  ? 0.1608 0.2285 0.1327 0.0008  -0.0448 -0.0381 63  SER C CB  
2255 O  OG  . SER C 63  ? 0.1736 0.2241 0.1348 0.0020  -0.0305 -0.0553 63  SER C OG  
2256 N  N   . ILE C 64  ? 0.1701 0.2268 0.1400 0.0163  -0.0341 -0.0089 64  ILE C N   
2257 C  CA  . ILE C 64  ? 0.1707 0.2397 0.1489 0.0133  -0.0317 -0.0098 64  ILE C CA  
2258 C  C   . ILE C 64  ? 0.1841 0.2641 0.1603 0.0242  -0.0392 -0.0222 64  ILE C C   
2259 O  O   . ILE C 64  ? 0.2179 0.2782 0.1682 0.0559  -0.0152 -0.0532 64  ILE C O   
2260 C  CB  . ILE C 64  ? 0.1749 0.2289 0.1436 -0.0075 -0.0509 -0.0146 64  ILE C CB  
2261 C  CG1 . ILE C 64  ? 0.1973 0.2278 0.1448 -0.0302 -0.0594 -0.0195 64  ILE C CG1 
2262 C  CG2 . ILE C 64  ? 0.1696 0.2198 0.1588 -0.0160 -0.0459 -0.0162 64  ILE C CG2 
2263 C  CD1 . ILE C 64  ? 0.2051 0.2269 0.1416 -0.0498 -0.0457 -0.0361 64  ILE C CD1 
2264 N  N   . GLY C 65  ? 0.1835 0.2769 0.1618 0.0039  -0.0451 0.0033  65  GLY C N   
2265 C  CA  . GLY C 65  ? 0.1937 0.2830 0.1648 0.0007  -0.0420 0.0054  65  GLY C CA  
2266 C  C   . GLY C 65  ? 0.1969 0.2680 0.1759 0.0011  -0.0482 0.0021  65  GLY C C   
2267 O  O   . GLY C 65  ? 0.1985 0.2457 0.1783 0.0101  -0.0556 0.0053  65  GLY C O   
2268 N  N   . LYS C 66  ? 0.1970 0.2713 0.1884 -0.0021 -0.0302 0.0014  66  LYS C N   
2269 C  CA  . LYS C 66  ? 0.1892 0.2655 0.1933 0.0096  -0.0186 -0.0075 66  LYS C CA  
2270 C  C   . LYS C 66  ? 0.1768 0.2609 0.1783 0.0331  -0.0144 -0.0219 66  LYS C C   
2271 O  O   . LYS C 66  ? 0.1692 0.2641 0.1941 0.0523  -0.0195 -0.0473 66  LYS C O   
2272 C  CB  . LYS C 66  ? 0.2090 0.2773 0.2198 0.0199  -0.0239 -0.0110 66  LYS C CB  
2273 C  CG  . LYS C 66  ? 0.2585 0.2917 0.2431 0.0298  -0.0350 -0.0185 66  LYS C CG  
2274 C  CD  . LYS C 66  ? 0.3080 0.3035 0.2755 0.0309  -0.0444 -0.0218 66  LYS C CD  
2275 C  CE  . LYS C 66  ? 0.3447 0.3244 0.3168 0.0407  -0.0385 -0.0258 66  LYS C CE  
2276 N  NZ  . LYS C 66  ? 0.3645 0.3365 0.3335 0.0444  -0.0417 -0.0320 66  LYS C NZ  
2277 N  N   . ILE C 67  ? 0.1791 0.2551 0.1645 0.0190  -0.0125 -0.0100 67  ILE C N   
2278 C  CA  . ILE C 67  ? 0.1617 0.2388 0.1715 0.0032  0.0059  -0.0063 67  ILE C CA  
2279 C  C   . ILE C 67  ? 0.1634 0.2441 0.1870 -0.0046 0.0099  0.0042  67  ILE C C   
2280 O  O   . ILE C 67  ? 0.1839 0.2641 0.2112 -0.0005 0.0012  0.0102  67  ILE C O   
2281 C  CB  . ILE C 67  ? 0.1567 0.2264 0.1681 -0.0243 0.0065  -0.0188 67  ILE C CB  
2282 C  CG1 . ILE C 67  ? 0.1565 0.2276 0.1832 -0.0209 -0.0036 -0.0146 67  ILE C CG1 
2283 C  CG2 . ILE C 67  ? 0.1289 0.2268 0.1603 -0.0308 0.0218  -0.0445 67  ILE C CG2 
2284 C  CD1 . ILE C 67  ? 0.1449 0.2414 0.1931 -0.0283 -0.0111 -0.0069 67  ILE C CD1 
2285 N  N   . GLY C 68  ? 0.1602 0.2326 0.1784 -0.0065 0.0231  0.0048  68  GLY C N   
2286 C  CA  . GLY C 68  ? 0.1613 0.2430 0.1670 -0.0076 0.0104  0.0171  68  GLY C CA  
2287 C  C   . GLY C 68  ? 0.1790 0.2402 0.1540 -0.0128 -0.0123 0.0110  68  GLY C C   
2288 O  O   . GLY C 68  ? 0.1750 0.2557 0.1381 -0.0096 -0.0276 0.0079  68  GLY C O   
2289 N  N   . GLY C 69  ? 0.1993 0.2179 0.1580 -0.0121 -0.0148 0.0143  69  GLY C N   
2290 C  CA  . GLY C 69  ? 0.1991 0.2294 0.1484 -0.0145 -0.0107 0.0131  69  GLY C CA  
2291 C  C   . GLY C 69  ? 0.2193 0.2356 0.1420 -0.0078 0.0036  0.0085  69  GLY C C   
2292 O  O   . GLY C 69  ? 0.2229 0.2301 0.1284 -0.0044 0.0030  0.0143  69  GLY C O   
2293 N  N   . ALA C 70  ? 0.2356 0.2461 0.1418 -0.0040 0.0057  0.0122  70  ALA C N   
2294 C  CA  . ALA C 70  ? 0.2318 0.2598 0.1341 0.0002  -0.0022 0.0108  70  ALA C CA  
2295 C  C   . ALA C 70  ? 0.2084 0.2464 0.1308 -0.0158 0.0034  -0.0035 70  ALA C C   
2296 O  O   . ALA C 70  ? 0.2054 0.2570 0.1347 -0.0117 0.0061  0.0085  70  ALA C O   
2297 C  CB  . ALA C 70  ? 0.2539 0.2754 0.1342 -0.0095 -0.0046 0.0163  70  ALA C CB  
2298 N  N   . GLN C 71  ? 0.1948 0.2344 0.1169 -0.0155 0.0136  0.0039  71  GLN C N   
2299 C  CA  . GLN C 71  ? 0.1774 0.2415 0.1181 -0.0025 0.0018  -0.0102 71  GLN C CA  
2300 C  C   . GLN C 71  ? 0.1616 0.2317 0.1183 0.0162  0.0022  -0.0189 71  GLN C C   
2301 O  O   . GLN C 71  ? 0.1501 0.2304 0.1196 0.0067  -0.0085 -0.0158 71  GLN C O   
2302 C  CB  . GLN C 71  ? 0.1886 0.2637 0.1355 0.0076  -0.0200 -0.0131 71  GLN C CB  
2303 C  CG  . GLN C 71  ? 0.1948 0.2808 0.1565 0.0145  -0.0368 -0.0240 71  GLN C CG  
2304 C  CD  . GLN C 71  ? 0.2101 0.2916 0.1824 0.0352  -0.0307 -0.0244 71  GLN C CD  
2305 O  OE1 . GLN C 71  ? 0.2524 0.3108 0.2112 0.0307  -0.0286 -0.0278 71  GLN C OE1 
2306 N  NE2 . GLN C 71  ? 0.2028 0.3101 0.1872 0.0584  -0.0250 -0.0082 71  GLN C NE2 
2307 N  N   . ASN C 72  ? 0.1608 0.2092 0.1083 0.0003  0.0255  -0.0170 72  ASN C N   
