data_9GKS
# 
_entry.id   9GKS 
# 
_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   9GKS         pdb_00009gks 10.2210/pdb9gks/pdb 
WWPDB D_1292141265 ?            ?                   
# 
_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                        9GKS 
_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 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Transcriptional regulator, PadR-like family' 15163.173 2  ? 'V15pAF, N19M, A92R, F93H' ? 
'LmrR carrying a C-terminal strep-tag, V15 replaced by para-aminophenylalanine (pAF) and with mutations A92R, N19M, F93H (RMH)' 
2 water   nat water                                         18.015    22 ? ?                          ? ? 
# 
_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         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
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 
HOH non-polymer         . WATER                   ? 'H2 O'           18.015  
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  ?   ?   ?   A . n 
A 1 71  SER 71  71  ?   ?   ?   A . n 
A 1 72  GLN 72  72  ?   ?   ?   A . n 
A 1 73  GLY 73  73  ?   ?   ?   A . n 
A 1 74  GLY 74  74  ?   ?   ?   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 ?   ?   ?   A . n 
A 1 113 GLU 113 113 ?   ?   ?   A . n 
A 1 114 ALA 114 114 ?   ?   ?   A . n 
A 1 115 ILE 115 115 ?   ?   ?   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   2   ALA ALA B . n 
B 1 3   GLU 3   3   3   GLU GLU 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  ?   ?   ?   B . n 
B 1 70  GLU 70  70  ?   ?   ?   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 111 111 111 LYS LYS 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_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1  201 14 HOH HOH A . 
C 2 HOH 2  202 11 HOH HOH A . 
C 2 HOH 3  203 7  HOH HOH A . 
C 2 HOH 4  204 19 HOH HOH A . 
C 2 HOH 5  205 25 HOH HOH A . 
C 2 HOH 6  206 20 HOH HOH A . 
C 2 HOH 7  207 21 HOH HOH A . 
C 2 HOH 8  208 8  HOH HOH A . 
C 2 HOH 9  209 6  HOH HOH A . 
C 2 HOH 10 210 2  HOH HOH A . 
C 2 HOH 11 211 16 HOH HOH A . 
C 2 HOH 12 212 3  HOH HOH A . 
C 2 HOH 13 213 5  HOH HOH A . 
C 2 HOH 14 214 28 HOH HOH A . 
C 2 HOH 15 215 1  HOH HOH A . 
C 2 HOH 16 216 12 HOH HOH A . 
C 2 HOH 17 217 9  HOH HOH A . 
C 2 HOH 18 218 13 HOH HOH A . 
C 2 HOH 19 219 26 HOH HOH A . 
D 2 HOH 1  201 22 HOH HOH B . 
D 2 HOH 2  202 27 HOH HOH B . 
D 2 HOH 3  203 24 HOH HOH B . 
# 
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' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .            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                   97.27 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GKS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.927 
_cell.length_a_esd                 ? 
_cell.length_b                     35.303 
_cell.length_b_esd                 ? 
_cell.length_c                     68.180 
_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                         9GKS 
_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                   9GKS 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.44 
_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         2021-10-03 
_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   0.96546 
_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        0.96546 
_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                                       9GKS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.24 
_reflns.d_resolution_low                               52.04 
_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                                     11930 
_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                           97.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.50 
_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                                0.051 
_reflns.pdbx_Rpim_I_all                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       34336 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.042 
_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                                    2.24 
_reflns_shell.d_res_low                                     2.31 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           2720 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             959 
_reflns_shell.percent_possible_obs                          86.2 
_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                               2.8 
_reflns_shell.pdbx_chi_squared                              0.19 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               0.702 
_reflns_shell.pdbx_Rpim_I_all                               0.403 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.467 
_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                                  0.570 
_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                                 9GKS 
_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                            2.24 
_refine.ls_d_res_low                             52.04 
_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                     10740 
_refine.ls_number_reflns_R_free                  1081 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.91 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2302 
_refine.ls_R_factor_R_free                       0.2945 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2268 
_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                          0.12 
_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                 36.03 
_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                            0.35 
_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        1734 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             22 
_refine_hist.number_atoms_total               1756 
_refine_hist.d_res_high                       2.24 
_refine_hist.d_res_low                        52.04 
# 
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' ? 0.014  ? 1760 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.369  ? 2354 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.287 ? 686  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059  ? 251  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 295  ? 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' 2.24 2.34  . . 111 2336 83.00 . . . . 0.3085 . . . . . . . . . . . 0.3502 
'X-RAY DIFFRACTION' 2.34 2.46  . . 123 2402 88.00 . . . . 0.2629 . . . . . . . . . . . 0.3364 
'X-RAY DIFFRACTION' 2.46 2.62  . . 121 2691 96.00 . . . . 0.2872 . . . . . . . . . . . 0.2667 
'X-RAY DIFFRACTION' 2.62 2.82  . . 133 2679 96.00 . . . . 0.2875 . . . . . . . . . . . 0.3713 
'X-RAY DIFFRACTION' 2.82 3.11  . . 156 2649 95.00 . . . . 0.2814 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 3.11 3.55  . . 154 2425 89.00 . . . . 0.2498 . . . . . . . . . . . 0.3392 
'X-RAY DIFFRACTION' 3.55 4.48  . . 136 2640 95.00 . . . . 0.2073 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 4.48 52.04 . . 147 2578 93.00 . . . . 0.1845 . . . . . . . . . . . 0.2573 
# 
_struct.entry_id                     9GKS 
_struct.title                        'Crystal structure of artificial enzyme LmrR_pAF variant RMH in crystal form 2' 
_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        9GKS 
_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 ? 
C N N 2 ? 
D N N 2 ? 
# 
_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 9GKS A 2 ? 116 ? A2RI36 2 ? 116 ? 2 116 
2 1 9GKS 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 9GKS GLY A 1   ? UNP A2RI36 ?   ?  'expression tag'      1   1  
1 9GKS HOX A 15  ? UNP A2RI36 VAL 15 'engineered mutation' 15  2  
1 9GKS MET A 19  ? UNP A2RI36 ASN 19 'engineered mutation' 19  3  
1 9GKS ARG A 92  ? UNP A2RI36 ALA 92 'engineered mutation' 92  4  
1 9GKS HIS A 93  ? UNP A2RI36 PHE 93 'engineered mutation' 93  5  
1 9GKS SER A 117 ? UNP A2RI36 ?   ?  'expression tag'      117 6  
1 9GKS ARG A 118 ? UNP A2RI36 ?   ?  'expression tag'      118 7  
1 9GKS GLY A 119 ? UNP A2RI36 ?   ?  'expression tag'      119 8  
1 9GKS GLY A 120 ? UNP A2RI36 ?   ?  'expression tag'      120 9  
1 9GKS SER A 121 ? UNP A2RI36 ?   ?  'expression tag'      121 10 
1 9GKS GLY A 122 ? UNP A2RI36 ?   ?  'expression tag'      122 11 
1 9GKS GLY A 123 ? UNP A2RI36 ?   ?  'expression tag'      123 12 
1 9GKS TRP A 124 ? UNP A2RI36 ?   ?  'expression tag'      124 13 
1 9GKS SER A 125 ? UNP A2RI36 ?   ?  'expression tag'      125 14 
1 9GKS HIS A 126 ? UNP A2RI36 ?   ?  'expression tag'      126 15 
1 9GKS PRO A 127 ? UNP A2RI36 ?   ?  'expression tag'      127 16 
1 9GKS GLN A 128 ? UNP A2RI36 ?   ?  'expression tag'      128 17 
1 9GKS PHE A 129 ? UNP A2RI36 ?   ?  'expression tag'      129 18 
1 9GKS GLU A 130 ? UNP A2RI36 ?   ?  'expression tag'      130 19 
1 9GKS LYS A 131 ? UNP A2RI36 ?   ?  'expression tag'      131 20 
2 9GKS GLY B 1   ? UNP A2RI36 ?   ?  'expression tag'      1   21 
2 9GKS HOX B 15  ? UNP A2RI36 VAL 15 'engineered mutation' 15  22 
2 9GKS MET B 19  ? UNP A2RI36 ASN 19 'engineered mutation' 19  23 
2 9GKS ARG B 92  ? UNP A2RI36 ALA 92 'engineered mutation' 92  24 
2 9GKS HIS B 93  ? UNP A2RI36 PHE 93 'engineered mutation' 93  25 
2 9GKS SER B 117 ? UNP A2RI36 ?   ?  'expression tag'      117 26 
2 9GKS ARG B 118 ? UNP A2RI36 ?   ?  'expression tag'      118 27 
2 9GKS GLY B 119 ? UNP A2RI36 ?   ?  'expression tag'      119 28 
2 9GKS GLY B 120 ? UNP A2RI36 ?   ?  'expression tag'      120 29 
2 9GKS SER B 121 ? UNP A2RI36 ?   ?  'expression tag'      121 30 
2 9GKS GLY B 122 ? UNP A2RI36 ?   ?  'expression tag'      122 31 
2 9GKS GLY B 123 ? UNP A2RI36 ?   ?  'expression tag'      123 32 
2 9GKS TRP B 124 ? UNP A2RI36 ?   ?  'expression tag'      124 33 
2 9GKS SER B 125 ? UNP A2RI36 ?   ?  'expression tag'      125 34 
2 9GKS HIS B 126 ? UNP A2RI36 ?   ?  'expression tag'      126 35 
2 9GKS PRO B 127 ? UNP A2RI36 ?   ?  'expression tag'      127 36 
2 9GKS GLN B 128 ? UNP A2RI36 ?   ?  'expression tag'      128 37 
2 9GKS PHE B 129 ? UNP A2RI36 ?   ?  'expression tag'      129 38 
2 9GKS GLU B 130 ? UNP A2RI36 ?   ?  'expression tag'      130 39 
2 9GKS 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)' 3150  ? 
1 MORE         -22   ? 
1 'SSA (A^2)'  12810 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 ? LYS A 111 ? THR A 82 LYS A 111 1 ? 30 
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 ? ? ? ? ? ? ? 1.330 ? ? 
covale2 covale both ? A HOX 15 C ? ? ? 1_555 A ILE 16 N ? ? A HOX 15 A ILE 16 1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale3 covale both ? B ASN 14 C ? ? ? 1_555 B HOX 15 N ? ? B ASN 14 B HOX 15 1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale4 covale both ? B HOX 15 C ? ? ? 1_555 B ILE 16 N ? ? B HOX 15 B ILE 16 1_555 ? ? ? ? ? ? ? 1.317 ? ? 
# 
_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 ? TRP A 67 ? ILE A 63 TRP A 67 
AA1 2 LYS A 77 ? LEU A 81 ? LYS A 77 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 TYR A 66 ? N TYR A 66 O TYR A 78 ? O TYR A 78 
AA2 1 2 N TYR B 66 ? N TYR B 66 O TYR B 78 ? O TYR B 78 
# 
_pdbx_entry_details.entry_id                   9GKS 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 87 ? ? HH21 A ARG 90  ? ? 1.56 
2 1 O   A LYS 59 ? ? O    A HOH 201 ? ? 2.11 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH22 A ARG 90 ? ? 1_555 OE1 B GLU 47 ? ? 4_546 1.49 
2 1 NH2  A ARG 90 ? ? 1_555 OE1 B GLU 47 ? ? 4_546 2.04 
# 
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 16.326 -1.561 10.245 0.3565 0.2841 0.4582 -0.0070 -0.0187 -0.0090 4.3541 2.5730 4.0413 0.0316  
-3.0271 0.9606 -0.1652 -0.0872 0.1671  -0.0999 -0.1891 -0.2127 0.2121 0.2750 -0.1590 
'X-RAY DIFFRACTION' 2 ? refined 8.761  2.421  31.243 0.7855 0.9062 0.5576 0.0750  -0.0384 0.0172  2.8467 1.0851 4.9872 -0.6018 
1.3729  1.3130 -0.2848 0.4320  -0.0825 -0.7500 -0.1110 -0.1833 0.4546 0.0873 -1.1614 
# 
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 A 4 A 111 '( CHAIN A AND RESID 4:111 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 2 B 111 '( CHAIN B AND RESID 2:111 )' ? ? ? ? ? 
# 
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 GLU 70  ? A GLU 70  
5  1 Y 1 A SER 71  ? A SER 71  
6  1 Y 1 A GLN 72  ? A GLN 72  
7  1 Y 1 A GLY 73  ? A GLY 73  
8  1 Y 1 A GLY 74  ? A GLY 74  
9  1 Y 1 A SER 112 ? A SER 112 
10 1 Y 1 A GLU 113 ? A GLU 113 
11 1 Y 1 A ALA 114 ? A ALA 114 
12 1 Y 1 A ILE 115 ? A ILE 115 
13 1 Y 1 A LYS 116 ? A LYS 116 
14 1 Y 1 A SER 117 ? A SER 117 
15 1 Y 1 A ARG 118 ? A ARG 118 
16 1 Y 1 A GLY 119 ? A GLY 119 
17 1 Y 1 A GLY 120 ? A GLY 120 
18 1 Y 1 A SER 121 ? A SER 121 
19 1 Y 1 A GLY 122 ? A GLY 122 
20 1 Y 1 A GLY 123 ? A GLY 123 
21 1 Y 1 A TRP 124 ? A TRP 124 
22 1 Y 1 A SER 125 ? A SER 125 
23 1 Y 1 A HIS 126 ? A HIS 126 
24 1 Y 1 A PRO 127 ? A PRO 127 
25 1 Y 1 A GLN 128 ? A GLN 128 
26 1 Y 1 A PHE 129 ? A PHE 129 
27 1 Y 1 A GLU 130 ? A GLU 130 
28 1 Y 1 A LYS 131 ? A LYS 131 
