data_9GKR
# 
_entry.id   9GKR 
# 
_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   9GKR         pdb_00009gkr 10.2210/pdb9gkr/pdb 
WWPDB D_1292141264 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GKR 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              g.roelfes@rug.nl 
_pdbx_contact_author.name_first         Gerard 
_pdbx_contact_author.name_last          Roelfes 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0364-9564 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thunnissen, A.M.W.H.' 1 0000-0002-1915-9850 
'Leveson-Gower, R.B.'  2 0000-0001-7254-3950 
'Rozeboom, H.J.'       3 0000-0002-1656-6477 
'Roelfes, G.'          4 0000-0002-0364-9564 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1544 
_citation.page_last                 1552 
_citation.title                     'Evolutionary Specialization of a Promiscuous Designer Enzyme.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c06409 
_citation.pdbx_database_id_PubMed   39944761 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Leveson-Gower, R.B.' 1 ?                   
primary 'Tiessler-Sala, L.'   2 ?                   
primary 'Rozeboom, H.J.'      3 ?                   
primary 'Thunnissen, A.W.H.'  4 0000-0002-1915-9850 
primary 'Marechal, J.D.'      5 0000-0002-8344-9043 
primary 'Roelfes, G.'         6 0000-0002-0364-9564 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Transcriptional regulator, PadR-like family' 
_entity.formula_weight             15163.173 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              'V15pAF, N19M, A92R, F93H' 
_entity.pdbx_fragment              ? 
_entity.details                    
'LmrR carrying a C-terminal strep-tag, with V15 replaced by para-aminophenylalanine (pAF) and with mutations A92R, N19M, F93H (RMH)' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GAEIPKEMLRAQTN(HOX)ILLMVLKQGDNYVYGIIKQVKEASNGEMELNEATLYTIFKRLEKDGIISSYWGDESQGGRR
KYYRLTEIGHENMRLRHESWSRVDKIIENLEANKKSEAIKSRGGSGGWSHPQFEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAEIPKEMLRAQTNXILLMVLKQGDNYVYGIIKQVKEASNGEMELNEATLYTIFKRLEKDGIISSYWGDESQGGRRKYYR
LTEIGHENMRLRHESWSRVDKIIENLEANKKSEAIKSRGGSGGWSHPQFEK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   GLU n 
1 4   ILE n 
1 5   PRO n 
1 6   LYS n 
1 7   GLU n 
1 8   MET n 
1 9   LEU n 
1 10  ARG n 
1 11  ALA n 
1 12  GLN n 
1 13  THR n 
1 14  ASN n 
1 15  HOX n 
1 16  ILE n 
1 17  LEU n 
1 18  LEU n 
1 19  MET n 
1 20  VAL n 
1 21  LEU n 
1 22  LYS n 
1 23  GLN n 
1 24  GLY n 
1 25  ASP n 
1 26  ASN n 
1 27  TYR n 
1 28  VAL n 
1 29  TYR n 
1 30  GLY n 
1 31  ILE n 
1 32  ILE n 
1 33  LYS n 
1 34  GLN n 
1 35  VAL n 
1 36  LYS n 
1 37  GLU n 
1 38  ALA n 
1 39  SER n 
1 40  ASN n 
1 41  GLY n 
1 42  GLU n 
1 43  MET n 
1 44  GLU n 
1 45  LEU n 
1 46  ASN n 
1 47  GLU n 
1 48  ALA n 
1 49  THR n 
1 50  LEU n 
1 51  TYR n 
1 52  THR n 
1 53  ILE n 
1 54  PHE n 
1 55  LYS n 
1 56  ARG n 
1 57  LEU n 
1 58  GLU n 
1 59  LYS n 
1 60  ASP n 
1 61  GLY n 
1 62  ILE n 
1 63  ILE n 
1 64  SER n 
1 65  SER n 
1 66  TYR n 
1 67  TRP n 
1 68  GLY n 
1 69  ASP n 
1 70  GLU n 
1 71  SER n 
1 72  GLN n 
1 73  GLY n 
1 74  GLY n 
1 75  ARG n 
1 76  ARG n 
1 77  LYS n 
1 78  TYR n 
1 79  TYR n 
1 80  ARG n 
1 81  LEU n 
1 82  THR n 
1 83  GLU n 
1 84  ILE n 
1 85  GLY n 
1 86  HIS n 
1 87  GLU n 
1 88  ASN n 
1 89  MET n 
1 90  ARG n 
1 91  LEU n 
1 92  ARG n 
1 93  HIS n 
1 94  GLU n 
1 95  SER n 
1 96  TRP n 
1 97  SER n 
1 98  ARG n 
1 99  VAL n 
1 100 ASP n 
1 101 LYS n 
1 102 ILE n 
1 103 ILE n 
1 104 GLU n 
1 105 ASN n 
1 106 LEU n 
1 107 GLU n 
1 108 ALA n 
1 109 ASN n 
1 110 LYS n 
1 111 LYS n 
1 112 SER n 
1 113 GLU n 
1 114 ALA n 
1 115 ILE n 
1 116 LYS n 
1 117 SER n 
1 118 ARG n 
1 119 GLY n 
1 120 GLY n 
1 121 SER n 
1 122 GLY n 
1 123 GLY n 
1 124 TRP n 
1 125 SER n 
1 126 HIS n 
1 127 PRO n 
1 128 GLN n 
1 129 PHE n 
1 130 GLU n 
1 131 LYS 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                   131 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 llmg_0323 
_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      'Lactococcus cremoris subsp. cremoris MG1363' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     416870 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
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 
HOX 'L-peptide linking' n 4-amino-L-phenylalanine ? 'C9 H12 N2 O2'   180.204 
ILE 'L-peptide linking' y ISOLEUCINE              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   PRO 5   5   5   PRO PRO A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  HOX 15  15  15  HOX HOX A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  MET 19  19  19  MET MET A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  MET 43  43  43  MET MET A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  TRP 67  67  67  TRP TRP A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  SER 71  71  ?   ?   ?   A . n 
A 1 72  GLN 72  72  ?   ?   ?   A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  MET 89  89  89  MET MET A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 LYS 116 116 ?   ?   ?   A . n 
A 1 117 SER 117 117 ?   ?   ?   A . n 
A 1 118 ARG 118 118 ?   ?   ?   A . n 
A 1 119 GLY 119 119 ?   ?   ?   A . n 
A 1 120 GLY 120 120 ?   ?   ?   A . n 
A 1 121 SER 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 GLY 123 123 ?   ?   ?   A . n 
A 1 124 TRP 124 124 ?   ?   ?   A . n 
A 1 125 SER 125 125 ?   ?   ?   A . n 
A 1 126 HIS 126 126 ?   ?   ?   A . n 
A 1 127 PRO 127 127 ?   ?   ?   A . n 
A 1 128 GLN 128 128 ?   ?   ?   A . n 
A 1 129 PHE 129 129 ?   ?   ?   A . n 
A 1 130 GLU 130 130 ?   ?   ?   A . n 
A 1 131 LYS 131 131 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   ?   ?   ?   B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   PRO 5   5   5   PRO PRO B . n 
B 1 6   LYS 6   6   6   LYS LYS B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   MET 8   8   8   MET MET B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  GLN 12  12  12  GLN GLN B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  HOX 15  15  15  HOX HOX B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  MET 19  19  19  MET MET B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  GLN 23  23  23  GLN GLN B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  TYR 27  27  27  TYR TYR B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  TYR 29  29  29  TYR TYR B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  GLN 34  34  34  GLN GLN B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  MET 43  43  43  MET MET B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  ASN 46  46  46  ASN ASN B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  ASP 60  60  60  ASP ASP B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  ILE 62  62  62  ILE ILE B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  TYR 66  66  66  TYR TYR B . n 
B 1 67  TRP 67  67  67  TRP TRP B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  GLU 70  70  70  GLU GLU B . n 
B 1 71  SER 71  71  ?   ?   ?   B . n 
B 1 72  GLN 72  72  ?   ?   ?   B . n 
B 1 73  GLY 73  73  ?   ?   ?   B . n 
B 1 74  GLY 74  74  ?   ?   ?   B . n 
B 1 75  ARG 75  75  75  ARG ARG B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  TYR 79  79  79  TYR TYR B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  THR 82  82  82  THR THR B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  MET 89  89  89  MET MET B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  ARG 92  92  92  ARG ARG B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  SER 95  95  95  SER SER B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  SER 97  97  97  SER SER B . n 
B 1 98  ARG 98  98  98  ARG ARG B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 ASP 100 100 100 ASP ASP B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 ILE 103 103 103 ILE ILE B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LYS 111 111 ?   ?   ?   B . n 
B 1 112 SER 112 112 ?   ?   ?   B . n 
B 1 113 GLU 113 113 ?   ?   ?   B . n 
B 1 114 ALA 114 114 ?   ?   ?   B . n 
B 1 115 ILE 115 115 ?   ?   ?   B . n 
B 1 116 LYS 116 116 ?   ?   ?   B . n 
B 1 117 SER 117 117 ?   ?   ?   B . n 
B 1 118 ARG 118 118 ?   ?   ?   B . n 
B 1 119 GLY 119 119 ?   ?   ?   B . n 
B 1 120 GLY 120 120 ?   ?   ?   B . n 
B 1 121 SER 121 121 ?   ?   ?   B . n 
B 1 122 GLY 122 122 ?   ?   ?   B . n 
B 1 123 GLY 123 123 ?   ?   ?   B . n 
B 1 124 TRP 124 124 ?   ?   ?   B . n 
B 1 125 SER 125 125 ?   ?   ?   B . n 
B 1 126 HIS 126 126 ?   ?   ?   B . n 
B 1 127 PRO 127 127 ?   ?   ?   B . n 
B 1 128 GLN 128 128 ?   ?   ?   B . n 
B 1 129 PHE 129 129 ?   ?   ?   B . n 
B 1 130 GLU 130 130 ?   ?   ?   B . n 
B 1 131 LYS 131 131 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HOX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HOX 
_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_
_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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .            1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .            2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .            3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20rc1_4395 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.78 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GKR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     107.026 
_cell.length_a_esd                 ? 
_cell.length_b                     36.463 
_cell.length_b_esd                 ? 
_cell.length_c                     69.116 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GKR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9GKR 
_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             2.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.17 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Protein solution: 7-8 mg/ml in 20 mM Tris-HCl, pH 8.0, 280 mM NaCl and 1 mM EDTA. Crystallization solution: 10-13% PEG 2000 MME in 0.1 M Bis-Tris propane, pH 8.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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         2021-03-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   0.87313 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.87313 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GKR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.55 
_reflns.d_resolution_low                               44.97 
_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                                     8855 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.06 
_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                                0.152 
_reflns.pdbx_Rpim_I_all                                0.063 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       50650 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.137 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_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                                    2.55 
_reflns_shell.d_res_low                                     2.66 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6308 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1059 
_reflns_shell.percent_possible_obs                          99.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_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                               6.0 
_reflns_shell.pdbx_chi_squared                              1.03 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               1.924 
_reflns_shell.pdbx_Rpim_I_all                               0.788 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.409 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.750 
_reflns_shell.pdbx_Rsym_value                               ? 
_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                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_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                                 9GKR 
_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                            2.55 
_refine.ls_d_res_low                             39.42 
_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                     8400 
_refine.ls_number_reflns_R_free                  799 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.35 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2626 
_refine.ls_R_factor_R_free                       0.3238 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2593 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.08 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 40.26 
_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                            0.57 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        1773 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               1773 
_refine_hist.d_res_high                       2.55 
_refine_hist.d_res_low                        39.42 
# 
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' ? 0.005  ? 1799 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.790  ? 2407 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.008 ? 699  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 256  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 304  ? f_plane_restr      ? ? 
# 
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_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 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.55 2.71  . . 145 2650 99.00 . . . . 0.4005 . . . . . . . . . . . 0.4403 
'X-RAY DIFFRACTION' 2.71 2.92  . . 113 2634 99.00 . . . . 0.3730 . . . . . . . . . . . 0.4468 
'X-RAY DIFFRACTION' 2.92 3.21  . . 126 2644 98.00 . . . . 0.3694 . . . . . . . . . . . 0.4242 
'X-RAY DIFFRACTION' 3.21 3.68  . . 136 2658 99.00 . . . . 0.2892 . . . . . . . . . . . 0.4025 
'X-RAY DIFFRACTION' 3.68 4.63  . . 152 2601 97.00 . . . . 0.2299 . . . . . . . . . . . 0.2720 
'X-RAY DIFFRACTION' 4.63 39.42 . . 127 2614 98.00 . . . . 0.1897 . . . . . . . . . . . 0.2586 
# 
_struct.entry_id                     9GKR 
_struct.title                        'Crystal structure of artificial enzyme LmrR_pAF variant RMH in crystal form 1' 
_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        9GKR 
_struct_keywords.text            
'Artificial enzyme, unnatural amino acid, 4-aminophenylalanine, directed evolution, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A2RI36_LACLM 
_struct_ref.pdbx_db_accession          A2RI36 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AEIPKEMLRAQTNVILLNVLKQGDNYVYGIIKQVKEASNGEMELNEATLYTIFKRLEKDGIISSYWGDESQGGRRKYYRL
TEIGHENMRLAFESWSRVDKIIENLEANKKSEAIK
;
_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 9GKR A 2 ? 116 ? A2RI36 2 ? 116 ? 2 116 
2 1 9GKR B 2 ? 116 ? A2RI36 2 ? 116 ? 2 116 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GKR GLY A 1   ? UNP A2RI36 ?   ?  'expression tag'      1   1  
1 9GKR HOX A 15  ? UNP A2RI36 VAL 15 'engineered mutation' 15  2  
1 9GKR MET A 19  ? UNP A2RI36 ASN 19 'engineered mutation' 19  3  
1 9GKR ARG A 92  ? UNP A2RI36 ALA 92 'engineered mutation' 92  4  
1 9GKR HIS A 93  ? UNP A2RI36 PHE 93 'engineered mutation' 93  5  
1 9GKR SER A 117 ? UNP A2RI36 ?   ?  'expression tag'      117 6  
1 9GKR ARG A 118 ? UNP A2RI36 ?   ?  'expression tag'      118 7  
1 9GKR GLY A 119 ? UNP A2RI36 ?   ?  'expression tag'      119 8  
1 9GKR GLY A 120 ? UNP A2RI36 ?   ?  'expression tag'      120 9  
1 9GKR SER A 121 ? UNP A2RI36 ?   ?  'expression tag'      121 10 
1 9GKR GLY A 122 ? UNP A2RI36 ?   ?  'expression tag'      122 11 
1 9GKR GLY A 123 ? UNP A2RI36 ?   ?  'expression tag'      123 12 
1 9GKR TRP A 124 ? UNP A2RI36 ?   ?  'expression tag'      124 13 
1 9GKR SER A 125 ? UNP A2RI36 ?   ?  'expression tag'      125 14 
1 9GKR HIS A 126 ? UNP A2RI36 ?   ?  'expression tag'      126 15 
1 9GKR PRO A 127 ? UNP A2RI36 ?   ?  'expression tag'      127 16 
1 9GKR GLN A 128 ? UNP A2RI36 ?   ?  'expression tag'      128 17 
1 9GKR PHE A 129 ? UNP A2RI36 ?   ?  'expression tag'      129 18 
1 9GKR GLU A 130 ? UNP A2RI36 ?   ?  'expression tag'      130 19 
1 9GKR LYS A 131 ? UNP A2RI36 ?   ?  'expression tag'      131 20 
2 9GKR GLY B 1   ? UNP A2RI36 ?   ?  'expression tag'      1   21 
2 9GKR HOX B 15  ? UNP A2RI36 VAL 15 'engineered mutation' 15  22 
2 9GKR MET B 19  ? UNP A2RI36 ASN 19 'engineered mutation' 19  23 
2 9GKR ARG B 92  ? UNP A2RI36 ALA 92 'engineered mutation' 92  24 
2 9GKR HIS B 93  ? UNP A2RI36 PHE 93 'engineered mutation' 93  25 
2 9GKR SER B 117 ? UNP A2RI36 ?   ?  'expression tag'      117 26 
2 9GKR ARG B 118 ? UNP A2RI36 ?   ?  'expression tag'      118 27 
2 9GKR GLY B 119 ? UNP A2RI36 ?   ?  'expression tag'      119 28 
2 9GKR GLY B 120 ? UNP A2RI36 ?   ?  'expression tag'      120 29 
2 9GKR SER B 121 ? UNP A2RI36 ?   ?  'expression tag'      121 30 
2 9GKR GLY B 122 ? UNP A2RI36 ?   ?  'expression tag'      122 31 
2 9GKR GLY B 123 ? UNP A2RI36 ?   ?  'expression tag'      123 32 
2 9GKR TRP B 124 ? UNP A2RI36 ?   ?  'expression tag'      124 33 
2 9GKR SER B 125 ? UNP A2RI36 ?   ?  'expression tag'      125 34 
2 9GKR HIS B 126 ? UNP A2RI36 ?   ?  'expression tag'      126 35 
2 9GKR PRO B 127 ? UNP A2RI36 ?   ?  'expression tag'      127 36 
2 9GKR GLN B 128 ? UNP A2RI36 ?   ?  'expression tag'      128 37 
2 9GKR PHE B 129 ? UNP A2RI36 ?   ?  'expression tag'      129 38 
2 9GKR GLU B 130 ? UNP A2RI36 ?   ?  'expression tag'      130 39 
2 9GKR LYS B 131 ? UNP A2RI36 ?   ?  'expression tag'      131 40 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 2910  ? 
1 MORE         -18   ? 
1 'SSA (A^2)'  13950 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_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 5  ? GLY A 24  ? PRO A 5  GLY A 24  1 ? 20 
HELX_P HELX_P2 AA2 TYR A 27 ? SER A 39  ? TYR A 27 SER A 39  1 ? 13 
HELX_P HELX_P3 AA3 ASN A 46 ? ASP A 60  ? ASN A 46 ASP A 60  1 ? 15 
HELX_P HELX_P4 AA4 THR A 82 ? ILE A 115 ? THR A 82 ILE A 115 1 ? 34 
HELX_P HELX_P5 AA5 PRO B 5  ? GLY B 24  ? PRO B 5  GLY B 24  1 ? 20 
HELX_P HELX_P6 AA6 TYR B 27 ? SER B 39  ? TYR B 27 SER B 39  1 ? 13 
HELX_P HELX_P7 AA7 ASN B 46 ? ASP B 60  ? ASN B 46 ASP B 60  1 ? 15 
HELX_P HELX_P8 AA8 THR B 82 ? LYS B 110 ? THR B 82 LYS B 110 1 ? 29 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A ASN 14 C ? ? ? 1_555 A HOX 15 N ? ? A ASN 14 A HOX 15 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale both ? A HOX 15 C ? ? ? 1_555 A ILE 16 N ? ? A HOX 15 A ILE 16 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale3 covale both ? B ASN 14 C ? ? ? 1_555 B HOX 15 N ? ? B ASN 14 B HOX 15 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale4 covale both ? B HOX 15 C ? ? ? 1_555 B ILE 16 N ? ? B HOX 15 B ILE 16 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 HOX A 15 ? . . . . HOX A 15 ? 1_555 . . . . . . . PHE 1 HOX Amination 'Named protein modification' 
2 HOX B 15 ? . . . . HOX B 15 ? 1_555 . . . . . . . PHE 1 HOX Amination 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
# 
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 
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 63 ? GLY A 68 ? ILE A 63 GLY A 68 
AA1 2 ARG A 76 ? LEU A 81 ? ARG A 76 LEU A 81 
AA2 1 ILE B 63 ? TRP B 67 ? ILE B 63 TRP B 67 
AA2 2 LYS B 77 ? LEU B 81 ? LYS B 77 LEU B 81 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N SER A 64 ? N SER A 64 O ARG A 80 ? O ARG A 80 
AA2 1 2 N TYR B 66 ? N TYR B 66 O TYR B 78 ? O TYR B 78 
# 
_pdbx_entry_details.entry_id                   9GKR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     69 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             57.70 
_pdbx_validate_torsion.psi             19.21 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 17.092 -4.656 9.835  0.4114 0.3070 0.5210 -0.0173 -0.0184 0.0150 1.9774 1.9475  2.3003 -0.2306 
-0.9659 1.3685 -0.0823 0.0494 -0.0250 0.1709  0.0456  -0.1861 0.3140 0.4480 -0.1388 
'X-RAY DIFFRACTION' 2 ? refined 8.178  -0.675 32.767 0.8894 0.8040 0.4856 -0.0191 0.0113  0.0014 0.7835 -1.0019 1.8905 -0.7403 
-0.2209 1.3519 -0.2135 0.0744 -0.0012 -0.3426 -0.3116 0.0759  0.2953 1.0089 -0.3678 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 B 4 B 110 '( CHAIN B AND RESID 4:110 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 4 A 110 '( CHAIN A AND RESID 4:110 )' ? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A GLU 3   ? A GLU 3   
4  1 Y 1 A SER 71  ? A SER 71  
5  1 Y 1 A GLN 72  ? A GLN 72  
6  1 Y 1 A LYS 116 ? A LYS 116 
7  1 Y 1 A SER 117 ? A SER 117 
8  1 Y 1 A ARG 118 ? A ARG 118 
9  1 Y 1 A GLY 119 ? A GLY 119 
10 1 Y 1 A GLY 120 ? A GLY 120 
11 1 Y 1 A SER 121 ? A SER 121 
12 1 Y 1 A GLY 122 ? A GLY 122 
13 1 Y 1 A GLY 123 ? A GLY 123 
14 1 Y 1 A TRP 124 ? A TRP 124 
15 1 Y 1 A SER 125 ? A SER 125 
16 1 Y 1 A HIS 126 ? A HIS 126 
17 1 Y 1 A PRO 127 ? A PRO 127 
18 1 Y 1 A GLN 128 ? A GLN 128 
19 1 Y 1 A PHE 129 ? A PHE 129 
20 1 Y 1 A GLU 130 ? A GLU 130 
21 1 Y 1 A LYS 131 ? A LYS 131 
22 1 Y 1 B GLY 1   ? B GLY 1   
23 1 Y 1 B ALA 2   ? B ALA 2   
24 1 Y 1 B GLU 3   ? B GLU 3   
25 1 Y 1 B SER 71  ? B SER 71  
26 1 Y 1 B GLN 72  ? B GLN 72  
27 1 Y 1 B GLY 73  ? B GLY 73  
28 1 Y 1 B GLY 74  ? B GLY 74  
29 1 Y 1 B LYS 111 ? B LYS 111 
30 1 Y 1 B SER 112 ? B SER 112 
31 1 Y 1 B GLU 113 ? B GLU 113 
32 1 Y 1 B ALA 114 ? B ALA 114 
33 1 Y 1 B ILE 115 ? B ILE 115 
34 1 Y 1 B LYS 116 ? B LYS 116 
35 1 Y 1 B SER 117 ? B SER 117 
36 1 Y 1 B ARG 118 ? B ARG 118 
37 1 Y 1 B GLY 119 ? B GLY 119 
38 1 Y 1 B GLY 120 ? B GLY 120 
39 1 Y 1 B SER 121 ? B SER 121 
40 1 Y 1 B GLY 122 ? B GLY 122 
41 1 Y 1 B GLY 123 ? B GLY 123 
42 1 Y 1 B TRP 124 ? B TRP 124 
43 1 Y 1 B SER 125 ? B SER 125 
44 1 Y 1 B HIS 126 ? B HIS 126 
45 1 Y 1 B PRO 127 ? B PRO 127 
46 1 Y 1 B GLN 128 ? B GLN 128 
47 1 Y 1 B PHE 129 ? B PHE 129 
48 1 Y 1 B GLU 130 ? B GLU 130 
49 1 Y 1 B LYS 131 ? B LYS 131 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOX O    O N N 144 
HOX C    C N N 145 
HOX N    N N N 146 
HOX OXT  O N N 147 
HOX CA   C N S 148 
HOX CB   C N N 149 
HOX CG   C Y N 150 
HOX CZ   C Y N 151 
HOX NZ   N N N 152 
HOX CD1  C Y N 153 
HOX CD2  C Y N 154 
HOX CE1  C Y N 155 
HOX CE2  C Y N 156 
HOX H    H N N 157 
HOX H2   H N N 158 
HOX HXT  H N N 159 
HOX HA   H N N 160 
HOX HB   H N N 161 
HOX HBA  H N N 162 
HOX HNZ  H N N 163 
HOX HNZA H N N 164 
HOX HD1  H N N 165 
HOX HD2  H N N 166 
HOX HE1  H N N 167 
HOX HE2  H N N 168 
ILE N    N N N 169 
ILE CA   C N S 170 
ILE C    C N N 171 
ILE O    O N N 172 
ILE CB   C N S 173 
ILE CG1  C N N 174 
ILE CG2  C N N 175 
ILE CD1  C N N 176 
ILE OXT  O N N 177 
ILE H    H N N 178 
ILE H2   H N N 179 
ILE HA   H N N 180 
ILE HB   H N N 181 
ILE HG12 H N N 182 
ILE HG13 H N N 183 
ILE HG21 H N N 184 
ILE HG22 H N N 185 
ILE HG23 H N N 186 
ILE HD11 H N N 187 
ILE HD12 H N N 188 
ILE HD13 H N N 189 
ILE HXT  H N N 190 
LEU N    N N N 191 
LEU CA   C N S 192 
LEU C    C N N 193 
LEU O    O N N 194 
LEU CB   C N N 195 
LEU CG   C N N 196 
LEU CD1  C N N 197 
LEU CD2  C N N 198 
LEU OXT  O N N 199 
LEU H    H N N 200 
LEU H2   H N N 201 
LEU HA   H N N 202 
LEU HB2  H N N 203 
LEU HB3  H N N 204 
LEU HG   H N N 205 
LEU HD11 H N N 206 
LEU HD12 H N N 207 
LEU HD13 H N N 208 
LEU HD21 H N N 209 
LEU HD22 H N N 210 
LEU HD23 H N N 211 
LEU HXT  H N N 212 
LYS N    N N N 213 
LYS CA   C N S 214 
LYS C    C N N 215 
LYS O    O N N 216 
LYS CB   C N N 217 
LYS CG   C N N 218 
LYS CD   C N N 219 
LYS CE   C N N 220 
LYS NZ   N N N 221 
LYS OXT  O N N 222 
LYS H    H N N 223 
LYS H2   H N N 224 
LYS HA   H N N 225 
LYS HB2  H N N 226 
LYS HB3  H N N 227 
LYS HG2  H N N 228 
LYS HG3  H N N 229 
LYS HD2  H N N 230 
LYS HD3  H N N 231 
LYS HE2  H N N 232 
LYS HE3  H N N 233 
LYS HZ1  H N N 234 
LYS HZ2  H N N 235 
LYS HZ3  H N N 236 
LYS HXT  H N N 237 
MET N    N N N 238 
MET CA   C N S 239 
MET C    C N N 240 
MET O    O N N 241 
MET CB   C N N 242 
MET CG   C N N 243 
MET SD   S N N 244 
MET CE   C N N 245 
MET OXT  O N N 246 
MET H    H N N 247 
MET H2   H N N 248 
MET HA   H N N 249 
MET HB2  H N N 250 
MET HB3  H N N 251 
MET HG2  H N N 252 
MET HG3  H N N 253 
MET HE1  H N N 254 
MET HE2  H N N 255 
MET HE3  H N N 256 
MET HXT  H N N 257 
PHE N    N N N 258 
PHE CA   C N S 259 
PHE C    C N N 260 
PHE O    O N N 261 
PHE CB   C N N 262 
PHE CG   C Y N 263 
PHE CD1  C Y N 264 
PHE CD2  C Y N 265 
PHE CE1  C Y N 266 
PHE CE2  C Y N 267 
PHE CZ   C Y N 268 
PHE OXT  O N N 269 
PHE H    H N N 270 
PHE H2   H N N 271 
PHE HA   H N N 272 
PHE HB2  H N N 273 
PHE HB3  H N N 274 
PHE HD1  H N N 275 
PHE HD2  H N N 276 
PHE HE1  H N N 277 
PHE HE2  H N N 278 
PHE HZ   H N N 279 
PHE HXT  H N N 280 
PRO N    N N N 281 
PRO CA   C N S 282 
PRO C    C N N 283 
PRO O    O N N 284 
PRO CB   C N N 285 
PRO CG   C N N 286 
PRO CD   C N N 287 
PRO OXT  O N N 288 
PRO H    H N N 289 
PRO HA   H N N 290 
PRO HB2  H N N 291 
PRO HB3  H N N 292 
PRO HG2  H N N 293 
PRO HG3  H N N 294 
PRO HD2  H N N 295 
PRO HD3  H N N 296 
PRO HXT  H N N 297 
SER N    N N N 298 
SER CA   C N S 299 
SER C    C N N 300 
SER O    O N N 301 
SER CB   C N N 302 
SER OG   O N N 303 
SER OXT  O N N 304 
SER H    H N N 305 
SER H2   H N N 306 
SER HA   H N N 307 
SER HB2  H N N 308 
SER HB3  H N N 309 
SER HG   H N N 310 
SER HXT  H N N 311 
THR N    N N N 312 
THR CA   C N S 313 
THR C    C N N 314 
THR O    O N N 315 
THR CB   C N R 316 
THR OG1  O N N 317 
THR CG2  C N N 318 
THR OXT  O N N 319 
THR H    H N N 320 
THR H2   H N N 321 
THR HA   H N N 322 
THR HB   H N N 323 
THR HG1  H N N 324 
THR HG21 H N N 325 
THR HG22 H N N 326 
THR HG23 H N N 327 
THR HXT  H N N 328 
TRP N    N N N 329 
TRP CA   C N S 330 
TRP C    C N N 331 
TRP O    O N N 332 
TRP CB   C N N 333 
TRP CG   C Y N 334 
TRP CD1  C Y N 335 
TRP CD2  C Y N 336 
TRP NE1  N Y N 337 
TRP CE2  C Y N 338 
TRP CE3  C Y N 339 
TRP CZ2  C Y N 340 
TRP CZ3  C Y N 341 
TRP CH2  C Y N 342 
TRP OXT  O N N 343 
TRP H    H N N 344 
TRP H2   H N N 345 
TRP HA   H N N 346 
TRP HB2  H N N 347 
TRP HB3  H N N 348 
TRP HD1  H N N 349 
TRP HE1  H N N 350 
TRP HE3  H N N 351 
TRP HZ2  H N N 352 
TRP HZ3  H N N 353 
TRP HH2  H N N 354 
TRP HXT  H N N 355 
TYR N    N N N 356 
TYR CA   C N S 357 
TYR C    C N N 358 
TYR O    O N N 359 
TYR CB   C N N 360 
TYR CG   C Y N 361 
TYR CD1  C Y N 362 
TYR CD2  C Y N 363 
TYR CE1  C Y N 364 
TYR CE2  C Y N 365 
TYR CZ   C Y N 366 
TYR OH   O N N 367 
TYR OXT  O N N 368 
TYR H    H N N 369 
TYR H2   H N N 370 
TYR HA   H N N 371 
TYR HB2  H N N 372 
TYR HB3  H N N 373 
TYR HD1  H N N 374 
TYR HD2  H N N 375 
TYR HE1  H N N 376 
TYR HE2  H N N 377 
TYR HH   H N N 378 
TYR HXT  H N N 379 
VAL N    N N N 380 
VAL CA   C N S 381 
VAL C    C N N 382 
VAL O    O N N 383 
VAL CB   C N N 384 
VAL CG1  C N N 385 
VAL CG2  C N N 386 
VAL OXT  O N N 387 
VAL H    H N N 388 
VAL H2   H N N 389 
VAL HA   H N N 390 
VAL HB   H N N 391 
VAL HG11 H N N 392 
VAL HG12 H N N 393 
VAL HG13 H N N 394 
VAL HG21 H N N 395 
VAL HG22 H N N 396 
VAL HG23 H N N 397 
VAL HXT  H N N 398 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOX O   C    doub N N 137 
HOX CA  C    sing N N 138 
HOX C   OXT  sing N N 139 
HOX N   CA   sing N N 140 
HOX N   H    sing N N 141 
HOX N   H2   sing N N 142 
HOX OXT HXT  sing N N 143 
HOX CA  CB   sing N N 144 
HOX CA  HA   sing N N 145 
HOX CB  CG   sing N N 146 
HOX CB  HB   sing N N 147 
HOX CB  HBA  sing N N 148 
HOX CD1 CG   doub Y N 149 
HOX CG  CD2  sing Y N 150 
HOX CE1 CZ   doub Y N 151 
HOX CZ  CE2  sing Y N 152 
HOX CZ  NZ   sing N N 153 
HOX NZ  HNZ  sing N N 154 
HOX NZ  HNZA sing N N 155 
HOX CD1 CE1  sing Y N 156 
HOX CD1 HD1  sing N N 157 
HOX CD2 CE2  doub Y N 158 
HOX CD2 HD2  sing N N 159 
HOX CE1 HE1  sing N N 160 
HOX CE2 HE2  sing N N 161 
ILE N   CA   sing N N 162 
ILE N   H    sing N N 163 
ILE N   H2   sing N N 164 
ILE CA  C    sing N N 165 
ILE CA  CB   sing N N 166 
ILE CA  HA   sing N N 167 
ILE C   O    doub N N 168 
ILE C   OXT  sing N N 169 
ILE CB  CG1  sing N N 170 
ILE CB  CG2  sing N N 171 
ILE CB  HB   sing N N 172 
ILE CG1 CD1  sing N N 173 
ILE CG1 HG12 sing N N 174 
ILE CG1 HG13 sing N N 175 
ILE CG2 HG21 sing N N 176 
ILE CG2 HG22 sing N N 177 
ILE CG2 HG23 sing N N 178 
ILE CD1 HD11 sing N N 179 
ILE CD1 HD12 sing N N 180 
ILE CD1 HD13 sing N N 181 
ILE OXT HXT  sing N N 182 
LEU N   CA   sing N N 183 
LEU N   H    sing N N 184 
LEU N   H2   sing N N 185 
LEU CA  C    sing N N 186 
LEU CA  CB   sing N N 187 
LEU CA  HA   sing N N 188 
LEU C   O    doub N N 189 
LEU C   OXT  sing N N 190 
LEU CB  CG   sing N N 191 
LEU CB  HB2  sing N N 192 
LEU CB  HB3  sing N N 193 
LEU CG  CD1  sing N N 194 
LEU CG  CD2  sing N N 195 
LEU CG  HG   sing N N 196 
LEU CD1 HD11 sing N N 197 
LEU CD1 HD12 sing N N 198 
LEU CD1 HD13 sing N N 199 
LEU CD2 HD21 sing N N 200 
LEU CD2 HD22 sing N N 201 
LEU CD2 HD23 sing N N 202 
LEU OXT HXT  sing N N 203 
LYS N   CA   sing N N 204 
LYS N   H    sing N N 205 
LYS N   H2   sing N N 206 
LYS CA  C    sing N N 207 
LYS CA  CB   sing N N 208 
LYS CA  HA   sing N N 209 
LYS C   O    doub N N 210 
LYS C   OXT  sing N N 211 
LYS CB  CG   sing N N 212 
LYS CB  HB2  sing N N 213 
LYS CB  HB3  sing N N 214 
LYS CG  CD   sing N N 215 
LYS CG  HG2  sing N N 216 
LYS CG  HG3  sing N N 217 
LYS CD  CE   sing N N 218 
LYS CD  HD2  sing N N 219 
LYS CD  HD3  sing N N 220 
LYS CE  NZ   sing N N 221 
LYS CE  HE2  sing N N 222 
LYS CE  HE3  sing N N 223 
LYS NZ  HZ1  sing N N 224 
LYS NZ  HZ2  sing N N 225 
LYS NZ  HZ3  sing N N 226 
LYS OXT HXT  sing N N 227 
MET N   CA   sing N N 228 
MET N   H    sing N N 229 
MET N   H2   sing N N 230 
MET CA  C    sing N N 231 
MET CA  CB   sing N N 232 
MET CA  HA   sing N N 233 
MET C   O    doub N N 234 
MET C   OXT  sing N N 235 
MET CB  CG   sing N N 236 
MET CB  HB2  sing N N 237 
MET CB  HB3  sing N N 238 
MET CG  SD   sing N N 239 
MET CG  HG2  sing N N 240 
MET CG  HG3  sing N N 241 
MET SD  CE   sing N N 242 
MET CE  HE1  sing N N 243 
MET CE  HE2  sing N N 244 
MET CE  HE3  sing N N 245 
MET OXT HXT  sing N N 246 
PHE N   CA   sing N N 247 
PHE N   H    sing N N 248 
PHE N   H2   sing N N 249 
PHE CA  C    sing N N 250 
PHE CA  CB   sing N N 251 
PHE CA  HA   sing N N 252 
PHE C   O    doub N N 253 
PHE C   OXT  sing N N 254 
PHE CB  CG   sing N N 255 
PHE CB  HB2  sing N N 256 
PHE CB  HB3  sing N N 257 
PHE CG  CD1  doub Y N 258 
PHE CG  CD2  sing Y N 259 
PHE CD1 CE1  sing Y N 260 
PHE CD1 HD1  sing N N 261 
PHE CD2 CE2  doub Y N 262 
PHE CD2 HD2  sing N N 263 
PHE CE1 CZ   doub Y N 264 
PHE CE1 HE1  sing N N 265 
PHE CE2 CZ   sing Y N 266 
PHE CE2 HE2  sing N N 267 
PHE CZ  HZ   sing N N 268 
PHE OXT HXT  sing N N 269 
PRO N   CA   sing N N 270 
PRO N   CD   sing N N 271 
PRO N   H    sing N N 272 
PRO CA  C    sing N N 273 
PRO CA  CB   sing N N 274 
PRO CA  HA   sing N N 275 
PRO C   O    doub N N 276 
PRO C   OXT  sing N N 277 
PRO CB  CG   sing N N 278 
PRO CB  HB2  sing N N 279 
PRO CB  HB3  sing N N 280 
PRO CG  CD   sing N N 281 
PRO CG  HG2  sing N N 282 
PRO CG  HG3  sing N N 283 
PRO CD  HD2  sing N N 284 
PRO CD  HD3  sing N N 285 
PRO OXT HXT  sing N N 286 
SER N   CA   sing N N 287 
SER N   H    sing N N 288 
SER N   H2   sing N N 289 
SER CA  C    sing N N 290 
SER CA  CB   sing N N 291 
SER CA  HA   sing N N 292 
SER C   O    doub N N 293 
SER C   OXT  sing N N 294 
SER CB  OG   sing N N 295 
SER CB  HB2  sing N N 296 
SER CB  HB3  sing N N 297 
SER OG  HG   sing N N 298 
SER OXT HXT  sing N N 299 
THR N   CA   sing N N 300 
THR N   H    sing N N 301 
THR N   H2   sing N N 302 
THR CA  C    sing N N 303 
THR CA  CB   sing N N 304 
THR CA  HA   sing N N 305 
THR C   O    doub N N 306 
THR C   OXT  sing N N 307 
THR CB  OG1  sing N N 308 
THR CB  CG2  sing N N 309 
THR CB  HB   sing N N 310 
THR OG1 HG1  sing N N 311 
THR CG2 HG21 sing N N 312 
THR CG2 HG22 sing N N 313 
THR CG2 HG23 sing N N 314 
THR OXT HXT  sing N N 315 
TRP N   CA   sing N N 316 
TRP N   H    sing N N 317 
TRP N   H2   sing N N 318 
TRP CA  C    sing N N 319 
TRP CA  CB   sing N N 320 
TRP CA  HA   sing N N 321 
TRP C   O    doub N N 322 
TRP C   OXT  sing N N 323 
TRP CB  CG   sing N N 324 
TRP CB  HB2  sing N N 325 
TRP CB  HB3  sing N N 326 
TRP CG  CD1  doub Y N 327 
TRP CG  CD2  sing Y N 328 
TRP CD1 NE1  sing Y N 329 
TRP CD1 HD1  sing N N 330 
TRP CD2 CE2  doub Y N 331 
TRP CD2 CE3  sing Y N 332 
TRP NE1 CE2  sing Y N 333 
TRP NE1 HE1  sing N N 334 
TRP CE2 CZ2  sing Y N 335 
TRP CE3 CZ3  doub Y N 336 
TRP CE3 HE3  sing N N 337 
TRP CZ2 CH2  doub Y N 338 
TRP CZ2 HZ2  sing N N 339 
TRP CZ3 CH2  sing Y N 340 
TRP CZ3 HZ3  sing N N 341 
TRP CH2 HH2  sing N N 342 
TRP OXT HXT  sing N N 343 
TYR N   CA   sing N N 344 
TYR N   H    sing N N 345 
TYR N   H2   sing N N 346 
TYR CA  C    sing N N 347 
TYR CA  CB   sing N N 348 
TYR CA  HA   sing N N 349 
TYR C   O    doub N N 350 
TYR C   OXT  sing N N 351 
TYR CB  CG   sing N N 352 
TYR CB  HB2  sing N N 353 
TYR CB  HB3  sing N N 354 
TYR CG  CD1  doub Y N 355 
TYR CG  CD2  sing Y N 356 
TYR CD1 CE1  sing Y N 357 
TYR CD1 HD1  sing N N 358 
TYR CD2 CE2  doub Y N 359 
TYR CD2 HD2  sing N N 360 
TYR CE1 CZ   doub Y N 361 
TYR CE1 HE1  sing N N 362 
TYR CE2 CZ   sing Y N 363 
TYR CE2 HE2  sing N N 364 
TYR CZ  OH   sing N N 365 
TYR OH  HH   sing N N 366 
TYR OXT HXT  sing N N 367 
VAL N   CA   sing N N 368 
VAL N   H    sing N N 369 
VAL N   H2   sing N N 370 
VAL CA  C    sing N N 371 
VAL CA  CB   sing N N 372 
VAL CA  HA   sing N N 373 
VAL C   O    doub N N 374 
VAL C   OXT  sing N N 375 
VAL CB  CG1  sing N N 376 
VAL CB  CG2  sing N N 377 
VAL CB  HB   sing N N 378 
VAL CG1 HG11 sing N N 379 
VAL CG1 HG12 sing N N 380 
VAL CG1 HG13 sing N N 381 
VAL CG2 HG21 sing N N 382 
VAL CG2 HG22 sing N N 383 
VAL CG2 HG23 sing N N 384 
VAL OXT HXT  sing N N 385 
# 
_pdbx_audit_support.funding_organization   'European Research Council (ERC)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           885396 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6I8N 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GKR 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009344 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001277 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.027425 
_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]   0.014603 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . ILE A 1 4   ? 24.848 -7.420  22.329  1.00 89.37  ? 4   ILE A N   1 
ATOM   2    C CA  . ILE A 1 4   ? 23.617 -6.794  22.797  1.00 93.13  ? 4   ILE A CA  1 
ATOM   3    C C   . ILE A 1 4   ? 23.861 -5.325  23.122  1.00 99.93  ? 4   ILE A C   1 
ATOM   4    O O   . ILE A 1 4   ? 24.651 -5.011  24.010  1.00 106.43 ? 4   ILE A O   1 
ATOM   5    C CB  . ILE A 1 4   ? 23.060 -7.514  24.025  1.00 90.99  ? 4   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 4   ? 22.876 -9.003  23.738  1.00 92.69  ? 4   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 4   ? 21.734 -6.900  24.418  1.00 90.99  ? 4   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 4   ? 21.831 -9.293  22.698  1.00 93.81  ? 4   ILE A CD1 1 
ATOM   9    N N   . PRO A 1 5   ? 23.183 -4.429  22.411  1.00 94.69  ? 5   PRO A N   1 
ATOM   10   C CA  . PRO A 1 5   ? 23.433 -2.995  22.601  1.00 96.74  ? 5   PRO A CA  1 
ATOM   11   C C   . PRO A 1 5   ? 22.887 -2.478  23.924  1.00 103.50 ? 5   PRO A C   1 
ATOM   12   O O   . PRO A 1 5   ? 21.912 -3.000  24.469  1.00 100.24 ? 5   PRO A O   1 
ATOM   13   C CB  . PRO A 1 5   ? 22.703 -2.349  21.419  1.00 88.76  ? 5   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 5   ? 22.554 -3.451  20.420  1.00 89.96  ? 5   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 5   ? 22.359 -4.691  21.224  1.00 88.84  ? 5   PRO A CD  1 
ATOM   16   N N   . LYS A 1 6   ? 23.530 -1.418  24.430  1.00 120.46 ? 6   LYS A N   1 
ATOM   17   C CA  . LYS A 1 6   ? 23.060 -0.785  25.659  1.00 119.93 ? 6   LYS A CA  1 
ATOM   18   C C   . LYS A 1 6   ? 21.632 -0.291  25.511  1.00 116.13 ? 6   LYS A C   1 
ATOM   19   O O   . LYS A 1 6   ? 20.800 -0.493  26.403  1.00 114.95 ? 6   LYS A O   1 
ATOM   20   C CB  . LYS A 1 6   ? 23.958 0.395   26.030  1.00 123.04 ? 6   LYS A CB  1 
ATOM   21   C CG  . LYS A 1 6   ? 23.457 1.157   27.258  1.00 131.94 ? 6   LYS A CG  1 
ATOM   22   C CD  . LYS A 1 6   ? 24.152 2.499   27.435  1.00 136.41 ? 6   LYS A CD  1 
ATOM   23   C CE  . LYS A 1 6   ? 23.626 3.248   28.659  1.00 137.63 ? 6   LYS A CE  1 
ATOM   24   N NZ  . LYS A 1 6   ? 24.150 2.704   29.942  1.00 143.71 ? 6   LYS A NZ  1 
ATOM   25   N N   . GLU A 1 7   ? 21.323 0.331   24.375  1.00 96.10  ? 7   GLU A N   1 
ATOM   26   C CA  . GLU A 1 7   ? 19.985 0.859   24.163  1.00 90.59  ? 7   GLU A CA  1 
ATOM   27   C C   . GLU A 1 7   ? 18.942 -0.245  24.168  1.00 87.40  ? 7   GLU A C   1 
ATOM   28   O O   . GLU A 1 7   ? 17.773 0.012   24.474  1.00 88.05  ? 7   GLU A O   1 
ATOM   29   C CB  . GLU A 1 7   ? 19.940 1.658   22.865  1.00 90.34  ? 7   GLU A CB  1 
ATOM   30   C CG  . GLU A 1 7   ? 20.947 2.798   22.831  1.00 100.18 ? 7   GLU A CG  1 
ATOM   31   C CD  . GLU A 1 7   ? 22.355 2.344   22.494  1.00 104.27 ? 7   GLU A CD  1 
ATOM   32   O OE1 . GLU A 1 7   ? 22.548 1.712   21.432  1.00 106.00 ? 7   GLU A OE1 1 
ATOM   33   O OE2 . GLU A 1 7   ? 23.270 2.616   23.298  1.00 106.52 ? 7   GLU A OE2 1 
ATOM   34   N N   . MET A 1 8   ? 19.335 -1.479  23.848  1.00 82.37  ? 8   MET A N   1 
ATOM   35   C CA  . MET A 1 8   ? 18.341 -2.543  23.828  1.00 81.24  ? 8   MET A CA  1 
ATOM   36   C C   . MET A 1 8   ? 18.065 -3.062  25.234  1.00 80.92  ? 8   MET A C   1 
ATOM   37   O O   . MET A 1 8   ? 16.904 -3.273  25.603  1.00 76.62  ? 8   MET A O   1 
ATOM   38   C CB  . MET A 1 8   ? 18.792 -3.686  22.918  1.00 81.36  ? 8   MET A CB  1 
ATOM   39   C CG  . MET A 1 8   ? 17.645 -4.562  22.446  1.00 71.43  ? 8   MET A CG  1 
ATOM   40   S SD  . MET A 1 8   ? 18.080 -5.725  21.149  1.00 66.08  ? 8   MET A SD  1 
ATOM   41   C CE  . MET A 1 8   ? 17.861 -7.235  22.077  1.00 77.78  ? 8   MET A CE  1 
ATOM   42   N N   . LEU A 1 9   ? 19.109 -3.250  26.042  1.00 82.74  ? 9   LEU A N   1 
ATOM   43   C CA  . LEU A 1 9   ? 18.880 -3.628  27.432  1.00 79.13  ? 9   LEU A CA  1 
ATOM   44   C C   . LEU A 1 9   ? 18.217 -2.489  28.193  1.00 78.65  ? 9   LEU A C   1 
ATOM   45   O O   . LEU A 1 9   ? 17.348 -2.723  29.042  1.00 75.12  ? 9   LEU A O   1 
ATOM   46   C CB  . LEU A 1 9   ? 20.191 -4.034  28.101  1.00 83.09  ? 9   LEU A CB  1 
ATOM   47   C CG  . LEU A 1 9   ? 20.040 -4.422  29.577  1.00 84.86  ? 9   LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 9   ? 19.063 -5.583  29.748  1.00 77.09  ? 9   LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 9   ? 21.386 -4.741  30.218  1.00 85.29  ? 9   LEU A CD2 1 
ATOM   50   N N   . ARG A 1 10  ? 18.601 -1.246  27.882  1.00 79.22  ? 10  ARG A N   1 
ATOM   51   C CA  . ARG A 1 10  ? 17.924 -0.091  28.461  1.00 79.41  ? 10  ARG A CA  1 
ATOM   52   C C   . ARG A 1 10  ? 16.443 -0.103  28.110  1.00 75.65  ? 10  ARG A C   1 
ATOM   53   O O   . ARG A 1 10  ? 15.590 0.131   28.973  1.00 73.54  ? 10  ARG A O   1 
ATOM   54   C CB  . ARG A 1 10  ? 18.594 1.197   27.974  1.00 85.29  ? 10  ARG A CB  1 
ATOM   55   C CG  . ARG A 1 10  ? 18.008 2.499   28.515  1.00 85.88  ? 10  ARG A CG  1 
ATOM   56   C CD  . ARG A 1 10  ? 19.040 3.629   28.453  1.00 91.86  ? 10  ARG A CD  1 
ATOM   57   N NE  . ARG A 1 10  ? 18.441 4.951   28.617  1.00 109.36 ? 10  ARG A NE  1 
ATOM   58   C CZ  . ARG A 1 10  ? 19.116 6.060   28.898  1.00 115.85 ? 10  ARG A CZ  1 
ATOM   59   N NH1 . ARG A 1 10  ? 20.428 6.048   29.075  1.00 119.70 ? 10  ARG A NH1 1 
ATOM   60   N NH2 . ARG A 1 10  ? 18.456 7.212   29.006  1.00 110.14 ? 10  ARG A NH2 1 
ATOM   61   N N   . ALA A 1 11  ? 16.119 -0.406  26.855  1.00 76.77  ? 11  ALA A N   1 
ATOM   62   C CA  . ALA A 1 11  ? 14.723 -0.451  26.441  1.00 73.43  ? 11  ALA A CA  1 
ATOM   63   C C   . ALA A 1 11  ? 13.974 -1.592  27.117  1.00 71.25  ? 11  ALA A C   1 
ATOM   64   O O   . ALA A 1 11  ? 12.802 -1.440  27.479  1.00 67.81  ? 11  ALA A O   1 
ATOM   65   C CB  . ALA A 1 11  ? 14.634 -0.580  24.922  1.00 74.63  ? 11  ALA A CB  1 
ATOM   66   N N   . GLN A 1 12  ? 14.624 -2.747  27.285  1.00 76.63  ? 12  GLN A N   1 
ATOM   67   C CA  . GLN A 1 12  ? 13.944 -3.894  27.883  1.00 74.11  ? 12  GLN A CA  1 
ATOM   68   C C   . GLN A 1 12  ? 13.633 -3.657  29.355  1.00 71.61  ? 12  GLN A C   1 
ATOM   69   O O   . GLN A 1 12  ? 12.522 -3.939  29.818  1.00 65.80  ? 12  GLN A O   1 
ATOM   70   C CB  . GLN A 1 12  ? 14.790 -5.158  27.729  1.00 78.52  ? 12  GLN A CB  1 
ATOM   71   C CG  . GLN A 1 12  ? 14.944 -5.667  26.307  1.00 78.24  ? 12  GLN A CG  1 
ATOM   72   C CD  . GLN A 1 12  ? 15.777 -6.934  26.247  1.00 84.24  ? 12  GLN A CD  1 
ATOM   73   O OE1 . GLN A 1 12  ? 16.362 -7.350  27.250  1.00 89.07  ? 12  GLN A OE1 1 
ATOM   74   N NE2 . GLN A 1 12  ? 15.824 -7.564  25.075  1.00 81.68  ? 12  GLN A NE2 1 
ATOM   75   N N   . THR A 1 13  ? 14.605 -3.151  30.114  1.00 64.37  ? 13  THR A N   1 
ATOM   76   C CA  . THR A 1 13  ? 14.335 -2.832  31.511  1.00 68.30  ? 13  THR A CA  1 
ATOM   77   C C   . THR A 1 13  ? 13.204 -1.820  31.627  1.00 68.29  ? 13  THR A C   1 
ATOM   78   O O   . THR A 1 13  ? 12.337 -1.941  32.500  1.00 66.34  ? 13  THR A O   1 
ATOM   79   C CB  . THR A 1 13  ? 15.599 -2.317  32.195  1.00 70.15  ? 13  THR A CB  1 
ATOM   80   O OG1 . THR A 1 13  ? 16.595 -3.343  32.197  1.00 74.50  ? 13  THR A OG1 1 
ATOM   81   C CG2 . THR A 1 13  ? 15.303 -1.921  33.617  1.00 71.92  ? 13  THR A CG2 1 
ATOM   82   N N   . ASN A 1 14  ? 13.197 -0.820  30.754  1.00 64.42  ? 14  ASN A N   1 
ATOM   83   C CA  . ASN A 1 14  ? 12.143 0.173   30.733  1.00 60.97  ? 14  ASN A CA  1 
ATOM   84   C C   . ASN A 1 14  ? 10.796 -0.514  30.576  1.00 60.81  ? 14  ASN A C   1 
ATOM   85   O O   . ASN A 1 14  ? 9.844  -0.203  31.283  1.00 57.85  ? 14  ASN A O   1 
ATOM   86   C CB  . ASN A 1 14  ? 12.379 1.161   29.591  1.00 64.53  ? 14  ASN A CB  1 
ATOM   87   C CG  . ASN A 1 14  ? 12.170 2.607   30.001  1.00 62.94  ? 14  ASN A CG  1 
ATOM   88   O OD1 . ASN A 1 14  ? 11.110 3.179   29.761  1.00 58.59  ? 14  ASN A OD1 1 
ATOM   89   N ND2 . ASN A 1 14  ? 13.194 3.213   30.599  1.00 60.37  ? 14  ASN A ND2 1 