2308 C  CA  . ASN C 72  ? 0.1584 0.2126 0.1237 -0.0163 0.0090  -0.0253 72  ASN C CA  
2309 C  C   . ASN C 72  ? 0.1598 0.2067 0.1292 -0.0252 0.0167  -0.0037 72  ASN C C   
2310 O  O   . ASN C 72  ? 0.1578 0.2105 0.1392 0.0011  0.0066  0.0111  72  ASN C O   
2311 C  CB  . ASN C 72  ? 0.1551 0.1972 0.1070 -0.0019 0.0284  -0.0160 72  ASN C CB  
2312 C  CG  . ASN C 72  ? 0.1785 0.1992 0.1036 -0.0122 0.0186  -0.0116 72  ASN C CG  
2313 O  OD1 . ASN C 72  ? 0.1661 0.2064 0.1102 -0.0226 0.0175  -0.0252 72  ASN C OD1 
2314 N  ND2 . ASN C 72  ? 0.1962 0.1897 0.0983 0.0080  0.0029  -0.0082 72  ASN C ND2 
2315 N  N   . ARG C 73  ? 0.1648 0.2173 0.1139 -0.0287 0.0304  -0.0160 73  ARG C N   
2316 C  CA  . ARG C 73  ? 0.1793 0.2315 0.1232 -0.0198 0.0281  0.0042  73  ARG C CA  
2317 C  C   . ARG C 73  ? 0.1802 0.2392 0.1295 -0.0130 0.0143  0.0022  73  ARG C C   
2318 O  O   . ARG C 73  ? 0.1755 0.2471 0.1348 -0.0095 0.0009  0.0006  73  ARG C O   
2319 C  CB  . ARG C 73  ? 0.2115 0.2344 0.1425 -0.0145 0.0324  0.0186  73  ARG C CB  
2320 C  CG  . ARG C 73  ? 0.2579 0.2543 0.1662 -0.0082 0.0163  0.0219  73  ARG C CG  
2321 C  CD  . ARG C 73  ? 0.2887 0.2663 0.1887 -0.0326 -0.0003 0.0191  73  ARG C CD  
2322 N  NE  . ARG C 73  ? 0.3104 0.2740 0.2106 -0.0394 0.0021  0.0079  73  ARG C NE  
2323 C  CZ  . ARG C 73  ? 0.3349 0.2886 0.2191 -0.0368 0.0110  0.0088  73  ARG C CZ  
2324 N  NH1 . ARG C 73  ? 0.3546 0.2882 0.2231 -0.0305 0.0141  0.0169  73  ARG C NH1 
2325 N  NH2 . ARG C 73  ? 0.3461 0.2949 0.2180 -0.0412 0.0228  0.0171  73  ARG C NH2 
2326 N  N   . SER C 74  ? 0.2047 0.2458 0.1249 0.0108  0.0246  -0.0165 74  SER C N   
2327 C  CA  . SER C 74  ? 0.2213 0.2408 0.1434 0.0276  0.0079  -0.0162 74  SER C CA  
2328 C  C   . SER C 74  ? 0.1856 0.2306 0.1460 0.0050  0.0087  -0.0286 74  SER C C   
2329 O  O   . SER C 74  ? 0.1655 0.2322 0.1618 0.0043  0.0124  -0.0484 74  SER C O   
2330 C  CB  . SER C 74  ? 0.2600 0.2560 0.1638 0.0508  -0.0021 -0.0300 74  SER C CB  
2331 O  OG  . SER C 74  ? 0.3080 0.2760 0.1899 0.0471  -0.0138 -0.0238 74  SER C OG  
2332 N  N   . TYR C 75  ? 0.1874 0.2247 0.1383 -0.0186 0.0125  -0.0141 75  TYR C N   
2333 C  CA  . TYR C 75  ? 0.1635 0.2199 0.1271 -0.0030 0.0047  -0.0132 75  TYR C CA  
2334 C  C   . TYR C 75  ? 0.1558 0.2223 0.1233 -0.0010 0.0050  -0.0142 75  TYR C C   
2335 O  O   . TYR C 75  ? 0.1580 0.2353 0.1277 0.0035  0.0138  -0.0102 75  TYR C O   
2336 C  CB  . TYR C 75  ? 0.1509 0.2232 0.1397 0.0124  0.0090  -0.0141 75  TYR C CB  
2337 C  CG  . TYR C 75  ? 0.1513 0.2275 0.1690 0.0167  -0.0096 -0.0330 75  TYR C CG  
2338 C  CD1 . TYR C 75  ? 0.1722 0.2494 0.2080 0.0110  -0.0163 -0.0501 75  TYR C CD1 
2339 C  CD2 . TYR C 75  ? 0.1339 0.2315 0.1721 0.0156  -0.0136 -0.0435 75  TYR C CD2 
2340 C  CE1 . TYR C 75  ? 0.1755 0.2770 0.2244 0.0067  -0.0272 -0.0511 75  TYR C CE1 
2341 C  CE2 . TYR C 75  ? 0.1301 0.2354 0.1832 0.0156  -0.0246 -0.0516 75  TYR C CE2 
2342 C  CZ  . TYR C 75  ? 0.1546 0.2712 0.2177 0.0069  -0.0379 -0.0646 75  TYR C CZ  
2343 O  OH  . TYR C 75  ? 0.1611 0.2945 0.2336 0.0107  -0.0422 -0.0797 75  TYR C OH  
2344 N  N   . SER C 76  ? 0.1731 0.2096 0.1093 -0.0074 0.0111  -0.0267 76  SER C N   
2345 C  CA  . SER C 76  ? 0.1743 0.2133 0.1292 0.0086  0.0176  -0.0222 76  SER C CA  
2346 C  C   . SER C 76  ? 0.1540 0.2187 0.1387 -0.0070 0.0272  -0.0092 76  SER C C   
2347 O  O   . SER C 76  ? 0.1408 0.2178 0.1480 -0.0062 0.0204  -0.0228 76  SER C O   
2348 C  CB  . SER C 76  ? 0.1689 0.2256 0.1559 0.0235  0.0251  -0.0085 76  SER C CB  
2349 O  OG  . SER C 76  ? 0.1586 0.2458 0.1703 0.0107  0.0205  -0.0157 76  SER C OG  
2350 N  N   . LYS C 77  ? 0.1580 0.2341 0.1373 -0.0081 0.0625  -0.0076 77  LYS C N   
2351 C  CA  . LYS C 77  ? 0.1664 0.2414 0.1458 0.0005  0.0597  -0.0038 77  LYS C CA  
2352 C  C   . LYS C 77  ? 0.1596 0.2393 0.1697 0.0002  0.0348  -0.0172 77  LYS C C   
2353 O  O   . LYS C 77  ? 0.1655 0.2481 0.1727 -0.0141 0.0227  -0.0157 77  LYS C O   
2354 C  CB  . LYS C 77  ? 0.1845 0.2553 0.1566 -0.0293 0.0678  0.0042  77  LYS C CB  
2355 C  CG  . LYS C 77  ? 0.1990 0.2719 0.1710 -0.0377 0.0608  0.0082  77  LYS C CG  
2356 C  CD  . LYS C 77  ? 0.1996 0.2942 0.1757 -0.0278 0.0764  0.0021  77  LYS C CD  
2357 N  N   . LEU C 78  ? 0.1589 0.2218 0.1653 -0.0134 0.0284  -0.0210 78  LEU C N   
2358 C  CA  . LEU C 78  ? 0.1783 0.2272 0.1695 -0.0191 0.0126  -0.0339 78  LEU C CA  
2359 C  C   . LEU C 78  ? 0.1824 0.2278 0.1589 0.0096  0.0120  -0.0261 78  LEU C C   
2360 O  O   . LEU C 78  ? 0.1984 0.2078 0.1421 0.0139  0.0010  -0.0316 78  LEU C O   
2361 C  CB  . LEU C 78  ? 0.1789 0.2508 0.1881 -0.0220 0.0034  -0.0535 78  LEU C CB  
2362 C  CG  . LEU C 78  ? 0.1951 0.2856 0.2059 -0.0187 0.0206  -0.0733 78  LEU C CG  