29 1 Y 1 B GLY 1   ? B GLY 1   
30 1 Y 1 B ASP 69  ? B ASP 69  
31 1 Y 1 B GLU 70  ? B GLU 70  
32 1 Y 1 B SER 71  ? B SER 71  
33 1 Y 1 B GLN 72  ? B GLN 72  
34 1 Y 1 B GLY 73  ? B GLY 73  
35 1 Y 1 B GLY 74  ? B GLY 74  
36 1 Y 1 B SER 112 ? B SER 112 
37 1 Y 1 B GLU 113 ? B GLU 113 
38 1 Y 1 B ALA 114 ? B ALA 114 
39 1 Y 1 B ILE 115 ? B ILE 115 
40 1 Y 1 B LYS 116 ? B LYS 116 
41 1 Y 1 B SER 117 ? B SER 117 
42 1 Y 1 B ARG 118 ? B ARG 118 
43 1 Y 1 B GLY 119 ? B GLY 119 
44 1 Y 1 B GLY 120 ? B GLY 120 
45 1 Y 1 B SER 121 ? B SER 121 
46 1 Y 1 B GLY 122 ? B GLY 122 
47 1 Y 1 B GLY 123 ? B GLY 123 
48 1 Y 1 B TRP 124 ? B TRP 124 
49 1 Y 1 B SER 125 ? B SER 125 
50 1 Y 1 B HIS 126 ? B HIS 126 
51 1 Y 1 B PRO 127 ? B PRO 127 
52 1 Y 1 B GLN 128 ? B GLN 128 
53 1 Y 1 B PHE 129 ? B PHE 129 
54 1 Y 1 B GLU 130 ? B GLU 130 
55 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 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
HOX O    O N N 147 
HOX C    C N N 148 
HOX N    N N N 149 
HOX OXT  O N N 150 
HOX CA   C N S 151 
HOX CB   C N N 152 
HOX CG   C Y N 153 
HOX CZ   C Y N 154 
HOX NZ   N N N 155 
HOX CD1  C Y N 156 
HOX CD2  C Y N 157 
HOX CE1  C Y N 158 
HOX CE2  C Y N 159 
HOX H    H N N 160 
HOX H2   H N N 161 
HOX HXT  H N N 162 
HOX HA   H N N 163 
HOX HB   H N N 164 
HOX HBA  H N N 165 
HOX HNZ  H N N 166 
HOX HNZA H N N 167 
HOX HD1  H N N 168 
HOX HD2  H N N 169 
HOX HE1  H N N 170 
HOX HE2  H N N 171 
ILE N    N N N 172 
ILE CA   C N S 173 
ILE C    C N N 174 
ILE O    O N N 175 
ILE CB   C N S 176 
ILE CG1  C N N 177 
ILE CG2  C N N 178 
ILE CD1  C N N 179 
ILE OXT  O N N 180 
ILE H    H N N 181 
ILE H2   H N N 182 
ILE HA   H N N 183 
ILE HB   H N N 184 
ILE HG12 H N N 185 
ILE HG13 H N N 186 
ILE HG21 H N N 187 
ILE HG22 H N N 188 
ILE HG23 H N N 189 
ILE HD11 H N N 190 
ILE HD12 H N N 191 
ILE HD13 H N N 192 
ILE HXT  H N N 193 
LEU N    N N N 194 
LEU CA   C N S 195 
LEU C    C N N 196 
LEU O    O N N 197 
LEU CB   C N N 198 
LEU CG   C N N 199 
LEU CD1  C N N 200 
LEU CD2  C N N 201 
LEU OXT  O N N 202 
LEU H    H N N 203 
LEU H2   H N N 204 
LEU HA   H N N 205 
LEU HB2  H N N 206 
LEU HB3  H N N 207 
LEU HG   H N N 208 
LEU HD11 H N N 209 
LEU HD12 H N N 210 
LEU HD13 H N N 211 
LEU HD21 H N N 212 
LEU HD22 H N N 213 
LEU HD23 H N N 214 
LEU HXT  H N N 215 
LYS N    N N N 216 
LYS CA   C N S 217 
LYS C    C N N 218 
LYS O    O N N 219 
LYS CB   C N N 220 
LYS CG   C N N 221 
LYS CD   C N N 222 
LYS CE   C N N 223 
LYS NZ   N N N 224 
LYS OXT  O N N 225 
LYS H    H N N 226 
LYS H2   H N N 227 
LYS HA   H N N 228 
LYS HB2  H N N 229 
LYS HB3  H N N 230 
LYS HG2  H N N 231 
LYS HG3  H N N 232 
LYS HD2  H N N 233 
LYS HD3  H N N 234 
LYS HE2  H N N 235 
LYS HE3  H N N 236 
LYS HZ1  H N N 237 
LYS HZ2  H N N 238 
LYS HZ3  H N N 239 
LYS HXT  H N N 240 
MET N    N N N 241 
MET CA   C N S 242 
MET C    C N N 243 
MET O    O N N 244 
MET CB   C N N 245 
MET CG   C N N 246 
MET SD   S N N 247 
MET CE   C N N 248 
MET OXT  O N N 249 
MET H    H N N 250 
MET H2   H N N 251 
MET HA   H N N 252 
MET HB2  H N N 253 
MET HB3  H N N 254 
MET HG2  H N N 255 
MET HG3  H N N 256 
MET HE1  H N N 257 
MET HE2  H N N 258 
MET HE3  H N N 259 
MET HXT  H N N 260 
PHE N    N N N 261 
PHE CA   C N S 262 
PHE C    C N N 263 
PHE O    O N N 264 
PHE CB   C N N 265 
PHE CG   C Y N 266 
PHE CD1  C Y N 267 
PHE CD2  C Y N 268 
PHE CE1  C Y N 269 
PHE CE2  C Y N 270 
PHE CZ   C Y N 271 
PHE OXT  O N N 272 
PHE H    H N N 273 
PHE H2   H N N 274 
PHE HA   H N N 275 
PHE HB2  H N N 276 
PHE HB3  H N N 277 
PHE HD1  H N N 278 
PHE HD2  H N N 279 
PHE HE1  H N N 280 
PHE HE2  H N N 281 
PHE HZ   H N N 282 
PHE HXT  H N N 283 
PRO N    N N N 284 
PRO CA   C N S 285 
PRO C    C N N 286 
PRO O    O N N 287 
PRO CB   C N N 288 
PRO CG   C N N 289 
PRO CD   C N N 290 
PRO OXT  O N N 291 
PRO H    H N N 292 
PRO HA   H N N 293 
PRO HB2  H N N 294 
PRO HB3  H N N 295 
PRO HG2  H N N 296 
PRO HG3  H N N 297 
PRO HD2  H N N 298 
PRO HD3  H N N 299 
PRO HXT  H N N 300 
SER N    N N N 301 
SER CA   C N S 302 
SER C    C N N 303 
SER O    O N N 304 
SER CB   C N N 305 
SER OG   O N N 306 
SER OXT  O N N 307 
SER H    H N N 308 
SER H2   H N N 309 
SER HA   H N N 310 
SER HB2  H N N 311 
SER HB3  H N N 312 
SER HG   H N N 313 
SER HXT  H N N 314 
THR N    N N N 315 
THR CA   C N S 316 
THR C    C N N 317 
THR O    O N N 318 
THR CB   C N R 319 
THR OG1  O N N 320 
THR CG2  C N N 321 
THR OXT  O N N 322 
THR H    H N N 323 
THR H2   H N N 324 
THR HA   H N N 325 
THR HB   H N N 326 
THR HG1  H N N 327 
THR HG21 H N N 328 
THR HG22 H N N 329 
THR HG23 H N N 330 
THR HXT  H N N 331 
TRP N    N N N 332 
TRP CA   C N S 333 
TRP C    C N N 334 
TRP O    O N N 335 
TRP CB   C N N 336 
TRP CG   C Y N 337 
TRP CD1  C Y N 338 
TRP CD2  C Y N 339 
TRP NE1  N Y N 340 
TRP CE2  C Y N 341 
TRP CE3  C Y N 342 
TRP CZ2  C Y N 343 
TRP CZ3  C Y N 344 
TRP CH2  C Y N 345 
TRP OXT  O N N 346 
TRP H    H N N 347 
TRP H2   H N N 348 
TRP HA   H N N 349 
TRP HB2  H N N 350 
TRP HB3  H N N 351 
TRP HD1  H N N 352 
TRP HE1  H N N 353 
TRP HE3  H N N 354 
TRP HZ2  H N N 355 
TRP HZ3  H N N 356 
TRP HH2  H N N 357 
TRP HXT  H N N 358 
TYR N    N N N 359 
TYR CA   C N S 360 
TYR C    C N N 361 
TYR O    O N N 362 
TYR CB   C N N 363 
TYR CG   C Y N 364 
TYR CD1  C Y N 365 
TYR CD2  C Y N 366 
TYR CE1  C Y N 367 
TYR CE2  C Y N 368 
TYR CZ   C Y N 369 
TYR OH   O N N 370 
TYR OXT  O N N 371 
TYR H    H N N 372 
TYR H2   H N N 373 
TYR HA   H N N 374 
TYR HB2  H N N 375 
TYR HB3  H N N 376 
TYR HD1  H N N 377 
TYR HD2  H N N 378 
TYR HE1  H N N 379 
TYR HE2  H N N 380 
TYR HH   H N N 381 
TYR HXT  H N N 382 
VAL N    N N N 383 
VAL CA   C N S 384 
VAL C    C N N 385 
VAL O    O N N 386 
VAL CB   C N N 387 
VAL CG1  C N N 388 
VAL CG2  C N N 389 
VAL OXT  O N N 390 
VAL H    H N N 391 
VAL H2   H N N 392 
VAL HA   H N N 393 
VAL HB   H N N 394 
VAL HG11 H N N 395 
VAL HG12 H N N 396 
VAL HG13 H N N 397 
VAL HG21 H N N 398 
VAL HG22 H N N 399 
VAL HG23 H N N 400 
VAL HXT  H N N 401 
# 
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 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
HOX O   C    doub N N 139 
HOX CA  C    sing N N 140 
HOX C   OXT  sing N N 141 
HOX N   CA   sing N N 142 
HOX N   H    sing N N 143 
HOX N   H2   sing N N 144 
HOX OXT HXT  sing N N 145 
HOX CA  CB   sing N N 146 
HOX CA  HA   sing N N 147 
HOX CB  CG   sing N N 148 
HOX CB  HB   sing N N 149 
HOX CB  HBA  sing N N 150 
HOX CD1 CG   doub Y N 151 
HOX CG  CD2  sing Y N 152 
HOX CE1 CZ   doub Y N 153 
HOX CZ  CE2  sing Y N 154 
HOX CZ  NZ   sing N N 155 
HOX NZ  HNZ  sing N N 156 
HOX NZ  HNZA sing N N 157 
HOX CD1 CE1  sing Y N 158 
HOX CD1 HD1  sing N N 159 
HOX CD2 CE2  doub Y N 160 
HOX CD2 HD2  sing N N 161 
HOX CE1 HE1  sing N N 162 
HOX CE2 HE2  sing N N 163 
ILE N   CA   sing N N 164 
ILE N   H    sing N N 165 
ILE N   H2   sing N N 166 
ILE CA  C    sing N N 167 
ILE CA  CB   sing N N 168 
ILE CA  HA   sing N N 169 
ILE C   O    doub N N 170 
ILE C   OXT  sing N N 171 
ILE CB  CG1  sing N N 172 
ILE CB  CG2  sing N N 173 
ILE CB  HB   sing N N 174 
ILE CG1 CD1  sing N N 175 
ILE CG1 HG12 sing N N 176 
ILE CG1 HG13 sing N N 177 
ILE CG2 HG21 sing N N 178 
ILE CG2 HG22 sing N N 179 
ILE CG2 HG23 sing N N 180 
ILE CD1 HD11 sing N N 181 
ILE CD1 HD12 sing N N 182 
ILE CD1 HD13 sing N N 183 
ILE OXT HXT  sing N N 184 
LEU N   CA   sing N N 185 
LEU N   H    sing N N 186 
LEU N   H2   sing N N 187 
LEU CA  C    sing N N 188 
LEU CA  CB   sing N N 189 
LEU CA  HA   sing N N 190 
LEU C   O    doub N N 191 
LEU C   OXT  sing N N 192 
LEU CB  CG   sing N N 193 
LEU CB  HB2  sing N N 194 
LEU CB  HB3  sing N N 195 
LEU CG  CD1  sing N N 196 
LEU CG  CD2  sing N N 197 
LEU CG  HG   sing N N 198 
LEU CD1 HD11 sing N N 199 
LEU CD1 HD12 sing N N 200 
LEU CD1 HD13 sing N N 201 
LEU CD2 HD21 sing N N 202 
LEU CD2 HD22 sing N N 203 
LEU CD2 HD23 sing N N 204 
LEU OXT HXT  sing N N 205 
LYS N   CA   sing N N 206 
LYS N   H    sing N N 207 
LYS N   H2   sing N N 208 
LYS CA  C    sing N N 209 
LYS CA  CB   sing N N 210 
LYS CA  HA   sing N N 211 
LYS C   O    doub N N 212 
LYS C   OXT  sing N N 213 
LYS CB  CG   sing N N 214 
LYS CB  HB2  sing N N 215 
LYS CB  HB3  sing N N 216 
LYS CG  CD   sing N N 217 
LYS CG  HG2  sing N N 218 
LYS CG  HG3  sing N N 219 
LYS CD  CE   sing N N 220 
LYS CD  HD2  sing N N 221 
LYS CD  HD3  sing N N 222 
LYS CE  NZ   sing N N 223 
LYS CE  HE2  sing N N 224 
LYS CE  HE3  sing N N 225 
LYS NZ  HZ1  sing N N 226 
LYS NZ  HZ2  sing N N 227 
LYS NZ  HZ3  sing N N 228 
LYS OXT HXT  sing N N 229 
MET N   CA   sing N N 230 
MET N   H    sing N N 231 
MET N   H2   sing N N 232 
MET CA  C    sing N N 233 
MET CA  CB   sing N N 234 
MET CA  HA   sing N N 235 
MET C   O    doub N N 236 
MET C   OXT  sing N N 237 
MET CB  CG   sing N N 238 
MET CB  HB2  sing N N 239 
MET CB  HB3  sing N N 240 
MET CG  SD   sing N N 241 
MET CG  HG2  sing N N 242 
MET CG  HG3  sing N N 243 
MET SD  CE   sing N N 244 
MET CE  HE1  sing N N 245 
MET CE  HE2  sing N N 246 
MET CE  HE3  sing N N 247 
MET OXT HXT  sing N N 248 
PHE N   CA   sing N N 249 
PHE N   H    sing N N 250 
PHE N   H2   sing N N 251 
PHE CA  C    sing N N 252 
PHE CA  CB   sing N N 253 
PHE CA  HA   sing N N 254 
PHE C   O    doub N N 255 
PHE C   OXT  sing N N 256 
PHE CB  CG   sing N N 257 
PHE CB  HB2  sing N N 258 
PHE CB  HB3  sing N N 259 
PHE CG  CD1  doub Y N 260 
PHE CG  CD2  sing Y N 261 
PHE CD1 CE1  sing Y N 262 
PHE CD1 HD1  sing N N 263 
PHE CD2 CE2  doub Y N 264 
PHE CD2 HD2  sing N N 265 
PHE CE1 CZ   doub Y N 266 
PHE CE1 HE1  sing N N 267 
PHE CE2 CZ   sing Y N 268 
PHE CE2 HE2  sing N N 269 
PHE CZ  HZ   sing N N 270 
PHE OXT HXT  sing N N 271 
PRO N   CA   sing N N 272 
PRO N   CD   sing N N 273 
PRO N   H    sing N N 274 
PRO CA  C    sing N N 275 
PRO CA  CB   sing N N 276 
PRO CA  HA   sing N N 277 
PRO C   O    doub N N 278 
PRO C   OXT  sing N N 279 
PRO CB  CG   sing N N 280 
PRO CB  HB2  sing N N 281 
PRO CB  HB3  sing N N 282 
PRO CG  CD   sing N N 283 
PRO CG  HG2  sing N N 284 
PRO CG  HG3  sing N N 285 
PRO CD  HD2  sing N N 286 
PRO CD  HD3  sing N N 287 
PRO OXT HXT  sing N N 288 
SER N   CA   sing N N 289 
SER N   H    sing N N 290 
SER N   H2   sing N N 291 
SER CA  C    sing N N 292 
SER CA  CB   sing N N 293 
SER CA  HA   sing N N 294 
SER C   O    doub N N 295 
SER C   OXT  sing N N 296 
SER CB  OG   sing N N 297 
SER CB  HB2  sing N N 298 
SER CB  HB3  sing N N 299 
SER OG  HG   sing N N 300 
SER OXT HXT  sing N N 301 
THR N   CA   sing N N 302 
THR N   H    sing N N 303 
THR N   H2   sing N N 304 
THR CA  C    sing N N 305 
THR CA  CB   sing N N 306 
THR CA  HA   sing N N 307 
THR C   O    doub N N 308 
THR C   OXT  sing N N 309 
THR CB  OG1  sing N N 310 
THR CB  CG2  sing N N 311 
THR CB  HB   sing N N 312 
THR OG1 HG1  sing N N 313 
THR CG2 HG21 sing N N 314 
THR CG2 HG22 sing N N 315 
THR CG2 HG23 sing N N 316 
THR OXT HXT  sing N N 317 
TRP N   CA   sing N N 318 
TRP N   H    sing N N 319 
TRP N   H2   sing N N 320 
TRP CA  C    sing N N 321 
TRP CA  CB   sing N N 322 
TRP CA  HA   sing N N 323 
TRP C   O    doub N N 324 
TRP C   OXT  sing N N 325 
TRP CB  CG   sing N N 326 
TRP CB  HB2  sing N N 327 
TRP CB  HB3  sing N N 328 
TRP CG  CD1  doub Y N 329 
TRP CG  CD2  sing Y N 330 
TRP CD1 NE1  sing Y N 331 
TRP CD1 HD1  sing N N 332 
TRP CD2 CE2  doub Y N 333 
TRP CD2 CE3  sing Y N 334 
TRP NE1 CE2  sing Y N 335 
TRP NE1 HE1  sing N N 336 
TRP CE2 CZ2  sing Y N 337 
TRP CE3 CZ3  doub Y N 338 
TRP CE3 HE3  sing N N 339 
TRP CZ2 CH2  doub Y N 340 
TRP CZ2 HZ2  sing N N 341 
TRP CZ3 CH2  sing Y N 342 
TRP CZ3 HZ3  sing N N 343 
TRP CH2 HH2  sing N N 344 
TRP OXT HXT  sing N N 345 
TYR N   CA   sing N N 346 
TYR N   H    sing N N 347 
TYR N   H2   sing N N 348 
TYR CA  C    sing N N 349 
TYR CA  CB   sing N N 350 
TYR CA  HA   sing N N 351 
TYR C   O    doub N N 352 
TYR C   OXT  sing N N 353 
TYR CB  CG   sing N N 354 
TYR CB  HB2  sing N N 355 
TYR CB  HB3  sing N N 356 
TYR CG  CD1  doub Y N 357 
TYR CG  CD2  sing Y N 358 
TYR CD1 CE1  sing Y N 359 
TYR CD1 HD1  sing N N 360 
TYR CD2 CE2  doub Y N 361 
TYR CD2 HD2  sing N N 362 
TYR CE1 CZ   doub Y N 363 
TYR CE1 HE1  sing N N 364 
TYR CE2 CZ   sing Y N 365 
TYR CE2 HE2  sing N N 366 
TYR CZ  OH   sing N N 367 
TYR OH  HH   sing N N 368 
TYR OXT HXT  sing N N 369 
VAL N   CA   sing N N 370 
VAL N   H    sing N N 371 
VAL N   H2   sing N N 372 
VAL CA  C    sing N N 373 
VAL CA  CB   sing N N 374 
VAL CA  HA   sing N N 375 
VAL C   O    doub N N 376 
VAL C   OXT  sing N N 377 
VAL CB  CG1  sing N N 378 
VAL CB  CG2  sing N N 379 
VAL CB  HB   sing N N 380 
VAL CG1 HG11 sing N N 381 
VAL CG1 HG12 sing N N 382 
VAL CG1 HG13 sing N N 383 
VAL CG2 HG21 sing N N 384 
VAL CG2 HG22 sing N N 385 
VAL CG2 HG23 sing N N 386 
VAL OXT HXT  sing N N 387 
# 
_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                    9GKS 
_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]   0.009530 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001216 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.028326 