HETATM 90   O O   . HOX A 1 15  ? 7.704  -3.032  30.697  1.00 73.61  ? 15  HOX A O   1 
HETATM 91   C C   . HOX A 1 15  ? 8.913  -2.997  30.453  1.00 72.75  ? 15  HOX A C   1 
HETATM 92   N N   . HOX A 1 15  ? 10.747 -1.485  29.671  1.00 71.21  ? 15  HOX A N   1 
HETATM 93   C CA  . HOX A 1 15  ? 9.520  -2.175  29.318  1.00 72.15  ? 15  HOX A CA  1 
HETATM 94   C CB  . HOX A 1 15  ? 9.713  -3.121  28.102  1.00 72.97  ? 15  HOX A CB  1 
HETATM 95   C CG  . HOX A 1 15  ? 8.438  -3.777  27.697  1.00 77.46  ? 15  HOX A CG  1 
HETATM 96   C CZ  . HOX A 1 15  ? 6.019  -5.019  26.934  1.00 71.75  ? 15  HOX A CZ  1 
HETATM 97   N NZ  . HOX A 1 15  ? 4.825  -5.625  26.558  1.00 77.09  ? 15  HOX A NZ  1 
HETATM 98   C CD1 . HOX A 1 15  ? 7.284  -3.018  27.481  1.00 74.95  ? 15  HOX A CD1 1 
HETATM 99   C CD2 . HOX A 1 15  ? 8.367  -5.164  27.515  1.00 78.81  ? 15  HOX A CD2 1 
HETATM 100  C CE1 . HOX A 1 15  ? 6.090  -3.619  27.111  1.00 75.55  ? 15  HOX A CE1 1 
HETATM 101  C CE2 . HOX A 1 15  ? 7.184  -5.787  27.141  1.00 74.08  ? 15  HOX A CE2 1 
ATOM   102  N N   . ILE A 1 16  ? 9.771  -3.701  31.178  1.00 62.03  ? 16  ILE A N   1 
ATOM   103  C CA  . ILE A 1 16  ? 9.284  -4.508  32.284  1.00 64.51  ? 16  ILE A CA  1 
ATOM   104  C C   . ILE A 1 16  ? 8.755  -3.608  33.379  1.00 64.08  ? 16  ILE A C   1 
ATOM   105  O O   . ILE A 1 16  ? 7.648  -3.817  33.871  1.00 62.33  ? 16  ILE A O   1 
ATOM   106  C CB  . ILE A 1 16  ? 10.366 -5.431  32.826  1.00 67.71  ? 16  ILE A CB  1 
ATOM   107  C CG1 . ILE A 1 16  ? 10.742 -6.478  31.776  1.00 68.28  ? 16  ILE A CG1 1 
ATOM   108  C CG2 . ILE A 1 16  ? 9.878  -6.102  34.084  1.00 77.66  ? 16  ILE A CG2 1 
ATOM   109  C CD1 . ILE A 1 16  ? 11.788 -7.459  32.223  1.00 64.49  ? 16  ILE A CD1 1 
ATOM   110  N N   . LEU A 1 17  ? 9.552  -2.588  33.723  1.00 64.12  ? 17  LEU A N   1 
ATOM   111  C CA  . LEU A 1 17  ? 9.199  -1.676  34.809  1.00 63.63  ? 17  LEU A CA  1 
ATOM   112  C C   . LEU A 1 17  ? 7.831  -1.061  34.590  1.00 64.07  ? 17  LEU A C   1 
ATOM   113  O O   . LEU A 1 17  ? 6.998  -1.032  35.501  1.00 66.18  ? 17  LEU A O   1 
ATOM   114  C CB  . LEU A 1 17  ? 10.249 -0.571  34.947  1.00 59.45  ? 17  LEU A CB  1 
ATOM   115  C CG  . LEU A 1 17  ? 11.605 -0.902  35.578  1.00 66.47  ? 17  LEU A CG  1 
ATOM   116  C CD1 . LEU A 1 17  ? 12.531 0.299   35.592  1.00 64.82  ? 17  LEU A CD1 1 
ATOM   117  C CD2 . LEU A 1 17  ? 11.407 -1.386  36.999  1.00 74.98  ? 17  LEU A CD2 1 
ATOM   118  N N   . LEU A 1 18  ? 7.575  -0.569  33.381  1.00 63.48  ? 18  LEU A N   1 
ATOM   119  C CA  . LEU A 1 18  ? 6.273  0.028   33.115  1.00 67.88  ? 18  LEU A CA  1 
ATOM   120  C C   . LEU A 1 18  ? 5.174  -1.018  33.171  1.00 71.98  ? 18  LEU A C   1 
ATOM   121  O O   . LEU A 1 18  ? 4.052  -0.712  33.587  1.00 73.91  ? 18  LEU A O   1 
ATOM   122  C CB  . LEU A 1 18  ? 6.282  0.741   31.762  1.00 66.43  ? 18  LEU A CB  1 
ATOM   123  C CG  . LEU A 1 18  ? 6.888  2.147   31.754  1.00 56.30  ? 18  LEU A CG  1 
ATOM   124  C CD1 . LEU A 1 18  ? 7.059  2.657   30.355  1.00 59.81  ? 18  LEU A CD1 1 
ATOM   125  C CD2 . LEU A 1 18  ? 5.997  3.086   32.518  1.00 65.22  ? 18  LEU A CD2 1 
ATOM   126  N N   . MET A 1 19  ? 5.473  -2.252  32.760  1.00 68.24  ? 19  MET A N   1 
ATOM   127  C CA  . MET A 1 19  ? 4.483  -3.314  32.874  1.00 75.91  ? 19  MET A CA  1 
ATOM   128  C C   . MET A 1 19  ? 4.160  -3.604  34.330  1.00 81.28  ? 19  MET A C   1 
ATOM   129  O O   . MET A 1 19  ? 3.000  -3.847  34.681  1.00 85.94  ? 19  MET A O   1 
ATOM   130  C CB  . MET A 1 19  ? 4.981  -4.580  32.181  1.00 82.95  ? 19  MET A CB  1 
ATOM   131  C CG  . MET A 1 19  ? 4.853  -4.554  30.670  1.00 80.68  ? 19  MET A CG  1 
ATOM   132  S SD  . MET A 1 19  ? 3.141  -4.371  30.139  1.00 86.23  ? 19  MET A SD  1 
ATOM   133  C CE  . MET A 1 19  ? 2.340  -5.645  31.105  1.00 99.94  ? 19  MET A CE  1 
ATOM   134  N N   . VAL A 1 20  ? 5.175  -3.566  35.193  1.00 81.41  ? 20  VAL A N   1 
ATOM   135  C CA  . VAL A 1 20  ? 4.959  -3.814  36.614  1.00 78.75  ? 20  VAL A CA  1 
ATOM   136  C C   . VAL A 1 20  ? 3.972  -2.806  37.184  1.00 81.80  ? 20  VAL A C   1 
ATOM   137  O O   . VAL A 1 20  ? 3.002  -3.173  37.855  1.00 92.82  ? 20  VAL A O   1 
ATOM   138  C CB  . VAL A 1 20  ? 6.295  -3.775  37.373  1.00 75.72  ? 20  VAL A CB  1 
ATOM   139  C CG1 . VAL A 1 20  ? 6.045  -3.826  38.868  1.00 84.88  ? 20  VAL A CG1 1 
ATOM   140  C CG2 . VAL A 1 20  ? 7.198  -4.911  36.927  1.00 79.30  ? 20  VAL A CG2 1 
ATOM   141  N N   . LEU A 1 21  ? 4.204  -1.519  36.931  1.00 78.89  ? 21  LEU A N   1 
ATOM   142  C CA  . LEU A 1 21  ? 3.288  -0.512  37.446  1.00 82.29  ? 21  LEU A CA  1 
ATOM   143  C C   . LEU A 1 21  ? 1.905  -0.678  36.851  1.00 91.29  ? 21  LEU A C   1 
ATOM   144  O O   . LEU A 1 21  ? 0.907  -0.323  37.487  1.00 97.74  ? 21  LEU A O   1 
ATOM   145  C CB  . LEU A 1 21  ? 3.811  0.886   37.156  1.00 72.12  ? 21  LEU A CB  1 
ATOM   146  C CG  . LEU A 1 21  ? 5.097  1.190   37.907  1.00 76.88  ? 21  LEU A CG  1 
ATOM   147  C CD1 . LEU A 1 21  ? 5.475  2.652   37.737  1.00 78.59  ? 21  LEU A CD1 1 
ATOM   148  C CD2 . LEU A 1 21  ? 4.968  0.804   39.373  1.00 77.90  ? 21  LEU A CD2 1 
ATOM   149  N N   . LYS A 1 22  ? 1.830  -1.195  35.627  1.00 90.69  ? 22  LYS A N   1 
ATOM   150  C CA  . LYS A 1 22  ? 0.536  -1.467  35.022  1.00 97.84  ? 22  LYS A CA  1 
ATOM   151  C C   . LYS A 1 22  ? -0.197 -2.581  35.759  1.00 102.05 ? 22  LYS A C   1 
ATOM   152  O O   . LYS A 1 22  ? -1.427 -2.540  35.872  1.00 102.01 ? 22  LYS A O   1 
ATOM   153  C CB  . LYS A 1 22  ? 0.722  -1.814  33.545  1.00 102.70 ? 22  LYS A CB  1 
ATOM   154  C CG  . LYS A 1 22  ? -0.555 -1.784  32.727  1.00 107.96 ? 22  LYS A CG  1 
ATOM   155  C CD  . LYS A 1 22  ? -0.350 -2.421  31.362  1.00 109.93 ? 22  LYS A CD  1 
ATOM   156  C CE  . LYS A 1 22  ? -1.674 -2.602  30.638  1.00 113.14 ? 22  LYS A CE  1 
ATOM   157  N NZ  . LYS A 1 22  ? -1.526 -3.431  29.411  1.00 113.38 ? 22  LYS A NZ  1 
ATOM   158  N N   . GLN A 1 23  ? 0.538  -3.571  36.277  1.00 101.38 ? 23  GLN A N   1 
ATOM   159  C CA  . GLN A 1 23  ? -0.075 -4.576  37.141  1.00 109.45 ? 23  GLN A CA  1 
ATOM   160  C C   . GLN A 1 23  ? -0.679 -3.947  38.387  1.00 111.28 ? 23  GLN A C   1 
ATOM   161  O O   . GLN A 1 23  ? -1.696 -4.430  38.898  1.00 122.57 ? 23  GLN A O   1 
ATOM   162  C CB  . GLN A 1 23  ? 0.954  -5.630  37.551  1.00 111.57 ? 23  GLN A CB  1 
ATOM   163  C CG  . GLN A 1 23  ? 1.676  -6.303  36.404  1.00 115.55 ? 23  GLN A CG  1 
ATOM   164  C CD  . GLN A 1 23  ? 0.759  -7.168  35.571  1.00 130.21 ? 23  GLN A CD  1 
ATOM   165  O OE1 . GLN A 1 23  ? -0.319 -7.561  36.016  1.00 137.02 ? 23  GLN A OE1 1 
ATOM   166  N NE2 . GLN A 1 23  ? 1.184  -7.475  34.353  1.00 128.68 ? 23  GLN A NE2 1 
ATOM   167  N N   . GLY A 1 24  ? -0.078 -2.883  38.883  1.00 114.21 ? 24  GLY A N   1 
ATOM   168  C CA  . GLY A 1 24  ? -0.548 -2.198  40.069  1.00 109.63 ? 24  GLY A CA  1 
ATOM   169  C C   . GLY A 1 24  ? 0.588  -1.458  40.736  1.00 98.95  ? 24  GLY A C   1 
ATOM   170  O O   . GLY A 1 24  ? 1.765  -1.736  40.518  1.00 96.21  ? 24  GLY A O   1 
ATOM   171  N N   . ASP A 1 25  ? 0.214  -0.503  41.585  1.00 92.52  ? 25  ASP A N   1 
ATOM   172  C CA  . ASP A 1 25  ? 1.186  0.336   42.271  1.00 85.73  ? 25  ASP A CA  1 
ATOM   173  C C   . ASP A 1 25  ? 2.191  -0.516  43.033  1.00 84.42  ? 25  ASP A C   1 
ATOM   174  O O   . ASP A 1 25  ? 1.919  -1.661  43.404  1.00 87.94  ? 25  ASP A O   1 
ATOM   175  C CB  . ASP A 1 25  ? 0.476  1.301   43.219  1.00 83.24  ? 25  ASP A CB  1 
ATOM   176  C CG  . ASP A 1 25  ? -0.528 2.174   42.502  1.00 83.32  ? 25  ASP A CG  1 
ATOM   177  O OD1 . ASP A 1 25  ? -0.776 1.911   41.313  1.00 91.28  ? 25  ASP A OD1 1 
ATOM   178  O OD2 . ASP A 1 25  ? -1.064 3.121   43.113  1.00 84.85  ? 25  ASP A OD2 1 
ATOM   179  N N   . ASN A 1 26  ? 3.383  0.036   43.223  1.00 79.83  ? 26  ASN A N   1 
ATOM   180  C CA  . ASN A 1 26  ? 4.452  -0.706  43.868  1.00 81.92  ? 26  ASN A CA  1 
ATOM   181  C C   . ASN A 1 26  ? 5.523  0.263   44.335  1.00 82.76  ? 26  ASN A C   1 
ATOM   182  O O   . ASN A 1 26  ? 5.527  1.444   43.979  1.00 78.87  ? 26  ASN A O   1 
ATOM   183  C CB  . ASN A 1 26  ? 5.049  -1.748  42.926  1.00 81.78  ? 26  ASN A CB  1 
ATOM   184  C CG  . ASN A 1 26  ? 5.734  -2.864  43.662  1.00 91.01  ? 26  ASN A CG  1 
ATOM   185  O OD1 . ASN A 1 26  ? 6.249  -2.670  44.763  1.00 86.89  ? 26  ASN A OD1 1 
ATOM   186  N ND2 . ASN A 1 26  ? 5.766  -4.040  43.052  1.00 97.29  ? 26  ASN A ND2 1 
ATOM   187  N N   . TYR A 1 27  ? 6.445  -0.271  45.126  1.00 82.61  ? 27  TYR A N   1 
ATOM   188  C CA  . TYR A 1 27  ? 7.573  0.456   45.677  1.00 85.29  ? 27  TYR A CA  1 
ATOM   189  C C   . TYR A 1 27  ? 8.854  -0.263  45.269  1.00 89.45  ? 27  TYR A C   1 
ATOM   190  O O   . TYR A 1 27  ? 8.828  -1.415  44.829  1.00 91.29  ? 27  TYR A O   1 
ATOM   191  C CB  . TYR A 1 27  ? 7.459  0.577   47.204  1.00 84.33  ? 27  TYR A CB  1 
ATOM   192  C CG  . TYR A 1 27  ? 7.528  -0.741  47.933  1.00 91.12  ? 27  TYR A CG  1 
ATOM   193  C CD1 . TYR A 1 27  ? 6.407  -1.549  48.059  1.00 91.79  ? 27  TYR A CD1 1 
ATOM   194  C CD2 . TYR A 1 27  ? 8.716  -1.177  48.500  1.00 92.79  ? 27  TYR A CD2 1 
ATOM   195  C CE1 . TYR A 1 27  ? 6.472  -2.758  48.722  1.00 99.96  ? 27  TYR A CE1 1 
ATOM   196  C CE2 . TYR A 1 27  ? 8.790  -2.379  49.168  1.00 94.76  ? 27  TYR A CE2 1 
ATOM   197  C CZ  . TYR A 1 27  ? 7.668  -3.169  49.275  1.00 102.00 ? 27  TYR A CZ  1 
ATOM   198  O OH  . TYR A 1 27  ? 7.749  -4.371  49.943  1.00 107.90 ? 27  TYR A OH  1 
ATOM   199  N N   . VAL A 1 28  ? 9.985  0.424   45.455  1.00 88.53  ? 28  VAL A N   1 
ATOM   200  C CA  . VAL A 1 28  ? 11.239 0.014   44.820  1.00 83.20  ? 28  VAL A CA  1 
ATOM   201  C C   . VAL A 1 28  ? 11.625 -1.400  45.238  1.00 84.00  ? 28  VAL A C   1 
ATOM   202  O O   . VAL A 1 28  ? 11.940 -2.250  44.396  1.00 88.21  ? 28  VAL A O   1 
ATOM   203  C CB  . VAL A 1 28  ? 12.357 1.020   45.146  1.00 76.24  ? 28  VAL A CB  1 
ATOM   204  C CG1 . VAL A 1 28  ? 13.714 0.441   44.806  1.00 77.59  ? 28  VAL A CG1 1 
ATOM   205  C CG2 . VAL A 1 28  ? 12.126 2.331   44.426  1.00 71.57  ? 28  VAL A CG2 1 
ATOM   206  N N   . TYR A 1 29  ? 11.611 -1.673  46.545  1.00 84.73  ? 29  TYR A N   1 
ATOM   207  C CA  . TYR A 1 29  ? 12.016 -2.990  47.030  1.00 85.98  ? 29  TYR A CA  1 
ATOM   208  C C   . TYR A 1 29  ? 11.030 -4.070  46.599  1.00 87.84  ? 29  TYR A C   1 
ATOM   209  O O   . TYR A 1 29  ? 11.432 -5.190  46.264  1.00 85.79  ? 29  TYR A O   1 
ATOM   210  C CB  . TYR A 1 29  ? 12.145 -2.957  48.549  1.00 89.30  ? 29  TYR A CB  1 
ATOM   211  C CG  . TYR A 1 29  ? 13.189 -1.981  49.035  1.00 98.64  ? 29  TYR A CG  1 
ATOM   212  C CD1 . TYR A 1 29  ? 14.331 -1.743  48.291  1.00 100.63 ? 29  TYR A CD1 1 
ATOM   213  C CD2 . TYR A 1 29  ? 13.023 -1.279  50.231  1.00 101.37 ? 29  TYR A CD2 1 
ATOM   214  C CE1 . TYR A 1 29  ? 15.283 -0.847  48.723  1.00 108.73 ? 29  TYR A CE1 1 
ATOM   215  C CE2 . TYR A 1 29  ? 13.979 -0.374  50.671  1.00 101.78 ? 29  TYR A CE2 1 
ATOM   216  C CZ  . TYR A 1 29  ? 15.107 -0.164  49.908  1.00 106.83 ? 29  TYR A CZ  1 
ATOM   217  O OH  . TYR A 1 29  ? 16.074 0.724   50.319  1.00 107.95 ? 29  TYR A OH  1 
ATOM   218  N N   . GLY A 1 30  ? 9.735  -3.750  46.599  1.00 88.00  ? 30  GLY A N   1 
ATOM   219  C CA  . GLY A 1 30  ? 8.754  -4.678  46.071  1.00 92.26  ? 30  GLY A CA  1 
ATOM   220  C C   . GLY A 1 30  ? 8.909  -4.897  44.582  1.00 95.92  ? 30  GLY A C   1 
ATOM   221  O O   . GLY A 1 30  ? 8.685  -6.005  44.088  1.00 103.20 ? 30  GLY A O   1 
ATOM   222  N N   . ILE A 1 31  ? 9.314  -3.860  43.851  1.00 93.13  ? 31  ILE A N   1 
ATOM   223  C CA  . ILE A 1 31  ? 9.538  -4.014  42.418  1.00 93.36  ? 31  ILE A CA  1 
ATOM   224  C C   . ILE A 1 31  ? 10.718 -4.939  42.176  1.00 95.29  ? 31  ILE A C   1 
ATOM   225  O O   . ILE A 1 31  ? 10.673 -5.811  41.302  1.00 99.04  ? 31  ILE A O   1 
ATOM   226  C CB  . ILE A 1 31  ? 9.747  -2.641  41.757  1.00 85.29  ? 31  ILE A CB  1 
ATOM   227  C CG1 . ILE A 1 31  ? 8.437  -1.864  41.737  1.00 80.80  ? 31  ILE A CG1 1 
ATOM   228  C CG2 . ILE A 1 31  ? 10.302 -2.797  40.356  1.00 83.14  ? 31  ILE A CG2 1 
ATOM   229  C CD1 . ILE A 1 31  ? 8.592  -0.450  41.285  1.00 80.90  ? 31  ILE A CD1 1 
ATOM   230  N N   . ILE A 1 32  ? 11.787 -4.777  42.953  1.00 89.63  ? 32  ILE A N   1 
ATOM   231  C CA  . ILE A 1 32  ? 12.896 -5.712  42.853  1.00 90.56  ? 32  ILE A CA  1 
ATOM   232  C C   . ILE A 1 32  ? 12.418 -7.108  43.218  1.00 102.73 ? 32  ILE A C   1 
ATOM   233  O O   . ILE A 1 32  ? 12.724 -8.091  42.533  1.00 107.65 ? 32  ILE A O   1 
ATOM   234  C CB  . ILE A 1 32  ? 14.058 -5.260  43.749  1.00 83.39  ? 32  ILE A CB  1 
ATOM   235  C CG1 . ILE A 1 32  ? 14.685 -3.988  43.191  1.00 82.76  ? 32  ILE A CG1 1 
ATOM   236  C CG2 . ILE A 1 32  ? 15.092 -6.359  43.864  1.00 80.61  ? 32  ILE A CG2 1 
ATOM   237  C CD1 . ILE A 1 32  ? 15.837 -3.475  44.007  1.00 83.83  ? 32  ILE A CD1 1 
ATOM   238  N N   . LYS A 1 33  ? 11.640 -7.207  44.296  1.00 96.43  ? 33  LYS A N   1 
ATOM   239  C CA  . LYS A 1 33  ? 11.148 -8.503  44.744  1.00 108.78 ? 33  LYS A CA  1 
ATOM   240  C C   . LYS A 1 33  ? 10.227 -9.144  43.712  1.00 114.91 ? 33  LYS A C   1 
ATOM   241  O O   . LYS A 1 33  ? 10.438 -10.295 43.312  1.00 122.74 ? 33  LYS A O   1 
ATOM   242  C CB  . LYS A 1 33  ? 10.430 -8.353  46.086  1.00 112.00 ? 33  LYS A CB  1 
ATOM   243  C CG  . LYS A 1 33  ? 9.860  -9.658  46.615  1.00 118.61 ? 33  LYS A CG  1 
ATOM   244  C CD  . LYS A 1 33  ? 10.975 -10.575 47.105  1.00 127.08 ? 33  LYS A CD  1 
ATOM   245  C CE  . LYS A 1 33  ? 10.426 -11.818 47.786  1.00 130.95 ? 33  LYS A CE  1 
ATOM   246  N NZ  . LYS A 1 33  ? 9.814  -12.754 46.800  1.00 132.19 ? 33  LYS A NZ  1 
ATOM   247  N N   . GLN A 1 34  ? 9.199  -8.413  43.263  1.00 124.16 ? 34  GLN A N   1 
ATOM   248  C CA  . GLN A 1 34  ? 8.199  -9.007  42.373  1.00 127.49 ? 34  GLN A CA  1 
ATOM   249  C C   . GLN A 1 34  ? 8.818  -9.569  41.099  1.00 131.68 ? 34  GLN A C   1 
ATOM   250  O O   . GLN A 1 34  ? 8.417  -10.641 40.630  1.00 139.80 ? 34  GLN A O   1 
ATOM   251  C CB  . GLN A 1 34  ? 7.115  -7.988  42.011  1.00 121.84 ? 34  GLN A CB  1 
ATOM   252  C CG  . GLN A 1 34  ? 6.165  -7.618  43.139  1.00 126.75 ? 34  GLN A CG  1 
ATOM   253  C CD  . GLN A 1 34  ? 4.876  -6.991  42.628  1.00 127.36 ? 34  GLN A CD  1 
ATOM   254  O OE1 . GLN A 1 34  ? 4.677  -6.849  41.422  1.00 121.21 ? 34  GLN A OE1 1 
ATOM   255  N NE2 . GLN A 1 34  ? 3.993  -6.616  43.547  1.00 130.37 ? 34  GLN A NE2 1 
ATOM   256  N N   . VAL A 1 35  ? 9.803  -8.875  40.531  1.00 125.05 ? 35  VAL A N   1 
ATOM   257  C CA  . VAL A 1 35  ? 10.345 -9.301  39.245  1.00 126.69 ? 35  VAL A CA  1 
ATOM   258  C C   . VAL A 1 35  ? 11.214 -10.538 39.405  1.00 132.12 ? 35  VAL A C   1 
ATOM   259  O O   . VAL A 1 35  ? 11.145 -11.470 38.593  1.00 133.93 ? 35  VAL A O   1 
ATOM   260  C CB  . VAL A 1 35  ? 11.121 -8.145  38.591  1.00 119.54 ? 35  VAL A CB  1 
ATOM   261  C CG1 . VAL A 1 35  ? 11.988 -8.659  37.456  1.00 113.70 ? 35  VAL A CG1 1 
ATOM   262  C CG2 . VAL A 1 35  ? 10.153 -7.093  38.084  1.00 111.18 ? 35  VAL A CG2 1 
ATOM   263  N N   . LYS A 1 36  ? 12.036 -10.575 40.454  1.00 125.31 ? 36  LYS A N   1 
ATOM   264  C CA  . LYS A 1 36  ? 12.957 -11.693 40.625  1.00 129.78 ? 36  LYS A CA  1 
ATOM   265  C C   . LYS A 1 36  ? 12.215 -13.021 40.750  1.00 129.79 ? 36  LYS A C   1 
ATOM   266  O O   . LYS A 1 36  ? 12.725 -14.057 40.308  1.00 129.82 ? 36  LYS A O   1 
ATOM   267  C CB  . LYS A 1 36  ? 13.868 -11.442 41.826  1.00 131.32 ? 36  LYS A CB  1 
ATOM   268  C CG  . LYS A 1 36  ? 15.161 -12.234 41.757  1.00 133.68 ? 36  LYS A CG  1 
ATOM   269  C CD  . LYS A 1 36  ? 16.114 -11.874 42.880  1.00 134.13 ? 36  LYS A CD  1 
ATOM   270  C CE  . LYS A 1 36  ? 17.509 -12.389 42.569  1.00 136.25 ? 36  LYS A CE  1 
ATOM   271  N NZ  . LYS A 1 36  ? 17.523 -13.861 42.353  1.00 141.24 ? 36  LYS A NZ  1 
ATOM   272  N N   . GLU A 1 37  ? 11.014 -13.016 41.336  1.00 127.70 ? 37  GLU A N   1 
ATOM   273  C CA  . GLU A 1 37  ? 10.281 -14.263 41.524  1.00 131.00 ? 37  GLU A CA  1 
ATOM   274  C C   . GLU A 1 37  ? 9.489  -14.667 40.289  1.00 130.09 ? 37  GLU A C   1 
ATOM   275  O O   . GLU A 1 37  ? 9.146  -15.846 40.148  1.00 130.45 ? 37  GLU A O   1 
ATOM   276  C CB  . GLU A 1 37  ? 9.317  -14.153 42.706  1.00 135.80 ? 37  GLU A CB  1 
ATOM   277  C CG  . GLU A 1 37  ? 7.903  -13.755 42.298  1.00 138.37 ? 37  GLU A CG  1 
ATOM   278  C CD  . GLU A 1 37  ? 6.965  -13.604 43.477  1.00 142.98 ? 37  GLU A CD  1 
ATOM   279  O OE1 . GLU A 1 37  ? 7.412  -13.825 44.622  1.00 140.24 ? 37  GLU A OE1 1 
ATOM   280  O OE2 . GLU A 1 37  ? 5.777  -13.281 43.254  1.00 144.83 ? 37  GLU A OE2 1 
ATOM   281  N N   . ALA A 1 38  ? 9.170  -13.716 39.408  1.00 134.41 ? 38  ALA A N   1 
ATOM   282  C CA  . ALA A 1 38  ? 8.530  -14.045 38.143  1.00 127.18 ? 38  ALA A CA  1 
ATOM   283  C C   . ALA A 1 38  ? 9.537  -14.463 37.086  1.00 124.07 ? 38  ALA A C   1 
ATOM   284  O O   . ALA A 1 38  ? 9.156  -15.112 36.107  1.00 123.00 ? 38  ALA A O   1 
ATOM   285  C CB  . ALA A 1 38  ? 7.711  -12.864 37.632  1.00 116.82 ? 38  ALA A CB  1 
ATOM   286  N N   . SER A 1 39  ? 10.806 -14.103 37.261  1.00 123.44 ? 39  SER A N   1 
ATOM   287  C CA  . SER A 1 39  ? 11.880 -14.594 36.413  1.00 121.57 ? 39  SER A CA  1 
ATOM   288  C C   . SER A 1 39  ? 12.525 -15.839 36.990  1.00 130.28 ? 39  SER A C   1 
ATOM   289  O O   . SER A 1 39  ? 13.580 -16.261 36.500  1.00 127.73 ? 39  SER A O   1 
ATOM   290  C CB  . SER A 1 39  ? 12.943 -13.514 36.218  1.00 120.65 ? 39  SER A CB  1 
ATOM   291  O OG  . SER A 1 39  ? 13.642 -13.269 37.426  1.00 124.85 ? 39  SER A OG  1 
ATOM   292  N N   . ASN A 1 40  ? 11.908 -16.428 38.016  1.00 132.27 ? 40  ASN A N   1 
ATOM   293  C CA  . ASN A 1 40  ? 12.439 -17.591 38.719  1.00 128.13 ? 40  ASN A CA  1 
ATOM   294  C C   . ASN A 1 40  ? 13.892 -17.355 39.118  1.00 132.38 ? 40  ASN A C   1 
ATOM   295  O O   . ASN A 1 40  ? 14.767 -18.203 38.931  1.00 131.90 ? 40  ASN A O   1 
ATOM   296  C CB  . ASN A 1 40  ? 12.283 -18.854 37.871  1.00 128.59 ? 40  ASN A CB  1 
ATOM   297  C CG  . ASN A 1 40  ? 10.837 -19.111 37.474  1.00 126.39 ? 40  ASN A CG  1 
ATOM   298  O OD1 . ASN A 1 40  ? 10.536 -19.411 36.317  1.00 116.34 ? 40  ASN A OD1 1 
ATOM   299  N ND2 . ASN A 1 40  ? 9.934  -18.985 38.438  1.00 132.33 ? 40  ASN A ND2 1 
ATOM   300  N N   . GLY A 1 41  ? 14.142 -16.164 39.664  1.00 151.88 ? 41  GLY A N   1 
ATOM   301  C CA  . GLY A 1 41  ? 15.445 -15.790 40.168  1.00 146.99 ? 41  GLY A CA  1 
ATOM   302  C C   . GLY A 1 41  ? 16.432 -15.272 39.145  1.00 143.60 ? 41  GLY A C   1 
ATOM   303  O O   . GLY A 1 41  ? 17.478 -14.747 39.541  1.00 139.88 ? 41  GLY A O   1 
ATOM   304  N N   . GLU A 1 42  ? 16.136 -15.371 37.845  1.00 131.22 ? 42  GLU A N   1 
ATOM   305  C CA  . GLU A 1 42  ? 17.155 -15.081 36.841  1.00 123.43 ? 42  GLU A CA  1 
ATOM   306  C C   . GLU A 1 42  ? 17.535 -13.605 36.810  1.00 126.84 ? 42  GLU A C   1 
ATOM   307  O O   . GLU A 1 42  ? 18.717 -13.273 36.661  1.00 130.89 ? 42  GLU A O   1 
ATOM   308  C CB  . GLU A 1 42  ? 16.697 -15.517 35.448  1.00 122.63 ? 42  GLU A CB  1 
ATOM   309  C CG  . GLU A 1 42  ? 16.617 -17.015 35.208  1.00 117.02 ? 42  GLU A CG  1 
ATOM   310  C CD  . GLU A 1 42  ? 16.179 -17.344 33.784  1.00 118.67 ? 42  GLU A CD  1 
ATOM   311  O OE1 . GLU A 1 42  ? 15.894 -16.403 33.012  1.00 117.65 ? 42  GLU A OE1 1 
ATOM   312  O OE2 . GLU A 1 42  ? 16.127 -18.541 33.430  1.00 116.74 ? 42  GLU A OE2 1 
ATOM   313  N N   . MET A 1 43  ? 16.566 -12.706 36.960  1.00 122.08 ? 43  MET A N   1 
ATOM   314  C CA  . MET A 1 43  ? 16.778 -11.290 36.680  1.00 125.65 ? 43  MET A CA  1 
ATOM   315  C C   . MET A 1 43  ? 16.917 -10.486 37.964  1.00 128.05 ? 43  MET A C   1 
ATOM   316  O O   . MET A 1 43  ? 16.069 -10.574 38.856  1.00 127.06 ? 43  MET A O   1 
ATOM   317  C CB  . MET A 1 43  ? 15.646 -10.715 35.831  1.00 121.45 ? 43  MET A CB  1 
ATOM   318  C CG  . MET A 1 43  ? 15.979 -9.340  35.276  1.00 117.56 ? 43  MET A CG  1 
ATOM   319  S SD  . MET A 1 43  ? 14.845 -8.786  33.996  1.00 97.13  ? 43  MET A SD  1 
ATOM   320  C CE  . MET A 1 43  ? 15.607 -7.230  33.543  1.00 93.91  ? 43  MET A CE  1 
ATOM   321  N N   . GLU A 1 44  ? 17.977 -9.680  38.027  1.00 144.95 ? 44  GLU A N   1 
ATOM   322  C CA  . GLU A 1 44  ? 18.396 -8.965  39.231  1.00 148.07 ? 44  GLU A CA  1 
ATOM   323  C C   . GLU A 1 44  ? 18.564 -7.480  38.920  1.00 141.14 ? 44  GLU A C   1 
ATOM   324  O O   . GLU A 1 44  ? 19.556 -7.076  38.307  1.00 144.53 ? 44  GLU A O   1 
ATOM   325  C CB  . GLU A 1 44  ? 19.701 -9.564  39.744  1.00 153.95 ? 44  GLU A CB  1 
ATOM   326  C CG  . GLU A 1 44  ? 20.329 -8.874  40.933  1.00 153.90 ? 44  GLU A CG  1 
ATOM   327  C CD  . GLU A 1 44  ? 21.673 -9.482  41.286  1.00 155.84 ? 44  GLU A CD  1 
ATOM   328  O OE1 . GLU A 1 44  ? 21.934 -10.627 40.859  1.00 160.06 ? 44  GLU A OE1 1 
ATOM   329  O OE2 . GLU A 1 44  ? 22.474 -8.813  41.970  1.00 154.37 ? 44  GLU A OE2 1 
ATOM   330  N N   . LEU A 1 45  ? 17.602 -6.666  39.348  1.00 119.97 ? 45  LEU A N   1 
ATOM   331  C CA  . LEU A 1 45  ? 17.593 -5.248  39.021  1.00 110.83 ? 45  LEU A CA  1 
ATOM   332  C C   . LEU A 1 45  ? 18.395 -4.485  40.062  1.00 108.20 ? 45  LEU A C   1 
ATOM   333  O O   . LEU A 1 45  ? 18.441 -4.868  41.231  1.00 108.57 ? 45  LEU A O   1 
ATOM   334  C CB  . LEU A 1 45  ? 16.163 -4.712  38.981  1.00 101.31 ? 45  LEU A CB  1 
ATOM   335  C CG  . LEU A 1 45  ? 15.195 -5.533  38.135  1.00 101.88 ? 45  LEU A CG  1 
ATOM   336  C CD1 . LEU A 1 45  ? 13.765 -5.049  38.307  1.00 92.53  ? 45  LEU A CD1 1 
ATOM   337  C CD2 . LEU A 1 45  ? 15.617 -5.451  36.694  1.00 99.73  ? 45  LEU A CD2 1 
ATOM   338  N N   . ASN A 1 46  ? 18.999 -3.379  39.645  1.00 110.63 ? 46  ASN A N   1 
ATOM   339  C CA  . ASN A 1 46  ? 19.841 -2.596  40.541  1.00 110.88 ? 46  ASN A CA  1 
ATOM   340  C C   . ASN A 1 46  ? 19.069 -1.429  41.133  1.00 108.61 ? 46  ASN A C   1 
ATOM   341  O O   . ASN A 1 46  ? 18.360 -0.716  40.416  1.00 104.22 ? 46  ASN A O   1 
ATOM   342  C CB  . ASN A 1 46  ? 21.075 -2.056  39.834  1.00 110.81 ? 46  ASN A CB  1 
ATOM   343  C CG  . ASN A 1 46  ? 21.900 -1.184  40.747  1.00 115.65 ? 46  ASN A CG  1 
ATOM   344  O OD1 . ASN A 1 46  ? 22.021 0.020   40.530  1.00 119.54 ? 46  ASN A OD1 1 
ATOM   345  N ND2 . ASN A 1 46  ? 22.436 -1.778  41.805  1.00 119.34 ? 46  ASN A ND2 1 
ATOM   346  N N   . GLU A 1 47  ? 19.213 -1.242  42.445  1.00 113.61 ? 47  GLU A N   1 
ATOM   347  C CA  . GLU A 1 47  ? 18.541 -0.149  43.138  1.00 108.32 ? 47  GLU A CA  1 
ATOM   348  C C   . GLU A 1 47  ? 18.877 1.191   42.510  1.00 109.82 ? 47  GLU A C   1 
ATOM   349  O O   . GLU A 1 47  ? 17.997 1.915   42.032  1.00 109.66 ? 47  GLU A O   1 
ATOM   350  C CB  . GLU A 1 47  ? 18.941 -0.150  44.608  1.00 116.45 ? 47  GLU A CB  1 
ATOM   351  C CG  . GLU A 1 47  ? 17.839 0.195   45.551  1.00 119.55 ? 47  GLU A CG  1 
ATOM   352  C CD  . GLU A 1 47  ? 18.331 0.248   46.986  1.00 120.92 ? 47  GLU A CD  1 
ATOM   353  O OE1 . GLU A 1 47  ? 19.432 -0.267  47.223  1.00 123.14 ? 47  GLU A OE1 1 
ATOM   354  O OE2 . GLU A 1 47  ? 17.575 0.687   47.901  1.00 119.35 ? 47  GLU A OE2 1 
ATOM   355  N N   . ALA A 1 48  ? 20.170 1.514   42.485  1.00 111.65 ? 48  ALA A N   1 
ATOM   356  C CA  . ALA A 1 48  ? 20.624 2.817   42.013  1.00 110.69 ? 48  ALA A CA  1 
ATOM   357  C C   . ALA A 1 48  ? 20.178 3.089   40.586  1.00 102.01 ? 48  ALA A C   1 
ATOM   358  O O   . ALA A 1 48  ? 19.960 4.247   40.207  1.00 95.44  ? 48  ALA A O   1 
ATOM   359  C CB  . ALA A 1 48  ? 22.144 2.906   42.130  1.00 113.22 ? 48  ALA A CB  1 
ATOM   360  N N   . THR A 1 49  ? 20.045 2.042   39.776  1.00 98.03  ? 49  THR A N   1 
ATOM   361  C CA  . THR A 1 49  ? 19.513 2.233   38.437  1.00 96.83  ? 49  THR A CA  1 
ATOM   362  C C   . THR A 1 49  ? 18.053 2.655   38.509  1.00 87.46  ? 49  THR A C   1 
ATOM   363  O O   . THR A 1 49  ? 17.671 3.702   37.976  1.00 83.30  ? 49  THR A O   1 
ATOM   364  C CB  . THR A 1 49  ? 19.687 0.958   37.608  1.00 99.49  ? 49  THR A CB  1 
ATOM   365  O OG1 . THR A 1 49  ? 20.994 0.416   37.835  1.00 101.15 ? 49  THR A OG1 1 
ATOM   366  C CG2 . THR A 1 49  ? 19.526 1.259   36.116  1.00 88.62  ? 49  THR A CG2 1 
ATOM   367  N N   . LEU A 1 50  ? 17.234 1.873   39.222  1.00 88.00  ? 50  LEU A N   1 
ATOM   368  C CA  . LEU A 1 50  ? 15.822 2.202   39.384  1.00 83.16  ? 50  LEU A CA  1 
ATOM   369  C C   . LEU A 1 50  ? 15.646 3.628   39.874  1.00 80.97  ? 50  LEU A C   1 
ATOM   370  O O   . LEU A 1 50  ? 14.725 4.331   39.445  1.00 77.71  ? 50  LEU A O   1 
ATOM   371  C CB  . LEU A 1 50  ? 15.160 1.221   40.354  1.00 85.81  ? 50  LEU A CB  1 
ATOM   372  C CG  . LEU A 1 50  ? 14.285 0.123   39.737  1.00 82.83  ? 50  LEU A CG  1 
ATOM   373  C CD1 . LEU A 1 50  ? 15.070 -0.741  38.760  1.00 85.52  ? 50  LEU A CD1 1 
ATOM   374  C CD2 . LEU A 1 50  ? 13.650 -0.736  40.820  1.00 82.18  ? 50  LEU A CD2 1 
ATOM   375  N N   . TYR A 1 51  ? 16.502 4.064   40.796  1.00 82.88  ? 51  TYR A N   1 
ATOM   376  C CA  . TYR A 1 51  ? 16.420 5.441   41.260  1.00 82.06  ? 51  TYR A CA  1 
ATOM   377  C C   . TYR A 1 51  ? 16.631 6.403   40.110  1.00 79.34  ? 51  TYR A C   1 
ATOM   378  O O   . TYR A 1 51  ? 15.845 7.333   39.901  1.00 75.11  ? 51  TYR A O   1 
ATOM   379  C CB  . TYR A 1 51  ? 17.453 5.700   42.349  1.00 89.68  ? 51  TYR A CB  1 
ATOM   380  C CG  . TYR A 1 51  ? 17.246 4.907   43.601  1.00 93.76  ? 51  TYR A CG  1 
ATOM   381  C CD1 . TYR A 1 51  ? 16.052 5.008   44.315  1.00 92.23  ? 51  TYR A CD1 1 
ATOM   382  C CD2 . TYR A 1 51  ? 18.255 4.104   44.113  1.00 99.77  ? 51  TYR A CD2 1 
ATOM   383  C CE1 . TYR A 1 51  ? 15.861 4.289   45.488  1.00 90.43  ? 51  TYR A CE1 1 
ATOM   384  C CE2 . TYR A 1 51  ? 18.072 3.409   45.272  1.00 106.65 ? 51  TYR A CE2 1 
ATOM   385  C CZ  . TYR A 1 51  ? 16.886 3.495   45.959  1.00 98.62  ? 51  TYR A CZ  1 
ATOM   386  O OH  . TYR A 1 51  ? 16.748 2.765   47.117  1.00 99.16  ? 51  TYR A OH  1 
ATOM   387  N N   . THR A 1 52  ? 17.666 6.157   39.319  1.00 77.39  ? 52  THR A N   1 
ATOM   388  C CA  . THR A 1 52  ? 17.920 6.991   38.159  1.00 76.11  ? 52  THR A CA  1 
ATOM   389  C C   . THR A 1 52  ? 16.799 6.879   37.129  1.00 76.24  ? 52  THR A C   1 
ATOM   390  O O   . THR A 1 52  ? 16.330 7.892   36.595  1.00 73.55  ? 52  THR A O   1 
ATOM   391  C CB  . THR A 1 52  ? 19.262 6.595   37.570  1.00 80.05  ? 52  THR A CB  1 
ATOM   392  O OG1 . THR A 1 52  ? 20.261 6.760   38.583  1.00 83.39  ? 52  THR A OG1 1 
ATOM   393  C CG2 . THR A 1 52  ? 19.585 7.470   36.403  1.00 80.14  ? 52  THR A CG2 1 
ATOM   394  N N   . ILE A 1 53  ? 16.320 5.660   36.872  1.00 76.76  ? 53  ILE A N   1 
ATOM   395  C CA  . ILE A 1 53  ? 15.345 5.474   35.803  1.00 72.63  ? 53  ILE A CA  1 
ATOM   396  C C   . ILE A 1 53  ? 13.992 6.065   36.171  1.00 72.08  ? 53  ILE A C   1 
ATOM   397  O O   . ILE A 1 53  ? 13.254 6.532   35.296  1.00 66.37  ? 53  ILE A O   1 
ATOM   398  C CB  . ILE A 1 53  ? 15.218 3.986   35.447  1.00 69.67  ? 53  ILE A CB  1 
ATOM   399  C CG1 . ILE A 1 53  ? 16.592 3.402   35.123  1.00 78.27  ? 53  ILE A CG1 1 
ATOM   400  C CG2 . ILE A 1 53  ? 14.294 3.820   34.275  1.00 59.33  ? 53  ILE A CG2 1 
ATOM   401  C CD1 . ILE A 1 53  ? 17.375 4.217   34.123  1.00 82.03  ? 53  ILE A CD1 1 
ATOM   402  N N   . PHE A 1 54  ? 13.639 6.067   37.456  1.00 73.45  ? 54  PHE A N   1 
ATOM   403  C CA  . PHE A 1 54  ? 12.326 6.570   37.847  1.00 72.39  ? 54  PHE A CA  1 
ATOM   404  C C   . PHE A 1 54  ? 12.249 8.090   37.773  1.00 73.90  ? 54  PHE A C   1 
ATOM   405  O O   . PHE A 1 54  ? 11.158 8.646   37.594  1.00 70.92  ? 54  PHE A O   1 
ATOM   406  C CB  . PHE A 1 54  ? 11.963 6.072   39.243  1.00 70.81  ? 54  PHE A CB  1 
ATOM   407  C CG  . PHE A 1 54  ? 11.418 4.673   39.256  1.00 68.42  ? 54  PHE A CG  1 
ATOM   408  C CD1 . PHE A 1 54  ? 11.349 3.934   38.087  1.00 68.12  ? 54  PHE A CD1 1 
ATOM   409  C CD2 . PHE A 1 54  ? 10.928 4.117   40.418  1.00 71.79  ? 54  PHE A CD2 1 
ATOM   410  C CE1 . PHE A 1 54  ? 10.842 2.658   38.086  1.00 63.68  ? 54  PHE A CE1 1 
ATOM   411  C CE2 . PHE A 1 54  ? 10.411 2.841   40.419  1.00 73.82  ? 54  PHE A CE2 1 
ATOM   412  C CZ  . PHE A 1 54  ? 10.370 2.111   39.248  1.00 64.73  ? 54  PHE A CZ  1 
ATOM   413  N N   . LYS A 1 55  ? 13.378 8.776   37.949  1.00 83.10  ? 55  LYS A N   1 
ATOM   414  C CA  . LYS A 1 55  ? 13.408 10.222  37.750  1.00 80.95  ? 55  LYS A CA  1 
ATOM   415  C C   . LYS A 1 55  ? 12.987 10.593  36.331  1.00 76.11  ? 55  LYS A C   1 
ATOM   416  O O   . LYS A 1 55  ? 12.143 11.473  36.133  1.00 76.10  ? 55  LYS A O   1 
ATOM   417  C CB  . LYS A 1 55  ? 14.809 10.761  38.051  1.00 81.04  ? 55  LYS A CB  1 
ATOM   418  C CG  . LYS A 1 55  ? 15.032 11.218  39.484  1.00 85.85  ? 55  LYS A CG  1 
ATOM   419  C CD  . LYS A 1 55  ? 16.463 11.717  39.670  1.00 92.56  ? 55  LYS A CD  1 
ATOM   420  C CE  . LYS A 1 55  ? 16.619 12.513  40.954  1.00 105.36 ? 55  LYS A CE  1 
ATOM   421  N NZ  . LYS A 1 55  ? 15.768 13.736  40.951  1.00 109.98 ? 55  LYS A NZ  1 
ATOM   422  N N   . ARG A 1 56  ? 13.548 9.906   35.333  1.00 70.04  ? 56  ARG A N   1 
ATOM   423  C CA  . ARG A 1 56  ? 13.252 10.228  33.940  1.00 73.63  ? 56  ARG A CA  1 
ATOM   424  C C   . ARG A 1 56  ? 11.766 10.089  33.649  1.00 74.04  ? 56  ARG A C   1 
ATOM   425  O O   . ARG A 1 56  ? 11.158 10.968  33.028  1.00 71.85  ? 56  ARG A O   1 
ATOM   426  C CB  . ARG A 1 56  ? 14.071 9.323   33.014  1.00 72.85  ? 56  ARG A CB  1 
ATOM   427  C CG  . ARG A 1 56  ? 13.784 9.504   31.532  1.00 76.35  ? 56  ARG A CG  1 
ATOM   428  C CD  . ARG A 1 56  ? 13.970 10.954  31.093  1.00 82.16  ? 56  ARG A CD  1 
ATOM   429  N NE  . ARG A 1 56  ? 13.284 11.252  29.838  1.00 81.87  ? 56  ARG A NE  1 
ATOM   430  C CZ  . ARG A 1 56  ? 13.811 11.080  28.631  1.00 87.92  ? 56  ARG A CZ  1 
ATOM   431  N NH1 . ARG A 1 56  ? 15.042 10.619  28.471  1.00 84.88  ? 56  ARG A NH1 1 
ATOM   432  N NH2 . ARG A 1 56  ? 13.086 11.382  27.555  1.00 85.33  ? 56  ARG A NH2 1 
ATOM   433  N N   . LEU A 1 57  ? 11.164 8.990   34.101  1.00 73.27  ? 57  LEU A N   1 
ATOM   434  C CA  . LEU A 1 57  ? 9.754  8.746   33.822  1.00 73.67  ? 57  LEU A CA  1 
ATOM   435  C C   . LEU A 1 57  ? 8.859  9.783   34.488  1.00 76.03  ? 57  LEU A C   1 
ATOM   436  O O   . LEU A 1 57  ? 7.821  10.160  33.932  1.00 74.87  ? 57  LEU A O   1 
ATOM   437  C CB  . LEU A 1 57  ? 9.371  7.341   34.267  1.00 65.71  ? 57  LEU A CB  1 
ATOM   438  C CG  . LEU A 1 57  ? 10.083 6.274   33.450  1.00 58.53  ? 57  LEU A CG  1 
ATOM   439  C CD1 . LEU A 1 57  ? 10.015 4.953   34.181  1.00 52.12  ? 57  LEU A CD1 1 
ATOM   440  C CD2 . LEU A 1 57  ? 9.496  6.167   32.057  1.00 52.09  ? 57  LEU A CD2 1 
ATOM   441  N N   . GLU A 1 58  ? 9.220  10.228  35.695  1.00 72.54  ? 58  GLU A N   1 
ATOM   442  C CA  . GLU A 1 58  ? 8.414  11.251  36.354  1.00 73.30  ? 58  GLU A CA  1 
ATOM   443  C C   . GLU A 1 58  ? 8.589  12.615  35.701  1.00 77.50  ? 58  GLU A C   1 
ATOM   444  O O   . GLU A 1 58  ? 7.650  13.419  35.686  1.00 76.67  ? 58  GLU A O   1 
ATOM   445  C CB  . GLU A 1 58  ? 8.767  11.338  37.832  1.00 79.03  ? 58  GLU A CB  1 
ATOM   446  C CG  . GLU A 1 58  ? 7.652  11.944  38.665  1.00 82.25  ? 58  GLU A CG  1 
ATOM   447  C CD  . GLU A 1 58  ? 7.966  11.953  40.145  1.00 81.34  ? 58  GLU A CD  1 
ATOM   448  O OE1 . GLU A 1 58  ? 8.822  11.153  40.581  1.00 74.32  ? 58  GLU A OE1 1 
ATOM   449  O OE2 . GLU A 1 58  ? 7.347  12.759  40.870  1.00 87.91  ? 58  GLU A OE2 1 
ATOM   450  N N   . LYS A 1 59  ? 9.778  12.896  35.167  1.00 82.68  ? 59  LYS A N   1 
ATOM   451  C CA  . LYS A 1 59  ? 9.985  14.140  34.438  1.00 86.52  ? 59  LYS A CA  1 
ATOM   452  C C   . LYS A 1 59  ? 9.088  14.207  33.212  1.00 84.30  ? 59  LYS A C   1 
ATOM   453  O O   . LYS A 1 59  ? 8.599  15.281  32.848  1.00 88.72  ? 59  LYS A O   1 
ATOM   454  C CB  . LYS A 1 59  ? 11.450 14.269  34.026  1.00 88.26  ? 59  LYS A CB  1 
ATOM   455  C CG  . LYS A 1 59  ? 11.891 15.693  33.775  1.00 100.28 ? 59  LYS A CG  1 
ATOM   456  C CD  . LYS A 1 59  ? 13.044 15.749  32.796  1.00 102.01 ? 59  LYS A CD  1 
ATOM   457  C CE  . LYS A 1 59  ? 14.279 15.079  33.365  1.00 101.75 ? 59  LYS A CE  1 
ATOM   458  N NZ  . LYS A 1 59  ? 15.465 15.320  32.501  1.00 114.30 ? 59  LYS A NZ  1 
ATOM   459  N N   . ASP A 1 60  ? 8.869  13.072  32.560  1.00 74.60  ? 60  ASP A N   1 
ATOM   460  C CA  . ASP A 1 60  ? 8.075  13.003  31.347  1.00 71.85  ? 60  ASP A CA  1 
ATOM   461  C C   . ASP A 1 60  ? 6.594  12.761  31.616  1.00 72.60  ? 60  ASP A C   1 
ATOM   462  O O   . ASP A 1 60  ? 5.847  12.473  30.679  1.00 70.87  ? 60  ASP A O   1 
ATOM   463  C CB  . ASP A 1 60  ? 8.637  11.914  30.440  1.00 78.14  ? 60  ASP A CB  1 
ATOM   464  C CG  . ASP A 1 60  ? 10.143 12.024  30.281  1.00 87.19  ? 60  ASP A CG  1 
ATOM   465  O OD1 . ASP A 1 60  ? 10.704 13.064  30.700  1.00 90.24  ? 60  ASP A OD1 1 
ATOM   466  O OD2 . ASP A 1 60  ? 10.766 11.080  29.742  1.00 87.22  ? 60  ASP A OD2 1 
ATOM   467  N N   . GLY A 1 61  ? 6.151  12.874  32.864  1.00 72.43  ? 61  GLY A N   1 
ATOM   468  C CA  . GLY A 1 61  ? 4.746  12.687  33.162  1.00 68.85  ? 61  GLY A CA  1 
ATOM   469  C C   . GLY A 1 61  ? 4.234  11.278  32.981  1.00 73.72  ? 61  GLY A C   1 
ATOM   470  O O   . GLY A 1 61  ? 3.026  11.086  32.815  1.00 75.19  ? 61  GLY A O   1 
ATOM   471  N N   . ILE A 1 62  ? 5.119  10.283  33.001  1.00 75.06  ? 62  ILE A N   1 
ATOM   472  C CA  . ILE A 1 62  ? 4.699  8.901   32.798  1.00 73.04  ? 62  ILE A CA  1 
ATOM   473  C C   . ILE A 1 62  ? 4.315  8.223   34.113  1.00 73.14  ? 62  ILE A C   1 
ATOM   474  O O   . ILE A 1 62  ? 3.389  7.405   34.136  1.00 71.86  ? 62  ILE A O   1 
ATOM   475  C CB  . ILE A 1 62  ? 5.799  8.110   32.061  1.00 70.26  ? 62  ILE A CB  1 
ATOM   476  C CG1 . ILE A 1 62  ? 6.029  8.674   30.653  1.00 67.79  ? 62  ILE A CG1 1 
ATOM   477  C CG2 . ILE A 1 62  ? 5.446  6.637   31.969  1.00 66.70  ? 62  ILE A CG2 1 
ATOM   478  C CD1 . ILE A 1 62  ? 4.815  8.599   29.744  1.00 71.03  ? 62  ILE A CD1 1 
ATOM   479  N N   . ILE A 1 63  ? 4.988  8.555   35.223  1.00 78.44  ? 63  ILE A N   1 
ATOM   480  C CA  . ILE A 1 63  ? 4.654  7.986   36.524  1.00 75.74  ? 63  ILE A CA  1 
ATOM   481  C C   . ILE A 1 63  ? 4.655  9.083   37.580  1.00 78.79  ? 63  ILE A C   1 
ATOM   482  O O   . ILE A 1 63  ? 5.230  10.159  37.396  1.00 73.93  ? 63  ILE A O   1 
ATOM   483  C CB  . ILE A 1 63  ? 5.624  6.872   36.968  1.00 71.28  ? 63  ILE A CB  1 
ATOM   484  C CG1 . ILE A 1 63  ? 7.020  7.444   37.183  1.00 71.77  ? 63  ILE A CG1 1 
ATOM   485  C CG2 . ILE A 1 63  ? 5.674  5.765   35.936  1.00 71.79  ? 63  ILE A CG2 1 
ATOM   486  C CD1 . ILE A 1 63  ? 7.946  6.508   37.939  1.00 69.33  ? 63  ILE A CD1 1 
ATOM   487  N N   . SER A 1 64  ? 4.007  8.779   38.707  1.00 84.51  ? 64  SER A N   1 
ATOM   488  C CA  . SER A 1 64  ? 3.988  9.636   39.887  1.00 82.62  ? 64  SER A CA  1 
ATOM   489  C C   . SER A 1 64  ? 3.936  8.754   41.135  1.00 87.43  ? 64  SER A C   1 
ATOM   490  O O   . SER A 1 64  ? 3.732  7.538   41.050  1.00 84.97  ? 64  SER A O   1 
ATOM   491  C CB  . SER A 1 64  ? 2.813  10.616  39.840  1.00 81.22  ? 64  SER A CB  1 
ATOM   492  O OG  . SER A 1 64  ? 1.642  10.016  40.358  1.00 80.06  ? 64  SER A OG  1 
ATOM   493  N N   . SER A 1 65  ? 4.125  9.380   42.305  1.00 89.60  ? 65  SER A N   1 
ATOM   494  C CA  . SER A 1 65  ? 4.275  8.668   43.574  1.00 81.46  ? 65  SER A CA  1 
ATOM   495  C C   . SER A 1 65  ? 3.353  9.235   44.651  1.00 79.71  ? 65  SER A C   1 
ATOM   496  O O   . SER A 1 65  ? 2.857  10.359  44.555  1.00 78.37  ? 65  SER A O   1 
ATOM   497  C CB  . SER A 1 65  ? 5.726  8.722   44.086  1.00 79.49  ? 65  SER A CB  1 
ATOM   498  O OG  . SER A 1 65  ? 6.179  10.056  44.238  1.00 82.28  ? 65  SER A OG  1 
ATOM   499  N N   . TYR A 1 66  ? 3.147  8.440   45.698  1.00 81.12  ? 66  TYR A N   1 
ATOM   500  C CA  . TYR A 1 66  ? 2.363  8.854   46.855  1.00 79.17  ? 66  TYR A CA  1 
ATOM   501  C C   . TYR A 1 66  ? 2.783  7.997   48.042  1.00 82.71  ? 66  TYR A C   1 
ATOM   502  O O   . TYR A 1 66  ? 3.474  6.987   47.892  1.00 79.67  ? 66  TYR A O   1 
ATOM   503  C CB  . TYR A 1 66  ? 0.861  8.724   46.609  1.00 74.69  ? 66  TYR A CB  1 
ATOM   504  C CG  . TYR A 1 66  ? 0.393  7.294   46.471  1.00 77.40  ? 66  TYR A CG  1 
ATOM   505  C CD1 . TYR A 1 66  ? 0.031  6.553   47.584  1.00 79.17  ? 66  TYR A CD1 1 
ATOM   506  C CD2 . TYR A 1 66  ? 0.314  6.685   45.230  1.00 79.64  ? 66  TYR A CD2 1 
ATOM   507  C CE1 . TYR A 1 66  ? -0.392 5.249   47.469  1.00 78.23  ? 66  TYR A CE1 1 
ATOM   508  C CE2 . TYR A 1 66  ? -0.111 5.377   45.104  1.00 79.76  ? 66  TYR A CE2 1 
ATOM   509  C CZ  . TYR A 1 66  ? -0.462 4.664   46.229  1.00 80.38  ? 66  TYR A CZ  1 
ATOM   510  O OH  . TYR A 1 66  ? -0.888 3.359   46.120  1.00 86.79  ? 66  TYR A OH  1 
ATOM   511  N N   . TRP A 1 67  ? 2.349  8.413   49.229  1.00 87.39  ? 67  TRP A N   1 
ATOM   512  C CA  . TRP A 1 67  ? 2.740  7.742   50.460  1.00 83.64  ? 67  TRP A CA  1 
ATOM   513  C C   . TRP A 1 67  ? 1.703  6.711   50.886  1.00 86.77  ? 67  TRP A C   1 
ATOM   514  O O   . TRP A 1 67  ? 0.496  6.976   50.863  1.00 86.55  ? 67  TRP A O   1 
ATOM   515  C CB  . TRP A 1 67  ? 2.967  8.782   51.550  1.00 82.35  ? 67  TRP A CB  1 
ATOM   516  C CG  . TRP A 1 67  ? 4.252  9.472   51.320  1.00 84.75  ? 67  TRP A CG  1 
ATOM   517  C CD1 . TRP A 1 67  ? 4.439  10.681  50.725  1.00 83.94  ? 67  TRP A CD1 1 
ATOM   518  C CD2 . TRP A 1 67  ? 5.554  8.986   51.667  1.00 87.14  ? 67  TRP A CD2 1 
ATOM   519  N NE1 . TRP A 1 67  ? 5.781  10.982  50.677  1.00 84.06  ? 67  TRP A NE1 1 
ATOM   520  C CE2 . TRP A 1 67  ? 6.487  9.958   51.253  1.00 82.55  ? 67  TRP A CE2 1 
ATOM   521  C CE3 . TRP A 1 67  ? 6.023  7.822   52.292  1.00 86.99  ? 67  TRP A CE3 1 
ATOM   522  C CZ2 . TRP A 1 67  ? 7.862  9.805   51.445  1.00 85.36  ? 67  TRP A CZ2 1 
ATOM   523  C CZ3 . TRP A 1 67  ? 7.391  7.668   52.480  1.00 82.22  ? 67  TRP A CZ3 1 
ATOM   524  C CH2 . TRP A 1 67  ? 8.293  8.656   52.059  1.00 83.27  ? 67  TRP A CH2 1 
ATOM   525  N N   . GLY A 1 68  ? 2.192  5.536   51.271  1.00 89.02  ? 68  GLY A N   1 
ATOM   526  C CA  . GLY A 1 68  ? 1.389  4.444   51.780  1.00 91.49  ? 68  GLY A CA  1 
ATOM   527  C C   . GLY A 1 68  ? 1.834  3.975   53.148  1.00 95.23  ? 68  GLY A C   1 
ATOM   528  O O   . GLY A 1 68  ? 2.984  4.197   53.538  1.00 91.99  ? 68  GLY A O   1 
ATOM   529  N N   . ASP A 1 69  ? 0.936  3.346   53.896  1.00 96.45  ? 69  ASP A N   1 
ATOM   530  C CA  . ASP A 1 69  ? 1.280  2.765   55.185  1.00 105.97 ? 69  ASP A CA  1 
ATOM   531  C C   . ASP A 1 69  ? 1.536  1.274   55.008  1.00 103.93 ? 69  ASP A C   1 
ATOM   532  O O   . ASP A 1 69  ? 0.717  0.566   54.415  1.00 105.25 ? 69  ASP A O   1 
ATOM   533  C CB  . ASP A 1 69  ? 0.172  3.002   56.216  1.00 111.42 ? 69  ASP A CB  1 
ATOM   534  C CG  . ASP A 1 69  ? 0.152  4.431   56.739  1.00 109.45 ? 69  ASP A CG  1 
ATOM   535  O OD1 . ASP A 1 69  ? 1.239  5.027   56.909  1.00 101.95 ? 69  ASP A OD1 1 
ATOM   536  O OD2 . ASP A 1 69  ? -0.957 4.955   56.981  1.00 109.64 ? 69  ASP A OD2 1 
ATOM   537  N N   . GLU A 1 70  ? 2.680  0.809   55.502  1.00 111.97 ? 70  GLU A N   1 
ATOM   538  C CA  . GLU A 1 70  ? 3.073  -0.596  55.402  1.00 113.51 ? 70  GLU A CA  1 
ATOM   539  C C   . GLU A 1 70  ? 2.347  -1.435  56.456  1.00 112.81 ? 70  GLU A C   1 
ATOM   540  O O   . GLU A 1 70  ? 2.095  -2.627  56.264  1.00 113.30 ? 70  GLU A O   1 
ATOM   541  C CB  . GLU A 1 70  ? 4.591  -0.737  55.561  1.00 108.08 ? 70  GLU A CB  1 
ATOM   542  C CG  . GLU A 1 70  ? 5.117  -2.159  55.437  1.00 117.28 ? 70  GLU A CG  1 
ATOM   543  C CD  . GLU A 1 70  ? 6.585  -2.273  55.814  1.00 125.06 ? 70  GLU A CD  1 
ATOM   544  O OE1 . GLU A 1 70  ? 7.172  -1.258  56.245  1.00 125.14 ? 70  GLU A OE1 1 
ATOM   545  O OE2 . GLU A 1 70  ? 7.148  -3.381  55.696  1.00 128.79 ? 70  GLU A OE2 1 
ATOM   546  N N   . GLY A 1 73  ? 3.460  -2.848  60.358  1.00 85.29  ? 73  GLY A N   1 
ATOM   547  C CA  . GLY A 1 73  ? 3.282  -1.440  60.043  1.00 90.11  ? 73  GLY A CA  1 
ATOM   548  C C   . GLY A 1 73  ? 4.535  -0.735  59.548  1.00 87.47  ? 73  GLY A C   1 
ATOM   549  O O   . GLY A 1 73  ? 5.605  -1.337  59.478  1.00 83.07  ? 73  GLY A O   1 
ATOM   550  N N   . GLY A 1 74  ? 4.397  0.542   59.210  1.00 93.19  ? 74  GLY A N   1 
ATOM   551  C CA  . GLY A 1 74  ? 5.503  1.357   58.723  1.00 87.06  ? 74  GLY A CA  1 
ATOM   552  C C   . GLY A 1 74  ? 4.972  2.524   57.905  1.00 91.92  ? 74  GLY A C   1 
ATOM   553  O O   . GLY A 1 74  ? 3.855  2.990   58.122  1.00 98.43  ? 74  GLY A O   1 
ATOM   554  N N   . ARG A 1 75  ? 5.795  2.978   56.962  1.00 90.43  ? 75  ARG A N   1 
ATOM   555  C CA  . ARG A 1 75  ? 5.361  4.021   56.033  1.00 90.21  ? 75  ARG A CA  1 
ATOM   556  C C   . ARG A 1 75  ? 6.235  3.952   54.786  1.00 89.72  ? 75  ARG A C   1 
ATOM   557  O O   . ARG A 1 75  ? 7.427  4.268   54.854  1.00 89.82  ? 75  ARG A O   1 
ATOM   558  C CB  . ARG A 1 75  ? 5.432  5.392   56.689  1.00 91.72  ? 75  ARG A CB  1 
ATOM   559  C CG  . ARG A 1 75  ? 4.876  6.510   55.834  1.00 89.19  ? 75  ARG A CG  1 
ATOM   560  C CD  . ARG A 1 75  ? 4.586  7.743   56.660  1.00 86.74  ? 75  ARG A CD  1 
ATOM   561  N NE  . ARG A 1 75  ? 4.223  8.882   55.826  1.00 92.19  ? 75  ARG A NE  1 
ATOM   562  C CZ  . ARG A 1 75  ? 2.999  9.129   55.378  1.00 97.14  ? 75  ARG A CZ  1 
ATOM   563  N NH1 . ARG A 1 75  ? 1.978  8.335   55.671  1.00 93.11  ? 75  ARG A NH1 1 
ATOM   564  N NH2 . ARG A 1 75  ? 2.791  10.203  54.621  1.00 97.82  ? 75  ARG A NH2 1 
ATOM   565  N N   . ARG A 1 76  ? 5.648  3.495   53.675  1.00 93.90  ? 76  ARG A N   1 
ATOM   566  C CA  . ARG A 1 76  ? 6.308  3.254   52.394  1.00 88.32  ? 76  ARG A CA  1 
ATOM   567  C C   . ARG A 1 76  ? 5.916  4.272   51.325  1.00 86.64  ? 76  ARG A C   1 
ATOM   568  O O   . ARG A 1 76  ? 4.844  4.882   51.369  1.00 88.37  ? 76  ARG A O   1 
ATOM   569  C CB  . ARG A 1 76  ? 5.993  1.849   51.872  1.00 85.61  ? 76  ARG A CB  1 