2363 C  CD1 . LEU C 78  ? 0.2190 0.3035 0.2097 -0.0005 0.0323  -0.0819 78  LEU C CD1 
2364 C  CD2 . LEU C 78  ? 0.1887 0.2899 0.2190 -0.0317 0.0168  -0.0692 78  LEU C CD2 
2365 N  N   . LEU C 79  ? 0.1707 0.2248 0.1503 0.0141  0.0191  -0.0301 79  LEU C N   
2366 C  CA  . LEU C 79  ? 0.1550 0.2237 0.1554 0.0149  -0.0045 -0.0174 79  LEU C CA  
2367 C  C   . LEU C 79  ? 0.1690 0.2184 0.1531 0.0039  0.0042  -0.0219 79  LEU C C   
2368 O  O   . LEU C 79  ? 0.1814 0.2124 0.1473 0.0025  0.0018  -0.0253 79  LEU C O   
2369 C  CB  . LEU C 79  ? 0.1368 0.2263 0.1681 -0.0011 -0.0142 -0.0095 79  LEU C CB  
2370 C  CG  . LEU C 79  ? 0.1541 0.2295 0.1867 -0.0133 -0.0176 -0.0058 79  LEU C CG  
2371 C  CD1 . LEU C 79  ? 0.1688 0.2348 0.1823 -0.0147 0.0074  0.0017  79  LEU C CD1 
2372 C  CD2 . LEU C 79  ? 0.1598 0.2311 0.2013 -0.0157 -0.0122 0.0014  79  LEU C CD2 
2373 N  N   . CYS C 80  ? 0.1685 0.2033 0.1512 -0.0036 0.0007  -0.0356 80  CYS C N   
2374 C  CA  . CYS C 80  ? 0.1663 0.2157 0.1625 -0.0135 0.0061  -0.0151 80  CYS C CA  
2375 C  C   . CYS C 80  ? 0.1728 0.2329 0.1666 -0.0063 0.0144  -0.0049 80  CYS C C   
2376 O  O   . CYS C 80  ? 0.1664 0.2292 0.1751 -0.0115 0.0124  0.0150  80  CYS C O   
2377 C  CB  . CYS C 80  ? 0.1937 0.2232 0.1693 -0.0247 0.0217  -0.0178 80  CYS C CB  
2378 S  SG  . CYS C 80  ? 0.2299 0.2407 0.1691 -0.0191 0.0243  -0.0143 80  CYS C SG  
2379 N  N   . GLY C 81  ? 0.1817 0.2641 0.1799 -0.0050 0.0262  -0.0003 81  GLY C N   
2380 C  CA  . GLY C 81  ? 0.1805 0.2752 0.1782 0.0149  0.0261  -0.0080 81  GLY C CA  
2381 C  C   . GLY C 81  ? 0.1704 0.2704 0.1810 0.0090  0.0238  -0.0289 81  GLY C C   
2382 O  O   . GLY C 81  ? 0.1672 0.2868 0.1751 0.0087  0.0129  -0.0255 81  GLY C O   
2383 N  N   . LEU C 82  ? 0.1729 0.2525 0.1858 0.0027  -0.0072 -0.0432 82  LEU C N   
2384 C  CA  . LEU C 82  ? 0.1832 0.2415 0.1931 -0.0082 -0.0263 -0.0566 82  LEU C CA  
2385 C  C   . LEU C 82  ? 0.1651 0.2356 0.1850 -0.0192 -0.0317 -0.0415 82  LEU C C   
2386 O  O   . LEU C 82  ? 0.1727 0.2542 0.1977 -0.0195 -0.0275 -0.0398 82  LEU C O   
2387 C  CB  . LEU C 82  ? 0.2049 0.2492 0.2049 -0.0162 -0.0363 -0.0879 82  LEU C CB  
2388 C  CG  . LEU C 82  ? 0.2347 0.2437 0.2246 0.0019  -0.0407 -0.1121 82  LEU C CG  
2389 C  CD1 . LEU C 82  ? 0.2482 0.2531 0.2413 -0.0064 -0.0400 -0.1172 82  LEU C CD1 
2390 C  CD2 . LEU C 82  ? 0.2535 0.2323 0.2345 0.0162  -0.0320 -0.1223 82  LEU C CD2 
2391 N  N   . LEU C 83  ? 0.1640 0.2306 0.1752 -0.0280 -0.0280 -0.0335 83  LEU C N   
2392 C  CA  . LEU C 83  ? 0.1565 0.2447 0.1762 -0.0153 -0.0296 -0.0207 83  LEU C CA  
2393 C  C   . LEU C 83  ? 0.1574 0.2636 0.1810 -0.0011 -0.0024 -0.0083 83  LEU C C   
2394 O  O   . LEU C 83  ? 0.1687 0.2685 0.1753 -0.0029 0.0144  -0.0104 83  LEU C O   
2395 C  CB  . LEU C 83  ? 0.1608 0.2414 0.1961 -0.0112 -0.0257 -0.0149 83  LEU C CB  
2396 C  CG  . LEU C 83  ? 0.1692 0.2410 0.2131 -0.0037 -0.0183 -0.0115 83  LEU C CG  
2397 C  CD1 . LEU C 83  ? 0.1919 0.2452 0.2312 0.0072  -0.0214 -0.0159 83  LEU C CD1 
2398 C  CD2 . LEU C 83  ? 0.1773 0.2486 0.2295 0.0064  -0.0214 0.0037  83  LEU C CD2 
2399 N  N   . ALA C 84  ? 0.1491 0.2679 0.1828 -0.0166 0.0202  0.0002  84  ALA C N   
2400 C  CA  . ALA C 84  ? 0.1488 0.2700 0.1937 -0.0312 0.0313  0.0081  84  ALA C CA  
2401 C  C   . ALA C 84  ? 0.1732 0.2868 0.2150 -0.0127 0.0343  -0.0024 84  ALA C C   
2402 O  O   . ALA C 84  ? 0.1981 0.3053 0.2151 -0.0134 0.0376  -0.0033 84  ALA C O   
2403 C  CB  . ALA C 84  ? 0.1580 0.2732 0.2011 -0.0703 0.0379  0.0235  84  ALA C CB  
2404 N  N   . GLU C 85  ? 0.1786 0.2934 0.2341 0.0114  0.0352  -0.0052 85  GLU C N   
2405 C  CA  . GLU C 85  ? 0.1785 0.3085 0.2686 0.0134  0.0331  -0.0069 85  GLU C CA  
2406 C  C   . GLU C 85  ? 0.1764 0.2910 0.2636 0.0065  0.0272  -0.0256 85  GLU C C   
2407 O  O   . GLU C 85  ? 0.2089 0.3051 0.2812 0.0111  0.0293  -0.0319 85  GLU C O   
2408 C  CB  . GLU C 85  ? 0.2130 0.3532 0.3133 0.0226  0.0527  -0.0004 85  GLU C CB  
2409 C  CG  . GLU C 85  ? 0.2632 0.4038 0.3685 0.0225  0.0524  0.0104  85  GLU C CG  
2410 C  CD  . GLU C 85  ? 0.3186 0.4545 0.4131 0.0169  0.0490  0.0151  85  GLU C CD  
2411 O  OE1 . GLU C 85  ? 0.3349 0.4708 0.4337 0.0069  0.0489  0.0205  85  GLU C OE1 
2412 O  OE2 . GLU C 85  ? 0.3491 0.4790 0.4261 0.0180  0.0535  0.0143  85  GLU C OE2 
2413 N  N   . ARG C 86  ? 0.1689 0.2684 0.2370 0.0006  0.0274  -0.0365 86  ARG C N   
2414 C  CA  . ARG C 86  ? 0.1739 0.2622 0.2331 0.0152  0.0188  -0.0483 86  ARG C CA  
2415 C  C   . ARG C 86  ? 0.1932 0.2343 0.2202 0.0129  0.0105  -0.0555 86  ARG C C   
2416 O  O   . ARG C 86  ? 0.2257 0.2335 0.2251 0.0126  0.0161  -0.0595 86  ARG C O   