_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]   0.014786 
_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 
H 
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   ? 4.957  11.717  19.691  1.00 115.11 ? 4   ILE A N    1 
ATOM   2    C CA   . ILE A 1 4   ? 6.002  10.688  19.764  1.00 120.75 ? 4   ILE A CA   1 
ATOM   3    C C    . ILE A 1 4   ? 7.404  11.293  19.849  1.00 115.33 ? 4   ILE A C    1 
ATOM   4    O O    . ILE A 1 4   ? 7.784  12.090  18.990  1.00 109.76 ? 4   ILE A O    1 
ATOM   5    C CB   . ILE A 1 4   ? 5.931  9.732   18.531  1.00 119.90 ? 4   ILE A CB   1 
ATOM   6    C CG1  . ILE A 1 4   ? 4.614  8.952   18.545  1.00 117.10 ? 4   ILE A CG1  1 
ATOM   7    C CG2  . ILE A 1 4   ? 7.115  8.737   18.488  1.00 104.87 ? 4   ILE A CG2  1 
ATOM   8    C CD1  . ILE A 1 4   ? 4.478  8.016   19.762  1.00 110.27 ? 4   ILE A CD1  1 
ATOM   9    H HA   . ILE A 1 4   ? 5.844  10.186  20.579  1.00 144.98 ? 4   ILE A HA   1 
ATOM   10   H HB   . ILE A 1 4   ? 5.982  10.290  17.739  1.00 143.96 ? 4   ILE A HB   1 
ATOM   11   H HG12 . ILE A 1 4   ? 3.876  9.582   18.569  1.00 140.60 ? 4   ILE A HG12 1 
ATOM   12   H HG13 . ILE A 1 4   ? 4.561  8.410   17.743  1.00 140.60 ? 4   ILE A HG13 1 
ATOM   13   H HG21 . ILE A 1 4   ? 6.916  8.036   17.848  1.00 125.92 ? 4   ILE A HG21 1 
ATOM   14   H HG22 . ILE A 1 4   ? 7.917  9.212   18.219  1.00 125.92 ? 4   ILE A HG22 1 
ATOM   15   H HG23 . ILE A 1 4   ? 7.238  8.354   19.370  1.00 125.92 ? 4   ILE A HG23 1 
ATOM   16   H HD11 . ILE A 1 4   ? 3.694  7.457   19.644  1.00 132.41 ? 4   ILE A HD11 1 
ATOM   17   H HD12 . ILE A 1 4   ? 5.272  7.463   19.825  1.00 132.41 ? 4   ILE A HD12 1 
ATOM   18   H HD13 . ILE A 1 4   ? 4.383  8.553   20.564  1.00 132.41 ? 4   ILE A HD13 1 
ATOM   19   N N    . PRO A 1 5   ? 8.180  10.906  20.869  1.00 142.03 ? 5   PRO A N    1 
ATOM   20   C CA   . PRO A 1 5   ? 9.546  11.439  20.983  1.00 135.50 ? 5   PRO A CA   1 
ATOM   21   C C    . PRO A 1 5   ? 10.381 11.135  19.744  1.00 113.71 ? 5   PRO A C    1 
ATOM   22   O O    . PRO A 1 5   ? 10.209 10.103  19.088  1.00 105.79 ? 5   PRO A O    1 
ATOM   23   C CB   . PRO A 1 5   ? 10.109 10.743  22.237  1.00 132.69 ? 5   PRO A CB   1 
ATOM   24   C CG   . PRO A 1 5   ? 9.120  9.661   22.599  1.00 134.19 ? 5   PRO A CG   1 
ATOM   25   C CD   . PRO A 1 5   ? 7.798  10.097  22.045  1.00 129.63 ? 5   PRO A CD   1 
ATOM   26   H HA   . PRO A 1 5   ? 9.524  12.398  21.129  1.00 162.68 ? 5   PRO A HA   1 
ATOM   27   H HB2  . PRO A 1 5   ? 10.977 10.360  22.035  1.00 159.30 ? 5   PRO A HB2  1 
ATOM   28   H HB3  . PRO A 1 5   ? 10.190 11.388  22.958  1.00 159.30 ? 5   PRO A HB3  1 
ATOM   29   H HG2  . PRO A 1 5   ? 9.397  8.820   22.202  1.00 161.11 ? 5   PRO A HG2  1 
ATOM   30   H HG3  . PRO A 1 5   ? 9.074  9.572   23.564  1.00 161.11 ? 5   PRO A HG3  1 
ATOM   31   H HD2  . PRO A 1 5   ? 7.264  9.331   21.780  1.00 155.64 ? 5   PRO A HD2  1 
ATOM   32   H HD3  . PRO A 1 5   ? 7.311  10.633  22.691  1.00 155.64 ? 5   PRO A HD3  1 
ATOM   33   N N    . LYS A 1 6   ? 11.284 12.073  19.414  1.00 95.73  ? 6   LYS A N    1 
ATOM   34   C CA   . LYS A 1 6   ? 12.115 11.915  18.222  1.00 94.80  ? 6   LYS A CA   1 
ATOM   35   C C    . LYS A 1 6   ? 13.010 10.684  18.287  1.00 88.97  ? 6   LYS A C    1 
ATOM   36   O O    . LYS A 1 6   ? 13.332 10.097  17.253  1.00 84.62  ? 6   LYS A O    1 
ATOM   37   C CB   . LYS A 1 6   ? 13.010 13.127  17.974  1.00 98.46  ? 6   LYS A CB   1 
ATOM   38   C CG   . LYS A 1 6   ? 12.297 14.424  17.746  1.00 98.37  ? 6   LYS A CG   1 
ATOM   39   C CD   . LYS A 1 6   ? 13.296 15.480  17.296  1.00 106.06 ? 6   LYS A CD   1 
ATOM   40   C CE   . LYS A 1 6   ? 14.400 15.701  18.306  1.00 111.16 ? 6   LYS A CE   1 
ATOM   41   N NZ   . LYS A 1 6   ? 15.126 16.966  17.980  1.00 111.13 ? 6   LYS A NZ   1 
ATOM   42   H H    . LYS A 1 6   ? 11.429 12.796  19.857  1.00 114.95 ? 6   LYS A H    1 
ATOM   43   H HA   . LYS A 1 6   ? 11.493 11.830  17.483  1.00 113.84 ? 6   LYS A HA   1 
ATOM   44   H HB2  . LYS A 1 6   ? 13.583 13.246  18.748  1.00 118.23 ? 6   LYS A HB2  1 
ATOM   45   H HB3  . LYS A 1 6   ? 13.548 12.952  17.186  1.00 118.23 ? 6   LYS A HB3  1 
ATOM   46   H HG2  . LYS A 1 6   ? 11.625 14.313  17.055  1.00 118.12 ? 6   LYS A HG2  1 
ATOM   47   H HG3  . LYS A 1 6   ? 11.879 14.719  18.570  1.00 118.12 ? 6   LYS A HG3  1 
ATOM   48   H HD2  . LYS A 1 6   ? 13.704 15.195  16.463  1.00 127.35 ? 6   LYS A HD2  1 
ATOM   49   H HD3  . LYS A 1 6   ? 12.833 16.322  17.168  1.00 127.35 ? 6   LYS A HD3  1 
ATOM   50   H HE2  . LYS A 1 6   ? 14.021 15.778  19.196  1.00 133.46 ? 6   LYS A HE2  1 
ATOM   51   H HE3  . LYS A 1 6   ? 15.027 14.962  18.275  1.00 133.46 ? 6   LYS A HE3  1 
ATOM   52   H HZ1  . LYS A 1 6   ? 15.760 17.118  18.586  1.00 133.44 ? 6   LYS A HZ1  1 
ATOM   53   H HZ2  . LYS A 1 6   ? 15.504 16.902  17.177  1.00 133.44 ? 6   LYS A HZ2  1 
ATOM   54   H HZ3  . LYS A 1 6   ? 14.558 17.651  17.978  1.00 133.44 ? 6   LYS A HZ3  1 
ATOM   55   N N    . GLU A 1 7   ? 13.460 10.308  19.476  1.00 88.38  ? 7   GLU A N    1 
ATOM   56   C CA   . GLU A 1 7   ? 14.299 9.128   19.572  1.00 85.12  ? 7   GLU A CA   1 
ATOM   57   C C    . GLU A 1 7   ? 13.550 7.884   19.114  1.00 77.87  ? 7   GLU A C    1 
ATOM   58   O O    . GLU A 1 7   ? 14.171 6.956   18.585  1.00 71.40  ? 7   GLU A O    1 
ATOM   59   C CB   . GLU A 1 7   ? 14.769 8.938   21.008  1.00 88.00  ? 7   GLU A CB   1 
ATOM   60   C CG   . GLU A 1 7   ? 15.518 10.141  21.617  1.00 95.91  ? 7   GLU A CG   1 
ATOM   61   C CD   . GLU A 1 7   ? 14.581 11.244  22.136  1.00 101.16 ? 7   GLU A CD   1 
ATOM   62   O OE1  . GLU A 1 7   ? 13.525 10.895  22.729  1.00 95.42  ? 7   GLU A OE1  1 
ATOM   63   O OE2  . GLU A 1 7   ? 14.883 12.447  21.910  1.00 103.62 ? 7   GLU A OE2  1 
ATOM   64   H H    . GLU A 1 7   ? 13.299 10.707  20.220  1.00 106.14 ? 7   GLU A H    1 
ATOM   65   H HA   . GLU A 1 7   ? 15.078 9.251   19.008  1.00 102.22 ? 7   GLU A HA   1 
ATOM   66   H HB2  . GLU A 1 7   ? 13.993 8.767   21.565  1.00 105.68 ? 7   GLU A HB2  1 
ATOM   67   H HB3  . GLU A 1 7   ? 15.371 8.178   21.035  1.00 105.68 ? 7   GLU A HB3  1 
ATOM   68   H HG2  . GLU A 1 7   ? 16.055 9.831   22.363  1.00 115.17 ? 7   GLU A HG2  1 
ATOM   69   H HG3  . GLU A 1 7   ? 16.089 10.532  20.937  1.00 115.17 ? 7   GLU A HG3  1 
ATOM   70   N N    . MET A 1 8   ? 12.221 7.871   19.265  1.00 77.44  ? 8   MET A N    1 
ATOM   71   C CA   . MET A 1 8   ? 11.428 6.686   18.969  1.00 75.22  ? 8   MET A CA   1 
ATOM   72   C C    . MET A 1 8   ? 11.203 6.555   17.477  1.00 66.90  ? 8   MET A C    1 
ATOM   73   O O    . MET A 1 8   ? 11.327 5.464   16.917  1.00 60.57  ? 8   MET A O    1 
ATOM   74   C CB   . MET A 1 8   ? 10.103 6.740   19.728  1.00 78.33  ? 8   MET A CB   1 
ATOM   75   C CG   . MET A 1 8   ? 9.332  5.434   19.732  1.00 84.38  ? 8   MET A CG   1 
ATOM   76   S SD   . MET A 1 8   ? 8.112  5.347   21.065  1.00 84.53  ? 8   MET A SD   1 
ATOM   77   C CE   . MET A 1 8   ? 9.189  5.503   22.473  1.00 98.97  ? 8   MET A CE   1 
ATOM   78   H H    . MET A 1 8   ? 11.756 8.541   19.538  1.00 93.01  ? 8   MET A H    1 
ATOM   79   H HA   . MET A 1 8   ? 11.896 5.897   19.283  1.00 90.34  ? 8   MET A HA   1 
ATOM   80   H HB2  . MET A 1 8   ? 10.284 6.977   20.651  1.00 94.07  ? 8   MET A HB2  1 
ATOM   81   H HB3  . MET A 1 8   ? 9.538  7.413   19.317  1.00 94.07  ? 8   MET A HB3  1 
ATOM   82   H HG2  . MET A 1 8   ? 8.862  5.341   18.888  1.00 101.33 ? 8   MET A HG2  1 
ATOM   83   H HG3  . MET A 1 8   ? 9.955  4.699   19.847  1.00 101.33 ? 8   MET A HG3  1 
ATOM   84   H HE1  . MET A 1 8   ? 8.872  4.918   23.179  1.00 118.85 ? 8   MET A HE1  1 
ATOM   85   H HE2  . MET A 1 8   ? 10.088 5.250   22.212  1.00 118.85 ? 8   MET A HE2  1 
ATOM   86   H HE3  . MET A 1 8   ? 9.179  6.424   22.777  1.00 118.85 ? 8   MET A HE3  1 
ATOM   87   N N    . LEU A 1 9   ? 10.882 7.652   16.813  1.00 72.06  ? 9   LEU A N    1 
ATOM   88   C CA   . LEU A 1 9   ? 10.749 7.612   15.369  1.00 69.43  ? 9   LEU A CA   1 
ATOM   89   C C    . LEU A 1 9   ? 12.065 7.253   14.681  1.00 66.58  ? 9   LEU A C    1 
ATOM   90   O O    . LEU A 1 9   ? 12.055 6.568   13.657  1.00 64.19  ? 9   LEU A O    1 
ATOM   91   C CB   . LEU A 1 9   ? 10.234 8.950   14.874  1.00 76.39  ? 9   LEU A CB   1 
ATOM   92   C CG   . LEU A 1 9   ? 8.814  9.249   15.384  1.00 86.34  ? 9   LEU A CG   1 
ATOM   93   C CD1  . LEU A 1 9   ? 8.378  10.659  14.937  1.00 90.78  ? 9   LEU A CD1  1 
ATOM   94   C CD2  . LEU A 1 9   ? 7.800  8.173   14.925  1.00 83.58  ? 9   LEU A CD2  1 
ATOM   95   H H    . LEU A 1 9   ? 10.738 8.421   17.170  1.00 86.55  ? 9   LEU A H    1 
ATOM   96   H HA   . LEU A 1 9   ? 10.106 6.925   15.134  1.00 83.39  ? 9   LEU A HA   1 
ATOM   97   H HB2  . LEU A 1 9   ? 10.824 9.653   15.188  1.00 91.74  ? 9   LEU A HB2  1 
ATOM   98   H HB3  . LEU A 1 9   ? 10.213 8.943   13.904  1.00 91.74  ? 9   LEU A HB3  1 
ATOM   99   H HG   . LEU A 1 9   ? 8.820  9.226   16.354  1.00 103.68 ? 9   LEU A HG   1 
ATOM   100  H HD11 . LEU A 1 9   ? 7.492  10.843  15.289  1.00 109.02 ? 9   LEU A HD11 1 
ATOM   101  H HD12 . LEU A 1 9   ? 9.011  11.310  15.280  1.00 109.02 ? 9   LEU A HD12 1 
ATOM   102  H HD13 . LEU A 1 9   ? 8.362  10.692  13.968  1.00 109.02 ? 9   LEU A HD13 1 
ATOM   103  H HD21 . LEU A 1 9   ? 6.905  8.543   14.970  1.00 100.38 ? 9   LEU A HD21 1 
ATOM   104  H HD22 . LEU A 1 9   ? 8.006  7.914   14.013  1.00 100.38 ? 9   LEU A HD22 1 
ATOM   105  H HD23 . LEU A 1 9   ? 7.870  7.403   15.511  1.00 100.38 ? 9   LEU A HD23 1 
ATOM   106  N N    . ARG A 1 10  ? 13.191 7.767   15.188  1.00 64.66  ? 10  ARG A N    1 
ATOM   107  C CA   . ARG A 1 10  ? 14.507 7.353   14.703  1.00 58.48  ? 10  ARG A CA   1 
ATOM   108  C C    . ARG A 1 10  ? 14.688 5.857   14.916  1.00 58.46  ? 10  ARG A C    1 
ATOM   109  O O    . ARG A 1 10  ? 15.106 5.129   14.005  1.00 49.40  ? 10  ARG A O    1 
ATOM   110  C CB   . ARG A 1 10  ? 15.605 8.169   15.407  1.00 66.93  ? 10  ARG A CB   1 
ATOM   111  C CG   . ARG A 1 10  ? 17.081 7.918   14.978  1.00 73.48  ? 10  ARG A CG   1 
ATOM   112  C CD   . ARG A 1 10  ? 17.331 8.352   13.499  1.00 85.24  ? 10  ARG A CD   1 
ATOM   113  N NE   . ARG A 1 10  ? 18.630 8.955   13.183  1.00 90.89  ? 10  ARG A NE   1 
ATOM   114  C CZ   . ARG A 1 10  ? 19.691 8.302   12.715  1.00 84.98  ? 10  ARG A CZ   1 
ATOM   115  N NH1  . ARG A 1 10  ? 19.676 6.985   12.555  1.00 67.24  ? 10  ARG A NH1  1 
ATOM   116  N NH2  . ARG A 1 10  ? 20.785 8.984   12.381  1.00 102.01 ? 10  ARG A NH2  1 
ATOM   117  H H    . ARG A 1 10  ? 13.220 8.358   15.812  1.00 77.67  ? 10  ARG A H    1 
ATOM   118  H HA   . ARG A 1 10  ? 14.589 7.533   13.754  1.00 70.25  ? 10  ARG A HA   1 
ATOM   119  H HB2  . ARG A 1 10  ? 15.424 9.108   15.248  1.00 80.39  ? 10  ARG A HB2  1 
ATOM   120  H HB3  . ARG A 1 10  ? 15.554 7.978   16.357  1.00 80.39  ? 10  ARG A HB3  1 
ATOM   121  H HG2  . ARG A 1 10  ? 17.673 8.430   15.550  1.00 88.25  ? 10  ARG A HG2  1 
ATOM   122  H HG3  . ARG A 1 10  ? 17.281 6.972   15.056  1.00 88.25  ? 10  ARG A HG3  1 
ATOM   123  H HD2  . ARG A 1 10  ? 17.244 7.565   12.939  1.00 102.37 ? 10  ARG A HD2  1 
ATOM   124  H HD3  . ARG A 1 10  ? 16.654 9.005   13.262  1.00 102.37 ? 10  ARG A HD3  1 
ATOM   125  H HE   . ARG A 1 10  ? 18.713 9.801   13.311  1.00 109.15 ? 10  ARG A HE   1 
ATOM   126  H HH11 . ARG A 1 10  ? 18.971 6.536   12.755  1.00 80.77  ? 10  ARG A HH11 1 
ATOM   127  H HH12 . ARG A 1 10  ? 20.372 6.581   12.251  1.00 80.77  ? 10  ARG A HH12 1 
ATOM   128  H HH21 . ARG A 1 10  ? 20.802 9.840   12.469  1.00 122.49 ? 10  ARG A HH21 1 
ATOM   129  H HH22 . ARG A 1 10  ? 21.475 8.569   12.078  1.00 122.49 ? 10  ARG A HH22 1 
ATOM   130  N N    . ALA A 1 11  ? 14.313 5.352   16.093  1.00 56.36  ? 11  ALA A N    1 
ATOM   131  C CA   . ALA A 1 11  ? 14.480 3.928   16.334  1.00 51.82  ? 11  ALA A CA   1 
ATOM   132  C C    . ALA A 1 11  ? 13.607 3.100   15.409  1.00 48.56  ? 11  ALA A C    1 
ATOM   133  O O    . ALA A 1 11  ? 14.042 2.041   14.917  1.00 46.46  ? 11  ALA A O    1 
ATOM   134  C CB   . ALA A 1 11  ? 14.179 3.593   17.785  1.00 63.45  ? 11  ALA A CB   1 
ATOM   135  H H    . ALA A 1 11  ? 13.972 5.800   16.743  1.00 67.71  ? 11  ALA A H    1 
ATOM   136  H HA   . ALA A 1 11  ? 15.406 3.699   16.161  1.00 62.27  ? 11  ALA A HA   1 
ATOM   137  H HB1  . ALA A 1 11  ? 14.318 2.644   17.925  1.00 76.22  ? 11  ALA A HB1  1 
ATOM   138  H HB2  . ALA A 1 11  ? 14.774 4.103   18.356  1.00 76.22  ? 11  ALA A HB2  1 
ATOM   139  H HB3  . ALA A 1 11  ? 13.257 3.825   17.978  1.00 76.22  ? 11  ALA A HB3  1 
ATOM   140  N N    . GLN A 1 12  ? 12.384 3.553   15.123  1.00 49.53  ? 12  GLN A N    1 
ATOM   141  C CA   . GLN A 1 12  ? 11.492 2.771   14.244  1.00 49.05  ? 12  GLN A CA   1 
ATOM   142  C C    . GLN A 1 12  ? 11.994 2.702   12.786  1.00 43.39  ? 12  GLN A C    1 