ATOM   570  C CG  . ARG A 1 76  ? 7.045  0.825   52.196  1.00 89.84  ? 76  ARG A CG  1 
ATOM   571  C CD  . ARG A 1 76  ? 6.592  -0.564  51.813  1.00 93.28  ? 76  ARG A CD  1 
ATOM   572  N NE  . ARG A 1 76  ? 7.399  -1.575  52.485  1.00 106.59 ? 76  ARG A NE  1 
ATOM   573  C CZ  . ARG A 1 76  ? 7.102  -2.866  52.522  1.00 106.21 ? 76  ARG A CZ  1 
ATOM   574  N NH1 . ARG A 1 76  ? 6.018  -3.342  51.931  1.00 101.67 ? 76  ARG A NH1 1 
ATOM   575  N NH2 . ARG A 1 76  ? 7.908  -3.698  53.176  1.00 100.20 ? 76  ARG A NH2 1 
ATOM   576  N N   . LYS A 1 77  ? 6.803  4.425   50.340  1.00 86.24  ? 77  LYS A N   1 
ATOM   577  C CA  . LYS A 1 77  ? 6.594  5.291   49.181  1.00 81.57  ? 77  LYS A CA  1 
ATOM   578  C C   . LYS A 1 77  ? 6.303  4.418   47.964  1.00 80.37  ? 77  LYS A C   1 
ATOM   579  O O   . LYS A 1 77  ? 7.118  3.564   47.602  1.00 79.42  ? 77  LYS A O   1 
ATOM   580  C CB  . LYS A 1 77  ? 7.819  6.165   48.915  1.00 72.28  ? 77  LYS A CB  1 
ATOM   581  C CG  . LYS A 1 77  ? 7.600  7.224   47.860  1.00 75.30  ? 77  LYS A CG  1 
ATOM   582  C CD  . LYS A 1 77  ? 8.850  8.053   47.647  1.00 72.15  ? 77  LYS A CD  1 
ATOM   583  C CE  . LYS A 1 77  ? 8.653  9.086   46.550  1.00 76.03  ? 77  LYS A CE  1 
ATOM   584  N NZ  . LYS A 1 77  ? 9.866  9.933   46.347  1.00 71.73  ? 77  LYS A NZ  1 
ATOM   585  N N   . TYR A 1 78  ? 5.157  4.645   47.330  1.00 76.62  ? 78  TYR A N   1 
ATOM   586  C CA  . TYR A 1 78  ? 4.708  3.868   46.182  1.00 77.22  ? 78  TYR A CA  1 
ATOM   587  C C   . TYR A 1 78  ? 4.851  4.669   44.892  1.00 79.57  ? 78  TYR A C   1 
ATOM   588  O O   . TYR A 1 78  ? 5.088  5.877   44.905  1.00 80.83  ? 78  TYR A O   1 
ATOM   589  C CB  . TYR A 1 78  ? 3.259  3.417   46.377  1.00 77.15  ? 78  TYR A CB  1 
ATOM   590  C CG  . TYR A 1 78  ? 3.120  2.290   47.369  1.00 79.17  ? 78  TYR A CG  1 
ATOM   591  C CD1 . TYR A 1 78  ? 3.200  2.531   48.733  1.00 82.84  ? 78  TYR A CD1 1 
ATOM   592  C CD2 . TYR A 1 78  ? 2.916  0.987   46.945  1.00 79.01  ? 78  TYR A CD2 1 
ATOM   593  C CE1 . TYR A 1 78  ? 3.078  1.506   49.646  1.00 83.69  ? 78  TYR A CE1 1 
ATOM   594  C CE2 . TYR A 1 78  ? 2.790  -0.045  47.849  1.00 81.00  ? 78  TYR A CE2 1 
ATOM   595  C CZ  . TYR A 1 78  ? 2.872  0.220   49.199  1.00 82.78  ? 78  TYR A CZ  1 
ATOM   596  O OH  . TYR A 1 78  ? 2.750  -0.805  50.108  1.00 87.66  ? 78  TYR A OH  1 
ATOM   597  N N   . TYR A 1 79  ? 4.729  3.971   43.761  1.00 78.10  ? 79  TYR A N   1 
ATOM   598  C CA  . TYR A 1 79  ? 4.795  4.597   42.446  1.00 76.85  ? 79  TYR A CA  1 
ATOM   599  C C   . TYR A 1 79  ? 3.599  4.179   41.601  1.00 74.43  ? 79  TYR A C   1 
ATOM   600  O O   . TYR A 1 79  ? 3.123  3.044   41.682  1.00 75.02  ? 79  TYR A O   1 
ATOM   601  C CB  . TYR A 1 79  ? 6.094  4.244   41.725  1.00 73.63  ? 79  TYR A CB  1 
ATOM   602  C CG  . TYR A 1 79  ? 7.306  4.948   42.279  1.00 73.73  ? 79  TYR A CG  1 
ATOM   603  C CD1 . TYR A 1 79  ? 7.611  6.238   41.878  1.00 76.75  ? 79  TYR A CD1 1 
ATOM   604  C CD2 . TYR A 1 79  ? 8.147  4.331   43.192  1.00 73.60  ? 79  TYR A CD2 1 
ATOM   605  C CE1 . TYR A 1 79  ? 8.718  6.899   42.366  1.00 70.36  ? 79  TYR A CE1 1 
ATOM   606  C CE2 . TYR A 1 79  ? 9.261  4.988   43.689  1.00 76.53  ? 79  TYR A CE2 1 
ATOM   607  C CZ  . TYR A 1 79  ? 9.539  6.276   43.267  1.00 73.28  ? 79  TYR A CZ  1 
ATOM   608  O OH  . TYR A 1 79  ? 10.636 6.956   43.744  1.00 72.44  ? 79  TYR A OH  1 
ATOM   609  N N   . ARG A 1 80  ? 3.132  5.100   40.764  1.00 73.32  ? 80  ARG A N   1 
ATOM   610  C CA  . ARG A 1 80  ? 1.894  4.884   40.032  1.00 81.38  ? 80  ARG A CA  1 
ATOM   611  C C   . ARG A 1 80  ? 1.985  5.437   38.615  1.00 82.49  ? 80  ARG A C   1 
ATOM   612  O O   . ARG A 1 80  ? 2.548  6.512   38.390  1.00 77.12  ? 80  ARG A O   1 
ATOM   613  C CB  . ARG A 1 80  ? 0.725  5.535   40.772  1.00 80.80  ? 80  ARG A CB  1 
ATOM   614  C CG  . ARG A 1 80  ? -0.630 5.027   40.370  1.00 82.46  ? 80  ARG A CG  1 
ATOM   615  C CD  . ARG A 1 80  ? -1.709 5.699   41.193  1.00 88.87  ? 80  ARG A CD  1 
ATOM   616  N NE  . ARG A 1 80  ? -2.976 5.742   40.475  1.00 95.84  ? 80  ARG A NE  1 
ATOM   617  C CZ  . ARG A 1 80  ? -3.225 6.557   39.459  1.00 93.90  ? 80  ARG A CZ  1 
ATOM   618  N NH1 . ARG A 1 80  ? -2.313 7.407   39.016  1.00 97.15  ? 80  ARG A NH1 1 
ATOM   619  N NH2 . ARG A 1 80  ? -4.419 6.519   38.872  1.00 90.23  ? 80  ARG A NH2 1 
ATOM   620  N N   . LEU A 1 81  ? 1.394  4.699   37.673  1.00 88.46  ? 81  LEU A N   1 
ATOM   621  C CA  . LEU A 1 81  ? 1.368  5.066   36.260  1.00 79.16  ? 81  LEU A CA  1 
ATOM   622  C C   . LEU A 1 81  ? 0.262  6.076   35.975  1.00 78.35  ? 81  LEU A C   1 
ATOM   623  O O   . LEU A 1 81  ? -0.900 5.840   36.313  1.00 83.44  ? 81  LEU A O   1 
ATOM   624  C CB  . LEU A 1 81  ? 1.153  3.814   35.415  1.00 79.48  ? 81  LEU A CB  1 
ATOM   625  C CG  . LEU A 1 81  ? 1.303  3.897   33.898  1.00 82.78  ? 81  LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 81  ? 2.691  4.380   33.532  1.00 80.28  ? 81  LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 81  ? 1.014  2.544   33.255  1.00 85.52  ? 81  LEU A CD2 1 
ATOM   628  N N   . THR A 1 82  ? 0.619  7.197   35.349  1.00 79.49  ? 82  THR A N   1 
ATOM   629  C CA  . THR A 1 82  ? -0.330 8.268   35.074  1.00 81.19  ? 82  THR A CA  1 
ATOM   630  C C   . THR A 1 82  ? -1.227 7.908   33.890  1.00 80.70  ? 82  THR A C   1 
ATOM   631  O O   . THR A 1 82  ? -1.173 6.804   33.344  1.00 80.58  ? 82  THR A O   1 
ATOM   632  C CB  . THR A 1 82  ? 0.399  9.573   34.771  1.00 80.72  ? 82  THR A CB  1 
ATOM   633  O OG1 . THR A 1 82  ? 1.012  9.483   33.481  1.00 82.86  ? 82  THR A OG1 1 
ATOM   634  C CG2 . THR A 1 82  ? 1.465  9.838   35.809  1.00 78.40  ? 82  THR A CG2 1 
ATOM   635  N N   . GLU A 1 83  ? -2.089 8.851   33.499  1.00 79.64  ? 83  GLU A N   1 
ATOM   636  C CA  . GLU A 1 83  ? -2.841 8.689   32.258  1.00 87.55  ? 83  GLU A CA  1 
ATOM   637  C C   . GLU A 1 83  ? -1.907 8.641   31.062  1.00 87.70  ? 83  GLU A C   1 
ATOM   638  O O   . GLU A 1 83  ? -1.972 7.715   30.243  1.00 87.86  ? 83  GLU A O   1 
ATOM   639  C CB  . GLU A 1 83  ? -3.849 9.816   32.054  1.00 87.55  ? 83  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 83  ? -5.232 9.539   32.564  1.00 87.68  ? 83  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 83  ? -6.280 10.240  31.723  1.00 89.53  ? 83  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 83  ? -6.065 10.374  30.498  1.00 89.67  ? 83  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 83  ? -7.306 10.675  32.275  1.00 96.59  ? 83  GLU A OE2 1 
ATOM   644  N N   . ILE A 1 84  ? -1.056 9.663   30.932  1.00 81.87  ? 84  ILE A N   1 
ATOM   645  C CA  . ILE A 1 84  ? -0.079 9.733   29.849  1.00 77.62  ? 84  ILE A CA  1 
ATOM   646  C C   . ILE A 1 84  ? 0.645  8.407   29.713  1.00 76.46  ? 84  ILE A C   1 
ATOM   647  O O   . ILE A 1 84  ? 0.934  7.948   28.602  1.00 75.00  ? 84  ILE A O   1 
ATOM   648  C CB  . ILE A 1 84  ? 0.912  10.880  30.110  1.00 78.19  ? 84  ILE A CB  1 
ATOM   649  C CG1 . ILE A 1 84  ? 0.179  12.108  30.648  1.00 75.49  ? 84  ILE A CG1 1 
ATOM   650  C CG2 . ILE A 1 84  ? 1.673  11.222  28.840  1.00 77.06  ? 84  ILE A CG2 1 
ATOM   651  C CD1 . ILE A 1 84  ? -0.872 12.634  29.719  1.00 75.24  ? 84  ILE A CD1 1 
ATOM   652  N N   . GLY A 1 85  ? 0.984  7.792   30.846  1.00 75.79  ? 85  GLY A N   1 
ATOM   653  C CA  . GLY A 1 85  ? 1.626  6.492   30.813  1.00 72.07  ? 85  GLY A CA  1 
ATOM   654  C C   . GLY A 1 85  ? 0.771  5.433   30.143  1.00 76.55  ? 85  GLY A C   1 
ATOM   655  O O   . GLY A 1 85  ? 1.234  4.726   29.249  1.00 83.16  ? 85  GLY A O   1 
ATOM   656  N N   . HIS A 1 86  ? -0.496 5.311   30.561  1.00 78.78  ? 86  HIS A N   1 
ATOM   657  C CA  . HIS A 1 86  ? -1.363 4.296   29.964  1.00 77.17  ? 86  HIS A CA  1 
ATOM   658  C C   . HIS A 1 86  ? -1.558 4.522   28.472  1.00 78.45  ? 86  HIS A C   1 
ATOM   659  O O   . HIS A 1 86  ? -1.646 3.559   27.702  1.00 79.16  ? 86  HIS A O   1 
ATOM   660  C CB  . HIS A 1 86  ? -2.721 4.243   30.667  1.00 80.05  ? 86  HIS A CB  1 
ATOM   661  C CG  . HIS A 1 86  ? -2.771 3.292   31.824  1.00 83.94  ? 86  HIS A CG  1 
ATOM   662  N ND1 . HIS A 1 86  ? -2.692 3.704   33.137  1.00 77.83  ? 86  HIS A ND1 1 
ATOM   663  C CD2 . HIS A 1 86  ? -2.882 1.943   31.859  1.00 87.38  ? 86  HIS A CD2 1 
ATOM   664  C CE1 . HIS A 1 86  ? -2.757 2.650   33.931  1.00 76.13  ? 86  HIS A CE1 1 
ATOM   665  N NE2 . HIS A 1 86  ? -2.871 1.569   33.182  1.00 83.70  ? 86  HIS A NE2 1 
ATOM   666  N N   . GLU A 1 87  ? -1.624 5.781   28.038  1.00 78.58  ? 87  GLU A N   1 
ATOM   667  C CA  . GLU A 1 87  ? -1.811 6.043   26.615  1.00 76.99  ? 87  GLU A CA  1 
ATOM   668  C C   . GLU A 1 87  ? -0.585 5.624   25.817  1.00 71.55  ? 87  GLU A C   1 
ATOM   669  O O   . GLU A 1 87  ? -0.712 5.053   24.730  1.00 72.39  ? 87  GLU A O   1 
ATOM   670  C CB  . GLU A 1 87  ? -2.129 7.515   26.384  1.00 81.16  ? 87  GLU A CB  1 
ATOM   671  C CG  . GLU A 1 87  ? -2.534 7.814   24.962  1.00 85.15  ? 87  GLU A CG  1 
ATOM   672  C CD  . GLU A 1 87  ? -3.002 9.241   24.779  1.00 97.56  ? 87  GLU A CD  1 
ATOM   673  O OE1 . GLU A 1 87  ? -3.404 9.871   25.782  1.00 96.53  ? 87  GLU A OE1 1 
ATOM   674  O OE2 . GLU A 1 87  ? -2.965 9.730   23.628  1.00 105.82 ? 87  GLU A OE2 1 
ATOM   675  N N   . ASN A 1 88  ? 0.611  5.900   26.342  1.00 76.93  ? 88  ASN A N   1 
ATOM   676  C CA  . ASN A 1 88  ? 1.832  5.461   25.679  1.00 76.99  ? 88  ASN A CA  1 
ATOM   677  C C   . ASN A 1 88  ? 1.920  3.946   25.620  1.00 72.92  ? 88  ASN A C   1 
ATOM   678  O O   . ASN A 1 88  ? 2.451  3.394   24.650  1.00 72.60  ? 88  ASN A O   1 
ATOM   679  C CB  . ASN A 1 88  ? 3.057  6.038   26.386  1.00 74.78  ? 88  ASN A CB  1 
ATOM   680  C CG  . ASN A 1 88  ? 3.247  7.509   26.100  1.00 81.32  ? 88  ASN A CG  1 
ATOM   681  O OD1 . ASN A 1 88  ? 2.287  8.227   25.818  1.00 84.26  ? 88  ASN A OD1 1 
ATOM   682  N ND2 . ASN A 1 88  ? 4.491  7.968   26.166  1.00 82.58  ? 88  ASN A ND2 1 
ATOM   683  N N   . MET A 1 89  ? 1.434  3.257   26.649  1.00 68.07  ? 89  MET A N   1 
ATOM   684  C CA  . MET A 1 89  ? 1.414  1.802   26.591  1.00 69.27  ? 89  MET A CA  1 
ATOM   685  C C   . MET A 1 89  ? 0.604  1.319   25.399  1.00 68.19  ? 89  MET A C   1 
ATOM   686  O O   . MET A 1 89  ? 1.007  0.374   24.711  1.00 65.41  ? 89  MET A O   1 
ATOM   687  C CB  . MET A 1 89  ? 0.867  1.226   27.895  1.00 76.46  ? 89  MET A CB  1 
ATOM   688  C CG  . MET A 1 89  ? 1.650  1.656   29.133  1.00 81.08  ? 89  MET A CG  1 
ATOM   689  S SD  . MET A 1 89  ? 3.255  0.846   29.308  1.00 80.87  ? 89  MET A SD  1 
ATOM   690  C CE  . MET A 1 89  ? 2.816  -0.856  28.970  1.00 86.27  ? 89  MET A CE  1 
ATOM   691  N N   . ARG A 1 90  ? -0.538 1.967   25.132  1.00 69.57  ? 90  ARG A N   1 
ATOM   692  C CA  . ARG A 1 90  ? -1.391 1.558   24.020  1.00 69.33  ? 90  ARG A CA  1 
ATOM   693  C C   . ARG A 1 90  ? -0.730 1.892   22.688  1.00 69.24  ? 90  ARG A C   1 
ATOM   694  O O   . ARG A 1 90  ? -0.693 1.061   21.772  1.00 69.13  ? 90  ARG A O   1 
ATOM   695  C CB  . ARG A 1 90  ? -2.758 2.247   24.103  1.00 67.57  ? 90  ARG A CB  1 
ATOM   696  C CG  . ARG A 1 90  ? -3.878 1.442   23.434  1.00 79.95  ? 90  ARG A CG  1 
ATOM   697  C CD  . ARG A 1 90  ? -5.208 2.188   23.242  1.00 77.32  ? 90  ARG A CD  1 
ATOM   698  N NE  . ARG A 1 90  ? -5.082 3.380   22.409  1.00 76.95  ? 90  ARG A NE  1 
ATOM   699  C CZ  . ARG A 1 90  ? -5.170 4.629   22.843  1.00 78.29  ? 90  ARG A CZ  1 
ATOM   700  N NH1 . ARG A 1 90  ? -5.314 4.906   24.128  1.00 81.42  ? 90  ARG A NH1 1 
ATOM   701  N NH2 . ARG A 1 90  ? -5.092 5.627   21.966  1.00 77.29  ? 90  ARG A NH2 1 
ATOM   702  N N   . LEU A 1 91  ? -0.216 3.118   22.561  1.00 69.47  ? 91  LEU A N   1 
ATOM   703  C CA  . LEU A 1 91  ? 0.494  3.516   21.349  1.00 68.13  ? 91  LEU A CA  1 
ATOM   704  C C   . LEU A 1 91  ? 1.637  2.558   21.049  1.00 66.51  ? 91  LEU A C   1 
ATOM   705  O O   . LEU A 1 91  ? 1.794  2.092   19.916  1.00 71.98  ? 91  LEU A O   1 
ATOM   706  C CB  . LEU A 1 91  ? 1.027  4.942   21.491  1.00 70.00  ? 91  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 91  ? 0.058  6.085   21.800  1.00 73.48  ? 91  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 91  ? 0.709  7.435   21.498  1.00 74.78  ? 91  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 91  ? -1.275 5.929   21.075  1.00 77.39  ? 91  LEU A CD2 1 
ATOM   710  N N   . ARG A 1 92  ? 2.450  2.256   22.058  1.00 66.32  ? 92  ARG A N   1 
ATOM   711  C CA  . ARG A 1 92  ? 3.622  1.424   21.835  1.00 64.00  ? 92  ARG A CA  1 
ATOM   712  C C   . ARG A 1 92  ? 3.229  0.046   21.328  1.00 61.33  ? 92  ARG A C   1 
ATOM   713  O O   . ARG A 1 92  ? 3.851  -0.481  20.401  1.00 66.50  ? 92  ARG A O   1 
ATOM   714  C CB  . ARG A 1 92  ? 4.430  1.315   23.126  1.00 66.51  ? 92  ARG A CB  1 
ATOM   715  C CG  . ARG A 1 92  ? 5.777  0.669   22.941  1.00 66.84  ? 92  ARG A CG  1 
ATOM   716  C CD  . ARG A 1 92  ? 5.931  -0.558  23.802  1.00 66.23  ? 92  ARG A CD  1 
ATOM   717  N NE  . ARG A 1 92  ? 7.210  -1.221  23.570  1.00 68.00  ? 92  ARG A NE  1 
ATOM   718  C CZ  . ARG A 1 92  ? 7.339  -2.413  23.008  1.00 69.63  ? 92  ARG A CZ  1 
ATOM   719  N NH1 . ARG A 1 92  ? 6.283  -3.109  22.619  1.00 71.48  ? 92  ARG A NH1 1 
ATOM   720  N NH2 . ARG A 1 92  ? 8.557  -2.918  22.827  1.00 65.37  ? 92  ARG A NH2 1 
ATOM   721  N N   . HIS A 1 93  ? 2.176  -0.539  21.899  1.00 62.30  ? 93  HIS A N   1 
ATOM   722  C CA  . HIS A 1 93  ? 1.730  -1.858  21.459  1.00 67.44  ? 93  HIS A CA  1 
ATOM   723  C C   . HIS A 1 93  ? 1.186  -1.828  20.040  1.00 67.22  ? 93  HIS A C   1 
ATOM   724  O O   . HIS A 1 93  ? 1.396  -2.771  19.269  1.00 70.37  ? 93  HIS A O   1 
ATOM   725  C CB  . HIS A 1 93  ? 0.653  -2.394  22.397  1.00 70.74  ? 93  HIS A CB  1 
ATOM   726  C CG  . HIS A 1 93  ? 0.057  -3.688  21.941  1.00 78.39  ? 93  HIS A CG  1 
ATOM   727  N ND1 . HIS A 1 93  ? 0.663  -4.906  22.153  1.00 83.03  ? 93  HIS A ND1 1 
ATOM   728  C CD2 . HIS A 1 93  ? -1.071 -3.946  21.235  1.00 85.29  ? 93  HIS A CD2 1 
ATOM   729  C CE1 . HIS A 1 93  ? -0.080 -5.863  21.624  1.00 87.03  ? 93  HIS A CE1 1 
ATOM   730  N NE2 . HIS A 1 93  ? -1.136 -5.307  21.059  1.00 86.52  ? 93  HIS A NE2 1 
ATOM   731  N N   . GLU A 1 94  ? 0.463  -0.774  19.684  1.00 64.51  ? 94  GLU A N   1 
ATOM   732  C CA  . GLU A 1 94  ? -0.124 -0.716  18.354  1.00 67.33  ? 94  GLU A CA  1 
ATOM   733  C C   . GLU A 1 94  ? 0.961  -0.628  17.285  1.00 64.64  ? 94  GLU A C   1 
ATOM   734  O O   . GLU A 1 94  ? 0.949  -1.392  16.313  1.00 62.80  ? 94  GLU A O   1 
ATOM   735  C CB  . GLU A 1 94  ? -1.110 0.451   18.275  1.00 72.58  ? 94  GLU A CB  1 
ATOM   736  C CG  . GLU A 1 94  ? -2.427 0.152   19.018  1.00 79.04  ? 94  GLU A CG  1 
ATOM   737  C CD  . GLU A 1 94  ? -3.511 1.208   18.810  1.00 87.56  ? 94  GLU A CD  1 
ATOM   738  O OE1 . GLU A 1 94  ? -3.488 1.889   17.763  1.00 93.66  ? 94  GLU A OE1 1 
ATOM   739  O OE2 . GLU A 1 94  ? -4.384 1.360   19.699  1.00 81.98  ? 94  GLU A OE2 1 
ATOM   740  N N   . SER A 1 95  ? 1.917  0.289   17.455  1.00 65.93  ? 95  SER A N   1 
ATOM   741  C CA  . SER A 1 95  ? 2.980  0.450   16.465  1.00 65.35  ? 95  SER A CA  1 
ATOM   742  C C   . SER A 1 95  ? 3.728  -0.857  16.248  1.00 62.75  ? 95  SER A C   1 
ATOM   743  O O   . SER A 1 95  ? 3.962  -1.271  15.108  1.00 64.42  ? 95  SER A O   1 
ATOM   744  C CB  . SER A 1 95  ? 3.947  1.552   16.894  1.00 62.86  ? 95  SER A CB  1 
ATOM   745  O OG  . SER A 1 95  ? 4.693  1.166   18.036  1.00 70.69  ? 95  SER A OG  1 
ATOM   746  N N   . TRP A 1 96  ? 4.105  -1.529  17.333  1.00 62.90  ? 96  TRP A N   1 
ATOM   747  C CA  . TRP A 1 96  ? 4.840  -2.774  17.185  1.00 60.35  ? 96  TRP A CA  1 
ATOM   748  C C   . TRP A 1 96  ? 3.982  -3.872  16.573  1.00 63.85  ? 96  TRP A C   1 
ATOM   749  O O   . TRP A 1 96  ? 4.529  -4.811  15.985  1.00 63.57  ? 96  TRP A O   1 
ATOM   750  C CB  . TRP A 1 96  ? 5.405  -3.208  18.531  1.00 61.82  ? 96  TRP A CB  1 
ATOM   751  C CG  . TRP A 1 96  ? 6.688  -2.523  18.839  1.00 63.74  ? 96  TRP A CG  1 
ATOM   752  C CD1 . TRP A 1 96  ? 6.874  -1.454  19.668  1.00 62.55  ? 96  TRP A CD1 1 
ATOM   753  C CD2 . TRP A 1 96  ? 7.970  -2.830  18.287  1.00 58.98  ? 96  TRP A CD2 1 
ATOM   754  N NE1 . TRP A 1 96  ? 8.199  -1.088  19.680  1.00 59.27  ? 96  TRP A NE1 1 
ATOM   755  C CE2 . TRP A 1 96  ? 8.892  -1.917  18.838  1.00 59.06  ? 96  TRP A CE2 1 
ATOM   756  C CE3 . TRP A 1 96  ? 8.429  -3.792  17.388  1.00 54.20  ? 96  TRP A CE3 1 
ATOM   757  C CZ2 . TRP A 1 96  ? 10.242 -1.942  18.519  1.00 53.02  ? 96  TRP A CZ2 1 
ATOM   758  C CZ3 . TRP A 1 96  ? 9.770  -3.813  17.071  1.00 55.35  ? 96  TRP A CZ3 1 
ATOM   759  C CH2 . TRP A 1 96  ? 10.661 -2.895  17.635  1.00 57.09  ? 96  TRP A CH2 1 
ATOM   760  N N   . SER A 1 97  ? 2.655  -3.769  16.675  1.00 61.40  ? 97  SER A N   1 
ATOM   761  C CA  . SER A 1 97  ? 1.808  -4.690  15.932  1.00 60.51  ? 97  SER A CA  1 
ATOM   762  C C   . SER A 1 97  ? 1.973  -4.473  14.435  1.00 62.88  ? 97  SER A C   1 
ATOM   763  O O   . SER A 1 97  ? 2.073  -5.438  13.669  1.00 63.05  ? 97  SER A O   1 
ATOM   764  C CB  . SER A 1 97  ? 0.344  -4.519  16.336  1.00 67.39  ? 97  SER A CB  1 
ATOM   765  O OG  . SER A 1 97  ? 0.069  -5.155  17.570  1.00 71.12  ? 97  SER A OG  1 
ATOM   766  N N   . ARG A 1 98  ? 2.018  -3.212  14.000  1.00 61.17  ? 98  ARG A N   1 
ATOM   767  C CA  . ARG A 1 98  ? 2.178  -2.933  12.578  1.00 61.94  ? 98  ARG A CA  1 
ATOM   768  C C   . ARG A 1 98  ? 3.508  -3.456  12.061  1.00 57.32  ? 98  ARG A C   1 
ATOM   769  O O   . ARG A 1 98  ? 3.579  -3.987  10.949  1.00 61.73  ? 98  ARG A O   1 
ATOM   770  C CB  . ARG A 1 98  ? 2.060  -1.437  12.325  1.00 59.66  ? 98  ARG A CB  1 
ATOM   771  C CG  . ARG A 1 98  ? 0.855  -0.834  12.986  1.00 64.10  ? 98  ARG A CG  1 
ATOM   772  C CD  . ARG A 1 98  ? 0.263  0.277   12.149  1.00 67.00  ? 98  ARG A CD  1 
ATOM   773  N NE  . ARG A 1 98  ? -0.202 1.376   12.985  1.00 69.93  ? 98  ARG A NE  1 
ATOM   774  C CZ  . ARG A 1 98  ? 0.577  2.352   13.430  1.00 69.63  ? 98  ARG A CZ  1 
ATOM   775  N NH1 . ARG A 1 98  ? 1.867  2.399   13.132  1.00 64.79  ? 98  ARG A NH1 1 
ATOM   776  N NH2 . ARG A 1 98  ? 0.052  3.302   14.195  1.00 72.13  ? 98  ARG A NH2 1 
ATOM   777  N N   . VAL A 1 99  ? 4.573  -3.308  12.850  1.00 59.12  ? 99  VAL A N   1 
ATOM   778  C CA  . VAL A 1 99  ? 5.880  -3.819  12.448  1.00 51.88  ? 99  VAL A CA  1 
ATOM   779  C C   . VAL A 1 99  ? 5.822  -5.324  12.230  1.00 53.26  ? 99  VAL A C   1 
ATOM   780  O O   . VAL A 1 99  ? 6.427  -5.855  11.295  1.00 55.19  ? 99  VAL A O   1 
ATOM   781  C CB  . VAL A 1 99  ? 6.939  -3.440  13.497  1.00 55.22  ? 99  VAL A CB  1 
ATOM   782  C CG1 . VAL A 1 99  ? 8.242  -4.169  13.230  1.00 58.81  ? 99  VAL A CG1 1 
ATOM   783  C CG2 . VAL A 1 99  ? 7.155  -1.941  13.513  1.00 52.78  ? 99  VAL A CG2 1 
ATOM   784  N N   . ASP A 1 100 ? 5.103  -6.036  13.096  1.00 54.29  ? 100 ASP A N   1 
ATOM   785  C CA  . ASP A 1 100 ? 4.970  -7.481  12.952  1.00 55.16  ? 100 ASP A CA  1 
ATOM   786  C C   . ASP A 1 100 ? 4.208  -7.853  11.682  1.00 59.10  ? 100 ASP A C   1 
ATOM   787  O O   . ASP A 1 100 ? 4.496  -8.887  11.068  1.00 57.14  ? 100 ASP A O   1 
ATOM   788  C CB  . ASP A 1 100 ? 4.273  -8.060  14.182  1.00 64.99  ? 100 ASP A CB  1 
ATOM   789  C CG  . ASP A 1 100 ? 5.109  -7.926  15.451  1.00 69.46  ? 100 ASP A CG  1 
ATOM   790  O OD1 . ASP A 1 100 ? 6.301  -7.563  15.350  1.00 68.96  ? 100 ASP A OD1 1 
ATOM   791  O OD2 . ASP A 1 100 ? 4.565  -8.160  16.552  1.00 69.88  ? 100 ASP A OD2 1 
ATOM   792  N N   . LYS A 1 101 ? 3.223  -7.039  11.288  1.00 55.56  ? 101 LYS A N   1 
ATOM   793  C CA  . LYS A 1 101 ? 2.509  -7.280  10.038  1.00 57.50  ? 101 LYS A CA  1 
ATOM   794  C C   . LYS A 1 101 ? 3.441  -7.134  8.841   1.00 56.23  ? 101 LYS A C   1 
ATOM   795  O O   . LYS A 1 101 ? 3.448  -7.975  7.935   1.00 54.76  ? 101 LYS A O   1 
ATOM   796  C CB  . LYS A 1 101 ? 1.322  -6.321  9.920   1.00 59.97  ? 101 LYS A CB  1 
ATOM   797  C CG  . LYS A 1 101 ? 0.254  -6.507  10.996  1.00 70.14  ? 101 LYS A CG  1 
ATOM   798  C CD  . LYS A 1 101 ? -0.536 -5.215  11.299  1.00 72.64  ? 101 LYS A CD  1 
ATOM   799  C CE  . LYS A 1 101 ? -1.195 -5.270  12.694  1.00 71.26  ? 101 LYS A CE  1 
ATOM   800  N NZ  . LYS A 1 101 ? -1.674 -3.948  13.228  1.00 71.71  ? 101 LYS A NZ  1 
ATOM   801  N N   . ILE A 1 102 ? 4.227  -6.055  8.815   1.00 54.25  ? 102 ILE A N   1 
ATOM   802  C CA  . ILE A 1 102 ? 5.173  -5.829  7.727   1.00 50.52  ? 102 ILE A CA  1 
ATOM   803  C C   . ILE A 1 102 ? 6.077  -7.043  7.556   1.00 53.88  ? 102 ILE A C   1 
ATOM   804  O O   . ILE A 1 102 ? 6.337  -7.496  6.435   1.00 52.41  ? 102 ILE A O   1 
ATOM   805  C CB  . ILE A 1 102 ? 5.986  -4.550  7.996   1.00 53.52  ? 102 ILE A CB  1 
ATOM   806  C CG1 . ILE A 1 102 ? 5.072  -3.329  8.089   1.00 53.71  ? 102 ILE A CG1 1 
ATOM   807  C CG2 . ILE A 1 102 ? 7.011  -4.325  6.905   1.00 51.46  ? 102 ILE A CG2 1 
ATOM   808  C CD1 . ILE A 1 102 ? 5.834  -2.007  8.119   1.00 44.02  ? 102 ILE A CD1 1 
ATOM   809  N N   . ILE A 1 103 ? 6.576  -7.588  8.667   1.00 54.97  ? 103 ILE A N   1 
ATOM   810  C CA  . ILE A 1 103 ? 7.429  -8.771  8.598   1.00 53.90  ? 103 ILE A CA  1 
ATOM   811  C C   . ILE A 1 103 ? 6.646  -9.957  8.066   1.00 58.36  ? 103 ILE A C   1 
ATOM   812  O O   . ILE A 1 103 ? 7.149  -10.745 7.260   1.00 62.22  ? 103 ILE A O   1 
ATOM   813  C CB  . ILE A 1 103 ? 8.034  -9.074  9.975   1.00 52.55  ? 103 ILE A CB  1 
ATOM   814  C CG1 . ILE A 1 103 ? 8.902  -7.900  10.427  1.00 53.43  ? 103 ILE A CG1 1 
ATOM   815  C CG2 . ILE A 1 103 ? 8.793  -10.373 9.934   1.00 51.67  ? 103 ILE A CG2 1 
ATOM   816  C CD1 . ILE A 1 103 ? 9.862  -7.427  9.373   1.00 50.65  ? 103 ILE A CD1 1 
ATOM   817  N N   . GLU A 1 104 ? 5.407  -10.106 8.523   1.00 57.84  ? 104 GLU A N   1 
ATOM   818  C CA  . GLU A 1 104 ? 4.537  -11.164 8.030   1.00 59.29  ? 104 GLU A CA  1 
ATOM   819  C C   . GLU A 1 104 ? 4.378  -11.104 6.511   1.00 60.11  ? 104 GLU A C   1 
ATOM   820  O O   . GLU A 1 104 ? 4.399  -12.137 5.831   1.00 57.39  ? 104 GLU A O   1 
ATOM   821  C CB  . GLU A 1 104 ? 3.187  -11.023 8.731   1.00 62.73  ? 104 GLU A CB  1 
ATOM   822  C CG  . GLU A 1 104 ? 2.223  -12.176 8.644   1.00 64.81  ? 104 GLU A CG  1 
ATOM   823  C CD  . GLU A 1 104 ? 1.011  -11.935 9.532   1.00 77.42  ? 104 GLU A CD  1 
ATOM   824  O OE1 . GLU A 1 104 ? 0.873  -10.801 10.045  1.00 74.03  ? 104 GLU A OE1 1 
ATOM   825  O OE2 . GLU A 1 104 ? 0.195  -12.866 9.717   1.00 87.62  ? 104 GLU A OE2 1 
ATOM   826  N N   . ASN A 1 105 ? 4.243  -9.901  5.957   1.00 55.60  ? 105 ASN A N   1 
ATOM   827  C CA  . ASN A 1 105 ? 4.030  -9.761  4.522   1.00 57.85  ? 105 ASN A CA  1 
ATOM   828  C C   . ASN A 1 105 ? 5.317  -9.871  3.724   1.00 62.62  ? 105 ASN A C   1 
ATOM   829  O O   . ASN A 1 105 ? 5.284  -10.304 2.567   1.00 64.24  ? 105 ASN A O   1 
ATOM   830  C CB  . ASN A 1 105 ? 3.347  -8.430  4.221   1.00 57.70  ? 105 ASN A CB  1 
ATOM   831  C CG  . ASN A 1 105 ? 1.902  -8.430  4.636   1.00 54.58  ? 105 ASN A CG  1 
ATOM   832  O OD1 . ASN A 1 105 ? 1.331  -9.484  4.869   1.00 59.68  ? 105 ASN A OD1 1 
ATOM   833  N ND2 . ASN A 1 105 ? 1.307  -7.250  4.752   1.00 55.70  ? 105 ASN A ND2 1 
ATOM   834  N N   . LEU A 1 106 ? 6.444  -9.457  4.300   1.00 57.87  ? 106 LEU A N   1 
ATOM   835  C CA  . LEU A 1 106 ? 7.712  -9.604  3.601   1.00 58.43  ? 106 LEU A CA  1 
ATOM   836  C C   . LEU A 1 106 ? 7.982  -11.058 3.242   1.00 63.84  ? 106 LEU A C   1 
ATOM   837  O O   . LEU A 1 106 ? 8.385  -11.357 2.115   1.00 63.66  ? 106 LEU A O   1 
ATOM   838  C CB  . LEU A 1 106 ? 8.845  -9.028  4.450   1.00 58.08  ? 106 LEU A CB  1 
ATOM   839  C CG  . LEU A 1 106 ? 8.918  -7.498  4.393   1.00 57.01  ? 106 LEU A CG  1 
ATOM   840  C CD1 . LEU A 1 106 ? 9.878  -6.918  5.414   1.00 53.43  ? 106 LEU A CD1 1 
ATOM   841  C CD2 . LEU A 1 106 ? 9.317  -7.047  3.010   1.00 57.63  ? 106 LEU A CD2 1 
ATOM   842  N N   . GLU A 1 107 ? 7.741  -11.981 4.174   1.00 72.59  ? 107 GLU A N   1 
ATOM   843  C CA  . GLU A 1 107 ? 8.006  -13.387 3.882   1.00 77.04  ? 107 GLU A CA  1 
ATOM   844  C C   . GLU A 1 107 ? 6.954  -13.994 2.963   1.00 78.38  ? 107 GLU A C   1 
ATOM   845  O O   . GLU A 1 107 ? 7.251  -14.950 2.240   1.00 77.15  ? 107 GLU A O   1 
ATOM   846  C CB  . GLU A 1 107 ? 8.111  -14.186 5.179   1.00 79.01  ? 107 GLU A CB  1 
ATOM   847  C CG  . GLU A 1 107 ? 7.048  -13.875 6.206   1.00 86.23  ? 107 GLU A CG  1 
ATOM   848  C CD  . GLU A 1 107 ? 7.507  -14.200 7.618   1.00 101.41 ? 107 GLU A CD  1 
ATOM   849  O OE1 . GLU A 1 107 ? 8.700  -14.540 7.792   1.00 105.73 ? 107 GLU A OE1 1 
ATOM   850  O OE2 . GLU A 1 107 ? 6.681  -14.112 8.555   1.00 106.09 ? 107 GLU A OE2 1 
ATOM   851  N N   . ALA A 1 108 ? 5.729  -13.468 2.983   1.00 76.25  ? 108 ALA A N   1 
ATOM   852  C CA  . ALA A 1 108 ? 4.687  -13.975 2.098   1.00 75.09  ? 108 ALA A CA  1 
ATOM   853  C C   . ALA A 1 108 ? 4.970  -13.604 0.649   1.00 79.01  ? 108 ALA A C   1 
ATOM   854  O O   . ALA A 1 108 ? 4.981  -14.470 -0.231  1.00 85.16  ? 108 ALA A O   1 
ATOM   855  C CB  . ALA A 1 108 ? 3.318  -13.449 2.530   1.00 71.63  ? 108 ALA A CB  1 
ATOM   856  N N   . ASN A 1 109 ? 5.170  -12.312 0.376   1.00 78.07  ? 109 ASN A N   1 
ATOM   857  C CA  . ASN A 1 109 ? 5.501  -11.892 -0.983  1.00 81.00  ? 109 ASN A CA  1 
ATOM   858  C C   . ASN A 1 109 ? 6.778  -12.557 -1.472  1.00 88.93  ? 109 ASN A C   1 
ATOM   859  O O   . ASN A 1 109 ? 6.954  -12.745 -2.679  1.00 93.51  ? 109 ASN A O   1 
ATOM   860  C CB  . ASN A 1 109 ? 5.624  -10.370 -1.056  1.00 72.09  ? 109 ASN A CB  1 
ATOM   861  C CG  . ASN A 1 109 ? 4.326  -9.656  -0.711  1.00 77.31  ? 109 ASN A CG  1 
ATOM   862  O OD1 . ASN A 1 109 ? 3.246  -10.253 -0.724  1.00 78.06  ? 109 ASN A OD1 1 
ATOM   863  N ND2 . ASN A 1 109 ? 4.428  -8.369  -0.396  1.00 73.01  ? 109 ASN A ND2 1 
ATOM   864  N N   . LYS A 1 110 ? 7.674  -12.921 -0.551  1.00 91.85  ? 110 LYS A N   1 
ATOM   865  C CA  . LYS A 1 110 ? 8.852  -13.706 -0.904  1.00 90.55  ? 110 LYS A CA  1 
ATOM   866  C C   . LYS A 1 110 ? 8.453  -15.078 -1.426  1.00 96.30  ? 110 LYS A C   1 
ATOM   867  O O   . LYS A 1 110 ? 8.811  -15.461 -2.545  1.00 103.87 ? 110 LYS A O   1 
ATOM   868  C CB  . LYS A 1 110 ? 9.765  -13.849 0.313   1.00 89.31  ? 110 LYS A CB  1 
ATOM   869  C CG  . LYS A 1 110 ? 10.898 -14.851 0.134   1.00 83.63  ? 110 LYS A CG  1 
ATOM   870  C CD  . LYS A 1 110 ? 11.634 -15.072 1.448   1.00 79.36  ? 110 LYS A CD  1 
ATOM   871  C CE  . LYS A 1 110 ? 12.657 -16.190 1.353   1.00 75.78  ? 110 LYS A CE  1 
ATOM   872  N NZ  . LYS A 1 110 ? 13.335 -16.418 2.664   1.00 76.93  ? 110 LYS A NZ  1 
ATOM   873  N N   . LYS A 1 111 ? 7.711  -15.838 -0.616  1.00 92.27  ? 111 LYS A N   1 
ATOM   874  C CA  . LYS A 1 111 ? 7.223  -17.144 -1.041  1.00 92.84  ? 111 LYS A CA  1 
ATOM   875  C C   . LYS A 1 111 ? 6.343  -17.056 -2.285  1.00 97.54  ? 111 LYS A C   1 
ATOM   876  O O   . LYS A 1 111 ? 6.246  -18.034 -3.033  1.00 100.36 ? 111 LYS A O   1 
ATOM   877  C CB  . LYS A 1 111 ? 6.457  -17.801 0.108   1.00 85.66  ? 111 LYS A CB  1 
ATOM   878  C CG  . LYS A 1 111 ? 6.557  -19.312 0.143   1.00 87.58  ? 111 LYS A CG  1 
ATOM   879  C CD  . LYS A 1 111 ? 5.817  -19.882 1.339   1.00 86.06  ? 111 LYS A CD  1 
ATOM   880  C CE  . LYS A 1 111 ? 5.778  -21.404 1.292   1.00 93.73  ? 111 LYS A CE  1 
ATOM   881  N NZ  . LYS A 1 111 ? 4.933  -21.996 2.375   1.00 94.72  ? 111 LYS A NZ  1 
ATOM   882  N N   . SER A 1 112 ? 5.713  -15.904 -2.531  1.00 98.63  ? 112 SER A N   1 
ATOM   883  C CA  . SER A 1 112 ? 4.884  -15.749 -3.723  1.00 99.94  ? 112 SER A CA  1 
ATOM   884  C C   . SER A 1 112 ? 5.736  -15.613 -4.978  1.00 105.00 ? 112 SER A C   1 
ATOM   885  O O   . SER A 1 112 ? 5.347  -16.090 -6.050  1.00 109.86 ? 112 SER A O   1 
ATOM   886  C CB  . SER A 1 112 ? 3.963  -14.538 -3.570  1.00 96.19  ? 112 SER A CB  1 
ATOM   887  O OG  . SER A 1 112 ? 3.195  -14.629 -2.381  1.00 95.52  ? 112 SER A OG  1 
ATOM   888  N N   . GLU A 1 113 ? 6.897  -14.957 -4.869  1.00 110.88 ? 113 GLU A N   1 
ATOM   889  C CA  . GLU A 1 113 ? 7.801  -14.844 -6.012  1.00 114.78 ? 113 GLU A CA  1 
ATOM   890  C C   . GLU A 1 113 ? 8.386  -16.195 -6.405  1.00 120.83 ? 113 GLU A C   1 
ATOM   891  O O   . GLU A 1 113 ? 8.729  -16.402 -7.576  1.00 118.78 ? 113 GLU A O   1 
ATOM   892  C CB  . GLU A 1 113 ? 8.936  -13.868 -5.703  1.00 113.18 ? 113 GLU A CB  1 
ATOM   893  C CG  . GLU A 1 113 ? 8.497  -12.472 -5.314  1.00 117.43 ? 113 GLU A CG  1 
ATOM   894  C CD  . GLU A 1 113 ? 9.404  -11.861 -4.255  1.00 121.40 ? 113 GLU A CD  1 
ATOM   895  O OE1 . GLU A 1 113 ? 10.458 -12.466 -3.955  1.00 114.26 ? 113 GLU A OE1 1 
ATOM   896  O OE2 . GLU A 1 113 ? 9.060  -10.785 -3.718  1.00 120.23 ? 113 GLU A OE2 1 
ATOM   897  N N   . ALA A 1 114 ? 8.524  -17.115 -5.443  1.00 113.08 ? 114 ALA A N   1 
ATOM   898  C CA  . ALA A 1 114 ? 9.057  -18.440 -5.744  1.00 109.02 ? 114 ALA A CA  1 
ATOM   899  C C   . ALA A 1 114 ? 8.183  -19.170 -6.757  1.00 112.52 ? 114 ALA A C   1 
ATOM   900  O O   . ALA A 1 114 ? 8.692  -19.875 -7.637  1.00 117.25 ? 114 ALA A O   1 
ATOM   901  C CB  . ALA A 1 114 ? 9.184  -19.257 -4.458  1.00 105.98 ? 114 ALA A CB  1 
ATOM   902  N N   . ILE A 1 115 ? 6.870  -19.007 -6.652  1.00 109.55 ? 115 ILE A N   1 
ATOM   903  C CA  . ILE A 1 115 ? 5.939  -19.616 -7.586  1.00 105.09 ? 115 ILE A CA  1 
ATOM   904  C C   . ILE A 1 115 ? 5.806  -18.757 -8.844  1.00 105.79 ? 115 ILE A C   1 
ATOM   905  O O   . ILE A 1 115 ? 6.790  -18.486 -9.539  1.00 97.32  ? 115 ILE A O   1 
ATOM   906  C CB  . ILE A 1 115 ? 4.576  -19.840 -6.914  1.00 98.56  ? 115 ILE A CB  1 
ATOM   907  C CG1 . ILE A 1 115 ? 4.745  -20.718 -5.670  1.00 94.67  ? 115 ILE A CG1 1 
ATOM   908  C CG2 . ILE A 1 115 ? 3.593  -20.453 -7.893  1.00 98.11  ? 115 ILE A CG2 1 
ATOM   909  C CD1 . ILE A 1 115 ? 3.462  -21.001 -4.941  1.00 83.75  ? 115 ILE A CD1 1 
ATOM   910  N N   . ILE B 1 4   ? 5.018  8.430   20.588  1.00 85.15  ? 4   ILE B N   1 
ATOM   911  C CA  . ILE B 1 4   ? 6.080  7.489   20.247  1.00 83.13  ? 4   ILE B CA  1 
ATOM   912  C C   . ILE B 1 4   ? 7.421  8.200   20.133  1.00 82.49  ? 4   ILE B C   1 
ATOM   913  O O   . ILE B 1 4   ? 7.593  9.075   19.291  1.00 81.48  ? 4   ILE B O   1 
ATOM   914  C CB  . ILE B 1 4   ? 5.764  6.737   18.950  1.00 83.86  ? 4   ILE B CB  1 
ATOM   915  C CG1 . ILE B 1 4   ? 4.411  6.033   19.061  1.00 83.67  ? 4   ILE B CG1 1 
ATOM   916  C CG2 . ILE B 1 4   ? 6.859  5.725   18.645  1.00 80.76  ? 4   ILE B CG2 1 
ATOM   917  C CD1 . ILE B 1 4   ? 4.384  4.934   20.094  1.00 82.23  ? 4   ILE B CD1 1 
ATOM   918  N N   . PRO B 1 5   ? 8.375  7.803   20.969  1.00 86.10  ? 5   PRO B N   1 
ATOM   919  C CA  . PRO B 1 5   ? 9.662  8.503   21.008  1.00 84.53  ? 5   PRO B CA  1 
ATOM   920  C C   . PRO B 1 5   ? 10.493 8.266   19.758  1.00 84.36  ? 5   PRO B C   1 
ATOM   921  O O   . PRO B 1 5   ? 10.353 7.255   19.063  1.00 82.97  ? 5   PRO B O   1 
ATOM   922  C CB  . PRO B 1 5   ? 10.350 7.911   22.244  1.00 85.44  ? 5   PRO B CB  1 
ATOM   923  C CG  . PRO B 1 5   ? 9.236  7.335   23.061  1.00 91.81  ? 5   PRO B CG  1 
ATOM   924  C CD  . PRO B 1 5   ? 8.240  6.836   22.067  1.00 85.87  ? 5   PRO B CD  1 
ATOM   925  N N   . LYS B 1 6   ? 11.375 9.229   19.485  1.00 84.78  ? 6   LYS B N   1 
ATOM   926  C CA  . LYS B 1 6   ? 12.273 9.121   18.341  1.00 87.72  ? 6   LYS B CA  1 
ATOM   927  C C   . LYS B 1 6   ? 13.132 7.865   18.428  1.00 84.82  ? 6   LYS B C   1 
ATOM   928  O O   . LYS B 1 6   ? 13.450 7.250   17.404  1.00 83.80  ? 6   LYS B O   1 
ATOM   929  C CB  . LYS B 1 6   ? 13.148 10.369  18.237  1.00 93.45  ? 6   LYS B CB  1 
ATOM   930  C CG  . LYS B 1 6   ? 14.101 10.335  17.056  1.00 104.28 ? 6   LYS B CG  1 
ATOM   931  C CD  . LYS B 1 6   ? 15.134 11.453  17.100  1.00 117.07 ? 6   LYS B CD  1 
ATOM   932  C CE  . LYS B 1 6   ? 16.040 11.393  15.871  1.00 115.30 ? 6   LYS B CE  1 
ATOM   933  N NZ  . LYS B 1 6   ? 17.072 12.466  15.846  1.00 112.53 ? 6   LYS B NZ  1 
ATOM   934  N N   . GLU B 1 7   ? 13.547 7.487   19.640  1.00 81.83  ? 7   GLU B N   1 
ATOM   935  C CA  . GLU B 1 7   ? 14.377 6.297   19.787  1.00 79.17  ? 7   GLU B CA  1 
ATOM   936  C C   . GLU B 1 7   ? 13.649 5.046   19.323  1.00 70.43  ? 7   GLU B C   1 
ATOM   937  O O   . GLU B 1 7   ? 14.290 4.077   18.905  1.00 64.31  ? 7   GLU B O   1 
ATOM   938  C CB  . GLU B 1 7   ? 14.803 6.108   21.245  1.00 80.64  ? 7   GLU B CB  1 
ATOM   939  C CG  . GLU B 1 7   ? 15.471 7.307   21.887  1.00 90.92  ? 7   GLU B CG  1 
ATOM   940  C CD  . GLU B 1 7   ? 14.463 8.320   22.401  1.00 98.19  ? 7   GLU B CD  1 
ATOM   941  O OE1 . GLU B 1 7   ? 13.609 7.934   23.230  1.00 96.24  ? 7   GLU B OE1 1 
ATOM   942  O OE2 . GLU B 1 7   ? 14.510 9.491   21.961  1.00 101.19 ? 7   GLU B OE2 1 
ATOM   943  N N   . MET B 1 8   ? 12.317 5.047   19.387  1.00 71.66  ? 8   MET B N   1 
ATOM   944  C CA  . MET B 1 8   ? 11.561 3.850   19.041  1.00 67.52  ? 8   MET B CA  1 
ATOM   945  C C   . MET B 1 8   ? 11.374 3.711   17.538  1.00 62.60  ? 8   MET B C   1 
ATOM   946  O O   . MET B 1 8   ? 11.408 2.594   17.015  1.00 58.48  ? 8   MET B O   1 
ATOM   947  C CB  . MET B 1 8   ? 10.214 3.839   19.766  1.00 67.43  ? 8   MET B CB  1 
ATOM   948  C CG  . MET B 1 8   ? 9.606  2.450   19.858  1.00 70.03  ? 8   MET B CG  1 
ATOM   949  S SD  . MET B 1 8   ? 8.222  2.281   21.002  1.00 73.16  ? 8   MET B SD  1 
ATOM   950  C CE  . MET B 1 8   ? 9.087  2.218   22.565  1.00 72.02  ? 8   MET B CE  1 
ATOM   951  N N   . LEU B 1 9   ? 11.147 4.819   16.828  1.00 68.83  ? 9   LEU B N   1 
ATOM   952  C CA  . LEU B 1 9   ? 11.042 4.736   15.373  1.00 66.10  ? 9   LEU B CA  1 
ATOM   953  C C   . LEU B 1 9   ? 12.373 4.346   14.745  1.00 58.59  ? 9   LEU B C   1 
ATOM   954  O O   . LEU B 1 9   ? 12.402 3.621   13.745  1.00 57.75  ? 9   LEU B O   1 
ATOM   955  C CB  . LEU B 1 9   ? 10.536 6.059   14.786  1.00 75.16  ? 9   LEU B CB  1 
ATOM   956  C CG  . LEU B 1 9   ? 10.387 6.141   13.248  1.00 84.61  ? 9   LEU B CG  1 
ATOM   957  C CD1 . LEU B 1 9   ? 9.433  5.084   12.668  1.00 70.52  ? 9   LEU B CD1 1 
ATOM   958  C CD2 . LEU B 1 9   ? 9.971  7.541   12.777  1.00 81.61  ? 9   LEU B CD2 1 
ATOM   959  N N   . ARG B 1 10  ? 13.485 4.839   15.291  1.00 60.36  ? 10  ARG B N   1 
ATOM   960  C CA  . ARG B 1 10  ? 14.786 4.378   14.824  1.00 60.73  ? 10  ARG B CA  1 
ATOM   961  C C   . ARG B 1 10  ? 14.955 2.885   15.067  1.00 59.53  ? 10  ARG B C   1 
ATOM   962  O O   . ARG B 1 10  ? 15.413 2.149   14.187  1.00 58.59  ? 10  ARG B O   1 
ATOM   963  C CB  . ARG B 1 10  ? 15.903 5.151   15.516  1.00 65.69  ? 10  ARG B CB  1 
ATOM   964  C CG  . ARG B 1 10  ? 16.068 6.583   15.067  1.00 76.36  ? 10  ARG B CG  1 
ATOM   965  C CD  . ARG B 1 10  ? 17.520 6.980   15.251  1.00 94.10  ? 10  ARG B CD  1 
ATOM   966  N NE  . ARG B 1 10  ? 17.714 8.398   15.536  1.00 106.14 ? 10  ARG B NE  1 
ATOM   967  C CZ  . ARG B 1 10  ? 18.901 8.953   15.749  1.00 114.56 ? 10  ARG B CZ  1 
ATOM   968  N NH1 . ARG B 1 10  ? 20.013 8.235   15.725  1.00 113.75 ? 10  ARG B NH1 1 
ATOM   969  N NH2 . ARG B 1 10  ? 18.976 10.259  15.991  1.00 112.71 ? 10  ARG B NH2 1 
ATOM   970  N N   . ALA B 1 11  ? 14.569 2.418   16.252  1.00 56.89  ? 11  ALA B N   1 
ATOM   971  C CA  . ALA B 1 11  ? 14.728 1.009   16.582  1.00 52.48  ? 11  ALA B CA  1 
ATOM   972  C C   . ALA B 1 11  ? 13.861 0.134   15.690  1.00 53.07  ? 11  ALA B C   1 
ATOM   973  O O   . ALA B 1 11  ? 14.274 -0.964  15.299  1.00 46.65  ? 11  ALA B O   1 
ATOM   974  C CB  . ALA B 1 11  ? 14.389 0.780   18.054  1.00 50.13  ? 11  ALA B CB  1 
ATOM   975  N N   . GLN B 1 12  ? 12.645 0.595   15.383  1.00 53.45  ? 12  GLN B N   1 
ATOM   976  C CA  . GLN B 1 12  ? 11.751 -0.166  14.514  1.00 51.82  ? 12  GLN B CA  1 
ATOM   977  C C   . GLN B 1 12  ? 12.282 -0.197  13.082  1.00 46.08  ? 12  GLN B C   1 
ATOM   978  O O   . GLN B 1 12  ? 12.265 -1.246  12.431  1.00 42.16  ? 12  GLN B O   1 
ATOM   979  C CB  . GLN B 1 12  ? 10.339 0.424   14.574  1.00 54.76  ? 12  GLN B CB  1 
ATOM   980  C CG  . GLN B 1 12  ? 9.625  0.253   15.920  1.00 52.84  ? 12  GLN B CG  1 
ATOM   981  C CD  . GLN B 1 12  ? 8.233  0.884   15.939  1.00 61.15  ? 12  GLN B CD  1 
ATOM   982  O OE1 . GLN B 1 12  ? 7.844  1.590   15.006  1.00 52.04  ? 12  GLN B OE1 1 
ATOM   983  N NE2 . GLN B 1 12  ? 7.478  0.628   17.004  1.00 59.50  ? 12  GLN B NE2 1 
ATOM   984  N N   . THR B 1 13  ? 12.768 0.944   12.585  1.00 43.87  ? 13  THR B N   1 
ATOM   985  C CA  . THR B 1 13  ? 13.377 0.996   11.259  1.00 42.23  ? 13  THR B CA  1 
ATOM   986  C C   . THR B 1 13  ? 14.565 0.048   11.144  1.00 44.80  ? 13  THR B C   1 
ATOM   987  O O   . THR B 1 13  ? 14.716 -0.653  10.137  1.00 43.18  ? 13  THR B O   1 
ATOM   988  C CB  . THR B 1 13  ? 13.831 2.423   10.956  1.00 47.00  ? 13  THR B CB  1 
ATOM   989  O OG1 . THR B 1 13  ? 12.704 3.308   10.960  1.00 47.29  ? 13  THR B OG1 1 
ATOM   990  C CG2 . THR B 1 13  ? 14.529 2.487   9.608   1.00 39.54  ? 13  THR B CG2 1 
ATOM   991  N N   . ASN B 1 14  ? 15.425 0.026   12.154  1.00 43.30  ? 14  ASN B N   1 
ATOM   992  C CA  . ASN B 1 14  ? 16.574 -0.867  12.184  1.00 43.03  ? 14  ASN B CA  1 
ATOM   993  C C   . ASN B 1 14  ? 16.169 -2.329  12.070  1.00 43.52  ? 14  ASN B C   1 
ATOM   994  O O   . ASN B 1 14  ? 16.748 -3.085  11.293  1.00 44.21  ? 14  ASN B O   1 
ATOM   995  C CB  . ASN B 1 14  ? 17.368 -0.653  13.472  1.00 51.52  ? 14  ASN B CB  1 
ATOM   996  C CG  . ASN B 1 14  ? 18.822 -0.323  13.214  1.00 52.53  ? 14  ASN B CG  1 
ATOM   997  O OD1 . ASN B 1 14  ? 19.178 0.829   12.957  1.00 55.70  ? 14  ASN B OD1 1 
ATOM   998  N ND2 . ASN B 1 14  ? 19.674 -1.334  13.284  1.00 43.05  ? 14  ASN B ND2 1 
HETATM 999  O O   . HOX B 1 15  ? 14.560 -5.687  11.068  1.00 47.17  ? 15  HOX B O   1 
HETATM 1000 C C   . HOX B 1 15  ? 14.249 -4.594  11.549  1.00 44.99  ? 15  HOX B C   1 
HETATM 1001 N N   . HOX B 1 15  ? 15.172 -2.720  12.858  1.00 44.96  ? 15  HOX B N   1 
HETATM 1002 C CA  . HOX B 1 15  ? 14.707 -4.090  12.916  1.00 45.25  ? 15  HOX B CA  1 
HETATM 1003 C CB  . HOX B 1 15  ? 13.539 -4.262  13.914  1.00 46.33  ? 15  HOX B CB  1 
HETATM 1004 C CG  . HOX B 1 15  ? 13.045 -5.658  14.028  1.00 49.75  ? 15  HOX B CG  1 
HETATM 1005 C CZ  . HOX B 1 15  ? 12.101 -8.310  14.269  1.00 52.33  ? 15  HOX B CZ  1 
HETATM 1006 N NZ  . HOX B 1 15  ? 11.645 -9.622  14.389  1.00 63.12  ? 15  HOX B NZ  1 
HETATM 1007 C CD1 . HOX B 1 15  ? 13.932 -6.712  14.260  1.00 51.17  ? 15  HOX B CD1 1 
HETATM 1008 C CD2 . HOX B 1 15  ? 11.681 -5.944  13.934  1.00 52.98  ? 15  HOX B CD2 1 
HETATM 1009 C CE1 . HOX B 1 15  ? 13.480 -8.019  14.373  1.00 51.46  ? 15  HOX B CE1 1 
HETATM 1010 C CE2 . HOX B 1 15  ? 11.203 -7.243  14.048  1.00 49.38  ? 15  HOX B CE2 1 
ATOM   1011 N N   . ILE B 1 16  ? 13.485 -3.739  10.881  1.00 38.53  ? 16  ILE B N   1 
ATOM   1012 C CA  . ILE B 1 16  ? 12.954 -4.066  9.573   1.00 40.22  ? 16  ILE B CA  1 
ATOM   1013 C C   . ILE B 1 16  ? 14.055 -4.274  8.531   1.00 37.34  ? 16  ILE B C   1 
ATOM   1014 O O   . ILE B 1 16  ? 14.050 -5.264  7.804   1.00 41.22  ? 16  ILE B O   1 
ATOM   1015 C CB  . ILE B 1 16  ? 11.951 -2.990  9.124   1.00 38.27  ? 16  ILE B CB  1 
ATOM   1016 C CG1 . ILE B 1 16  ? 10.722 -3.040  10.038  1.00 36.93  ? 16  ILE B CG1 1 
ATOM   1017 C CG2 . ILE B 1 16  ? 11.575 -3.179  7.646   1.00 33.04  ? 16  ILE B CG2 1 
ATOM   1018 C CD1 . ILE B 1 16  ? 9.642  -2.064  9.697   1.00 33.39  ? 16  ILE B CD1 1 
ATOM   1019 N N   . LEU B 1 17  ? 14.999 -3.345  8.457   1.00 36.91  ? 17  LEU B N   1 
ATOM   1020 C CA  . LEU B 1 17  ? 16.065 -3.463  7.471   1.00 36.36  ? 17  LEU B CA  1 
ATOM   1021 C C   . LEU B 1 17  ? 16.846 -4.759  7.654   1.00 38.51  ? 17  LEU B C   1 
ATOM   1022 O O   . LEU B 1 17  ? 17.121 -5.473  6.686   1.00 37.79  ? 17  LEU B O   1 
ATOM   1023 C CB  . LEU B 1 17  ? 16.991 -2.255  7.558   1.00 36.19  ? 17  LEU B CB  1 
ATOM   1024 C CG  . LEU B 1 17  ? 16.305 -0.991  7.042   1.00 44.64  ? 17  LEU B CG  1 
ATOM   1025 C CD1 . LEU B 1 17  ? 17.223 0.224   7.120   1.00 33.68  ? 17  LEU B CD1 1 
ATOM   1026 C CD2 . LEU B 1 17  ? 15.746 -1.194  5.636   1.00 36.15  ? 17  LEU B CD2 1 
ATOM   1027 N N   . LEU B 1 18  ? 17.203 -5.084  8.898   1.00 38.79  ? 18  LEU B N   1 
ATOM   1028 C CA  . LEU B 1 18  ? 17.991 -6.288  9.148   1.00 41.51  ? 18  LEU B CA  1 
ATOM   1029 C C   . LEU B 1 18  ? 17.205 -7.557  8.839   1.00 43.57  ? 18  LEU B C   1 
ATOM   1030 O O   . LEU B 1 18  ? 17.766 -8.534  8.333   1.00 42.53  ? 18  LEU B O   1 
ATOM   1031 C CB  . LEU B 1 18  ? 18.482 -6.290  10.594  1.00 41.07  ? 18  LEU B CB  1 
ATOM   1032 C CG  . LEU B 1 18  ? 19.714 -5.397  10.728  1.00 39.71  ? 18  LEU B CG  1 
ATOM   1033 C CD1 . LEU B 1 18  ? 20.124 -5.158  12.165  1.00 35.12  ? 18  LEU B CD1 1 
ATOM   1034 C CD2 . LEU B 1 18  ? 20.852 -6.021  9.944   1.00 42.34  ? 18  LEU B CD2 1 
ATOM   1035 N N   . MET B 1 19  ? 15.902 -7.558  9.111   1.00 44.39  ? 19  MET B N   1 
ATOM   1036 C CA  . MET B 1 19  ? 15.093 -8.718  8.762   1.00 42.22  ? 19  MET B CA  1 
ATOM   1037 C C   . MET B 1 19  ? 15.051 -8.918  7.250   1.00 44.47  ? 19  MET B C   1 
ATOM   1038 O O   . MET B 1 19  ? 15.041 -10.055 6.771   1.00 45.21  ? 19  MET B O   1 
ATOM   1039 C CB  . MET B 1 19  ? 13.691 -8.560  9.345   1.00 46.30  ? 19  MET B CB  1 
ATOM   1040 C CG  . MET B 1 19  ? 13.586 -8.871  10.840  1.00 50.33  ? 19  MET B CG  1 
ATOM   1041 S SD  . MET B 1 19  ? 13.988 -10.590 11.242  1.00 57.90  ? 19  MET B SD  1 
ATOM   1042 C CE  . MET B 1 19  ? 12.954 -11.434 10.040  1.00 48.73  ? 19  MET B CE  1 
ATOM   1043 N N   . VAL B 1 20  ? 15.028 -7.822  6.483   1.00 45.11  ? 20  VAL B N   1 
ATOM   1044 C CA  . VAL B 1 20  ? 15.026 -7.925  5.021   1.00 45.25  ? 20  VAL B CA  1 
ATOM   1045 C C   . VAL B 1 20  ? 16.273 -8.651  4.524   1.00 45.71  ? 20  VAL B C   1 
ATOM   1046 O O   . VAL B 1 20  ? 16.187 -9.581  3.713   1.00 46.42  ? 20  VAL B O   1 
ATOM   1047 C CB  . VAL B 1 20  ? 14.892 -6.529  4.381   1.00 40.52  ? 20  VAL B CB  1 
ATOM   1048 C CG1 . VAL B 1 20  ? 15.152 -6.606  2.904   1.00 35.98  ? 20  VAL B CG1 1 