2417 C  CB  . ARG C 86  ? 0.1796 0.2781 0.2507 0.0219  0.0195  -0.0636 86  ARG C CB  
2418 C  CG  . ARG C 86  ? 0.1880 0.2989 0.2743 0.0303  0.0260  -0.0820 86  ARG C CG  
2419 C  CD  . ARG C 86  ? 0.2111 0.3097 0.3074 0.0323  0.0347  -0.0816 86  ARG C CD  
2420 N  NE  . ARG C 86  ? 0.2247 0.3161 0.3295 0.0261  0.0453  -0.0835 86  ARG C NE  
2421 C  CZ  . ARG C 86  ? 0.2630 0.3445 0.3388 -0.0056 0.0366  -0.0853 86  ARG C CZ  
2422 N  NH1 . ARG C 86  ? 0.2795 0.3589 0.3446 -0.0132 0.0524  -0.0942 86  ARG C NH1 
2423 N  NH2 . ARG C 86  ? 0.2731 0.3400 0.3391 -0.0161 0.0237  -0.0759 86  ARG C NH2 
2424 N  N   . LEU C 87  ? 0.1919 0.2212 0.2101 0.0055  0.0208  -0.0548 87  LEU C N   
2425 C  CA  . LEU C 87  ? 0.1791 0.2063 0.2043 0.0111  0.0179  -0.0468 87  LEU C CA  
2426 C  C   . LEU C 87  ? 0.1616 0.2150 0.2139 0.0187  0.0102  -0.0383 87  LEU C C   
2427 O  O   . LEU C 87  ? 0.1546 0.2227 0.2150 0.0051  -0.0156 -0.0351 87  LEU C O   
2428 C  CB  . LEU C 87  ? 0.1871 0.1999 0.2035 0.0082  0.0023  -0.0391 87  LEU C CB  
2429 C  CG  . LEU C 87  ? 0.2070 0.1941 0.2087 -0.0038 0.0163  -0.0268 87  LEU C CG  
2430 C  CD1 . LEU C 87  ? 0.2013 0.1966 0.2086 -0.0200 0.0336  -0.0207 87  LEU C CD1 
2431 C  CD2 . LEU C 87  ? 0.2311 0.2105 0.2203 -0.0009 0.0090  -0.0099 87  LEU C CD2 
2432 N  N   . ARG C 88  ? 0.1606 0.2238 0.2324 0.0219  0.0141  -0.0327 88  ARG C N   
2433 C  CA  . ARG C 88  ? 0.1713 0.2490 0.2372 0.0258  -0.0149 -0.0408 88  ARG C CA  
2434 C  C   . ARG C 88  ? 0.1669 0.2473 0.2152 0.0137  -0.0130 -0.0203 88  ARG C C   
2435 O  O   . ARG C 88  ? 0.1758 0.2647 0.2254 0.0037  -0.0322 -0.0244 88  ARG C O   
2436 C  CB  . ARG C 88  ? 0.2090 0.2973 0.2628 0.0343  -0.0273 -0.0428 88  ARG C CB  
2437 C  CG  . ARG C 88  ? 0.2591 0.3599 0.3051 0.0222  -0.0188 -0.0369 88  ARG C CG  
2438 C  CD  . ARG C 88  ? 0.3072 0.4200 0.3527 0.0130  0.0110  -0.0178 88  ARG C CD  
2439 N  NE  . ARG C 88  ? 0.3493 0.4718 0.3898 -0.0005 0.0398  -0.0114 88  ARG C NE  
2440 C  CZ  . ARG C 88  ? 0.3777 0.5144 0.4187 -0.0138 0.0632  -0.0096 88  ARG C CZ  
2441 N  NH1 . ARG C 88  ? 0.3983 0.5313 0.4288 -0.0217 0.0682  -0.0034 88  ARG C NH1 
2442 N  NH2 . ARG C 88  ? 0.3756 0.5279 0.4308 -0.0128 0.0720  -0.0127 88  ARG C NH2 
2443 N  N   . ILE C 89  ? 0.1491 0.2293 0.1771 0.0191  0.0134  0.0081  89  ILE C N   
2444 C  CA  . ILE C 89  ? 0.1537 0.2241 0.1602 0.0157  0.0239  0.0142  89  ILE C CA  
2445 C  C   . ILE C 89  ? 0.1769 0.2306 0.1607 0.0004  0.0030  0.0145  89  ILE C C   
2446 O  O   . ILE C 89  ? 0.1812 0.2472 0.1632 0.0165  0.0046  -0.0029 89  ILE C O   
2447 C  CB  . ILE C 89  ? 0.1573 0.2067 0.1514 0.0059  0.0372  0.0137  89  ILE C CB  
2448 C  CG1 . ILE C 89  ? 0.1732 0.1953 0.1608 -0.0180 0.0524  0.0106  89  ILE C CG1 
2449 C  CG2 . ILE C 89  ? 0.1628 0.2034 0.1544 0.0150  0.0307  -0.0026 89  ILE C CG2 
2450 C  CD1 . ILE C 89  ? 0.1854 0.1874 0.1667 -0.0274 0.0460  -0.0014 89  ILE C CD1 
2451 N  N   . SER C 90  ? 0.1783 0.2271 0.1655 -0.0147 -0.0049 0.0321  90  SER C N   
2452 C  CA  . SER C 90  ? 0.1926 0.2374 0.1806 -0.0366 -0.0110 0.0238  90  SER C CA  
2453 C  C   . SER C 90  ? 0.1996 0.2156 0.1705 -0.0337 0.0067  0.0207  90  SER C C   
2454 O  O   . SER C 90  ? 0.2117 0.2156 0.1623 -0.0505 0.0041  0.0289  90  SER C O   
2455 C  CB  . SER C 90  ? 0.2070 0.2768 0.2126 -0.0448 -0.0377 0.0200  90  SER C CB  
2456 O  OG  . SER C 90  ? 0.2540 0.3280 0.2467 -0.0195 -0.0369 0.0212  90  SER C OG  
2457 N  N   . PRO C 91  ? 0.2058 0.2110 0.1637 -0.0171 0.0189  0.0171  91  PRO C N   
2458 C  CA  . PRO C 91  ? 0.2011 0.2117 0.1659 -0.0104 0.0258  0.0152  91  PRO C CA  
2459 C  C   . PRO C 91  ? 0.1885 0.2031 0.1734 -0.0218 0.0077  0.0193  91  PRO C C   
2460 O  O   . PRO C 91  ? 0.1924 0.2204 0.1879 -0.0179 0.0065  0.0061  91  PRO C O   
2461 C  CB  . PRO C 91  ? 0.2081 0.2303 0.1661 0.0110  0.0342  0.0008  91  PRO C CB  
2462 C  CG  . PRO C 91  ? 0.2306 0.2440 0.1713 0.0159  0.0270  0.0087  91  PRO C CG  
2463 C  CD  . PRO C 91  ? 0.2186 0.2325 0.1639 0.0047  0.0233  0.0077  91  PRO C CD  
2464 N  N   . ASP C 92  ? 0.2136 0.1994 0.1736 -0.0457 -0.0037 0.0327  92  ASP C N   
2465 C  CA  . ASP C 92  ? 0.2038 0.2096 0.1879 -0.0469 -0.0111 0.0348  92  ASP C CA  
2466 C  C   . ASP C 92  ? 0.1868 0.1967 0.1678 -0.0582 -0.0150 0.0323  92  ASP C C   
2467 O  O   . ASP C 92  ? 0.2073 0.2036 0.1777 -0.0325 -0.0194 0.0370  92  ASP C O   
2468 C  CB  . ASP C 92  ? 0.2031 0.2245 0.2332 -0.0675 -0.0102 0.0383  92  ASP C CB  
2469 C  CG  . ASP C 92  ? 0.1997 0.2278 0.2671 -0.1124 0.0122  0.0384  92  ASP C CG  
2470 O  OD1 . ASP C 92  ? 0.2073 0.2392 0.2667 -0.0935 0.0243  0.0445  92  ASP C OD1 