ATOM   143  O O    . GLN A 1 12  ? 11.879 1.683   12.127  1.00 42.46  ? 12  GLN A O    1 
ATOM   144  C CB   . GLN A 1 12  ? 10.095 3.388   14.322  1.00 53.41  ? 12  GLN A CB   1 
ATOM   145  C CG   . GLN A 1 12  ? 9.362  3.121   15.648  1.00 59.47  ? 12  GLN A CG   1 
ATOM   146  C CD   . GLN A 1 12  ? 8.080  3.931   15.869  1.00 64.27  ? 12  GLN A CD   1 
ATOM   147  O OE1  . GLN A 1 12  ? 7.322  3.641   16.810  1.00 70.15  ? 12  GLN A OE1  1 
ATOM   148  N NE2  . GLN A 1 12  ? 7.894  4.999   15.109  1.00 63.47  ? 12  GLN A NE2  1 
ATOM   149  H H    . GLN A 1 12  ? 12.048 4.290   15.415  1.00 59.51  ? 12  GLN A H    1 
ATOM   150  H HA   . GLN A 1 12  ? 11.461 1.852   14.552  1.00 58.94  ? 12  GLN A HA   1 
ATOM   151  H HB2  . GLN A 1 12  ? 10.174 4.349   14.218  1.00 64.17  ? 12  GLN A HB2  1 
ATOM   152  H HB3  . GLN A 1 12  ? 9.552  3.021   13.607  1.00 64.17  ? 12  GLN A HB3  1 
ATOM   153  H HG2  . GLN A 1 12  ? 9.119  2.183   15.678  1.00 71.45  ? 12  GLN A HG2  1 
ATOM   154  H HG3  . GLN A 1 12  ? 9.965  3.332   16.378  1.00 71.45  ? 12  GLN A HG3  1 
ATOM   155  H HE21 . GLN A 1 12  ? 8.481  5.214   14.519  1.00 76.24  ? 12  GLN A HE21 1 
ATOM   156  H HE22 . GLN A 1 12  ? 7.185  5.477   15.206  1.00 76.24  ? 12  GLN A HE22 1 
ATOM   157  N N    . THR A 1 13  ? 12.472 3.821   12.261  1.00 43.65  ? 13  THR A N    1 
ATOM   158  C CA   . THR A 1 13  ? 13.043 3.874   10.938  1.00 46.16  ? 13  THR A CA   1 
ATOM   159  C C    . THR A 1 13  ? 14.295 3.011   10.817  1.00 47.04  ? 13  THR A C    1 
ATOM   160  O O    . THR A 1 13  ? 14.499 2.404   9.774   1.00 39.86  ? 13  THR A O    1 
ATOM   161  C CB   . THR A 1 13  ? 13.433 5.335   10.627  1.00 49.61  ? 13  THR A CB   1 
ATOM   162  O OG1  . THR A 1 13  ? 12.318 6.186   10.830  1.00 51.51  ? 13  THR A OG1  1 
ATOM   163  C CG2  . THR A 1 13  ? 13.920 5.518   9.174   1.00 48.78  ? 13  THR A CG2  1 
ATOM   164  H H    . THR A 1 13  ? 12.476 4.581   12.664  1.00 52.46  ? 13  THR A H    1 
ATOM   165  H HA   . THR A 1 13  ? 12.381 3.549   10.307  1.00 55.47  ? 13  THR A HA   1 
ATOM   166  H HB   . THR A 1 13  ? 14.161 5.576   11.221  1.00 59.61  ? 13  THR A HB   1 
ATOM   167  H HG1  . THR A 1 13  ? 12.106 6.192   11.642  1.00 61.89  ? 13  THR A HG1  1 
ATOM   168  H HG21 . THR A 1 13  ? 14.092 6.457   8.998   1.00 58.61  ? 13  THR A HG21 1 
ATOM   169  H HG22 . THR A 1 13  ? 14.737 5.016   9.032   1.00 58.61  ? 13  THR A HG22 1 
ATOM   170  H HG23 . THR A 1 13  ? 13.244 5.201   8.555   1.00 58.61  ? 13  THR A HG23 1 
ATOM   171  N N    . ASN A 1 14  ? 15.204 3.037   11.801  1.00 46.82  ? 14  ASN A N    1 
ATOM   172  C CA   . ASN A 1 14  ? 16.383 2.165   11.771  1.00 44.80  ? 14  ASN A CA   1 
ATOM   173  C C    . ASN A 1 14  ? 15.942 0.746   11.752  1.00 43.51  ? 14  ASN A C    1 
ATOM   174  O O    . ASN A 1 14  ? 16.430 -0.051  10.969  1.00 42.74  ? 14  ASN A O    1 
ATOM   175  C CB   . ASN A 1 14  ? 17.283 2.378   12.948  1.00 46.36  ? 14  ASN A CB   1 
ATOM   176  C CG   . ASN A 1 14  ? 18.110 3.587   12.785  1.00 52.69  ? 14  ASN A CG   1 
ATOM   177  O OD1  . ASN A 1 14  ? 17.573 4.692   12.618  1.00 55.96  ? 14  ASN A OD1  1 
ATOM   178  N ND2  . ASN A 1 14  ? 19.417 3.413   12.753  1.00 54.87  ? 14  ASN A ND2  1 
ATOM   179  H H    . ASN A 1 14  ? 15.160 3.548   12.492  1.00 56.27  ? 14  ASN A H    1 
ATOM   180  H HA   . ASN A 1 14  ? 16.901 2.376   10.978  1.00 53.83  ? 14  ASN A HA   1 
ATOM   181  H HB2  . ASN A 1 14  ? 16.745 2.481   13.748  1.00 55.71  ? 14  ASN A HB2  1 
ATOM   182  H HB3  . ASN A 1 14  ? 17.874 1.614   13.041  1.00 55.71  ? 14  ASN A HB3  1 
ATOM   183  H HD21 . ASN A 1 14  ? 19.938 4.090   12.659  1.00 65.92  ? 14  ASN A HD21 1 
ATOM   184  H HD22 . ASN A 1 14  ? 19.747 2.622   12.825  1.00 65.92  ? 14  ASN A HD22 1 
HETATM 185  O O    . HOX A 1 15  ? 14.148 -2.629  10.765  1.00 42.03  ? 15  HOX A O    1 
HETATM 186  C C    . HOX A 1 15  ? 13.971 -1.475  11.237  1.00 42.27  ? 15  HOX A C    1 
HETATM 187  N N    . HOX A 1 15  ? 14.967 0.408   12.591  1.00 42.56  ? 15  HOX A N    1 
HETATM 188  C CA   . HOX A 1 15  ? 14.470 -0.968  12.610  1.00 41.80  ? 15  HOX A CA   1 
HETATM 189  C CB   . HOX A 1 15  ? 13.316 -1.079  13.663  1.00 40.52  ? 15  HOX A CB   1 
HETATM 190  C CG   . HOX A 1 15  ? 12.760 -2.467  13.773  1.00 39.96  ? 15  HOX A CG   1 
HETATM 191  C CZ   . HOX A 1 15  ? 11.720 -5.074  13.905  1.00 42.39  ? 15  HOX A CZ   1 
HETATM 192  N NZ   . HOX A 1 15  ? 11.279 -6.383  13.997  1.00 47.69  ? 15  HOX A NZ   1 
HETATM 193  C CD1  . HOX A 1 15  ? 13.598 -3.533  13.990  1.00 43.49  ? 15  HOX A CD1  1 
HETATM 194  C CD2  . HOX A 1 15  ? 11.391 -2.691  13.651  1.00 47.62  ? 15  HOX A CD2  1 
HETATM 195  C CE1  . HOX A 1 15  ? 13.106 -4.835  14.058  1.00 43.62  ? 15  HOX A CE1  1 
HETATM 196  C CE2  . HOX A 1 15  ? 10.848 -3.980  13.703  1.00 44.31  ? 15  HOX A CE2  1 
HETATM 197  H HA   . HOX A 1 15  ? 15.315 -1.695  12.814  1.00 50.23  ? 15  HOX A HA   1 
HETATM 198  H HB   . HOX A 1 15  ? 12.496 -0.369  13.373  1.00 48.70  ? 15  HOX A HB   1 
HETATM 199  H HBA  . HOX A 1 15  ? 13.709 -0.753  14.662  1.00 48.70  ? 15  HOX A HBA  1 
HETATM 200  H HNZ  . HOX A 1 15  ? 11.928 -7.124  14.125  1.00 57.30  ? 15  HOX A HNZ  1 
HETATM 201  H HNZA . HOX A 1 15  ? 10.301 -6.597  13.949  1.00 57.30  ? 15  HOX A HNZA 1 
HETATM 202  H HD1  . HOX A 1 15  ? 14.678 -3.358  14.113  1.00 52.27  ? 15  HOX A HD1  1 
HETATM 203  H HD2  . HOX A 1 15  ? 10.715 -1.834  13.510  1.00 57.22  ? 15  HOX A HD2  1 
HETATM 204  H HE1  . HOX A 1 15  ? 13.798 -5.671  14.231  1.00 52.42  ? 15  HOX A HE1  1 
HETATM 205  H HE2  . HOX A 1 15  ? 9.765  -4.132  13.589  1.00 53.25  ? 15  HOX A HE2  1 
ATOM   206  N N    . ILE A 1 16  ? 13.225 -0.604  10.577  1.00 37.69  ? 16  ILE A N    1 
ATOM   207  C CA   . ILE A 1 16  ? 12.529 -0.975  9.335   1.00 43.60  ? 16  ILE A CA   1 
ATOM   208  C C    . ILE A 1 16  ? 13.550 -1.211  8.239   1.00 39.11  ? 16  ILE A C    1 
ATOM   209  O O    . ILE A 1 16  ? 13.527 -2.208  7.487   1.00 42.26  ? 16  ILE A O    1 
ATOM   210  C CB   . ILE A 1 16  ? 11.550 0.137   8.920   1.00 43.90  ? 16  ILE A CB   1 
ATOM   211  C CG1  . ILE A 1 16  ? 10.271 0.033   9.733   1.00 41.67  ? 16  ILE A CG1  1 
ATOM   212  C CG2  . ILE A 1 16  ? 11.192 0.046   7.414   1.00 44.32  ? 16  ILE A CG2  1 
ATOM   213  C CD1  . ILE A 1 16  ? 9.396  1.276   9.777   1.00 45.99  ? 16  ILE A CD1  1 
ATOM   214  H H    . ILE A 1 16  ? 13.100 0.211   10.819  1.00 45.30  ? 16  ILE A H    1 
ATOM   215  H HA   . ILE A 1 16  ? 12.024 -1.791  9.477   1.00 52.40  ? 16  ILE A HA   1 
ATOM   216  H HB   . ILE A 1 16  ? 11.989 0.985   9.088   1.00 52.75  ? 16  ILE A HB   1 
ATOM   217  H HG12 . ILE A 1 16  ? 9.733  -0.681  9.358   1.00 50.08  ? 16  ILE A HG12 1 
ATOM   218  H HG13 . ILE A 1 16  ? 10.512 -0.178  10.648  1.00 50.08  ? 16  ILE A HG13 1 
ATOM   219  H HG21 . ILE A 1 16  ? 10.389 0.565   7.249   1.00 53.26  ? 16  ILE A HG21 1 
ATOM   220  H HG22 . ILE A 1 16  ? 11.928 0.401   6.892   1.00 53.26  ? 16  ILE A HG22 1 
ATOM   221  H HG23 . ILE A 1 16  ? 11.039 -0.883  7.181   1.00 53.26  ? 16  ILE A HG23 1 
ATOM   222  H HD11 . ILE A 1 16  ? 8.643  1.111   10.366  1.00 55.27  ? 16  ILE A HD11 1 
ATOM   223  H HD12 . ILE A 1 16  ? 9.920  2.020   10.112  1.00 55.27  ? 16  ILE A HD12 1 
ATOM   224  H HD13 . ILE A 1 16  ? 9.079  1.471   8.881   1.00 55.27  ? 16  ILE A HD13 1 
ATOM   225  N N    . LEU A 1 17  ? 14.497 -0.281  8.188   1.00 40.14  ? 17  LEU A N    1 
ATOM   226  C CA   . LEU A 1 17  ? 15.567 -0.353  7.196   1.00 41.51  ? 17  LEU A CA   1 
ATOM   227  C C    . LEU A 1 17  ? 16.389 -1.614  7.381   1.00 41.96  ? 17  LEU A C    1 
ATOM   228  O O    . LEU A 1 17  ? 16.700 -2.317  6.425   1.00 36.69  ? 17  LEU A O    1 
ATOM   229  C CB   . LEU A 1 17  ? 16.458 0.879   7.319   1.00 37.14  ? 17  LEU A CB   1 
ATOM   230  C CG   . LEU A 1 17  ? 15.710 2.106   6.820   1.00 41.64  ? 17  LEU A CG   1 
ATOM   231  C CD1  . LEU A 1 17  ? 16.600 3.356   6.998   1.00 41.28  ? 17  LEU A CD1  1 
ATOM   232  C CD2  . LEU A 1 17  ? 15.364 2.004   5.366   1.00 40.30  ? 17  LEU A CD2  1 
ATOM   233  H H    . LEU A 1 17  ? 14.545 0.400   8.712   1.00 48.24  ? 17  LEU A H    1 
ATOM   234  H HA   . LEU A 1 17  ? 15.177 -0.369  6.308   1.00 49.89  ? 17  LEU A HA   1 
ATOM   235  H HB2  . LEU A 1 17  ? 16.700 1.015   8.248   1.00 44.65  ? 17  LEU A HB2  1 
ATOM   236  H HB3  . LEU A 1 17  ? 17.257 0.759   6.782   1.00 44.65  ? 17  LEU A HB3  1 
ATOM   237  H HG   . LEU A 1 17  ? 14.888 2.179   7.332   1.00 50.04  ? 17  LEU A HG   1 
ATOM   238  H HD11 . LEU A 1 17  ? 16.122 4.134   6.669   1.00 49.61  ? 17  LEU A HD11 1 
ATOM   239  H HD12 . LEU A 1 17  ? 16.803 3.468   7.940   1.00 49.61  ? 17  LEU A HD12 1 
ATOM   240  H HD13 . LEU A 1 17  ? 17.420 3.234   6.495   1.00 49.61  ? 17  LEU A HD13 1 
ATOM   241  H HD21 . LEU A 1 17  ? 15.125 2.884   5.035   1.00 48.43  ? 17  LEU A HD21 1 
ATOM   242  H HD22 . LEU A 1 17  ? 16.134 1.667   4.881   1.00 48.43  ? 17  LEU A HD22 1 
ATOM   243  H HD23 . LEU A 1 17  ? 14.615 1.396   5.261   1.00 48.43  ? 17  LEU A HD23 1 
ATOM   244  N N    . LEU A 1 18  ? 16.767 -1.911  8.619   1.00 42.80  ? 18  LEU A N    1 
ATOM   245  C CA   . LEU A 1 18  ? 17.543 -3.115  8.868   1.00 40.94  ? 18  LEU A CA   1 
ATOM   246  C C    . LEU A 1 18  ? 16.729 -4.346  8.611   1.00 42.46  ? 18  LEU A C    1 
ATOM   247  O O    . LEU A 1 18  ? 17.312 -5.368  8.233   1.00 42.79  ? 18  LEU A O    1 
ATOM   248  C CB   . LEU A 1 18  ? 18.064 -3.131  10.287  1.00 46.71  ? 18  LEU A CB   1 
ATOM   249  C CG   . LEU A 1 18  ? 19.202 -2.134  10.514  1.00 41.84  ? 18  LEU A CG   1 
ATOM   250  C CD1  . LEU A 1 18  ? 19.474 -1.981  11.978  1.00 45.92  ? 18  LEU A CD1  1 
ATOM   251  C CD2  . LEU A 1 18  ? 20.445 -2.655  9.772   1.00 43.61  ? 18  LEU A CD2  1 
ATOM   252  H H    . LEU A 1 18  ? 16.591 -1.442  9.317   1.00 51.44  ? 18  LEU A H    1 
ATOM   253  H HA   . LEU A 1 18  ? 18.309 -3.116  8.273   1.00 49.21  ? 18  LEU A HA   1 
ATOM   254  H HB2  . LEU A 1 18  ? 17.339 -2.903  10.890  1.00 56.13  ? 18  LEU A HB2  1 
ATOM   255  H HB3  . LEU A 1 18  ? 18.398 -4.019  10.490  1.00 56.13  ? 18  LEU A HB3  1 
ATOM   256  H HG   . LEU A 1 18  ? 18.967 -1.255  10.175  1.00 50.28  ? 18  LEU A HG   1 
ATOM   257  H HD11 . LEU A 1 18  ? 20.206 -1.356  12.099  1.00 55.18  ? 18  LEU A HD11 1 
ATOM   258  H HD12 . LEU A 1 18  ? 18.676 -1.644  12.414  1.00 55.18  ? 18  LEU A HD12 1 
ATOM   259  H HD13 . LEU A 1 18  ? 19.713 -2.845  12.347  1.00 55.18  ? 18  LEU A HD13 1 
ATOM   260  H HD21 . LEU A 1 18  ? 21.218 -2.139  10.049  1.00 52.40  ? 18  LEU A HD21 1 
ATOM   261  H HD22 . LEU A 1 18  ? 20.575 -3.591  9.992   1.00 52.40  ? 18  LEU A HD22 1 
ATOM   262  H HD23 . LEU A 1 18  ? 20.307 -2.556  8.816   1.00 52.40  ? 18  LEU A HD23 1 
ATOM   263  N N    . MET A 1 19  ? 15.410 -4.290  8.772   1.00 39.23  ? 19  MET A N    1 
ATOM   264  C CA   . MET A 1 19  ? 14.622 -5.481  8.459   1.00 41.98  ? 19  MET A CA   1 
ATOM   265  C C    . MET A 1 19  ? 14.496 -5.695  6.943   1.00 43.58  ? 19  MET A C    1 
ATOM   266  O O    . MET A 1 19  ? 14.485 -6.830  6.459   1.00 48.10  ? 19  MET A O    1 
ATOM   267  C CB   . MET A 1 19  ? 13.267 -5.425  9.150   1.00 45.95  ? 19  MET A CB   1 
ATOM   268  C CG   . MET A 1 19  ? 13.314 -5.737  10.693  1.00 46.68  ? 19  MET A CG   1 
ATOM   269  S SD   . MET A 1 19  ? 13.789 -7.384  11.015  1.00 51.09  ? 19  MET A SD   1 
ATOM   270  C CE   . MET A 1 19  ? 12.355 -8.266  10.438  1.00 48.84  ? 19  MET A CE   1 
ATOM   271  H H    . MET A 1 19  ? 14.965 -3.608  9.048   1.00 47.16  ? 19  MET A H    1 
ATOM   272  H HA   . MET A 1 19  ? 15.079 -6.255  8.824   1.00 50.45  ? 19  MET A HA   1 
ATOM   273  H HB2  . MET A 1 19  ? 12.900 -4.533  9.042   1.00 55.21  ? 19  MET A HB2  1 
ATOM   274  H HB3  . MET A 1 19  ? 12.681 -6.077  8.736   1.00 55.21  ? 19  MET A HB3  1 
ATOM   275  H HG2  . MET A 1 19  ? 13.957 -5.148  11.118  1.00 56.09  ? 19  MET A HG2  1 
ATOM   276  H HG3  . MET A 1 19  ? 12.433 -5.596  11.074  1.00 56.09  ? 19  MET A HG3  1 
ATOM   277  H HE1  . MET A 1 19  ? 12.444 -9.203  10.673  1.00 58.68  ? 19  MET A HE1  1 
ATOM   278  H HE2  . MET A 1 19  ? 11.564 -7.893  10.859  1.00 58.68  ? 19  MET A HE2  1 
ATOM   279  H HE3  . MET A 1 19  ? 12.292 -8.172  9.475   1.00 58.68  ? 19  MET A HE3  1 
ATOM   280  N N    . VAL A 1 20  ? 14.387 -4.620  6.165   1.00 41.42  ? 20  VAL A N    1 
ATOM   281  C CA   . VAL A 1 20  ? 14.438 -4.745  4.702   1.00 38.94  ? 20  VAL A CA   1 
ATOM   282  C C    . VAL A 1 20  ? 15.718 -5.446  4.264   1.00 42.22  ? 20  VAL A C    1 
ATOM   283  O O    . VAL A 1 20  ? 15.696 -6.312  3.379   1.00 43.28  ? 20  VAL A O    1 
ATOM   284  C CB   . VAL A 1 20  ? 14.355 -3.330  4.069   1.00 37.03  ? 20  VAL A CB   1 
ATOM   285  C CG1  . VAL A 1 20  ? 14.715 -3.370  2.619   1.00 43.59  ? 20  VAL A CG1  1 
ATOM   286  C CG2  . VAL A 1 20  ? 12.924 -2.762  4.235   1.00 38.03  ? 20  VAL A CG2  1 
ATOM   287  H H    . VAL A 1 20  ? 14.284 -3.815  6.450   1.00 49.79  ? 20  VAL A H    1 
ATOM   288  H HA   . VAL A 1 20  ? 13.686 -5.283  4.408   1.00 46.80  ? 20  VAL A HA   1 