ATOM   1049 C CG2 . VAL B 1 20  ? 13.500 -5.974  4.608   1.00 39.42  ? 20  VAL B CG2 1 
ATOM   1050 N N   . LEU B 1 21  ? 17.454 -8.226  4.985   1.00 44.25  ? 21  LEU B N   1 
ATOM   1051 C CA  . LEU B 1 21  ? 18.685 -8.887  4.556   1.00 48.06  ? 21  LEU B CA  1 
ATOM   1052 C C   . LEU B 1 21  ? 18.734 -10.341 5.011   1.00 48.78  ? 21  LEU B C   1 
ATOM   1053 O O   . LEU B 1 21  ? 19.312 -11.188 4.325   1.00 48.86  ? 21  LEU B O   1 
ATOM   1054 C CB  . LEU B 1 21  ? 19.902 -8.126  5.069   1.00 41.58  ? 21  LEU B CB  1 
ATOM   1055 C CG  . LEU B 1 21  ? 20.147 -6.740  4.475   1.00 41.06  ? 21  LEU B CG  1 
ATOM   1056 C CD1 . LEU B 1 21  ? 21.453 -6.213  5.009   1.00 40.45  ? 21  LEU B CD1 1 
ATOM   1057 C CD2 . LEU B 1 21  ? 20.182 -6.788  2.950   1.00 35.12  ? 21  LEU B CD2 1 
ATOM   1058 N N   . LYS B 1 22  ? 18.112 -10.655 6.143   1.00 50.74  ? 22  LYS B N   1 
ATOM   1059 C CA  . LYS B 1 22  ? 18.029 -12.045 6.565   1.00 49.60  ? 22  LYS B CA  1 
ATOM   1060 C C   . LYS B 1 22  ? 17.199 -12.863 5.581   1.00 57.40  ? 22  LYS B C   1 
ATOM   1061 O O   . LYS B 1 22  ? 17.449 -14.062 5.409   1.00 58.96  ? 22  LYS B O   1 
ATOM   1062 C CB  . LYS B 1 22  ? 17.449 -12.126 7.974   1.00 50.68  ? 22  LYS B CB  1 
ATOM   1063 C CG  . LYS B 1 22  ? 17.622 -13.458 8.635   1.00 50.60  ? 22  LYS B CG  1 
ATOM   1064 C CD  . LYS B 1 22  ? 16.752 -13.555 9.861   1.00 49.10  ? 22  LYS B CD  1 
ATOM   1065 C CE  . LYS B 1 22  ? 16.720 -14.976 10.389  1.00 52.41  ? 22  LYS B CE  1 
ATOM   1066 N NZ  . LYS B 1 22  ? 15.677 -15.143 11.440  1.00 63.93  ? 22  LYS B NZ  1 
ATOM   1067 N N   . GLN B 1 23  ? 16.194 -12.244 4.946   1.00 59.12  ? 23  GLN B N   1 
ATOM   1068 C CA  . GLN B 1 23  ? 15.504 -12.909 3.841   1.00 59.30  ? 23  GLN B CA  1 
ATOM   1069 C C   . GLN B 1 23  ? 16.461 -13.211 2.692   1.00 63.28  ? 23  GLN B C   1 
ATOM   1070 O O   . GLN B 1 23  ? 16.269 -14.197 1.975   1.00 64.30  ? 23  GLN B O   1 
ATOM   1071 C CB  . GLN B 1 23  ? 14.353 -12.057 3.298   1.00 58.40  ? 23  GLN B CB  1 
ATOM   1072 C CG  . GLN B 1 23  ? 13.323 -11.538 4.280   1.00 57.29  ? 23  GLN B CG  1 
ATOM   1073 C CD  . GLN B 1 23  ? 12.481 -12.615 4.896   1.00 73.19  ? 23  GLN B CD  1 
ATOM   1074 O OE1 . GLN B 1 23  ? 12.408 -13.735 4.388   1.00 82.32  ? 23  GLN B OE1 1 
ATOM   1075 N NE2 . GLN B 1 23  ? 11.794 -12.273 5.980   1.00 80.07  ? 23  GLN B NE2 1 
ATOM   1076 N N   . GLY B 1 24  ? 17.466 -12.368 2.482   1.00 58.30  ? 24  GLY B N   1 
ATOM   1077 C CA  . GLY B 1 24  ? 18.439 -12.555 1.418   1.00 54.07  ? 24  GLY B CA  1 
ATOM   1078 C C   . GLY B 1 24  ? 19.085 -11.246 0.998   1.00 52.98  ? 24  GLY B C   1 
ATOM   1079 O O   . GLY B 1 24  ? 18.610 -10.155 1.300   1.00 53.52  ? 24  GLY B O   1 
ATOM   1080 N N   . ASP B 1 25  ? 20.216 -11.369 0.295   1.00 43.95  ? 25  ASP B N   1 
ATOM   1081 C CA  . ASP B 1 25  ? 20.957 -10.205 -0.184  1.00 44.24  ? 25  ASP B CA  1 
ATOM   1082 C C   . ASP B 1 25  ? 20.068 -9.313  -1.046  1.00 47.73  ? 25  ASP B C   1 
ATOM   1083 O O   . ASP B 1 25  ? 19.182 -9.794  -1.754  1.00 44.28  ? 25  ASP B O   1 
ATOM   1084 C CB  . ASP B 1 25  ? 22.175 -10.645 -0.999  1.00 41.03  ? 25  ASP B CB  1 
ATOM   1085 C CG  . ASP B 1 25  ? 23.148 -11.512 -0.202  1.00 47.49  ? 25  ASP B CG  1 
ATOM   1086 O OD1 . ASP B 1 25  ? 22.838 -11.890 0.951   1.00 51.32  ? 25  ASP B OD1 1 
ATOM   1087 O OD2 . ASP B 1 25  ? 24.223 -11.844 -0.745  1.00 47.26  ? 25  ASP B OD2 1 
ATOM   1088 N N   . ASN B 1 26  ? 20.336 -8.004  -1.023  1.00 41.39  ? 26  ASN B N   1 
ATOM   1089 C CA  . ASN B 1 26  ? 19.470 -7.080  -1.740  1.00 43.59  ? 26  ASN B CA  1 
ATOM   1090 C C   . ASN B 1 26  ? 20.182 -5.745  -1.919  1.00 45.80  ? 26  ASN B C   1 
ATOM   1091 O O   . ASN B 1 26  ? 21.271 -5.525  -1.385  1.00 45.27  ? 26  ASN B O   1 
ATOM   1092 C CB  . ASN B 1 26  ? 18.141 -6.905  -1.004  1.00 44.98  ? 26  ASN B CB  1 
ATOM   1093 C CG  . ASN B 1 26  ? 16.999 -6.570  -1.944  1.00 47.14  ? 26  ASN B CG  1 
ATOM   1094 O OD1 . ASN B 1 26  ? 17.199 -5.962  -2.985  1.00 44.99  ? 26  ASN B OD1 1 
ATOM   1095 N ND2 . ASN B 1 26  ? 15.797 -6.994  -1.585  1.00 52.64  ? 26  ASN B ND2 1 
ATOM   1096 N N   . TYR B 1 27  ? 19.553 -4.854  -2.689  1.00 44.54  ? 27  TYR B N   1 
ATOM   1097 C CA  . TYR B 1 27  ? 20.087 -3.523  -2.960  1.00 47.60  ? 27  TYR B CA  1 
ATOM   1098 C C   . TYR B 1 27  ? 19.080 -2.453  -2.548  1.00 49.94  ? 27  TYR B C   1 
ATOM   1099 O O   . TYR B 1 27  ? 17.906 -2.737  -2.309  1.00 49.95  ? 27  TYR B O   1 
ATOM   1100 C CB  . TYR B 1 27  ? 20.482 -3.373  -4.439  1.00 46.19  ? 27  TYR B CB  1 
ATOM   1101 C CG  . TYR B 1 27  ? 19.346 -3.466  -5.431  1.00 47.78  ? 27  TYR B CG  1 
ATOM   1102 C CD1 . TYR B 1 27  ? 18.850 -4.700  -5.849  1.00 49.03  ? 27  TYR B CD1 1 
ATOM   1103 C CD2 . TYR B 1 27  ? 18.796 -2.323  -5.986  1.00 54.90  ? 27  TYR B CD2 1 
ATOM   1104 C CE1 . TYR B 1 27  ? 17.807 -4.783  -6.767  1.00 49.05  ? 27  TYR B CE1 1 
ATOM   1105 C CE2 . TYR B 1 27  ? 17.761 -2.394  -6.913  1.00 57.54  ? 27  TYR B CE2 1 
ATOM   1106 C CZ  . TYR B 1 27  ? 17.270 -3.621  -7.302  1.00 53.10  ? 27  TYR B CZ  1 
ATOM   1107 O OH  . TYR B 1 27  ? 16.241 -3.667  -8.216  1.00 42.69  ? 27  TYR B OH  1 
ATOM   1108 N N   . VAL B 1 28  ? 19.569 -1.206  -2.466  1.00 46.66  ? 28  VAL B N   1 
ATOM   1109 C CA  . VAL B 1 28  ? 18.832 -0.127  -1.803  1.00 44.14  ? 28  VAL B CA  1 
ATOM   1110 C C   . VAL B 1 28  ? 17.493 0.134   -2.483  1.00 47.12  ? 28  VAL B C   1 
ATOM   1111 O O   . VAL B 1 28  ? 16.451 0.248   -1.823  1.00 46.08  ? 28  VAL B O   1 
ATOM   1112 C CB  . VAL B 1 28  ? 19.687 1.150   -1.742  1.00 48.52  ? 28  VAL B CB  1 
ATOM   1113 C CG1 . VAL B 1 28  ? 18.803 2.351   -1.477  1.00 48.86  ? 28  VAL B CG1 1 
ATOM   1114 C CG2 . VAL B 1 28  ? 20.723 1.033   -0.642  1.00 41.51  ? 28  VAL B CG2 1 
ATOM   1115 N N   . TYR B 1 29  ? 17.499 0.274   -3.804  1.00 46.79  ? 29  TYR B N   1 
ATOM   1116 C CA  . TYR B 1 29  ? 16.240 0.523   -4.495  1.00 47.88  ? 29  TYR B CA  1 
ATOM   1117 C C   . TYR B 1 29  ? 15.303 -0.675  -4.380  1.00 49.78  ? 29  TYR B C   1 
ATOM   1118 O O   . TYR B 1 29  ? 14.083 -0.508  -4.286  1.00 51.45  ? 29  TYR B O   1 
ATOM   1119 C CB  . TYR B 1 29  ? 16.506 0.901   -5.948  1.00 52.50  ? 29  TYR B CB  1 
ATOM   1120 C CG  . TYR B 1 29  ? 17.203 2.236   -6.102  1.00 61.91  ? 29  TYR B CG  1 
ATOM   1121 C CD1 . TYR B 1 29  ? 16.935 3.280   -5.225  1.00 62.82  ? 29  TYR B CD1 1 
ATOM   1122 C CD2 . TYR B 1 29  ? 18.126 2.456   -7.122  1.00 69.86  ? 29  TYR B CD2 1 
ATOM   1123 C CE1 . TYR B 1 29  ? 17.559 4.510   -5.357  1.00 70.84  ? 29  TYR B CE1 1 
ATOM   1124 C CE2 . TYR B 1 29  ? 18.759 3.688   -7.264  1.00 70.65  ? 29  TYR B CE2 1 
ATOM   1125 C CZ  . TYR B 1 29  ? 18.471 4.711   -6.377  1.00 77.15  ? 29  TYR B CZ  1 
ATOM   1126 O OH  . TYR B 1 29  ? 19.090 5.939   -6.505  1.00 77.93  ? 29  TYR B OH  1 
ATOM   1127 N N   . GLY B 1 30  ? 15.848 -1.891  -4.377  1.00 46.38  ? 30  GLY B N   1 
ATOM   1128 C CA  . GLY B 1 30  ? 15.015 -3.051  -4.124  1.00 47.19  ? 30  GLY B CA  1 
ATOM   1129 C C   . GLY B 1 30  ? 14.450 -3.092  -2.717  1.00 49.70  ? 30  GLY B C   1 
ATOM   1130 O O   . GLY B 1 30  ? 13.330 -3.569  -2.507  1.00 49.59  ? 30  GLY B O   1 
ATOM   1131 N N   . ILE B 1 31  ? 15.211 -2.602  -1.738  1.00 48.75  ? 31  ILE B N   1 
ATOM   1132 C CA  . ILE B 1 31  ? 14.744 -2.616  -0.354  1.00 49.88  ? 31  ILE B CA  1 
ATOM   1133 C C   . ILE B 1 31  ? 13.594 -1.629  -0.159  1.00 44.15  ? 31  ILE B C   1 
ATOM   1134 O O   . ILE B 1 31  ? 12.611 -1.933  0.522   1.00 43.46  ? 31  ILE B O   1 
ATOM   1135 C CB  . ILE B 1 31  ? 15.921 -2.344  0.605   1.00 43.17  ? 31  ILE B CB  1 
ATOM   1136 C CG1 . ILE B 1 31  ? 16.897 -3.508  0.577   1.00 44.95  ? 31  ILE B CG1 1 
ATOM   1137 C CG2 . ILE B 1 31  ? 15.463 -2.254  2.033   1.00 37.83  ? 31  ILE B CG2 1 
ATOM   1138 C CD1 . ILE B 1 31  ? 18.150 -3.246  1.349   1.00 42.10  ? 31  ILE B CD1 1 
ATOM   1139 N N   . ILE B 1 32  ? 13.693 -0.442  -0.754  1.00 48.80  ? 32  ILE B N   1 
ATOM   1140 C CA  . ILE B 1 32  ? 12.628 0.552   -0.630  1.00 47.01  ? 32  ILE B CA  1 
ATOM   1141 C C   . ILE B 1 32  ? 11.327 0.043   -1.237  1.00 46.84  ? 32  ILE B C   1 
ATOM   1142 O O   . ILE B 1 32  ? 10.257 0.140   -0.626  1.00 47.94  ? 32  ILE B O   1 
ATOM   1143 C CB  . ILE B 1 32  ? 13.062 1.875   -1.275  1.00 48.08  ? 32  ILE B CB  1 
ATOM   1144 C CG1 . ILE B 1 32  ? 14.166 2.522   -0.437  1.00 44.86  ? 32  ILE B CG1 1 
ATOM   1145 C CG2 . ILE B 1 32  ? 11.857 2.786   -1.446  1.00 46.66  ? 32  ILE B CG2 1 
ATOM   1146 C CD1 . ILE B 1 32  ? 14.665 3.828   -1.003  1.00 48.63  ? 32  ILE B CD1 1 
ATOM   1147 N N   . LYS B 1 33  ? 11.398 -0.525  -2.439  1.00 47.38  ? 33  LYS B N   1 
ATOM   1148 C CA  . LYS B 1 33  ? 10.193 -1.019  -3.095  1.00 53.30  ? 33  LYS B CA  1 
ATOM   1149 C C   . LYS B 1 33  ? 9.534  -2.105  -2.257  1.00 52.73  ? 33  LYS B C   1 
ATOM   1150 O O   . LYS B 1 33  ? 8.335  -2.036  -1.963  1.00 50.71  ? 33  LYS B O   1 
ATOM   1151 C CB  . LYS B 1 33  ? 10.540 -1.534  -4.493  1.00 58.43  ? 33  LYS B CB  1 
ATOM   1152 C CG  . LYS B 1 33  ? 9.380  -2.141  -5.284  1.00 75.44  ? 33  LYS B CG  1 
ATOM   1153 C CD  . LYS B 1 33  ? 8.392  -1.089  -5.788  1.00 82.32  ? 33  LYS B CD  1 
ATOM   1154 C CE  . LYS B 1 33  ? 7.353  -1.698  -6.748  1.00 85.63  ? 33  LYS B CE  1 
ATOM   1155 N NZ  . LYS B 1 33  ? 6.344  -2.573  -6.072  1.00 81.36  ? 33  LYS B NZ  1 
ATOM   1156 N N   . GLN B 1 34  ? 10.314 -3.108  -1.849  1.00 53.47  ? 34  GLN B N   1 
ATOM   1157 C CA  . GLN B 1 34  ? 9.773  -4.229  -1.091  1.00 50.95  ? 34  GLN B CA  1 
ATOM   1158 C C   . GLN B 1 34  ? 9.094  -3.758  0.187   1.00 52.34  ? 34  GLN B C   1 
ATOM   1159 O O   . GLN B 1 34  ? 8.054  -4.299  0.577   1.00 56.85  ? 34  GLN B O   1 
ATOM   1160 C CB  . GLN B 1 34  ? 10.887 -5.216  -0.771  1.00 55.64  ? 34  GLN B CB  1 
ATOM   1161 C CG  . GLN B 1 34  ? 11.430 -5.928  -1.991  1.00 61.74  ? 34  GLN B CG  1 
ATOM   1162 C CD  . GLN B 1 34  ? 12.229 -7.161  -1.641  1.00 60.92  ? 34  GLN B CD  1 
ATOM   1163 O OE1 . GLN B 1 34  ? 12.377 -7.507  -0.473  1.00 61.90  ? 34  GLN B OE1 1 
ATOM   1164 N NE2 . GLN B 1 34  ? 12.753 -7.832  -2.657  1.00 67.62  ? 34  GLN B NE2 1 
ATOM   1165 N N   . VAL B 1 35  ? 9.659  -2.748  0.853   1.00 43.88  ? 35  VAL B N   1 
ATOM   1166 C CA  . VAL B 1 35  ? 9.071  -2.300  2.113   1.00 49.70  ? 35  VAL B CA  1 
ATOM   1167 C C   . VAL B 1 35  ? 7.788  -1.517  1.851   1.00 51.23  ? 35  VAL B C   1 
ATOM   1168 O O   . VAL B 1 35  ? 6.793  -1.673  2.570   1.00 44.29  ? 35  VAL B O   1 
ATOM   1169 C CB  . VAL B 1 35  ? 10.098 -1.490  2.926   1.00 49.55  ? 35  VAL B CB  1 
ATOM   1170 C CG1 . VAL B 1 35  ? 9.425  -0.721  4.071   1.00 41.19  ? 35  VAL B CG1 1 
ATOM   1171 C CG2 . VAL B 1 35  ? 11.192 -2.419  3.462   1.00 40.88  ? 35  VAL B CG2 1 
ATOM   1172 N N   . LYS B 1 36  ? 7.783  -0.684  0.807   1.00 50.32  ? 36  LYS B N   1 
ATOM   1173 C CA  . LYS B 1 36  ? 6.605  0.113   0.490   1.00 47.18  ? 36  LYS B CA  1 
ATOM   1174 C C   . LYS B 1 36  ? 5.377  -0.759  0.260   1.00 58.16  ? 36  LYS B C   1 
ATOM   1175 O O   . LYS B 1 36  ? 4.259  -0.397  0.653   1.00 52.86  ? 36  LYS B O   1 
ATOM   1176 C CB  . LYS B 1 36  ? 6.873  0.935   -0.761  1.00 48.26  ? 36  LYS B CB  1 
ATOM   1177 C CG  . LYS B 1 36  ? 5.875  2.047   -1.005  1.00 58.53  ? 36  LYS B CG  1 
ATOM   1178 C CD  . LYS B 1 36  ? 6.262  2.846   -2.244  1.00 61.79  ? 36  LYS B CD  1 
ATOM   1179 C CE  . LYS B 1 36  ? 5.460  4.134   -2.372  1.00 69.68  ? 36  LYS B CE  1 
ATOM   1180 N NZ  . LYS B 1 36  ? 3.987  3.882   -2.454  1.00 75.33  ? 36  LYS B NZ  1 
ATOM   1181 N N   . GLU B 1 37  ? 5.564  -1.913  -0.372  1.00 60.77  ? 37  GLU B N   1 
ATOM   1182 C CA  . GLU B 1 37  ? 4.445  -2.771  -0.710  1.00 55.52  ? 37  GLU B CA  1 
ATOM   1183 C C   . GLU B 1 37  ? 4.075  -3.738  0.403   1.00 53.46  ? 37  GLU B C   1 
ATOM   1184 O O   . GLU B 1 37  ? 2.935  -4.211  0.443   1.00 61.42  ? 37  GLU B O   1 
ATOM   1185 C CB  . GLU B 1 37  ? 4.754  -3.517  -2.013  1.00 63.51  ? 37  GLU B CB  1 
ATOM   1186 C CG  . GLU B 1 37  ? 5.406  -4.872  -1.855  1.00 73.88  ? 37  GLU B CG  1 
ATOM   1187 C CD  . GLU B 1 37  ? 5.736  -5.505  -3.203  1.00 83.21  ? 37  GLU B CD  1 
ATOM   1188 O OE1 . GLU B 1 37  ? 5.411  -4.889  -4.244  1.00 86.78  ? 37  GLU B OE1 1 
ATOM   1189 O OE2 . GLU B 1 37  ? 6.331  -6.607  -3.221  1.00 88.07  ? 37  GLU B OE2 1 
ATOM   1190 N N   . ALA B 1 38  ? 4.987  -4.021  1.323   1.00 51.33  ? 38  ALA B N   1 
ATOM   1191 C CA  . ALA B 1 38  ? 4.626  -4.873  2.444   1.00 52.50  ? 38  ALA B CA  1 
ATOM   1192 C C   . ALA B 1 38  ? 3.904  -4.110  3.545   1.00 52.73  ? 38  ALA B C   1 
ATOM   1193 O O   . ALA B 1 38  ? 3.207  -4.731  4.351   1.00 56.48  ? 38  ALA B O   1 
ATOM   1194 C CB  . ALA B 1 38  ? 5.869  -5.553  3.011   1.00 52.86  ? 38  ALA B CB  1 
ATOM   1195 N N   . SER B 1 39  ? 4.055  -2.790  3.599   1.00 49.92  ? 39  SER B N   1 
ATOM   1196 C CA  . SER B 1 39  ? 3.280  -1.942  4.489   1.00 48.92  ? 39  SER B CA  1 
ATOM   1197 C C   . SER B 1 39  ? 2.051  -1.362  3.802   1.00 54.95  ? 39  SER B C   1 
ATOM   1198 O O   . SER B 1 39  ? 1.417  -0.455  4.346   1.00 51.50  ? 39  SER B O   1 
ATOM   1199 C CB  . SER B 1 39  ? 4.157  -0.814  5.026   1.00 51.05  ? 39  SER B CB  1 
ATOM   1200 O OG  . SER B 1 39  ? 4.504  0.089   3.991   1.00 53.31  ? 39  SER B OG  1 
ATOM   1201 N N   . ASN B 1 40  ? 1.715  -1.857  2.615   1.00 53.93  ? 40  ASN B N   1 
ATOM   1202 C CA  . ASN B 1 40  ? 0.607  -1.338  1.825   1.00 48.66  ? 40  ASN B CA  1 
ATOM   1203 C C   . ASN B 1 40  ? 0.702  0.179   1.691   1.00 50.47  ? 40  ASN B C   1 
ATOM   1204 O O   . ASN B 1 40  ? -0.266 0.916   1.890   1.00 53.81  ? 40  ASN B O   1 
ATOM   1205 C CB  . ASN B 1 40  ? -0.733 -1.774  2.412   1.00 48.93  ? 40  ASN B CB  1 
ATOM   1206 C CG  . ASN B 1 40  ? -0.850 -3.285  2.529   1.00 49.82  ? 40  ASN B CG  1 
ATOM   1207 O OD1 . ASN B 1 40  ? -1.292 -3.804  3.551   1.00 55.88  ? 40  ASN B OD1 1 
ATOM   1208 N ND2 . ASN B 1 40  ? -0.437 -3.997  1.488   1.00 46.13  ? 40  ASN B ND2 1 
ATOM   1209 N N   . GLY B 1 41  ? 1.904  0.641   1.346   1.00 51.19  ? 41  GLY B N   1 
ATOM   1210 C CA  . GLY B 1 41  ? 2.170  2.040   1.108   1.00 49.68  ? 41  GLY B CA  1 
ATOM   1211 C C   . GLY B 1 41  ? 2.489  2.856   2.335   1.00 57.32  ? 41  GLY B C   1 
ATOM   1212 O O   . GLY B 1 41  ? 2.892  4.015   2.193   1.00 60.81  ? 41  GLY B O   1 
ATOM   1213 N N   . GLU B 1 42  ? 2.332  2.297   3.536   1.00 68.61  ? 42  GLU B N   1 
ATOM   1214 C CA  . GLU B 1 42  ? 2.440  3.100   4.750   1.00 67.73  ? 42  GLU B CA  1 
ATOM   1215 C C   . GLU B 1 42  ? 3.869  3.570   4.990   1.00 68.37  ? 42  GLU B C   1 
ATOM   1216 O O   . GLU B 1 42  ? 4.095  4.726   5.365   1.00 74.62  ? 42  GLU B O   1 
ATOM   1217 C CB  . GLU B 1 42  ? 1.926  2.288   5.935   1.00 72.62  ? 42  GLU B CB  1 
ATOM   1218 C CG  . GLU B 1 42  ? 0.416  2.055   5.897   1.00 76.40  ? 42  GLU B CG  1 
ATOM   1219 C CD  . GLU B 1 42  ? -0.071 1.163   7.021   1.00 82.61  ? 42  GLU B CD  1 
ATOM   1220 O OE1 . GLU B 1 42  ? 0.771  0.666   7.804   1.00 81.45  ? 42  GLU B OE1 1 
ATOM   1221 O OE2 . GLU B 1 42  ? -1.297 0.943   7.108   1.00 85.52  ? 42  GLU B OE2 1 
ATOM   1222 N N   . MET B 1 43  ? 4.846  2.694   4.799   1.00 59.42  ? 43  MET B N   1 
ATOM   1223 C CA  . MET B 1 43  ? 6.234  3.004   5.106   1.00 53.59  ? 43  MET B CA  1 
ATOM   1224 C C   . MET B 1 43  ? 7.001  3.129   3.800   1.00 53.14  ? 43  MET B C   1 
ATOM   1225 O O   . MET B 1 43  ? 7.085  2.166   3.029   1.00 54.15  ? 43  MET B O   1 
ATOM   1226 C CB  . MET B 1 43  ? 6.847  1.920   5.991   1.00 50.43  ? 43  MET B CB  1 
ATOM   1227 C CG  . MET B 1 43  ? 8.217  2.247   6.536   1.00 49.22  ? 43  MET B CG  1 
ATOM   1228 S SD  . MET B 1 43  ? 8.721  1.072   7.800   1.00 47.27  ? 43  MET B SD  1 
ATOM   1229 C CE  . MET B 1 43  ? 10.325 1.718   8.255   1.00 45.98  ? 43  MET B CE  1 
ATOM   1230 N N   . GLU B 1 44  ? 7.583  4.298   3.565   1.00 54.44  ? 44  GLU B N   1 
ATOM   1231 C CA  . GLU B 1 44  ? 8.267  4.581   2.307   1.00 56.18  ? 44  GLU B CA  1 
ATOM   1232 C C   . GLU B 1 44  ? 9.602  5.221   2.662   1.00 56.47  ? 44  GLU B C   1 
ATOM   1233 O O   . GLU B 1 44  ? 9.654  6.405   3.004   1.00 61.07  ? 44  GLU B O   1 
ATOM   1234 C CB  . GLU B 1 44  ? 7.427  5.473   1.412   1.00 58.46  ? 44  GLU B CB  1 
ATOM   1235 C CG  . GLU B 1 44  ? 8.091  5.818   0.112   1.00 70.01  ? 44  GLU B CG  1 
ATOM   1236 C CD  . GLU B 1 44  ? 7.265  6.786   -0.707  1.00 85.90  ? 44  GLU B CD  1 
ATOM   1237 O OE1 . GLU B 1 44  ? 6.051  6.911   -0.428  1.00 88.36  ? 44  GLU B OE1 1 
ATOM   1238 O OE2 . GLU B 1 44  ? 7.827  7.417   -1.629  1.00 88.89  ? 44  GLU B OE2 1 
ATOM   1239 N N   . LEU B 1 45  ? 10.678 4.454   2.546   1.00 51.15  ? 45  LEU B N   1 
ATOM   1240 C CA  . LEU B 1 45  ? 11.966 4.885   3.060   1.00 52.75  ? 45  LEU B CA  1 
ATOM   1241 C C   . LEU B 1 45  ? 12.729 5.745   2.065   1.00 53.88  ? 45  LEU B C   1 
ATOM   1242 O O   . LEU B 1 45  ? 12.583 5.614   0.848   1.00 55.51  ? 45  LEU B O   1 
ATOM   1243 C CB  . LEU B 1 45  ? 12.819 3.682   3.456   1.00 52.16  ? 45  LEU B CB  1 
ATOM   1244 C CG  . LEU B 1 45  ? 12.150 2.715   4.420   1.00 41.59  ? 45  LEU B CG  1 
ATOM   1245 C CD1 . LEU B 1 45  ? 13.000 1.497   4.589   1.00 38.47  ? 45  LEU B CD1 1 
ATOM   1246 C CD2 . LEU B 1 45  ? 11.990 3.416   5.725   1.00 45.71  ? 45  LEU B CD2 1 
ATOM   1247 N N   . ASN B 1 46  ? 13.564 6.619   2.613   1.00 53.13  ? 46  ASN B N   1 
ATOM   1248 C CA  . ASN B 1 46  ? 14.342 7.573   1.844   1.00 55.68  ? 46  ASN B CA  1 
ATOM   1249 C C   . ASN B 1 46  ? 15.740 7.019   1.615   1.00 55.88  ? 46  ASN B C   1 
ATOM   1250 O O   . ASN B 1 46  ? 16.345 6.438   2.520   1.00 56.13  ? 46  ASN B O   1 
ATOM   1251 C CB  . ASN B 1 46  ? 14.416 8.913   2.575   1.00 61.92  ? 46  ASN B CB  1 
ATOM   1252 C CG  . ASN B 1 46  ? 15.213 9.951   1.816   1.00 66.86  ? 46  ASN B CG  1 
ATOM   1253 O OD1 . ASN B 1 46  ? 15.260 9.940   0.585   1.00 69.92  ? 46  ASN B OD1 1 
ATOM   1254 N ND2 . ASN B 1 46  ? 15.841 10.863  2.549   1.00 73.20  ? 46  ASN B ND2 1 
ATOM   1255 N N   . GLU B 1 47  ? 16.237 7.203   0.392   1.00 53.97  ? 47  GLU B N   1 
ATOM   1256 C CA  . GLU B 1 47  ? 17.567 6.749   0.006   1.00 49.08  ? 47  GLU B CA  1 
ATOM   1257 C C   . GLU B 1 47  ? 18.613 7.167   1.036   1.00 54.83  ? 47  GLU B C   1 
ATOM   1258 O O   . GLU B 1 47  ? 19.306 6.324   1.613   1.00 55.35  ? 47  GLU B O   1 
ATOM   1259 C CB  . GLU B 1 47  ? 17.887 7.331   -1.371  1.00 53.93  ? 47  GLU B CB  1 
ATOM   1260 C CG  . GLU B 1 47  ? 18.655 6.452   -2.330  1.00 61.72  ? 47  GLU B CG  1 
ATOM   1261 C CD  . GLU B 1 47  ? 18.949 7.162   -3.657  1.00 64.15  ? 47  GLU B CD  1 
ATOM   1262 O OE1 . GLU B 1 47  ? 18.282 8.176   -3.959  1.00 62.62  ? 47  GLU B OE1 1 
ATOM   1263 O OE2 . GLU B 1 47  ? 19.835 6.700   -4.409  1.00 66.78  ? 47  GLU B OE2 1 
ATOM   1264 N N   . ALA B 1 48  ? 18.716 8.472   1.301   1.00 56.02  ? 48  ALA B N   1 
ATOM   1265 C CA  . ALA B 1 48  ? 19.743 8.986   2.203   1.00 53.01  ? 48  ALA B CA  1 
ATOM   1266 C C   . ALA B 1 48  ? 19.656 8.373   3.593   1.00 53.48  ? 48  ALA B C   1 
ATOM   1267 O O   . ALA B 1 48  ? 20.675 8.250   4.286   1.00 54.14  ? 48  ALA B O   1 
ATOM   1268 C CB  . ALA B 1 48  ? 19.636 10.504  2.305   1.00 55.06  ? 48  ALA B CB  1 
ATOM   1269 N N   . THR B 1 49  ? 18.456 7.995   4.022   1.00 50.54  ? 49  THR B N   1 
ATOM   1270 C CA  . THR B 1 49  ? 18.299 7.360   5.322   1.00 44.89  ? 49  THR B CA  1 
ATOM   1271 C C   . THR B 1 49  ? 18.980 6.001   5.356   1.00 48.97  ? 49  THR B C   1 
ATOM   1272 O O   . THR B 1 49  ? 19.749 5.699   6.277   1.00 47.05  ? 49  THR B O   1 
ATOM   1273 C CB  . THR B 1 49  ? 16.819 7.232   5.642   1.00 53.25  ? 49  THR B CB  1 
ATOM   1274 O OG1 . THR B 1 49  ? 16.165 8.453   5.270   1.00 66.57  ? 49  THR B OG1 1 
ATOM   1275 C CG2 . THR B 1 49  ? 16.623 6.980   7.131   1.00 51.84  ? 49  THR B CG2 1 
ATOM   1276 N N   . LEU B 1 50  ? 18.668 5.149   4.382   1.00 47.63  ? 50  LEU B N   1 
ATOM   1277 C CA  . LEU B 1 50  ? 19.301 3.842   4.310   1.00 43.05  ? 50  LEU B CA  1 
ATOM   1278 C C   . LEU B 1 50  ? 20.817 3.966   4.307   1.00 43.56  ? 50  LEU B C   1 
ATOM   1279 O O   . LEU B 1 50  ? 21.505 3.229   5.020   1.00 42.60  ? 50  LEU B O   1 
ATOM   1280 C CB  . LEU B 1 50  ? 18.827 3.108   3.054   1.00 45.25  ? 50  LEU B CB  1 
ATOM   1281 C CG  . LEU B 1 50  ? 17.763 2.018   3.179   1.00 45.47  ? 50  LEU B CG  1 
ATOM   1282 C CD1 . LEU B 1 50  ? 16.492 2.583   3.791   1.00 39.98  ? 50  LEU B CD1 1 
ATOM   1283 C CD2 . LEU B 1 50  ? 17.485 1.397   1.821   1.00 39.79  ? 50  LEU B CD2 1 
ATOM   1284 N N   . TYR B 1 51  ? 21.353 4.923   3.542   1.00 43.06  ? 51  TYR B N   1 
ATOM   1285 C CA  . TYR B 1 51  ? 22.803 5.095   3.490   1.00 45.59  ? 51  TYR B CA  1 
ATOM   1286 C C   . TYR B 1 51  ? 23.381 5.419   4.860   1.00 46.80  ? 51  TYR B C   1 
ATOM   1287 O O   . TYR B 1 51  ? 24.428 4.882   5.238   1.00 45.45  ? 51  TYR B O   1 
ATOM   1288 C CB  . TYR B 1 51  ? 23.205 6.163   2.469   1.00 46.37  ? 51  TYR B CB  1 
ATOM   1289 C CG  . TYR B 1 51  ? 22.835 5.816   1.043   1.00 50.41  ? 51  TYR B CG  1 
ATOM   1290 C CD1 . TYR B 1 51  ? 23.251 4.615   0.474   1.00 50.54  ? 51  TYR B CD1 1 
ATOM   1291 C CD2 . TYR B 1 51  ? 22.134 6.712   0.245   1.00 47.13  ? 51  TYR B CD2 1 
ATOM   1292 C CE1 . TYR B 1 51  ? 22.921 4.293   -0.830  1.00 52.58  ? 51  TYR B CE1 1 
ATOM   1293 C CE2 . TYR B 1 51  ? 21.810 6.405   -1.056  1.00 48.10  ? 51  TYR B CE2 1 
ATOM   1294 C CZ  . TYR B 1 51  ? 22.202 5.198   -1.593  1.00 56.57  ? 51  TYR B CZ  1 
ATOM   1295 O OH  . TYR B 1 51  ? 21.880 4.893   -2.902  1.00 62.28  ? 51  TYR B OH  1 
ATOM   1296 N N   . THR B 1 52  ? 22.723 6.293   5.620   1.00 48.25  ? 52  THR B N   1 
ATOM   1297 C CA  . THR B 1 52  ? 23.233 6.601   6.946   1.00 41.04  ? 52  THR B CA  1 
ATOM   1298 C C   . THR B 1 52  ? 23.300 5.348   7.803   1.00 45.52  ? 52  THR B C   1 
ATOM   1299 O O   . THR B 1 52  ? 24.305 5.110   8.482   1.00 47.90  ? 52  THR B O   1 
ATOM   1300 C CB  . THR B 1 52  ? 22.351 7.645   7.620   1.00 45.41  ? 52  THR B CB  1 
ATOM   1301 O OG1 . THR B 1 52  ? 22.309 8.821   6.811   1.00 53.04  ? 52  THR B OG1 1 
ATOM   1302 C CG2 . THR B 1 52  ? 22.903 7.997   8.996   1.00 52.50  ? 52  THR B CG2 1 
ATOM   1303 N N   . ILE B 1 53  ? 22.258 4.512   7.748   1.00 44.27  ? 53  ILE B N   1 
ATOM   1304 C CA  . ILE B 1 53  ? 22.192 3.348   8.625   1.00 39.95  ? 53  ILE B CA  1 
ATOM   1305 C C   . ILE B 1 53  ? 23.184 2.276   8.195   1.00 41.68  ? 53  ILE B C   1 
ATOM   1306 O O   . ILE B 1 53  ? 23.741 1.560   9.037   1.00 42.40  ? 53  ILE B O   1 
ATOM   1307 C CB  . ILE B 1 53  ? 20.748 2.818   8.666   1.00 40.61  ? 53  ILE B CB  1 
ATOM   1308 C CG1 . ILE B 1 53  ? 19.797 3.955   9.048   1.00 41.49  ? 53  ILE B CG1 1 
ATOM   1309 C CG2 . ILE B 1 53  ? 20.615 1.699   9.673   1.00 39.51  ? 53  ILE B CG2 1 
ATOM   1310 C CD1 . ILE B 1 53  ? 18.419 3.510   9.422   1.00 34.79  ? 53  ILE B CD1 1 
ATOM   1311 N N   . PHE B 1 54  ? 23.449 2.168   6.893   1.00 44.67  ? 54  PHE B N   1 
ATOM   1312 C CA  . PHE B 1 54  ? 24.347 1.137   6.381   1.00 39.58  ? 54  PHE B CA  1 
ATOM   1313 C C   . PHE B 1 54  ? 25.813 1.454   6.671   1.00 40.39  ? 54  PHE B C   1 
ATOM   1314 O O   . PHE B 1 54  ? 26.611 0.541   6.898   1.00 39.94  ? 54  PHE B O   1 
ATOM   1315 C CB  . PHE B 1 54  ? 24.100 0.980   4.880   1.00 39.74  ? 54  PHE B CB  1 
ATOM   1316 C CG  . PHE B 1 54  ? 22.911 0.108   4.546   1.00 39.72  ? 54  PHE B CG  1 
ATOM   1317 C CD1 . PHE B 1 54  ? 22.175 -0.502  5.543   1.00 38.06  ? 54  PHE B CD1 1 
ATOM   1318 C CD2 . PHE B 1 54  ? 22.500 -0.052  3.234   1.00 44.26  ? 54  PHE B CD2 1 
ATOM   1319 C CE1 . PHE B 1 54  ? 21.086 -1.290  5.241   1.00 36.12  ? 54  PHE B CE1 1 
ATOM   1320 C CE2 . PHE B 1 54  ? 21.406 -0.838  2.922   1.00 40.12  ? 54  PHE B CE2 1 
ATOM   1321 C CZ  . PHE B 1 54  ? 20.699 -1.457  3.929   1.00 38.14  ? 54  PHE B CZ  1 
ATOM   1322 N N   . LYS B 1 55  ? 26.175 2.734   6.706   1.00 48.70  ? 55  LYS B N   1 
ATOM   1323 C CA  . LYS B 1 55  ? 27.529 3.119   7.094   1.00 51.67  ? 55  LYS B CA  1 
ATOM   1324 C C   . LYS B 1 55  ? 27.861 2.623   8.499   1.00 55.60  ? 55  LYS B C   1 
ATOM   1325 O O   . LYS B 1 55  ? 28.945 2.079   8.739   1.00 53.72  ? 55  LYS B O   1 
ATOM   1326 C CB  . LYS B 1 55  ? 27.670 4.638   6.998   1.00 52.49  ? 55  LYS B CB  1 
ATOM   1327 C CG  . LYS B 1 55  ? 29.065 5.172   7.237   1.00 57.37  ? 55  LYS B CG  1 
ATOM   1328 C CD  . LYS B 1 55  ? 29.158 6.628   6.781   1.00 57.56  ? 55  LYS B CD  1 
ATOM   1329 C CE  . LYS B 1 55  ? 30.550 7.199   6.974   1.00 58.37  ? 55  LYS B CE  1 
ATOM   1330 N NZ  . LYS B 1 55  ? 30.926 7.276   8.413   1.00 65.29  ? 55  LYS B NZ  1 
ATOM   1331 N N   . ARG B 1 56  ? 26.947 2.838   9.448   1.00 47.95  ? 56  ARG B N   1 
ATOM   1332 C CA  . ARG B 1 56  ? 27.158 2.380   10.817  1.00 44.68  ? 56  ARG B CA  1 
ATOM   1333 C C   . ARG B 1 56  ? 27.230 0.858   10.895  1.00 49.88  ? 56  ARG B C   1 
ATOM   1334 O O   . ARG B 1 56  ? 28.121 0.300   11.548  1.00 50.84  ? 56  ARG B O   1 
ATOM   1335 C CB  . ARG B 1 56  ? 26.047 2.909   11.715  1.00 45.60  ? 56  ARG B CB  1 
ATOM   1336 C CG  . ARG B 1 56  ? 26.170 2.434   13.116  1.00 51.43  ? 56  ARG B CG  1 
ATOM   1337 C CD  . ARG B 1 56  ? 25.489 3.370   14.057  1.00 65.82  ? 56  ARG B CD  1 
ATOM   1338 N NE  . ARG B 1 56  ? 25.889 3.078   15.427  1.00 82.51  ? 56  ARG B NE  1 
ATOM   1339 C CZ  . ARG B 1 56  ? 25.208 2.298   16.255  1.00 84.48  ? 56  ARG B CZ  1 
ATOM   1340 N NH1 . ARG B 1 56  ? 24.068 1.730   15.889  1.00 79.13  ? 56  ARG B NH1 1 
ATOM   1341 N NH2 . ARG B 1 56  ? 25.686 2.080   17.478  1.00 80.35  ? 56  ARG B NH2 1 
ATOM   1342 N N   . LEU B 1 57  ? 26.291 0.168   10.239  1.00 44.84  ? 57  LEU B N   1 
ATOM   1343 C CA  . LEU B 1 57  ? 26.269 -1.291  10.301  1.00 45.38  ? 57  LEU B CA  1 
ATOM   1344 C C   . LEU B 1 57  ? 27.522 -1.895  9.684   1.00 48.24  ? 57  LEU B C   1 
ATOM   1345 O O   . LEU B 1 57  ? 28.069 -2.875  10.200  1.00 48.32  ? 57  LEU B O   1 
ATOM   1346 C CB  . LEU B 1 57  ? 25.031 -1.822  9.588   1.00 40.57  ? 57  LEU B CB  1 
ATOM   1347 C CG  . LEU B 1 57  ? 23.710 -1.488  10.263  1.00 39.99  ? 57  LEU B CG  1 
ATOM   1348 C CD1 . LEU B 1 57  ? 22.590 -1.613  9.278   1.00 40.27  ? 57  LEU B CD1 1 
ATOM   1349 C CD2 . LEU B 1 57  ? 23.492 -2.459  11.387  1.00 43.29  ? 57  LEU B CD2 1 
ATOM   1350 N N   . GLU B 1 58  ? 28.005 -1.316  8.589   1.00 43.99  ? 58  GLU B N   1 
ATOM   1351 C CA  . GLU B 1 58  ? 29.216 -1.838  7.988   1.00 44.27  ? 58  GLU B CA  1 
ATOM   1352 C C   . GLU B 1 58  ? 30.436 -1.522  8.833   1.00 52.70  ? 58  GLU B C   1 
ATOM   1353 O O   . GLU B 1 58  ? 31.396 -2.298  8.840   1.00 48.88  ? 58  GLU B O   1 
ATOM   1354 C CB  . GLU B 1 58  ? 29.390 -1.278  6.585   1.00 46.73  ? 58  GLU B CB  1 
ATOM   1355 C CG  . GLU B 1 58  ? 30.252 -2.162  5.726   1.00 57.07  ? 58  GLU B CG  1 
ATOM   1356 C CD  . GLU B 1 58  ? 30.326 -1.676  4.307   1.00 67.77  ? 58  GLU B CD  1 
ATOM   1357 O OE1 . GLU B 1 58  ? 29.422 -0.908  3.911   1.00 67.94  ? 58  GLU B OE1 1 
ATOM   1358 O OE2 . GLU B 1 58  ? 31.255 -2.094  3.581   1.00 70.56  ? 58  GLU B OE2 1 
ATOM   1359 N N   . LYS B 1 59  ? 30.425 -0.388  9.540   1.00 56.26  ? 59  LYS B N   1 
ATOM   1360 C CA  . LYS B 1 59  ? 31.534 -0.066  10.429  1.00 56.47  ? 59  LYS B CA  1 
ATOM   1361 C C   . LYS B 1 59  ? 31.642 -1.081  11.561  1.00 59.27  ? 59  LYS B C   1 
ATOM   1362 O O   . LYS B 1 59  ? 32.749 -1.435  11.987  1.00 58.89  ? 59  LYS B O   1 
ATOM   1363 C CB  . LYS B 1 59  ? 31.378 1.351   10.990  1.00 57.63  ? 59  LYS B CB  1 
ATOM   1364 C CG  . LYS B 1 59  ? 32.709 1.970   11.397  1.00 68.06  ? 59  LYS B CG  1 
ATOM   1365 C CD  . LYS B 1 59  ? 32.590 2.990   12.522  1.00 82.65  ? 59  LYS B CD  1 
ATOM   1366 C CE  . LYS B 1 59  ? 33.960 3.229   13.169  1.00 89.18  ? 59  LYS B CE  1 
ATOM   1367 N NZ  . LYS B 1 59  ? 33.889 4.054   14.410  1.00 99.11  ? 59  LYS B NZ  1 
ATOM   1368 N N   . ASP B 1 60  ? 30.505 -1.564  12.057  1.00 68.08  ? 60  ASP B N   1 
ATOM   1369 C CA  . ASP B 1 60  ? 30.472 -2.514  13.160  1.00 68.35  ? 60  ASP B CA  1 
ATOM   1370 C C   . ASP B 1 60  ? 30.562 -3.961  12.695  1.00 62.31  ? 60  ASP B C   1 
ATOM   1371 O O   . ASP B 1 60  ? 30.332 -4.866  13.498  1.00 65.13  ? 60  ASP B O   1 
ATOM   1372 C CB  . ASP B 1 60  ? 29.190 -2.328  13.982  1.00 64.04  ? 60  ASP B CB  1 
ATOM   1373 C CG  . ASP B 1 60  ? 28.945 -0.880  14.371  1.00 69.00  ? 60  ASP B CG  1 
ATOM   1374 O OD1 . ASP B 1 60  ? 29.874 -0.058  14.227  1.00 71.03  ? 60  ASP B OD1 1 
ATOM   1375 O OD2 . ASP B 1 60  ? 27.812 -0.563  14.804  1.00 69.94  ? 60  ASP B OD2 1 
ATOM   1376 N N   . GLY B 1 61  ? 30.880 -4.198  11.424  1.00 51.60  ? 61  GLY B N   1 
ATOM   1377 C CA  . GLY B 1 61  ? 31.025 -5.548  10.922  1.00 51.29  ? 61  GLY B CA  1 
ATOM   1378 C C   . GLY B 1 61  ? 29.755 -6.360  10.838  1.00 54.75  ? 61  GLY B C   1 
ATOM   1379 O O   . GLY B 1 61  ? 29.826 -7.591  10.832  1.00 62.89  ? 61  GLY B O   1 
ATOM   1380 N N   . ILE B 1 62  ? 28.592 -5.717  10.768  1.00 53.15  ? 62  ILE B N   1 
ATOM   1381 C CA  . ILE B 1 62  ? 27.332 -6.458  10.757  1.00 52.75  ? 62  ILE B CA  1 
ATOM   1382 C C   . ILE B 1 62  ? 26.900 -6.856  9.346   1.00 54.18  ? 62  ILE B C   1 
ATOM   1383 O O   . ILE B 1 62  ? 26.287 -7.914  9.164   1.00 51.21  ? 62  ILE B O   1 
ATOM   1384 C CB  . ILE B 1 62  ? 26.232 -5.640  11.456  1.00 51.67  ? 62  ILE B CB  1 
ATOM   1385 C CG1 . ILE B 1 62  ? 26.565 -5.422  12.932  1.00 52.17  ? 62  ILE B CG1 1 
ATOM   1386 C CG2 . ILE B 1 62  ? 24.893 -6.331  11.346  1.00 45.70  ? 62  ILE B CG2 1 
ATOM   1387 C CD1 . ILE B 1 62  ? 26.652 -6.693  13.719  1.00 57.05  ? 62  ILE B CD1 1 
ATOM   1388 N N   . ILE B 1 63  ? 27.209 -6.027  8.342   1.00 53.99  ? 63  ILE B N   1 
ATOM   1389 C CA  . ILE B 1 63  ? 26.874 -6.288  6.948   1.00 48.88  ? 63  ILE B CA  1 
ATOM   1390 C C   . ILE B 1 63  ? 28.090 -5.960  6.097   1.00 47.95  ? 63  ILE B C   1 
ATOM   1391 O O   . ILE B 1 63  ? 29.020 -5.287  6.542   1.00 50.47  ? 63  ILE B O   1 
ATOM   1392 C CB  . ILE B 1 63  ? 25.641 -5.481  6.472   1.00 41.52  ? 63  ILE B CB  1 
ATOM   1393 C CG1 . ILE B 1 63  ? 25.893 -3.982  6.591   1.00 40.79  ? 63  ILE B CG1 1 
ATOM   1394 C CG2 . ILE B 1 63  ? 24.398 -5.886  7.226   1.00 40.50  ? 63  ILE B CG2 1 
ATOM   1395 C CD1 . ILE B 1 63  ? 24.839 -3.138  5.897   1.00 39.58  ? 63  ILE B CD1 1 
ATOM   1396 N N   . SER B 1 64  ? 28.084 -6.454  4.863   1.00 43.36  ? 64  SER B N   1 
ATOM   1397 C CA  . SER B 1 64  ? 29.130 -6.126  3.908   1.00 46.77  ? 64  SER B CA  1 
ATOM   1398 C C   . SER B 1 64  ? 28.513 -6.031  2.522   1.00 47.36  ? 64  SER B C   1 
ATOM   1399 O O   . SER B 1 64  ? 27.383 -6.468  2.294   1.00 47.64  ? 64  SER B O   1 
ATOM   1400 C CB  . SER B 1 64  ? 30.260 -7.167  3.912   1.00 49.12  ? 64  SER B CB  1 
ATOM   1401 O OG  . SER B 1 64  ? 29.989 -8.243  3.022   1.00 45.92  ? 64  SER B OG  1 
ATOM   1402 N N   . SER B 1 65  ? 29.285 -5.491  1.579   1.00 44.22  ? 65  SER B N   1 
ATOM   1403 C CA  . SER B 1 65  ? 28.775 -5.177  0.255   1.00 41.86  ? 65  SER B CA  1 
ATOM   1404 C C   . SER B 1 65  ? 29.680 -5.748  -0.827  1.00 45.16  ? 65  SER B C   1 
ATOM   1405 O O   . SER B 1 65  ? 30.849 -6.060  -0.594  1.00 49.51  ? 65  SER B O   1 
ATOM   1406 C CB  . SER B 1 65  ? 28.623 -3.667  0.077   1.00 52.36  ? 65  SER B CB  1 
ATOM   1407 O OG  . SER B 1 65  ? 29.839 -2.991  0.343   1.00 51.69  ? 65  SER B OG  1 
ATOM   1408 N N   . TYR B 1 66  ? 29.112 -5.889  -2.023  1.00 43.92  ? 66  TYR B N   1 
ATOM   1409 C CA  . TYR B 1 66  ? 29.846 -6.400  -3.169  1.00 44.50  ? 66  TYR B CA  1 
ATOM   1410 C C   . TYR B 1 66  ? 29.110 -6.015  -4.446  1.00 46.55  ? 66  TYR B C   1 
ATOM   1411 O O   . TYR B 1 66  ? 27.956 -5.588  -4.418  1.00 45.54  ? 66  TYR B O   1 
ATOM   1412 C CB  . TYR B 1 66  ? 30.034 -7.916  -3.064  1.00 53.03  ? 66  TYR B CB  1 
ATOM   1413 C CG  . TYR B 1 66  ? 28.734 -8.689  -3.118  1.00 48.32  ? 66  TYR B CG  1 
ATOM   1414 C CD1 . TYR B 1 66  ? 28.176 -9.061  -4.330  1.00 50.43  ? 66  TYR B CD1 1 
ATOM   1415 C CD2 . TYR B 1 66  ? 28.075 -9.054  -1.961  1.00 44.36  ? 66  TYR B CD2 1 
ATOM   1416 C CE1 . TYR B 1 66  ? 26.997 -9.750  -4.389  1.00 46.79  ? 66  TYR B CE1 1 
ATOM   1417 C CE2 . TYR B 1 66  ? 26.892 -9.756  -2.014  1.00 42.29  ? 66  TYR B CE2 1 
ATOM   1418 C CZ  . TYR B 1 66  ? 26.358 -10.093 -3.232  1.00 44.43  ? 66  TYR B CZ  1 
ATOM   1419 O OH  . TYR B 1 66  ? 25.175 -10.791 -3.302  1.00 49.70  ? 66  TYR B OH  1 
ATOM   1420 N N   . TRP B 1 67  ? 29.789 -6.209  -5.571  1.00 52.29  ? 67  TRP B N   1 
ATOM   1421 C CA  . TRP B 1 67  ? 29.297 -5.834  -6.888  1.00 55.86  ? 67  TRP B CA  1 
ATOM   1422 C C   . TRP B 1 67  ? 28.552 -6.991  -7.525  1.00 60.20  ? 67  TRP B C   1 
ATOM   1423 O O   . TRP B 1 67  ? 28.894 -8.155  -7.314  1.00 58.97  ? 67  TRP B O   1 
ATOM   1424 C CB  . TRP B 1 67  ? 30.437 -5.423  -7.822  1.00 60.83  ? 67  TRP B CB  1 
ATOM   1425 C CG  . TRP B 1 67  ? 30.996 -4.091  -7.534  1.00 64.59  ? 67  TRP B CG  1 
ATOM   1426 C CD1 . TRP B 1 67  ? 32.171 -3.808  -6.906  1.00 66.53  ? 67  TRP B CD1 1 
ATOM   1427 C CD2 . TRP B 1 67  ? 30.367 -2.837  -7.800  1.00 69.02  ? 67  TRP B CD2 1 
ATOM   1428 N NE1 . TRP B 1 67  ? 32.331 -2.448  -6.798  1.00 66.17  ? 67  TRP B NE1 1 
ATOM   1429 C CE2 . TRP B 1 67  ? 31.232 -1.830  -7.336  1.00 70.08  ? 67  TRP B CE2 1 
ATOM   1430 C CE3 . TRP B 1 67  ? 29.156 -2.467  -8.398  1.00 65.88  ? 67  TRP B CE3 1 
ATOM   1431 C CZ2 . TRP B 1 67  ? 30.928 -0.479  -7.453  1.00 70.57  ? 67  TRP B CZ2 1 
ATOM   1432 C CZ3 . TRP B 1 67  ? 28.859 -1.131  -8.516  1.00 67.71  ? 67  TRP B CZ3 1 
ATOM   1433 C CH2 . TRP B 1 67  ? 29.739 -0.150  -8.048  1.00 70.62  ? 67  TRP B CH2 1 
ATOM   1434 N N   . GLY B 1 68  ? 27.533 -6.667  -8.314  1.00 61.82  ? 68  GLY B N   1 
ATOM   1435 C CA  . GLY B 1 68  ? 26.803 -7.664  -9.076  1.00 72.77  ? 68  GLY B CA  1 
ATOM   1436 C C   . GLY B 1 68  ? 27.052 -7.458  -10.559 1.00 89.20  ? 68  GLY B C   1 
ATOM   1437 O O   . GLY B 1 68  ? 27.335 -6.343  -11.002 1.00 95.07  ? 68  GLY B O   1 
ATOM   1438 N N   . ASP B 1 69  ? 26.964 -8.549  -11.325 1.00 95.72  ? 69  ASP B N   1 
ATOM   1439 C CA  . ASP B 1 69  ? 27.163 -8.547  -12.777 1.00 99.57  ? 69  ASP B CA  1 
ATOM   1440 C C   . ASP B 1 69  ? 28.528 -8.013  -13.193 1.00 107.21 ? 69  ASP B C   1 
ATOM   1441 O O   . ASP B 1 69  ? 28.714 -7.637  -14.354 1.00 122.32 ? 69  ASP B O   1 
ATOM   1442 C CB  . ASP B 1 69  ? 26.075 -7.744  -13.497 1.00 101.91 ? 69  ASP B CB  1 
ATOM   1443 C CG  . ASP B 1 69  ? 24.767 -8.482  -13.579 1.00 107.14 ? 69  ASP B CG  1 
ATOM   1444 O OD1 . ASP B 1 69  ? 24.284 -8.952  -12.525 1.00 104.91 ? 69  ASP B OD1 1 
ATOM   1445 O OD2 . ASP B 1 69  ? 24.223 -8.581  -14.700 1.00 101.84 ? 69  ASP B OD2 1 
ATOM   1446 N N   . GLU B 1 70  ? 29.501 -7.982  -12.289 1.00 96.00  ? 70  GLU B N   1 
ATOM   1447 C CA  . GLU B 1 70  ? 30.790 -7.391  -12.630 1.00 96.81  ? 70  GLU B CA  1 
ATOM   1448 C C   . GLU B 1 70  ? 31.630 -8.339  -13.474 1.00 96.01  ? 70  GLU B C   1 
ATOM   1449 O O   . GLU B 1 70  ? 32.124 -7.956  -14.533 1.00 94.83  ? 70  GLU B O   1 
ATOM   1450 C CB  . GLU B 1 70  ? 31.560 -6.998  -11.372 1.00 87.99  ? 70  GLU B CB  1 
ATOM   1451 C CG  . GLU B 1 70  ? 32.863 -6.287  -11.674 1.00 94.63  ? 70  GLU B CG  1 
ATOM   1452 C CD  . GLU B 1 70  ? 33.729 -6.092  -10.450 1.00 96.74  ? 70  GLU B CD  1 
ATOM   1453 O OE1 . GLU B 1 70  ? 33.370 -6.615  -9.372  1.00 89.65  ? 70  GLU B OE1 1 
ATOM   1454 O OE2 . GLU B 1 70  ? 34.761 -5.396  -10.566 1.00 105.13 ? 70  GLU B OE2 1 
ATOM   1455 N N   . ARG B 1 75  ? 27.600 -3.123  -11.863 1.00 85.06  ? 75  ARG B N   1 
ATOM   1456 C CA  . ARG B 1 75  ? 26.824 -1.886  -11.896 1.00 90.59  ? 75  ARG B CA  1 
ATOM   1457 C C   . ARG B 1 75  ? 26.104 -1.606  -10.578 1.00 85.50  ? 75  ARG B C   1 
ATOM   1458 O O   . ARG B 1 75  ? 26.244 -0.525  -9.998  1.00 77.41  ? 75  ARG B O   1 
ATOM   1459 C CB  . ARG B 1 75  ? 25.796 -1.932  -13.022 1.00 94.88  ? 75  ARG B CB  1 
ATOM   1460 C CG  . ARG B 1 75  ? 26.373 -2.304  -14.353 1.00 107.11 ? 75  ARG B CG  1 
ATOM   1461 C CD  . ARG B 1 75  ? 25.362 -2.101  -15.456 1.00 116.40 ? 75  ARG B CD  1 
ATOM   1462 N NE  . ARG B 1 75  ? 26.037 -1.970  -16.740 1.00 130.83 ? 75  ARG B NE  1 
ATOM   1463 C CZ  . ARG B 1 75  ? 26.300 -2.980  -17.556 1.00 124.79 ? 75  ARG B CZ  1 
ATOM   1464 N NH1 . ARG B 1 75  ? 25.938 -4.219  -17.264 1.00 124.04 ? 75  ARG B NH1 1 
ATOM   1465 N NH2 . ARG B 1 75  ? 26.954 -2.744  -18.689 1.00 126.31 ? 75  ARG B NH2 1 
ATOM   1466 N N   . ARG B 1 76  ? 25.370 -2.600  -10.083 1.00 75.98  ? 76  ARG B N   1 
ATOM   1467 C CA  . ARG B 1 76  ? 24.529 -2.419  -8.915  1.00 62.52  ? 76  ARG B CA  1 
ATOM   1468 C C   . ARG B 1 76  ? 25.277 -2.938  -7.699  1.00 61.71  ? 76  ARG B C   1 
ATOM   1469 O O   . ARG B 1 76  ? 26.102 -3.849  -7.795  1.00 72.69  ? 76  ARG B O   1 
ATOM   1470 C CB  . ARG B 1 76  ? 23.192 -3.153  -9.081  1.00 56.29  ? 76  ARG B CB  1 
ATOM   1471 C CG  . ARG B 1 76  ? 22.037 -2.497  -8.351  1.00 59.13  ? 76  ARG B CG  1 
ATOM   1472 C CD  . ARG B 1 76  ? 20.669 -2.930  -8.877  1.00 62.42  ? 76  ARG B CD  1 
ATOM   1473 N NE  . ARG B 1 76  ? 20.379 -2.402  -10.205 1.00 69.89  ? 76  ARG B NE  1 
ATOM   1474 C CZ  . ARG B 1 76  ? 19.604 -1.355  -10.456 1.00 74.95  ? 76  ARG B CZ  1 
ATOM   1475 N NH1 . ARG B 1 76  ? 19.007 -0.687  -9.483  1.00 72.82  ? 76  ARG B NH1 1 
ATOM   1476 N NH2 . ARG B 1 76  ? 19.431 -0.962  -11.715 1.00 83.59  ? 76  ARG B NH2 1 
ATOM   1477 N N   . LYS B 1 77  ? 24.992 -2.343  -6.553  1.00 54.63  ? 77  LYS B N   1 
ATOM   1478 C CA  . LYS B 1 77  ? 25.682 -2.680  -5.323  1.00 46.55  ? 77  LYS B CA  1 
ATOM   1479 C C   . LYS B 1 77  ? 24.742 -3.443  -4.403  1.00 49.43  ? 77  LYS B C   1 
ATOM   1480 O O   . LYS B 1 77  ? 23.657 -2.955  -4.066  1.00 48.72  ? 77  LYS B O   1 
ATOM   1481 C CB  . LYS B 1 77  ? 26.207 -1.414  -4.660  1.00 39.49  ? 77  LYS B CB  1 
ATOM   1482 C CG  . LYS B 1 77  ? 27.180 -1.661  -3.550  1.00 47.35  ? 77  LYS B CG  1 
ATOM   1483 C CD  . LYS B 1 77  ? 27.691 -0.348  -3.006  1.00 51.95  ? 77  LYS B CD  1 
ATOM   1484 C CE  . LYS B 1 77  ? 28.669 -0.556  -1.863  1.00 64.32  ? 77  LYS B CE  1 
ATOM   1485 N NZ  . LYS B 1 77  ? 29.213 0.740   -1.341  1.00 68.23  ? 77  LYS B NZ  1 
ATOM   1486 N N   . TYR B 1 78  ? 25.167 -4.626  -3.989  1.00 44.40  ? 78  TYR B N   1 
ATOM   1487 C CA  . TYR B 1 78  ? 24.375 -5.470  -3.116  1.00 45.71  ? 78  TYR B CA  1 
ATOM   1488 C C   . TYR B 1 78  ? 24.907 -5.408  -1.692  1.00 43.46  ? 78  TYR B C   1 
ATOM   1489 O O   . TYR B 1 78  ? 26.025 -4.953  -1.445  1.00 45.38  ? 78  TYR B O   1 
ATOM   1490 C CB  . TYR B 1 78  ? 24.378 -6.914  -3.617  1.00 45.25  ? 78  TYR B CB  1 
ATOM   1491 C CG  . TYR B 1 78  ? 23.472 -7.163  -4.797  1.00 44.93  ? 78  TYR B CG  1 
ATOM   1492 C CD1 . TYR B 1 78  ? 23.826 -6.764  -6.081  1.00 48.49  ? 78  TYR B CD1 1 
ATOM   1493 C CD2 . TYR B 1 78  ? 22.261 -7.812  -4.626  1.00 47.25  ? 78  TYR B CD2 1 
ATOM   1494 C CE1 . TYR B 1 78  ? 22.985 -7.008  -7.164  1.00 52.15  ? 78  TYR B CE1 1 
ATOM   1495 C CE2 . TYR B 1 78  ? 21.415 -8.054  -5.694  1.00 50.59  ? 78  TYR B CE2 1 
ATOM   1496 C CZ  . TYR B 1 78  ? 21.778 -7.655  -6.954  1.00 55.54  ? 78  TYR B CZ  1 
ATOM   1497 O OH  . TYR B 1 78  ? 20.919 -7.911  -7.992  1.00 53.30  ? 78  TYR B OH  1 
ATOM   1498 N N   . TYR B 1 79  ? 24.065 -5.850  -0.753  1.00 40.13  ? 79  TYR B N   1 
ATOM   1499 C CA  . TYR B 1 79  ? 24.381 -5.893  0.667   1.00 39.93  ? 79  TYR B CA  1 
ATOM   1500 C C   . TYR B 1 79  ? 24.010 -7.256  1.238   1.00 42.79  ? 79  TYR B C   1 
ATOM   1501 O O   . TYR B 1 79  ? 23.033 -7.879  0.813   1.00 43.18  ? 79  TYR B O   1 
ATOM   1502 C CB  . TYR B 1 79  ? 23.649 -4.790  1.427   1.00 38.10  ? 79  TYR B CB  1 
ATOM   1503 C CG  . TYR B 1 79  ? 24.183 -3.409  1.140   1.00 44.63  ? 79  TYR B CG  1 
ATOM   1504 C CD1 . TYR B 1 79  ? 23.783 -2.715  0.013   1.00 48.26  ? 79  TYR B CD1 1 
ATOM   1505 C CD2 . TYR B 1 79  ? 25.096 -2.800  1.992   1.00 47.30  ? 79  TYR B CD2 1 
ATOM   1506 C CE1 . TYR B 1 79  ? 24.278 -1.459  -0.262  1.00 44.84  ? 79  TYR B CE1 1 
ATOM   1507 C CE2 . TYR B 1 79  ? 25.592 -1.547  1.727   1.00 43.62  ? 79  TYR B CE2 1 
ATOM   1508 C CZ  . TYR B 1 79  ? 25.182 -0.884  0.596   1.00 44.29  ? 79  TYR B CZ  1 
ATOM   1509 O OH  . TYR B 1 79  ? 25.668 0.370   0.322   1.00 52.32  ? 79  TYR B OH  1 
ATOM   1510 N N   . ARG B 1 80  ? 24.791 -7.710  2.218   1.00 42.55  ? 80  ARG B N   1 
ATOM   1511 C CA  . ARG B 1 80  ? 24.634 -9.043  2.785   1.00 44.99  ? 80  ARG B CA  1 
ATOM   1512 C C   . ARG B 1 80  ? 24.888 -9.029  4.287   1.00 40.22  ? 80  ARG B C   1 
ATOM   1513 O O   . ARG B 1 80  ? 25.762 -8.312  4.781   1.00 42.48  ? 80  ARG B O   1 
ATOM   1514 C CB  . ARG B 1 80  ? 25.576 -10.049 2.116   1.00 41.91  ? 80  ARG B CB  1 
ATOM   1515 C CG  . ARG B 1 80  ? 27.036 -9.662  2.175   1.00 44.42  ? 80  ARG B CG  1 
ATOM   1516 C CD  . ARG B 1 80  ? 27.911 -10.757 1.595   1.00 50.59  ? 80  ARG B CD  1 
ATOM   1517 N NE  . ARG B 1 80  ? 27.870 -11.971 2.406   1.00 52.72  ? 80  ARG B NE  1 
ATOM   1518 C CZ  . ARG B 1 80  ? 28.718 -12.235 3.391   1.00 51.53  ? 80  ARG B CZ  1 
ATOM   1519 N NH1 . ARG B 1 80  ? 29.690 -11.397 3.711   1.00 52.57  ? 80  ARG B NH1 1 
ATOM   1520 N NH2 . ARG B 1 80  ? 28.583 -13.365 4.074   1.00 51.17  ? 80  ARG B NH2 1 
ATOM   1521 N N   . LEU B 1 81  ? 24.123 -9.830  5.008   1.00 43.23  ? 81  LEU B N   1 
ATOM   1522 C CA  . LEU B 1 81  ? 24.271 -9.929  6.450   1.00 46.80  ? 81  LEU B CA  1 
ATOM   1523 C C   . LEU B 1 81  ? 25.434 -10.872 6.771   1.00 52.18  ? 81  LEU B C   1 
ATOM   1524 O O   . LEU B 1 81  ? 25.462 -12.014 6.303   1.00 50.18  ? 81  LEU B O   1 
ATOM   1525 C CB  . LEU B 1 81  ? 22.950 -10.414 7.054   1.00 43.14  ? 81  LEU B CB  1 
ATOM   1526 C CG  . LEU B 1 81  ? 22.755 -10.366 8.568   1.00 55.51  ? 81  LEU B CG  1 
ATOM   1527 C CD1 . LEU B 1 81  ? 22.961 -8.950  9.062   1.00 59.61  ? 81  LEU B CD1 1 
ATOM   1528 C CD2 . LEU B 1 81  ? 21.370 -10.860 8.964   1.00 50.81  ? 81  LEU B CD2 1 
ATOM   1529 N N   . THR B 1 82  ? 26.399 -10.395 7.563   1.00 53.62  ? 82  THR B N   1 