2471 O  OD2 . ASP C 92  ? 0.2390 0.2528 0.3093 -0.1183 0.0097  0.0234  92  ASP C OD2 
2472 N  N   . ARG C 93  ? 0.1706 0.1945 0.1511 -0.0588 -0.0196 0.0208  93  ARG C N   
2473 C  CA  . ARG C 93  ? 0.1850 0.1980 0.1444 -0.0423 -0.0166 0.0103  93  ARG C CA  
2474 C  C   . ARG C 93  ? 0.1839 0.1800 0.1363 -0.0511 -0.0216 0.0007  93  ARG C C   
2475 O  O   . ARG C 93  ? 0.1944 0.1904 0.1411 -0.0393 -0.0150 0.0078  93  ARG C O   
2476 C  CB  . ARG C 93  ? 0.1807 0.2352 0.1502 -0.0453 -0.0195 0.0057  93  ARG C CB  
2477 C  CG  . ARG C 93  ? 0.1959 0.2374 0.1499 -0.0610 -0.0212 0.0176  93  ARG C CG  
2478 C  CD  . ARG C 93  ? 0.1980 0.2584 0.1510 -0.0662 -0.0222 0.0311  93  ARG C CD  
2479 N  NE  . ARG C 93  ? 0.1922 0.2688 0.1647 -0.0697 -0.0145 0.0298  93  ARG C NE  
2480 C  CZ  . ARG C 93  ? 0.1990 0.2695 0.1590 -0.0751 -0.0139 0.0298  93  ARG C CZ  
2481 N  NH1 . ARG C 93  ? 0.2107 0.2632 0.1695 -0.0554 -0.0249 0.0187  93  ARG C NH1 
2482 N  NH2 . ARG C 93  ? 0.1853 0.2923 0.1554 -0.0730 0.0027  0.0353  93  ARG C NH2 
2483 N  N   . VAL C 94  ? 0.1755 0.1614 0.1349 -0.0543 -0.0147 -0.0067 94  VAL C N   
2484 C  CA  . VAL C 94  ? 0.1801 0.1668 0.1541 -0.0444 -0.0192 -0.0185 94  VAL C CA  
2485 C  C   . VAL C 94  ? 0.1692 0.1790 0.1393 -0.0200 -0.0121 -0.0034 94  VAL C C   
2486 O  O   . VAL C 94  ? 0.1593 0.1867 0.1366 -0.0300 -0.0097 0.0268  94  VAL C O   
2487 C  CB  . VAL C 94  ? 0.1757 0.1491 0.1683 -0.0388 -0.0219 -0.0191 94  VAL C CB  
2488 C  CG1 . VAL C 94  ? 0.1746 0.1534 0.1886 -0.0457 -0.0400 -0.0401 94  VAL C CG1 
2489 C  CG2 . VAL C 94  ? 0.1943 0.1500 0.1841 -0.0238 -0.0173 -0.0020 94  VAL C CG2 
2490 N  N   . TYR C 95  ? 0.1523 0.1849 0.1216 0.0011  0.0039  -0.0168 95  TYR C N   
2491 C  CA  . TYR C 95  ? 0.1481 0.1704 0.1192 -0.0359 0.0061  -0.0127 95  TYR C CA  
2492 C  C   . TYR C 95  ? 0.1474 0.1607 0.1206 -0.0408 -0.0005 -0.0156 95  TYR C C   
2493 O  O   . TYR C 95  ? 0.1532 0.1620 0.1207 -0.0318 0.0066  0.0165  95  TYR C O   
2494 C  CB  . TYR C 95  ? 0.1728 0.1685 0.1198 -0.0392 0.0339  -0.0100 95  TYR C CB  
2495 C  CG  . TYR C 95  ? 0.1826 0.1563 0.1256 -0.0348 0.0152  0.0019  95  TYR C CG  
2496 C  CD1 . TYR C 95  ? 0.2004 0.1506 0.1309 -0.0184 0.0189  0.0194  95  TYR C CD1 
2497 C  CD2 . TYR C 95  ? 0.2063 0.1404 0.1328 -0.0238 0.0063  -0.0138 95  TYR C CD2 
2498 C  CE1 . TYR C 95  ? 0.2177 0.1568 0.1317 -0.0303 0.0084  0.0091  95  TYR C CE1 
2499 C  CE2 . TYR C 95  ? 0.2170 0.1238 0.1276 -0.0434 0.0116  -0.0109 95  TYR C CE2 
2500 C  CZ  . TYR C 95  ? 0.2156 0.1321 0.1282 -0.0680 0.0285  -0.0096 95  TYR C CZ  
2501 O  OH  . TYR C 95  ? 0.2406 0.1570 0.1356 -0.0788 0.0459  -0.0184 95  TYR C OH  
2502 N  N   . ILE C 96  ? 0.1412 0.1717 0.1160 -0.0536 0.0230  -0.0258 96  ILE C N   
2503 C  CA  . ILE C 96  ? 0.1445 0.1834 0.1188 -0.0451 0.0281  -0.0160 96  ILE C CA  
2504 C  C   . ILE C 96  ? 0.1644 0.1771 0.1311 -0.0175 0.0179  -0.0091 96  ILE C C   
2505 O  O   . ILE C 96  ? 0.1849 0.1900 0.1468 -0.0201 0.0269  0.0141  96  ILE C O   
2506 C  CB  . ILE C 96  ? 0.1590 0.1935 0.1253 -0.0345 0.0126  -0.0257 96  ILE C CB  
2507 C  CG1 . ILE C 96  ? 0.1737 0.2023 0.1339 -0.0245 0.0066  -0.0279 96  ILE C CG1 
2508 C  CG2 . ILE C 96  ? 0.1741 0.2017 0.1291 -0.0220 -0.0132 -0.0262 96  ILE C CG2 
2509 C  CD1 . ILE C 96  ? 0.1978 0.2247 0.1369 -0.0391 0.0100  -0.0364 96  ILE C CD1 
2510 N  N   . ASN C 97  ? 0.1415 0.1588 0.1374 -0.0223 0.0115  -0.0149 97  ASN C N   
2511 C  CA  . ASN C 97  ? 0.1460 0.1614 0.1313 -0.0147 0.0065  -0.0227 97  ASN C CA  
2512 C  C   . ASN C 97  ? 0.1552 0.1703 0.1192 -0.0206 -0.0035 -0.0083 97  ASN C C   
2513 O  O   . ASN C 97  ? 0.1777 0.1571 0.1297 -0.0206 -0.0168 -0.0059 97  ASN C O   
2514 C  CB  . ASN C 97  ? 0.1785 0.1821 0.1429 -0.0033 0.0160  -0.0310 97  ASN C CB  
2515 C  CG  . ASN C 97  ? 0.2173 0.2114 0.1501 -0.0081 0.0129  -0.0353 97  ASN C CG  
2516 O  OD1 . ASN C 97  ? 0.2609 0.2266 0.1818 -0.0225 0.0095  -0.0429 97  ASN C OD1 
2517 N  ND2 . ASN C 97  ? 0.2284 0.2240 0.1363 -0.0021 0.0101  -0.0566 97  ASN C ND2 
2518 N  N   . TYR C 98  ? 0.1340 0.1860 0.1177 -0.0156 -0.0082 -0.0080 98  TYR C N   
2519 C  CA  . TYR C 98  ? 0.1518 0.1778 0.1147 -0.0057 0.0111  -0.0049 98  TYR C CA  
2520 C  C   . TYR C 98  ? 0.1574 0.1723 0.1339 -0.0130 0.0117  -0.0013 98  TYR C C   
2521 O  O   . TYR C 98  ? 0.1666 0.1720 0.1486 -0.0090 0.0185  0.0087  98  TYR C O   
2522 C  CB  . TYR C 98  ? 0.1509 0.2065 0.1128 -0.0020 0.0196  0.0053  98  TYR C CB  
2523 C  CG  . TYR C 98  ? 0.1371 0.1976 0.1228 0.0086  0.0083  -0.0082 98  TYR C CG  
2524 C  CD1 . TYR C 98  ? 0.1454 0.1987 0.1234 0.0162  0.0234  -0.0134 98  TYR C CD1 