ATOM   289  H HB   . VAL A 1 20  ? 14.986 -2.750  4.524   1.00 44.51  ? 20  VAL A HB   1 
ATOM   290  H HG11 . VAL A 1 20  ? 14.354 -2.583  2.182   1.00 52.38  ? 20  VAL A HG11 1 
ATOM   291  H HG12 . VAL A 1 20  ? 15.681 -3.382  2.534   1.00 52.38  ? 20  VAL A HG12 1 
ATOM   292  H HG13 . VAL A 1 20  ? 14.338 -4.171  2.222   1.00 52.38  ? 20  VAL A HG13 1 
ATOM   293  H HG21 . VAL A 1 20  ? 12.896 -1.864  3.868   1.00 45.71  ? 20  VAL A HG21 1 
ATOM   294  H HG22 . VAL A 1 20  ? 12.300 -3.333  3.760   1.00 45.71  ? 20  VAL A HG22 1 
ATOM   295  H HG23 . VAL A 1 20  ? 12.700 -2.741  5.179   1.00 45.71  ? 20  VAL A HG23 1 
ATOM   296  N N    . LEU A 1 21  ? 16.879 -4.983  4.797   1.00 38.98  ? 21  LEU A N    1 
ATOM   297  C CA   . LEU A 1 21  ? 18.158 -5.573  4.387   1.00 39.07  ? 21  LEU A CA   1 
ATOM   298  C C    . LEU A 1 21  ? 18.248 -7.027  4.810   1.00 45.28  ? 21  LEU A C    1 
ATOM   299  O O    . LEU A 1 21  ? 18.867 -7.839  4.108   1.00 45.89  ? 21  LEU A O    1 
ATOM   300  C CB   . LEU A 1 21  ? 19.359 -4.816  4.955   1.00 36.10  ? 21  LEU A CB   1 
ATOM   301  C CG   . LEU A 1 21  ? 19.617 -3.457  4.341   1.00 40.46  ? 21  LEU A CG   1 
ATOM   302  C CD1  . LEU A 1 21  ? 20.940 -2.837  4.885   1.00 39.74  ? 21  LEU A CD1  1 
ATOM   303  C CD2  . LEU A 1 21  ? 19.624 -3.540  2.764   1.00 38.78  ? 21  LEU A CD2  1 
ATOM   304  H H    . LEU A 1 21  ? 16.940 -4.351  5.377   1.00 46.86  ? 21  LEU A H    1 
ATOM   305  H HA   . LEU A 1 21  ? 18.206 -5.502  3.421   1.00 46.97  ? 21  LEU A HA   1 
ATOM   306  H HB2  . LEU A 1 21  ? 19.214 -4.682  5.905   1.00 43.40  ? 21  LEU A HB2  1 
ATOM   307  H HB3  . LEU A 1 21  ? 20.153 -5.354  4.813   1.00 43.40  ? 21  LEU A HB3  1 
ATOM   308  H HG   . LEU A 1 21  ? 18.896 -2.860  4.596   1.00 48.63  ? 21  LEU A HG   1 
ATOM   309  H HD11 . LEU A 1 21  ? 21.101 -1.992  4.436   1.00 47.76  ? 21  LEU A HD11 1 
ATOM   310  H HD12 . LEU A 1 21  ? 20.852 -2.692  5.840   1.00 47.76  ? 21  LEU A HD12 1 
ATOM   311  H HD13 . LEU A 1 21  ? 21.672 -3.449  4.710   1.00 47.76  ? 21  LEU A HD13 1 
ATOM   312  H HD21 . LEU A 1 21  ? 19.989 -2.715  2.406   1.00 46.61  ? 21  LEU A HD21 1 
ATOM   313  H HD22 . LEU A 1 21  ? 20.172 -4.291  2.490   1.00 46.61  ? 21  LEU A HD22 1 
ATOM   314  H HD23 . LEU A 1 21  ? 18.714 -3.662  2.451   1.00 46.61  ? 21  LEU A HD23 1 
ATOM   315  N N    . LYS A 1 22  ? 17.618 -7.396  5.928   1.00 47.29  ? 22  LYS A N    1 
ATOM   316  C CA   . LYS A 1 22  ? 17.577 -8.793  6.360   1.00 45.13  ? 22  LYS A CA   1 
ATOM   317  C C    . LYS A 1 22  ? 16.869 -9.653  5.332   1.00 49.81  ? 22  LYS A C    1 
ATOM   318  O O    . LYS A 1 22  ? 17.188 -10.838 5.201   1.00 50.97  ? 22  LYS A O    1 
ATOM   319  C CB   . LYS A 1 22  ? 16.879 -8.873  7.727   1.00 51.24  ? 22  LYS A CB   1 
ATOM   320  C CG   . LYS A 1 22  ? 17.028 -10.195 8.538   1.00 54.59  ? 22  LYS A CG   1 
ATOM   321  C CD   . LYS A 1 22  ? 16.333 -10.033 9.932   1.00 56.51  ? 22  LYS A CD   1 
ATOM   322  C CE   . LYS A 1 22  ? 16.275 -11.310 10.758  1.00 70.58  ? 22  LYS A CE   1 
ATOM   323  N NZ   . LYS A 1 22  ? 15.291 -12.260 10.196  1.00 77.04  ? 22  LYS A NZ   1 
ATOM   324  H H    . LYS A 1 22  ? 17.206 -6.856  6.455   1.00 56.83  ? 22  LYS A H    1 
ATOM   325  H HA   . LYS A 1 22  ? 18.477 -9.141  6.462   1.00 54.24  ? 22  LYS A HA   1 
ATOM   326  H HB2  . LYS A 1 22  ? 17.235 -8.162  8.283   1.00 61.57  ? 22  LYS A HB2  1 
ATOM   327  H HB3  . LYS A 1 22  ? 15.929 -8.738  7.583   1.00 61.57  ? 22  LYS A HB3  1 
ATOM   328  H HG2  . LYS A 1 22  ? 16.604 -10.924 8.059   1.00 65.58  ? 22  LYS A HG2  1 
ATOM   329  H HG3  . LYS A 1 22  ? 17.968 -10.391 8.677   1.00 65.58  ? 22  LYS A HG3  1 
ATOM   330  H HD2  . LYS A 1 22  ? 16.822 -9.373  10.448  1.00 67.88  ? 22  LYS A HD2  1 
ATOM   331  H HD3  . LYS A 1 22  ? 15.421 -9.734  9.791   1.00 67.88  ? 22  LYS A HD3  1 
ATOM   332  H HE2  . LYS A 1 22  ? 17.147 -11.735 10.757  1.00 84.78  ? 22  LYS A HE2  1 
ATOM   333  H HE3  . LYS A 1 22  ? 16.011 -11.096 11.666  1.00 84.78  ? 22  LYS A HE3  1 
ATOM   334  H HZ1  . LYS A 1 22  ? 15.281 -13.008 10.678  1.00 92.52  ? 22  LYS A HZ1  1 
ATOM   335  H HZ2  . LYS A 1 22  ? 14.478 -11.898 10.208  1.00 92.52  ? 22  LYS A HZ2  1 
ATOM   336  H HZ3  . LYS A 1 22  ? 15.507 -12.460 9.356   1.00 92.52  ? 22  LYS A HZ3  1 
ATOM   337  N N    . GLN A 1 23  ? 15.927 -9.076  4.558   1.00 56.08  ? 23  GLN A N    1 
ATOM   338  C CA   . GLN A 1 23  ? 15.269 -9.824  3.480   1.00 52.85  ? 23  GLN A CA   1 
ATOM   339  C C    . GLN A 1 23  ? 16.113 -9.981  2.229   1.00 53.96  ? 23  GLN A C    1 
ATOM   340  O O    . GLN A 1 23  ? 15.855 -10.901 1.421   1.00 51.43  ? 23  GLN A O    1 
ATOM   341  C CB   . GLN A 1 23  ? 13.971 -9.158  3.069   1.00 54.64  ? 23  GLN A CB   1 
ATOM   342  C CG   . GLN A 1 23  ? 12.976 -9.223  4.193   1.00 62.74  ? 23  GLN A CG   1 
ATOM   343  C CD   . GLN A 1 23  ? 11.726 -8.509  3.878   1.00 67.60  ? 23  GLN A CD   1 
ATOM   344  O OE1  . GLN A 1 23  ? 11.437 -8.207  2.723   1.00 71.07  ? 23  GLN A OE1  1 
ATOM   345  N NE2  . GLN A 1 23  ? 10.961 -8.202  4.910   1.00 75.07  ? 23  GLN A NE2  1 
ATOM   346  H H    . GLN A 1 23  ? 15.659 -8.263  4.640   1.00 67.37  ? 23  GLN A H    1 
ATOM   347  H HA   . GLN A 1 23  ? 15.078 -10.704 3.839   1.00 63.50  ? 23  GLN A HA   1 
ATOM   348  H HB2  . GLN A 1 23  ? 14.137 -8.227  2.854   1.00 65.64  ? 23  GLN A HB2  1 
ATOM   349  H HB3  . GLN A 1 23  ? 13.601 -9.616  2.299   1.00 65.64  ? 23  GLN A HB3  1 
ATOM   350  H HG2  . GLN A 1 23  ? 12.756 -10.151 4.369   1.00 75.36  ? 23  GLN A HG2  1 
ATOM   351  H HG3  . GLN A 1 23  ? 13.364 -8.818  4.984   1.00 75.36  ? 23  GLN A HG3  1 
ATOM   352  H HE21 . GLN A 1 23  ? 11.205 -8.420  5.706   1.00 90.17  ? 23  GLN A HE21 1 
ATOM   353  H HE22 . GLN A 1 23  ? 10.219 -7.785  4.787   1.00 90.17  ? 23  GLN A HE22 1 
ATOM   354  N N    . GLY A 1 24  ? 17.067 -9.068  2.006   1.00 52.81  ? 24  GLY A N    1 
ATOM   355  C CA   . GLY A 1 24  ? 17.964 -9.210  0.863   1.00 49.66  ? 24  GLY A CA   1 
ATOM   356  C C    . GLY A 1 24  ? 18.729 -7.929  0.631   1.00 44.47  ? 24  GLY A C    1 
ATOM   357  O O    . GLY A 1 24  ? 18.193 -6.859  0.910   1.00 44.21  ? 24  GLY A O    1 
ATOM   358  H H    . GLY A 1 24  ? 17.208 -8.373  2.494   1.00 63.45  ? 24  GLY A H    1 
ATOM   359  H HA2  . GLY A 1 24  ? 18.595 -9.928  1.029   1.00 59.67  ? 24  GLY A HA2  1 
ATOM   360  H HA3  . GLY A 1 24  ? 17.451 -9.418  0.067   1.00 59.67  ? 24  GLY A HA3  1 
ATOM   361  N N    . ASP A 1 25  ? 19.966 -8.035  0.156   1.00 46.04  ? 25  ASP A N    1 
ATOM   362  C CA   . ASP A 1 25  ? 20.708 -6.875  -0.306  1.00 40.00  ? 25  ASP A CA   1 
ATOM   363  C C    . ASP A 1 25  ? 19.808 -6.072  -1.229  1.00 44.93  ? 25  ASP A C    1 
ATOM   364  O O    . ASP A 1 25  ? 18.973 -6.633  -1.943  1.00 46.08  ? 25  ASP A O    1 
ATOM   365  C CB   . ASP A 1 25  ? 21.967 -7.323  -1.028  1.00 42.71  ? 25  ASP A CB   1 
ATOM   366  C CG   . ASP A 1 25  ? 22.837 -8.278  -0.212  1.00 44.01  ? 25  ASP A CG   1 
ATOM   367  O OD1  . ASP A 1 25  ? 22.459 -8.631  0.930   1.00 45.02  ? 25  ASP A OD1  1 
ATOM   368  O OD2  . ASP A 1 25  ? 23.914 -8.706  -0.756  1.00 44.43  ? 25  ASP A OD2  1 
ATOM   369  H H    . ASP A 1 25  ? 20.400 -8.775  0.092   1.00 55.32  ? 25  ASP A H    1 
ATOM   370  H HA   . ASP A 1 25  ? 20.987 -6.313  0.433   1.00 48.08  ? 25  ASP A HA   1 
ATOM   371  H HB2  . ASP A 1 25  ? 21.713 -7.780  -1.845  1.00 51.32  ? 25  ASP A HB2  1 
ATOM   372  H HB3  . ASP A 1 25  ? 22.502 -6.542  -1.237  1.00 51.32  ? 25  ASP A HB3  1 
ATOM   373  N N    . ASN A 1 26  ? 19.990 -4.747  -1.240  1.00 42.48  ? 26  ASN A N    1 
ATOM   374  C CA   . ASN A 1 26  ? 19.070 -3.875  -1.963  1.00 43.07  ? 26  ASN A CA   1 
ATOM   375  C C    . ASN A 1 26  ? 19.721 -2.513  -2.086  1.00 42.14  ? 26  ASN A C    1 
ATOM   376  O O    . ASN A 1 26  ? 20.699 -2.220  -1.407  1.00 45.28  ? 26  ASN A O    1 
ATOM   377  C CB   . ASN A 1 26  ? 17.741 -3.783  -1.199  1.00 46.48  ? 26  ASN A CB   1 
ATOM   378  C CG   . ASN A 1 26  ? 16.525 -3.543  -2.110  1.00 45.64  ? 26  ASN A CG   1 
ATOM   379  O OD1  . ASN A 1 26  ? 16.659 -2.992  -3.169  1.00 41.70  ? 26  ASN A OD1  1 
ATOM   380  N ND2  . ASN A 1 26  ? 15.304 -3.887  -1.622  1.00 51.31  ? 26  ASN A ND2  1 
ATOM   381  H H    . ASN A 1 26  ? 20.633 -4.338  -0.841  1.00 51.06  ? 26  ASN A H    1 
ATOM   382  H HA   . ASN A 1 26  ? 18.897 -4.207  -2.858  1.00 51.76  ? 26  ASN A HA   1 
ATOM   383  H HB2  . ASN A 1 26  ? 17.596 -4.615  -0.722  1.00 55.86  ? 26  ASN A HB2  1 
ATOM   384  H HB3  . ASN A 1 26  ? 17.791 -3.045  -0.571  1.00 55.86  ? 26  ASN A HB3  1 
ATOM   385  H HD21 . ASN A 1 26  ? 14.600 -3.769  -2.101  1.00 61.65  ? 26  ASN A HD21 1 
ATOM   386  H HD22 . ASN A 1 26  ? 15.235 -4.224  -0.833  1.00 61.65  ? 26  ASN A HD22 1 
ATOM   387  N N    . TYR A 1 27  ? 19.202 -1.715  -3.010  1.00 46.22  ? 27  TYR A N    1 
ATOM   388  C CA   . TYR A 1 27  ? 19.731 -0.396  -3.318  1.00 46.08  ? 27  TYR A CA   1 
ATOM   389  C C    . TYR A 1 27  ? 18.685 0.626   -2.909  1.00 43.87  ? 27  TYR A C    1 
ATOM   390  O O    . TYR A 1 27  ? 17.510 0.279   -2.709  1.00 48.18  ? 27  TYR A O    1 
ATOM   391  C CB   . TYR A 1 27  ? 20.103 -0.225  -4.820  1.00 51.07  ? 27  TYR A CB   1 
ATOM   392  C CG   . TYR A 1 27  ? 18.949 -0.307  -5.829  1.00 59.48  ? 27  TYR A CG   1 
ATOM   393  C CD1  . TYR A 1 27  ? 18.381 -1.527  -6.162  1.00 63.78  ? 27  TYR A CD1  1 
ATOM   394  C CD2  . TYR A 1 27  ? 18.417 0.825   -6.450  1.00 62.42  ? 27  TYR A CD2  1 
ATOM   395  C CE1  . TYR A 1 27  ? 17.334 -1.618  -7.071  1.00 63.92  ? 27  TYR A CE1  1 
ATOM   396  C CE2  . TYR A 1 27  ? 17.342 0.719   -7.328  1.00 64.97  ? 27  TYR A CE2  1 
ATOM   397  C CZ   . TYR A 1 27  ? 16.825 -0.498  -7.630  1.00 65.25  ? 27  TYR A CZ   1 
ATOM   398  O OH   . TYR A 1 27  ? 15.772 -0.642  -8.503  1.00 73.54  ? 27  TYR A OH   1 
ATOM   399  H H    . TYR A 1 27  ? 18.519 -1.924  -3.488  1.00 55.55  ? 27  TYR A H    1 
ATOM   400  H HA   . TYR A 1 27  ? 20.556 -0.249  -2.829  1.00 55.37  ? 27  TYR A HA   1 
ATOM   401  H HB2  . TYR A 1 27  ? 20.515 0.646   -4.930  1.00 61.36  ? 27  TYR A HB2  1 
ATOM   402  H HB3  . TYR A 1 27  ? 20.735 -0.923  -5.054  1.00 61.36  ? 27  TYR A HB3  1 
ATOM   403  H HD1  . TYR A 1 27  ? 18.708 -2.303  -5.768  1.00 76.61  ? 27  TYR A HD1  1 
ATOM   404  H HD2  . TYR A 1 27  ? 18.786 1.661   -6.274  1.00 74.98  ? 27  TYR A HD2  1 
ATOM   405  H HE1  . TYR A 1 27  ? 16.983 -2.450  -7.296  1.00 76.78  ? 27  TYR A HE1  1 
ATOM   406  H HE2  . TYR A 1 27  ? 16.978 1.485   -7.709  1.00 78.05  ? 27  TYR A HE2  1 
ATOM   407  H HH   . TYR A 1 27  ? 15.531 0.110   -8.788  1.00 88.32  ? 27  TYR A HH   1 
ATOM   408  N N    . VAL A 1 28  ? 19.125 1.880   -2.768  1.00 43.16  ? 28  VAL A N    1 
ATOM   409  C CA   . VAL A 1 28  ? 18.378 2.901   -2.007  1.00 39.62  ? 28  VAL A CA   1 
ATOM   410  C C    . VAL A 1 28  ? 16.980 3.159   -2.603  1.00 42.91  ? 28  VAL A C    1 
ATOM   411  O O    . VAL A 1 28  ? 15.989 3.028   -1.901  1.00 36.01  ? 28  VAL A O    1 
ATOM   412  C CB   . VAL A 1 28  ? 19.201 4.182   -1.927  1.00 42.29  ? 28  VAL A CB   1 
ATOM   413  C CG1  . VAL A 1 28  ? 18.352 5.364   -1.455  1.00 47.20  ? 28  VAL A CG1  1 
ATOM   414  C CG2  . VAL A 1 28  ? 20.356 3.914   -0.983  1.00 43.75  ? 28  VAL A CG2  1 
ATOM   415  H H    . VAL A 1 28  ? 19.860 2.174   -3.105  1.00 51.87  ? 28  VAL A H    1 
ATOM   416  H HA   . VAL A 1 28  ? 18.233 2.560   -1.111  1.00 47.62  ? 28  VAL A HA   1 
ATOM   417  H HB   . VAL A 1 28  ? 19.536 4.432   -2.802  1.00 50.83  ? 28  VAL A HB   1 
ATOM   418  H HG11 . VAL A 1 28  ? 18.940 6.087   -1.186  1.00 56.72  ? 28  VAL A HG11 1 
ATOM   419  H HG12 . VAL A 1 28  ? 17.783 5.655   -2.185  1.00 56.72  ? 28  VAL A HG12 1 
ATOM   420  H HG13 . VAL A 1 28  ? 17.808 5.083   -0.703  1.00 56.72  ? 28  VAL A HG13 1 
ATOM   421  H HG21 . VAL A 1 28  ? 20.906 4.711   -0.921  1.00 52.58  ? 28  VAL A HG21 1 
ATOM   422  H HG22 . VAL A 1 28  ? 20.004 3.687   -0.108  1.00 52.58  ? 28  VAL A HG22 1 
ATOM   423  H HG23 . VAL A 1 28  ? 20.882 3.176   -1.329  1.00 52.58  ? 28  VAL A HG23 1 
ATOM   424  N N    . TYR A 1 29  ? 16.901 3.473   -3.896  1.00 48.27  ? 29  TYR A N    1 
ATOM   425  C CA   . TYR A 1 29  ? 15.586 3.602   -4.544  1.00 53.38  ? 29  TYR A CA   1 
ATOM   426  C C    . TYR A 1 29  ? 14.752 2.332   -4.371  1.00 52.21  ? 29  TYR A C    1 
ATOM   427  O O    . TYR A 1 29  ? 13.513 2.401   -4.289  1.00 45.66  ? 29  TYR A O    1 
ATOM   428  C CB   . TYR A 1 29  ? 15.747 3.938   -6.062  1.00 78.08  ? 29  TYR A CB   1 
ATOM   429  C CG   . TYR A 1 29  ? 14.464 3.800   -6.951  1.00 103.39 ? 29  TYR A CG   1 
ATOM   430  C CD1  . TYR A 1 29  ? 14.051 2.543   -7.475  1.00 103.42 ? 29  TYR A CD1  1 
ATOM   431  C CD2  . TYR A 1 29  ? 13.677 4.920   -7.287  1.00 118.16 ? 29  TYR A CD2  1 
ATOM   432  C CE1  . TYR A 1 29  ? 12.881 2.412   -8.255  1.00 114.09 ? 29  TYR A CE1  1 
ATOM   433  C CE2  . TYR A 1 29  ? 12.512 4.788   -8.088  1.00 123.27 ? 29  TYR A CE2  1 