ATOM   1530 C CA  . THR B 1 82  ? 27.622 -11.147 7.814   1.00 58.45  ? 82  THR B CA  1 
ATOM   1531 C C   . THR B 1 82  ? 27.404 -12.302 8.786   1.00 66.29  ? 82  THR B C   1 
ATOM   1532 O O   . THR B 1 82  ? 26.308 -12.534 9.304   1.00 68.43  ? 82  THR B O   1 
ATOM   1533 C CB  . THR B 1 82  ? 28.723 -10.246 8.371   1.00 57.44  ? 82  THR B CB  1 
ATOM   1534 O OG1 . THR B 1 82  ? 28.373 -9.820  9.697   1.00 62.12  ? 82  THR B OG1 1 
ATOM   1535 C CG2 . THR B 1 82  ? 28.951 -9.054  7.481   1.00 54.67  ? 82  THR B CG2 1 
ATOM   1536 N N   . GLU B 1 83  ? 28.508 -12.995 9.077   1.00 60.53  ? 83  GLU B N   1 
ATOM   1537 C CA  . GLU B 1 83  ? 28.504 -14.066 10.067  1.00 64.72  ? 83  GLU B CA  1 
ATOM   1538 C C   . GLU B 1 83  ? 28.092 -13.541 11.433  1.00 63.52  ? 83  GLU B C   1 
ATOM   1539 O O   . GLU B 1 83  ? 27.146 -14.042 12.049  1.00 63.89  ? 83  GLU B O   1 
ATOM   1540 C CB  . GLU B 1 83  ? 29.897 -14.695 10.123  1.00 70.40  ? 83  GLU B CB  1 
ATOM   1541 C CG  . GLU B 1 83  ? 30.082 -15.863 9.179   1.00 76.73  ? 83  GLU B CG  1 
ATOM   1542 C CD  . GLU B 1 83  ? 31.204 -16.804 9.591   1.00 76.27  ? 83  GLU B CD  1 
ATOM   1543 O OE1 . GLU B 1 83  ? 31.476 -16.933 10.807  1.00 76.79  ? 83  GLU B OE1 1 
ATOM   1544 O OE2 . GLU B 1 83  ? 31.796 -17.434 8.684   1.00 67.73  ? 83  GLU B OE2 1 
ATOM   1545 N N   . ILE B 1 84  ? 28.819 -12.541 11.931  1.00 63.59  ? 84  ILE B N   1 
ATOM   1546 C CA  . ILE B 1 84  ? 28.467 -11.891 13.191  1.00 69.00  ? 84  ILE B CA  1 
ATOM   1547 C C   . ILE B 1 84  ? 27.019 -11.433 13.185  1.00 67.91  ? 84  ILE B C   1 
ATOM   1548 O O   . ILE B 1 84  ? 26.297 -11.592 14.178  1.00 67.07  ? 84  ILE B O   1 
ATOM   1549 C CB  . ILE B 1 84  ? 29.413 -10.708 13.462  1.00 68.90  ? 84  ILE B CB  1 
ATOM   1550 C CG1 . ILE B 1 84  ? 30.866 -11.089 13.155  1.00 72.40  ? 84  ILE B CG1 1 
ATOM   1551 C CG2 . ILE B 1 84  ? 29.219 -10.193 14.876  1.00 70.76  ? 84  ILE B CG2 1 
ATOM   1552 C CD1 . ILE B 1 84  ? 31.336 -10.669 11.760  1.00 75.25  ? 84  ILE B CD1 1 
ATOM   1553 N N   . GLY B 1 85  ? 26.572 -10.869 12.058  1.00 64.25  ? 85  GLY B N   1 
ATOM   1554 C CA  . GLY B 1 85  ? 25.220 -10.335 11.985  1.00 64.20  ? 85  GLY B CA  1 
ATOM   1555 C C   . GLY B 1 85  ? 24.169 -11.368 12.327  1.00 64.56  ? 85  GLY B C   1 
ATOM   1556 O O   . GLY B 1 85  ? 23.253 -11.111 13.110  1.00 64.99  ? 85  GLY B O   1 
ATOM   1557 N N   . HIS B 1 86  ? 24.288 -12.551 11.739  1.00 65.53  ? 86  HIS B N   1 
ATOM   1558 C CA  . HIS B 1 86  ? 23.340 -13.613 12.030  1.00 66.59  ? 86  HIS B CA  1 
ATOM   1559 C C   . HIS B 1 86  ? 23.348 -13.966 13.511  1.00 64.80  ? 86  HIS B C   1 
ATOM   1560 O O   . HIS B 1 86  ? 22.312 -14.335 14.070  1.00 62.60  ? 86  HIS B O   1 
ATOM   1561 C CB  . HIS B 1 86  ? 23.679 -14.826 11.173  1.00 61.22  ? 86  HIS B CB  1 
ATOM   1562 C CG  . HIS B 1 86  ? 23.092 -14.773 9.798   1.00 60.46  ? 86  HIS B CG  1 
ATOM   1563 N ND1 . HIS B 1 86  ? 23.820 -14.374 8.698   1.00 55.41  ? 86  HIS B ND1 1 
ATOM   1564 C CD2 . HIS B 1 86  ? 21.858 -15.088 9.339   1.00 56.94  ? 86  HIS B CD2 1 
ATOM   1565 C CE1 . HIS B 1 86  ? 23.057 -14.437 7.623   1.00 54.10  ? 86  HIS B CE1 1 
ATOM   1566 N NE2 . HIS B 1 86  ? 21.862 -14.867 7.985   1.00 54.20  ? 86  HIS B NE2 1 
ATOM   1567 N N   . GLU B 1 87  ? 24.506 -13.863 14.160  1.00 76.74  ? 87  GLU B N   1 
ATOM   1568 C CA  . GLU B 1 87  ? 24.582 -14.199 15.576  1.00 86.00  ? 87  GLU B CA  1 
ATOM   1569 C C   . GLU B 1 87  ? 23.828 -13.189 16.433  1.00 84.95  ? 87  GLU B C   1 
ATOM   1570 O O   . GLU B 1 87  ? 23.123 -13.572 17.376  1.00 86.63  ? 87  GLU B O   1 
ATOM   1571 C CB  . GLU B 1 87  ? 26.046 -14.313 16.003  1.00 88.57  ? 87  GLU B CB  1 
ATOM   1572 C CG  . GLU B 1 87  ? 26.795 -15.426 15.259  1.00 96.31  ? 87  GLU B CG  1 
ATOM   1573 C CD  . GLU B 1 87  ? 28.213 -15.666 15.767  1.00 112.66 ? 87  GLU B CD  1 
ATOM   1574 O OE1 . GLU B 1 87  ? 28.527 -15.264 16.908  1.00 121.86 ? 87  GLU B OE1 1 
ATOM   1575 O OE2 . GLU B 1 87  ? 29.016 -16.265 15.018  1.00 116.39 ? 87  GLU B OE2 1 
ATOM   1576 N N   . ASN B 1 88  ? 23.949 -11.897 16.117  1.00 79.09  ? 88  ASN B N   1 
ATOM   1577 C CA  . ASN B 1 88  ? 23.234 -10.885 16.889  1.00 75.45  ? 88  ASN B CA  1 
ATOM   1578 C C   . ASN B 1 88  ? 21.729 -11.041 16.749  1.00 75.00  ? 88  ASN B C   1 
ATOM   1579 O O   . ASN B 1 88  ? 20.985 -10.828 17.710  1.00 81.09  ? 88  ASN B O   1 
ATOM   1580 C CB  . ASN B 1 88  ? 23.654 -9.489  16.451  1.00 74.07  ? 88  ASN B CB  1 
ATOM   1581 C CG  . ASN B 1 88  ? 25.059 -9.158  16.868  1.00 80.85  ? 88  ASN B CG  1 
ATOM   1582 O OD1 . ASN B 1 88  ? 25.901 -10.048 16.987  1.00 85.71  ? 88  ASN B OD1 1 
ATOM   1583 N ND2 . ASN B 1 88  ? 25.323 -7.880  17.121  1.00 77.48  ? 88  ASN B ND2 1 
ATOM   1584 N N   . MET B 1 89  ? 21.261 -11.422 15.562  1.00 70.60  ? 89  MET B N   1 
ATOM   1585 C CA  . MET B 1 89  ? 19.834 -11.653 15.380  1.00 69.73  ? 89  MET B CA  1 
ATOM   1586 C C   . MET B 1 89  ? 19.326 -12.679 16.372  1.00 73.37  ? 89  MET B C   1 
ATOM   1587 O O   . MET B 1 89  ? 18.258 -12.509 16.968  1.00 76.86  ? 89  MET B O   1 
ATOM   1588 C CB  . MET B 1 89  ? 19.560 -12.130 13.955  1.00 63.86  ? 89  MET B CB  1 
ATOM   1589 C CG  . MET B 1 89  ? 20.017 -11.192 12.865  1.00 62.34  ? 89  MET B CG  1 
ATOM   1590 S SD  . MET B 1 89  ? 18.911 -9.788  12.641  1.00 86.25  ? 89  MET B SD  1 
ATOM   1591 C CE  . MET B 1 89  ? 19.551 -8.584  13.807  1.00 67.19  ? 89  MET B CE  1 
ATOM   1592 N N   . ARG B 1 90  ? 20.097 -13.742 16.578  1.00 79.05  ? 90  ARG B N   1 
ATOM   1593 C CA  . ARG B 1 90  ? 19.675 -14.811 17.471  1.00 79.16  ? 90  ARG B CA  1 
ATOM   1594 C C   . ARG B 1 90  ? 19.712 -14.366 18.929  1.00 79.96  ? 90  ARG B C   1 
ATOM   1595 O O   . ARG B 1 90  ? 18.771 -14.635 19.683  1.00 79.60  ? 90  ARG B O   1 
ATOM   1596 C CB  . ARG B 1 90  ? 20.535 -16.044 17.218  1.00 83.64  ? 90  ARG B CB  1 
ATOM   1597 C CG  . ARG B 1 90  ? 19.942 -17.368 17.679  1.00 86.95  ? 90  ARG B CG  1 
ATOM   1598 C CD  . ARG B 1 90  ? 20.996 -18.426 17.476  1.00 81.50  ? 90  ARG B CD  1 
ATOM   1599 N NE  . ARG B 1 90  ? 22.230 -17.919 18.054  1.00 93.60  ? 90  ARG B NE  1 
ATOM   1600 C CZ  . ARG B 1 90  ? 22.470 -17.819 19.352  1.00 103.08 ? 90  ARG B CZ  1 
ATOM   1601 N NH1 . ARG B 1 90  ? 21.625 -18.297 20.253  1.00 102.21 ? 90  ARG B NH1 1 
ATOM   1602 N NH2 . ARG B 1 90  ? 23.566 -17.182 19.758  1.00 105.46 ? 90  ARG B NH2 1 
ATOM   1603 N N   . LEU B 1 91  ? 20.791 -13.692 19.353  1.00 78.42  ? 91  LEU B N   1 
ATOM   1604 C CA  . LEU B 1 91  ? 20.835 -13.171 20.719  1.00 77.58  ? 91  LEU B CA  1 
ATOM   1605 C C   . LEU B 1 91  ? 19.639 -12.290 21.004  1.00 84.08  ? 91  LEU B C   1 
ATOM   1606 O O   . LEU B 1 91  ? 18.930 -12.475 22.001  1.00 86.84  ? 91  LEU B O   1 
ATOM   1607 C CB  . LEU B 1 91  ? 22.086 -12.333 20.965  1.00 75.09  ? 91  LEU B CB  1 
ATOM   1608 C CG  . LEU B 1 91  ? 23.476 -12.893 20.795  1.00 87.58  ? 91  LEU B CG  1 
ATOM   1609 C CD1 . LEU B 1 91  ? 24.467 -11.985 21.535  1.00 79.22  ? 91  LEU B CD1 1 
ATOM   1610 C CD2 . LEU B 1 91  ? 23.467 -14.311 21.308  1.00 93.03  ? 91  LEU B CD2 1 
ATOM   1611 N N   . ARG B 1 92  ? 19.411 -11.315 20.126  1.00 77.46  ? 92  ARG B N   1 
ATOM   1612 C CA  . ARG B 1 92  ? 18.373 -10.325 20.355  1.00 73.75  ? 92  ARG B CA  1 
ATOM   1613 C C   . ARG B 1 92  ? 17.002 -10.968 20.401  1.00 72.92  ? 92  ARG B C   1 
ATOM   1614 O O   . ARG B 1 92  ? 16.161 -10.600 21.226  1.00 75.51  ? 92  ARG B O   1 
ATOM   1615 C CB  . ARG B 1 92  ? 18.456 -9.252  19.276  1.00 78.86  ? 92  ARG B CB  1 
ATOM   1616 C CG  . ARG B 1 92  ? 19.764 -8.483  19.344  1.00 75.50  ? 92  ARG B CG  1 
ATOM   1617 C CD  . ARG B 1 92  ? 19.872 -7.472  18.239  1.00 74.40  ? 92  ARG B CD  1 
ATOM   1618 N NE  . ARG B 1 92  ? 21.175 -6.824  18.249  1.00 75.23  ? 92  ARG B NE  1 
ATOM   1619 C CZ  . ARG B 1 92  ? 21.652 -6.090  17.253  1.00 81.39  ? 92  ARG B CZ  1 
ATOM   1620 N NH1 . ARG B 1 92  ? 20.955 -5.894  16.145  1.00 79.64  ? 92  ARG B NH1 1 
ATOM   1621 N NH2 . ARG B 1 92  ? 22.862 -5.550  17.367  1.00 84.45  ? 92  ARG B NH2 1 
ATOM   1622 N N   . HIS B 1 93  ? 16.758 -11.936 19.528  1.00 73.47  ? 93  HIS B N   1 
ATOM   1623 C CA  . HIS B 1 93  ? 15.468 -12.610 19.543  1.00 82.97  ? 93  HIS B CA  1 
ATOM   1624 C C   . HIS B 1 93  ? 15.283 -13.397 20.839  1.00 87.40  ? 93  HIS B C   1 
ATOM   1625 O O   . HIS B 1 93  ? 14.169 -13.478 21.371  1.00 89.09  ? 93  HIS B O   1 
ATOM   1626 C CB  . HIS B 1 93  ? 15.345 -13.507 18.313  1.00 83.17  ? 93  HIS B CB  1 
ATOM   1627 C CG  . HIS B 1 93  ? 14.055 -14.262 18.233  1.00 89.27  ? 93  HIS B CG  1 
ATOM   1628 N ND1 . HIS B 1 93  ? 12.880 -13.676 17.811  1.00 95.75  ? 93  HIS B ND1 1 
ATOM   1629 C CD2 . HIS B 1 93  ? 13.763 -15.561 18.477  1.00 90.77  ? 93  HIS B CD2 1 
ATOM   1630 C CE1 . HIS B 1 93  ? 11.914 -14.578 17.819  1.00 95.74  ? 93  HIS B CE1 1 
ATOM   1631 N NE2 . HIS B 1 93  ? 12.423 -15.729 18.218  1.00 97.14  ? 93  HIS B NE2 1 
ATOM   1632 N N   . GLU B 1 94  ? 16.362 -13.982 21.364  1.00 82.94  ? 94  GLU B N   1 
ATOM   1633 C CA  . GLU B 1 94  ? 16.251 -14.759 22.594  1.00 85.76  ? 94  GLU B CA  1 
ATOM   1634 C C   . GLU B 1 94  ? 15.874 -13.882 23.778  1.00 87.98  ? 94  GLU B C   1 
ATOM   1635 O O   . GLU B 1 94  ? 14.923 -14.185 24.509  1.00 89.54  ? 94  GLU B O   1 
ATOM   1636 C CB  . GLU B 1 94  ? 17.560 -15.486 22.883  1.00 93.80  ? 94  GLU B CB  1 
ATOM   1637 C CG  . GLU B 1 94  ? 17.791 -16.720 22.046  1.00 97.24  ? 94  GLU B CG  1 
ATOM   1638 C CD  . GLU B 1 94  ? 18.991 -17.499 22.524  1.00 107.02 ? 94  GLU B CD  1 
ATOM   1639 O OE1 . GLU B 1 94  ? 19.334 -17.372 23.723  1.00 112.42 ? 94  GLU B OE1 1 
ATOM   1640 O OE2 . GLU B 1 94  ? 19.582 -18.243 21.710  1.00 109.18 ? 94  GLU B OE2 1 
ATOM   1641 N N   . SER B 1 95  ? 16.613 -12.792 23.985  1.00 84.39  ? 95  SER B N   1 
ATOM   1642 C CA  . SER B 1 95  ? 16.355 -11.934 25.135  1.00 83.85  ? 95  SER B CA  1 
ATOM   1643 C C   . SER B 1 95  ? 14.912 -11.455 25.144  1.00 84.94  ? 95  SER B C   1 
ATOM   1644 O O   . SER B 1 95  ? 14.231 -11.521 26.172  1.00 91.02  ? 95  SER B O   1 
ATOM   1645 C CB  . SER B 1 95  ? 17.315 -10.746 25.131  1.00 78.76  ? 95  SER B CB  1 
ATOM   1646 O OG  . SER B 1 95  ? 17.011 -9.864  24.066  1.00 80.95  ? 95  SER B OG  1 
ATOM   1647 N N   . TRP B 1 96  ? 14.419 -10.986 24.000  1.00 80.23  ? 96  TRP B N   1 
ATOM   1648 C CA  . TRP B 1 96  ? 13.057 -10.479 23.958  1.00 82.41  ? 96  TRP B CA  1 
ATOM   1649 C C   . TRP B 1 96  ? 12.019 -11.569 24.156  1.00 91.91  ? 96  TRP B C   1 
ATOM   1650 O O   . TRP B 1 96  ? 10.892 -11.262 24.558  1.00 94.52  ? 96  TRP B O   1 
ATOM   1651 C CB  . TRP B 1 96  ? 12.808 -9.746  22.645  1.00 78.81  ? 96  TRP B CB  1 
ATOM   1652 C CG  . TRP B 1 96  ? 13.246 -8.335  22.712  1.00 78.30  ? 96  TRP B CG  1 
ATOM   1653 C CD1 . TRP B 1 96  ? 14.409 -7.812  22.235  1.00 77.21  ? 96  TRP B CD1 1 
ATOM   1654 C CD2 . TRP B 1 96  ? 12.529 -7.250  23.303  1.00 79.62  ? 96  TRP B CD2 1 
ATOM   1655 N NE1 . TRP B 1 96  ? 14.463 -6.464  22.494  1.00 75.06  ? 96  TRP B NE1 1 
ATOM   1656 C CE2 . TRP B 1 96  ? 13.318 -6.093  23.148  1.00 76.54  ? 96  TRP B CE2 1 
ATOM   1657 C CE3 . TRP B 1 96  ? 11.295 -7.143  23.951  1.00 79.33  ? 96  TRP B CE3 1 
ATOM   1658 C CZ2 . TRP B 1 96  ? 12.913 -4.845  23.614  1.00 74.19  ? 96  TRP B CZ2 1 
ATOM   1659 C CZ3 . TRP B 1 96  ? 10.895 -5.902  24.418  1.00 77.56  ? 96  TRP B CZ3 1 
ATOM   1660 C CH2 . TRP B 1 96  ? 11.703 -4.770  24.247  1.00 75.23  ? 96  TRP B CH2 1 
ATOM   1661 N N   . SER B 1 97  ? 12.360 -12.827 23.880  1.00 104.56 ? 97  SER B N   1 
ATOM   1662 C CA  . SER B 1 97  ? 11.446 -13.914 24.217  1.00 107.20 ? 97  SER B CA  1 
ATOM   1663 C C   . SER B 1 97  ? 11.329 -14.095 25.723  1.00 106.94 ? 97  SER B C   1 
ATOM   1664 O O   . SER B 1 97  ? 10.223 -14.265 26.246  1.00 112.05 ? 97  SER B O   1 
ATOM   1665 C CB  . SER B 1 97  ? 11.900 -15.210 23.556  1.00 107.32 ? 97  SER B CB  1 
ATOM   1666 O OG  . SER B 1 97  ? 11.539 -15.219 22.190  1.00 108.68 ? 97  SER B OG  1 
ATOM   1667 N N   . ARG B 1 98  ? 12.456 -14.055 26.436  1.00 90.86  ? 98  ARG B N   1 
ATOM   1668 C CA  . ARG B 1 98  ? 12.421 -14.255 27.880  1.00 98.94  ? 98  ARG B CA  1 
ATOM   1669 C C   . ARG B 1 98  ? 11.608 -13.172 28.575  1.00 98.19  ? 98  ARG B C   1 
ATOM   1670 O O   . ARG B 1 98  ? 10.863 -13.455 29.520  1.00 101.06 ? 98  ARG B O   1 
ATOM   1671 C CB  . ARG B 1 98  ? 13.839 -14.298 28.443  1.00 103.09 ? 98  ARG B CB  1 
ATOM   1672 C CG  . ARG B 1 98  ? 13.892 -14.645 29.932  1.00 114.69 ? 98  ARG B CG  1 
ATOM   1673 C CD  . ARG B 1 98  ? 13.352 -16.051 30.195  1.00 117.62 ? 98  ARG B CD  1 
ATOM   1674 N NE  . ARG B 1 98  ? 13.340 -16.398 31.611  1.00 122.29 ? 98  ARG B NE  1 
ATOM   1675 C CZ  . ARG B 1 98  ? 12.282 -16.278 32.402  1.00 124.27 ? 98  ARG B CZ  1 
ATOM   1676 N NH1 . ARG B 1 98  ? 11.129 -15.818 31.947  1.00 116.79 ? 98  ARG B NH1 1 
ATOM   1677 N NH2 . ARG B 1 98  ? 12.382 -16.637 33.680  1.00 129.75 ? 98  ARG B NH2 1 
ATOM   1678 N N   . VAL B 1 99  ? 11.732 -11.926 28.122  1.00 92.34  ? 99  VAL B N   1 
ATOM   1679 C CA  . VAL B 1 99  ? 10.972 -10.843 28.734  1.00 90.98  ? 99  VAL B CA  1 
ATOM   1680 C C   . VAL B 1 99  ? 9.481  -11.138 28.670  1.00 96.76  ? 99  VAL B C   1 
ATOM   1681 O O   . VAL B 1 99  ? 8.743  -10.885 29.629  1.00 99.01  ? 99  VAL B O   1 
ATOM   1682 C CB  . VAL B 1 99  ? 11.317 -9.504  28.057  1.00 90.77  ? 99  VAL B CB  1 
ATOM   1683 C CG1 . VAL B 1 99  ? 10.350 -8.411  28.494  1.00 86.77  ? 99  VAL B CG1 1 
ATOM   1684 C CG2 . VAL B 1 99  ? 12.748 -9.107  28.370  1.00 87.53  ? 99  VAL B CG2 1 
ATOM   1685 N N   . ASP B 1 100 ? 9.018  -11.710 27.557  1.00 100.71 ? 100 ASP B N   1 
ATOM   1686 C CA  . ASP B 1 100 ? 7.596  -12.006 27.415  1.00 102.10 ? 100 ASP B CA  1 
ATOM   1687 C C   . ASP B 1 100 ? 7.130  -13.023 28.449  1.00 104.44 ? 100 ASP B C   1 
ATOM   1688 O O   . ASP B 1 100 ? 6.003  -12.938 28.948  1.00 105.69 ? 100 ASP B O   1 
ATOM   1689 C CB  . ASP B 1 100 ? 7.305  -12.512 26.003  1.00 106.61 ? 100 ASP B CB  1 
ATOM   1690 C CG  . ASP B 1 100 ? 7.500  -11.442 24.952  1.00 113.68 ? 100 ASP B CG  1 
ATOM   1691 O OD1 . ASP B 1 100 ? 7.680  -10.268 25.335  1.00 110.56 ? 100 ASP B OD1 1 
ATOM   1692 O OD2 . ASP B 1 100 ? 7.477  -11.772 23.746  1.00 114.99 ? 100 ASP B OD2 1 
ATOM   1693 N N   . LYS B 1 101 ? 7.977  -14.000 28.774  1.00 99.30  ? 101 LYS B N   1 
ATOM   1694 C CA  . LYS B 1 101 ? 7.640  -14.955 29.824  1.00 101.62 ? 101 LYS B CA  1 
ATOM   1695 C C   . LYS B 1 101 ? 7.584  -14.272 31.186  1.00 104.70 ? 101 LYS B C   1 
ATOM   1696 O O   . LYS B 1 101 ? 6.632  -14.465 31.949  1.00 105.65 ? 101 LYS B O   1 
ATOM   1697 C CB  . LYS B 1 101 ? 8.657  -16.094 29.832  1.00 101.05 ? 101 LYS B CB  1 
ATOM   1698 C CG  . LYS B 1 101 ? 8.678  -16.894 28.544  1.00 107.72 ? 101 LYS B CG  1 
ATOM   1699 C CD  . LYS B 1 101 ? 10.048 -17.505 28.283  1.00 105.29 ? 101 LYS B CD  1 
ATOM   1700 C CE  . LYS B 1 101 ? 10.234 -17.796 26.799  1.00 96.94  ? 101 LYS B CE  1 
ATOM   1701 N NZ  . LYS B 1 101 ? 11.660 -18.027 26.448  1.00 95.01  ? 101 LYS B NZ  1 
ATOM   1702 N N   . ILE B 1 102 ? 8.603  -13.464 31.498  1.00 110.31 ? 102 ILE B N   1 
ATOM   1703 C CA  . ILE B 1 102 ? 8.677  -12.784 32.790  1.00 107.29 ? 102 ILE B CA  1 
ATOM   1704 C C   . ILE B 1 102 ? 7.404  -12.000 33.062  1.00 107.26 ? 102 ILE B C   1 
ATOM   1705 O O   . ILE B 1 102 ? 6.831  -12.066 34.155  1.00 109.10 ? 102 ILE B O   1 
ATOM   1706 C CB  . ILE B 1 102 ? 9.912  -11.867 32.841  1.00 98.95  ? 102 ILE B CB  1 
ATOM   1707 C CG1 . ILE B 1 102 ? 11.201 -12.680 32.724  1.00 100.94 ? 102 ILE B CG1 1 
ATOM   1708 C CG2 . ILE B 1 102 ? 9.908  -11.036 34.102  1.00 96.77  ? 102 ILE B CG2 1 
ATOM   1709 C CD1 . ILE B 1 102 ? 12.447 -11.874 32.994  1.00 94.56  ? 102 ILE B CD1 1 
ATOM   1710 N N   . ILE B 1 103 ? 6.936  -11.253 32.065  1.00 100.79 ? 103 ILE B N   1 
ATOM   1711 C CA  . ILE B 1 103 ? 5.736  -10.445 32.250  1.00 101.72 ? 103 ILE B CA  1 
ATOM   1712 C C   . ILE B 1 103 ? 4.523  -11.335 32.465  1.00 109.46 ? 103 ILE B C   1 
ATOM   1713 O O   . ILE B 1 103 ? 3.685  -11.074 33.338  1.00 112.25 ? 103 ILE B O   1 
ATOM   1714 C CB  . ILE B 1 103 ? 5.542  -9.512  31.043  1.00 92.07  ? 103 ILE B CB  1 
ATOM   1715 C CG1 . ILE B 1 103 ? 6.760  -8.604  30.879  1.00 91.13  ? 103 ILE B CG1 1 
ATOM   1716 C CG2 . ILE B 1 103 ? 4.266  -8.707  31.196  1.00 87.81  ? 103 ILE B CG2 1 
ATOM   1717 C CD1 . ILE B 1 103 ? 7.203  -7.927  32.151  1.00 88.55  ? 103 ILE B CD1 1 
ATOM   1718 N N   . GLU B 1 104 ? 4.404  -12.393 31.664  1.00 112.15 ? 104 GLU B N   1 
ATOM   1719 C CA  . GLU B 1 104 ? 3.321  -13.349 31.841  1.00 111.46 ? 104 GLU B CA  1 
ATOM   1720 C C   . GLU B 1 104 ? 3.348  -13.940 33.245  1.00 121.71 ? 104 GLU B C   1 
ATOM   1721 O O   . GLU B 1 104 ? 2.296  -14.165 33.853  1.00 126.01 ? 104 GLU B O   1 
ATOM   1722 C CB  . GLU B 1 104 ? 3.423  -14.427 30.765  1.00 108.72 ? 104 GLU B CB  1 
ATOM   1723 C CG  . GLU B 1 104 ? 2.188  -15.272 30.571  1.00 115.56 ? 104 GLU B CG  1 
ATOM   1724 C CD  . GLU B 1 104 ? 2.295  -16.164 29.343  1.00 118.09 ? 104 GLU B CD  1 
ATOM   1725 O OE1 . GLU B 1 104 ? 3.399  -16.255 28.760  1.00 106.58 ? 104 GLU B OE1 1 
ATOM   1726 O OE2 . GLU B 1 104 ? 1.272  -16.767 28.956  1.00 121.82 ? 104 GLU B OE2 1 
ATOM   1727 N N   . ASN B 1 105 ? 4.550  -14.170 33.786  1.00 124.59 ? 105 ASN B N   1 
ATOM   1728 C CA  . ASN B 1 105 ? 4.689  -14.770 35.109  1.00 130.81 ? 105 ASN B CA  1 
ATOM   1729 C C   . ASN B 1 105 ? 4.451  -13.767 36.233  1.00 129.57 ? 105 ASN B C   1 
ATOM   1730 O O   . ASN B 1 105 ? 3.955  -14.153 37.298  1.00 138.51 ? 105 ASN B O   1 
ATOM   1731 C CB  . ASN B 1 105 ? 6.075  -15.401 35.258  1.00 131.69 ? 105 ASN B CB  1 
ATOM   1732 C CG  . ASN B 1 105 ? 6.235  -16.664 34.428  1.00 131.32 ? 105 ASN B CG  1 
ATOM   1733 O OD1 . ASN B 1 105 ? 5.255  -17.232 33.947  1.00 134.68 ? 105 ASN B OD1 1 
ATOM   1734 N ND2 . ASN B 1 105 ? 7.475  -17.114 34.265  1.00 131.56 ? 105 ASN B ND2 1 
ATOM   1735 N N   . LEU B 1 106 ? 4.802  -12.494 36.033  1.00 124.62 ? 106 LEU B N   1 
ATOM   1736 C CA  . LEU B 1 106 ? 4.467  -11.479 37.028  1.00 123.05 ? 106 LEU B CA  1 
ATOM   1737 C C   . LEU B 1 106 ? 2.970  -11.453 37.274  1.00 134.16 ? 106 LEU B C   1 
ATOM   1738 O O   . LEU B 1 106 ? 2.517  -11.354 38.420  1.00 137.10 ? 106 LEU B O   1 
ATOM   1739 C CB  . LEU B 1 106 ? 4.940  -10.101 36.571  1.00 120.30 ? 106 LEU B CB  1 
ATOM   1740 C CG  . LEU B 1 106 ? 6.404  -9.704  36.719  1.00 114.08 ? 106 LEU B CG  1 
ATOM   1741 C CD1 . LEU B 1 106 ? 6.656  -8.408  35.983  1.00 109.83 ? 106 LEU B CD1 1 
ATOM   1742 C CD2 . LEU B 1 106 ? 6.745  -9.539  38.178  1.00 121.12 ? 106 LEU B CD2 1 
ATOM   1743 N N   . GLU B 1 107 ? 2.187  -11.537 36.200  1.00 147.54 ? 107 GLU B N   1 
ATOM   1744 C CA  . GLU B 1 107 ? 0.737  -11.540 36.321  1.00 151.22 ? 107 GLU B CA  1 
ATOM   1745 C C   . GLU B 1 107 ? 0.225  -12.877 36.836  1.00 152.98 ? 107 GLU B C   1 
ATOM   1746 O O   . GLU B 1 107 ? -0.843 -12.934 37.454  1.00 154.97 ? 107 GLU B O   1 
ATOM   1747 C CB  . GLU B 1 107 ? 0.117  -11.209 34.966  1.00 148.05 ? 107 GLU B CB  1 
ATOM   1748 C CG  . GLU B 1 107 ? -1.340 -10.812 35.014  1.00 152.24 ? 107 GLU B CG  1 
ATOM   1749 C CD  . GLU B 1 107 ? -1.813 -10.250 33.693  1.00 153.49 ? 107 GLU B CD  1 
ATOM   1750 O OE1 . GLU B 1 107 ? -0.964 -10.049 32.799  1.00 151.57 ? 107 GLU B OE1 1 
ATOM   1751 O OE2 . GLU B 1 107 ? -3.029 -10.009 33.546  1.00 157.79 ? 107 GLU B OE2 1 
ATOM   1752 N N   . ALA B 1 108 ? 0.971  -13.956 36.599  1.00 145.23 ? 108 ALA B N   1 
ATOM   1753 C CA  . ALA B 1 108 ? 0.546  -15.271 37.065  1.00 150.02 ? 108 ALA B CA  1 
ATOM   1754 C C   . ALA B 1 108 ? 0.597  -15.354 38.584  1.00 152.17 ? 108 ALA B C   1 
ATOM   1755 O O   . ALA B 1 108 ? -0.404 -15.675 39.235  1.00 157.96 ? 108 ALA B O   1 
ATOM   1756 C CB  . ALA B 1 108 ? 1.419  -16.357 36.436  1.00 155.45 ? 108 ALA B CB  1 
ATOM   1757 N N   . ASN B 1 109 ? 1.761  -15.062 39.168  1.00 138.29 ? 109 ASN B N   1 
ATOM   1758 C CA  . ASN B 1 109 ? 1.872  -15.073 40.621  1.00 139.39 ? 109 ASN B CA  1 
ATOM   1759 C C   . ASN B 1 109 ? 0.895  -14.091 41.249  1.00 137.15 ? 109 ASN B C   1 
ATOM   1760 O O   . ASN B 1 109 ? 0.442  -14.297 42.381  1.00 139.66 ? 109 ASN B O   1 
ATOM   1761 C CB  . ASN B 1 109 ? 3.308  -14.752 41.038  1.00 138.00 ? 109 ASN B CB  1 
ATOM   1762 C CG  . ASN B 1 109 ? 4.314  -15.748 40.480  1.00 134.43 ? 109 ASN B CG  1 
ATOM   1763 O OD1 . ASN B 1 109 ? 3.947  -16.829 40.023  1.00 126.10 ? 109 ASN B OD1 1 
ATOM   1764 N ND2 . ASN B 1 109 ? 5.592  -15.390 40.530  1.00 131.12 ? 109 ASN B ND2 1 
ATOM   1765 N N   . LYS B 1 110 ? 0.548  -13.034 40.523  1.00 136.13 ? 110 LYS B N   1 
ATOM   1766 C CA  . LYS B 1 110 ? -0.487 -12.094 40.925  1.00 132.79 ? 110 LYS B CA  1 
ATOM   1767 C C   . LYS B 1 110 ? -1.857 -12.766 40.973  1.00 128.62 ? 110 LYS B C   1 
ATOM   1768 O O   . LYS B 1 110 ? -2.698 -12.430 41.807  1.00 113.76 ? 110 LYS B O   1 
ATOM   1769 C CB  . LYS B 1 110 ? -0.505 -10.908 39.960  1.00 131.59 ? 110 LYS B CB  1 
ATOM   1770 C CG  . LYS B 1 110 ? -1.675 -9.960  40.116  1.00 125.26 ? 110 LYS B CG  1 
ATOM   1771 C CD  . LYS B 1 110 ? -1.667 -8.931  38.998  1.00 124.75 ? 110 LYS B CD  1 
ATOM   1772 C CE  . LYS B 1 110 ? -2.907 -8.057  39.022  1.00 115.90 ? 110 LYS B CE  1 
ATOM   1773 N NZ  . LYS B 1 110 ? -2.918 -7.081  37.896  1.00 119.16 ? 110 LYS B NZ  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   . ILE A 4   ? 1.4288 1.1022 0.8646 0.1916  -0.1592 -0.0807 4   ILE A N   
2    C CA  . ILE A 4   ? 1.4643 1.1480 0.9260 0.1727  -0.1410 -0.0705 4   ILE A CA  
3    C C   . ILE A 4   ? 1.5254 1.2553 1.0163 0.1764  -0.1386 -0.0785 4   ILE A C   
4    O O   . ILE A 4   ? 1.6128 1.3477 1.0834 0.1956  -0.1393 -0.0852 4   ILE A O   
5    C CB  . ILE A 4   ? 1.4638 1.1059 0.8875 0.1734  -0.1269 -0.0578 4   ILE A CB  
6    C CG1 . ILE A 4   ? 1.5138 1.1043 0.9037 0.1701  -0.1284 -0.0501 4   ILE A CG1 
7    C CG2 . ILE A 4   ? 1.4497 1.1062 0.9013 0.1519  -0.1097 -0.0484 4   ILE A CG2 
8    C CD1 . ILE A 4   ? 1.5171 1.1089 0.9385 0.1436  -0.1244 -0.0450 4   ILE A CD1 
9    N N   . PRO A 5   ? 1.4321 1.1957 0.9698 0.1590  -0.1351 -0.0787 5   PRO A N   
10   C CA  . PRO A 5   ? 1.4346 1.2404 1.0008 0.1618  -0.1334 -0.0869 5   PRO A CA  
11   C C   . PRO A 5   ? 1.5206 1.3290 1.0829 0.1622  -0.1191 -0.0811 5   PRO A C   
12   O O   . PRO A 5   ? 1.4902 1.2764 1.0421 0.1518  -0.1081 -0.0688 5   PRO A O   
13   C CB  . PRO A 5   ? 1.3087 1.1424 0.9213 0.1428  -0.1327 -0.0865 5   PRO A CB  
14   C CG  . PRO A 5   ? 1.3319 1.1455 0.9408 0.1362  -0.1399 -0.0835 5   PRO A CG  
15   C CD  . PRO A 5   ? 1.3474 1.1145 0.9136 0.1392  -0.1352 -0.0745 5   PRO A CD  
16   N N   . LYS A 6   ? 1.7220 1.5605 1.2944 0.1737  -0.1194 -0.0911 6   LYS A N   
17   C CA  . LYS A 6   ? 1.7109 1.5601 1.2859 0.1753  -0.1073 -0.0872 6   LYS A CA  
18   C C   . LYS A 6   ? 1.6487 1.5094 1.2542 0.1527  -0.0970 -0.0774 6   LYS A C   
19   O O   . LYS A 6   ? 1.6402 1.4906 1.2368 0.1472  -0.0866 -0.0674 6   LYS A O   
20   C CB  . LYS A 6   ? 1.7334 1.6191 1.3224 0.1890  -0.1093 -0.1018 6   LYS A CB  
21   C CG  . LYS A 6   ? 1.8372 1.7404 1.4355 0.1908  -0.0977 -0.0989 6   LYS A CG  
22   C CD  . LYS A 6   ? 1.8724 1.8160 1.4947 0.1991  -0.0983 -0.1138 6   LYS A CD  
23   C CE  . LYS A 6   ? 1.8772 1.8407 1.5115 0.2014  -0.0877 -0.1112 6   LYS A CE  
24   N NZ  . LYS A 6   ? 1.9678 1.9223 1.5702 0.2225  -0.0842 -0.1124 6   LYS A NZ  
25   N N   . GLU A 7   ? 1.3762 1.2590 1.0160 0.1401  -0.1000 -0.0806 7   GLU A N   
26   C CA  . GLU A 7   ? 1.2924 1.1897 0.9598 0.1208  -0.0908 -0.0738 7   GLU A CA  
27   C C   . GLU A 7   ? 1.2664 1.1350 0.9193 0.1062  -0.0837 -0.0621 7   GLU A C   
28   O O   . GLU A 7   ? 1.2684 1.1450 0.9323 0.0920  -0.0736 -0.0560 7   GLU A O   
29   C CB  . GLU A 7   ? 1.2684 1.1928 0.9714 0.1132  -0.0955 -0.0802 7   GLU A CB  
30   C CG  . GLU A 7   ? 1.3793 1.3309 1.0964 0.1249  -0.1009 -0.0923 7   GLU A CG  
31   C CD  . GLU A 7   ? 1.4391 1.3838 1.1387 0.1396  -0.1132 -0.1019 7   GLU A CD  
32   O OE1 . GLU A 7   ? 1.4634 1.4001 1.1639 0.1363  -0.1216 -0.1025 7   GLU A OE1 
33   O OE2 . GLU A 7   ? 1.4709 1.4207 1.1557 0.1551  -0.1147 -0.1102 7   GLU A OE2 
34   N N   . MET A 8   ? 1.2225 1.0578 0.8494 0.1091  -0.0887 -0.0596 8   MET A N   
35   C CA  . MET A 8   ? 1.2226 1.0286 0.8354 0.0934  -0.0805 -0.0493 8   MET A CA  
36   C C   . MET A 8   ? 1.2385 1.0182 0.8177 0.0964  -0.0711 -0.0403 8   MET A C   
37   O O   . MET A 8   ? 1.1862 0.9601 0.7650 0.0795  -0.0593 -0.0324 8   MET A O   
38   C CB  . MET A 8   ? 1.2381 1.0168 0.8365 0.0942  -0.0891 -0.0499 8   MET A CB  
39   C CG  . MET A 8   ? 1.1183 0.8781 0.7176 0.0731  -0.0803 -0.0428 8   MET A CG  
40   S SD  . MET A 8   ? 1.0590 0.7974 0.6542 0.0724  -0.0913 -0.0455 8   MET A SD  
41   C CE  . MET A 8   ? 1.2456 0.9223 0.7874 0.0706  -0.0831 -0.0343 8   MET A CE  
42   N N   . LEU A 9   ? 1.2756 1.0420 0.8261 0.1181  -0.0756 -0.0423 9   LEU A N   
43   C CA  . LEU A 9   ? 1.2468 0.9928 0.7672 0.1237  -0.0662 -0.0338 9   LEU A CA  
44   C C   . LEU A 9   ? 1.2200 1.0024 0.7657 0.1188  -0.0585 -0.0332 9   LEU A C   
45   O O   . LEU A 9   ? 1.1816 0.9554 0.7170 0.1099  -0.0479 -0.0238 9   LEU A O   
46   C CB  . LEU A 9   ? 1.3149 1.0430 0.7991 0.1515  -0.0726 -0.0382 9   LEU A CB  
47   C CG  . LEU A 9   ? 1.3548 1.0631 0.8065 0.1612  -0.0626 -0.0294 9   LEU A CG  
48   C CD1 . LEU A 9   ? 1.2798 0.9439 0.7054 0.1442  -0.0524 -0.0147 9   LEU A CD1 
49   C CD2 . LEU A 9   ? 1.3762 1.0723 0.7922 0.1924  -0.0688 -0.0364 9   LEU A CD2 
50   N N   . ARG A 10  ? 1.2026 1.0260 0.7812 0.1239  -0.0640 -0.0435 10  ARG A N   
51   C CA  . ARG A 10  ? 1.1839 1.0436 0.7898 0.1185  -0.0581 -0.0440 10  ARG A CA  
52   C C   . ARG A 10  ? 1.1294 0.9939 0.7512 0.0932  -0.0502 -0.0372 10  ARG A C   
53   O O   . ARG A 10  ? 1.0990 0.9733 0.7218 0.0860  -0.0423 -0.0317 10  ARG A O   
54   C CB  . ARG A 10  ? 1.2351 1.1327 0.8727 0.1263  -0.0652 -0.0567 10  ARG A CB  
55   C CG  . ARG A 10  ? 1.2201 1.1561 0.8869 0.1228  -0.0607 -0.0589 10  ARG A CG  
56   C CD  . ARG A 10  ? 1.2797 1.2450 0.9655 0.1374  -0.0665 -0.0723 10  ARG A CD  
57   N NE  . ARG A 10  ? 1.4788 1.4796 1.1967 0.1316  -0.0635 -0.0753 10  ARG A NE  
58   C CZ  . ARG A 10  ? 1.5459 1.5745 1.2814 0.1426  -0.0653 -0.0860 10  ARG A CZ  
59   N NH1 . ARG A 10  ? 1.5979 1.6271 1.3231 0.1599  -0.0694 -0.0963 10  ARG A NH1 
60   N NH2 . ARG A 10  ? 1.4549 1.5120 1.2178 0.1362  -0.0627 -0.0878 10  ARG A NH2 
61   N N   . ALA A 11  ? 1.1411 1.0010 0.7747 0.0802  -0.0522 -0.0386 11  ALA A N   
62   C CA  . ALA A 11  ? 1.0915 0.9591 0.7396 0.0571  -0.0439 -0.0350 11  ALA A CA  
63   C C   . ALA A 11  ? 1.0849 0.9194 0.7027 0.0451  -0.0337 -0.0246 11  ALA A C   
64   O O   . ALA A 11  ? 1.0355 0.8822 0.6588 0.0289  -0.0246 -0.0216 11  ALA A O   
65   C CB  . ALA A 11  ? 1.0986 0.9706 0.7665 0.0485  -0.0480 -0.0402 11  ALA A CB  
66   N N   . GLN A 12  ? 1.1786 0.9707 0.7621 0.0527  -0.0350 -0.0197 12  GLN A N   
67   C CA  . GLN A 12  ? 1.1702 0.9245 0.7213 0.0407  -0.0242 -0.0093 12  GLN A CA  
68   C C   . GLN A 12  ? 1.1420 0.9000 0.6788 0.0444  -0.0171 -0.0026 12  GLN A C   
69   O O   . GLN A 12  ? 1.0717 0.8263 0.6021 0.0259  -0.0061 0.0036  12  GLN A O   
70   C CB  . GLN A 12  ? 1.2547 0.9597 0.7690 0.0508  -0.0280 -0.0056 12  GLN A CB  
71   C CG  . GLN A 12  ? 1.2505 0.9470 0.7754 0.0443  -0.0343 -0.0107 12  GLN A CG  
72   C CD  . GLN A 12  ? 1.3563 1.0029 0.8415 0.0556  -0.0393 -0.0072 12  GLN A CD  
73   O OE1 . GLN A 12  ? 1.4389 1.0579 0.8873 0.0717  -0.0387 -0.0020 12  GLN A OE1 
74   N NE2 . GLN A 12  ? 1.3255 0.9608 0.8171 0.0486  -0.0443 -0.0105 12  GLN A NE2 
75   N N   . THR A 13  ? 1.0487 0.8164 0.5806 0.0682  -0.0229 -0.0046 13  THR A N   
76   C CA  . THR A 13  ? 1.0975 0.8761 0.6214 0.0738  -0.0170 0.0008  13  THR A CA  
77   C C   . THR A 13  ? 1.0716 0.8942 0.6290 0.0575  -0.0134 -0.0013 13  THR A C   
78   O O   . THR A 13  ? 1.0487 0.8740 0.5979 0.0473  -0.0052 0.0056  13  THR A O   
79   C CB  . THR A 13  ? 1.1181 0.9092 0.6382 0.1035  -0.0240 -0.0047 13  THR A CB  
80   O OG1 . THR A 13  ? 1.1998 0.9489 0.6818 0.1201  -0.0270 -0.0032 13  THR A OG1 
81   C CG2 . THR A 13  ? 1.1352 0.9445 0.6528 0.1105  -0.0181 0.0001  13  THR A CG2 
82   N N   . ASN A 14  ? 0.9989 0.8562 0.5925 0.0554  -0.0198 -0.0111 14  ASN A N   
83   C CA  . ASN A 14  ? 0.9315 0.8300 0.5550 0.0418  -0.0177 -0.0147 14  ASN A CA  
84   C C   . ASN A 14  ? 0.9357 0.8242 0.5507 0.0156  -0.0076 -0.0100 14  ASN A C   
85   O O   . ASN A 14  ? 0.8903 0.7993 0.5083 0.0049  -0.0024 -0.0081 14  ASN A O   
86   C CB  . ASN A 14  ? 0.9557 0.8828 0.6134 0.0435  -0.0252 -0.0255 14  ASN A CB  
87   C CG  . ASN A 14  ? 0.9109 0.8833 0.5971 0.0486  -0.0284 -0.0316 14  ASN A CG  
88   O OD1 . ASN A 14  ? 0.8414 0.8396 0.5453 0.0349  -0.0260 -0.0342 14  ASN A OD1 
89   N ND2 . ASN A 14  ? 0.8733 0.8567 0.5637 0.0692  -0.0337 -0.0352 14  ASN A ND2 
90   O O   . HOX A 15  ? 1.1314 0.9690 0.6966 -0.0525 0.0255  0.0021  15  HOX A O   
91   C C   . HOX A 15  ? 1.1251 0.9489 0.6900 -0.0315 0.0166  0.0025  15  HOX A C   
92   N N   . HOX A 15  ? 1.0816 0.9391 0.6850 0.0053  -0.0049 -0.0091 15  HOX A N   
93   C CA  . HOX A 15  ? 1.0984 0.9470 0.6957 -0.0208 0.0058  -0.0077 15  HOX A CA  
94   C CB  . HOX A 15  ? 1.1203 0.9395 0.7126 -0.0278 0.0063  -0.0094 15  HOX A CB  
95   C CG  . HOX A 15  ? 1.1796 0.9945 0.7690 -0.0552 0.0187  -0.0108 15  HOX A CG  
96   C CZ  . HOX A 15  ? 1.1099 0.9224 0.6939 -0.1085 0.0447  -0.0182 15  HOX A CZ  
97   N NZ  . HOX A 15  ? 1.1778 0.9922 0.7592 -0.1354 0.0587  -0.0243 15  HOX A NZ  
98   C CD1 . HOX A 15  ? 1.1253 0.9834 0.7389 -0.0702 0.0232  -0.0188 15  HOX A CD1 
99   C CD2 . HOX A 15  ? 1.2218 0.9898 0.7829 -0.0662 0.0264  -0.0055 15  HOX A CD2 
100  C CE1 . HOX A 15  ? 1.1339 0.9924 0.7442 -0.0957 0.0356  -0.0229 15  HOX A CE1 
101  C CE2 . HOX A 15  ? 1.1635 0.9287 0.7224 -0.0931 0.0395  -0.0086 15  HOX A CE2 
102  N N   . ILE A 16  ? 1.0124 0.7985 0.5458 -0.0164 0.0164  0.0113  16  ILE A N   
103  C CA  . ILE A 16  ? 1.0644 0.8228 0.5637 -0.0245 0.0272  0.0224  16  ILE A CA  
104  C C   . ILE A 16  ? 1.0414 0.8402 0.5532 -0.0233 0.0275  0.0232  16  ILE A C   
105  O O   . ILE A 16  ? 1.0196 0.8243 0.5242 -0.0437 0.0368  0.0263  16  ILE A O   
106  C CB  . ILE A 16  ? 1.1347 0.8432 0.5947 -0.0047 0.0267  0.0314  16  ILE A CB  
107  C CG1 . ILE A 16  ? 1.1620 0.8269 0.6053 -0.0088 0.0265  0.0311  16  ILE A CG1 
108  C CG2 . ILE A 16  ? 1.2804 0.9642 0.7060 -0.0102 0.0381  0.0436  16  ILE A CG2 
109  C CD1 . ILE A 16  ? 1.1461 0.7584 0.5458 0.0113  0.0253  0.0389  16  ILE A CD1 
110  N N   . LEU A 17  ? 1.0250 0.8543 0.5569 0.0001  0.0172  0.0191  17  LEU A N   
111  C CA  . LEU A 17  ? 1.0002 0.8706 0.5467 0.0053  0.0156  0.0193  17  LEU A CA  
112  C C   . LEU A 17  ? 0.9851 0.8947 0.5544 -0.0180 0.0179  0.0135  17  LEU A C   
113  O O   . LEU A 17  ? 1.0086 0.9338 0.5722 -0.0282 0.0226  0.0174  17  LEU A O   
114  C CB  . LEU A 17  ? 0.9289 0.8299 0.5000 0.0318  0.0043  0.0121  17  LEU A CB  
115  C CG  . LEU A 17  ? 1.0321 0.9111 0.5826 0.0602  0.0015  0.0151  17  LEU A CG  
116  C CD1 . LEU A 17  ? 0.9890 0.9052 0.5687 0.0823  -0.0085 0.0043  17  LEU A CD1 
117  C CD2 . LEU A 17  ? 1.1512 1.0210 0.6765 0.0657  0.0085  0.0258  17  LEU A CD2 
118  N N   . LEU A 18  ? 0.9634 0.8909 0.5575 -0.0259 0.0144  0.0033  18  LEU A N   
119  C CA  . LEU A 18  ? 0.9999 0.9662 0.6130 -0.0458 0.0165  -0.0044 18  LEU A CA  
120  C C   . LEU A 18  ? 1.0664 1.0130 0.6556 -0.0732 0.0295  -0.0012 18  LEU A C   
121  O O   . LEU A 18  ? 1.0794 1.0567 0.6722 -0.0892 0.0329  -0.0048 18  LEU A O   
122  C CB  . LEU A 18  ? 0.9648 0.9524 0.6069 -0.0457 0.0109  -0.0161 18  LEU A CB  
123  C CG  . LEU A 18  ? 0.8145 0.8381 0.4864 -0.0257 -0.0007 -0.0225 18  LEU A CG  
124  C CD1 . LEU A 18  ? 0.8483 0.8817 0.5427 -0.0244 -0.0048 -0.0319 18  LEU A CD1 
125  C CD2 . LEU A 18  ? 0.9081 0.9766 0.5935 -0.0295 -0.0030 -0.0262 18  LEU A CD2 
126  N N   . MET A 19  ? 1.0441 0.9407 0.6080 -0.0793 0.0368  0.0044  19  MET A N   
127  C CA  . MET A 19  ? 1.1578 1.0306 0.6960 -0.1063 0.0511  0.0075  19  MET A CA  
128  C C   . MET A 19  ? 1.2360 1.1026 0.7498 -0.1093 0.0566  0.0180  19  MET A C   
129  O O   . MET A 19  ? 1.2942 1.1720 0.7991 -0.1333 0.0658  0.0165  19  MET A O   
130  C CB  . MET A 19  ? 1.2735 1.0900 0.7884 -0.1098 0.0572  0.0119  19  MET A CB  
131  C CG  . MET A 19  ? 1.2343 1.0592 0.7719 -0.1171 0.0561  0.0005  19  MET A CG  
132  S SD  . MET A 19  ? 1.2862 1.1512 0.8390 -0.1490 0.0669  -0.0135 19  MET A SD  
133  C CE  . MET A 19  ? 1.4869 1.3136 0.9967 -0.1748 0.0845  -0.0046 19  MET A CE  
134  N N   . VAL A 20  ? 1.2460 1.0981 0.7491 -0.0845 0.0512  0.0275  20  VAL A N   
135  C CA  . VAL A 20  ? 1.2208 1.0693 0.7021 -0.0833 0.0560  0.0382  20  VAL A CA  
136  C C   . VAL A 20  ? 1.2313 1.1400 0.7365 -0.0924 0.0524  0.0320  20  VAL A C   
137  O O   . VAL A 20  ? 1.3746 1.2880 0.8643 -0.1123 0.0606  0.0352  20  VAL A O   
138  C CB  . VAL A 20  ? 1.1912 1.0235 0.6624 -0.0502 0.0498  0.0464  20  VAL A CB  
139  C CG1 . VAL A 20  ? 1.3094 1.1500 0.7655 -0.0457 0.0535  0.0562  20  VAL A CG1 
140  C CG2 . VAL A 20  ? 1.2682 1.0376 0.7073 -0.0416 0.0535  0.0527  20  VAL A CG2 
141  N N   . LEU A 21  ? 1.1666 1.1223 0.7087 -0.0781 0.0396  0.0225  21  LEU A N   
142  C CA  . LEU A 21  ? 1.1827 1.1967 0.7472 -0.0847 0.0342  0.0155  21  LEU A CA  
143  C C   . LEU A 21  ? 1.2917 1.3217 0.8554 -0.1158 0.0412  0.0061  21  LEU A C   
144  O O   . LEU A 21  ? 1.3600 1.4273 0.9262 -0.1289 0.0409  0.0025  21  LEU A O   
145  C CB  . LEU A 21  ? 1.0273 1.0832 0.6296 -0.0640 0.0199  0.0063  21  LEU A CB  
146  C CG  . LEU A 21  ? 1.0878 1.1396 0.6938 -0.0334 0.0134  0.0125  21  LEU A CG  
147  C CD1 . LEU A 21  ? 1.0814 1.1791 0.7256 -0.0162 0.0005  0.0022  21  LEU A CD1 
148  C CD2 . LEU A 21  ? 1.1066 1.1589 0.6945 -0.0297 0.0170  0.0234  21  LEU A CD2 
149  N N   . LYS A 22  ? 1.2928 1.2991 0.8540 -0.1272 0.0471  0.0005  22  LYS A N   
150  C CA  . LYS A 22  ? 1.3794 1.4001 0.9380 -0.1567 0.0562  -0.0104 22  LYS A CA  
151  C C   . LYS A 22  ? 1.4529 1.4479 0.9766 -0.1808 0.0706  -0.0033 22  LYS A C   
152  O O   . LYS A 22  ? 1.4433 1.4682 0.9645 -0.2046 0.0762  -0.0125 22  LYS A O   
153  C CB  . LYS A 22  ? 1.4448 1.4463 1.0109 -0.1608 0.0597  -0.0179 22  LYS A CB  
154  C CG  . LYS A 22  ? 1.4992 1.5301 1.0727 -0.1856 0.0672  -0.0342 22  LYS A CG  
155  C CD  . LYS A 22  ? 1.5317 1.5367 1.1085 -0.1908 0.0735  -0.0397 22  LYS A CD  
156  C CE  . LYS A 22  ? 1.5623 1.5944 1.1421 -0.2171 0.0846  -0.0567 22  LYS A CE  
157  N NZ  . LYS A 22  ? 1.5741 1.5786 1.1552 -0.2245 0.0932  -0.0614 22  LYS A NZ  
158  N N   . GLN A 23  ? 1.4725 1.4125 0.9670 -0.1748 0.0769  0.0121  23  GLN A N   
159  C CA  . GLN A 23  ? 1.5959 1.5082 1.0543 -0.1954 0.0907  0.0212  23  GLN A CA  
160  C C   . GLN A 23  ? 1.6031 1.5598 1.0651 -0.1966 0.0861  0.0229  23  GLN A C   
161  O O   . GLN A 23  ? 1.7514 1.7119 1.1938 -0.2225 0.0963  0.0226  23  GLN A O   
162  C CB  . GLN A 23  ? 1.6565 1.5013 1.0812 -0.1821 0.0965  0.0385  23  GLN A CB  
163  C CG  . GLN A 23  ? 1.7241 1.5232 1.1431 -0.1778 0.0988  0.0378  23  GLN A CG  
164  C CD  . GLN A 23  ? 1.9203 1.6999 1.3273 -0.2106 0.1136  0.0302  23  GLN A CD  
165  O OE1 . GLN A 23  ? 2.0103 1.7947 1.4011 -0.2377 0.1256  0.0286  23  GLN A OE1 
166  N NE2 . GLN A 23  ? 1.9045 1.6645 1.3202 -0.2085 0.1130  0.0245  23  GLN A NE2 
167  N N   . GLY A 24  ? 1.6201 1.6119 1.1074 -0.1698 0.0710  0.0239  24  GLY A N   
168  C CA  . GLY A 24  ? 1.5436 1.5824 1.0396 -0.1669 0.0640  0.0251  24  GLY A CA  
169  C C   . GLY A 24  ? 1.3979 1.4495 0.9121 -0.1313 0.0512  0.0319  24  GLY A C   
170  O O   . GLY A 24  ? 1.3772 1.3918 0.8864 -0.1101 0.0507  0.0384  24  GLY A O   
171  N N   . ASP A 25  ? 1.2906 1.3986 0.8262 -0.1246 0.0406  0.0288  25  ASP A N   
172  C CA  . ASP A 25  ? 1.1892 1.3205 0.7476 -0.0915 0.0284  0.0322  25  ASP A CA  
173  C C   . ASP A 25  ? 1.1967 1.2817 0.7290 -0.0730 0.0352  0.0483  25  ASP A C   
174  O O   . ASP A 25  ? 1.2674 1.3111 0.7629 -0.0869 0.0483  0.0591  25  ASP A O   
175  C CB  . ASP A 25  ? 1.1279 1.3257 0.7089 -0.0906 0.0174  0.0276  25  ASP A CB  
176  C CG  . ASP A 25  ? 1.1061 1.3508 0.7090 -0.1063 0.0097  0.0104  25  ASP A CG  
177  O OD1 . ASP A 25  ? 1.2151 1.4398 0.8132 -0.1204 0.0154  0.0028  25  ASP A OD1 
178  O OD2 . ASP A 25  ? 1.0989 1.4015 0.7236 -0.1031 -0.0023 0.0039  25  ASP A OD2 
179  N N   . ASN A 26  ? 1.1312 1.2214 0.6804 -0.0409 0.0271  0.0489  26  ASN A N   
180  C CA  . ASN A 26  ? 1.1800 1.2287 0.7039 -0.0184 0.0329  0.0614  26  ASN A CA  
181  C C   . ASN A 26  ? 1.1699 1.2518 0.7229 0.0166  0.0217  0.0573  26  ASN A C   
182  O O   . ASN A 26  ? 1.0929 1.2201 0.6839 0.0220  0.0103  0.0452  26  ASN A O   
183  C CB  . ASN A 26  ? 1.2105 1.1921 0.7048 -0.0210 0.0417  0.0650  26  ASN A CB  
184  C CG  . ASN A 26  ? 1.3589 1.2877 0.8115 -0.0071 0.0515  0.0799  26  ASN A CG  
185  O OD1 . ASN A 26  ? 1.3016 1.2457 0.7541 0.0168  0.0496  0.0855  26  ASN A OD1 
186  N ND2 . ASN A 26  ? 1.4712 1.3377 0.8877 -0.0201 0.0624  0.0856  26  ASN A ND2 
187  N N   . TYR A 27  ? 1.1829 1.2403 0.7155 0.0408  0.0261  0.0667  27  TYR A N   
188  C CA  . TYR A 27  ? 1.2006 1.2851 0.7549 0.0762  0.0187  0.0623  27  TYR A CA  
189  C C   . TYR A 27  ? 1.2799 1.3115 0.8073 0.0965  0.0234  0.0643  27  TYR A C   
190  O O   . TYR A 27  ? 1.3358 1.3086 0.8244 0.0852  0.0327  0.0724  27  TYR A O   
191  C CB  . TYR A 27  ? 1.1763 1.2943 0.7335 0.0909  0.0189  0.0695  27  TYR A CB  
192  C CG  . TYR A 27  ? 1.2947 1.3635 0.8040 0.0931  0.0323  0.0858  27  TYR A CG  
193  C CD1 . TYR A 27  ? 1.3200 1.3657 0.8019 0.0626  0.0415  0.0957  27  TYR A CD1 
194  C CD2 . TYR A 27  ? 1.3304 1.3756 0.8195 0.1263  0.0367  0.0904  27  TYR A CD2 
195  C CE1 . TYR A 27  ? 1.4556 1.4517 0.8907 0.0641  0.0549  0.1113  27  TYR A CE1 
196  C CE2 . TYR A 27  ? 1.3873 1.3842 0.8288 0.1305  0.0494  0.1058  27  TYR A CE2 
197  C CZ  . TYR A 27  ? 1.4969 1.4672 0.9113 0.0990  0.0588  0.1170  27  TYR A CZ  
198  O OH  . TYR A 27  ? 1.6059 1.5236 0.9700 0.1028  0.0726  0.1330  27  TYR A OH  
199  N N   . VAL A 28  ? 1.2540 1.3083 0.8015 0.1273  0.0168  0.0559  28  VAL A N   
200  C CA  . VAL A 28  ? 1.2054 1.2207 0.7351 0.1460  0.0175  0.0520  28  VAL A CA  
201  C C   . VAL A 28  ? 1.2537 1.2085 0.7296 0.1545  0.0287  0.0652  28  VAL A C   
202  O O   . VAL A 28  ? 1.3347 1.2357 0.7810 0.1487  0.0322  0.0674  28  VAL A O   
203  C CB  . VAL A 28  ? 1.0933 1.1503 0.6530 0.1780  0.0099  0.0390  28  VAL A CB  
204  C CG1 . VAL A 28  ? 1.1322 1.1507 0.6651 0.2018  0.0118  0.0352  28  VAL A CG1 
205  C CG2 . VAL A 28  ? 1.0037 1.1054 0.6103 0.1688  -0.0005 0.0253  28  VAL A CG2 
206  N N   . TYR A 29  ? 1.2650 1.2276 0.7269 0.1694  0.0342  0.0742  29  TYR A N   
207  C CA  . TYR A 29  ? 1.3188 1.2223 0.7260 0.1811  0.0455  0.0872  29  TYR A CA  
208  C C   . TYR A 29  ? 1.3717 1.2217 0.7441 0.1470  0.0552  0.0997  29  TYR A C   
209  O O   . TYR A 29  ? 1.3825 1.1677 0.7097 0.1488  0.0626  0.1067  29  TYR A O   
210  C CB  . TYR A 29  ? 1.3534 1.2830 0.7565 0.2050  0.0496  0.0940  29  TYR A CB  
211  C CG  . TYR A 29  ? 1.4435 1.4254 0.8790 0.2410  0.0421  0.0801  29  TYR A CG  
212  C CD1 . TYR A 29  ? 1.4699 1.4449 0.9088 0.2590  0.0370  0.0664  29  TYR A CD1 
213  C CD2 . TYR A 29  ? 1.4484 1.4902 0.9129 0.2562  0.0402  0.0794  29  TYR A CD2 
214  C CE1 . TYR A 29  ? 1.5463 1.5704 1.0145 0.2901  0.0316  0.0516  29  TYR A CE1 
215  C CE2 . TYR A 29  ? 1.4261 1.5185 0.9225 0.2887  0.0344  0.0648  29  TYR A CE2 
216  C CZ  . TYR A 29  ? 1.4931 1.5755 0.9905 0.3049  0.0309  0.0505  29  TYR A CZ  
217  O OH  . TYR A 29  ? 1.4803 1.6130 1.0083 0.3357  0.0267  0.0339  29  TYR A OH  
218  N N   . GLY A 30  ? 1.3582 1.2352 0.7501 0.1158  0.0553  0.1014  30  GLY A N   
219  C CA  . GLY A 30  ? 1.4365 1.2690 0.8002 0.0802  0.0650  0.1093  30  GLY A CA  
220  C C   . GLY A 30  ? 1.4930 1.2950 0.8566 0.0663  0.0629  0.1017  30  GLY A C   
221  O O   . GLY A 30  ? 1.6168 1.3604 0.9437 0.0494  0.0726  0.1086  30  GLY A O   
222  N N   . ILE A 31  ? 1.4313 1.2717 0.8357 0.0736  0.0507  0.0873  31  ILE A N   
223  C CA  . ILE A 31  ? 1.4414 1.2573 0.8487 0.0632  0.0477  0.0797  31  ILE A CA  
224  C C   . ILE A 31  ? 1.4974 1.2563 0.8671 0.0843  0.0500  0.0832  31  ILE A C   
225  O O   . ILE A 31  ? 1.5688 1.2793 0.9149 0.0703  0.0542  0.0853  31  ILE A O   
226  C CB  . ILE A 31  ? 1.3040 1.1745 0.7622 0.0681  0.0345  0.0640  31  ILE A CB  
227  C CG1 . ILE A 31  ? 1.2207 1.1394 0.7099 0.0429  0.0322  0.0596  31  ILE A CG1 
228  C CG2 . ILE A 31  ? 1.2845 1.1298 0.7445 0.0662  0.0304  0.0564  31  ILE A CG2 
229  C CD1 . ILE A 31  ? 1.1882 1.1610 0.7247 0.0501  0.0197  0.0455  31  ILE A CD1 
230  N N   . ILE A 32  ? 1.4258 1.1912 0.7885 0.1192  0.0471  0.0827  32  ILE A N   
231  C CA  . ILE A 32  ? 1.4697 1.1811 0.7900 0.1420  0.0492  0.0855  32  ILE A CA  
232  C C   . ILE A 32  ? 1.6630 1.3104 0.9299 0.1299  0.0631  0.1020  32  ILE A C   
233  O O   . ILE A 32  ? 1.7561 1.3457 0.9885 0.1265  0.0661  0.1050  32  ILE A O   
234  C CB  . ILE A 32  ? 1.3703 1.1066 0.6916 0.1830  0.0451  0.0802  32  ILE A CB  
235  C CG1 . ILE A 32  ? 1.3286 1.1180 0.6978 0.1938  0.0323  0.0622  32  ILE A CG1 
236  C CG2 . ILE A 32  ? 1.3724 1.0506 0.6399 0.2082  0.0489  0.0842  32  ILE A CG2 
237  C CD1 . ILE A 32  ? 1.3304 1.1502 0.7047 0.2327  0.0290  0.0533  32  ILE A CD1 
238  N N   . LYS A 33  ? 1.5824 1.2395 0.8419 0.1224  0.0716  0.1126  33  LYS A N   
239  C CA  . LYS A 33  ? 1.7768 1.3727 0.9838 0.1099  0.0865  0.1290  33  LYS A CA  
240  C C   . LYS A 33  ? 1.8688 1.4298 1.0675 0.0701  0.0927  0.1304  33  LYS A C   
241  O O   . LYS A 33  ? 2.0048 1.4988 1.1600 0.0662  0.1002  0.1370  33  LYS A O   
242  C CB  . LYS A 33  ? 1.8087 1.4312 1.0154 0.1075  0.0936  0.1390  33  LYS A CB  
243  C CG  . LYS A 33  ? 1.9318 1.4914 1.0833 0.0924  0.1106  0.1566  33  LYS A CG  
244  C CD  . LYS A 33  ? 2.0761 1.5781 1.1740 0.1271  0.1162  0.1652  33  LYS A CD  