2525 C  CD2 . TYR C 98  ? 0.1435 0.1976 0.1233 -0.0036 0.0032  -0.0225 98  TYR C CD2 
2526 C  CE1 . TYR C 98  ? 0.1389 0.1943 0.1226 0.0014  0.0232  -0.0156 98  TYR C CE1 
2527 C  CE2 . TYR C 98  ? 0.1517 0.1891 0.1155 0.0189  0.0139  -0.0186 98  TYR C CE2 
2528 C  CZ  . TYR C 98  ? 0.1467 0.1966 0.1165 0.0111  0.0240  -0.0166 98  TYR C CZ  
2529 O  OH  . TYR C 98  ? 0.1699 0.2008 0.1266 0.0372  0.0196  -0.0237 98  TYR C OH  
2530 N  N   . TYR C 99  ? 0.1376 0.1921 0.1336 -0.0224 0.0106  -0.0226 99  TYR C N   
2531 C  CA  . TYR C 99  ? 0.1431 0.1832 0.1261 -0.0222 0.0118  -0.0207 99  TYR C CA  
2532 C  C   . TYR C 99  ? 0.1654 0.1923 0.1388 -0.0001 -0.0041 -0.0268 99  TYR C C   
2533 O  O   . TYR C 99  ? 0.1790 0.1732 0.1398 -0.0106 -0.0139 -0.0432 99  TYR C O   
2534 C  CB  . TYR C 99  ? 0.1913 0.1829 0.1240 -0.0050 0.0186  -0.0272 99  TYR C CB  
2535 C  CG  . TYR C 99  ? 0.2072 0.1915 0.1226 0.0162  0.0137  -0.0421 99  TYR C CG  
2536 C  CD1 . TYR C 99  ? 0.2190 0.1975 0.1298 0.0021  0.0103  -0.0385 99  TYR C CD1 
2537 C  CD2 . TYR C 99  ? 0.2388 0.2255 0.1271 0.0455  0.0023  -0.0434 99  TYR C CD2 
2538 C  CE1 . TYR C 99  ? 0.2294 0.2133 0.1285 0.0209  -0.0022 -0.0559 99  TYR C CE1 
2539 C  CE2 . TYR C 99  ? 0.2434 0.2422 0.1379 0.0569  -0.0028 -0.0657 99  TYR C CE2 
2540 C  CZ  . TYR C 99  ? 0.2341 0.2468 0.1321 0.0588  -0.0053 -0.0726 99  TYR C CZ  
2541 O  OH  . TYR C 99  ? 0.2507 0.2775 0.1507 0.0762  -0.0221 -0.0794 99  TYR C OH  
2542 N  N   . ASP C 100 ? 0.1697 0.1994 0.1484 0.0092  -0.0051 -0.0157 100 ASP C N   
2543 C  CA  . ASP C 100 ? 0.1566 0.2082 0.1535 0.0247  -0.0096 -0.0176 100 ASP C CA  
2544 C  C   . ASP C 100 ? 0.1381 0.1906 0.1622 0.0188  -0.0130 -0.0178 100 ASP C C   
2545 O  O   . ASP C 100 ? 0.1421 0.2142 0.1828 0.0147  0.0158  -0.0088 100 ASP C O   
2546 C  CB  . ASP C 100 ? 0.1813 0.2256 0.1538 0.0297  -0.0127 -0.0151 100 ASP C CB  
2547 C  CG  . ASP C 100 ? 0.2370 0.2493 0.1725 0.0294  -0.0290 -0.0070 100 ASP C CG  
2548 O  OD1 . ASP C 100 ? 0.2480 0.2388 0.1642 0.0475  -0.0451 -0.0130 100 ASP C OD1 
2549 O  OD2 . ASP C 100 ? 0.2794 0.2655 0.1830 0.0225  -0.0272 0.0010  100 ASP C OD2 
2550 N  N   . MET C 101 ? 0.1438 0.1734 0.1562 -0.0062 -0.0086 -0.0261 101 MET C N   
2551 C  CA  . MET C 101 ? 0.1682 0.1863 0.1638 -0.0017 -0.0217 -0.0240 101 MET C CA  
2552 C  C   . MET C 101 ? 0.1616 0.1945 0.1698 0.0106  -0.0251 -0.0479 101 MET C C   
2553 O  O   . MET C 101 ? 0.1848 0.2175 0.1698 0.0155  -0.0128 -0.0580 101 MET C O   
2554 C  CB  . MET C 101 ? 0.2048 0.2038 0.1605 -0.0153 -0.0306 -0.0144 101 MET C CB  
2555 C  CG  . MET C 101 ? 0.2243 0.2120 0.1618 -0.0247 -0.0317 -0.0217 101 MET C CG  
2556 S  SD  . MET C 101 ? 0.2589 0.2145 0.1616 -0.0373 -0.0334 -0.0130 101 MET C SD  
2557 C  CE  . MET C 101 ? 0.2682 0.2175 0.1693 -0.0031 -0.0087 -0.0248 101 MET C CE  
2558 N  N   . ASN C 102 ? 0.1599 0.2052 0.1882 -0.0031 -0.0182 -0.0393 102 ASN C N   
2559 C  CA  . ASN C 102 ? 0.1852 0.2169 0.2019 -0.0032 -0.0252 -0.0478 102 ASN C CA  
2560 C  C   . ASN C 102 ? 0.1969 0.2192 0.1920 -0.0292 -0.0176 -0.0500 102 ASN C C   
2561 O  O   . ASN C 102 ? 0.2086 0.2277 0.1879 -0.0406 0.0008  -0.0282 102 ASN C O   
2562 C  CB  . ASN C 102 ? 0.2090 0.2370 0.2278 0.0115  -0.0211 -0.0480 102 ASN C CB  
2563 C  CG  . ASN C 102 ? 0.2591 0.2933 0.2708 0.0192  -0.0118 -0.0427 102 ASN C CG  
2564 O  OD1 . ASN C 102 ? 0.2852 0.3196 0.2958 0.0266  -0.0099 -0.0214 102 ASN C OD1 
2565 N  ND2 . ASN C 102 ? 0.2771 0.3084 0.2871 0.0186  -0.0190 -0.0550 102 ASN C ND2 
2566 N  N   . ALA C 103 ? 0.1977 0.2343 0.1970 -0.0343 -0.0153 -0.0733 103 ALA C N   
2567 C  CA  . ALA C 103 ? 0.1952 0.2344 0.1939 -0.0185 -0.0164 -0.0865 103 ALA C CA  
2568 C  C   . ALA C 103 ? 0.1833 0.2373 0.2072 -0.0263 -0.0101 -0.0741 103 ALA C C   
2569 O  O   . ALA C 103 ? 0.1941 0.2308 0.2183 -0.0080 0.0040  -0.0781 103 ALA C O   
2570 C  CB  . ALA C 103 ? 0.2006 0.2397 0.1924 -0.0329 -0.0367 -0.0955 103 ALA C CB  
2571 N  N   . ALA C 104 ? 0.1604 0.2393 0.2001 -0.0200 0.0022  -0.0680 104 ALA C N   
2572 C  CA  . ALA C 104 ? 0.1590 0.2382 0.2144 -0.0076 -0.0014 -0.0488 104 ALA C CA  
2573 C  C   . ALA C 104 ? 0.1600 0.2252 0.2048 -0.0075 -0.0087 -0.0494 104 ALA C C   
2574 O  O   . ALA C 104 ? 0.1504 0.2349 0.2086 -0.0294 -0.0151 -0.0556 104 ALA C O   
2575 C  CB  . ALA C 104 ? 0.1537 0.2387 0.2224 0.0054  0.0088  -0.0454 104 ALA C CB  
2576 N  N   . ASN C 105 ? 0.1696 0.2014 0.1893 0.0006  -0.0235 -0.0410 105 ASN C N   
2577 C  CA  . ASN C 105 ? 0.1623 0.1880 0.1812 -0.0104 -0.0203 -0.0289 105 ASN C CA  
2578 C  C   . ASN C 105 ? 0.1706 0.1757 0.1728 -0.0012 -0.0129 -0.0396 105 ASN C C   
2579 O  O   . ASN C 105 ? 0.1776 0.1872 0.1604 -0.0027 -0.0112 -0.0403 105 ASN C O   