ATOM   434  C CZ   . TYR A 1 29  ? 12.126 3.536   -8.564  1.00 135.50 ? 29  TYR A CZ   1 
ATOM   435  O OH   . TYR A 1 29  ? 10.993 3.403   -9.350  1.00 146.01 ? 29  TYR A OH   1 
ATOM   436  H H    . TYR A 1 29  ? 17.574 3.615   -4.413  1.00 58.00  ? 29  TYR A H    1 
ATOM   437  H HA   . TYR A 1 29  ? 15.111 4.339   -4.129  1.00 64.13  ? 29  TYR A HA   1 
ATOM   438  H HB2  . TYR A 1 29  ? 16.046 4.858   -6.136  1.00 93.78  ? 29  TYR A HB2  1 
ATOM   439  H HB3  . TYR A 1 29  ? 16.415 3.341   -6.433  1.00 93.78  ? 29  TYR A HB3  1 
ATOM   440  H HD1  . TYR A 1 29  ? 14.565 1.789   -7.299  1.00 124.19 ? 29  TYR A HD1  1 
ATOM   441  H HD2  . TYR A 1 29  ? 13.925 5.762   -6.978  1.00 141.88 ? 29  TYR A HD2  1 
ATOM   442  H HE1  . TYR A 1 29  ? 12.617 1.574   -8.562  1.00 136.98 ? 29  TYR A HE1  1 
ATOM   443  H HE2  . TYR A 1 29  ? 12.005 5.539   -8.296  1.00 148.01 ? 29  TYR A HE2  1 
ATOM   444  H HH   . TYR A 1 29  ? 10.438 4.003   -9.158  1.00 175.29 ? 29  TYR A HH   1 
ATOM   445  N N    . GLY A 1 30  ? 15.388 1.147   -4.330  1.00 43.78  ? 30  GLY A N    1 
ATOM   446  C CA   . GLY A 1 30  ? 14.601 -0.072  -4.143  1.00 47.44  ? 30  GLY A CA   1 
ATOM   447  C C    . GLY A 1 30  ? 14.044 -0.191  -2.741  1.00 44.37  ? 30  GLY A C    1 
ATOM   448  O O    . GLY A 1 30  ? 12.893 -0.610  -2.535  1.00 43.43  ? 30  GLY A O    1 
ATOM   449  H H    . GLY A 1 30  ? 16.237 1.031   -4.406  1.00 52.61  ? 30  GLY A H    1 
ATOM   450  H HA2  . GLY A 1 30  ? 13.859 -0.073  -4.767  1.00 57.00  ? 30  GLY A HA2  1 
ATOM   451  H HA3  . GLY A 1 30  ? 15.161 -0.845  -4.316  1.00 57.00  ? 30  GLY A HA3  1 
ATOM   452  N N    . ILE A 1 31  ? 14.833 0.227   -1.765  1.00 39.90  ? 31  ILE A N    1 
ATOM   453  C CA   . ILE A 1 31  ? 14.388 0.229   -0.379  1.00 39.99  ? 31  ILE A CA   1 
ATOM   454  C C    . ILE A 1 31  ? 13.227 1.190   -0.248  1.00 47.21  ? 31  ILE A C    1 
ATOM   455  O O    . ILE A 1 31  ? 12.209 0.926   0.436   1.00 44.40  ? 31  ILE A O    1 
ATOM   456  C CB   . ILE A 1 31  ? 15.568 0.624   0.527   1.00 34.51  ? 31  ILE A CB   1 
ATOM   457  C CG1  . ILE A 1 31  ? 16.724 -0.357  0.277   1.00 41.18  ? 31  ILE A CG1  1 
ATOM   458  C CG2  . ILE A 1 31  ? 15.210 0.657   1.956   1.00 42.52  ? 31  ILE A CG2  1 
ATOM   459  C CD1  . ILE A 1 31  ? 18.036 -0.129  1.034   1.00 38.48  ? 31  ILE A CD1  1 
ATOM   460  H H    . ILE A 1 31  ? 15.635 0.517   -1.877  1.00 47.96  ? 31  ILE A H    1 
ATOM   461  H HA   . ILE A 1 31  ? 14.087 -0.654  -0.112  1.00 48.07  ? 31  ILE A HA   1 
ATOM   462  H HB   . ILE A 1 31  ? 15.832 1.528   0.298   1.00 41.49  ? 31  ILE A HB   1 
ATOM   463  H HG12 . ILE A 1 31  ? 16.415 -1.245  0.517   1.00 49.49  ? 31  ILE A HG12 1 
ATOM   464  H HG13 . ILE A 1 31  ? 16.939 -0.325  -0.668  1.00 49.49  ? 31  ILE A HG13 1 
ATOM   465  H HG21 . ILE A 1 31  ? 16.001 0.871   2.475   1.00 51.10  ? 31  ILE A HG21 1 
ATOM   466  H HG22 . ILE A 1 31  ? 14.529 1.333   2.096   1.00 51.10  ? 31  ILE A HG22 1 
ATOM   467  H HG23 . ILE A 1 31  ? 14.869 -0.214  2.217   1.00 51.10  ? 31  ILE A HG23 1 
ATOM   468  H HD11 . ILE A 1 31  ? 18.717 -0.717  0.671   1.00 46.26  ? 31  ILE A HD11 1 
ATOM   469  H HD12 . ILE A 1 31  ? 18.307 0.796   0.926   1.00 46.26  ? 31  ILE A HD12 1 
ATOM   470  H HD13 . ILE A 1 31  ? 17.897 -0.324  1.974   1.00 46.26  ? 31  ILE A HD13 1 
ATOM   471  N N    . ILE A 1 32  ? 13.376 2.380   -0.851  1.00 39.67  ? 32  ILE A N    1 
ATOM   472  C CA   . ILE A 1 32  ? 12.313 3.377   -0.675  1.00 40.52  ? 32  ILE A CA   1 
ATOM   473  C C    . ILE A 1 32  ? 11.012 2.840   -1.226  1.00 40.48  ? 32  ILE A C    1 
ATOM   474  O O    . ILE A 1 32  ? 9.957  2.909   -0.591  1.00 41.65  ? 32  ILE A O    1 
ATOM   475  C CB   . ILE A 1 32  ? 12.748 4.706   -1.354  1.00 41.54  ? 32  ILE A CB   1 
ATOM   476  C CG1  . ILE A 1 32  ? 14.019 5.223   -0.635  1.00 38.24  ? 32  ILE A CG1  1 
ATOM   477  C CG2  . ILE A 1 32  ? 11.557 5.628   -1.420  1.00 40.87  ? 32  ILE A CG2  1 
ATOM   478  C CD1  . ILE A 1 32  ? 14.578 6.493   -1.301  1.00 41.20  ? 32  ILE A CD1  1 
ATOM   479  H H    . ILE A 1 32  ? 14.044 2.620   -1.336  1.00 47.69  ? 32  ILE A H    1 
ATOM   480  H HA   . ILE A 1 32  ? 12.172 3.557   0.267   1.00 48.70  ? 32  ILE A HA   1 
ATOM   481  H HB   . ILE A 1 32  ? 13.019 4.606   -2.281  1.00 49.93  ? 32  ILE A HB   1 
ATOM   482  H HG12 . ILE A 1 32  ? 13.800 5.433   0.287   1.00 45.96  ? 32  ILE A HG12 1 
ATOM   483  H HG13 . ILE A 1 32  ? 14.704 4.537   -0.665  1.00 45.96  ? 32  ILE A HG13 1 
ATOM   484  H HG21 . ILE A 1 32  ? 11.858 6.516   -1.666  1.00 49.12  ? 32  ILE A HG21 1 
ATOM   485  H HG22 . ILE A 1 32  ? 10.935 5.293   -2.085  1.00 49.12  ? 32  ILE A HG22 1 
ATOM   486  H HG23 . ILE A 1 32  ? 11.129 5.653   -0.550  1.00 49.12  ? 32  ILE A HG23 1 
ATOM   487  H HD11 . ILE A 1 32  ? 15.484 6.642   -0.988  1.00 49.52  ? 32  ILE A HD11 1 
ATOM   488  H HD12 . ILE A 1 32  ? 14.576 6.372   -2.264  1.00 49.52  ? 32  ILE A HD12 1 
ATOM   489  H HD13 . ILE A 1 32  ? 14.017 7.248   -1.062  1.00 49.52  ? 32  ILE A HD13 1 
ATOM   490  N N    . LYS A 1 33  ? 11.082 2.225   -2.397  1.00 43.48  ? 33  LYS A N    1 
ATOM   491  C CA   . LYS A 1 33  ? 9.908  1.677   -3.037  1.00 45.84  ? 33  LYS A CA   1 
ATOM   492  C C    . LYS A 1 33  ? 9.266  0.624   -2.152  1.00 43.83  ? 33  LYS A C    1 
ATOM   493  O O    . LYS A 1 33  ? 8.049  0.657   -1.939  1.00 50.80  ? 33  LYS A O    1 
ATOM   494  C CB   . LYS A 1 33  ? 10.303 1.155   -4.426  1.00 52.71  ? 33  LYS A CB   1 
ATOM   495  C CG   . LYS A 1 33  ? 9.303  0.175   -5.078  1.00 57.52  ? 33  LYS A CG   1 
ATOM   496  C CD   . LYS A 1 33  ? 9.807  -0.407  -6.451  1.00 64.36  ? 33  LYS A CD   1 
ATOM   497  C CE   . LYS A 1 33  ? 8.892  -1.492  -6.948  1.00 65.45  ? 33  LYS A CE   1 
ATOM   498  N NZ   . LYS A 1 33  ? 7.503  -0.923  -7.041  1.00 71.33  ? 33  LYS A NZ   1 
ATOM   499  H H    . LYS A 1 33  ? 11.808 2.113   -2.845  1.00 52.26  ? 33  LYS A H    1 
ATOM   500  H HA   . LYS A 1 33  ? 9.233  2.359   -3.177  1.00 55.09  ? 33  LYS A HA   1 
ATOM   501  H HB2  . LYS A 1 33  ? 10.394 1.914   -5.022  1.00 63.33  ? 33  LYS A HB2  1 
ATOM   502  H HB3  . LYS A 1 33  ? 11.152 0.691   -4.347  1.00 63.33  ? 33  LYS A HB3  1 
ATOM   503  H HG2  . LYS A 1 33  ? 9.155  -0.571  -4.475  1.00 69.10  ? 33  LYS A HG2  1 
ATOM   504  H HG3  . LYS A 1 33  ? 8.468  0.641   -5.241  1.00 69.10  ? 33  LYS A HG3  1 
ATOM   505  H HD2  . LYS A 1 33  ? 9.830  0.302   -7.113  1.00 77.31  ? 33  LYS A HD2  1 
ATOM   506  H HD3  . LYS A 1 33  ? 10.694 -0.782  -6.337  1.00 77.31  ? 33  LYS A HD3  1 
ATOM   507  H HE2  . LYS A 1 33  ? 9.174  -1.792  -7.827  1.00 78.62  ? 33  LYS A HE2  1 
ATOM   508  H HE3  . LYS A 1 33  ? 8.891  -2.238  -6.328  1.00 78.62  ? 33  LYS A HE3  1 
ATOM   509  H HZ1  . LYS A 1 33  ? 6.949  -1.528  -7.386  1.00 85.67  ? 33  LYS A HZ1  1 
ATOM   510  H HZ2  . LYS A 1 33  ? 7.213  -0.695  -6.231  1.00 85.67  ? 33  LYS A HZ2  1 
ATOM   511  H HZ3  . LYS A 1 33  ? 7.504  -0.201  -7.561  1.00 85.67  ? 33  LYS A HZ3  1 
ATOM   512  N N    . GLN A 1 34  ? 10.053 -0.339  -1.668  1.00 42.39  ? 34  GLN A N    1 
ATOM   513  C CA   . GLN A 1 34  ? 9.459  -1.432  -0.898  1.00 46.03  ? 34  GLN A CA   1 
ATOM   514  C C    . GLN A 1 34  ? 8.849  -0.939  0.386   1.00 48.51  ? 34  GLN A C    1 
ATOM   515  O O    . GLN A 1 34  ? 7.875  -1.521  0.864   1.00 52.66  ? 34  GLN A O    1 
ATOM   516  C CB   . GLN A 1 34  ? 10.478 -2.489  -0.497  1.00 48.68  ? 34  GLN A CB   1 
ATOM   517  C CG   . GLN A 1 34  ? 10.988 -3.298  -1.617  1.00 57.35  ? 34  GLN A CG   1 
ATOM   518  C CD   . GLN A 1 34  ? 11.859 -4.499  -1.170  1.00 60.19  ? 34  GLN A CD   1 
ATOM   519  O OE1  . GLN A 1 34  ? 11.944 -4.873  -0.002  1.00 60.10  ? 34  GLN A OE1  1 
ATOM   520  N NE2  . GLN A 1 34  ? 12.477 -5.137  -2.156  1.00 70.23  ? 34  GLN A NE2  1 
ATOM   521  H H    . GLN A 1 34  ? 10.906 -0.382  -1.768  1.00 50.94  ? 34  GLN A H    1 
ATOM   522  H HA   . GLN A 1 34  ? 8.796  -1.830  -1.484  1.00 55.31  ? 34  GLN A HA   1 
ATOM   523  H HB2  . GLN A 1 34  ? 11.237 -2.047  -0.085  1.00 58.49  ? 34  GLN A HB2  1 
ATOM   524  H HB3  . GLN A 1 34  ? 10.063 -3.095  0.136   1.00 58.49  ? 34  GLN A HB3  1 
ATOM   525  H HG2  . GLN A 1 34  ? 10.235 -3.648  -2.118  1.00 68.89  ? 34  GLN A HG2  1 
ATOM   526  H HG3  . GLN A 1 34  ? 11.533 -2.733  -2.187  1.00 68.89  ? 34  GLN A HG3  1 
ATOM   527  H HE21 . GLN A 1 34  ? 12.377 -4.874  -2.968  1.00 84.35  ? 34  GLN A HE21 1 
ATOM   528  H HE22 . GLN A 1 34  ? 12.978 -5.815  -1.982  1.00 84.35  ? 34  GLN A HE22 1 
ATOM   529  N N    . VAL A 1 35  ? 9.469  0.076   1.006   1.00 44.52  ? 35  VAL A N    1 
ATOM   530  C CA   . VAL A 1 35  ? 8.937  0.606   2.263   1.00 41.64  ? 35  VAL A CA   1 
ATOM   531  C C    . VAL A 1 35  ? 7.632  1.322   2.019   1.00 45.79  ? 35  VAL A C    1 
ATOM   532  O O    . VAL A 1 35  ? 6.699  1.266   2.839   1.00 47.21  ? 35  VAL A O    1 
ATOM   533  C CB   . VAL A 1 35  ? 9.972  1.529   2.910   1.00 45.24  ? 35  VAL A CB   1 
ATOM   534  C CG1  . VAL A 1 35  ? 9.341  2.384   3.991   1.00 44.25  ? 35  VAL A CG1  1 
ATOM   535  C CG2  . VAL A 1 35  ? 11.158 0.658   3.465   1.00 41.47  ? 35  VAL A CG2  1 
ATOM   536  H H    . VAL A 1 35  ? 10.181 0.466   0.723   1.00 53.50  ? 35  VAL A H    1 
ATOM   537  H HA   . VAL A 1 35  ? 8.763  -0.131  2.869   1.00 50.05  ? 35  VAL A HA   1 
ATOM   538  H HB   . VAL A 1 35  ? 10.326 2.144   2.249   1.00 54.36  ? 35  VAL A HB   1 
ATOM   539  H HG11 . VAL A 1 35  ? 10.041 2.738   4.562   1.00 53.17  ? 35  VAL A HG11 1 
ATOM   540  H HG12 . VAL A 1 35  ? 8.854  3.112   3.574   1.00 53.17  ? 35  VAL A HG12 1 
ATOM   541  H HG13 . VAL A 1 35  ? 8.734  1.836   4.513   1.00 53.17  ? 35  VAL A HG13 1 
ATOM   542  H HG21 . VAL A 1 35  ? 11.810 1.243   3.884   1.00 49.84  ? 35  VAL A HG21 1 
ATOM   543  H HG22 . VAL A 1 35  ? 10.811 0.030   4.118   1.00 49.84  ? 35  VAL A HG22 1 
ATOM   544  H HG23 . VAL A 1 35  ? 11.569 0.177   2.730   1.00 49.84  ? 35  VAL A HG23 1 
ATOM   545  N N    . LYS A 1 36  ? 7.551  2.034   0.892   1.00 51.71  ? 36  LYS A N    1 
ATOM   546  C CA   . LYS A 1 36  ? 6.330  2.758   0.577   1.00 45.82  ? 36  LYS A CA   1 
ATOM   547  C C    . LYS A 1 36  ? 5.173  1.831   0.234   1.00 50.88  ? 36  LYS A C    1 
ATOM   548  O O    . LYS A 1 36  ? 4.014  2.165   0.489   1.00 55.78  ? 36  LYS A O    1 
ATOM   549  C CB   . LYS A 1 36  ? 6.572  3.677   -0.601  1.00 50.26  ? 36  LYS A CB   1 
ATOM   550  C CG   . LYS A 1 36  ? 5.409  4.660   -0.771  1.00 62.48  ? 36  LYS A CG   1 
ATOM   551  C CD   . LYS A 1 36  ? 5.581  5.412   -2.091  1.00 66.71  ? 36  LYS A CD   1 
ATOM   552  C CE   . LYS A 1 36  ? 4.321  6.244   -2.418  1.00 80.30  ? 36  LYS A CE   1 
ATOM   553  N NZ   . LYS A 1 36  ? 4.417  6.762   -3.802  1.00 75.46  ? 36  LYS A NZ   1 
ATOM   554  H H    . LYS A 1 36  ? 8.177  2.109   0.307   1.00 62.14  ? 36  LYS A H    1 
ATOM   555  H HA   . LYS A 1 36  ? 6.086  3.279   1.358   1.00 55.06  ? 36  LYS A HA   1 
ATOM   556  H HB2  . LYS A 1 36  ? 7.386  4.184   -0.454  1.00 60.39  ? 36  LYS A HB2  1 
ATOM   557  H HB3  . LYS A 1 36  ? 6.652  3.150   -1.411  1.00 60.39  ? 36  LYS A HB3  1 
ATOM   558  H HG2  . LYS A 1 36  ? 4.568  4.178   -0.791  1.00 75.05  ? 36  LYS A HG2  1 
ATOM   559  H HG3  . LYS A 1 36  ? 5.407  5.300   -0.042  1.00 75.05  ? 36  LYS A HG3  1 
ATOM   560  H HD2  . LYS A 1 36  ? 6.339  6.014   -2.024  1.00 80.13  ? 36  LYS A HD2  1 
ATOM   561  H HD3  . LYS A 1 36  ? 5.725  4.776   -2.809  1.00 80.13  ? 36  LYS A HD3  1 
ATOM   562  H HE2  . LYS A 1 36  ? 3.531  5.686   -2.346  1.00 96.44  ? 36  LYS A HE2  1 
ATOM   563  H HE3  . LYS A 1 36  ? 4.255  6.994   -1.807  1.00 96.44  ? 36  LYS A HE3  1 
ATOM   564  H HZ1  . LYS A 1 36  ? 3.695  7.246   -3.997  1.00 90.62  ? 36  LYS A HZ1  1 
ATOM   565  H HZ2  . LYS A 1 36  ? 5.140  7.274   -3.887  1.00 90.62  ? 36  LYS A HZ2  1 
ATOM   566  H HZ3  . LYS A 1 36  ? 4.474  6.085   -4.377  1.00 90.62  ? 36  LYS A HZ3  1 
ATOM   567  N N    . GLU A 1 37  ? 5.465  0.684   -0.400  1.00 55.08  ? 37  GLU A N    1 
ATOM   568  C CA   . GLU A 1 37  ? 4.423  -0.291  -0.679  1.00 53.95  ? 37  GLU A CA   1 
ATOM   569  C C    . GLU A 1 37  ? 3.970  -0.993  0.590   1.00 52.53  ? 37  GLU A C    1 
ATOM   570  O O    . GLU A 1 37  ? 2.795  -1.318  0.748   1.00 54.61  ? 37  GLU A O    1 
ATOM   571  C CB   . GLU A 1 37  ? 4.885  -1.364  -1.641  1.00 55.12  ? 37  GLU A CB   1 
ATOM   572  C CG   . GLU A 1 37  ? 5.042  -0.977  -3.041  1.00 60.80  ? 37  GLU A CG   1 
ATOM   573  C CD   . GLU A 1 37  ? 5.522  -2.153  -3.861  1.00 68.58  ? 37  GLU A CD   1 
ATOM   574  O OE1  . GLU A 1 37  ? 6.078  -3.132  -3.265  1.00 68.67  ? 37  GLU A OE1  1 
ATOM   575  O OE2  . GLU A 1 37  ? 5.275  -2.127  -5.090  1.00 76.08  ? 37  GLU A OE2  1 
ATOM   576  H H    . GLU A 1 37  ? 6.249  0.458   -0.672  1.00 66.18  ? 37  GLU A H    1 
ATOM   577  H HA   . GLU A 1 37  ? 3.694  0.204   -1.085  1.00 64.82  ? 37  GLU A HA   1 
ATOM   578  H HB2  . GLU A 1 37  ? 5.749  -1.685  -1.339  1.00 66.22  ? 37  GLU A HB2  1 