245  C CE  . LYS A 33  ? 2.1654 1.6042 1.2058 0.1149  0.1342  0.1842  33  LYS A CE  
246  N NZ  . LYS A 33  ? 2.2095 1.5890 1.2243 0.0794  0.1426  0.1873  33  LYS A NZ  
247  N N   . GLN A 34  ? 1.9570 1.5638 1.1966 0.0413  0.0899  0.1230  34  GLN A N   
248  C CA  . GLN A 34  ? 2.0099 1.5910 1.2430 0.0025  0.0979  0.1226  34  GLN A CA  
249  C C   . GLN A 34  ? 2.0804 1.6194 1.3033 0.0031  0.0951  0.1173  34  GLN A C   
250  O O   . GLN A 34  ? 2.2115 1.6971 1.4031 -0.0179 0.1057  0.1224  34  GLN A O   
251  C CB  . GLN A 34  ? 1.9010 1.5462 1.1822 -0.0230 0.0930  0.1116  34  GLN A CB  
252  C CG  . GLN A 34  ? 1.9480 1.6320 1.2359 -0.0345 0.0970  0.1163  34  GLN A CG  
253  C CD  . GLN A 34  ? 1.9291 1.6604 1.2496 -0.0675 0.0956  0.1054  34  GLN A CD  
254  O OE1 . GLN A 34  ? 1.8445 1.5786 1.1824 -0.0813 0.0930  0.0945  34  GLN A OE1 
255  N NE2 . GLN A 34  ? 1.9515 1.7225 1.2797 -0.0791 0.0970  0.1074  34  GLN A NE2 
256  N N   . VAL A 35  ? 1.9800 1.5426 1.2287 0.0267  0.0809  0.1066  35  VAL A N   
257  C CA  . VAL A 35  ? 2.0119 1.5441 1.2575 0.0261  0.0760  0.1001  35  VAL A CA  
258  C C   . VAL A 35  ? 2.1229 1.5841 1.3130 0.0443  0.0802  0.1092  35  VAL A C   
259  O O   . VAL A 35  ? 2.1694 1.5823 1.3371 0.0306  0.0842  0.1106  35  VAL A O   
260  C CB  . VAL A 35  ? 1.8904 1.4714 1.1800 0.0444  0.0595  0.0855  35  VAL A CB  
261  C CG1 . VAL A 35  ? 1.8310 1.3783 1.1106 0.0527  0.0526  0.0799  35  VAL A CG1 
262  C CG2 . VAL A 35  ? 1.7486 1.3877 1.0882 0.0215  0.0561  0.0759  35  VAL A CG2 
263  N N   . LYS A 36  ? 2.0468 1.5014 1.2130 0.0766  0.0796  0.1147  36  LYS A N   
264  C CA  . LYS A 36  ? 2.1440 1.5328 1.2543 0.0994  0.0823  0.1217  36  LYS A CA  
265  C C   . LYS A 36  ? 2.1829 1.5034 1.2450 0.0759  0.0988  0.1361  36  LYS A C   
266  O O   . LYS A 36  ? 2.2177 1.4763 1.2385 0.0818  0.1004  0.1395  36  LYS A O   
267  C CB  . LYS A 36  ? 2.1651 1.5656 1.2589 0.1391  0.0805  0.1239  36  LYS A CB  
268  C CG  . LYS A 36  ? 2.2274 1.5781 1.2738 0.1724  0.0767  0.1233  36  LYS A CG  
269  C CD  . LYS A 36  ? 2.2298 1.6020 1.2645 0.2145  0.0745  0.1213  36  LYS A CD  
270  C CE  . LYS A 36  ? 2.2798 1.6193 1.2777 0.2493  0.0663  0.1135  36  LYS A CE  
271  N NZ  . LYS A 36  ? 2.3926 1.6467 1.3273 0.2461  0.0737  0.1252  36  LYS A NZ  
272  N N   . GLU A 37  ? 2.1519 1.4826 1.2176 0.0486  0.1110  0.1438  37  GLU A N   
273  C CA  . GLU A 37  ? 2.2311 1.4969 1.2496 0.0241  0.1287  0.1570  37  GLU A CA  
274  C C   . GLU A 37  ? 2.2205 1.4716 1.2509 -0.0135 0.1329  0.1509  37  GLU A C   
275  O O   . GLU A 37  ? 2.2607 1.4471 1.2489 -0.0311 0.1463  0.1591  37  GLU A O   
276  C CB  . GLU A 37  ? 2.2877 1.5704 1.3016 0.0092  0.1411  0.1672  37  GLU A CB  
277  C CG  . GLU A 37  ? 2.2957 1.6168 1.3449 -0.0342 0.1461  0.1612  37  GLU A CG  
278  C CD  . GLU A 37  ? 2.3479 1.6915 1.3934 -0.0488 0.1562  0.1699  37  GLU A CD  
279  O OE1 . GLU A 37  ? 2.3278 1.6563 1.3443 -0.0248 0.1600  0.1820  37  GLU A OE1 
280  O OE2 . GLU A 37  ? 2.3515 1.7295 1.4220 -0.0836 0.1604  0.1639  37  GLU A OE2 
281  N N   . ALA A 38  ? 2.2369 1.5466 1.3232 -0.0260 0.1229  0.1363  38  ALA A N   
282  C CA  . ALA A 38  ? 2.1429 1.4448 1.2444 -0.0568 0.1257  0.1280  38  ALA A CA  
283  C C   . ALA A 38  ? 2.1153 1.3875 1.2113 -0.0405 0.1151  0.1223  38  ALA A C   
284  O O   . ALA A 38  ? 2.1109 1.3573 1.2054 -0.0625 0.1196  0.1183  38  ALA A O   
285  C CB  . ALA A 38  ? 1.9666 1.3441 1.1279 -0.0760 0.1201  0.1144  38  ALA A CB  
286  N N   . SER A 39  ? 2.1060 1.3843 1.1997 -0.0026 0.1011  0.1204  39  SER A N   
287  C CA  . SER A 39  ? 2.0977 1.3441 1.1772 0.0167  0.0900  0.1155  39  SER A CA  
288  C C   . SER A 39  ? 2.2562 1.4258 1.2679 0.0352  0.0961  0.1277  39  SER A C   
289  O O   . SER A 39  ? 2.2399 1.3817 1.2315 0.0586  0.0852  0.1240  39  SER A O   
290  C CB  . SER A 39  ? 2.0582 1.3554 1.1707 0.0475  0.0712  0.1039  39  SER A CB  
291  O OG  . SER A 39  ? 2.1168 1.4182 1.2086 0.0787  0.0701  0.1088  39  SER A OG  
292  N N   . ASN A 40  ? 2.3053 1.4404 1.2799 0.0256  0.1131  0.1419  40  ASN A N   
293  C CA  . ASN A 40  ? 2.3013 1.3606 1.2064 0.0440  0.1213  0.1554  40  ASN A CA  
294  C C   . ASN A 40  ? 2.3599 1.4223 1.2477 0.0925  0.1073  0.1522  40  ASN A C   
295  O O   . ASN A 40  ? 2.3870 1.3951 1.2293 0.1145  0.1032  0.1537  40  ASN A O   
296  C CB  . ASN A 40  ? 2.3414 1.3314 1.2129 0.0259  0.1276  0.1580  40  ASN A CB  
297  C CG  . ASN A 40  ? 2.3081 1.2977 1.1964 -0.0227 0.1433  0.1585  40  ASN A CG  
298  O OD1 . ASN A 40  ? 2.1764 1.1610 1.0828 -0.0438 0.1421  0.1501  40  ASN A OD1 
299  N ND2 . ASN A 40  ? 2.3820 1.3806 1.2652 -0.0403 0.1582  0.1671  40  ASN A ND2 
300  N N   . GLY A 41  ? 2.5719 1.7015 1.4973 0.1093  0.0997  0.1460  41  GLY A N   
301  C CA  . GLY A 41  ? 2.5085 1.6534 1.4231 0.1543  0.0884  0.1404  41  GLY A CA  
302  C C   . GLY A 41  ? 2.4466 1.6208 1.3887 0.1711  0.0688  0.1231  41  GLY A C   
303  O O   . GLY A 41  ? 2.3902 1.5917 1.3327 0.2065  0.0590  0.1146  41  GLY A O   
304  N N   . GLU A 42  ? 2.2820 1.4553 1.2485 0.1471  0.0629  0.1164  42  GLU A N   
305  C CA  . GLU A 42  ? 2.1716 1.3628 1.1552 0.1642  0.0441  0.1011  42  GLU A CA  
306  C C   . GLU A 42  ? 2.1698 1.4406 1.2090 0.1755  0.0327  0.0873  42  GLU A C   
307  O O   . GLU A 42  ? 2.2156 1.5035 1.2540 0.2053  0.0192  0.0754  42  GLU A O   
308  C CB  . GLU A 42  ? 2.1609 1.3369 1.1616 0.1357  0.0409  0.0973  42  GLU A CB  
309  C CG  . GLU A 42  ? 2.1351 1.2303 1.0810 0.1288  0.0480  0.1067  42  GLU A CG  
310  C CD  . GLU A 42  ? 2.1487 1.2397 1.1204 0.1015  0.0440  0.1004  42  GLU A CD  
311  O OE1 . GLU A 42  ? 2.0961 1.2471 1.1270 0.0880  0.0367  0.0896  42  GLU A OE1 
312  O OE2 . GLU A 42  ? 2.1582 1.1864 1.0910 0.0944  0.0484  0.1060  42  GLU A OE2 
313  N N   . MET A 43  ? 2.0776 1.3976 1.1635 0.1524  0.0379  0.0875  43  MET A N   
314  C CA  . MET A 43  ? 2.0792 1.4723 1.2226 0.1566  0.0271  0.0739  43  MET A CA  
315  C C   . MET A 43  ? 2.0934 1.5262 1.2459 0.1756  0.0300  0.0744  43  MET A C   
316  O O   . MET A 43  ? 2.0836 1.5147 1.2295 0.1641  0.0423  0.0858  43  MET A O   
317  C CB  . MET A 43  ? 1.9981 1.4252 1.1912 0.1202  0.0285  0.0708  43  MET A CB  
318  C CG  . MET A 43  ? 1.9083 1.4017 1.1567 0.1252  0.0158  0.0559  43  MET A CG  
319  S SD  . MET A 43  ? 1.6210 1.1478 0.9215 0.0880  0.0154  0.0500  43  MET A SD  
320  C CE  . MET A 43  ? 1.5410 1.1346 0.8926 0.1045  0.0001  0.0337  43  MET A CE  
321  N N   . GLU A 44  ? 2.2886 1.7605 1.4584 0.2036  0.0187  0.0610  44  GLU A N   
322  C CA  . GLU A 44  ? 2.3132 1.8234 1.4893 0.2291  0.0202  0.0582  44  GLU A CA  
323  C C   . GLU A 44  ? 2.1815 1.7634 1.4178 0.2294  0.0107  0.0432  44  GLU A C   
324  O O   . GLU A 44  ? 2.2151 1.8142 1.4622 0.2452  -0.0006 0.0285  44  GLU A O   
325  C CB  . GLU A 44  ? 2.4131 1.8953 1.5409 0.2691  0.0175  0.0544  44  GLU A CB  
326  C CG  . GLU A 44  ? 2.3969 1.9210 1.5297 0.3011  0.0188  0.0480  44  GLU A CG  
327  C CD  . GLU A 44  ? 2.4464 1.9450 1.5297 0.3420  0.0155  0.0406  44  GLU A CD  
328  O OE1 . GLU A 44  ? 2.5366 1.9736 1.5715 0.3448  0.0148  0.0458  44  GLU A OE1 
329  O OE2 . GLU A 44  ? 2.4105 1.9518 1.5029 0.3720  0.0134  0.0281  44  GLU A OE2 
330  N N   . LEU A 45  ? 1.8871 1.5104 1.1607 0.2120  0.0153  0.0463  45  LEU A N   
331  C CA  . LEU A 45  ? 1.7310 1.4186 1.0614 0.2086  0.0073  0.0333  45  LEU A CA  
332  C C   . LEU A 45  ? 1.6806 1.4096 1.0208 0.2400  0.0057  0.0248  45  LEU A C   
333  O O   . LEU A 45  ? 1.6964 1.4175 1.0112 0.2564  0.0134  0.0325  45  LEU A O   
334  C CB  . LEU A 45  ? 1.5902 1.3046 0.9545 0.1763  0.0118  0.0390  45  LEU A CB  
335  C CG  . LEU A 45  ? 1.6139 1.2902 0.9669 0.1437  0.0170  0.0473  45  LEU A CG  
336  C CD1 . LEU A 45  ? 1.4765 1.1823 0.8567 0.1145  0.0229  0.0516  45  LEU A CD1 
337  C CD2 . LEU A 45  ? 1.5826 1.2555 0.9510 0.1382  0.0076  0.0372  45  LEU A CD2 
338  N N   . ASN A 46  ? 1.6831 1.4585 1.0616 0.2481  -0.0034 0.0086  46  ASN A N   
339  C CA  . ASN A 46  ? 1.6675 1.4864 1.0591 0.2779  -0.0047 -0.0031 46  ASN A CA  
340  C C   . ASN A 46  ? 1.6043 1.4794 1.0431 0.2684  -0.0032 -0.0037 46  ASN A C   
341  O O   . ASN A 46  ? 1.5293 1.4261 1.0045 0.2439  -0.0071 -0.0054 46  ASN A O   
342  C CB  . ASN A 46  ? 1.6563 1.4944 1.0597 0.2944  -0.0145 -0.0229 46  ASN A CB  
343  C CG  . ASN A 46  ? 1.6953 1.5832 1.1158 0.3231  -0.0143 -0.0375 46  ASN A CG  
344  O OD1 . ASN A 46  ? 1.7137 1.6496 1.1786 0.3201  -0.0185 -0.0500 46  ASN A OD1 
345  N ND2 . ASN A 46  ? 1.7571 1.6346 1.1427 0.3516  -0.0083 -0.0361 46  ASN A ND2 
346  N N   . GLU A 47  ? 1.6600 1.5596 1.0973 0.2893  0.0020  -0.0026 47  GLU A N   
347  C CA  . GLU A 47  ? 1.5593 1.5156 1.0408 0.2839  0.0022  -0.0038 47  GLU A CA  
348  C C   . GLU A 47  ? 1.5465 1.5500 1.0761 0.2819  -0.0063 -0.0210 47  GLU A C   
349  O O   . GLU A 47  ? 1.5259 1.5513 1.0894 0.2576  -0.0097 -0.0203 47  GLU A O   
350  C CB  . GLU A 47  ? 1.6572 1.6367 1.1306 0.3138  0.0081  -0.0035 47  GLU A CB  
351  C CG  . GLU A 47  ? 1.6793 1.6895 1.1734 0.3030  0.0118  0.0071  47  GLU A CG  
352  C CD  . GLU A 47  ? 1.6884 1.7276 1.1786 0.3359  0.0171  0.0059  47  GLU A CD  
353  O OE1 . GLU A 47  ? 1.7326 1.7542 1.1919 0.3655  0.0201  -0.0003 47  GLU A OE1 
354  O OE2 . GLU A 47  ? 1.6479 1.7253 1.1615 0.3327  0.0187  0.0119  47  GLU A OE2 
355  N N   . ALA A 48  ? 1.5646 1.5830 1.0948 0.3077  -0.0092 -0.0377 48  ALA A N   
356  C CA  . ALA A 48  ? 1.5227 1.5864 1.0965 0.3084  -0.0155 -0.0555 48  ALA A CA  
357  C C   . ALA A 48  ? 1.4117 1.4625 1.0016 0.2801  -0.0218 -0.0556 48  ALA A C   
358  O O   . ALA A 48  ? 1.3029 1.3898 0.9336 0.2701  -0.0259 -0.0639 48  ALA A O   
359  C CB  . ALA A 48  ? 1.5548 1.6294 1.1177 0.3395  -0.0165 -0.0745 48  ALA A CB  
360  N N   . THR A 49  ? 1.3888 1.3887 0.9472 0.2681  -0.0224 -0.0468 49  THR A N   
361  C CA  . THR A 49  ? 1.3716 1.3613 0.9463 0.2413  -0.0275 -0.0459 49  THR A CA  
362  C C   . THR A 49  ? 1.2395 1.2451 0.8385 0.2156  -0.0252 -0.0359 49  THR A C   
363  O O   . THR A 49  ? 1.1643 1.2007 0.8000 0.2034  -0.0293 -0.0422 49  THR A O   
364  C CB  . THR A 49  ? 1.4367 1.3705 0.9731 0.2353  -0.0285 -0.0393 49  THR A CB  
365  O OG1 . THR A 49  ? 1.4735 1.3915 0.9783 0.2632  -0.0304 -0.0477 49  THR A OG1 
366  C CG2 . THR A 49  ? 1.2932 1.2242 0.8499 0.2151  -0.0352 -0.0438 49  THR A CG2 
367  N N   . LEU A 50  ? 1.2601 1.2463 0.8372 0.2083  -0.0185 -0.0210 50  LEU A N   
368  C CA  . LEU A 50  ? 1.1866 1.1904 0.7826 0.1840  -0.0163 -0.0127 50  LEU A CA  
369  C C   . LEU A 50  ? 1.1245 1.1877 0.7642 0.1885  -0.0205 -0.0217 50  LEU A C   
370  O O   . LEU A 50  ? 1.0670 1.1527 0.7332 0.1688  -0.0234 -0.0225 50  LEU A O   
371  C CB  . LEU A 50  ? 1.2383 1.2188 0.8032 0.1804  -0.0077 0.0029  50  LEU A CB  
372  C CG  . LEU A 50  ? 1.2253 1.1589 0.7629 0.1539  -0.0021 0.0148  50  LEU A CG  
373  C CD1 . LEU A 50  ? 1.2844 1.1701 0.7949 0.1574  -0.0034 0.0134  50  LEU A CD1 
374  C CD2 . LEU A 50  ? 1.2339 1.1473 0.7412 0.1504  0.0075  0.0296  50  LEU A CD2 
375  N N   . TYR A 51  ? 1.1374 1.2276 0.7842 0.2151  -0.0206 -0.0292 51  TYR A N   
376  C CA  . TYR A 51  ? 1.0936 1.2407 0.7834 0.2206  -0.0247 -0.0392 51  TYR A CA  
377  C C   . TYR A 51  ? 1.0455 1.2057 0.7634 0.2119  -0.0309 -0.0513 51  TYR A C   
378  O O   . TYR A 51  ? 0.9724 1.1613 0.7203 0.1980  -0.0347 -0.0534 51  TYR A O   
379  C CB  . TYR A 51  ? 1.1801 1.3542 0.8731 0.2525  -0.0226 -0.0482 51  TYR A CB  
380  C CG  . TYR A 51  ? 1.2415 1.4104 0.9107 0.2646  -0.0162 -0.0367 51  TYR A CG  
381  C CD1 . TYR A 51  ? 1.2120 1.4006 0.8917 0.2514  -0.0154 -0.0256 51  TYR A CD1 
382  C CD2 . TYR A 51  ? 1.3358 1.4834 0.9716 0.2908  -0.0110 -0.0379 51  TYR A CD2 
383  C CE1 . TYR A 51  ? 1.1979 1.3826 0.8557 0.2625  -0.0091 -0.0144 51  TYR A CE1 
384  C CE2 . TYR A 51  ? 1.4323 1.5748 1.0452 0.3037  -0.0043 -0.0270 51  TYR A CE2 
385  C CZ  . TYR A 51  ? 1.3207 1.4812 0.9451 0.2893  -0.0030 -0.0147 51  TYR A CZ  
386  O OH  . TYR A 51  ? 1.3380 1.4920 0.9377 0.3028  0.0043  -0.0032 51  TYR A OH  
387  N N   . THR A 52  ? 1.0323 1.1700 0.7381 0.2197  -0.0323 -0.0593 52  THR A N   
388  C CA  . THR A 52  ? 1.0055 1.1515 0.7347 0.2112  -0.0375 -0.0700 52  THR A CA  
389  C C   . THR A 52  ? 1.0115 1.1410 0.7441 0.1832  -0.0391 -0.0617 52  THR A C   
390  O O   . THR A 52  ? 0.9600 1.1130 0.7215 0.1725  -0.0425 -0.0668 52  THR A O   
391  C CB  . THR A 52  ? 1.0685 1.1934 0.7795 0.2253  -0.0391 -0.0798 52  THR A CB  
392  O OG1 . THR A 52  ? 1.1045 1.2510 0.8129 0.2526  -0.0366 -0.0902 52  THR A OG1 
393  C CG2 . THR A 52  ? 1.0584 1.1932 0.7934 0.2169  -0.0441 -0.0909 52  THR A CG2 
394  N N   . ILE A 53  ? 1.0413 1.1313 0.7438 0.1717  -0.0359 -0.0495 53  ILE A N   
395  C CA  . ILE A 53  ? 0.9931 1.0683 0.6983 0.1463  -0.0363 -0.0443 53  ILE A CA  
396  C C   . ILE A 53  ? 0.9701 1.0742 0.6943 0.1303  -0.0356 -0.0403 53  ILE A C   
397  O O   . ILE A 53  ? 0.8897 1.0021 0.6298 0.1137  -0.0375 -0.0425 53  ILE A O   
398  C CB  . ILE A 53  ? 0.9846 1.0100 0.6527 0.1380  -0.0322 -0.0338 53  ILE A CB  
399  C CG1 . ILE A 53  ? 1.1095 1.1083 0.7562 0.1561  -0.0349 -0.0389 53  ILE A CG1 
400  C CG2 . ILE A 53  ? 0.8550 0.8698 0.5293 0.1131  -0.0319 -0.0313 53  ILE A CG2 
401  C CD1 . ILE A 53  ? 1.1445 1.1586 0.8138 0.1603  -0.0420 -0.0524 53  ILE A CD1 
402  N N   . PHE A 54  ? 0.9821 1.1042 0.7045 0.1361  -0.0332 -0.0353 54  PHE A N   
403  C CA  . PHE A 54  ? 0.9536 1.1053 0.6916 0.1207  -0.0339 -0.0323 54  PHE A CA  
404  C C   . PHE A 54  ? 0.9450 1.1420 0.7210 0.1246  -0.0408 -0.0435 54  PHE A C   
405  O O   . PHE A 54  ? 0.8951 1.1143 0.6851 0.1097  -0.0435 -0.0442 54  PHE A O   
406  C CB  . PHE A 54  ? 0.9360 1.0944 0.6602 0.1254  -0.0300 -0.0230 54  PHE A CB  
407  C CG  . PHE A 54  ? 0.9321 1.0480 0.6194 0.1108  -0.0221 -0.0102 54  PHE A CG  
408  C CD1 . PHE A 54  ? 0.9472 1.0236 0.6175 0.0964  -0.0193 -0.0084 54  PHE A CD1 
409  C CD2 . PHE A 54  ? 0.9802 1.0968 0.6508 0.1104  -0.0171 0.0000  54  PHE A CD2 
410  C CE1 . PHE A 54  ? 0.9156 0.9517 0.5523 0.0819  -0.0112 0.0025  54  PHE A CE1 
411  C CE2 . PHE A 54  ? 1.0319 1.1063 0.6667 0.0952  -0.0085 0.0116  54  PHE A CE2 
412  C CZ  . PHE A 54  ? 0.9362 0.9693 0.5539 0.0806  -0.0053 0.0126  54  PHE A CZ  
413  N N   . LYS A 55  ? 1.0514 1.2632 0.8427 0.1448  -0.0434 -0.0533 55  LYS A N   
414  C CA  . LYS A 55  ? 1.0005 1.2489 0.8263 0.1479  -0.0490 -0.0647 55  LYS A CA  
415  C C   . LYS A 55  ? 0.9404 1.1784 0.7729 0.1319  -0.0511 -0.0678 55  LYS A C   
416  O O   . LYS A 55  ? 0.9260 1.1887 0.7769 0.1232  -0.0548 -0.0710 55  LYS A O   
417  C CB  . LYS A 55  ? 0.9937 1.2543 0.8312 0.1706  -0.0492 -0.0763 55  LYS A CB  
418  C CG  . LYS A 55  ? 1.0370 1.3356 0.8895 0.1886  -0.0492 -0.0797 55  LYS A CG  
419  C CD  . LYS A 55  ? 1.1142 1.4253 0.9774 0.2105  -0.0477 -0.0943 55  LYS A CD  
420  C CE  . LYS A 55  ? 1.2513 1.6110 1.1409 0.2276  -0.0482 -0.1016 55  LYS A CE  
421  N NZ  . LYS A 55  ? 1.2878 1.6814 1.2096 0.2180  -0.0543 -0.1050 55  LYS A NZ  
422  N N   . ARG A 56  ? 0.8807 1.0831 0.6972 0.1289  -0.0491 -0.0671 56  ARG A N   
423  C CA  . ARG A 56  ? 0.9266 1.1203 0.7506 0.1162  -0.0507 -0.0704 56  ARG A CA  
424  C C   . ARG A 56  ? 0.9309 1.1293 0.7529 0.0963  -0.0498 -0.0650 56  ARG A C   
425  O O   . ARG A 56  ? 0.8917 1.1081 0.7304 0.0896  -0.0524 -0.0703 56  ARG A O   
426  C CB  . ARG A 56  ? 0.9353 1.0914 0.7410 0.1166  -0.0494 -0.0696 56  ARG A CB  
427  C CG  . ARG A 56  ? 0.9803 1.1273 0.7934 0.1043  -0.0507 -0.0721 56  ARG A CG  
428  C CD  . ARG A 56  ? 1.0363 1.2088 0.8767 0.1083  -0.0541 -0.0822 56  ARG A CD  
429  N NE  . ARG A 56  ? 1.0303 1.2014 0.8788 0.0957  -0.0543 -0.0832 56  ARG A NE  
430  C CZ  . ARG A 56  ? 1.1125 1.2667 0.9612 0.0942  -0.0551 -0.0857 56  ARG A CZ  
431  N NH1 . ARG A 56  ? 1.0827 1.2195 0.9230 0.1034  -0.0568 -0.0881 56  ARG A NH1 
432  N NH2 . ARG A 56  ? 1.0759 1.2331 0.9330 0.0843  -0.0546 -0.0866 56  ARG A NH2 
433  N N   . LEU A 57  ? 0.9340 1.1162 0.7337 0.0868  -0.0453 -0.0554 57  LEU A N   
434  C CA  . LEU A 57  ? 0.9390 1.1262 0.7340 0.0662  -0.0431 -0.0522 57  LEU A CA  
435  C C   . LEU A 57  ? 0.9483 1.1791 0.7614 0.0646  -0.0477 -0.0562 57  LEU A C   
436  O O   . LEU A 57  ? 0.9268 1.1730 0.7451 0.0516  -0.0487 -0.0602 57  LEU A O   
437  C CB  . LEU A 57  ? 0.8574 1.0165 0.6228 0.0559  -0.0361 -0.0415 57  LEU A CB  
438  C CG  . LEU A 57  ? 0.7879 0.9024 0.5337 0.0552  -0.0324 -0.0381 57  LEU A CG  
439  C CD1 . LEU A 57  ? 0.7277 0.8109 0.4415 0.0516  -0.0256 -0.0271 57  LEU A CD1 
440  C CD2 . LEU A 57  ? 0.7071 0.8146 0.4575 0.0394  -0.0309 -0.0418 57  LEU A CD2 
441  N N   . GLU A 58  ? 0.8935 1.1469 0.7157 0.0785  -0.0509 -0.0562 58  GLU A N   
442  C CA  . GLU A 58  ? 0.8819 1.1798 0.7232 0.0784  -0.0572 -0.0608 58  GLU A CA  
443  C C   . GLU A 58  ? 0.9205 1.2379 0.7864 0.0849  -0.0630 -0.0717 58  GLU A C   
444  O O   . GLU A 58  ? 0.8966 1.2432 0.7732 0.0796  -0.0683 -0.0767 58  GLU A O   
445  C CB  . GLU A 58  ? 0.9452 1.2651 0.7923 0.0927  -0.0592 -0.0580 58  GLU A CB  
446  C CG  . GLU A 58  ? 0.9675 1.3312 0.8266 0.0877  -0.0656 -0.0593 58  GLU A CG  
447  C CD  . GLU A 58  ? 0.9453 1.3337 0.8116 0.1023  -0.0674 -0.0559 58  GLU A CD  
448  O OE1 . GLU A 58  ? 0.8686 1.2340 0.7213 0.1127  -0.0612 -0.0500 58  GLU A OE1 
449  O OE2 . GLU A 58  ? 1.0073 1.4400 0.8928 0.1044  -0.0754 -0.0598 58  GLU A OE2 
450  N N   . LYS A 59  ? 0.9889 1.2907 0.8619 0.0965  -0.0621 -0.0760 59  LYS A N   
451  C CA  . LYS A 59  ? 1.0268 1.3405 0.9199 0.1011  -0.0658 -0.0858 59  LYS A CA  
452  C C   . LYS A 59  ? 1.0029 1.3092 0.8910 0.0867  -0.0653 -0.0871 59  LYS A C   
453  O O   . LYS A 59  ? 1.0482 1.3739 0.9489 0.0872  -0.0693 -0.0939 59  LYS A O   
454  C CB  . LYS A 59  ? 1.0534 1.3488 0.9511 0.1134  -0.0637 -0.0905 59  LYS A CB  
455  C CG  . LYS A 59  ? 1.1920 1.5052 1.1131 0.1221  -0.0668 -0.1014 59  LYS A CG  
456  C CD  . LYS A 59  ? 1.2219 1.5111 1.1429 0.1262  -0.0638 -0.1064 59  LYS A CD  
457  C CE  . LYS A 59  ? 1.2246 1.5035 1.1380 0.1381  -0.0610 -0.1075 59  LYS A CE  
458  N NZ  . LYS A 59  ? 1.3880 1.6513 1.3035 0.1430  -0.0595 -0.1157 59  LYS A NZ  
459  N N   . ASP A 60  ? 0.8956 1.1741 0.7647 0.0750  -0.0599 -0.0813 60  ASP A N   
460  C CA  . ASP A 60  ? 0.8641 1.1367 0.7290 0.0624  -0.0578 -0.0835 60  ASP A CA  
461  C C   . ASP A 60  ? 0.8703 1.1621 0.7260 0.0479  -0.0573 -0.0833 60  ASP A C   
462  O O   . ASP A 60  ? 0.8520 1.1400 0.7008 0.0363  -0.0537 -0.0859 60  ASP A O   
463  C CB  . ASP A 60  ? 0.9604 1.1961 0.8124 0.0576  -0.0523 -0.0793 60  ASP A CB  
464  C CG  . ASP A 60  ? 1.0790 1.2975 0.9363 0.0717  -0.0535 -0.0805 60  ASP A CG  
465  O OD1 . ASP A 60  ? 1.1066 1.3424 0.9798 0.0840  -0.0572 -0.0862 60  ASP A OD1 
466  O OD2 . ASP A 60  ? 1.0932 1.2824 0.9384 0.0705  -0.0509 -0.0770 60  ASP A OD2 
467  N N   . GLY A 61  ? 0.8603 1.1758 0.7161 0.0484  -0.0608 -0.0815 61  GLY A N   
468  C CA  . GLY A 61  ? 0.8106 1.1486 0.6569 0.0338  -0.0612 -0.0829 61  GLY A CA  
469  C C   . GLY A 61  ? 0.8875 1.2027 0.7108 0.0159  -0.0523 -0.0770 61  GLY A C   
470  O O   . GLY A 61  ? 0.9039 1.2349 0.7179 0.0007  -0.0503 -0.0814 61  GLY A O   
471  N N   . ILE A 62  ? 0.9205 1.1988 0.7327 0.0175  -0.0466 -0.0683 62  ILE A N   
472  C CA  . ILE A 62  ? 0.9119 1.1628 0.7006 0.0004  -0.0373 -0.0624 62  ILE A CA  
473  C C   . ILE A 62  ? 0.9178 1.1706 0.6905 -0.0059 -0.0349 -0.0544 62  ILE A C   
474  O O   . ILE A 62  ? 0.9094 1.1571 0.6640 -0.0254 -0.0280 -0.0529 62  ILE A O   
475  C CB  . ILE A 62  ? 0.8936 1.1011 0.6750 0.0052  -0.0330 -0.0575 62  ILE A CB  
476  C CG1 . ILE A 62  ? 0.8575 1.0644 0.6538 0.0083  -0.0345 -0.0653 62  ILE A CG1 
477  C CG2 . ILE A 62  ? 0.8678 1.0429 0.6234 -0.0113 -0.0233 -0.0506 62  ILE A CG2 
478  C CD1 . ILE A 62  ? 0.8947 1.1142 0.6898 -0.0078 -0.0301 -0.0724 62  ILE A CD1 
479  N N   . ILE A 63  ? 0.9796 1.2419 0.7590 0.0099  -0.0397 -0.0499 63  ILE A N   
480  C CA  . ILE A 63  ? 0.9481 1.2157 0.7139 0.0065  -0.0378 -0.0418 63  ILE A CA  
481  C C   . ILE A 63  ? 0.9645 1.2771 0.7522 0.0206  -0.0478 -0.0449 63  ILE A C   
482  O O   . ILE A 63  ? 0.8893 1.2194 0.7004 0.0361  -0.0548 -0.0519 63  ILE A O   
483  C CB  . ILE A 63  ? 0.9127 1.1380 0.6576 0.0141  -0.0310 -0.0303 63  ILE A CB  
484  C CG1 . ILE A 63  ? 0.9140 1.1389 0.6739 0.0402  -0.0359 -0.0318 63  ILE A CG1 
485  C CG2 . ILE A 63  ? 0.9415 1.1211 0.6651 0.0010  -0.0221 -0.0273 63  ILE A CG2 
486  C CD1 . ILE A 63  ? 0.9003 1.0947 0.6392 0.0530  -0.0308 -0.0222 63  ILE A CD1 
487  N N   . SER A 64  ? 1.0333 1.3648 0.8131 0.0147  -0.0480 -0.0399 64  SER A N   
488  C CA  . SER A 64  ? 0.9877 1.3638 0.7878 0.0282  -0.0574 -0.0414 64  SER A CA  
489  C C   . SER A 64  ? 1.0554 1.4277 0.8389 0.0277  -0.0529 -0.0298 64  SER A C   
490  O O   . SER A 64  ? 1.0463 1.3818 0.8005 0.0138  -0.0425 -0.0213 64  SER A O   
491  C CB  . SER A 64  ? 0.9494 1.3731 0.7636 0.0197  -0.0671 -0.0520 64  SER A CB  
492  O OG  . SER A 64  ? 0.9359 1.3736 0.7326 0.0000  -0.0653 -0.0497 64  SER A OG  
493  N N   . SER A 65  ? 1.0636 1.4745 0.8662 0.0437  -0.0605 -0.0296 65  SER A N   
494  C CA  . SER A 65  ? 0.9644 1.3754 0.7552 0.0497  -0.0566 -0.0185 65  SER A CA  
495  C C   . SER A 65  ? 0.9183 1.3863 0.7242 0.0472  -0.0662 -0.0202 65  SER A C   
496  O O   . SER A 65  ? 0.8786 1.3899 0.7092 0.0479  -0.0780 -0.0311 65  SER A O   
497  C CB  . SER A 65  ? 0.9396 1.3415 0.7390 0.0785  -0.0549 -0.0161 65  SER A CB  
498  O OG  . SER A 65  ? 0.9490 1.3919 0.7852 0.0966  -0.0651 -0.0271 65  SER A OG  
499  N N   . TYR A 66  ? 0.9417 1.4092 0.7314 0.0453  -0.0615 -0.0093 66  TYR A N   
500  C CA  . TYR A 66  ? 0.8940 1.4167 0.6975 0.0444  -0.0707 -0.0093 66  TYR A CA  
501  C C   . TYR A 66  ? 0.9470 1.4598 0.7360 0.0551  -0.0633 0.0047  66  TYR A C   
502  O O   . TYR A 66  ? 0.9355 1.3944 0.6972 0.0586  -0.0503 0.0142  66  TYR A O   
503  C CB  . TYR A 66  ? 0.8360 1.3760 0.6261 0.0144  -0.0731 -0.0134 66  TYR A CB  
504  C CG  . TYR A 66  ? 0.8994 1.3933 0.6483 -0.0093 -0.0580 -0.0033 66  TYR A CG  
505  C CD1 . TYR A 66  ? 0.9263 1.4239 0.6580 -0.0151 -0.0533 0.0079  66  TYR A CD1 
506  C CD2 . TYR A 66  ? 0.9507 1.3972 0.6780 -0.0258 -0.0478 -0.0051 66  TYR A CD2 
507  C CE1 . TYR A 66  ? 0.9428 1.3947 0.6349 -0.0378 -0.0382 0.0171  66  TYR A CE1 
508  C CE2 . TYR A 66  ? 0.9790 1.3824 0.6692 -0.0481 -0.0332 0.0033  66  TYR A CE2 
509  C CZ  . TYR A 66  ? 0.9928 1.3972 0.6643 -0.0546 -0.0280 0.0144  66  TYR A CZ  
510  O OH  . TYR A 66  ? 1.1023 1.4604 0.7348 -0.0779 -0.0122 0.0227  66  TYR A OH  
511  N N   . TRP A 67  ? 0.9824 1.5488 0.7894 0.0614  -0.0721 0.0055  67  TRP A N   
512  C CA  . TRP A 67  ? 0.9380 1.5042 0.7357 0.0754  -0.0661 0.0182  67  TRP A CA  
513  C C   . TRP A 67  ? 0.9932 1.5466 0.7572 0.0497  -0.0588 0.0289  67  TRP A C   
514  O O   . TRP A 67  ? 0.9788 1.5650 0.7447 0.0269  -0.0662 0.0234  67  TRP A O   
515  C CB  . TRP A 67  ? 0.8848 1.5194 0.7246 0.1000  -0.0794 0.0129  67  TRP A CB  
516  C CG  . TRP A 67  ? 0.9067 1.5417 0.7718 0.1281  -0.0805 0.0050  67  TRP A CG  
517  C CD1 . TRP A 67  ? 0.8774 1.5377 0.7743 0.1341  -0.0908 -0.0095 67  TRP A CD1 
518  C CD2 . TRP A 67  ? 0.9485 1.5563 0.8063 0.1542  -0.0701 0.0099  67  TRP A CD2 
519  N NE1 . TRP A 67  ? 0.8772 1.5283 0.7885 0.1603  -0.0869 -0.0142 67  TRP A NE1 
520  C CE2 . TRP A 67  ? 0.8757 1.4970 0.7637 0.1736  -0.0746 -0.0034 67  TRP A CE2 
521  C CE3 . TRP A 67  ? 0.9686 1.5417 0.7950 0.1637  -0.0570 0.0236  67  TRP A CE3 
522  C CZ2 . TRP A 67  ? 0.9164 1.5219 0.8051 0.2015  -0.0668 -0.0053 67  TRP A CZ2 
523  C CZ3 . TRP A 67  ? 0.9141 1.4701 0.7397 0.1937  -0.0497 0.0223  67  TRP A CZ3 
524  C CH2 . TRP A 67  ? 0.9108 1.4852 0.7679 0.2119  -0.0548 0.0071  67  TRP A CH2 
525  N N   . GLY A 68  ? 1.0487 1.5538 0.7796 0.0537  -0.0440 0.0434  68  GLY A N   
526  C CA  . GLY A 68  ? 1.0990 1.5833 0.7937 0.0317  -0.0340 0.0558  68  GLY A CA  
527  C C   . GLY A 68  ? 1.1465 1.6372 0.8345 0.0525  -0.0292 0.0692  68  GLY A C   
528  O O   . GLY A 68  ? 1.1003 1.5928 0.8021 0.0858  -0.0290 0.0701  68  GLY A O   
529  N N   . ASP A 69  ? 1.1668 1.6639 0.8339 0.0341  -0.0249 0.0787  69  ASP A N   
530  C CA  . ASP A 69  ? 1.2912 1.7891 0.9460 0.0524  -0.0182 0.0934  69  ASP A CA  
531  C C   . ASP A 69  ? 1.3125 1.7258 0.9105 0.0435  0.0030  0.1089  69  ASP A C   
532  O O   . ASP A 69  ? 1.3522 1.7284 0.9186 0.0090  0.0117  0.1110  69  ASP A O   
533  C CB  . ASP A 69  ? 1.3358 1.8953 1.0024 0.0393  -0.0270 0.0953  69  ASP A CB  
534  C CG  . ASP A 69  ? 1.2627 1.9093 0.9866 0.0586  -0.0485 0.0826  69  ASP A CG  
535  O OD1 . ASP A 69  ? 1.1535 1.8146 0.9057 0.0927  -0.0524 0.0785  69  ASP A OD1 
536  O OD2 . ASP A 69  ? 1.2416 1.9429 0.9813 0.0395  -0.0615 0.0756  69  ASP A OD2 
537  N N   . GLU A 70  ? 1.4289 1.8120 1.0133 0.0754  0.0116  0.1182  70  GLU A N   
538  C CA  . GLU A 70  ? 1.4950 1.7948 1.0230 0.0734  0.0312  0.1332  70  GLU A CA  
539  C C   . GLU A 70  ? 1.4989 1.7917 0.9957 0.0608  0.0411  0.1493  70  GLU A C   
540  O O   . GLU A 70  ? 1.5445 1.7697 0.9906 0.0413  0.0576  0.1611  70  GLU A O   
541  C CB  . GLU A 70  ? 1.4367 1.7106 0.9595 0.1154  0.0358  0.1351  70  GLU A CB  
542  C CG  . GLU A 70  ? 1.6028 1.7884 1.0649 0.1184  0.0546  0.1496  70  GLU A CG  
543  C CD  . GLU A 70  ? 1.7087 1.8791 1.1639 0.1641  0.0581  0.1503  70  GLU A CD  
544  O OE1 . GLU A 70  ? 1.6746 1.9061 1.1741 0.1926  0.0473  0.1396  70  GLU A OE1 
545  O OE2 . GLU A 70  ? 1.7969 1.8953 1.2014 0.1721  0.0720  0.1606  70  GLU A OE2 
546  N N   . GLY A 73  ? 1.1629 1.4644 0.6135 0.1388  0.0638  0.1929  73  GLY A N   
547  C CA  . GLY A 73  ? 1.1773 1.5558 0.6908 0.1389  0.0429  0.1738  73  GLY A CA  
548  C C   . GLY A 73  ? 1.1317 1.5184 0.6736 0.1725  0.0366  0.1602  73  GLY A C   
549  O O   . GLY A 73  ? 1.1023 1.4385 0.6156 0.1984  0.0477  0.1646  73  GLY A O   
550  N N   . GLY A 74  ? 1.1648 1.6151 0.7610 0.1721  0.0187  0.1430  74  GLY A N   
551  C CA  . GLY A 74  ? 1.0714 1.5370 0.6996 0.2002  0.0119  0.1279  74  GLY A CA  
552  C C   . GLY A 74  ? 1.1041 1.6131 0.7754 0.1812  -0.0049 0.1108  74  GLY A C   
553  O O   . GLY A 74  ? 1.1646 1.7200 0.8554 0.1585  -0.0155 0.1084  74  GLY A O   
554  N N   . ARG A 75  ? 1.0866 1.5794 0.7699 0.1913  -0.0071 0.0986  75  ARG A N   
555  C CA  . ARG A 75  ? 1.0627 1.5846 0.7802 0.1738  -0.0209 0.0830  75  ARG A CA  
556  C C   . ARG A 75  ? 1.0774 1.5479 0.7838 0.1771  -0.0163 0.0757  75  ARG A C   
557  O O   . ARG A 75  ? 1.0731 1.5471 0.7926 0.2084  -0.0156 0.0688  75  ARG A O   
558  C CB  . ARG A 75  ? 1.0334 1.6415 0.8099 0.1936  -0.0374 0.0703  75  ARG A CB  
559  C CG  . ARG A 75  ? 0.9797 1.6200 0.7892 0.1760  -0.0523 0.0549  75  ARG A CG  
560  C CD  . ARG A 75  ? 0.9018 1.6296 0.7645 0.1891  -0.0696 0.0450  75  ARG A CD  
561  N NE  . ARG A 75  ? 0.9518 1.7066 0.8446 0.1778  -0.0836 0.0293  75  ARG A NE  
562  C CZ  . ARG A 75  ? 1.0108 1.7782 0.9018 0.1475  -0.0922 0.0257  75  ARG A CZ  
563  N NH1 . ARG A 75  ? 0.9718 1.7326 0.8333 0.1228  -0.0893 0.0358  75  ARG A NH1 
564  N NH2 . ARG A 75  ? 1.0093 1.7760 0.9315 0.1384  -0.0956 0.0096  75  ARG A NH2 
565  N N   . ARG A 76  ? 1.1539 1.5784 0.8354 0.1452  -0.0126 0.0765  76  ARG A N   
566  C CA  . ARG A 76  ? 1.1065 1.4770 0.7724 0.1427  -0.0079 0.0715  76  ARG A CA  
567  C C   . ARG A 76  ? 1.0668 1.4613 0.7639 0.1268  -0.0194 0.0564  76  ARG A C   
568  O O   . ARG A 76  ? 1.0677 1.5051 0.7848 0.1076  -0.0289 0.0516  76  ARG A O   
569  C CB  . ARG A 76  ? 1.1156 1.4103 0.7271 0.1197  0.0068  0.0840  76  ARG A CB  
570  C CG  . ARG A 76  ? 1.2003 1.4401 0.7730 0.1434  0.0198  0.0944  76  ARG A CG  
571  C CD  . ARG A 76  ? 1.2864 1.4531 0.8047 0.1188  0.0342  0.1078  76  ARG A CD  
572  N NE  . ARG A 76  ? 1.4842 1.6043 0.9612 0.1427  0.0466  0.1205  76  ARG A NE  
573  C CZ  . ARG A 76  ? 1.5184 1.5739 0.9431 0.1280  0.0610  0.1352  76  ARG A CZ  
574  N NH1 . ARG A 76  ? 1.4747 1.5054 0.8829 0.0880  0.0659  0.1384  76  ARG A NH1 
575  N NH2 . ARG A 76  ? 1.4686 1.4836 0.8551 0.1547  0.0715  0.1460  76  ARG A NH2 
576  N N   . LYS A 77  ? 1.0709 1.4364 0.7693 0.1355  -0.0185 0.0487  77  LYS A N   
577  C CA  . LYS A 77  ? 1.0001 1.3768 0.7223 0.1228  -0.0271 0.0353  77  LYS A CA  
578  C C   . LYS A 77  ? 1.0164 1.3321 0.7050 0.0976  -0.0186 0.0386  77  LYS A C   
579  O O   . LYS A 77  ? 1.0321 1.2937 0.6919 0.1056  -0.0093 0.0439  77  LYS A O   
580  C CB  . LYS A 77  ? 0.8678 1.2597 0.6186 0.1501  -0.0321 0.0230  77  LYS A CB  
581  C CG  . LYS A 77  ? 0.8906 1.3009 0.6696 0.1397  -0.0416 0.0093  77  LYS A CG  
582  C CD  . LYS A 77  ? 0.8379 1.2609 0.6427 0.1655  -0.0449 -0.0029 77  LYS A CD  
583  C CE  . LYS A 77  ? 0.8748 1.3100 0.7039 0.1551  -0.0530 -0.0155 77  LYS A CE  
584  N NZ  . LYS A 77  ? 0.8079 1.2556 0.6620 0.1780  -0.0553 -0.0282 77  LYS A NZ  
585  N N   . TYR A 78  ? 0.9639 1.2908 0.6564 0.0688  -0.0222 0.0341  78  TYR A N   
586  C CA  . TYR A 78  ? 0.9970 1.2751 0.6620 0.0428  -0.0141 0.0353  78  TYR A CA  
587  C C   . TYR A 78  ? 1.0176 1.3009 0.7049 0.0400  -0.0207 0.0219  78  TYR A C   
588  O O   . TYR A 78  ? 1.0074 1.3338 0.7301 0.0537  -0.0319 0.0117  78  TYR A O   
589  C CB  . TYR A 78  ? 0.9988 1.2850 0.6476 0.0110  -0.0107 0.0386  78  TYR A CB  
590  C CG  . TYR A 78  ? 1.0448 1.3041 0.6592 0.0077  0.0005  0.0542  78  TYR A CG  
591  C CD1 . TYR A 78  ? 1.0757 1.3718 0.7002 0.0246  -0.0033 0.0600  78  TYR A CD1 
592  C CD2 . TYR A 78  ? 1.0776 1.2747 0.6495 -0.0117 0.0154  0.0630  78  TYR A CD2 
593  C CE1 . TYR A 78  ? 1.1059 1.3765 0.6974 0.0227  0.0077  0.0751  78  TYR A CE1 
594  C CE2 . TYR A 78  ? 1.1242 1.2921 0.6613 -0.0149 0.0268  0.0779  78  TYR A CE2 
595  C CZ  . TYR A 78  ? 1.1316 1.3358 0.6777 0.0026  0.0230  0.0843  78  TYR A CZ  
596  O OH  . TYR A 78  ? 1.2155 1.3897 0.7254 0.0005  0.0351  0.0999  78  TYR A OH  
597  N N   . TYR A 79  ? 1.0213 1.2590 0.6872 0.0227  -0.0132 0.0221  79  TYR A N   
598  C CA  . TYR A 79  ? 0.9993 1.2380 0.6827 0.0184  -0.0179 0.0104  79  TYR A CA  
599  C C   . TYR A 79  ? 0.9761 1.2058 0.6462 -0.0133 -0.0129 0.0070  79  TYR A C   
600  O O   . TYR A 79  ? 1.0051 1.2014 0.6439 -0.0314 -0.0018 0.0149  79  TYR A O   
601  C CB  . TYR A 79  ? 0.9756 1.1709 0.6513 0.0342  -0.0146 0.0109  79  TYR A CB  
602  C CG  . TYR A 79  ? 0.9638 1.1777 0.6597 0.0657  -0.0207 0.0076  79  TYR A CG  
603  C CD1 . TYR A 79  ? 0.9786 1.2279 0.7098 0.0757  -0.0305 -0.0048 79  TYR A CD1 
604  C CD2 . TYR A 79  ? 0.9740 1.1701 0.6523 0.0859  -0.0158 0.0157  79  TYR A CD2 
605  C CE1 . TYR A 79  ? 0.8850 1.1530 0.6355 0.1030  -0.0347 -0.0100 79  TYR A CE1 
606  C CE2 . TYR A 79  ? 0.9975 1.2152 0.6950 0.1153  -0.0203 0.0098  79  TYR A CE2 
607  C CZ  . TYR A 79  ? 0.9317 1.1861 0.6664 0.1227  -0.0296 -0.0036 79  TYR A CZ  
608  O OH  . TYR A 79  ? 0.9065 1.1845 0.6615 0.1502  -0.0328 -0.0116 79  TYR A OH  
609  N N   . ARG A 80  ? 0.9446 1.2034 0.6377 -0.0192 -0.0202 -0.0058 80  ARG A N   
610  C CA  . ARG A 80  ? 1.0480 1.3117 0.7323 -0.0470 -0.0163 -0.0127 80  ARG A CA  
611  C C   . ARG A 80  ? 1.0574 1.3201 0.7569 -0.0473 -0.0189 -0.0239 80  ARG A C   
612  O O   . ARG A 80  ? 0.9735 1.2574 0.6991 -0.0291 -0.0285 -0.0302 80  ARG A O   
613  C CB  . ARG A 80  ? 1.0188 1.3385 0.7130 -0.0570 -0.0238 -0.0188 80  ARG A CB  
614  C CG  . ARG A 80  ? 1.0440 1.3691 0.7200 -0.0879 -0.0171 -0.0251 80  ARG A CG  
615  C CD  . ARG A 80  ? 1.1026 1.4870 0.7872 -0.0955 -0.0266 -0.0321 80  ARG A CD  
616  N NE  . ARG A 80  ? 1.1862 1.5921 0.8634 -0.1196 -0.0246 -0.0465 80  ARG A NE  
617  C CZ  . ARG A 80  ? 1.1499 1.5753 0.8424 -0.1169 -0.0302 -0.0606 80  ARG A CZ  
618  N NH1 . ARG A 80  ? 1.1838 1.6077 0.8997 -0.0932 -0.0380 -0.0617 80  ARG A NH1 
619  N NH2 . ARG A 80  ? 1.0995 1.5469 0.7820 -0.1380 -0.0272 -0.0750 80  ARG A NH2 
620  N N   . LEU A 81  ? 1.1462 1.3854 0.8294 -0.0684 -0.0095 -0.0270 81  LEU A N   
621  C CA  . LEU A 81  ? 1.0250 1.2626 0.7203 -0.0704 -0.0100 -0.0375 81  LEU A CA  
622  C C   . LEU A 81  ? 0.9924 1.2815 0.7032 -0.0778 -0.0168 -0.0521 81  LEU A C   
623  O O   . LEU A 81  ? 1.0536 1.3645 0.7525 -0.0972 -0.0139 -0.0567 81  LEU A O   
624  C CB  . LEU A 81  ? 1.0507 1.2458 0.7233 -0.0894 0.0034  -0.0358 81  LEU A CB  
625  C CG  . LEU A 81  ? 1.0925 1.2773 0.7755 -0.0902 0.0050  -0.0444 81  LEU A CG  
626  C CD1 . LEU A 81  ? 1.0606 1.2304 0.7595 -0.0653 -0.0024 -0.0414 81  LEU A CD1 
627  C CD2 . LEU A 81  ? 1.1480 1.2932 0.8082 -0.1103 0.0188  -0.0424 81  LEU A CD2 
628  N N   . THR A 82  ? 0.9925 1.3005 0.7273 -0.0623 -0.0257 -0.0601 82  THR A N   
629  C CA  . THR A 82  ? 0.9939 1.3493 0.7417 -0.0643 -0.0334 -0.0743 82  THR A CA  
630  C C   . THR A 82  ? 0.9908 1.3460 0.7293 -0.0821 -0.0253 -0.0853 82  THR A C   
631  O O   . THR A 82  ? 1.0060 1.3261 0.7296 -0.0949 -0.0135 -0.0818 82  THR A O   
632  C CB  . THR A 82  ? 0.9744 1.3444 0.7482 -0.0412 -0.0442 -0.0787 82  THR A CB  
633  O OG1 . THR A 82  ? 1.0097 1.3509 0.7876 -0.0370 -0.0396 -0.0804 82  THR A OG1 
634  C CG2 . THR A 82  ? 0.9423 1.3092 0.7271 -0.0223 -0.0499 -0.0693 82  THR A CG2 
635  N N   . GLU A 83  ? 0.9609 1.3574 0.7076 -0.0821 -0.0315 -0.1000 83  GLU A N   
636  C CA  . GLU A 83  ? 1.0613 1.4626 0.8028 -0.0934 -0.0240 -0.1130 83  GLU A CA  
637  C C   . GLU A 83  ? 1.0704 1.4391 0.8227 -0.0825 -0.0203 -0.1106 83  GLU A C   
638  O O   . GLU A 83  ? 1.0833 1.4277 0.8274 -0.0941 -0.0091 -0.1114 83  GLU A O   
639  C CB  . GLU A 83  ? 1.0426 1.4950 0.7891 -0.0902 -0.0325 -0.1300 83  GLU A CB  
640  C CG  . GLU A 83  ? 1.0381 1.5264 0.7670 -0.1105 -0.0308 -0.1409 83  GLU A CG  
641  C CD  . GLU A 83  ? 1.0491 1.5557 0.7970 -0.1058 -0.0294 -0.1532 83  GLU A CD  
642  O OE1 . GLU A 83  ? 1.0527 1.5503 0.8042 -0.0995 -0.0249 -0.1593 83  GLU A OE1 
643  O OE2 . GLU A 83  ? 1.1268 1.6550 0.8883 -0.1065 -0.0320 -0.1555 83  GLU A OE2 
644  N N   . ILE A 84  ? 0.9897 1.3599 0.7612 -0.0605 -0.0299 -0.1088 84  ILE A N   
645  C CA  . ILE A 84  ? 0.9415 1.2834 0.7244 -0.0489 -0.0280 -0.1065 84  ILE A CA  
646  C C   . ILE A 84  ? 0.9454 1.2419 0.7180 -0.0559 -0.0192 -0.0953 84  ILE A C   
647  O O   . ILE A 84  ? 0.9332 1.2088 0.7078 -0.0575 -0.0134 -0.0966 84  ILE A O   
648  C CB  . ILE A 84  ? 0.9413 1.2863 0.7432 -0.0262 -0.0387 -0.1034 84  ILE A CB  
649  C CG1 . ILE A 84  ? 0.8902 1.2792 0.6988 -0.0198 -0.0488 -0.1124 84  ILE A CG1 
650  C CG2 . ILE A 84  ? 0.9291 1.2558 0.7432 -0.0153 -0.0376 -0.1053 84  ILE A CG2 
651  C CD1 . ILE A 84  ? 0.8793 1.2942 0.6851 -0.0227 -0.0481 -0.1271 84  ILE A CD1 
652  N N   . GLY A 85  ? 0.9458 1.2266 0.7071 -0.0583 -0.0187 -0.0842 85  GLY A N   
653  C CA  . GLY A 85  ? 0.9190 1.1542 0.6651 -0.0641 -0.0105 -0.0735 85  GLY A CA  
654  C C   . GLY A 85  ? 0.9847 1.2084 0.7154 -0.0868 0.0018  -0.0779 85  GLY A C   
655  O O   . GLY A 85  ? 1.0792 1.2726 0.8081 -0.0886 0.0074  -0.0762 85  GLY A O   
656  N N   . HIS A 86  ? 1.0079 1.2579 0.7276 -0.1047 0.0061  -0.0848 86  HIS A N   
657  C CA  . HIS A 86  ? 0.9952 1.2372 0.6999 -0.1282 0.0196  -0.0913 86  HIS A CA  
658  C C   . HIS A 86  ? 1.0033 1.2550 0.7224 -0.1267 0.0226  -0.1037 86  HIS A C   
659  O O   . HIS A 86  ? 1.0215 1.2512 0.7349 -0.1386 0.0332  -0.1056 86  HIS A O   
660  C CB  . HIS A 86  ? 1.0251 1.3007 0.7157 -0.1480 0.0233  -0.0997 86  HIS A CB  
661  C CG  . HIS A 86  ? 1.0901 1.3421 0.7573 -0.1614 0.0292  -0.0877 86  HIS A CG  
662  N ND1 . HIS A 86  ? 1.0085 1.2753 0.6736 -0.1548 0.0209  -0.0800 86  HIS A ND1 
663  C CD2 . HIS A 86  ? 1.1542 1.3677 0.7983 -0.1804 0.0431  -0.0818 86  HIS A CD2 
664  C CE1 . HIS A 86  ? 1.0043 1.2430 0.6453 -0.1687 0.0297  -0.0693 86  HIS A CE1 
665  N NE2 . HIS A 86  ? 1.1166 1.3204 0.7431 -0.1848 0.0435  -0.0700 86  HIS A NE2 
666  N N   . GLU A 87  ? 0.9878 1.2723 0.7256 -0.1113 0.0136  -0.1124 87  GLU A N   
667  C CA  . GLU A 87  ? 0.9596 1.2551 0.7107 -0.1075 0.0167  -0.1240 87  GLU A CA  
668  C C   . GLU A 87  ? 0.9000 1.1572 0.6613 -0.0971 0.0169  -0.1151 87  GLU A C   
669  O O   . GLU A 87  ? 0.9115 1.1620 0.6771 -0.1028 0.0246  -0.1208 87  GLU A O   
670  C CB  . GLU A 87  ? 0.9945 1.3297 0.7594 -0.0916 0.0072  -0.1343 87  GLU A CB  
671  C CG  . GLU A 87  ? 1.0359 1.3884 0.8112 -0.0874 0.0118  -0.1481 87  GLU A CG  
672  C CD  . GLU A 87  ? 1.1778 1.5687 0.9602 -0.0721 0.0034  -0.1592 87  GLU A CD  
673  O OE1 . GLU A 87  ? 1.1595 1.5725 0.9357 -0.0708 -0.0047 -0.1604 87  GLU A OE1 
674  O OE2 . GLU A 87  ? 1.2760 1.6749 1.0696 -0.0605 0.0046  -0.1667 87  GLU A OE2 
675  N N   . ASN A 88  ? 0.9741 1.2089 0.7398 -0.0816 0.0081  -0.1025 88  ASN A N   
676  C CA  . ASN A 88  ? 0.9845 1.1839 0.7568 -0.0718 0.0069  -0.0947 88  ASN A CA  
677  C C   . ASN A 88  ? 0.9509 1.1136 0.7060 -0.0867 0.0163  -0.0885 88  ASN A C   
678  O O   . ASN A 88  ? 0.9519 1.0940 0.7127 -0.0849 0.0182  -0.0881 88  ASN A O   
679  C CB  . ASN A 88  ? 0.9591 1.1457 0.7365 -0.0529 -0.0036 -0.0848 88  ASN A CB  
680  C CG  . ASN A 88  ? 1.0261 1.2402 0.8236 -0.0364 -0.0123 -0.0910 88  ASN A CG  
681  O OD1 . ASN A 88  ? 1.0504 1.2978 0.8533 -0.0385 -0.0122 -0.1015 88  ASN A OD1 
682  N ND2 . ASN A 88  ? 1.0435 1.2436 0.8504 -0.0196 -0.0194 -0.0857 88  ASN A ND2 
683  N N   . MET A 89  ? 0.9000 1.0529 0.6334 -0.1010 0.0219  -0.0835 89  MET A N   
684  C CA  . MET A 89  ? 0.9346 1.0495 0.6480 -0.1168 0.0324  -0.0781 89  MET A CA  
685  C C   . MET A 89  ? 0.9153 1.0408 0.6348 -0.1317 0.0427  -0.0908 89  MET A C   
686  O O   . MET A 89  ? 0.8910 0.9863 0.6081 -0.1357 0.0476  -0.0884 89  MET A O   
687  C CB  . MET A 89  ? 1.0371 1.1432 0.7249 -0.1314 0.0383  -0.0716 89  MET A CB  
688  C CG  . MET A 89  ? 1.0995 1.1988 0.7825 -0.1152 0.0290  -0.0595 89  MET A CG  
689  S SD  . MET A 89  ? 1.1202 1.1629 0.7898 -0.0990 0.0262  -0.0441 89  MET A SD  
690  C CE  . MET A 89  ? 1.2126 1.2110 0.8543 -0.1227 0.0415  -0.0409 89  MET A CE  
691  N N   . ARG A 90  ? 0.9151 1.0857 0.6426 -0.1388 0.0457  -0.1057 90  ARG A N   
692  C CA  . ARG A 90  ? 0.9040 1.0922 0.6380 -0.1518 0.0567  -0.1208 90  ARG A CA  
693  C C   . ARG A 90  ? 0.8938 1.0844 0.6528 -0.1353 0.0523  -0.1240 90  ARG A C   
694  O O   . ARG A 90  ? 0.8947 1.0728 0.6591 -0.1418 0.0597  -0.1276 90  ARG A O   
695  C CB  . ARG A 90  ? 0.8644 1.1046 0.5982 -0.1603 0.0602  -0.1379 90  ARG A CB  
696  C CG  . ARG A 90  ? 1.0177 1.2735 0.7465 -0.1826 0.0766  -0.1544 90  ARG A CG  
697  C CD  . ARG A 90  ? 0.9646 1.2786 0.6946 -0.1874 0.0799  -0.1761 90  ARG A CD  
698  N NE  . ARG A 90  ? 0.9426 1.2871 0.6940 -0.1640 0.0713  -0.1838 90  ARG A NE  
699  C CZ  . ARG A 90  ? 0.9500 1.3207 0.7038 -0.1488 0.0593  -0.1852 90  ARG A CZ  
700  N NH1 . ARG A 90  ? 0.9934 1.3669 0.7332 -0.1528 0.0526  -0.1788 90  ARG A NH1 
701  N NH2 . ARG A 90  ? 0.9239 1.3181 0.6946 -0.1285 0.0539  -0.1929 90  ARG A NH2 
702  N N   . LEU A 91  ? 0.8857 1.0932 0.6607 -0.1141 0.0404  -0.1232 91  LEU A N   
703  C CA  . LEU A 91  ? 0.8604 1.0695 0.6585 -0.0975 0.0354  -0.1249 91  LEU A CA  
704  C C   . LEU A 91  ? 0.8547 1.0201 0.6522 -0.0951 0.0335  -0.1135 91  LEU A C   
705  O O   . LEU A 91  ? 0.9202 1.0836 0.7312 -0.0947 0.0364  -0.1178 91  LEU A O   
706  C CB  . LEU A 91  ? 0.8749 1.0995 0.6852 -0.0763 0.0231  -0.1230 91  LEU A CB  
707  C CG  . LEU A 91  ? 0.9049 1.1716 0.7155 -0.0734 0.0214  -0.1337 91  LEU A CG  
708  C CD1 . LEU A 91  ? 0.9127 1.1895 0.7391 -0.0508 0.0107  -0.1329 91  LEU A CD1 
709  C CD2 . LEU A 91  ? 0.9430 1.2441 0.7534 -0.0844 0.0322  -0.1514 91  LEU A CD2 
710  N N   . ARG A 92  ? 0.8686 1.0009 0.6503 -0.0920 0.0280  -0.0995 92  ARG A N   
711  C CA  . ARG A 92  ? 0.8544 0.9455 0.6318 -0.0862 0.0241  -0.0894 92  ARG A CA  
712  C C   . ARG A 92  ? 0.8304 0.9008 0.5990 -0.1036 0.0349  -0.0913 92  ARG A C   
713  O O   . ARG A 92  ? 0.8976 0.9532 0.6759 -0.0990 0.0325  -0.0910 92  ARG A O   
714  C CB  . ARG A 92  ? 0.9025 0.9647 0.6600 -0.0793 0.0181  -0.0760 92  ARG A CB  
715  C CG  . ARG A 92  ? 0.9216 0.9451 0.6729 -0.0678 0.0113  -0.0671 92  ARG A CG  
716  C CD  . ARG A 92  ? 0.9387 0.9198 0.6580 -0.0763 0.0165  -0.0569 92  ARG A CD  
717  N NE  . ARG A 92  ? 0.9764 0.9207 0.6865 -0.0637 0.0093  -0.0501 92  ARG A NE  
718  C CZ  . ARG A 92  ? 1.0110 0.9245 0.7102 -0.0712 0.0128  -0.0485 92  ARG A CZ  
719  N NH1 . ARG A 92  ? 1.0349 0.9489 0.7322 -0.0922 0.0252  -0.0534 92  ARG A NH1 
720  N NH2 . ARG A 92  ? 0.9704 0.8534 0.6598 -0.0570 0.0038  -0.0433 92  ARG A NH2 
721  N N   . HIS A 93  ? 0.8484 0.9194 0.5993 -0.1244 0.0469  -0.0944 93  HIS A N   
722  C CA  . HIS A 93  ? 0.9236 0.9740 0.6649 -0.1434 0.0593  -0.0976 93  HIS A CA  
723  C C   . HIS A 93  ? 0.9014 0.9836 0.6690 -0.1460 0.0648  -0.1130 93  HIS A C   
724  O O   . HIS A 93  ? 0.9458 1.0100 0.7178 -0.1511 0.0690  -0.1144 93  HIS A O   
725  C CB  . HIS A 93  ? 0.9746 1.0226 0.6908 -0.1670 0.0722  -0.0992 93  HIS A CB  
726  C CG  . HIS A 93  ? 1.0807 1.1107 0.7871 -0.1894 0.0875  -0.1050 93  HIS A CG  
727  N ND1 . HIS A 93  ? 1.1648 1.1404 0.8497 -0.1950 0.0905  -0.0936 93  HIS A ND1 
728  C CD2 . HIS A 93  ? 1.1551 1.2149 0.8705 -0.2069 0.1010  -0.1225 93  HIS A CD2 
729  C CE1 . HIS A 93  ? 1.2182 1.1889 0.8997 -0.2164 0.1055  -0.1030 93  HIS A CE1 
730  N NE2 . HIS A 93  ? 1.1877 1.2108 0.8887 -0.2243 0.1125  -0.1212 93  HIS A NE2 
731  N N   . GLU A 94  ? 0.8454 0.9759 0.6299 -0.1416 0.0651  -0.1255 94  GLU A N   
732  C CA  . GLU A 94  ? 0.8615 1.0266 0.6702 -0.1420 0.0717  -0.1416 94  GLU A CA  
733  C C   . GLU A 94  ? 0.8219 0.9799 0.6543 -0.1233 0.0618  -0.1377 94  GLU A C   
734  O O   . GLU A 94  ? 0.7942 0.9519 0.6402 -0.1274 0.0670  -0.1434 94  GLU A O   
735  C CB  . GLU A 94  ? 0.9078 1.1252 0.7245 -0.1383 0.0736  -0.1559 94  GLU A CB  
736  C CG  . GLU A 94  ? 0.9909 1.2254 0.7868 -0.1611 0.0861  -0.1662 94  GLU A CG  
737  C CD  . GLU A 94  ? 1.0781 1.3688 0.8799 -0.1574 0.0883  -0.1842 94  GLU A CD  
738  O OE1 . GLU A 94  ? 1.1386 1.4573 0.9625 -0.1408 0.0860  -0.1930 94  GLU A OE1 
739  O OE2 . GLU A 94  ? 1.0082 1.3157 0.7910 -0.1702 0.0920  -0.1899 94  GLU A OE2 
740  N N   . SER A 95  ? 0.8376 0.9915 0.6760 -0.1032 0.0475  -0.1285 95  SER A N   
741  C CA  . SER A 95  ? 0.8245 0.9741 0.6845 -0.0859 0.0372  -0.1253 95  SER A CA  