2580 C  CB  . ASN C 105 ? 0.1523 0.1984 0.1863 -0.0050 -0.0126 -0.0145 105 ASN C CB  
2581 C  CG  . ASN C 105 ? 0.1698 0.2054 0.1929 0.0033  -0.0035 -0.0158 105 ASN C CG  
2582 O  OD1 . ASN C 105 ? 0.2043 0.2157 0.1966 0.0157  0.0149  -0.0102 105 ASN C OD1 
2583 N  ND2 . ASN C 105 ? 0.1924 0.2228 0.1918 0.0031  0.0120  0.0015  105 ASN C ND2 
2584 N  N   . VAL C 106 ? 0.1923 0.1651 0.1863 -0.0016 -0.0095 -0.0477 106 VAL C N   
2585 C  CA  . VAL C 106 ? 0.2004 0.1783 0.1902 0.0005  -0.0039 -0.0299 106 VAL C CA  
2586 C  C   . VAL C 106 ? 0.2152 0.1831 0.2046 -0.0021 -0.0066 -0.0454 106 VAL C C   
2587 O  O   . VAL C 106 ? 0.2301 0.1991 0.2205 -0.0072 -0.0075 -0.0464 106 VAL C O   
2588 C  CB  . VAL C 106 ? 0.1776 0.1915 0.1945 -0.0153 -0.0067 -0.0248 106 VAL C CB  
2589 C  CG1 . VAL C 106 ? 0.1791 0.2057 0.1993 -0.0151 -0.0008 -0.0158 106 VAL C CG1 
2590 C  CG2 . VAL C 106 ? 0.1824 0.1929 0.1943 -0.0244 -0.0057 -0.0372 106 VAL C CG2 
2591 N  N   . GLY C 107 ? 0.1975 0.1581 0.2098 -0.0063 0.0030  -0.0356 107 GLY C N   
2592 C  CA  . GLY C 107 ? 0.2104 0.1431 0.2254 -0.0130 0.0004  -0.0274 107 GLY C CA  
2593 C  C   . GLY C 107 ? 0.2082 0.1471 0.2433 -0.0230 -0.0018 -0.0451 107 GLY C C   
2594 O  O   . GLY C 107 ? 0.2093 0.1548 0.2420 -0.0308 -0.0079 -0.0359 107 GLY C O   
2595 N  N   . TRP C 108 ? 0.2059 0.1505 0.2625 -0.0052 0.0022  -0.0883 108 TRP C N   
2596 C  CA  . TRP C 108 ? 0.1957 0.1709 0.2848 0.0140  -0.0054 -0.0972 108 TRP C CA  
2597 C  C   . TRP C 108 ? 0.1993 0.1872 0.3104 0.0030  -0.0117 -0.1096 108 TRP C C   
2598 O  O   . TRP C 108 ? 0.2013 0.2068 0.3133 0.0090  -0.0204 -0.1004 108 TRP C O   
2599 C  CB  . TRP C 108 ? 0.2235 0.2093 0.2836 0.0352  -0.0210 -0.0983 108 TRP C CB  
2600 C  CG  . TRP C 108 ? 0.2524 0.2381 0.2929 0.0404  -0.0334 -0.1104 108 TRP C CG  
2601 C  CD1 . TRP C 108 ? 0.2614 0.2480 0.2958 0.0441  -0.0323 -0.1111 108 TRP C CD1 
2602 C  CD2 . TRP C 108 ? 0.2664 0.2650 0.2996 0.0432  -0.0485 -0.1278 108 TRP C CD2 
2603 N  NE1 . TRP C 108 ? 0.2724 0.2606 0.3022 0.0405  -0.0470 -0.1158 108 TRP C NE1 
2604 C  CE2 . TRP C 108 ? 0.2775 0.2567 0.3018 0.0393  -0.0501 -0.1366 108 TRP C CE2 
2605 C  CE3 . TRP C 108 ? 0.2725 0.2802 0.3005 0.0499  -0.0545 -0.1425 108 TRP C CE3 
2606 C  CZ2 . TRP C 108 ? 0.2814 0.2636 0.3024 0.0469  -0.0438 -0.1552 108 TRP C CZ2 
2607 C  CZ3 . TRP C 108 ? 0.2849 0.2893 0.3050 0.0490  -0.0442 -0.1496 108 TRP C CZ3 
2608 C  CH2 . TRP C 108 ? 0.2928 0.2850 0.3061 0.0517  -0.0438 -0.1524 108 TRP C CH2 
2609 N  N   . ASN C 109 ? 0.2155 0.1827 0.3376 -0.0326 -0.0054 -0.1242 109 ASN C N   
2610 C  CA  . ASN C 109 ? 0.2351 0.2015 0.3720 -0.0391 -0.0091 -0.1139 109 ASN C CA  
2611 C  C   . ASN C 109 ? 0.2391 0.2051 0.3811 -0.0147 -0.0031 -0.0941 109 ASN C C   
2612 O  O   . ASN C 109 ? 0.2660 0.2175 0.3720 -0.0016 0.0051  -0.1089 109 ASN C O   
2613 C  CB  . ASN C 109 ? 0.2732 0.2313 0.3995 -0.0359 -0.0053 -0.1138 109 ASN C CB  
2614 C  CG  . ASN C 109 ? 0.3124 0.2635 0.4244 -0.0394 -0.0042 -0.1062 109 ASN C CG  
2615 O  OD1 . ASN C 109 ? 0.3246 0.2562 0.4344 -0.0426 -0.0054 -0.0987 109 ASN C OD1 
2616 N  ND2 . ASN C 109 ? 0.3224 0.2924 0.4349 -0.0408 -0.0054 -0.1087 109 ASN C ND2 
2617 N  N   . ASN C 110 ? 0.2267 0.2021 0.3907 -0.0156 0.0044  -0.0621 110 ASN C N   
2618 C  CA  . ASN C 110 ? 0.2116 0.1896 0.4049 -0.0214 -0.0099 -0.0388 110 ASN C CA  
2619 C  C   . ASN C 110 ? 0.1990 0.2041 0.4012 -0.0117 -0.0184 -0.0247 110 ASN C C   
2620 O  O   . ASN C 110 ? 0.2138 0.2352 0.4153 0.0022  -0.0075 -0.0025 110 ASN C O   
2621 C  CB  . ASN C 110 ? 0.2432 0.1974 0.4285 -0.0432 -0.0255 -0.0302 110 ASN C CB  
2622 C  CG  . ASN C 110 ? 0.2780 0.2136 0.4501 -0.0502 -0.0317 -0.0233 110 ASN C CG  
2623 O  OD1 . ASN C 110 ? 0.2964 0.2311 0.4626 -0.0668 -0.0411 -0.0149 110 ASN C OD1 
2624 N  ND2 . ASN C 110 ? 0.2863 0.2224 0.4609 -0.0329 -0.0322 -0.0193 110 ASN C ND2 
2625 N  N   . SER C 111 ? 0.1885 0.1976 0.3753 -0.0260 -0.0406 -0.0372 111 SER C N   
2626 C  CA  . SER C 111 ? 0.2112 0.2269 0.3614 -0.0341 -0.0517 -0.0412 111 SER C CA  
2627 C  C   . SER C 111 ? 0.2025 0.2099 0.3309 -0.0282 -0.0385 -0.0518 111 SER C C   
2628 O  O   . SER C 111 ? 0.2207 0.1884 0.3290 -0.0208 -0.0359 -0.0556 111 SER C O   
2629 C  CB  . SER C 111 ? 0.2342 0.2563 0.3805 -0.0495 -0.0670 -0.0277 111 SER C CB  
2630 O  OG  . SER C 111 ? 0.2635 0.2792 0.3996 -0.0604 -0.0754 -0.0130 111 SER C OG  
2631 N  N   . THR C 112 ? 0.2120 0.2351 0.3108 -0.0536 -0.0282 -0.0476 112 THR C N   
2632 C  CA  . THR C 112 ? 0.2212 0.2640 0.2834 -0.0331 -0.0161 -0.0406 112 THR C CA  
2633 C  C   . THR C 112 ? 0.2483 0.2890 0.2674 -0.0351 -0.0221 -0.0510 112 THR C C   