ATOM   579  H HB3  . GLU A 1 37  ? 4.236  -2.085  -1.619  1.00 66.22  ? 37  GLU A HB3  1 
ATOM   580  H HG2  . GLU A 1 37  ? 4.189  -0.679  -3.394  1.00 73.04  ? 37  GLU A HG2  1 
ATOM   581  H HG3  . GLU A 1 37  ? 5.696  -0.264  -3.109  1.00 73.04  ? 37  GLU A HG3  1 
ATOM   582  N N    . ALA A 1 38  ? 4.910  -1.292  1.472   1.00 50.33  ? 38  ALA A N    1 
ATOM   583  C CA   . ALA A 1 38  ? 4.543  -2.008  2.682   1.00 53.55  ? 38  ALA A CA   1 
ATOM   584  C C    . ALA A 1 38  ? 3.793  -1.133  3.665   1.00 50.40  ? 38  ALA A C    1 
ATOM   585  O O    . ALA A 1 38  ? 3.099  -1.668  4.522   1.00 60.03  ? 38  ALA A O    1 
ATOM   586  C CB   . ALA A 1 38  ? 5.802  -2.579  3.357   1.00 48.79  ? 38  ALA A CB   1 
ATOM   587  H H    . ALA A 1 38  ? 5.744  -1.098  1.396   1.00 60.48  ? 38  ALA A H    1 
ATOM   588  H HA   . ALA A 1 38  ? 3.965  -2.749  2.439   1.00 64.34  ? 38  ALA A HA   1 
ATOM   589  H HB1  . ALA A 1 38  ? 5.547  -3.005  4.191   1.00 58.62  ? 38  ALA A HB1  1 
ATOM   590  H HB2  . ALA A 1 38  ? 6.211  -3.229  2.765   1.00 58.62  ? 38  ALA A HB2  1 
ATOM   591  H HB3  . ALA A 1 38  ? 6.422  -1.854  3.533   1.00 58.62  ? 38  ALA A HB3  1 
ATOM   592  N N    . SER A 1 39  ? 3.937  0.195   3.600   1.00 44.78  ? 39  SER A N    1 
ATOM   593  C CA   . SER A 1 39  ? 3.199  1.101   4.452   1.00 43.75  ? 39  SER A CA   1 
ATOM   594  C C    . SER A 1 39  ? 2.017  1.743   3.784   1.00 51.49  ? 39  SER A C    1 
ATOM   595  O O    . SER A 1 39  ? 1.545  2.764   4.263   1.00 54.91  ? 39  SER A O    1 
ATOM   596  C CB   . SER A 1 39  ? 4.129  2.190   4.941   1.00 48.25  ? 39  SER A CB   1 
ATOM   597  O OG   . SER A 1 39  ? 4.479  3.091   3.921   1.00 49.27  ? 39  SER A OG   1 
ATOM   598  H H    . SER A 1 39  ? 4.470  0.593   3.055   1.00 53.82  ? 39  SER A H    1 
ATOM   599  H HA   . SER A 1 39  ? 2.862  0.589   5.204   1.00 52.58  ? 39  SER A HA   1 
ATOM   600  H HB2  . SER A 1 39  ? 3.685  2.682   5.649   1.00 57.98  ? 39  SER A HB2  1 
ATOM   601  H HB3  . SER A 1 39  ? 4.938  1.777   5.280   1.00 57.98  ? 39  SER A HB3  1 
ATOM   602  H HG   . SER A 1 39  ? 5.077  2.756   3.436   1.00 59.21  ? 39  SER A HG   1 
ATOM   603  N N    . ASN A 1 40  ? 1.599  1.251   2.624   1.00 55.31  ? 40  ASN A N    1 
ATOM   604  C CA   . ASN A 1 40  ? 0.449  1.785   1.916   1.00 53.16  ? 40  ASN A CA   1 
ATOM   605  C C    . ASN A 1 40  ? 0.567  3.286   1.737   1.00 50.06  ? 40  ASN A C    1 
ATOM   606  O O    . ASN A 1 40  ? -0.428 4.015   1.726   1.00 54.37  ? 40  ASN A O    1 
ATOM   607  C CB   . ASN A 1 40  ? -0.853 1.377   2.633   1.00 55.03  ? 40  ASN A CB   1 
ATOM   608  C CG   . ASN A 1 40  ? -1.006 -0.148  2.720   1.00 56.25  ? 40  ASN A CG   1 
ATOM   609  O OD1  . ASN A 1 40  ? -0.817 -0.880  1.717   1.00 60.39  ? 40  ASN A OD1  1 
ATOM   610  N ND2  . ASN A 1 40  ? -1.223 -0.630  3.920   1.00 54.22  ? 40  ASN A ND2  1 
ATOM   611  H H    . ASN A 1 40  ? 1.975  0.592   2.219   1.00 66.45  ? 40  ASN A H    1 
ATOM   612  H HA   . ASN A 1 40  ? 0.419  1.410   1.022   1.00 63.86  ? 40  ASN A HA   1 
ATOM   613  H HB2  . ASN A 1 40  ? -0.846 1.733   3.535   1.00 66.11  ? 40  ASN A HB2  1 
ATOM   614  H HB3  . ASN A 1 40  ? -1.612 1.731   2.142   1.00 66.11  ? 40  ASN A HB3  1 
ATOM   615  H HD21 . ASN A 1 40  ? -1.318 -1.477  4.033   1.00 65.14  ? 40  ASN A HD21 1 
ATOM   616  H HD22 . ASN A 1 40  ? -1.271 -0.099  4.595   1.00 65.14  ? 40  ASN A HD22 1 
ATOM   617  N N    . GLY A 1 41  ? 1.798  3.739   1.515   1.00 52.42  ? 41  GLY A N    1 
ATOM   618  C CA   . GLY A 1 41  ? 2.042  5.118   1.157   1.00 51.79  ? 41  GLY A CA   1 
ATOM   619  C C    . GLY A 1 41  ? 2.293  5.998   2.343   1.00 56.64  ? 41  GLY A C    1 
ATOM   620  O O    . GLY A 1 41  ? 2.608  7.179   2.152   1.00 66.06  ? 41  GLY A O    1 
ATOM   621  H H    . GLY A 1 41  ? 2.509  3.258   1.568   1.00 62.98  ? 41  GLY A H    1 
ATOM   622  H HA2  . GLY A 1 41  ? 2.819  5.163   0.577   1.00 62.23  ? 41  GLY A HA2  1 
ATOM   623  H HA3  . GLY A 1 41  ? 1.272  5.464   0.681   1.00 62.23  ? 41  GLY A HA3  1 
ATOM   624  N N    . GLU A 1 42  ? 2.149  5.456   3.560   1.00 57.14  ? 42  GLU A N    1 
ATOM   625  C CA   . GLU A 1 42  ? 2.267  6.246   4.781   1.00 59.59  ? 42  GLU A CA   1 
ATOM   626  C C    . GLU A 1 42  ? 3.712  6.677   5.012   1.00 60.32  ? 42  GLU A C    1 
ATOM   627  O O    . GLU A 1 42  ? 3.990  7.780   5.509   1.00 63.02  ? 42  GLU A O    1 
ATOM   628  C CB   . GLU A 1 42  ? 1.775  5.405   5.979   1.00 57.28  ? 42  GLU A CB   1 
ATOM   629  C CG   . GLU A 1 42  ? 0.249  5.072   6.041   1.00 58.44  ? 42  GLU A CG   1 
ATOM   630  C CD   . GLU A 1 42  ? -0.127 4.129   7.228   1.00 70.79  ? 42  GLU A CD   1 
ATOM   631  O OE1  . GLU A 1 42  ? 0.744  3.824   8.091   1.00 74.46  ? 42  GLU A OE1  1 
ATOM   632  O OE2  . GLU A 1 42  ? -1.304 3.694   7.288   1.00 71.66  ? 42  GLU A OE2  1 
ATOM   633  H H    . GLU A 1 42  ? 1.980  4.625   3.703   1.00 68.64  ? 42  GLU A H    1 
ATOM   634  H HA   . GLU A 1 42  ? 1.716  7.041   4.705   1.00 71.58  ? 42  GLU A HA   1 
ATOM   635  H HB2  . GLU A 1 42  ? 2.247  4.558   5.962   1.00 68.82  ? 42  GLU A HB2  1 
ATOM   636  H HB3  . GLU A 1 42  ? 1.990  5.889   6.792   1.00 68.82  ? 42  GLU A HB3  1 
ATOM   637  H HG2  . GLU A 1 42  ? -0.249 5.898   6.147   1.00 70.21  ? 42  GLU A HG2  1 
ATOM   638  H HG3  . GLU A 1 42  ? -0.010 4.632   5.217   1.00 70.21  ? 42  GLU A HG3  1 
ATOM   639  N N    . MET A 1 43  ? 4.656  5.819   4.690   1.00 52.75  ? 43  MET A N    1 
ATOM   640  C CA   . MET A 1 43  ? 6.044  6.105   5.020   1.00 49.97  ? 43  MET A CA   1 
ATOM   641  C C    . MET A 1 43  ? 6.789  6.093   3.713   1.00 49.15  ? 43  MET A C    1 
ATOM   642  O O    . MET A 1 43  ? 7.087  5.023   3.172   1.00 47.90  ? 43  MET A O    1 
ATOM   643  C CB   . MET A 1 43  ? 6.609  5.088   5.998   1.00 51.45  ? 43  MET A CB   1 
ATOM   644  C CG   . MET A 1 43  ? 8.054  5.343   6.408   1.00 53.23  ? 43  MET A CG   1 
ATOM   645  S SD   . MET A 1 43  ? 8.561  4.100   7.608   1.00 53.22  ? 43  MET A SD   1 
ATOM   646  C CE   . MET A 1 43  ? 10.235 4.645   7.867   1.00 58.03  ? 43  MET A CE   1 
ATOM   647  H H    . MET A 1 43  ? 4.522  5.072   4.285   1.00 63.38  ? 43  MET A H    1 
ATOM   648  H HA   . MET A 1 43  ? 6.113  6.974   5.445   1.00 60.04  ? 43  MET A HA   1 
ATOM   649  H HB2  . MET A 1 43  ? 6.069  5.102   6.804   1.00 61.81  ? 43  MET A HB2  1 
ATOM   650  H HB3  . MET A 1 43  ? 6.571  4.210   5.588   1.00 61.81  ? 43  MET A HB3  1 
ATOM   651  H HG2  . MET A 1 43  ? 8.631  5.283   5.631   1.00 63.96  ? 43  MET A HG2  1 
ATOM   652  H HG3  . MET A 1 43  ? 8.131  6.221   6.812   1.00 63.96  ? 43  MET A HG3  1 
ATOM   653  H HE1  . MET A 1 43  ? 10.654 4.074   8.529   1.00 69.71  ? 43  MET A HE1  1 
ATOM   654  H HE2  . MET A 1 43  ? 10.718 4.590   7.028   1.00 69.71  ? 43  MET A HE2  1 
ATOM   655  H HE3  . MET A 1 43  ? 10.223 5.563   8.182   1.00 69.71  ? 43  MET A HE3  1 
ATOM   656  N N    . GLU A 1 44  ? 7.104  7.288   3.240   1.00 55.05  ? 44  GLU A N    1 
ATOM   657  C CA   . GLU A 1 44  ? 7.830  7.519   1.998   1.00 58.07  ? 44  GLU A CA   1 
ATOM   658  C C    . GLU A 1 44  ? 9.143  8.237   2.344   1.00 52.26  ? 44  GLU A C    1 
ATOM   659  O O    . GLU A 1 44  ? 9.168  9.447   2.567   1.00 55.29  ? 44  GLU A O    1 
ATOM   660  C CB   . GLU A 1 44  ? 6.987  8.336   1.039   1.00 59.47  ? 44  GLU A CB   1 
ATOM   661  C CG   . GLU A 1 44  ? 7.440  8.170   -0.434  1.00 70.76  ? 44  GLU A CG   1 
ATOM   662  C CD   . GLU A 1 44  ? 6.442  8.770   -1.455  1.00 90.28  ? 44  GLU A CD   1 
ATOM   663  O OE1  . GLU A 1 44  ? 5.397  9.319   -1.008  1.00 94.74  ? 44  GLU A OE1  1 
ATOM   664  O OE2  . GLU A 1 44  ? 6.716  8.721   -2.695  1.00 88.94  ? 44  GLU A OE2  1 
ATOM   665  H H    . GLU A 1 44  ? 6.898  8.020   3.640   1.00 66.14  ? 44  GLU A H    1 
ATOM   666  H HA   . GLU A 1 44  ? 8.047  6.670   1.581   1.00 69.76  ? 44  GLU A HA   1 
ATOM   667  H HB2  . GLU A 1 44  ? 6.063  8.048   1.105   1.00 71.44  ? 44  GLU A HB2  1 
ATOM   668  H HB3  . GLU A 1 44  ? 7.061  9.274   1.273   1.00 71.44  ? 44  GLU A HB3  1 
ATOM   669  H HG2  . GLU A 1 44  ? 8.293  8.618   -0.553  1.00 84.99  ? 44  GLU A HG2  1 
ATOM   670  H HG3  . GLU A 1 44  ? 7.533  7.224   -0.629  1.00 84.99  ? 44  GLU A HG3  1 
ATOM   671  N N    . LEU A 1 45  ? 10.233 7.467   2.405   1.00 49.85  ? 45  LEU A N    1 
ATOM   672  C CA   . LEU A 1 45  ? 11.536 8.023   2.770   1.00 46.86  ? 45  LEU A CA   1 
ATOM   673  C C    . LEU A 1 45  ? 12.209 8.744   1.619   1.00 51.08  ? 45  LEU A C    1 
ATOM   674  O O    . LEU A 1 45  ? 11.944 8.466   0.448   1.00 53.01  ? 45  LEU A O    1 
ATOM   675  C CB   . LEU A 1 45  ? 12.450 6.921   3.261   1.00 48.03  ? 45  LEU A CB   1 
ATOM   676  C CG   . LEU A 1 45  ? 11.827 6.191   4.450   1.00 49.69  ? 45  LEU A CG   1 
ATOM   677  C CD1  . LEU A 1 45  ? 12.604 4.945   4.796   1.00 46.00  ? 45  LEU A CD1  1 
ATOM   678  C CD2  . LEU A 1 45  ? 11.901 7.121   5.604   1.00 45.45  ? 45  LEU A CD2  1 
ATOM   679  H H    . LEU A 1 45  ? 10.243 6.623   2.240   1.00 59.90  ? 45  LEU A H    1 
ATOM   680  H HA   . LEU A 1 45  ? 11.397 8.674   3.475   1.00 56.30  ? 45  LEU A HA   1 
ATOM   681  H HB2  . LEU A 1 45  ? 12.596 6.280   2.547   1.00 57.71  ? 45  LEU A HB2  1 
ATOM   682  H HB3  . LEU A 1 45  ? 13.296 7.304   3.541   1.00 57.71  ? 45  LEU A HB3  1 
ATOM   683  H HG   . LEU A 1 45  ? 10.916 5.927   4.245   1.00 59.71  ? 45  LEU A HG   1 
ATOM   684  H HD11 . LEU A 1 45  ? 12.024 4.335   5.279   1.00 55.28  ? 45  LEU A HD11 1 
ATOM   685  H HD12 . LEU A 1 45  ? 12.913 4.528   3.976   1.00 55.28  ? 45  LEU A HD12 1 
ATOM   686  H HD13 . LEU A 1 45  ? 13.362 5.189   5.349   1.00 55.28  ? 45  LEU A HD13 1 
ATOM   687  H HD21 . LEU A 1 45  ? 11.715 6.629   6.419   1.00 54.62  ? 45  LEU A HD21 1 
ATOM   688  H HD22 . LEU A 1 45  ? 12.791 7.505   5.644   1.00 54.62  ? 45  LEU A HD22 1 
ATOM   689  H HD23 . LEU A 1 45  ? 11.243 7.824   5.485   1.00 54.62  ? 45  LEU A HD23 1 
ATOM   690  N N    . ASN A 1 46  ? 13.059 9.696   1.951   1.00 54.42  ? 46  ASN A N    1 
ATOM   691  C CA   . ASN A 1 46  ? 13.825 10.404  0.925   1.00 56.07  ? 46  ASN A CA   1 
ATOM   692  C C    . ASN A 1 46  ? 15.285 9.943   0.982   1.00 53.92  ? 46  ASN A C    1 
ATOM   693  O O    . ASN A 1 46  ? 15.747 9.443   2.007   1.00 51.65  ? 46  ASN A O    1 
ATOM   694  C CB   . ASN A 1 46  ? 13.670 11.916  1.085   1.00 59.58  ? 46  ASN A CB   1 
ATOM   695  C CG   . ASN A 1 46  ? 14.967 12.604  1.346   1.00 67.51  ? 46  ASN A CG   1 
ATOM   696  O OD1  . ASN A 1 46  ? 15.641 13.084  0.398   1.00 65.35  ? 46  ASN A OD1  1 
ATOM   697  N ND2  . ASN A 1 46  ? 15.360 12.668  2.644   1.00 67.90  ? 46  ASN A ND2  1 
ATOM   698  H H    . ASN A 1 46  ? 13.213 9.954   2.757   1.00 65.38  ? 46  ASN A H    1 
ATOM   699  H HA   . ASN A 1 46  ? 13.505 10.197  0.033   1.00 67.36  ? 46  ASN A HA   1 
ATOM   700  H HB2  . ASN A 1 46  ? 13.294 12.284  0.270   1.00 71.58  ? 46  ASN A HB2  1 
ATOM   701  H HB3  . ASN A 1 46  ? 13.079 12.096  1.833   1.00 71.58  ? 46  ASN A HB3  1 
ATOM   702  H HD21 . ASN A 1 46  ? 16.100 13.053  2.852   1.00 81.56  ? 46  ASN A HD21 1 
ATOM   703  H HD22 . ASN A 1 46  ? 14.868 12.323  3.260   1.00 81.56  ? 46  ASN A HD22 1 
ATOM   704  N N    . GLU A 1 47  ? 15.949 10.012  -0.179  1.00 53.80  ? 47  GLU A N    1 
ATOM   705  C CA   . GLU A 1 47  ? 17.327 9.564   -0.347  1.00 52.25  ? 47  GLU A CA   1 
ATOM   706  C C    . GLU A 1 47  ? 18.251 9.971   0.785   1.00 48.83  ? 47  GLU A C    1 
ATOM   707  O O    . GLU A 1 47  ? 19.046 9.175   1.269   1.00 47.64  ? 47  GLU A O    1 
ATOM   708  C CB   . GLU A 1 47  ? 17.879 10.197  -1.629  1.00 54.70  ? 47  GLU A CB   1 
ATOM   709  C CG   . GLU A 1 47  ? 17.798 9.358   -2.818  1.00 57.60  ? 47  GLU A CG   1 
ATOM   710  C CD   . GLU A 1 47  ? 18.492 9.975   -3.977  1.00 61.54  ? 47  GLU A CD   1 
ATOM   711  O OE1  . GLU A 1 47  ? 18.025 11.050  -4.351  1.00 62.31  ? 47  GLU A OE1  1 
ATOM   712  O OE2  . GLU A 1 47  ? 19.446 9.361   -4.518  1.00 63.53  ? 47  GLU A OE2  1 
ATOM   713  H H    . GLU A 1 47  ? 15.610 10.324  -0.904  1.00 64.64  ? 47  GLU A H    1 
ATOM   714  H HA   . GLU A 1 47  ? 17.308 8.595   -0.388  1.00 62.78  ? 47  GLU A HA   1 
ATOM   715  H HB2  . GLU A 1 47  ? 17.378 11.008  -1.811  1.00 65.72  ? 47  GLU A HB2  1 
ATOM   716  H HB3  . GLU A 1 47  ? 18.815 10.410  -1.488  1.00 65.72  ? 47  GLU A HB3  1 
ATOM   717  H HG2  . GLU A 1 47  ? 18.215 8.502   -2.634  1.00 69.20  ? 47  GLU A HG2  1 
ATOM   718  H HG3  . GLU A 1 47  ? 16.867 9.229   -3.056  1.00 69.20  ? 47  GLU A HG3  1 
ATOM   719  N N    . ALA A 1 48  ? 18.209 11.259  1.128   1.00 46.87  ? 48  ALA A N    1 
ATOM   720  C CA   . ALA A 1 48  ? 19.148 11.833  2.079   1.00 44.74  ? 48  ALA A CA   1 
ATOM   721  C C    . ALA A 1 48  ? 18.985 11.217  3.444   1.00 49.52  ? 48  ALA A C    1 
ATOM   722  O O    . ALA A 1 48  ? 19.975 11.034  4.164   1.00 52.68  ? 48  ALA A O    1 
ATOM   723  C CB   . ALA A 1 48  ? 18.950 13.350  2.166   1.00 46.58  ? 48  ALA A CB   1 