742  C C   . SER A 95  ? 0.8067 0.9168 0.6605 -0.0905 0.0355  -0.1179 95  SER A C   
743  O O   . SER A 95  ? 0.8188 0.9356 0.6931 -0.0870 0.0347  -0.1226 95  SER A O   
744  C CB  . SER A 95  ? 0.7938 0.9392 0.6553 -0.0668 0.0233  -0.1164 95  SER A CB  
745  O OG  . SER A 95  ? 0.9135 1.0209 0.7516 -0.0670 0.0178  -0.1033 95  SER A OG  
746  N N   . TRP A 96  ? 0.8318 0.9011 0.6569 -0.0971 0.0348  -0.1064 96  TRP A N   
747  C CA  . TRP A 96  ? 0.8172 0.8448 0.6310 -0.0997 0.0324  -0.0991 96  TRP A CA  
748  C C   . TRP A 96  ? 0.8607 0.8884 0.6769 -0.1189 0.0464  -0.1081 96  TRP A C   
749  O O   . TRP A 96  ? 0.8643 0.8687 0.6825 -0.1188 0.0437  -0.1061 96  TRP A O   
750  C CB  . TRP A 96  ? 0.8622 0.8456 0.6410 -0.1002 0.0295  -0.0851 96  TRP A CB  
751  C CG  . TRP A 96  ? 0.8897 0.8641 0.6682 -0.0782 0.0138  -0.0769 96  TRP A CG  
752  C CD1 . TRP A 96  ? 0.8712 0.8581 0.6474 -0.0684 0.0088  -0.0737 96  TRP A CD1 
753  C CD2 . TRP A 96  ? 0.8347 0.7896 0.6165 -0.0632 0.0008  -0.0729 96  TRP A CD2 
754  N NE1 . TRP A 96  ? 0.8330 0.8085 0.6106 -0.0490 -0.0049 -0.0685 96  TRP A NE1 
755  C CE2 . TRP A 96  ? 0.8358 0.7922 0.6158 -0.0455 -0.0104 -0.0681 96  TRP A CE2 
756  C CE3 . TRP A 96  ? 0.7784 0.7165 0.5645 -0.0630 -0.0029 -0.0739 96  TRP A CE3 
757  C CZ2 . TRP A 96  ? 0.7638 0.7065 0.5443 -0.0285 -0.0244 -0.0654 96  TRP A CZ2 
758  C CZ3 . TRP A 96  ? 0.7972 0.7218 0.5839 -0.0452 -0.0185 -0.0702 96  TRP A CZ3 
759  C CH2 . TRP A 96  ? 0.8196 0.7470 0.6027 -0.0285 -0.0289 -0.0665 96  TRP A CH2 
760  N N   . SER A 97  ? 0.8202 0.8760 0.6368 -0.1352 0.0610  -0.1195 97  SER A N   
761  C CA  . SER A 97  ? 0.8030 0.8684 0.6277 -0.1528 0.0756  -0.1321 97  SER A CA  
762  C C   . SER A 97  ? 0.8089 0.9083 0.6719 -0.1405 0.0720  -0.1423 97  SER A C   
763  O O   . SER A 97  ? 0.8104 0.9014 0.6839 -0.1457 0.0753  -0.1462 97  SER A O   
764  C CB  . SER A 97  ? 0.8826 0.9782 0.6996 -0.1720 0.0920  -0.1452 97  SER A CB  
765  O OG  . SER A 97  ? 0.9535 1.0139 0.7348 -0.1896 0.0991  -0.1372 97  SER A OG  
766  N N   . ARG A 98  ? 0.7674 0.9051 0.6516 -0.1233 0.0652  -0.1465 98  ARG A N   
767  C CA  . ARG A 98  ? 0.7536 0.9256 0.6741 -0.1097 0.0620  -0.1556 98  ARG A CA  
768  C C   . ARG A 98  ? 0.7016 0.8457 0.6307 -0.0981 0.0474  -0.1452 98  ARG A C   
769  O O   . ARG A 98  ? 0.7442 0.9028 0.6983 -0.0959 0.0478  -0.1522 98  ARG A O   
770  C CB  . ARG A 98  ? 0.7069 0.9175 0.6423 -0.0924 0.0570  -0.1598 98  ARG A CB  
771  C CG  . ARG A 98  ? 0.7593 0.9953 0.6810 -0.1014 0.0678  -0.1691 98  ARG A CG  
772  C CD  . ARG A 98  ? 0.7714 1.0595 0.7149 -0.0872 0.0701  -0.1827 98  ARG A CD  
773  N NE  . ARG A 98  ? 0.8093 1.1107 0.7369 -0.0837 0.0686  -0.1834 98  ARG A NE  
774  C CZ  . ARG A 98  ? 0.8106 1.1003 0.7347 -0.0686 0.0554  -0.1718 98  ARG A CZ  
775  N NH1 . ARG A 98  ? 0.7541 1.0196 0.6880 -0.0559 0.0430  -0.1595 98  ARG A NH1 
776  N NH2 . ARG A 98  ? 0.8420 1.1462 0.7523 -0.0664 0.0546  -0.1740 98  ARG A NH2 
777  N N   . VAL A 99  ? 0.7433 0.8505 0.6524 -0.0895 0.0341  -0.1299 99  VAL A N   
778  C CA  . VAL A 99  ? 0.6595 0.7400 0.5716 -0.0779 0.0190  -0.1213 99  VAL A CA  
779  C C   . VAL A 99  ? 0.6890 0.7414 0.5932 -0.0913 0.0240  -0.1219 99  VAL A C   
780  O O   . VAL A 99  ? 0.7073 0.7601 0.6297 -0.0843 0.0157  -0.1233 99  VAL A O   
781  C CB  . VAL A 99  ? 0.7217 0.7684 0.6081 -0.0675 0.0064  -0.1072 99  VAL A CB  
782  C CG1 . VAL A 99  ? 0.7796 0.7945 0.6603 -0.0575 -0.0085 -0.0999 99  VAL A CG1 
783  C CG2 . VAL A 99  ? 0.6769 0.7522 0.5763 -0.0526 0.0000  -0.1077 99  VAL A CG2 
784  N N   . ASP A 100 ? 0.7199 0.7469 0.5962 -0.1109 0.0375  -0.1208 100 ASP A N   
785  C CA  . ASP A 100 ? 0.7449 0.7406 0.6101 -0.1257 0.0445  -0.1215 100 ASP A CA  
786  C C   . ASP A 100 ? 0.7701 0.8050 0.6703 -0.1329 0.0546  -0.1382 100 ASP A C   
787  O O   . ASP A 100 ? 0.7482 0.7676 0.6551 -0.1360 0.0532  -0.1398 100 ASP A O   
788  C CB  . ASP A 100 ? 0.8936 0.8555 0.7203 -0.1467 0.0590  -0.1172 100 ASP A CB  
789  C CG  . ASP A 100 ? 0.9766 0.8953 0.7672 -0.1384 0.0494  -0.1002 100 ASP A CG  
790  O OD1 . ASP A 100 ? 0.9723 0.8824 0.7654 -0.1175 0.0317  -0.0926 100 ASP A OD1 
791  O OD2 . ASP A 100 ? 0.9994 0.8960 0.7596 -0.1525 0.0599  -0.0955 100 ASP A OD2 
792  N N   . LYS A 101 ? 0.7006 0.7877 0.6228 -0.1346 0.0649  -0.1518 101 LYS A N   
793  C CA  . LYS A 101 ? 0.6980 0.8305 0.6564 -0.1376 0.0749  -0.1697 101 LYS A CA  
794  C C   . LYS A 101 ? 0.6642 0.8153 0.6571 -0.1164 0.0589  -0.1692 101 LYS A C   
795  O O   . LYS A 101 ? 0.6352 0.7950 0.6504 -0.1187 0.0605  -0.1766 101 LYS A O   
796  C CB  . LYS A 101 ? 0.7075 0.8934 0.6778 -0.1396 0.0879  -0.1849 101 LYS A CB  
797  C CG  . LYS A 101 ? 0.8496 1.0267 0.7886 -0.1627 0.1045  -0.1892 101 LYS A CG  
798  C CD  . LYS A 101 ? 0.8674 1.0864 0.8060 -0.1579 0.1085  -0.1974 101 LYS A CD  
799  C CE  . LYS A 101 ? 0.8695 1.0682 0.7699 -0.1771 0.1171  -0.1944 101 LYS A CE  
800  N NZ  . LYS A 101 ? 0.8670 1.0964 0.7614 -0.1692 0.1146  -0.1972 101 LYS A NZ  
801  N N   . ILE A 102 ? 0.6344 0.7938 0.6332 -0.0961 0.0436  -0.1611 102 ILE A N   
802  C CA  . ILE A 102 ? 0.5708 0.7483 0.6004 -0.0761 0.0274  -0.1599 102 ILE A CA  
803  C C   . ILE A 102 ? 0.6279 0.7677 0.6517 -0.0770 0.0161  -0.1530 102 ILE A C   
804  O O   . ILE A 102 ? 0.5918 0.7530 0.6467 -0.0706 0.0105  -0.1591 102 ILE A O   
805  C CB  . ILE A 102 ? 0.6091 0.7886 0.6357 -0.0576 0.0130  -0.1503 102 ILE A CB  
806  C CG1 . ILE A 102 ? 0.5971 0.8143 0.6295 -0.0551 0.0234  -0.1579 102 ILE A CG1 
807  C CG2 . ILE A 102 ? 0.5675 0.7643 0.6233 -0.0386 -0.0039 -0.1489 102 ILE A CG2 
808  C CD1 . ILE A 102 ? 0.4709 0.6952 0.5064 -0.0360 0.0105  -0.1507 102 ILE A CD1 
809  N N   . ILE A 103 ? 0.6738 0.7579 0.6569 -0.0835 0.0121  -0.1404 103 ILE A N   
810  C CA  . ILE A 103 ? 0.6783 0.7213 0.6484 -0.0832 0.0013  -0.1339 103 ILE A CA  
811  C C   . ILE A 103 ? 0.7309 0.7749 0.7115 -0.1002 0.0151  -0.1443 103 ILE A C   
812  O O   . ILE A 103 ? 0.7750 0.8171 0.7719 -0.0957 0.0059  -0.1466 103 ILE A O   
813  C CB  . ILE A 103 ? 0.6980 0.6809 0.6179 -0.0851 -0.0034 -0.1190 103 ILE A CB  
814  C CG1 . ILE A 103 ? 0.7101 0.6964 0.6238 -0.0669 -0.0176 -0.1108 103 ILE A CG1 
815  C CG2 . ILE A 103 ? 0.7083 0.6458 0.6091 -0.0849 -0.0128 -0.1135 103 ILE A CG2 
816  C CD1 . ILE A 103 ? 0.6553 0.6696 0.5995 -0.0472 -0.0361 -0.1128 103 ILE A CD1 
817  N N   . GLU A 104 ? 0.7261 0.7743 0.6971 -0.1205 0.0372  -0.1518 104 GLU A N   
818  C CA  . GLU A 104 ? 0.7390 0.7929 0.7210 -0.1392 0.0539  -0.1648 104 GLU A CA  
819  C C   . GLU A 104 ? 0.7120 0.8242 0.7477 -0.1296 0.0526  -0.1798 104 GLU A C   
820  O O   . GLU A 104 ? 0.6730 0.7830 0.7244 -0.1347 0.0537  -0.1862 104 GLU A O   
821  C CB  . GLU A 104 ? 0.7851 0.8475 0.7511 -0.1610 0.0778  -0.1732 104 GLU A CB  
822  C CG  . GLU A 104 ? 0.8152 0.8699 0.7774 -0.1867 0.0992  -0.1855 104 GLU A CG  
823  C CD  . GLU A 104 ? 0.9811 1.0408 0.9199 -0.2081 0.1203  -0.1923 104 GLU A CD  
824  O OE1 . GLU A 104 ? 0.9338 1.0123 0.8666 -0.2002 0.1173  -0.1891 104 GLU A OE1 
825  O OE2 . GLU A 104 ? 1.1192 1.1650 1.0452 -0.2331 0.1398  -0.2014 104 GLU A OE2 
826  N N   . ASN A 105 ? 0.6279 0.7925 0.6923 -0.1143 0.0499  -0.1853 105 ASN A N   
827  C CA  . ASN A 105 ? 0.6193 0.8438 0.7351 -0.1032 0.0501  -0.1998 105 ASN A CA  
828  C C   . ASN A 105 ? 0.6722 0.8975 0.8097 -0.0831 0.0258  -0.1924 105 ASN A C   
829  O O   . ASN A 105 ? 0.6674 0.9288 0.8447 -0.0776 0.0243  -0.2030 105 ASN A O   
830  C CB  . ASN A 105 ? 0.5927 0.8719 0.7277 -0.0933 0.0577  -0.2090 105 ASN A CB  
831  C CG  . ASN A 105 ? 0.5505 0.8479 0.6753 -0.1123 0.0829  -0.2237 105 ASN A CG  
832  O OD1 . ASN A 105 ? 0.6246 0.9043 0.7386 -0.1335 0.0968  -0.2304 105 ASN A OD1 
833  N ND2 . ASN A 105 ? 0.5530 0.8846 0.6786 -0.1052 0.0888  -0.2292 105 ASN A ND2 
834  N N   . LEU A 106 ? 0.6314 0.8225 0.7450 -0.0715 0.0067  -0.1759 106 LEU A N   
835  C CA  . LEU A 106 ? 0.6332 0.8242 0.7628 -0.0537 -0.0175 -0.1699 106 LEU A CA  
836  C C   . LEU A 106 ? 0.7088 0.8767 0.8402 -0.0604 -0.0222 -0.1719 106 LEU A C   
837  O O   . LEU A 106 ? 0.6837 0.8829 0.8521 -0.0495 -0.0337 -0.1778 106 LEU A O   
838  C CB  . LEU A 106 ? 0.6523 0.8058 0.7486 -0.0429 -0.0350 -0.1539 106 LEU A CB  
839  C CG  . LEU A 106 ? 0.6243 0.8101 0.7318 -0.0296 -0.0371 -0.1526 106 LEU A CG  
840  C CD1 . LEU A 106 ? 0.6033 0.7515 0.6751 -0.0225 -0.0497 -0.1388 106 LEU A CD1 
841  C CD2 . LEU A 106 ? 0.5997 0.8366 0.7535 -0.0123 -0.0481 -0.1587 106 LEU A CD2 
842  N N   . GLU A 107 ? 0.8509 0.9647 0.9426 -0.0781 -0.0132 -0.1674 107 GLU A N   
843  C CA  . GLU A 107 ? 0.9178 1.0029 1.0062 -0.0846 -0.0174 -0.1688 107 GLU A CA  
844  C C   . GLU A 107 ? 0.9083 1.0339 1.0358 -0.0967 0.0003  -0.1871 107 GLU A C   
845  O O   . GLU A 107 ? 0.8864 1.0124 1.0325 -0.0956 -0.0070 -0.1919 107 GLU A O   
846  C CB  . GLU A 107 ? 0.9874 0.9974 1.0173 -0.0988 -0.0126 -0.1573 107 GLU A CB  
847  C CG  . GLU A 107 ? 1.0920 1.0892 1.0952 -0.1179 0.0111  -0.1574 107 GLU A CG  
848  C CD  . GLU A 107 ? 1.3277 1.2542 1.2710 -0.1226 0.0091  -0.1410 107 GLU A CD  
849  O OE1 . GLU A 107 ? 1.4017 1.2920 1.3237 -0.1082 -0.0113 -0.1303 107 GLU A OE1 
850  O OE2 . GLU A 107 ? 1.4015 1.3110 1.3184 -0.1397 0.0277  -0.1397 107 GLU A OE2 
851  N N   . ALA A 108 ? 0.8652 1.0267 1.0051 -0.1076 0.0234  -0.1988 108 ALA A N   
852  C CA  . ALA A 108 ? 0.8224 1.0298 1.0008 -0.1180 0.0422  -0.2194 108 ALA A CA  
853  C C   . ALA A 108 ? 0.8305 1.1043 1.0674 -0.0967 0.0310  -0.2289 108 ALA A C   
854  O O   . ALA A 108 ? 0.8914 1.1842 1.1602 -0.0968 0.0294  -0.2388 108 ALA A O   
855  C CB  . ALA A 108 ? 0.7724 1.0043 0.9451 -0.1337 0.0692  -0.2314 108 ALA A CB  
856  N N   . ASN A 109 ? 0.8008 1.1120 1.0535 -0.0783 0.0238  -0.2266 109 ASN A N   
857  C CA  . ASN A 109 ? 0.7993 1.1725 1.1057 -0.0565 0.0124  -0.2338 109 ASN A CA  
858  C C   . ASN A 109 ? 0.9023 1.2586 1.2179 -0.0449 -0.0145 -0.2252 109 ASN A C   
859  O O   . ASN A 109 ? 0.9280 1.3331 1.2918 -0.0323 -0.0224 -0.2341 109 ASN A O   
860  C CB  . ASN A 109 ? 0.6745 1.0780 0.9867 -0.0390 0.0082  -0.2295 109 ASN A CB  
861  C CG  . ASN A 109 ? 0.7340 1.1630 1.0404 -0.0471 0.0333  -0.2406 109 ASN A CG  
862  O OD1 . ASN A 109 ? 0.7374 1.1802 1.0481 -0.0635 0.0550  -0.2560 109 ASN A OD1 
863  N ND2 . ASN A 109 ? 0.6810 1.1169 0.9762 -0.0357 0.0303  -0.2338 109 ASN A ND2 
864  N N   . LYS A 110 ? 0.9766 1.2671 1.2464 -0.0477 -0.0291 -0.2088 110 LYS A N   
865  C CA  . LYS A 110 ? 0.9672 1.2359 1.2374 -0.0382 -0.0547 -0.2022 110 LYS A CA  
866  C C   . LYS A 110 ? 1.0344 1.3024 1.3223 -0.0496 -0.0484 -0.2133 110 LYS A C   
867  O O   . LYS A 110 ? 1.1029 1.4097 1.4339 -0.0381 -0.0615 -0.2206 110 LYS A O   
868  C CB  . LYS A 110 ? 0.9956 1.1917 1.2062 -0.0392 -0.0679 -0.1846 110 LYS A CB  
869  C CG  . LYS A 110 ? 0.9385 1.1017 1.1374 -0.0315 -0.0925 -0.1791 110 LYS A CG  
870  C CD  . LYS A 110 ? 0.9307 1.0199 1.0648 -0.0331 -0.1007 -0.1637 110 LYS A CD  
871  C CE  . LYS A 110 ? 0.9047 0.9555 1.0191 -0.0258 -0.1232 -0.1598 110 LYS A CE  
872  N NZ  . LYS A 110 ? 0.9652 0.9443 1.0134 -0.0253 -0.1293 -0.1459 110 LYS A NZ  
910  N N   . ILE B 4   ? 0.9998 1.0007 1.2347 -0.0320 0.0382  -0.0410 4   ILE B N   
911  C CA  . ILE B 4   ? 0.9875 0.9707 1.2004 -0.0337 0.0305  -0.0332 4   ILE B CA  
912  C C   . ILE B 4   ? 0.9793 0.9510 1.2039 -0.0240 0.0219  -0.0272 4   ILE B C   
913  O O   . ILE B 4   ? 0.9531 0.9368 1.2058 -0.0145 0.0206  -0.0200 4   ILE B O   
914  C CB  . ILE B 4   ? 0.9905 0.9904 1.2054 -0.0347 0.0295  -0.0258 4   ILE B CB  
915  C CG1 . ILE B 4   ? 0.9858 1.0006 1.1928 -0.0462 0.0392  -0.0352 4   ILE B CG1 
916  C CG2 . ILE B 4   ? 0.9653 0.9455 1.1575 -0.0365 0.0227  -0.0193 4   ILE B CG2 
917  C CD1 . ILE B 4   ? 0.9889 0.9774 1.1579 -0.0604 0.0453  -0.0425 4   ILE B CD1 
918  N N   . PRO B 5   ? 1.0403 0.9887 1.2425 -0.0262 0.0164  -0.0307 5   PRO B N   
919  C CA  . PRO B 5   ? 1.0183 0.9589 1.2344 -0.0184 0.0087  -0.0295 5   PRO B CA  
920  C C   . PRO B 5   ? 1.0115 0.9560 1.2380 -0.0131 0.0030  -0.0182 5   PRO B C   
921  O O   . PRO B 5   ? 0.9977 0.9443 1.2104 -0.0160 0.0021  -0.0120 5   PRO B O   
922  C CB  . PRO B 5   ? 1.0479 0.9661 1.2324 -0.0216 0.0028  -0.0375 5   PRO B CB  
923  C CG  . PRO B 5   ? 1.1394 1.0519 1.2972 -0.0310 0.0111  -0.0437 5   PRO B CG  
924  C CD  . PRO B 5   ? 1.0569 0.9853 1.2205 -0.0353 0.0181  -0.0377 5   PRO B CD  
925  N N   . LYS B 6   ? 1.0082 0.9533 1.2599 -0.0064 0.0006  -0.0167 6   LYS B N   
926  C CA  . LYS B 6   ? 1.0407 0.9887 1.3037 -0.0020 -0.0030 -0.0072 6   LYS B CA  
927  C C   . LYS B 6   ? 1.0159 0.9526 1.2541 -0.0041 -0.0117 -0.0077 6   LYS B C   
928  O O   . LYS B 6   ? 1.0021 0.9428 1.2391 -0.0031 -0.0133 0.0004  6   LYS B O   
929  C CB  . LYS B 6   ? 1.1037 1.0503 1.3965 0.0031  -0.0017 -0.0085 6   LYS B CB  
930  C CG  . LYS B 6   ? 1.2359 1.1850 1.5414 0.0065  -0.0029 0.0006  6   LYS B CG  
931  C CD  . LYS B 6   ? 1.3901 1.3347 1.7234 0.0086  -0.0002 -0.0040 6   LYS B CD  
932  C CE  . LYS B 6   ? 1.3628 1.3100 1.7080 0.0105  0.0012  0.0050  6   LYS B CE  
933  N NZ  . LYS B 6   ? 1.3198 1.2622 1.6938 0.0103  0.0067  -0.0006 6   LYS B NZ  
934  N N   . GLU B 7   ? 0.9899 0.9119 1.2074 -0.0057 -0.0175 -0.0174 7   GLU B N   
935  C CA  . GLU B 7   ? 0.9691 0.8778 1.1612 -0.0047 -0.0266 -0.0176 7   GLU B CA  
936  C C   . GLU B 7   ? 0.8683 0.7725 1.0351 -0.0099 -0.0232 -0.0109 7   GLU B C   
937  O O   . GLU B 7   ? 0.7980 0.6942 0.9514 -0.0082 -0.0283 -0.0074 7   GLU B O   
938  C CB  . GLU B 7   ? 1.0010 0.8936 1.1695 -0.0035 -0.0339 -0.0284 7   GLU B CB  
939  C CG  . GLU B 7   ? 1.1215 1.0197 1.3133 -0.0001 -0.0372 -0.0393 7   GLU B CG  
940  C CD  . GLU B 7   ? 1.2080 1.1114 1.4114 -0.0043 -0.0274 -0.0443 7   GLU B CD  
941  O OE1 . GLU B 7   ? 1.1951 1.0900 1.3717 -0.0090 -0.0239 -0.0476 7   GLU B OE1 
942  O OE2 . GLU B 7   ? 1.2305 1.1451 1.4691 -0.0029 -0.0219 -0.0449 7   GLU B OE2 
943  N N   . MET B 8   ? 0.8836 0.7937 1.0455 -0.0166 -0.0138 -0.0108 8   MET B N   
944  C CA  . MET B 8   ? 0.8401 0.7465 0.9788 -0.0241 -0.0087 -0.0079 8   MET B CA  
945  C C   . MET B 8   ? 0.7654 0.6914 0.9219 -0.0237 -0.0066 0.0002  8   MET B C   
946  O O   . MET B 8   ? 0.7204 0.6411 0.8603 -0.0275 -0.0063 0.0027  8   MET B O   
947  C CB  . MET B 8   ? 0.8425 0.7499 0.9695 -0.0331 0.0014  -0.0141 8   MET B CB  
948  C CG  . MET B 8   ? 0.8911 0.7845 0.9852 -0.0435 0.0080  -0.0150 8   MET B CG  
949  S SD  . MET B 8   ? 0.9399 0.8268 1.0129 -0.0564 0.0218  -0.0250 8   MET B SD  
950  C CE  . MET B 8   ? 0.9483 0.8010 0.9872 -0.0523 0.0156  -0.0284 8   MET B CE  
951  N N   . LEU B 9   ? 0.8266 0.7739 1.0146 -0.0187 -0.0046 0.0042  9   LEU B N   
952  C CA  . LEU B 9   ? 0.7814 0.7472 0.9830 -0.0164 -0.0036 0.0128  9   LEU B CA  
953  C C   . LEU B 9   ? 0.6885 0.6470 0.8905 -0.0123 -0.0098 0.0175  9   LEU B C   
954  O O   . LEU B 9   ? 0.6771 0.6424 0.8747 -0.0138 -0.0094 0.0220  9   LEU B O   
955  C CB  . LEU B 9   ? 0.8794 0.8656 1.1108 -0.0094 -0.0001 0.0180  9   LEU B CB  
956  C CG  . LEU B 9   ? 0.9883 0.9946 1.2317 -0.0046 0.0007  0.0284  9   LEU B CG  
957  C CD1 . LEU B 9   ? 0.8092 0.8313 1.0390 -0.0114 0.0026  0.0264  9   LEU B CD1 
958  C CD2 . LEU B 9   ? 0.9372 0.9572 1.2064 0.0055  0.0040  0.0354  9   LEU B CD2 
959  N N   . ARG B 10  ? 0.7123 0.6594 0.9218 -0.0073 -0.0151 0.0148  10  ARG B N   
960  C CA  . ARG B 10  ? 0.7186 0.6598 0.9291 -0.0037 -0.0211 0.0162  10  ARG B CA  
961  C C   . ARG B 10  ? 0.7189 0.6442 0.8986 -0.0068 -0.0250 0.0138  10  ARG B C   
962  O O   . ARG B 10  ? 0.7074 0.6340 0.8846 -0.0064 -0.0259 0.0172  10  ARG B O   
963  C CB  . ARG B 10  ? 0.7784 0.7134 1.0040 0.0015  -0.0265 0.0098  10  ARG B CB  
964  C CG  . ARG B 10  ? 0.8988 0.8450 1.1574 0.0044  -0.0209 0.0125  10  ARG B CG  
965  C CD  . ARG B 10  ? 1.1187 1.0620 1.3948 0.0077  -0.0256 0.0056  10  ARG B CD  
966  N NE  . ARG B 10  ? 1.2613 1.2068 1.5647 0.0085  -0.0204 0.0016  10  ARG B NE  
967  C CZ  . ARG B 10  ? 1.3607 1.3066 1.6853 0.0094  -0.0221 -0.0075 10  ARG B CZ  
968  N NH1 . ARG B 10  ? 1.3508 1.2975 1.6736 0.0112  -0.0304 -0.0137 10  ARG B NH1 
969  N NH2 . ARG B 10  ? 1.3290 1.2749 1.6785 0.0085  -0.0148 -0.0118 10  ARG B NH2 
970  N N   . ALA B 11  ? 0.6996 0.6076 0.8541 -0.0098 -0.0259 0.0081  11  ALA B N   
971  C CA  . ALA B 11  ? 0.6624 0.5482 0.7834 -0.0119 -0.0281 0.0069  11  ALA B CA  
972  C C   . ALA B 11  ? 0.6712 0.5621 0.7830 -0.0204 -0.0198 0.0102  11  ALA B C   
973  O O   . ALA B 11  ? 0.5993 0.4779 0.6953 -0.0208 -0.0207 0.0111  11  ALA B O   
974  C CB  . ALA B 11  ? 0.6496 0.5134 0.7417 -0.0137 -0.0286 0.0014  11  ALA B CB  
975  N N   . GLN B 12  ? 0.6663 0.5763 0.7884 -0.0269 -0.0116 0.0103  12  GLN B N   
976  C CA  . GLN B 12  ? 0.6434 0.5648 0.7605 -0.0357 -0.0041 0.0105  12  GLN B CA  
977  C C   . GLN B 12  ? 0.5593 0.4983 0.6934 -0.0316 -0.0064 0.0161  12  GLN B C   
978  O O   . GLN B 12  ? 0.5143 0.4510 0.6366 -0.0366 -0.0039 0.0152  12  GLN B O   
979  C CB  . GLN B 12  ? 0.6700 0.6129 0.7978 -0.0417 0.0036  0.0071  12  GLN B CB  
980  C CG  . GLN B 12  ? 0.6580 0.5843 0.7654 -0.0493 0.0096  -0.0003 12  GLN B CG  
981  C CD  . GLN B 12  ? 0.7494 0.7015 0.8727 -0.0546 0.0175  -0.0056 12  GLN B CD  
982  O OE1 . GLN B 12  ? 0.6150 0.5972 0.7653 -0.0497 0.0164  -0.0026 12  GLN B OE1 
983  N NE2 . GLN B 12  ? 0.7383 0.6785 0.8439 -0.0639 0.0257  -0.0137 12  GLN B NE2 
984  N N   . THR B 13  ? 0.5171 0.4717 0.6779 -0.0232 -0.0098 0.0216  13  THR B N   
985  C CA  . THR B 13  ? 0.4870 0.4558 0.6618 -0.0191 -0.0108 0.0277  13  THR B CA  
986  C C   . THR B 13  ? 0.5290 0.4804 0.6929 -0.0174 -0.0152 0.0261  13  THR B C   
987  O O   . THR B 13  ? 0.5072 0.4652 0.6684 -0.0195 -0.0133 0.0271  13  THR B O   
988  C CB  . THR B 13  ? 0.5345 0.5145 0.7366 -0.0107 -0.0117 0.0340  13  THR B CB  
989  O OG1 . THR B 13  ? 0.5293 0.5253 0.7422 -0.0098 -0.0076 0.0363  13  THR B OG1 
990  C CG2 . THR B 13  ? 0.4325 0.4239 0.6459 -0.0070 -0.0108 0.0408  13  THR B CG2 
991  N N   . ASN B 14  ? 0.5187 0.4498 0.6769 -0.0126 -0.0215 0.0225  14  ASN B N   
992  C CA  . ASN B 14  ? 0.5241 0.4386 0.6724 -0.0081 -0.0273 0.0198  14  ASN B CA  
993  C C   . ASN B 14  ? 0.5450 0.4436 0.6652 -0.0143 -0.0237 0.0177  14  ASN B C   
994  O O   . ASN B 14  ? 0.5546 0.4517 0.6734 -0.0132 -0.0238 0.0174  14  ASN B O   
995  C CB  . ASN B 14  ? 0.6391 0.5361 0.7824 -0.0008 -0.0362 0.0148  14  ASN B CB  
996  C CG  . ASN B 14  ? 0.6429 0.5454 0.8077 0.0082  -0.0434 0.0120  14  ASN B CG  
997  O OD1 . ASN B 14  ? 0.6682 0.5868 0.8613 0.0098  -0.0424 0.0123  14  ASN B OD1 
998  N ND2 . ASN B 14  ? 0.5316 0.4202 0.6840 0.0140  -0.0497 0.0086  14  ASN B ND2 
999  O O   . HOX B 15  ? 0.6188 0.4906 0.6827 -0.0394 -0.0031 0.0092  15  HOX B O   
1000 C C   . HOX B 15  ? 0.5829 0.4672 0.6594 -0.0372 -0.0057 0.0116  15  HOX B C   
1001 N N   . HOX B 15  ? 0.5749 0.4604 0.6730 -0.0216 -0.0190 0.0153  15  HOX B N   
1002 C CA  . HOX B 15  ? 0.5951 0.4600 0.6641 -0.0295 -0.0127 0.0124  15  HOX B CA  
1003 C CB  . HOX B 15  ? 0.6205 0.4722 0.6678 -0.0391 -0.0050 0.0091  15  HOX B CB  
1004 C CG  . HOX B 15  ? 0.6826 0.5086 0.6989 -0.0492 0.0045  0.0055  15  HOX B CG  
1005 C CZ  . HOX B 15  ? 0.7542 0.5236 0.7107 -0.0708 0.0277  -0.0024 15  HOX B CZ  
1006 N NZ  . HOX B 15  ? 0.9114 0.6489 0.8379 -0.0826 0.0415  -0.0068 15  HOX B NZ  
1007 C CD1 . HOX B 15  ? 0.7199 0.5122 0.7122 -0.0431 0.0016  0.0066  15  HOX B CD1 
1008 C CD2 . HOX B 15  ? 0.7225 0.5569 0.7336 -0.0647 0.0175  -0.0001 15  HOX B CD2 
1009 C CE1 . HOX B 15  ? 0.7436 0.5064 0.7054 -0.0527 0.0126  0.0037  15  HOX B CE1 
1010 C CE2 . HOX B 15  ? 0.6949 0.5034 0.6779 -0.0765 0.0292  -0.0050 15  HOX B CE2 
1011 N N   . ILE B 16  ? 0.4831 0.3999 0.5809 -0.0403 -0.0028 0.0132  16  ILE B N   
1012 C CA  . ILE B 16  ? 0.4938 0.4354 0.5991 -0.0466 0.0024  0.0117  16  ILE B CA  
1013 C C   . ILE B 16  ? 0.4525 0.3991 0.5670 -0.0404 -0.0010 0.0146  16  ILE B C   
1014 O O   . ILE B 16  ? 0.5047 0.4508 0.6106 -0.0460 0.0032  0.0101  16  ILE B O   
1015 C CB  . ILE B 16  ? 0.4507 0.4271 0.5763 -0.0472 0.0039  0.0140  16  ILE B CB  
1016 C CG1 . ILE B 16  ? 0.4374 0.4118 0.5538 -0.0561 0.0098  0.0075  16  ILE B CG1 
1017 C CG2 . ILE B 16  ? 0.3714 0.3781 0.5057 -0.0498 0.0063  0.0135  16  ILE B CG2 
1018 C CD1 . ILE B 16  ? 0.3744 0.3835 0.5110 -0.0555 0.0110  0.0077  16  ILE B CD1 
1019 N N   . LEU B 17  ? 0.4393 0.3909 0.5723 -0.0299 -0.0073 0.0205  17  LEU B N   
1020 C CA  . LEU B 17  ? 0.4265 0.3846 0.5705 -0.0248 -0.0088 0.0222  17  LEU B CA  
1021 C C   . LEU B 17  ? 0.4676 0.4003 0.5951 -0.0240 -0.0101 0.0163  17  LEU B C   
1022 O O   . LEU B 17  ? 0.4572 0.3949 0.5836 -0.0264 -0.0066 0.0135  17  LEU B O   
1023 C CB  . LEU B 17  ? 0.4147 0.3785 0.5817 -0.0153 -0.0134 0.0273  17  LEU B CB  
1024 C CG  . LEU B 17  ? 0.5081 0.4960 0.6918 -0.0145 -0.0102 0.0350  17  LEU B CG  
1025 C CD1 . LEU B 17  ? 0.3612 0.3506 0.5678 -0.0069 -0.0117 0.0395  17  LEU B CD1 
1026 C CD2 . LEU B 17  ? 0.3929 0.4045 0.5760 -0.0179 -0.0051 0.0380  17  LEU B CD2 
1027 N N   . LEU B 18  ? 0.4855 0.3899 0.5985 -0.0197 -0.0150 0.0142  18  LEU B N   
1028 C CA  . LEU B 18  ? 0.5350 0.4117 0.6305 -0.0153 -0.0174 0.0099  18  LEU B CA  
1029 C C   . LEU B 18  ? 0.5734 0.4364 0.6456 -0.0263 -0.0077 0.0055  18  LEU B C   
1030 O O   . LEU B 18  ? 0.5664 0.4176 0.6319 -0.0250 -0.0059 0.0016  18  LEU B O   
1031 C CB  . LEU B 18  ? 0.5432 0.3928 0.6245 -0.0062 -0.0259 0.0096  18  LEU B CB  
1032 C CG  . LEU B 18  ? 0.5135 0.3750 0.6203 0.0061  -0.0362 0.0092  18  LEU B CG  
1033 C CD1 . LEU B 18  ? 0.4651 0.3083 0.5612 0.0153  -0.0462 0.0076  18  LEU B CD1 
1034 C CD2 . LEU B 18  ? 0.5430 0.4060 0.6597 0.0129  -0.0384 0.0054  18  LEU B CD2 
1035 N N   . MET B 19  ? 0.5865 0.4521 0.6482 -0.0379 -0.0004 0.0043  19  MET B N   
1036 C CA  . MET B 19  ? 0.5683 0.4244 0.6115 -0.0512 0.0109  -0.0025 19  MET B CA  
1037 C C   . MET B 19  ? 0.5821 0.4672 0.6404 -0.0562 0.0148  -0.0064 19  MET B C   
1038 O O   . MET B 19  ? 0.5996 0.4726 0.6458 -0.0628 0.0219  -0.0135 19  MET B O   
1039 C CB  . MET B 19  ? 0.6218 0.4811 0.6561 -0.0636 0.0186  -0.0053 19  MET B CB  
1040 C CG  . MET B 19  ? 0.6951 0.5154 0.7017 -0.0631 0.0198  -0.0040 19  MET B CG  
1041 S SD  . MET B 19  ? 0.8217 0.5883 0.7901 -0.0648 0.0272  -0.0070 19  MET B SD  
1042 C CE  . MET B 19  ? 0.6984 0.4827 0.6704 -0.0852 0.0430  -0.0187 19  MET B CE  
1043 N N   . VAL B 20  ? 0.5698 0.4916 0.6527 -0.0528 0.0110  -0.0018 20  VAL B N   
1044 C CA  . VAL B 20  ? 0.5580 0.5087 0.6524 -0.0560 0.0141  -0.0043 20  VAL B CA  
1045 C C   . VAL B 20  ? 0.5687 0.5055 0.6626 -0.0503 0.0134  -0.0068 20  VAL B C   
1046 O O   . VAL B 20  ? 0.5791 0.5180 0.6666 -0.0574 0.0199  -0.0148 20  VAL B O   
1047 C CB  . VAL B 20  ? 0.4790 0.4651 0.5957 -0.0504 0.0101  0.0041  20  VAL B CB  
1048 C CG1 . VAL B 20  ? 0.4104 0.4218 0.5349 -0.0508 0.0124  0.0035  20  VAL B CG1 
1049 C CG2 . VAL B 20  ? 0.4578 0.4636 0.5763 -0.0562 0.0118  0.0040  20  VAL B CG2 
1050 N N   . LEU B 21  ? 0.5512 0.4761 0.6539 -0.0375 0.0056  -0.0019 21  LEU B N   
1051 C CA  . LEU B 21  ? 0.6020 0.5163 0.7077 -0.0306 0.0044  -0.0058 21  LEU B CA  
1052 C C   . LEU B 21  ? 0.6313 0.5094 0.7126 -0.0325 0.0081  -0.0129 21  LEU B C   
1053 O O   . LEU B 21  ? 0.6344 0.5070 0.7149 -0.0318 0.0117  -0.0194 21  LEU B O   
1054 C CB  . LEU B 21  ? 0.5151 0.4267 0.6378 -0.0167 -0.0051 -0.0018 21  LEU B CB  
1055 C CG  . LEU B 21  ? 0.4897 0.4321 0.6384 -0.0144 -0.0060 0.0046  21  LEU B CG  
1056 C CD1 . LEU B 21  ? 0.4776 0.4151 0.6441 -0.0026 -0.0137 0.0039  21  LEU B CD1 
1057 C CD2 . LEU B 21  ? 0.4034 0.3709 0.5602 -0.0194 0.0015  0.0038  21  LEU B CD2 
1058 N N   . LYS B 22  ? 0.6723 0.5235 0.7322 -0.0352 0.0088  -0.0120 22  LYS B N   
1059 C CA  . LYS B 22  ? 0.6802 0.4919 0.7123 -0.0382 0.0152  -0.0174 22  LYS B CA  
1060 C C   . LYS B 22  ? 0.7778 0.5983 0.8049 -0.0547 0.0286  -0.0269 22  LYS B C   
1061 O O   . LYS B 22  ? 0.8114 0.6051 0.8237 -0.0566 0.0356  -0.0337 22  LYS B O   
1062 C CB  . LYS B 22  ? 0.7126 0.4933 0.7199 -0.0391 0.0154  -0.0135 22  LYS B CB  
1063 C CG  . LYS B 22  ? 0.7394 0.4695 0.7138 -0.0372 0.0208  -0.0155 22  LYS B CG  
1064 C CD  . LYS B 22  ? 0.7391 0.4411 0.6853 -0.0435 0.0258  -0.0123 22  LYS B CD  
1065 C CE  . LYS B 22  ? 0.8118 0.4591 0.7203 -0.0450 0.0360  -0.0139 22  LYS B CE  
1066 N NZ  . LYS B 22  ? 0.9765 0.5968 0.8555 -0.0563 0.0463  -0.0121 22  LYS B NZ  
1067 N N   . GLN B 23  ? 0.7831 0.6411 0.8222 -0.0661 0.0322  -0.0285 23  GLN B N   
1068 C CA  . GLN B 23  ? 0.7789 0.6558 0.8182 -0.0807 0.0427  -0.0398 23  GLN B CA  
1069 C C   . GLN B 23  ? 0.8216 0.7104 0.8724 -0.0757 0.0423  -0.0435 23  GLN B C   
1070 O O   . GLN B 23  ? 0.8373 0.7243 0.8816 -0.0854 0.0518  -0.0552 23  GLN B O   
1071 C CB  . GLN B 23  ? 0.7480 0.6699 0.8008 -0.0896 0.0433  -0.0406 23  GLN B CB  
1072 C CG  . GLN B 23  ? 0.7356 0.6571 0.7840 -0.0947 0.0438  -0.0381 23  GLN B CG  
1073 C CD  . GLN B 23  ? 0.9535 0.8475 0.9800 -0.1101 0.0566  -0.0484 23  GLN B CD  
1074 O OE1 . GLN B 23  ? 1.0761 0.9587 1.0930 -0.1201 0.0666  -0.0597 23  GLN B OE1 
1075 N NE2 . GLN B 23  ? 1.0470 0.9300 1.0654 -0.1134 0.0582  -0.0458 23  GLN B NE2 
1076 N N   . GLY B 24  ? 0.7480 0.6503 0.8168 -0.0620 0.0329  -0.0354 24  GLY B N   
1077 C CA  . GLY B 24  ? 0.6861 0.6011 0.7674 -0.0571 0.0334  -0.0391 24  GLY B CA  
1078 C C   . GLY B 24  ? 0.6550 0.5987 0.7593 -0.0478 0.0263  -0.0299 24  GLY B C   
1079 O O   . GLY B 24  ? 0.6543 0.6136 0.7656 -0.0466 0.0219  -0.0209 24  GLY B O   
1080 N N   . ASP B 25  ? 0.5348 0.4837 0.6514 -0.0412 0.0267  -0.0327 25  ASP B N   
1081 C CA  . ASP B 25  ? 0.5231 0.4962 0.6616 -0.0340 0.0233  -0.0254 25  ASP B CA  
1082 C C   . ASP B 25  ? 0.5549 0.5627 0.6959 -0.0407 0.0262  -0.0190 25  ASP B C   
1083 O O   . ASP B 25  ? 0.5100 0.5324 0.6400 -0.0507 0.0316  -0.0246 25  ASP B O   
1084 C CB  . ASP B 25  ? 0.4775 0.4539 0.6276 -0.0294 0.0269  -0.0328 25  ASP B CB  
1085 C CG  . ASP B 25  ? 0.5702 0.5144 0.7199 -0.0190 0.0225  -0.0395 25  ASP B CG  
1086 O OD1 . ASP B 25  ? 0.6331 0.5488 0.7680 -0.0158 0.0173  -0.0378 25  ASP B OD1 
1087 O OD2 . ASP B 25  ? 0.5619 0.5090 0.7247 -0.0133 0.0246  -0.0467 25  ASP B OD2 
1088 N N   . ASN B 26  ? 0.4651 0.4866 0.6210 -0.0345 0.0229  -0.0079 26  ASN B N   
1089 C CA  . ASN B 26  ? 0.4832 0.5336 0.6392 -0.0374 0.0247  0.0006  26  ASN B CA  
1090 C C   . ASN B 26  ? 0.5026 0.5616 0.6761 -0.0296 0.0246  0.0120  26  ASN B C   
1091 O O   . ASN B 26  ? 0.4956 0.5407 0.6835 -0.0235 0.0227  0.0113  26  ASN B O   
1092 C CB  . ASN B 26  ? 0.5038 0.5546 0.6507 -0.0414 0.0211  0.0029  26  ASN B CB  
1093 C CG  . ASN B 26  ? 0.5221 0.6058 0.6634 -0.0463 0.0231  0.0050  26  ASN B CG  
1094 O OD1 . ASN B 26  ? 0.4866 0.5917 0.6311 -0.0429 0.0254  0.0113  26  ASN B OD1 
1095 N ND2 . ASN B 26  ? 0.5934 0.6816 0.7252 -0.0540 0.0227  -0.0012 26  ASN B ND2 
1096 N N   . TYR B 27  ? 0.4794 0.5616 0.6513 -0.0295 0.0271  0.0219  27  TYR B N   
1097 C CA  . TYR B 27  ? 0.5119 0.5995 0.6971 -0.0231 0.0300  0.0344  27  TYR B CA  
1098 C C   . TYR B 27  ? 0.5396 0.6332 0.7245 -0.0194 0.0263  0.0461  27  TYR B C   
1099 O O   . TYR B 27  ? 0.5408 0.6420 0.7152 -0.0222 0.0220  0.0441  27  TYR B O   
1100 C CB  . TYR B 27  ? 0.4893 0.5952 0.6705 -0.0240 0.0391  0.0375  27  TYR B CB  
1101 C CG  . TYR B 27  ? 0.5075 0.6385 0.6694 -0.0264 0.0397  0.0405  27  TYR B CG  
1102 C CD1 . TYR B 27  ? 0.5245 0.6652 0.6731 -0.0341 0.0393  0.0271  27  TYR B CD1 
1103 C CD2 . TYR B 27  ? 0.5945 0.7400 0.7512 -0.0202 0.0408  0.0558  27  TYR B CD2 
1104 C CE1 . TYR B 27  ? 0.5207 0.6895 0.6532 -0.0363 0.0387  0.0270  27  TYR B CE1 
1105 C CE2 . TYR B 27  ? 0.6252 0.7975 0.7636 -0.0199 0.0392  0.0578  27  TYR B CE2 
1106 C CZ  . TYR B 27  ? 0.5679 0.7543 0.6952 -0.0283 0.0377  0.0425  27  TYR B CZ  
1107 O OH  . TYR B 27  ? 0.4312 0.6488 0.5421 -0.0279 0.0350  0.0422  27  TYR B OH  
1108 N N   . VAL B 28  ? 0.4949 0.5847 0.6933 -0.0134 0.0292  0.0570  28  VAL B N   
1109 C CA  . VAL B 28  ? 0.4620 0.5501 0.6650 -0.0084 0.0258  0.0668  28  VAL B CA  
1110 C C   . VAL B 28  ? 0.4971 0.6075 0.6857 -0.0062 0.0244  0.0742  28  VAL B C   
1111 O O   . VAL B 28  ? 0.4833 0.5974 0.6701 -0.0055 0.0185  0.0737  28  VAL B O   
1112 C CB  . VAL B 28  ? 0.5148 0.5932 0.7354 -0.0034 0.0321  0.0761  28  VAL B CB  
1113 C CG1 . VAL B 28  ? 0.5183 0.5980 0.7403 0.0029  0.0314  0.0887  28  VAL B CG1 
1114 C CG2 . VAL B 28  ? 0.4262 0.4860 0.6649 -0.0043 0.0292  0.0662  28  VAL B CG2 
1115 N N   . TYR B 29  ? 0.4908 0.6179 0.6690 -0.0044 0.0298  0.0807  29  TYR B N   
1116 C CA  . TYR B 29  ? 0.5011 0.6533 0.6649 0.0001  0.0264  0.0869  29  TYR B CA  
1117 C C   . TYR B 29  ? 0.5229 0.6908 0.6775 -0.0079 0.0202  0.0717  29  TYR B C   
1118 O O   . TYR B 29  ? 0.5392 0.7255 0.6902 -0.0055 0.0144  0.0717  29  TYR B O   
1119 C CB  . TYR B 29  ? 0.5596 0.7253 0.7099 0.0048  0.0333  0.0973  29  TYR B CB  
1120 C CG  . TYR B 29  ? 0.6821 0.8311 0.8390 0.0125  0.0420  0.1142  29  TYR B CG  
1121 C CD1 . TYR B 29  ? 0.6940 0.8291 0.8638 0.0191  0.0404  0.1229  29  TYR B CD1 
1122 C CD2 . TYR B 29  ? 0.7861 0.9320 0.9363 0.0123  0.0535  0.1207  29  TYR B CD2 
1123 C CE1 . TYR B 29  ? 0.7994 0.9164 0.9759 0.0249  0.0505  0.1373  29  TYR B CE1 
1124 C CE2 . TYR B 29  ? 0.8003 0.9279 0.9562 0.0176  0.0644  0.1357  29  TYR B CE2 
1125 C CZ  . TYR B 29  ? 0.8832 0.9956 1.0526 0.0237  0.0630  0.1439  29  TYR B CZ  
1126 O OH  . TYR B 29  ? 0.8980 0.9892 1.0737 0.0277  0.0758  0.1577  29  TYR B OH  
1127 N N   . GLY B 30  ? 0.4832 0.6438 0.6352 -0.0174 0.0221  0.0577  30  GLY B N   
1128 C CA  . GLY B 30  ? 0.4934 0.6618 0.6377 -0.0270 0.0188  0.0421  30  GLY B CA  
1129 C C   . GLY B 30  ? 0.5283 0.6814 0.6787 -0.0294 0.0144  0.0382  30  GLY B C   
1130 O O   . GLY B 30  ? 0.5242 0.6905 0.6694 -0.0356 0.0122  0.0292  30  GLY B O   
1131 N N   . ILE B 31  ? 0.5214 0.6479 0.6828 -0.0254 0.0138  0.0433  31  ILE B N   
1132 C CA  . ILE B 31  ? 0.5402 0.6502 0.7046 -0.0274 0.0100  0.0398  31  ILE B CA  
1133 C C   . ILE B 31  ? 0.4604 0.5879 0.6293 -0.0224 0.0068  0.0467  31  ILE B C   
1134 O O   . ILE B 31  ? 0.4514 0.5821 0.6177 -0.0276 0.0051  0.0394  31  ILE B O   
1135 C CB  . ILE B 31  ? 0.4618 0.5421 0.6364 -0.0234 0.0089  0.0419  31  ILE B CB  
1136 C CG1 . ILE B 31  ? 0.4917 0.5550 0.6614 -0.0272 0.0104  0.0322  31  ILE B CG1 
1137 C CG2 . ILE B 31  ? 0.3999 0.4632 0.5744 -0.0243 0.0049  0.0393  31  ILE B CG2 
1138 C CD1 . ILE B 31  ? 0.4590 0.4999 0.6407 -0.0213 0.0079  0.0326  31  ILE B CD1 
1139 N N   . ILE B 32  ? 0.5136 0.6515 0.6891 -0.0119 0.0072  0.0607  32  ILE B N   
1140 C CA  . ILE B 32  ? 0.4840 0.6378 0.6645 -0.0041 0.0040  0.0682  32  ILE B CA  
1141 C C   . ILE B 32  ? 0.4734 0.6610 0.6454 -0.0069 0.0007  0.0604  32  ILE B C   
1142 O O   . ILE B 32  ? 0.4821 0.6808 0.6587 -0.0079 -0.0024 0.0550  32  ILE B O   
1143 C CB  . ILE B 32  ? 0.4957 0.6495 0.6814 0.0086  0.0068  0.0860  32  ILE B CB  
1144 C CG1 . ILE B 32  ? 0.4606 0.5836 0.6604 0.0100  0.0103  0.0903  32  ILE B CG1 
1145 C CG2 . ILE B 32  ? 0.4704 0.6450 0.6576 0.0194  0.0029  0.0941  32  ILE B CG2 
1146 C CD1 . ILE B 32  ? 0.5083 0.6253 0.7142 0.0201  0.0165  0.1068  32  ILE B CD1 
1147 N N   . LYS B 33  ? 0.4775 0.6841 0.6384 -0.0089 0.0017  0.0578  33  LYS B N   
1148 C CA  . LYS B 33  ? 0.5425 0.7862 0.6966 -0.0118 -0.0021 0.0477  33  LYS B CA  
1149 C C   . LYS B 33  ? 0.5356 0.7773 0.6906 -0.0270 -0.0010 0.0284  33  LYS B C   
1150 O O   . LYS B 33  ? 0.5008 0.7647 0.6611 -0.0285 -0.0040 0.0209  33  LYS B O   
1151 C CB  . LYS B 33  ? 0.6060 0.8678 0.7464 -0.0128 -0.0004 0.0461  33  LYS B CB  
1152 C CG  . LYS B 33  ? 0.8096 1.1141 0.9427 -0.0168 -0.0048 0.0324  33  LYS B CG  
1153 C CD  . LYS B 33  ? 0.8854 1.2232 1.0191 -0.0006 -0.0131 0.0422  33  LYS B CD  
1154 C CE  . LYS B 33  ? 0.9135 1.3002 1.0398 -0.0031 -0.0189 0.0270  33  LYS B CE  
1155 N NZ  . LYS B 33  ? 0.8504 1.2531 0.9876 -0.0184 -0.0192 0.0033  33  LYS B NZ  
1156 N N   . GLN B 34  ? 0.5561 0.7698 0.7058 -0.0381 0.0042  0.0201  34  GLN B N   
1157 C CA  . GLN B 34  ? 0.5287 0.7330 0.6744 -0.0533 0.0080  0.0028  34  GLN B CA  
1158 C C   . GLN B 34  ? 0.5469 0.7419 0.7001 -0.0535 0.0070  0.0029  34  GLN B C   
1159 O O   . GLN B 34  ? 0.6004 0.8065 0.7532 -0.0642 0.0098  -0.0110 34  GLN B O   
1160 C CB  . GLN B 34  ? 0.6030 0.7709 0.7403 -0.0604 0.0133  -0.0017 34  GLN B CB  
1161 C CG  . GLN B 34  ? 0.6793 0.8572 0.8093 -0.0636 0.0163  -0.0070 34  GLN B CG  
1162 C CD  . GLN B 34  ? 0.6829 0.8273 0.8044 -0.0722 0.0224  -0.0166 34  GLN B CD  
1163 O OE1 . GLN B 34  ? 0.7071 0.8193 0.8256 -0.0751 0.0237  -0.0183 34  GLN B OE1 
1164 N NE2 . GLN B 34  ? 0.7674 0.9183 0.8835 -0.0754 0.0261  -0.0229 34  GLN B NE2 
1165 N N   . VAL B 35  ? 0.4437 0.6190 0.6045 -0.0430 0.0044  0.0167  35  VAL B N   
1166 C CA  . VAL B 35  ? 0.5188 0.6838 0.6859 -0.0434 0.0042  0.0158  35  VAL B CA  
1167 C C   . VAL B 35  ? 0.5220 0.7241 0.7003 -0.0375 0.0006  0.0158  35  VAL B C   
1168 O O   . VAL B 35  ? 0.4304 0.6401 0.6124 -0.0445 0.0026  0.0053  35  VAL B O   
1169 C CB  . VAL B 35  ? 0.5253 0.6592 0.6981 -0.0347 0.0026  0.0278  35  VAL B CB  
1170 C CG1 . VAL B 35  ? 0.4181 0.5477 0.5993 -0.0324 0.0018  0.0285  35  VAL B CG1 
1171 C CG2 . VAL B 35  ? 0.4309 0.5294 0.5928 -0.0407 0.0048  0.0238  35  VAL B CG2 
1172 N N   . LYS B 36  ? 0.5011 0.7267 0.6840 -0.0240 -0.0042 0.0272  36  LYS B N   
1173 C CA  . LYS B 36  ? 0.4460 0.7076 0.6390 -0.0141 -0.0093 0.0285  36  LYS B CA  
1174 C C   . LYS B 36  ? 0.5733 0.8699 0.7668 -0.0253 -0.0094 0.0084  36  LYS B C   
1175 O O   . LYS B 36  ? 0.4942 0.8142 0.7000 -0.0236 -0.0114 0.0014  36  LYS B O   
1176 C CB  . LYS B 36  ? 0.4548 0.7334 0.6453 0.0025  -0.0139 0.0444  36  LYS B CB  
1177 C CG  . LYS B 36  ? 0.5721 0.8791 0.7725 0.0193  -0.0203 0.0517  36  LYS B CG  
1178 C CD  . LYS B 36  ? 0.6137 0.9290 0.8050 0.0368  -0.0234 0.0705  36  LYS B CD  
1179 C CE  . LYS B 36  ? 0.7052 1.0374 0.9049 0.0579  -0.0293 0.0826  36  LYS B CE  
1180 N NZ  . LYS B 36  ? 0.7585 1.1371 0.9667 0.0597  -0.0372 0.0672  36  LYS B NZ  
1181 N N   . GLU B 37  ? 0.6082 0.9100 0.7905 -0.0375 -0.0064 -0.0029 37  GLU B N   
1182 C CA  . GLU B 37  ? 0.5294 0.8667 0.7135 -0.0499 -0.0052 -0.0244 37  GLU B CA  
1183 C C   . GLU B 37  ? 0.5106 0.8272 0.6935 -0.0702 0.0048  -0.0415 37  GLU B C   
1184 O O   . GLU B 37  ? 0.5991 0.9451 0.7895 -0.0812 0.0076  -0.0606 37  GLU B O   
1185 C CB  . GLU B 37  ? 0.6283 0.9839 0.8009 -0.0536 -0.0058 -0.0301 37  GLU B CB  
1186 C CG  . GLU B 37  ? 0.7735 1.0996 0.9339 -0.0720 0.0039  -0.0418 37  GLU B CG  
1187 C CD  . GLU B 37  ? 0.8885 1.2343 1.0388 -0.0745 0.0035  -0.0476 37  GLU B CD  
1188 O OE1 . GLU B 37  ? 0.9210 1.3048 1.0715 -0.0619 -0.0048 -0.0424 37  GLU B OE1 
1189 O OE2 . GLU B 37  ? 0.9612 1.2834 1.1017 -0.0878 0.0116  -0.0570 37  GLU B OE2 
1190 N N   . ALA B 38  ? 0.5031 0.7706 0.6766 -0.0750 0.0105  -0.0357 38  ALA B N   
1191 C CA  . ALA B 38  ? 0.5283 0.7709 0.6956 -0.0924 0.0207  -0.0492 38  ALA B CA  
1192 C C   . ALA B 38  ? 0.5277 0.7702 0.7057 -0.0901 0.0213  -0.0487 38  ALA B C   
1193 O O   . ALA B 38  ? 0.5786 0.8137 0.7538 -0.1057 0.0309  -0.0631 38  ALA B O   
1194 C CB  . ALA B 38  ? 0.5563 0.7461 0.7058 -0.0966 0.0256  -0.0436 38  ALA B CB  
1195 N N   . SER B 39  ? 0.4861 0.7348 0.6758 -0.0720 0.0130  -0.0331 39  SER B N   
1196 C CA  . SER B 39  ? 0.4666 0.7221 0.6699 -0.0677 0.0130  -0.0336 39  SER B CA  
1197 C C   . SER B 39  ? 0.5184 0.8285 0.7411 -0.0598 0.0071  -0.0402 39  SER B C   
1198 O O   . SER B 39  ? 0.4658 0.7874 0.7037 -0.0514 0.0052  -0.0388 39  SER B O   
1199 C CB  . SER B 39  ? 0.5019 0.7300 0.7080 -0.0524 0.0084  -0.0144 39  SER B CB  
1200 O OG  . SER B 39  ? 0.5221 0.7676 0.7357 -0.0346 0.0001  0.0005  39  SER B OG  
1201 N N   . ASN B 40  ? 0.4936 0.8389 0.7164 -0.0613 0.0036  -0.0480 40  ASN B N   
1202 C CA  . ASN B 40  ? 0.4025 0.8043 0.6422 -0.0509 -0.0047 -0.0545 40  ASN B CA  
1203 C C   . ASN B 40  ? 0.4206 0.8272 0.6700 -0.0250 -0.0144 -0.0337 40  ASN B C   
1204 O O   . ASN B 40  ? 0.4472 0.8827 0.7148 -0.0151 -0.0186 -0.0372 40  ASN B O   
1205 C CB  . ASN B 40  ? 0.3914 0.8214 0.6461 -0.0654 0.0016  -0.0791 40  ASN B CB  
1206 C CG  . ASN B 40  ? 0.4093 0.8305 0.6533 -0.0925 0.0141  -0.1001 40  ASN B CG  
1207 O OD1 . ASN B 40  ? 0.4916 0.8961 0.7356 -0.1099 0.0266  -0.1133 40  ASN B OD1 
1208 N ND2 . ASN B 40  ? 0.3634 0.7927 0.5966 -0.0964 0.0123  -0.1030 40  ASN B ND2 
1209 N N   . GLY B 41  ? 0.4434 0.8202 0.6812 -0.0143 -0.0169 -0.0125 41  GLY B N   
1210 C CA  . GLY B 41  ? 0.4236 0.7971 0.6670 0.0090  -0.0233 0.0088  41  GLY B CA  
1211 C C   . GLY B 41  ? 0.5292 0.8678 0.7807 0.0125  -0.0192 0.0172  41  GLY B C   
1212 O O   . GLY B 41  ? 0.5759 0.9031 0.8315 0.0302  -0.0221 0.0355  41  GLY B O   
1213 N N   . GLU B 42  ? 0.6782 0.9981 0.9308 -0.0040 -0.0117 0.0042  42  GLU B N   
1214 C CA  . GLU B 42  ? 0.6730 0.9665 0.9340 -0.0007 -0.0083 0.0089  42  GLU B CA  
1215 C C   . GLU B 42  ? 0.6982 0.9483 0.9513 0.0044  -0.0074 0.0258  42  GLU B C   
1216 O O   . GLU B 42  ? 0.7782 1.0153 1.0416 0.0169  -0.0080 0.0369  42  GLU B O   
1217 C CB  . GLU B 42  ? 0.7391 1.0225 0.9978 -0.0205 0.0005  -0.0096 42  GLU B CB  
1218 C CG  . GLU B 42  ? 0.7671 1.0951 1.0407 -0.0258 0.0018  -0.0287 42  GLU B CG  
1219 C CD  . GLU B 42  ? 0.8519 1.1668 1.1201 -0.0484 0.0139  -0.0474 42  GLU B CD  
1220 O OE1 . GLU B 42  ? 0.8586 1.1283 1.1077 -0.0585 0.0202  -0.0441 42  GLU B OE1 
1221 O OE2 . GLU B 42  ? 0.8722 1.2225 1.1546 -0.0557 0.0176  -0.0658 42  GLU B OE2 
1222 N N   . MET B 43  ? 0.5976 0.8256 0.8345 -0.0054 -0.0053 0.0264  43  MET B N   
1223 C CA  . MET B 43  ? 0.5382 0.7280 0.7701 -0.0026 -0.0043 0.0383  43  MET B CA  
1224 C C   . MET B 43  ? 0.5326 0.7269 0.7595 0.0056  -0.0069 0.0506  43  MET B C   
1225 O O   . MET B 43  ? 0.5455 0.7508 0.7612 -0.0015 -0.0071 0.0452  43  MET B O   
1226 C CB  . MET B 43  ? 0.5135 0.6721 0.7306 -0.0182 0.0001  0.0291  43  MET B CB  
1227 C CG  . MET B 43  ? 0.5108 0.6334 0.7258 -0.0150 -0.0002 0.0376  43  MET B CG  
1228 S SD  . MET B 43  ? 0.5046 0.5913 0.7002 -0.0291 0.0030  0.0268  43  MET B SD  
1229 C CE  . MET B 43  ? 0.4970 0.5533 0.6969 -0.0206 -0.0007 0.0361  43  MET B CE  
1230 N N   . GLU B 44  ? 0.5501 0.7338 0.7846 0.0194  -0.0072 0.0664  44  GLU B N   
1231 C CA  . GLU B 44  ? 0.5731 0.7598 0.8017 0.0280  -0.0076 0.0798  44  GLU B CA  
1232 C C   . GLU B 44  ? 0.5868 0.7386 0.8202 0.0303  -0.0029 0.0896  44  GLU B C   
1233 O O   . GLU B 44  ? 0.6449 0.7855 0.8901 0.0400  -0.0008 0.0986  44  GLU B O   
1234 C CB  . GLU B 44  ? 0.5917 0.8061 0.8236 0.0449  -0.0114 0.0902  44  GLU B CB  
1235 C CG  . GLU B 44  ? 0.7414 0.9563 0.9625 0.0545  -0.0103 0.1057  44  GLU B CG  
1236 C CD  . GLU B 44  ? 0.9352 1.1731 1.1557 0.0746  -0.0146 0.1185  44  GLU B CD  
1237 O OE1 . GLU B 44  ? 0.9546 1.2187 1.1840 0.0799  -0.0206 0.1111  44  GLU B OE1 
1238 O OE2 . GLU B 44  ? 0.9791 1.2087 1.1896 0.0858  -0.0117 0.1358  44  GLU B OE2 
1239 N N   . LEU B 45  ? 0.5272 0.6630 0.7531 0.0216  -0.0009 0.0866  45  LEU B N   
1240 C CA  . LEU B 45  ? 0.5549 0.6609 0.7885 0.0212  0.0029  0.0902  45  LEU B CA  
1241 C C   . LEU B 45  ? 0.5697 0.6713 0.8063 0.0299  0.0083  0.1052  45  LEU B C   
1242 O O   . LEU B 45  ? 0.5883 0.7064 0.8143 0.0338  0.0090  0.1120  45  LEU B O   
1243 C CB  . LEU B 45  ? 0.5550 0.6459 0.7809 0.0097  0.0022  0.0792  45  LEU B CB  
1244 C CG  . LEU B 45  ? 0.4249 0.5132 0.6421 0.0000  -0.0008 0.0654  45  LEU B CG  
1245 C CD1 . LEU B 45  ? 0.3947 0.4663 0.6006 -0.0084 -0.0011 0.0571  45  LEU B CD1 
1246 C CD2 . LEU B 45  ? 0.4790 0.5526 0.7051 0.0015  -0.0014 0.0636  45  LEU B CD2 
1247 N N   . ASN B 46  ? 0.5632 0.6417 0.8138 0.0320  0.0132  0.1092  46  ASN B N   
1248 C CA  . ASN B 46  ? 0.5973 0.6653 0.8529 0.0384  0.0219  0.1227  46  ASN B CA  
1249 C C   . ASN B 46  ? 0.6030 0.6597 0.8604 0.0302  0.0259  0.1176  46  ASN B C   
1250 O O   . ASN B 46  ? 0.6075 0.6542 0.8712 0.0227  0.0224  0.1048  46  ASN B O   
1251 C CB  . ASN B 46  ? 0.6767 0.7261 0.9498 0.0442  0.0270  0.1277  46  ASN B CB  
1252 C CG  . ASN B 46  ? 0.7428 0.7764 1.0212 0.0495  0.0392  0.1416  46  ASN B CG  
1253 O OD1 . ASN B 46  ? 0.7839 0.8245 1.0484 0.0540  0.0433  0.1530  46  ASN B OD1 
1254 N ND2 . ASN B 46  ? 0.8240 0.8356 1.1215 0.0482  0.0463  0.1400  46  ASN B ND2 
1255 N N   . GLU B 47  ? 0.5802 0.6394 0.8309 0.0327  0.0334  0.1277  47  GLU B N   
1256 C CA  . GLU B 47  ? 0.5197 0.5714 0.7739 0.0255  0.0392  0.1228  47  GLU B CA  
1257 C C   . GLU B 47  ? 0.5915 0.6234 0.8686 0.0209  0.0420  0.1142  47  GLU B C   
1258 O O   . GLU B 47  ? 0.5971 0.6264 0.8794 0.0144  0.0369  0.1001  47  GLU B O   
1259 C CB  . GLU B 47  ? 0.5837 0.6363 0.8289 0.0302  0.0505  0.1379  47  GLU B CB  
1260 C CG  . GLU B 47  ? 0.6830 0.7434 0.9187 0.0239  0.0545  0.1339  47  GLU B CG  
1261 C CD  . GLU B 47  ? 0.7185 0.7769 0.9421 0.0287  0.0678  0.1503  47  GLU B CD  
1262 O OE1 . GLU B 47  ? 0.7031 0.7573 0.9190 0.0393  0.0711  0.1666  47  GLU B OE1 
1263 O OE2 . GLU B 47  ? 0.7525 0.8124 0.9725 0.0227  0.0755  0.1473  47  GLU B OE2 
1264 N N   . ALA B 48  ? 0.6066 0.6243 0.8974 0.0250  0.0497  0.1215  48  ALA B N   
1265 C CA  . ALA B 48  ? 0.5659 0.5675 0.8809 0.0199  0.0536  0.1115  48  ALA B CA  
1266 C C   . ALA B 48  ? 0.5702 0.5716 0.8903 0.0166  0.0407  0.0956  48  ALA B C   
1267 O O   . ALA B 48  ? 0.5754 0.5705 0.9112 0.0118  0.0392  0.0824  48  ALA B O   
1268 C CB  . ALA B 48  ? 0.5930 0.5784 0.9207 0.0246  0.0647  0.1215  48  ALA B CB  
1269 N N   . THR B 49  ? 0.5350 0.5437 0.8415 0.0193  0.0317  0.0960  49  THR B N   
1270 C CA  . THR B 49  ? 0.4649 0.4706 0.7702 0.0158  0.0211  0.0822  49  THR B CA  
1271 C C   . THR B 49  ? 0.5189 0.5262 0.8155 0.0108  0.0146  0.0717  49  THR B C   
1272 O O   . THR B 49  ? 0.4952 0.4938 0.7987 0.0089  0.0090  0.0597  49  THR B O   
1273 C CB  . THR B 49  ? 0.5723 0.5865 0.8646 0.0184  0.0159  0.0847  49  THR B CB  
1274 O OG1 . THR B 49  ? 0.7383 0.7537 1.0374 0.0261  0.0224  0.0970  49  THR B OG1 
1275 C CG2 . THR B 49  ? 0.5573 0.5628 0.8494 0.0151  0.0086  0.0724  49  THR B CG2 
1276 N N   . LEU B 50  ? 0.5035 0.5222 0.7840 0.0097  0.0146  0.0753  50  LEU B N   