2634 O  O   . THR C 112 ? 0.2516 0.3058 0.2605 -0.0508 -0.0278 -0.0532 112 THR C O   
2635 C  CB  . THR C 112 ? 0.1992 0.2801 0.2704 -0.0094 -0.0122 -0.0333 112 THR C CB  
2636 O  OG1 . THR C 112 ? 0.2017 0.2855 0.2681 0.0036  -0.0209 -0.0353 112 THR C OG1 
2637 C  CG2 . THR C 112 ? 0.1796 0.2864 0.2609 -0.0264 -0.0120 -0.0216 112 THR C CG2 
2638 N  N   . PHE C 113 ? 0.2746 0.3003 0.2614 -0.0183 -0.0310 -0.0558 113 PHE C N   
2639 C  CA  . PHE C 113 ? 0.2995 0.3192 0.2665 -0.0109 -0.0391 -0.0534 113 PHE C CA  
2640 C  C   . PHE C 113 ? 0.3181 0.3388 0.2746 -0.0136 -0.0659 -0.0466 113 PHE C C   
2641 O  O   . PHE C 113 ? 0.3377 0.3565 0.2700 0.0001  -0.0586 -0.0431 113 PHE C O   
2642 C  CB  . PHE C 113 ? 0.3012 0.3169 0.2667 -0.0009 -0.0323 -0.0572 113 PHE C CB  
2643 C  CG  . PHE C 113 ? 0.3094 0.3007 0.2722 0.0081  -0.0279 -0.0782 113 PHE C CG  
2644 C  CD1 . PHE C 113 ? 0.3109 0.3012 0.2738 0.0096  -0.0383 -0.0906 113 PHE C CD1 
2645 C  CD2 . PHE C 113 ? 0.3168 0.2972 0.2780 -0.0034 -0.0288 -0.0820 113 PHE C CD2 
2646 C  CE1 . PHE C 113 ? 0.3263 0.3111 0.2746 0.0031  -0.0456 -0.0927 113 PHE C CE1 
2647 C  CE2 . PHE C 113 ? 0.3207 0.2959 0.2777 -0.0044 -0.0348 -0.0861 113 PHE C CE2 
2648 C  CZ  . PHE C 113 ? 0.3223 0.3040 0.2743 -0.0044 -0.0460 -0.0951 113 PHE C CZ  
2649 N  N   . ALA C 114 ? 0.3311 0.3417 0.2898 -0.0159 -0.0979 -0.0496 114 ALA C N   
2650 C  CA  . ALA C 114 ? 0.3446 0.3671 0.3151 -0.0205 -0.1141 -0.0549 114 ALA C CA  
2651 C  C   . ALA C 114 ? 0.3794 0.3979 0.3366 -0.0325 -0.1232 -0.0496 114 ALA C C   
2652 O  O   . ALA C 114 ? 0.3788 0.3970 0.3407 -0.0419 -0.1337 -0.0556 114 ALA C O   
2653 C  CB  . ALA C 114 ? 0.3377 0.3606 0.3205 -0.0124 -0.1166 -0.0536 114 ALA C CB  
2654 O  OXT . ALA C 114 ? 0.4007 0.4193 0.3470 -0.0364 -0.1218 -0.0394 114 ALA C OXT 
2655 CL CL  . CL  D .   ? 0.3563 0.3771 0.2630 -0.0646 0.0508  0.1105  201 CL  A CL  
2656 CL CL  . CL  E .   ? 0.3593 0.3042 0.2769 -0.0497 0.0783  -0.0190 202 CL  A CL  
2657 CL CL  . CL  F .   ? 0.2487 0.1879 0.1747 -0.0258 0.0184  -0.0248 203 CL  A CL  
2658 C  C1  . 7Y8 G .   ? 0.3832 0.3363 0.2797 -0.0001 0.0118  0.0917  204 7Y8 A C1  
2659 C  C2  . 7Y8 G .   ? 0.3962 0.3405 0.2856 -0.0113 0.0229  0.0957  204 7Y8 A C2  
2660 C  C11 . 7Y8 G .   ? 0.3694 0.3290 0.3152 -0.0096 0.0344  0.0509  204 7Y8 A C11 
2661 C  C12 . 7Y8 G .   ? 0.3646 0.3155 0.3110 -0.0364 0.0574  0.0253  204 7Y8 A C12 
2662 C  C13 . 7Y8 G .   ? 0.3365 0.3054 0.3017 -0.0392 0.0715  0.0071  204 7Y8 A C13 
2663 C  C14 . 7Y8 G .   ? 0.3545 0.3234 0.3154 -0.0302 0.0509  -0.0076 204 7Y8 A C14 
2664 C  C15 . 7Y8 G .   ? 0.3509 0.3303 0.3132 -0.0144 0.0402  -0.0124 204 7Y8 A C15 
2665 C  C17 . 7Y8 G .   ? 0.3677 0.3389 0.3136 -0.0030 0.0319  0.0228  204 7Y8 A C17 
2666 C  C8  . 7Y8 G .   ? 0.3853 0.3533 0.3185 -0.0224 0.0158  0.0827  204 7Y8 A C8  
2667 N  N4  . 7Y8 G .   ? 0.4056 0.3510 0.2708 0.0038  0.0624  0.0805  204 7Y8 A N4  
2668 O  O10 . 7Y8 G .   ? 0.4065 0.3643 0.3384 -0.0371 0.0031  0.0802  204 7Y8 A O10 
2669 O  O16 . 7Y8 G .   ? 0.3619 0.3463 0.3241 -0.0125 0.0337  -0.0164 204 7Y8 A O16 
2670 CL CL  . CL  H .   ? 0.3738 0.3759 0.3712 -0.0047 0.0576  -0.0841 201 CL  B CL  
2671 CL CL  . CL  I .   ? 0.4615 0.3919 0.4451 0.0012  -0.0266 0.0699  202 CL  B CL  
2672 CL CL  . CL  J .   ? 0.2143 0.2170 0.1785 -0.0147 0.0363  -0.0119 203 CL  B CL  
2673 C  C1  . J23 K .   ? 0.3634 0.3506 0.2624 0.0876  0.0143  0.0230  204 J23 B C1  
2674 C  C2  . J23 K .   ? 0.3844 0.3647 0.2696 0.0610  0.0434  0.0129  204 J23 B C2  
2675 C  C11 . J23 K .   ? 0.3226 0.2764 0.2423 0.0426  0.0555  -0.0170 204 J23 B C11 
2676 C  C12 . J23 K .   ? 0.3079 0.2512 0.2275 0.0170  0.0759  -0.0151 204 J23 B C12 
2677 C  C13 . J23 K .   ? 0.3039 0.2453 0.2140 0.0121  0.0716  -0.0339 204 J23 B C13 
2678 C  C14 . J23 K .   ? 0.3014 0.2539 0.2141 0.0174  0.0729  -0.0243 204 J23 B C14 
2679 C  C15 . J23 K .   ? 0.3103 0.2470 0.2177 0.0028  0.0601  -0.0312 204 J23 B C15 
2680 C  C17 . J23 K .   ? 0.3137 0.2573 0.2376 0.0422  0.0571  -0.0322 204 J23 B C17 
2681 C  C8  . J23 K .   ? 0.3779 0.3286 0.2483 0.0675  0.0592  -0.0013 204 J23 B C8  
2682 N  N4  . J23 K .   ? 0.4451 0.4139 0.3107 0.0178  0.0266  0.0259  204 J23 B N4  
2683 O  O10 . J23 K .   ? 0.4066 0.3423 0.2363 0.0778  0.0563  0.0021  204 J23 B O10 
2684 O  O16 . J23 K .   ? 0.3395 0.2385 0.2063 -0.0131 0.0508  -0.0217 204 J23 B O16 
2685 CL CL  . CL  L .   ? 0.2384 0.2918 0.1695 -0.0179 0.0259  -0.0303 201 CL  C CL  
2686 CL CL  . CL  M .   ? 0.3261 0.3286 0.4107 -0.0117 -0.0293 -0.0239 202 CL  C CL  
2687 CL CL  . CL  N .   ? 0.3785 0.3785 0.3785 -0.0000 0.0000  -0.0000 203 CL  C CL  
# 