1277 C CA  . LEU B 50  ? 0.4486 0.4667 0.7206 0.0056  0.0100  0.0657  50  LEU B CA  
1278 C C   . LEU B 50  ? 0.4508 0.4629 0.7413 0.0051  0.0126  0.0589  50  LEU B C   
1279 O O   . LEU B 50  ? 0.4405 0.4457 0.7323 0.0048  0.0053  0.0471  50  LEU B O   
1280 C CB  . LEU B 50  ? 0.4769 0.5098 0.7324 0.0039  0.0125  0.0704  50  LEU B CB  
1281 C CG  . LEU B 50  ? 0.4845 0.5237 0.7196 0.0000  0.0069  0.0656  50  LEU B CG  
1282 C CD1 . LEU B 50  ? 0.4142 0.4578 0.6471 0.0017  0.0045  0.0688  50  LEU B CD1 
1283 C CD2 . LEU B 50  ? 0.4109 0.4676 0.6334 -0.0022 0.0104  0.0680  50  LEU B CD2 
1284 N N   . TYR B 51  ? 0.4390 0.4531 0.7440 0.0055  0.0236  0.0659  51  TYR B N   
1285 C CA  . TYR B 51  ? 0.4647 0.4763 0.7913 0.0033  0.0284  0.0573  51  TYR B CA  
1286 C C   . TYR B 51  ? 0.4767 0.4802 0.8211 0.0039  0.0214  0.0444  51  TYR B C   
1287 O O   . TYR B 51  ? 0.4555 0.4603 0.8112 0.0039  0.0162  0.0307  51  TYR B O   
1288 C CB  . TYR B 51  ? 0.4708 0.4824 0.8086 0.0019  0.0446  0.0675  51  TYR B CB  
1289 C CG  . TYR B 51  ? 0.5254 0.5463 0.8437 0.0021  0.0514  0.0791  51  TYR B CG  
1290 C CD1 . TYR B 51  ? 0.5268 0.5569 0.8364 -0.0005 0.0490  0.0720  51  TYR B CD1 
1291 C CD2 . TYR B 51  ? 0.4875 0.5075 0.7957 0.0059  0.0605  0.0967  51  TYR B CD2 
1292 C CE1 . TYR B 51  ? 0.5555 0.5959 0.8465 -0.0009 0.0552  0.0808  51  TYR B CE1 
1293 C CE2 . TYR B 51  ? 0.5031 0.5335 0.7910 0.0072  0.0656  0.1068  51  TYR B CE2 
1294 C CZ  . TYR B 51  ? 0.6094 0.6510 0.8888 0.0030  0.0630  0.0982  51  TYR B CZ  
1295 O OH  . TYR B 51  ? 0.6848 0.7385 0.9430 0.0037  0.0682  0.1067  51  TYR B OH  
1296 N N   . THR B 52  ? 0.4963 0.4931 0.8439 0.0053  0.0207  0.0475  52  THR B N   
1297 C CA  . THR B 52  ? 0.4019 0.3929 0.7645 0.0057  0.0136  0.0339  52  THR B CA  
1298 C C   . THR B 52  ? 0.4646 0.4535 0.8115 0.0083  -0.0017 0.0234  52  THR B C   
1299 O O   . THR B 52  ? 0.4906 0.4798 0.8494 0.0102  -0.0090 0.0093  52  THR B O   
1300 C CB  . THR B 52  ? 0.4588 0.4426 0.8237 0.0067  0.0156  0.0386  52  THR B CB  
1301 O OG1 . THR B 52  ? 0.5523 0.5332 0.9299 0.0060  0.0307  0.0497  52  THR B OG1 
1302 C CG2 . THR B 52  ? 0.5452 0.5245 0.9250 0.0065  0.0085  0.0227  52  THR B CG2 
1303 N N   . ILE B 53  ? 0.4585 0.4453 0.7781 0.0088  -0.0061 0.0297  53  ILE B N   
1304 C CA  . ILE B 53  ? 0.4133 0.3915 0.7131 0.0110  -0.0183 0.0218  53  ILE B CA  
1305 C C   . ILE B 53  ? 0.4352 0.4145 0.7339 0.0131  -0.0219 0.0149  53  ILE B C   
1306 O O   . ILE B 53  ? 0.4493 0.4201 0.7416 0.0183  -0.0326 0.0050  53  ILE B O   
1307 C CB  . ILE B 53  ? 0.4316 0.4066 0.7047 0.0085  -0.0187 0.0291  53  ILE B CB  
1308 C CG1 . ILE B 53  ? 0.4405 0.4172 0.7189 0.0077  -0.0147 0.0348  53  ILE B CG1 
1309 C CG2 . ILE B 53  ? 0.4307 0.3905 0.6800 0.0097  -0.0283 0.0220  53  ILE B CG2 
1310 C CD1 . ILE B 53  ? 0.3634 0.3387 0.6199 0.0051  -0.0160 0.0374  53  ILE B CD1 
1311 N N   . PHE B 54  ? 0.4679 0.4573 0.7722 0.0105  -0.0131 0.0196  54  PHE B N   
1312 C CA  . PHE B 54  ? 0.4026 0.3941 0.7070 0.0124  -0.0149 0.0124  54  PHE B CA  
1313 C C   . PHE B 54  ? 0.4015 0.3988 0.7345 0.0160  -0.0173 -0.0006 54  PHE B C   
1314 O O   . PHE B 54  ? 0.3961 0.3920 0.7294 0.0218  -0.0252 -0.0111 54  PHE B O   
1315 C CB  . PHE B 54  ? 0.4025 0.4049 0.7027 0.0076  -0.0037 0.0209  54  PHE B CB  
1316 C CG  . PHE B 54  ? 0.4124 0.4128 0.6839 0.0047  -0.0044 0.0268  54  PHE B CG  
1317 C CD1 . PHE B 54  ? 0.4023 0.3894 0.6543 0.0053  -0.0126 0.0246  54  PHE B CD1 
1318 C CD2 . PHE B 54  ? 0.4683 0.4811 0.7322 0.0007  0.0041  0.0337  54  PHE B CD2 
1319 C CE1 . PHE B 54  ? 0.3858 0.3722 0.6145 0.0005  -0.0112 0.0275  54  PHE B CE1 
1320 C CE2 . PHE B 54  ? 0.4229 0.4380 0.6635 -0.0030 0.0034  0.0360  54  PHE B CE2 
1321 C CZ  . PHE B 54  ? 0.4074 0.4095 0.6322 -0.0039 -0.0036 0.0322  54  PHE B CZ  
1322 N N   . LYS B 55  ? 0.4962 0.4999 0.8542 0.0131  -0.0103 -0.0013 55  LYS B N   
1323 C CA  . LYS B 55  ? 0.5205 0.5330 0.9097 0.0149  -0.0122 -0.0171 55  LYS B CA  
1324 C C   . LYS B 55  ? 0.5734 0.5809 0.9584 0.0235  -0.0302 -0.0299 55  LYS B C   
1325 O O   . LYS B 55  ? 0.5428 0.5577 0.9406 0.0301  -0.0385 -0.0442 55  LYS B O   
1326 C CB  . LYS B 55  ? 0.5213 0.5373 0.9357 0.0083  0.0002  -0.0157 55  LYS B CB  
1327 C CG  . LYS B 55  ? 0.5664 0.5949 1.0183 0.0067  0.0024  -0.0339 55  LYS B CG  
1328 C CD  . LYS B 55  ? 0.5615 0.5893 1.0360 -0.0026 0.0212  -0.0298 55  LYS B CD  
1329 C CE  . LYS B 55  ? 0.5534 0.5953 1.0689 -0.0072 0.0264  -0.0506 55  LYS B CE  
1330 N NZ  . LYS B 55  ? 0.6349 0.6828 1.1629 -0.0022 0.0100  -0.0690 55  LYS B NZ  
1331 N N   . ARG B 56  ? 0.4864 0.4821 0.8533 0.0246  -0.0364 -0.0254 56  ARG B N   
1332 C CA  . ARG B 56  ? 0.4512 0.4394 0.8070 0.0333  -0.0531 -0.0357 56  ARG B CA  
1333 C C   . ARG B 56  ? 0.5298 0.5066 0.8587 0.0414  -0.0630 -0.0359 56  ARG B C   
1334 O O   . ARG B 56  ? 0.5414 0.5183 0.8719 0.0522  -0.0761 -0.0480 56  ARG B O   
1335 C CB  . ARG B 56  ? 0.4725 0.4491 0.8111 0.0310  -0.0547 -0.0296 56  ARG B CB  
1336 C CG  . ARG B 56  ? 0.5557 0.5222 0.8764 0.0396  -0.0707 -0.0385 56  ARG B CG  
1337 C CD  . ARG B 56  ? 0.7398 0.7024 1.0585 0.0364  -0.0706 -0.0390 56  ARG B CD  
1338 N NE  . ARG B 56  ? 0.9574 0.9143 1.2632 0.0454  -0.0866 -0.0507 56  ARG B NE  
1339 C CZ  . ARG B 56  ? 1.0020 0.9389 1.2688 0.0497  -0.0940 -0.0463 56  ARG B CZ  
1340 N NH1 . ARG B 56  ? 0.9481 0.8703 1.1882 0.0442  -0.0863 -0.0324 56  ARG B NH1 
1341 N NH2 . ARG B 56  ? 0.9559 0.8879 1.2093 0.0596  -0.1089 -0.0569 56  ARG B NH2 
1342 N N   . LEU B 57  ? 0.4779 0.4443 0.7815 0.0372  -0.0568 -0.0234 57  LEU B N   
1343 C CA  . LEU B 57  ? 0.4990 0.4498 0.7754 0.0434  -0.0634 -0.0234 57  LEU B CA  
1344 C C   . LEU B 57  ? 0.5261 0.4866 0.8201 0.0499  -0.0654 -0.0331 57  LEU B C   
1345 O O   . LEU B 57  ? 0.5349 0.4841 0.8168 0.0615  -0.0767 -0.0398 57  LEU B O   
1346 C CB  . LEU B 57  ? 0.4490 0.3915 0.7008 0.0347  -0.0538 -0.0110 57  LEU B CB  
1347 C CG  . LEU B 57  ? 0.4519 0.3842 0.6833 0.0292  -0.0525 -0.0033 57  LEU B CG  
1348 C CD1 . LEU B 57  ? 0.4570 0.3945 0.6786 0.0193  -0.0412 0.0066  57  LEU B CD1 
1349 C CD2 . LEU B 57  ? 0.5130 0.4197 0.7122 0.0351  -0.0618 -0.0055 57  LEU B CD2 
1350 N N   . GLU B 58  ? 0.4564 0.4367 0.7783 0.0434  -0.0540 -0.0341 58  GLU B N   
1351 C CA  . GLU B 58  ? 0.4493 0.4415 0.7913 0.0486  -0.0543 -0.0453 58  GLU B CA  
1352 C C   . GLU B 58  ? 0.5432 0.5476 0.9117 0.0585  -0.0661 -0.0624 58  GLU B C   
1353 O O   . GLU B 58  ? 0.4903 0.4995 0.8673 0.0692  -0.0740 -0.0741 58  GLU B O   
1354 C CB  . GLU B 58  ? 0.4680 0.4773 0.8303 0.0378  -0.0369 -0.0418 58  GLU B CB  
1355 C CG  . GLU B 58  ? 0.5933 0.6105 0.9645 0.0409  -0.0339 -0.0500 58  GLU B CG  
1356 C CD  . GLU B 58  ? 0.7197 0.7514 1.1039 0.0296  -0.0153 -0.0451 58  GLU B CD  
1357 O OE1 . GLU B 58  ? 0.7253 0.7556 1.1004 0.0208  -0.0060 -0.0312 58  GLU B OE1 
1358 O OE2 . GLU B 58  ? 0.7454 0.7891 1.1465 0.0304  -0.0101 -0.0549 58  GLU B OE2 
1359 N N   . LYS B 59  ? 0.5810 0.5922 0.9645 0.0555  -0.0676 -0.0657 59  LYS B N   
1360 C CA  . LYS B 59  ? 0.5702 0.5963 0.9791 0.0645  -0.0801 -0.0847 59  LYS B CA  
1361 C C   . LYS B 59  ? 0.6197 0.6308 1.0014 0.0815  -0.1008 -0.0890 59  LYS B C   
1362 O O   . LYS B 59  ? 0.6054 0.6292 1.0031 0.0949  -0.1141 -0.1052 59  LYS B O   
1363 C CB  . LYS B 59  ? 0.5759 0.6099 1.0037 0.0564  -0.0764 -0.0878 59  LYS B CB  
1364 C CG  . LYS B 59  ? 0.6852 0.7455 1.1554 0.0593  -0.0815 -0.1111 59  LYS B CG  
1365 C CD  . LYS B 59  ? 0.8660 0.9297 1.3448 0.0574  -0.0870 -0.1191 59  LYS B CD  
1366 C CE  . LYS B 59  ? 0.9272 1.0189 1.4423 0.0647  -0.0990 -0.1466 59  LYS B CE  
1367 N NZ  . LYS B 59  ? 1.0499 1.1461 1.5698 0.0649  -0.1079 -0.1576 59  LYS B NZ  
1368 N N   . ASP B 60  ? 0.7542 0.7383 1.0943 0.0819  -0.1034 -0.0749 60  ASP B N   
1369 C CA  . ASP B 60  ? 0.7762 0.7387 1.0823 0.0973  -0.1204 -0.0756 60  ASP B CA  
1370 C C   . ASP B 60  ? 0.7134 0.6574 0.9968 0.1058  -0.1218 -0.0714 60  ASP B C   
1371 O O   . ASP B 60  ? 0.7703 0.6873 1.0171 0.1175  -0.1323 -0.0676 60  ASP B O   
1372 C CB  . ASP B 60  ? 0.7408 0.6806 1.0117 0.0920  -0.1199 -0.0635 60  ASP B CB  
1373 C CG  . ASP B 60  ? 0.7914 0.7465 1.0836 0.0824  -0.1159 -0.0666 60  ASP B CG  
1374 O OD1 . ASP B 60  ? 0.7952 0.7762 1.1274 0.0815  -0.1159 -0.0800 60  ASP B OD1 
1375 O OD2 . ASP B 60  ? 0.8154 0.7563 1.0856 0.0751  -0.1113 -0.0567 60  ASP B OD2 
1376 N N   . GLY B 61  ? 0.5675 0.5232 0.8698 0.1000  -0.1104 -0.0720 61  GLY B N   
1377 C CA  . GLY B 61  ? 0.5749 0.5143 0.8595 0.1074  -0.1104 -0.0703 61  GLY B CA  
1378 C C   . GLY B 61  ? 0.6440 0.5510 0.8852 0.1009  -0.1032 -0.0549 61  GLY B C   
1379 O O   . GLY B 61  ? 0.7626 0.6464 0.9804 0.1099  -0.1059 -0.0540 61  GLY B O   
1380 N N   . ILE B 62  ? 0.6279 0.5328 0.8589 0.0856  -0.0934 -0.0439 62  ILE B N   
1381 C CA  . ILE B 62  ? 0.6448 0.5224 0.8371 0.0779  -0.0861 -0.0320 62  ILE B CA  
1382 C C   . ILE B 62  ? 0.6598 0.5439 0.8548 0.0658  -0.0709 -0.0281 62  ILE B C   
1383 O O   . ILE B 62  ? 0.6391 0.5005 0.8060 0.0630  -0.0659 -0.0242 62  ILE B O   
1384 C CB  . ILE B 62  ? 0.6366 0.5104 0.8161 0.0686  -0.0839 -0.0241 62  ILE B CB  
1385 C CG1 . ILE B 62  ? 0.6502 0.5134 0.8187 0.0807  -0.0989 -0.0284 62  ILE B CG1 
1386 C CG2 . ILE B 62  ? 0.5799 0.4315 0.7252 0.0581  -0.0741 -0.0143 62  ILE B CG2 
1387 C CD1 . ILE B 62  ? 0.7366 0.5648 0.8661 0.0940  -0.1077 -0.0272 62  ILE B CD1 
1388 N N   . ILE B 63  ? 0.6370 0.5506 0.8639 0.0580  -0.0626 -0.0296 63  ILE B N   
1389 C CA  . ILE B 63  ? 0.5677 0.4918 0.7975 0.0472  -0.0488 -0.0265 63  ILE B CA  
1390 C C   . ILE B 63  ? 0.5361 0.4849 0.8009 0.0494  -0.0453 -0.0354 63  ILE B C   
1391 O O   . ILE B 63  ? 0.5550 0.5168 0.8458 0.0559  -0.0517 -0.0433 63  ILE B O   
1392 C CB  . ILE B 63  ? 0.4724 0.4069 0.6981 0.0328  -0.0385 -0.0153 63  ILE B CB  
1393 C CG1 . ILE B 63  ? 0.4478 0.4016 0.7003 0.0310  -0.0377 -0.0137 63  ILE B CG1 
1394 C CG2 . ILE B 63  ? 0.4774 0.3904 0.6707 0.0287  -0.0397 -0.0089 63  ILE B CG2 
1395 C CD1 . ILE B 63  ? 0.4286 0.3947 0.6806 0.0198  -0.0270 -0.0023 63  ILE B CD1 
1396 N N   . SER B 64  ? 0.4751 0.4314 0.7409 0.0431  -0.0344 -0.0357 64  SER B N   
1397 C CA  . SER B 64  ? 0.5000 0.4802 0.7970 0.0422  -0.0272 -0.0436 64  SER B CA  
1398 C C   . SER B 64  ? 0.5051 0.4975 0.7969 0.0289  -0.0116 -0.0365 64  SER B C   
1399 O O   . SER B 64  ? 0.5205 0.5037 0.7859 0.0221  -0.0084 -0.0288 64  SER B O   
1400 C CB  . SER B 64  ? 0.5279 0.5046 0.8339 0.0547  -0.0330 -0.0576 64  SER B CB  
1401 O OG  . SER B 64  ? 0.4953 0.4642 0.7852 0.0511  -0.0248 -0.0583 64  SER B OG  
1402 N N   . SER B 65  ? 0.4498 0.4638 0.7667 0.0250  -0.0015 -0.0405 65  SER B N   
1403 C CA  . SER B 65  ? 0.4172 0.4448 0.7284 0.0134  0.0133  -0.0326 65  SER B CA  
1404 C C   . SER B 65  ? 0.4508 0.4908 0.7744 0.0122  0.0229  -0.0430 65  SER B C   
1405 O O   . SER B 65  ? 0.4972 0.5407 0.8433 0.0200  0.0195  -0.0568 65  SER B O   
1406 C CB  . SER B 65  ? 0.5418 0.5813 0.8661 0.0075  0.0206  -0.0227 65  SER B CB  
1407 O OG  . SER B 65  ? 0.5192 0.5681 0.8768 0.0103  0.0218  -0.0321 65  SER B OG  
1408 N N   . TYR B 66  ? 0.4372 0.4858 0.7458 0.0030  0.0345  -0.0374 66  TYR B N   
1409 C CA  . TYR B 66  ? 0.4376 0.4990 0.7541 0.0000  0.0459  -0.0468 66  TYR B CA  
1410 C C   . TYR B 66  ? 0.4649 0.5397 0.7640 -0.0109 0.0590  -0.0362 66  TYR B C   
1411 O O   . TYR B 66  ? 0.4591 0.5327 0.7385 -0.0144 0.0572  -0.0229 66  TYR B O   
1412 C CB  . TYR B 66  ? 0.5530 0.6015 0.8606 0.0057  0.0407  -0.0592 66  TYR B CB  
1413 C CG  . TYR B 66  ? 0.5090 0.5443 0.7829 0.0007  0.0390  -0.0537 66  TYR B CG  
1414 C CD1 . TYR B 66  ? 0.5371 0.5838 0.7951 -0.0093 0.0498  -0.0535 66  TYR B CD1 
1415 C CD2 . TYR B 66  ? 0.4716 0.4841 0.7296 0.0052  0.0273  -0.0501 66  TYR B CD2 
1416 C CE1 . TYR B 66  ? 0.5028 0.5414 0.7337 -0.0153 0.0488  -0.0516 66  TYR B CE1 
1417 C CE2 . TYR B 66  ? 0.4586 0.4599 0.6883 -0.0015 0.0281  -0.0472 66  TYR B CE2 
1418 C CZ  . TYR B 66  ? 0.4847 0.5005 0.7028 -0.0121 0.0387  -0.0488 66  TYR B CZ  
1419 O OH  . TYR B 66  ? 0.5622 0.5708 0.7555 -0.0202 0.0400  -0.0489 66  TYR B OH  
1420 N N   . TRP B 67  ? 0.5306 0.6195 0.8365 -0.0153 0.0720  -0.0431 67  TRP B N   
1421 C CA  . TRP B 67  ? 0.5768 0.6802 0.8654 -0.0243 0.0855  -0.0341 67  TRP B CA  
1422 C C   . TRP B 67  ? 0.6399 0.7450 0.9026 -0.0282 0.0855  -0.0388 67  TRP B C   
1423 O O   . TRP B 67  ? 0.6264 0.7229 0.8914 -0.0253 0.0819  -0.0531 67  TRP B O   
1424 C CB  . TRP B 67  ? 0.6289 0.7466 0.9359 -0.0285 0.1021  -0.0399 67  TRP B CB  
1425 C CG  . TRP B 67  ? 0.6690 0.7877 0.9975 -0.0292 0.1080  -0.0336 67  TRP B CG  
1426 C CD1 . TRP B 67  ? 0.6811 0.8013 1.0452 -0.0261 0.1079  -0.0458 67  TRP B CD1 
1427 C CD2 . TRP B 67  ? 0.7293 0.8470 1.0460 -0.0328 0.1147  -0.0142 67  TRP B CD2 
1428 N NE1 . TRP B 67  ? 0.6727 0.7926 1.0488 -0.0300 0.1161  -0.0364 67  TRP B NE1 
1429 C CE2 . TRP B 67  ? 0.7336 0.8494 1.0799 -0.0336 0.1207  -0.0158 67  TRP B CE2 
1430 C CE3 . TRP B 67  ? 0.6999 0.8189 0.9845 -0.0347 0.1160  0.0036  67  TRP B CE3 
1431 C CZ2 . TRP B 67  ? 0.7426 0.8528 1.0860 -0.0367 0.1297  0.0007  67  TRP B CZ2 
1432 C CZ3 . TRP B 67  ? 0.7257 0.8404 1.0065 -0.0353 0.1232  0.0209  67  TRP B CZ3 
1433 C CH2 . TRP B 67  ? 0.7553 0.8633 1.0647 -0.0366 0.1309  0.0200  67  TRP B CH2 
1434 N N   . GLY B 68  ? 0.6649 0.7811 0.9029 -0.0341 0.0897  -0.0275 68  GLY B N   
1435 C CA  . GLY B 68  ? 0.8089 0.9329 1.0232 -0.0398 0.0913  -0.0338 68  GLY B CA  
1436 C C   . GLY B 68  ? 1.0134 1.1580 1.2179 -0.0458 0.1060  -0.0333 68  GLY B C   
1437 O O   . GLY B 68  ? 1.0846 1.2361 1.2913 -0.0459 0.1143  -0.0213 68  GLY B O   
1438 N N   . ASP B 69  ? 1.0973 1.2499 1.2898 -0.0511 0.1106  -0.0469 69  ASP B N   
1439 C CA  . ASP B 69  ? 1.1437 1.3169 1.3227 -0.0574 0.1247  -0.0493 69  ASP B CA  
1440 C C   . ASP B 69  ? 1.2329 1.4084 1.4322 -0.0573 0.1386  -0.0513 69  ASP B C   
1441 O O   . ASP B 69  ? 1.4237 1.6142 1.6098 -0.0622 0.1524  -0.0478 69  ASP B O   
1442 C CB  . ASP B 69  ? 1.1771 1.3674 1.3277 -0.0590 0.1249  -0.0324 69  ASP B CB  
1443 C CG  . ASP B 69  ? 1.2473 1.4472 1.3763 -0.0625 0.1157  -0.0373 69  ASP B CG  
1444 O OD1 . ASP B 69  ? 1.2218 1.4071 1.3571 -0.0614 0.1046  -0.0412 69  ASP B OD1 
1445 O OD2 . ASP B 69  ? 1.1807 1.4033 1.2857 -0.0668 0.1200  -0.0380 69  ASP B OD2 
1446 N N   . GLU B 70  ? 1.0848 1.2471 1.3155 -0.0519 0.1359  -0.0580 70  GLU B N   
1447 C CA  . GLU B 70  ? 1.0853 1.2529 1.3400 -0.0531 0.1498  -0.0618 70  GLU B CA  
1448 C C   . GLU B 70  ? 1.0694 1.2472 1.3312 -0.0569 0.1617  -0.0819 70  GLU B C   
1449 O O   . GLU B 70  ? 1.0512 1.2424 1.3094 -0.0636 0.1792  -0.0821 70  GLU B O   
1450 C CB  . GLU B 70  ? 0.9662 1.1218 1.2553 -0.0457 0.1419  -0.0650 70  GLU B CB  
1451 C CG  . GLU B 70  ? 1.0378 1.2018 1.3559 -0.0485 0.1571  -0.0707 70  GLU B CG  
1452 C CD  . GLU B 70  ? 1.0539 1.2117 1.4099 -0.0409 0.1480  -0.0801 70  GLU B CD  
1453 O OE1 . GLU B 70  ? 0.9682 1.1131 1.3251 -0.0320 0.1294  -0.0821 70  GLU B OE1 
1454 O OE2 . GLU B 70  ? 1.1480 1.3144 1.5322 -0.0441 0.1600  -0.0862 70  GLU B OE2 
1455 N N   . ARG B 75  ? 0.9585 1.1125 1.1610 -0.0447 0.1364  0.0191  75  ARG B N   
1456 C CA  . ARG B 75  ? 1.0348 1.1850 1.2223 -0.0406 0.1365  0.0414  75  ARG B CA  
1457 C C   . ARG B 75  ? 0.9710 1.1101 1.1673 -0.0347 0.1201  0.0462  75  ARG B C   
1458 O O   . ARG B 75  ? 0.8685 0.9952 1.0777 -0.0317 0.1218  0.0565  75  ARG B O   
1459 C CB  . ARG B 75  ? 1.0964 1.2630 1.2456 -0.0397 0.1371  0.0517  75  ARG B CB  
1460 C CG  . ARG B 75  ? 1.2520 1.4311 1.3866 -0.0456 0.1525  0.0463  75  ARG B CG  
1461 C CD  . ARG B 75  ? 1.3776 1.5734 1.4716 -0.0426 0.1526  0.0592  75  ARG B CD  
1462 N NE  . ARG B 75  ? 1.5640 1.7661 1.6408 -0.0472 0.1717  0.0608  75  ARG B NE  
1463 C CZ  . ARG B 75  ? 1.4853 1.7037 1.5525 -0.0539 0.1768  0.0446  75  ARG B CZ  
1464 N NH1 . ARG B 75  ? 1.4704 1.6991 1.5434 -0.0569 0.1650  0.0255  75  ARG B NH1 
1465 N NH2 . ARG B 75  ? 1.5086 1.7311 1.5596 -0.0584 0.1960  0.0471  75  ARG B NH2 
1466 N N   . ARG B 76  ? 0.8515 0.9938 1.0416 -0.0341 0.1058  0.0372  76  ARG B N   
1467 C CA  . ARG B 76  ? 0.6831 0.8164 0.8761 -0.0295 0.0913  0.0415  76  ARG B CA  
1468 C C   . ARG B 76  ? 0.6695 0.7872 0.8879 -0.0286 0.0842  0.0279  76  ARG B C   
1469 O O   . ARG B 76  ? 0.8057 0.9226 1.0338 -0.0307 0.0863  0.0126  76  ARG B O   
1470 C CB  . ARG B 76  ? 0.6078 0.7537 0.7773 -0.0304 0.0815  0.0398  76  ARG B CB  
1471 C CG  . ARG B 76  ? 0.6458 0.7903 0.8106 -0.0254 0.0712  0.0511  76  ARG B CG  
1472 C CD  . ARG B 76  ? 0.6882 0.8540 0.8294 -0.0263 0.0647  0.0510  76  ARG B CD  
1473 N NE  . ARG B 76  ? 0.7833 0.9687 0.9037 -0.0233 0.0710  0.0618  76  ARG B NE  
1474 C CZ  . ARG B 76  ? 0.8486 1.0418 0.9574 -0.0147 0.0687  0.0791  76  ARG B CZ  
1475 N NH1 . ARG B 76  ? 0.8212 1.0058 0.9397 -0.0091 0.0610  0.0867  76  ARG B NH1 
1476 N NH2 . ARG B 76  ? 0.9604 1.1696 1.0462 -0.0106 0.0745  0.0891  76  ARG B NH2 
1477 N N   . LYS B 77  ? 0.5805 0.6860 0.8090 -0.0243 0.0755  0.0332  77  LYS B N   
1478 C CA  . LYS B 77  ? 0.4759 0.5669 0.7259 -0.0214 0.0674  0.0219  77  LYS B CA  
1479 C C   . LYS B 77  ? 0.5196 0.6015 0.7570 -0.0198 0.0536  0.0186  77  LYS B C   
1480 O O   . LYS B 77  ? 0.5142 0.5964 0.7405 -0.0191 0.0487  0.0286  77  LYS B O   
1481 C CB  . LYS B 77  ? 0.3817 0.4650 0.6537 -0.0187 0.0693  0.0278  77  LYS B CB  
1482 C CG  . LYS B 77  ? 0.4759 0.5498 0.7733 -0.0150 0.0619  0.0140  77  LYS B CG  
1483 C CD  . LYS B 77  ? 0.5278 0.5978 0.8484 -0.0144 0.0657  0.0176  77  LYS B CD  
1484 C CE  . LYS B 77  ? 0.6772 0.7425 1.0241 -0.0097 0.0564  0.0018  77  LYS B CE  
1485 N NZ  . LYS B 77  ? 0.7184 0.7826 1.0913 -0.0109 0.0611  0.0018  77  LYS B NZ  
1486 N N   . TYR B 78  ? 0.4585 0.5308 0.6975 -0.0190 0.0485  0.0046  78  TYR B N   
1487 C CA  . TYR B 78  ? 0.4846 0.5430 0.7093 -0.0186 0.0383  0.0007  78  TYR B CA  
1488 C C   . TYR B 78  ? 0.4583 0.4972 0.6958 -0.0111 0.0283  -0.0030 78  TYR B C   
1489 O O   . TYR B 78  ? 0.4750 0.5141 0.7353 -0.0063 0.0283  -0.0069 78  TYR B O   
1490 C CB  . TYR B 78  ? 0.4839 0.5395 0.6959 -0.0223 0.0406  -0.0119 78  TYR B CB  
1491 C CG  . TYR B 78  ? 0.4798 0.5547 0.6728 -0.0306 0.0472  -0.0105 78  TYR B CG  
1492 C CD1 . TYR B 78  ? 0.5179 0.6132 0.7115 -0.0331 0.0572  -0.0080 78  TYR B CD1 
1493 C CD2 . TYR B 78  ? 0.5160 0.5897 0.6898 -0.0362 0.0439  -0.0130 78  TYR B CD2 
1494 C CE1 . TYR B 78  ? 0.5641 0.6796 0.7378 -0.0395 0.0617  -0.0077 78  TYR B CE1 
1495 C CE2 . TYR B 78  ? 0.5560 0.6521 0.7141 -0.0437 0.0486  -0.0146 78  TYR B CE2 
1496 C CZ  . TYR B 78  ? 0.6118 0.7294 0.7691 -0.0445 0.0564  -0.0118 78  TYR B CZ  
1497 O OH  . TYR B 78  ? 0.5813 0.7232 0.7208 -0.0507 0.0594  -0.0142 78  TYR B OH  
1498 N N   . TYR B 79  ? 0.4265 0.4500 0.6484 -0.0108 0.0200  -0.0024 79  TYR B N   
1499 C CA  . TYR B 79  ? 0.4294 0.4326 0.6552 -0.0033 0.0095  -0.0051 79  TYR B CA  
1500 C C   . TYR B 79  ? 0.4806 0.4607 0.6845 -0.0028 0.0050  -0.0119 79  TYR B C   
1501 O O   . TYR B 79  ? 0.4919 0.4720 0.6766 -0.0111 0.0097  -0.0120 79  TYR B O   
1502 C CB  . TYR B 79  ? 0.4060 0.4093 0.6324 -0.0034 0.0055  0.0049  79  TYR B CB  
1503 C CG  . TYR B 79  ? 0.4763 0.4938 0.7257 -0.0022 0.0100  0.0109  79  TYR B CG  
1504 C CD1 . TYR B 79  ? 0.5167 0.5515 0.7657 -0.0069 0.0198  0.0203  79  TYR B CD1 
1505 C CD2 . TYR B 79  ? 0.5046 0.5172 0.7752 0.0038  0.0050  0.0066  79  TYR B CD2 
1506 C CE1 . TYR B 79  ? 0.4648 0.5068 0.7322 -0.0062 0.0265  0.0267  79  TYR B CE1 
1507 C CE2 . TYR B 79  ? 0.4472 0.4704 0.7400 0.0029  0.0116  0.0104  79  TYR B CE2 
1508 C CZ  . TYR B 79  ? 0.4523 0.4877 0.7427 -0.0024 0.0234  0.0212  79  TYR B CZ  
1509 O OH  . TYR B 79  ? 0.5459 0.5864 0.8557 -0.0037 0.0326  0.0263  79  TYR B OH  
1510 N N   . ARG B 80  ? 0.4835 0.4434 0.6898 0.0073  -0.0036 -0.0180 80  ARG B N   
1511 C CA  . ARG B 80  ? 0.5315 0.4626 0.7152 0.0103  -0.0068 -0.0235 80  ARG B CA  
1512 C C   . ARG B 80  ? 0.4812 0.3888 0.6582 0.0212  -0.0189 -0.0228 80  ARG B C   
1513 O O   . ARG B 80  ? 0.5005 0.4156 0.6978 0.0303  -0.0267 -0.0245 80  ARG B O   
1514 C CB  . ARG B 80  ? 0.4919 0.4195 0.6810 0.0149  -0.0036 -0.0344 80  ARG B CB  
1515 C CG  . ARG B 80  ? 0.5105 0.4487 0.7287 0.0267  -0.0088 -0.0410 80  ARG B CG  
1516 C CD  . ARG B 80  ? 0.5886 0.5219 0.8118 0.0327  -0.0059 -0.0532 80  ARG B CD  
1517 N NE  . ARG B 80  ? 0.6353 0.5326 0.8353 0.0420  -0.0121 -0.0564 80  ARG B NE  
1518 C CZ  . ARG B 80  ? 0.6244 0.5057 0.8277 0.0595  -0.0248 -0.0604 80  ARG B CZ  
1519 N NH1 . ARG B 80  ? 0.6212 0.5227 0.8535 0.0687  -0.0332 -0.0645 80  ARG B NH1 
1520 N NH2 . ARG B 80  ? 0.6414 0.4852 0.8177 0.0683  -0.0288 -0.0609 80  ARG B NH2 
1521 N N   . LEU B 81  ? 0.5386 0.4178 0.6861 0.0197  -0.0198 -0.0212 81  LEU B N   
1522 C CA  . LEU B 81  ? 0.5974 0.4503 0.7304 0.0302  -0.0306 -0.0195 81  LEU B CA  
1523 C C   . LEU B 81  ? 0.6731 0.5055 0.8038 0.0466  -0.0381 -0.0270 81  LEU B C   
1524 O O   . LEU B 81  ? 0.6578 0.4732 0.7755 0.0463  -0.0320 -0.0312 81  LEU B O   
1525 C CB  . LEU B 81  ? 0.5700 0.3990 0.6700 0.0209  -0.0257 -0.0145 81  LEU B CB  
1526 C CG  . LEU B 81  ? 0.7431 0.5449 0.8213 0.0279  -0.0340 -0.0104 81  LEU B CG  
1527 C CD1 . LEU B 81  ? 0.7803 0.6047 0.8800 0.0313  -0.0420 -0.0075 81  LEU B CD1 
1528 C CD2 . LEU B 81  ? 0.7008 0.4815 0.7481 0.0146  -0.0245 -0.0069 81  LEU B CD2 
1529 N N   . THR B 82  ? 0.6859 0.5212 0.8304 0.0615  -0.0514 -0.0298 82  THR B N   
1530 C CA  . THR B 82  ? 0.7493 0.5733 0.8981 0.0801  -0.0609 -0.0383 82  THR B CA  
1531 C C   . THR B 82  ? 0.8775 0.6552 0.9860 0.0909  -0.0660 -0.0352 82  THR B C   
1532 O O   . THR B 82  ? 0.9232 0.6766 1.0001 0.0821  -0.0607 -0.0270 82  THR B O   
1533 C CB  . THR B 82  ? 0.7192 0.5655 0.8976 0.0930  -0.0745 -0.0449 82  THR B CB  
1534 O OG1 . THR B 82  ? 0.7890 0.6217 0.9496 0.0981  -0.0850 -0.0398 82  THR B OG1 
1535 C CG2 . THR B 82  ? 0.6582 0.5447 0.8743 0.0816  -0.0671 -0.0472 82  THR B CG2 
1536 N N   . GLU B 83  ? 0.8080 0.5735 0.9184 0.1113  -0.0763 -0.0421 83  GLU B N   
1537 C CA  . GLU B 83  ? 0.8901 0.6083 0.9608 0.1267  -0.0829 -0.0381 83  GLU B CA  
1538 C C   . GLU B 83  ? 0.8873 0.5916 0.9346 0.1310  -0.0930 -0.0303 83  GLU B C   
1539 O O   . GLU B 83  ? 0.9178 0.5854 0.9245 0.1255  -0.0870 -0.0211 83  GLU B O   
1540 C CB  . GLU B 83  ? 0.9586 0.6743 1.0420 0.1517  -0.0953 -0.0479 83  GLU B CB  
1541 C CG  . GLU B 83  ? 1.0448 0.7446 1.1260 0.1520  -0.0841 -0.0530 83  GLU B CG  
1542 C CD  . GLU B 83  ? 1.0478 0.7258 1.1244 0.1809  -0.0967 -0.0592 83  GLU B CD  
1543 O OE1 . GLU B 83  ? 1.0697 0.7248 1.1231 0.2008  -0.1124 -0.0546 83  GLU B OE1 
1544 O OE2 . GLU B 83  ? 0.9317 0.6152 1.0265 0.1845  -0.0908 -0.0690 83  GLU B OE2 
1545 N N   . ILE B 84  ? 0.8699 0.6035 0.9429 0.1403  -0.1073 -0.0355 84  ILE B N   
1546 C CA  . ILE B 84  ? 0.9465 0.6734 1.0016 0.1434  -0.1169 -0.0303 84  ILE B CA  
1547 C C   . ILE B 84  ? 0.9394 0.6619 0.9789 0.1201  -0.1027 -0.0207 84  ILE B C   
1548 O O   . ILE B 84  ? 0.9508 0.6441 0.9533 0.1195  -0.1031 -0.0130 84  ILE B O   
1549 C CB  . ILE B 84  ? 0.9179 0.6866 1.0134 0.1510  -0.1308 -0.0408 84  ILE B CB  
1550 C CG1 . ILE B 84  ? 0.9473 0.7326 1.0708 0.1707  -0.1421 -0.0542 84  ILE B CG1 
1551 C CG2 . ILE B 84  ? 0.9517 0.7112 1.0258 0.1582  -0.1434 -0.0381 84  ILE B CG2 
1552 C CD1 . ILE B 84  ? 0.9552 0.7785 1.1255 0.1591  -0.1311 -0.0629 84  ILE B CD1 
1553 N N   . GLY B 85  ? 0.8743 0.6261 0.9409 0.1014  -0.0898 -0.0213 85  GLY B N   
1554 C CA  . GLY B 85  ? 0.8756 0.6305 0.9332 0.0810  -0.0778 -0.0138 85  GLY B CA  
1555 C C   . GLY B 85  ? 0.9084 0.6226 0.9219 0.0735  -0.0676 -0.0071 85  GLY B C   
1556 O O   . GLY B 85  ? 0.9256 0.6268 0.9170 0.0660  -0.0646 -0.0015 85  GLY B O   
1557 N N   . HIS B 86  ? 0.9317 0.6249 0.9330 0.0744  -0.0606 -0.0089 86  HIS B N   
1558 C CA  . HIS B 86  ? 0.9731 0.6240 0.9330 0.0660  -0.0482 -0.0042 86  HIS B CA  
1559 C C   . HIS B 86  ? 0.9778 0.5871 0.8972 0.0789  -0.0559 0.0023  86  HIS B C   
1560 O O   . HIS B 86  ? 0.9712 0.5509 0.8565 0.0677  -0.0450 0.0079  86  HIS B O   
1561 C CB  . HIS B 86  ? 0.9120 0.5458 0.8682 0.0674  -0.0402 -0.0091 86  HIS B CB  
1562 C CG  . HIS B 86  ? 0.8856 0.5483 0.8633 0.0474  -0.0259 -0.0143 86  HIS B CG  
1563 N ND1 . HIS B 86  ? 0.7965 0.4971 0.8116 0.0486  -0.0278 -0.0208 86  HIS B ND1 
1564 C CD2 . HIS B 86  ? 0.8457 0.5060 0.8118 0.0259  -0.0096 -0.0149 86  HIS B CD2 
1565 C CE1 . HIS B 86  ? 0.7711 0.4905 0.7938 0.0299  -0.0141 -0.0239 86  HIS B CE1 
1566 N NE2 . HIS B 86  ? 0.7889 0.4865 0.7839 0.0162  -0.0037 -0.0213 86  HIS B NE2 
1567 N N   . GLU B 87  ? 1.1288 0.7363 1.0508 0.1025  -0.0743 0.0009  87  GLU B N   
1568 C CA  . GLU B 87  ? 1.2731 0.8414 1.1530 0.1178  -0.0836 0.0074  87  GLU B CA  
1569 C C   . GLU B 87  ? 1.2589 0.8371 1.1318 0.1083  -0.0845 0.0111  87  GLU B C   
1570 O O   . GLU B 87  ? 1.3074 0.8478 1.1363 0.1060  -0.0793 0.0186  87  GLU B O   
1571 C CB  . GLU B 87  ? 1.3023 0.8731 1.1900 0.1473  -0.1053 0.0027  87  GLU B CB  
1572 C CG  . GLU B 87  ? 1.4042 0.9598 1.2954 0.1594  -0.1041 -0.0013 87  GLU B CG  
1573 C CD  . GLU B 87  ? 1.6097 1.1653 1.5057 0.1916  -0.1264 -0.0066 87  GLU B CD  
1574 O OE1 . GLU B 87  ? 1.7322 1.2850 1.6129 0.2070  -0.1429 -0.0049 87  GLU B OE1 
1575 O OE2 . GLU B 87  ? 1.6488 1.2090 1.5645 0.2021  -0.1277 -0.0138 87  GLU B OE2 
1576 N N   . ASN B 88  ? 1.1544 0.7813 1.0694 0.1021  -0.0895 0.0058  88  ASN B N   
1577 C CA  . ASN B 88  ? 1.1058 0.7434 1.0177 0.0931  -0.0896 0.0080  88  ASN B CA  
1578 C C   . ASN B 88  ? 1.1103 0.7356 1.0036 0.0698  -0.0697 0.0132  88  ASN B C   
1579 O O   . ASN B 88  ? 1.2018 0.8108 1.0685 0.0646  -0.0665 0.0171  88  ASN B O   
1580 C CB  . ASN B 88  ? 1.0542 0.7435 1.0167 0.0903  -0.0960 0.0010  88  ASN B CB  
1581 C CG  . ASN B 88  ? 1.1285 0.8334 1.1100 0.1116  -0.1159 -0.0071 88  ASN B CG  
1582 O OD1 . ASN B 88  ? 1.2000 0.8870 1.1695 0.1295  -0.1250 -0.0089 88  ASN B OD1 
1583 N ND2 . ASN B 88  ? 1.0645 0.8029 1.0765 0.1102  -0.1226 -0.0133 88  ASN B ND2 
1584 N N   . MET B 89  ? 1.0468 0.6816 0.9541 0.0555  -0.0560 0.0118  89  MET B N   
1585 C CA  . MET B 89  ? 1.0434 0.6703 0.9358 0.0333  -0.0373 0.0137  89  MET B CA  
1586 C C   . MET B 89  ? 1.1253 0.6977 0.9645 0.0328  -0.0293 0.0190  89  MET B C   
1587 O O   . MET B 89  ? 1.1791 0.7420 0.9993 0.0191  -0.0188 0.0208  89  MET B O   
1588 C CB  . MET B 89  ? 0.9574 0.6000 0.8688 0.0208  -0.0254 0.0094  89  MET B CB  
1589 C CG  . MET B 89  ? 0.9057 0.5985 0.8646 0.0203  -0.0304 0.0056  89  MET B CG  
1590 S SD  . MET B 89  ? 1.1866 0.9205 1.1701 0.0044  -0.0253 0.0066  89  MET B SD  
1591 C CE  . MET B 89  ? 0.9396 0.6809 0.9322 0.0181  -0.0411 0.0084  89  MET B CE  
1592 N N   . ARG B 90  ? 1.2184 0.7530 1.0324 0.0485  -0.0333 0.0214  90  ARG B N   
1593 C CA  . ARG B 90  ? 1.2581 0.7331 1.0167 0.0494  -0.0238 0.0281  90  ARG B CA  
1594 C C   . ARG B 90  ? 1.2843 0.7414 1.0125 0.0601  -0.0336 0.0342  90  ARG B C   
1595 O O   . ARG B 90  ? 1.3027 0.7283 0.9933 0.0486  -0.0201 0.0387  90  ARG B O   
1596 C CB  . ARG B 90  ? 1.3327 0.7714 1.0738 0.0657  -0.0257 0.0296  90  ARG B CB  
1597 C CG  . ARG B 90  ? 1.4144 0.7876 1.1016 0.0606  -0.0078 0.0358  90  ARG B CG  
1598 C CD  . ARG B 90  ? 1.3607 0.7009 1.0350 0.0826  -0.0139 0.0375  90  ARG B CD  
1599 N NE  . ARG B 90  ? 1.5068 0.8608 1.1889 0.1118  -0.0406 0.0392  90  ARG B NE  
1600 C CZ  . ARG B 90  ? 1.6478 0.9758 1.2931 0.1289  -0.0524 0.0472  90  ARG B CZ  
1601 N NH1 . ARG B 90  ? 1.6710 0.9494 1.2632 0.1215  -0.0387 0.0566  90  ARG B NH1 
1602 N NH2 . ARG B 90  ? 1.6631 1.0180 1.3261 0.1529  -0.0779 0.0446  90  ARG B NH2 
1603 N N   . LEU B 91  ? 1.2528 0.7303 0.9963 0.0814  -0.0562 0.0329  91  LEU B N   
1604 C CA  . LEU B 91  ? 1.2545 0.7214 0.9715 0.0913  -0.0668 0.0364  91  LEU B CA  
1605 C C   . LEU B 91  ? 1.3289 0.8143 1.0513 0.0691  -0.0551 0.0350  91  LEU B C   
1606 O O   . LEU B 91  ? 1.3886 0.8419 1.0689 0.0639  -0.0469 0.0400  91  LEU B O   
1607 C CB  . LEU B 91  ? 1.2016 0.7033 0.9482 0.1126  -0.0921 0.0302  91  LEU B CB  
1608 C CG  . LEU B 91  ? 1.3589 0.8573 1.1115 0.1389  -0.1095 0.0278  91  LEU B CG  
1609 C CD1 . LEU B 91  ? 1.2374 0.7656 1.0070 0.1582  -0.1340 0.0205  91  LEU B CD1 
1610 C CD2 . LEU B 91  ? 1.4684 0.9030 1.1631 0.1510  -0.1050 0.0380  91  LEU B CD2 
1611 N N   . ARG B 92  ? 1.2109 0.7475 0.9847 0.0567  -0.0539 0.0282  92  ARG B N   
1612 C CA  . ARG B 92  ? 1.1517 0.7123 0.9381 0.0392  -0.0456 0.0258  92  ARG B CA  
1613 C C   . ARG B 92  ? 1.1588 0.6943 0.9176 0.0177  -0.0223 0.0278  92  ARG B C   
1614 O O   . ARG B 92  ? 1.1999 0.7287 0.9406 0.0079  -0.0146 0.0280  92  ARG B O   
1615 C CB  . ARG B 92  ? 1.1784 0.7945 1.0233 0.0327  -0.0483 0.0197  92  ARG B CB  
1616 C CG  . ARG B 92  ? 1.1175 0.7596 0.9916 0.0510  -0.0687 0.0154  92  ARG B CG  
1617 C CD  . ARG B 92  ? 1.0695 0.7599 0.9976 0.0441  -0.0684 0.0108  92  ARG B CD  
1618 N NE  . ARG B 92  ? 1.0625 0.7761 1.0200 0.0596  -0.0852 0.0049  92  ARG B NE  
1619 C CZ  . ARG B 92  ? 1.1132 0.8634 1.1160 0.0576  -0.0860 0.0008  92  ARG B CZ  
1620 N NH1 . ARG B 92  ? 1.0785 0.8468 1.1006 0.0430  -0.0730 0.0033  92  ARG B NH1 
1621 N NH2 . ARG B 92  ? 1.1368 0.9063 1.1656 0.0707  -0.0999 -0.0067 92  ARG B NH2 
1622 N N   . HIS B 93  ? 1.1709 0.6933 0.9272 0.0090  -0.0099 0.0276  93  HIS B N   
1623 C CA  . HIS B 93  ? 1.3068 0.8063 1.0392 -0.0132 0.0137  0.0267  93  HIS B CA  
1624 C C   . HIS B 93  ? 1.4033 0.8427 1.0746 -0.0099 0.0210  0.0340  93  HIS B C   
1625 O O   . HIS B 93  ? 1.4370 0.8615 1.0864 -0.0278 0.0387  0.0329  93  HIS B O   
1626 C CB  . HIS B 93  ? 1.3058 0.8045 1.0496 -0.0228 0.0250  0.0228  93  HIS B CB  
1627 C CG  . HIS B 93  ? 1.3967 0.8749 1.1204 -0.0474 0.0504  0.0185  93  HIS B CG  
1628 N ND1 . HIS B 93  ? 1.4574 0.9736 1.2069 -0.0687 0.0617  0.0101  93  HIS B ND1 
1629 C CD2 . HIS B 93  ? 1.4472 0.8718 1.1297 -0.0543 0.0675  0.0200  93  HIS B CD2 
1630 C CE1 . HIS B 93  ? 1.4735 0.9639 1.2005 -0.0889 0.0844  0.0049  93  HIS B CE1 
1631 N NE2 . HIS B 93  ? 1.5242 0.9569 1.2098 -0.0817 0.0896  0.0110  93  HIS B NE2 
1632 N N   . GLU B 94  ? 1.3684 0.7726 1.0104 0.0136  0.0079  0.0413  94  GLU B N   
1633 C CA  . GLU B 94  ? 1.4460 0.7885 1.0238 0.0199  0.0141  0.0505  94  GLU B CA  
1634 C C   . GLU B 94  ? 1.4781 0.8253 1.0395 0.0194  0.0104  0.0515  94  GLU B C   
1635 O O   . GLU B 94  ? 1.5213 0.8364 1.0443 0.0049  0.0290  0.0539  94  GLU B O   
1636 C CB  . GLU B 94  ? 1.5678 0.8762 1.1199 0.0497  -0.0029 0.0583  94  GLU B CB  
1637 C CG  . GLU B 94  ? 1.6233 0.9022 1.1693 0.0503  0.0069  0.0595  94  GLU B CG  
1638 C CD  . GLU B 94  ? 1.7721 1.0096 1.2847 0.0820  -0.0087 0.0682  94  GLU B CD  
1639 O OE1 . GLU B 94  ? 1.8610 1.0750 1.3353 0.0998  -0.0206 0.0758  94  GLU B OE1 
1640 O OE2 . GLU B 94  ? 1.7983 1.0275 1.3224 0.0900  -0.0093 0.0668  94  GLU B OE2 
1641 N N   . SER B 95  ? 1.4097 0.7966 1.0003 0.0342  -0.0122 0.0482  95  SER B N   
1642 C CA  . SER B 95  ? 1.4059 0.7983 0.9817 0.0352  -0.0171 0.0474  95  SER B CA  
1643 C C   . SER B 95  ? 1.4116 0.8190 0.9966 0.0072  0.0044  0.0419  95  SER B C   
1644 O O   . SER B 95  ? 1.5113 0.8910 1.0560 -0.0003 0.0157  0.0440  95  SER B O   
1645 C CB  . SER B 95  ? 1.3112 0.7521 0.9293 0.0511  -0.0422 0.0408  95  SER B CB  
1646 O OG  . SER B 95  ? 1.3009 0.7950 0.9797 0.0374  -0.0397 0.0328  95  SER B OG  
1647 N N   . TRP B 96  ? 1.3200 0.7716 0.9568 -0.0081 0.0106  0.0343  96  TRP B N   
1648 C CA  . TRP B 96  ? 1.3359 0.8084 0.9869 -0.0325 0.0289  0.0274  96  TRP B CA  
1649 C C   . TRP B 96  ? 1.4832 0.9140 1.0950 -0.0521 0.0555  0.0281  96  TRP B C   
1650 O O   . TRP B 96  ? 1.5154 0.9520 1.1240 -0.0708 0.0719  0.0223  96  TRP B O   
1651 C CB  . TRP B 96  ? 1.2506 0.7801 0.9639 -0.0411 0.0275  0.0199  96  TRP B CB  
1652 C CG  . TRP B 96  ? 1.2169 0.7895 0.9686 -0.0317 0.0108  0.0166  96  TRP B CG  
1653 C CD1 . TRP B 96  ? 1.1848 0.7815 0.9673 -0.0149 -0.0087 0.0169  96  TRP B CD1 
1654 C CD2 . TRP B 96  ? 1.2218 0.8173 0.9861 -0.0392 0.0139  0.0110  96  TRP B CD2 
1655 N NE1 . TRP B 96  ? 1.1360 0.7672 0.9489 -0.0124 -0.0172 0.0121  96  TRP B NE1 
1656 C CE2 . TRP B 96  ? 1.1583 0.7891 0.9606 -0.0264 -0.0040 0.0087  96  TRP B CE2 
1657 C CE3 . TRP B 96  ? 1.2255 0.8151 0.9738 -0.0561 0.0314  0.0067  96  TRP B CE3 
1658 C CZ2 . TRP B 96  ? 1.1125 0.7701 0.9363 -0.0292 -0.0052 0.0028  96  TRP B CZ2 
1659 C CZ3 . TRP B 96  ? 1.1859 0.8047 0.9563 -0.0581 0.0293  0.0005  96  TRP B CZ3 
1660 C CH2 . TRP B 96  ? 1.1333 0.7844 0.9406 -0.0443 0.0110  -0.0011 96  TRP B CH2 
1661 N N   . SER B 97  ? 1.6668 1.0557 1.2503 -0.0490 0.0616  0.0339  97  SER B N   
1662 C CA  . SER B 97  ? 1.7310 1.0711 1.2708 -0.0676 0.0890  0.0348  97  SER B CA  
1663 C C   . SER B 97  ? 1.7643 1.0555 1.2434 -0.0631 0.0943  0.0428  97  SER B C   
1664 O O   . SER B 97  ? 1.8423 1.1162 1.2987 -0.0845 0.1179  0.0391  97  SER B O   
1665 C CB  . SER B 97  ? 1.7501 1.0535 1.2740 -0.0642 0.0947  0.0390  97  SER B CB  
1666 O OG  . SER B 97  ? 1.7378 1.0816 1.3100 -0.0785 0.1003  0.0286  97  SER B OG  
1667 N N   . ARG B 98  ? 1.5765 0.8470 1.0287 -0.0355 0.0727  0.0527  98  ARG B N   
1668 C CA  . ARG B 98  ? 1.7161 0.9385 1.1048 -0.0283 0.0759  0.0613  98  ARG B CA  
1669 C C   . ARG B 98  ? 1.6937 0.9455 1.0914 -0.0417 0.0809  0.0533  98  ARG B C   
1670 O O   . ARG B 98  ? 1.7581 0.9731 1.1087 -0.0534 0.1000  0.0555  98  ARG B O   
1671 C CB  . ARG B 98  ? 1.7821 0.9880 1.1470 0.0066  0.0473  0.0710  98  ARG B CB  
1672 C CG  . ARG B 98  ? 1.9723 1.1228 1.2625 0.0179  0.0489  0.0819  98  ARG B CG  
1673 C CD  . ARG B 98  ? 2.0552 1.1305 1.2832 0.0084  0.0763  0.0926  98  ARG B CD  
1674 N NE  . ARG B 98  ? 2.1593 1.1772 1.3100 0.0186  0.0804  0.1047  98  ARG B NE  
1675 C CZ  . ARG B 98  ? 2.2016 1.2004 1.3198 -0.0027 0.1039  0.1033  98  ARG B CZ  
1676 N NH1 . ARG B 98  ? 2.0815 1.1159 1.2400 -0.0348 0.1249  0.0894  98  ARG B NH1 
1677 N NH2 . ARG B 98  ? 2.3146 1.2580 1.3573 0.0093  0.1065  0.1158  98  ARG B NH2 
1678 N N   . VAL B 99  ? 1.5785 0.8945 1.0356 -0.0403 0.0655  0.0438  99  VAL B N   
1679 C CA  . VAL B 99  ? 1.5469 0.8927 1.0174 -0.0520 0.0701  0.0351  99  VAL B CA  
1680 C C   . VAL B 99  ? 1.6230 0.9636 1.0899 -0.0827 0.1017  0.0278  99  VAL B C   
1681 O O   . VAL B 99  ? 1.6641 0.9929 1.1048 -0.0937 0.1154  0.0246  99  VAL B O   
1682 C CB  . VAL B 99  ? 1.4985 0.9122 1.0381 -0.0465 0.0510  0.0262  99  VAL B CB  
1683 C CG1 . VAL B 99  ? 1.4299 0.8763 0.9906 -0.0614 0.0598  0.0155  99  VAL B CG1 
1684 C CG2 . VAL B 99  ? 1.4551 0.8747 0.9959 -0.0182 0.0216  0.0300  99  VAL B CG2 
1685 N N   . ASP B 100 ? 1.6614 1.0111 1.1540 -0.0975 0.1145  0.0236  100 ASP B N   
1686 C CA  . ASP B 100 ? 1.6775 1.0289 1.1730 -0.1277 0.1444  0.0133  100 ASP B CA  
1687 C C   . ASP B 100 ? 1.7535 1.0362 1.1785 -0.1382 0.1688  0.0190  100 ASP B C   
1688 O O   . ASP B 100 ? 1.7730 1.0541 1.1888 -0.1606 0.1923  0.0102  100 ASP B O   
1689 C CB  . ASP B 100 ? 1.7143 1.0881 1.2483 -0.1398 0.1515  0.0066  100 ASP B CB  
1690 C CG  . ASP B 100 ? 1.7577 1.2013 1.3605 -0.1338 0.1326  0.0000  100 ASP B CG  
1691 O OD1 . ASP B 100 ? 1.7007 1.1757 1.3244 -0.1242 0.1181  -0.0012 100 ASP B OD1 
1692 O OD2 . ASP B 100 ? 1.7565 1.2218 1.3907 -0.1387 0.1331  -0.0042 100 ASP B OD2 
1693 N N   . LYS B 101 ? 1.7248 0.9491 1.0989 -0.1221 0.1649  0.0337  101 LYS B N   
1694 C CA  . LYS B 101 ? 1.8036 0.9547 1.1028 -0.1286 0.1875  0.0425  101 LYS B CA  
1695 C C   . LYS B 101 ? 1.8574 0.9994 1.1213 -0.1221 0.1838  0.0454  101 LYS B C   
1696 O O   . LYS B 101 ? 1.8900 1.0053 1.1191 -0.1422 0.2104  0.0423  101 LYS B O   
1697 C CB  . LYS B 101 ? 1.8317 0.9227 1.0852 -0.1075 0.1807  0.0590  101 LYS B CB  
1698 C CG  . LYS B 101 ? 1.9060 0.9987 1.1882 -0.1156 0.1880  0.0552  101 LYS B CG  
1699 C CD  . LYS B 101 ? 1.8898 0.9544 1.1564 -0.0850 0.1661  0.0686  101 LYS B CD  
1700 C CE  . LYS B 101 ? 1.7557 0.8522 1.0754 -0.0896 0.1635  0.0606  101 LYS B CE  
1701 N NZ  . LYS B 101 ? 1.7319 0.8232 1.0549 -0.0578 0.1363  0.0699  101 LYS B NZ  
1702 N N   . ILE B 102 ? 1.9175 1.0830 1.1909 -0.0952 0.1519  0.0498  102 ILE B N   
1703 C CA  . ILE B 102 ? 1.8923 1.0519 1.1325 -0.0866 0.1451  0.0512  102 ILE B CA  
1704 C C   . ILE B 102 ? 1.8730 1.0659 1.1367 -0.1131 0.1650  0.0359  102 ILE B C   
1705 O O   . ILE B 102 ? 1.9228 1.0843 1.1381 -0.1223 0.1823  0.0363  102 ILE B O   
1706 C CB  . ILE B 102 ? 1.7652 0.9624 1.0321 -0.0572 0.1072  0.0521  102 ILE B CB  
1707 C CG1 . ILE B 102 ? 1.8110 0.9739 1.0502 -0.0287 0.0872  0.0663  102 ILE B CG1 
1708 C CG2 . ILE B 102 ? 1.7446 0.9459 0.9862 -0.0510 0.1003  0.0492  102 ILE B CG2 
1709 C CD1 . ILE B 102 ? 1.7142 0.9084 0.9703 0.0006  0.0512  0.0658  102 ILE B CD1 
1710 N N   . ILE B 103 ? 1.7452 1.0018 1.0824 -0.1248 0.1633  0.0220  103 ILE B N   
1711 C CA  . ILE B 103 ? 1.7347 1.0290 1.1013 -0.1473 0.1800  0.0061  103 ILE B CA  
1712 C C   . ILE B 103 ? 1.8543 1.1141 1.1904 -0.1767 0.2179  0.0012  103 ILE B C   
1713 O O   . ILE B 103 ? 1.8986 1.1520 1.2142 -0.1921 0.2371  -0.0062 103 ILE B O   
1714 C CB  . ILE B 103 ? 1.5600 0.9278 1.0104 -0.1502 0.1686  -0.0059 103 ILE B CB  
1715 C CG1 . ILE B 103 ? 1.5283 0.9268 1.0076 -0.1230 0.1342  -0.0017 103 ILE B CG1 
1716 C CG2 . ILE B 103 ? 1.4820 0.8895 0.9648 -0.1714 0.1858  -0.0229 103 ILE B CG2 
1717 C CD1 . ILE B 103 ? 1.5085 0.8981 0.9581 -0.1095 0.1226  -0.0005 103 ILE B CD1 
1718 N N   . GLU B 104 ? 1.8963 1.1343 1.2308 -0.1862 0.2305  0.0034  104 GLU B N   
1719 C CA  . GLU B 104 ? 1.9100 1.1105 1.2143 -0.2154 0.2684  -0.0022 104 GLU B CA  
1720 C C   . GLU B 104 ? 2.0927 1.2200 1.3117 -0.2146 0.2842  0.0099  104 GLU B C   
1721 O O   . GLU B 104 ? 2.1618 1.2697 1.3564 -0.2399 0.3159  0.0017  104 GLU B O   
1722 C CB  . GLU B 104 ? 1.8780 1.0619 1.1908 -0.2217 0.2760  -0.0008 104 GLU B CB  
1723 C CG  . GLU B 104 ? 1.9725 1.1386 1.2794 -0.2566 0.3152  -0.0137 104 GLU B CG  
1724 C CD  . GLU B 104 ? 1.9945 1.1651 1.3271 -0.2605 0.3173  -0.0176 104 GLU B CD  
1725 O OE1 . GLU B 104 ? 1.8488 1.0139 1.1869 -0.2386 0.2934  -0.0052 104 GLU B OE1 
1726 O OE2 . GLU B 104 ? 2.0299 1.2173 1.3813 -0.2828 0.3408  -0.0357 104 GLU B OE2 
1727 N N   . ASN B 105 ? 2.1580 1.2455 1.3305 -0.1849 0.2622  0.0289  105 ASN B N   
1728 C CA  . ASN B 105 ? 2.2905 1.3047 1.3750 -0.1792 0.2741  0.0432  105 ASN B CA  
1729 C C   . ASN B 105 ? 2.2741 1.3049 1.3441 -0.1777 0.2707  0.0383  105 ASN B C   
1730 O O   . ASN B 105 ? 2.4254 1.4062 1.4312 -0.1880 0.2944  0.0424  105 ASN B O   
1731 C CB  . ASN B 105 ? 2.3317 1.2999 1.3721 -0.1450 0.2496  0.0647  105 ASN B CB  
1732 C CG  . ASN B 105 ? 2.3381 1.2748 1.3767 -0.1464 0.2591  0.0693  105 ASN B CG  
1733 O OD1 . ASN B 105 ? 2.3703 1.3154 1.4316 -0.1725 0.2860  0.0552  105 ASN B OD1 
1734 N ND2 . ASN B 105 ? 2.3534 1.2691 1.3762 -0.1151 0.2338  0.0837  105 ASN B ND2 
1735 N N   . LEU B 106 ? 2.1704 1.2680 1.2967 -0.1653 0.2433  0.0293  106 LEU B N   
1736 C CA  . LEU B 106 ? 2.1452 1.2642 1.2659 -0.1670 0.2425  0.0207  106 LEU B CA  
1737 C C   . LEU B 106 ? 2.2828 1.4069 1.4079 -0.2022 0.2801  0.0051  106 LEU B C   
1738 O O   . LEU B 106 ? 2.3448 1.4425 1.4219 -0.2102 0.2966  0.0038  106 LEU B O   
1739 C CB  . LEU B 106 ? 2.0616 1.2552 1.2540 -0.1528 0.2116  0.0105  106 LEU B CB  
1740 C CG  . LEU B 106 ? 1.9817 1.1817 1.1711 -0.1182 0.1730  0.0201  106 LEU B CG  
1741 C CD1 . LEU B 106 ? 1.8753 1.1506 1.1472 -0.1122 0.1506  0.0074  106 LEU B CD1 
1742 C CD2 . LEU B 106 ? 2.1035 1.2709 1.2275 -0.1054 0.1678  0.0253  106 LEU B CD2 
1743 N N   . GLU B 107 ? 2.4208 1.5811 1.6039 -0.2234 0.2940  -0.0081 107 GLU B N   
1744 C CA  . GLU B 107 ? 2.4590 1.6317 1.6551 -0.2575 0.3297  -0.0263 107 GLU B CA  
1745 C C   . GLU B 107 ? 2.5296 1.6270 1.6561 -0.2776 0.3663  -0.0198 107 GLU B C   
1746 O O   . GLU B 107 ? 2.5619 1.6521 1.6742 -0.3026 0.3973  -0.0326 107 GLU B O   
1747 C CB  . GLU B 107 ? 2.3681 1.6074 1.6495 -0.2711 0.3298  -0.0433 107 GLU B CB  
1748 C CG  . GLU B 107 ? 2.3969 1.6743 1.7131 -0.3013 0.3578  -0.0671 107 GLU B CG  
1749 C CD  . GLU B 107 ? 2.3584 1.7114 1.7622 -0.3067 0.3492  -0.0833 107 GLU B CD  
1750 O OE1 . GLU B 107 ? 2.3158 1.6915 1.7516 -0.2864 0.3206  -0.0750 107 GLU B OE1 
1751 O OE2 . GLU B 107 ? 2.3883 1.7786 1.8282 -0.3306 0.3709  -0.1045 107 GLU B OE2 
1752 N N   . ALA B 108 ? 2.4631 1.5057 1.5493 -0.2655 0.3628  -0.0018 108 ALA B N   
1753 C CA  . ALA B 108 ? 2.5550 1.5459 1.5993 -0.2722 0.3849  -0.0032 108 ALA B CA  
1754 C C   . ALA B 108 ? 2.6223 1.5640 1.5953 -0.2648 0.3911  0.0051  108 ALA B C   
1755 O O   . ALA B 108 ? 2.7057 1.6327 1.6635 -0.2855 0.4188  -0.0076 108 ALA B O   
1756 C CB  . ALA B 108 ? 2.6398 1.5966 1.6702 -0.2536 0.3730  0.0107  108 ALA B CB  
1757 N N   . ASN B 109 ? 2.4694 1.3865 1.3986 -0.2346 0.3643  0.0254  109 ASN B N   
1758 C CA  . ASN B 109 ? 2.5196 1.3950 1.3815 -0.2248 0.3665  0.0332  109 ASN B CA  
1759 C C   . ASN B 109 ? 2.4752 1.3845 1.3512 -0.2469 0.3831  0.0159  109 ASN B C   
1760 O O   . ASN B 109 ? 2.5327 1.4099 1.3640 -0.2527 0.3991  0.0144  109 ASN B O   
1761 C CB  . ASN B 109 ? 2.5205 1.3796 1.3432 -0.1867 0.3298  0.0540  109 ASN B CB  
1762 C CG  . ASN B 109 ? 2.4904 1.3170 1.3003 -0.1622 0.3123  0.0701  109 ASN B CG  
1763 O OD1 . ASN B 109 ? 2.3915 1.1945 1.2053 -0.1725 0.3307  0.0677  109 ASN B OD1 
1764 N ND2 . ASN B 109 ? 2.4530 1.2805 1.2485 -0.1289 0.2766  0.0847  109 ASN B ND2 
1765 N N   . LYS B 110 ? 2.4195 1.3941 1.3588 -0.2592 0.3804  0.0022  110 LYS B N   
1766 C CA  . LYS B 110 ? 2.3533 1.3709 1.3211 -0.2818 0.3981  -0.0188 110 LYS B CA  
1767 C C   . LYS B 110 ? 2.2960 1.3102 1.2809 -0.3130 0.4331  -0.0378 110 LYS B C   
1768 O O   . LYS B 110 ? 2.1082 1.1275 1.0868 -0.3290 0.4518  -0.0513 110 LYS B O   
1769 C CB  . LYS B 110 ? 2.2801 1.3823 1.3374 -0.2797 0.3778  -0.0333 110 LYS B CB  
1770 C CG  . LYS B 110 ? 2.1648 1.3230 1.2715 -0.3023 0.3949  -0.0589 110 LYS B CG  
1771 C CD  . LYS B 110 ? 2.0980 1.3397 1.3022 -0.2951 0.3704  -0.0723 110 LYS B CD  
1772 C CE  . LYS B 110 ? 1.9487 1.2477 1.2074 -0.3168 0.3882  -0.0985 110 LYS B CE  
1773 N NZ  . LYS B 110 ? 1.9337 1.3100 1.2839 -0.3079 0.3648  -0.1096 110 LYS B NZ  
# 