ATOM   724  H H    . ALA A 1 48  ? 17.640 11.825  0.819   1.00 56.32  ? 48  ALA A H    1 
ATOM   725  H HA   . ALA A 1 48  ? 20.049 11.657  1.766   1.00 53.76  ? 48  ALA A HA   1 
ATOM   726  H HB1  . ALA A 1 48  ? 19.594 13.717  2.792   1.00 55.98  ? 48  ALA A HB1  1 
ATOM   727  H HB2  . ALA A 1 48  ? 19.085 13.737  1.287   1.00 55.98  ? 48  ALA A HB2  1 
ATOM   728  H HB3  . ALA A 1 48  ? 18.048 13.533  2.474   1.00 55.98  ? 48  ALA A HB3  1 
ATOM   729  N N    . THR A 1 49  ? 17.747 10.908  3.860   1.00 51.51  ? 49  THR A N    1 
ATOM   730  C CA   . THR A 1 49  ? 17.604 10.255  5.167   1.00 49.07  ? 49  THR A CA   1 
ATOM   731  C C    . THR A 1 49  ? 18.315 8.922   5.174   1.00 42.84  ? 49  THR A C    1 
ATOM   732  O O    . THR A 1 49  ? 18.997 8.578   6.157   1.00 45.40  ? 49  THR A O    1 
ATOM   733  C CB   . THR A 1 49  ? 16.147 10.064  5.562   1.00 49.22  ? 49  THR A CB   1 
ATOM   734  O OG1  . THR A 1 49  ? 15.405 11.216  5.157   1.00 56.00  ? 49  THR A OG1  1 
ATOM   735  C CG2  . THR A 1 49  ? 16.025 9.953   7.086   1.00 58.49  ? 49  THR A CG2  1 
ATOM   736  H H    . THR A 1 49  ? 17.018 11.057  3.429   1.00 61.89  ? 49  THR A H    1 
ATOM   737  H HA   . THR A 1 49  ? 17.998 10.843  5.831   1.00 58.97  ? 49  THR A HA   1 
ATOM   738  H HB   . THR A 1 49  ? 15.798 9.260   5.146   1.00 59.14  ? 49  THR A HB   1 
ATOM   739  H HG1  . THR A 1 49  ? 14.582 11.071  5.237   1.00 67.27  ? 49  THR A HG1  1 
ATOM   740  H HG21 . THR A 1 49  ? 15.098 9.813   7.335   1.00 70.26  ? 49  THR A HG21 1 
ATOM   741  H HG22 . THR A 1 49  ? 16.553 9.207   7.408   1.00 70.26  ? 49  THR A HG22 1 
ATOM   742  H HG23 . THR A 1 49  ? 16.343 10.769  7.504   1.00 70.26  ? 49  THR A HG23 1 
ATOM   743  N N    . LEU A 1 50  ? 18.224 8.165   4.079   1.00 41.61  ? 50  LEU A N    1 
ATOM   744  C CA   . LEU A 1 50  ? 18.882 6.848   4.071   1.00 40.12  ? 50  LEU A CA   1 
ATOM   745  C C    . LEU A 1 50  ? 20.381 7.013   4.139   1.00 41.81  ? 50  LEU A C    1 
ATOM   746  O O    . LEU A 1 50  ? 21.079 6.247   4.802   1.00 41.27  ? 50  LEU A O    1 
ATOM   747  C CB   . LEU A 1 50  ? 18.521 6.041   2.809   1.00 39.83  ? 50  LEU A CB   1 
ATOM   748  C CG   . LEU A 1 50  ? 17.388 5.019   3.011   1.00 41.62  ? 50  LEU A CG   1 
ATOM   749  C CD1  . LEU A 1 50  ? 16.120 5.793   3.189   1.00 44.14  ? 50  LEU A CD1  1 
ATOM   750  C CD2  . LEU A 1 50  ? 17.222 4.096   1.879   1.00 44.18  ? 50  LEU A CD2  1 
ATOM   751  H H    . LEU A 1 50  ? 17.806 8.376   3.357   1.00 50.01  ? 50  LEU A H    1 
ATOM   752  H HA   . LEU A 1 50  ? 18.564 6.350   4.840   1.00 48.23  ? 50  LEU A HA   1 
ATOM   753  H HB2  . LEU A 1 50  ? 18.240 6.660   2.117   1.00 47.87  ? 50  LEU A HB2  1 
ATOM   754  H HB3  . LEU A 1 50  ? 19.308 5.555   2.518   1.00 47.87  ? 50  LEU A HB3  1 
ATOM   755  H HG   . LEU A 1 50  ? 17.601 4.470   3.782   1.00 50.02  ? 50  LEU A HG   1 
ATOM   756  H HD11 . LEU A 1 50  ? 15.381 5.172   3.282   1.00 53.05  ? 50  LEU A HD11 1 
ATOM   757  H HD12 . LEU A 1 50  ? 16.193 6.341   3.987   1.00 53.05  ? 50  LEU A HD12 1 
ATOM   758  H HD13 . LEU A 1 50  ? 15.982 6.357   2.412   1.00 53.05  ? 50  LEU A HD13 1 
ATOM   759  H HD21 . LEU A 1 50  ? 16.836 3.267   2.201   1.00 53.09  ? 50  LEU A HD21 1 
ATOM   760  H HD22 . LEU A 1 50  ? 16.633 4.502   1.224   1.00 53.09  ? 50  LEU A HD22 1 
ATOM   761  H HD23 . LEU A 1 50  ? 18.090 3.925   1.481   1.00 53.09  ? 50  LEU A HD23 1 
ATOM   762  N N    . TYR A 1 51  ? 20.920 7.978   3.406   1.00 42.99  ? 51  TYR A N    1 
ATOM   763  C CA   . TYR A 1 51  ? 22.374 8.063   3.350   1.00 42.38  ? 51  TYR A CA   1 
ATOM   764  C C    . TYR A 1 51  ? 22.932 8.426   4.720   1.00 43.27  ? 51  TYR A C    1 
ATOM   765  O O    . TYR A 1 51  ? 23.943 7.871   5.163   1.00 46.26  ? 51  TYR A O    1 
ATOM   766  C CB   . TYR A 1 51  ? 22.800 9.076   2.274   1.00 43.97  ? 51  TYR A CB   1 
ATOM   767  C CG   . TYR A 1 51  ? 22.500 8.613   0.834   1.00 44.11  ? 51  TYR A CG   1 
ATOM   768  C CD1  . TYR A 1 51  ? 22.962 7.410   0.320   1.00 50.87  ? 51  TYR A CD1  1 
ATOM   769  C CD2  . TYR A 1 51  ? 21.762 9.428   0.012   1.00 45.46  ? 51  TYR A CD2  1 
ATOM   770  C CE1  . TYR A 1 51  ? 22.631 7.038   -1.026  1.00 51.30  ? 51  TYR A CE1  1 
ATOM   771  C CE2  . TYR A 1 51  ? 21.466 9.090   -1.256  1.00 53.39  ? 51  TYR A CE2  1 
ATOM   772  C CZ   . TYR A 1 51  ? 21.879 7.921   -1.780  1.00 51.40  ? 51  TYR A CZ   1 
ATOM   773  O OH   . TYR A 1 51  ? 21.500 7.787   -3.107  1.00 63.20  ? 51  TYR A OH   1 
ATOM   774  H H    . TYR A 1 51  ? 20.490 8.569   2.954   1.00 51.66  ? 51  TYR A H    1 
ATOM   775  H HA   . TYR A 1 51  ? 22.747 7.205   3.092   1.00 50.93  ? 51  TYR A HA   1 
ATOM   776  H HB2  . TYR A 1 51  ? 22.325 9.908   2.423   1.00 52.84  ? 51  TYR A HB2  1 
ATOM   777  H HB3  . TYR A 1 51  ? 23.756 9.223   2.344   1.00 52.84  ? 51  TYR A HB3  1 
ATOM   778  H HD1  . TYR A 1 51  ? 23.485 6.848   0.845   1.00 61.13  ? 51  TYR A HD1  1 
ATOM   779  H HD2  . TYR A 1 51  ? 21.456 10.241  0.343   1.00 54.64  ? 51  TYR A HD2  1 
ATOM   780  H HE1  . TYR A 1 51  ? 22.914 6.227   -1.381  1.00 61.64  ? 51  TYR A HE1  1 
ATOM   781  H HE2  . TYR A 1 51  ? 20.966 9.674   -1.780  1.00 64.15  ? 51  TYR A HE2  1 
ATOM   782  H HH   . TYR A 1 51  ? 21.081 8.471   -3.356  1.00 75.92  ? 51  TYR A HH   1 
ATOM   783  N N    . THR A 1 52  ? 22.274 9.340   5.423   1.00 43.76  ? 52  THR A N    1 
ATOM   784  C CA   . THR A 1 52  ? 22.648 9.668   6.792   1.00 40.77  ? 52  THR A CA   1 
ATOM   785  C C    . THR A 1 52  ? 22.646 8.429   7.666   1.00 40.97  ? 52  THR A C    1 
ATOM   786  O O    . THR A 1 52  ? 23.624 8.123   8.359   1.00 42.45  ? 52  THR A O    1 
ATOM   787  C CB   . THR A 1 52  ? 21.619 10.671  7.369   1.00 45.67  ? 52  THR A CB   1 
ATOM   788  O OG1  . THR A 1 52  ? 21.645 11.882  6.610   1.00 47.75  ? 52  THR A OG1  1 
ATOM   789  C CG2  . THR A 1 52  ? 21.891 10.974  8.832   1.00 46.65  ? 52  THR A CG2  1 
ATOM   790  H H    . THR A 1 52  ? 21.602 9.789   5.128   1.00 52.59  ? 52  THR A H    1 
ATOM   791  H HA   . THR A 1 52  ? 23.536 10.059  6.789   1.00 49.00  ? 52  THR A HA   1 
ATOM   792  H HB   . THR A 1 52  ? 20.735 10.277  7.314   1.00 54.88  ? 52  THR A HB   1 
ATOM   793  H HG1  . THR A 1 52  ? 21.236 11.775  5.884   1.00 57.38  ? 52  THR A HG1  1 
ATOM   794  H HG21 . THR A 1 52  ? 21.246 11.618  9.163   1.00 56.06  ? 52  THR A HG21 1 
ATOM   795  H HG22 . THR A 1 52  ? 21.822 10.161  9.357   1.00 56.06  ? 52  THR A HG22 1 
ATOM   796  H HG23 . THR A 1 52  ? 22.783 11.340  8.935   1.00 56.06  ? 52  THR A HG23 1 
ATOM   797  N N    . ILE A 1 53  ? 21.530 7.705   7.644   1.00 39.62  ? 53  ILE A N    1 
ATOM   798  C CA   . ILE A 1 53  ? 21.451 6.515   8.490   1.00 41.05  ? 53  ILE A CA   1 
ATOM   799  C C    . ILE A 1 53  ? 22.491 5.509   8.070   1.00 40.39  ? 53  ILE A C    1 
ATOM   800  O O    . ILE A 1 53  ? 23.156 4.889   8.912   1.00 40.19  ? 53  ILE A O    1 
ATOM   801  C CB   . ILE A 1 53  ? 20.014 5.935   8.440   1.00 43.63  ? 53  ILE A CB   1 
ATOM   802  C CG1  . ILE A 1 53  ? 19.022 6.920   9.113   1.00 48.93  ? 53  ILE A CG1  1 
ATOM   803  C CG2  . ILE A 1 53  ? 19.939 4.576   9.077   1.00 45.49  ? 53  ILE A CG2  1 
ATOM   804  C CD1  . ILE A 1 53  ? 17.521 6.597   8.867   1.00 48.40  ? 53  ILE A CD1  1 
ATOM   805  H H    . ILE A 1 53  ? 20.833 7.873   7.170   1.00 47.62  ? 53  ILE A H    1 
ATOM   806  H HA   . ILE A 1 53  ? 21.640 6.759   9.410   1.00 49.34  ? 53  ILE A HA   1 
ATOM   807  H HB   . ILE A 1 53  ? 19.768 5.827   7.508   1.00 52.44  ? 53  ILE A HB   1 
ATOM   808  H HG12 . ILE A 1 53  ? 19.172 6.902   10.071  1.00 58.79  ? 53  ILE A HG12 1 
ATOM   809  H HG13 . ILE A 1 53  ? 19.190 7.810   8.767   1.00 58.79  ? 53  ILE A HG13 1 
ATOM   810  H HG21 . ILE A 1 53  ? 19.010 4.362   9.256   1.00 54.67  ? 53  ILE A HG21 1 
ATOM   811  H HG22 . ILE A 1 53  ? 20.318 3.921   8.469   1.00 54.67  ? 53  ILE A HG22 1 
ATOM   812  H HG23 . ILE A 1 53  ? 20.442 4.587   9.906   1.00 54.67  ? 53  ILE A HG23 1 
ATOM   813  H HD11 . ILE A 1 53  ? 16.986 7.357   9.143   1.00 58.16  ? 53  ILE A HD11 1 
ATOM   814  H HD12 . ILE A 1 53  ? 17.386 6.422   7.923   1.00 58.16  ? 53  ILE A HD12 1 
ATOM   815  H HD13 . ILE A 1 53  ? 17.277 5.815   9.387   1.00 58.16  ? 53  ILE A HD13 1 
ATOM   816  N N    . PHE A 1 54  ? 22.637 5.290   6.756   1.00 38.26  ? 54  PHE A N    1 
ATOM   817  C CA   . PHE A 1 54  ? 23.552 4.233   6.300   1.00 39.94  ? 54  PHE A CA   1 
ATOM   818  C C    . PHE A 1 54  ? 25.004 4.574   6.569   1.00 39.57  ? 54  PHE A C    1 
ATOM   819  O O    . PHE A 1 54  ? 25.849 3.678   6.735   1.00 40.57  ? 54  PHE A O    1 
ATOM   820  C CB   . PHE A 1 54  ? 23.358 3.968   4.804   1.00 39.61  ? 54  PHE A CB   1 
ATOM   821  C CG   . PHE A 1 54  ? 22.148 3.078   4.479   1.00 41.46  ? 54  PHE A CG   1 
ATOM   822  C CD1  . PHE A 1 54  ? 21.358 2.535   5.496   1.00 38.74  ? 54  PHE A CD1  1 
ATOM   823  C CD2  . PHE A 1 54  ? 21.780 2.859   3.158   1.00 38.33  ? 54  PHE A CD2  1 
ATOM   824  C CE1  . PHE A 1 54  ? 20.268 1.739   5.206   1.00 38.21  ? 54  PHE A CE1  1 
ATOM   825  C CE2  . PHE A 1 54  ? 20.708 2.085   2.868   1.00 39.19  ? 54  PHE A CE2  1 
ATOM   826  C CZ   . PHE A 1 54  ? 19.942 1.506   3.901   1.00 38.79  ? 54  PHE A CZ   1 
ATOM   827  H H    . PHE A 1 54  ? 22.234 5.722   6.131   1.00 45.98  ? 54  PHE A H    1 
ATOM   828  H HA   . PHE A 1 54  ? 23.335 3.423   6.788   1.00 48.00  ? 54  PHE A HA   1 
ATOM   829  H HB2  . PHE A 1 54  ? 23.230 4.817   4.352   1.00 47.61  ? 54  PHE A HB2  1 
ATOM   830  H HB3  . PHE A 1 54  ? 24.150 3.526   4.461   1.00 47.61  ? 54  PHE A HB3  1 
ATOM   831  H HD1  . PHE A 1 54  ? 21.571 2.713   6.384   1.00 46.57  ? 54  PHE A HD1  1 
ATOM   832  H HD2  . PHE A 1 54  ? 22.272 3.245   2.470   1.00 46.07  ? 54  PHE A HD2  1 
ATOM   833  H HE1  . PHE A 1 54  ? 19.761 1.366   5.891   1.00 45.93  ? 54  PHE A HE1  1 
ATOM   834  H HE2  . PHE A 1 54  ? 20.475 1.933   1.980   1.00 47.10  ? 54  PHE A HE2  1 
ATOM   835  H HZ   . PHE A 1 54  ? 19.214 0.966   3.693   1.00 46.62  ? 54  PHE A HZ   1 
ATOM   836  N N    . LYS A 1 55  ? 25.344 5.870   6.610   1.00 39.34  ? 55  LYS A N    1 
ATOM   837  C CA   . LYS A 1 55  ? 26.731 6.210   6.877   1.00 41.62  ? 55  LYS A CA   1 
ATOM   838  C C    . LYS A 1 55  ? 27.177 5.690   8.239   1.00 46.84  ? 55  LYS A C    1 
ATOM   839  O O    . LYS A 1 55  ? 28.270 5.152   8.399   1.00 52.36  ? 55  LYS A O    1 
ATOM   840  C CB   . LYS A 1 55  ? 26.915 7.730   6.846   1.00 47.69  ? 55  LYS A CB   1 
ATOM   841  C CG   . LYS A 1 55  ? 28.427 8.183   7.004   1.00 47.90  ? 55  LYS A CG   1 
ATOM   842  C CD   . LYS A 1 55  ? 28.551 9.737   7.209   1.00 51.33  ? 55  LYS A CD   1 
ATOM   843  C CE   . LYS A 1 55  ? 30.011 10.123  7.329   1.00 58.02  ? 55  LYS A CE   1 
ATOM   844  N NZ   . LYS A 1 55  ? 30.778 9.713   6.007   1.00 66.63  ? 55  LYS A NZ   1 
ATOM   845  H H    . LYS A 1 55  ? 24.810 6.534   6.492   1.00 47.28  ? 55  LYS A H    1 
ATOM   846  H HA   . LYS A 1 55  ? 27.276 5.804   6.185   1.00 50.02  ? 55  LYS A HA   1 
ATOM   847  H HB2  . LYS A 1 55  ? 26.591 8.069   5.997   1.00 57.31  ? 55  LYS A HB2  1 
ATOM   848  H HB3  . LYS A 1 55  ? 26.409 8.123   7.575   1.00 57.31  ? 55  LYS A HB3  1 
ATOM   849  H HG2  . LYS A 1 55  ? 28.814 7.743   7.777   1.00 57.56  ? 55  LYS A HG2  1 
ATOM   850  H HG3  . LYS A 1 55  ? 28.920 7.941   6.204   1.00 57.56  ? 55  LYS A HG3  1 
ATOM   851  H HD2  . LYS A 1 55  ? 28.168 10.199  6.447   1.00 61.67  ? 55  LYS A HD2  1 
ATOM   852  H HD3  . LYS A 1 55  ? 28.091 9.999   8.022   1.00 61.67  ? 55  LYS A HD3  1 
ATOM   853  H HE2  . LYS A 1 55  ? 30.088 11.082  7.451   1.00 69.70  ? 55  LYS A HE2  1 
ATOM   854  H HE3  . LYS A 1 55  ? 30.413 9.659   8.080   1.00 69.70  ? 55  LYS A HE3  1 
ATOM   855  H HZ1  . LYS A 1 55  ? 31.622 9.993   6.045   1.00 80.04  ? 55  LYS A HZ1  1 
ATOM   856  H HZ2  . LYS A 1 55  ? 30.770 8.829   5.912   1.00 80.04  ? 55  LYS A HZ2  1 
ATOM   857  H HZ3  . LYS A 1 55  ? 30.384 10.083  5.299   1.00 80.04  ? 55  LYS A HZ3  1 
ATOM   858  N N    . ARG A 1 56  ? 26.323 5.909   9.247   1.00 46.92  ? 56  ARG A N    1 
ATOM   859  C CA   . ARG A 1 56  ? 26.578 5.517   10.626  1.00 49.57  ? 56  ARG A CA   1 
ATOM   860  C C    . ARG A 1 56  ? 26.573 4.005   10.791  1.00 49.48  ? 56  ARG A C    1 
ATOM   861  O O    . ARG A 1 56  ? 27.474 3.431   11.403  1.00 51.30  ? 56  ARG A O    1 
ATOM   862  C CB   . ARG A 1 56  ? 25.487 6.162   11.491  1.00 48.39  ? 56  ARG A CB   1 
ATOM   863  C CG   . ARG A 1 56  ? 25.360 5.646   12.906  1.00 62.71  ? 56  ARG A CG   1 
ATOM   864  C CD   . ARG A 1 56  ? 26.497 6.082   13.801  1.00 66.06  ? 56  ARG A CD   1 
ATOM   865  N NE   . ARG A 1 56  ? 26.585 5.322   15.055  1.00 80.12  ? 56  ARG A NE   1 
ATOM   866  C CZ   . ARG A 1 56  ? 25.979 5.632   16.204  1.00 78.81  ? 56  ARG A CZ   1 
ATOM   867  N NH1  . ARG A 1 56  ? 25.144 6.658   16.298  1.00 78.47  ? 56  ARG A NH1  1 
ATOM   868  N NH2  . ARG A 1 56  ? 26.236 4.910   17.294  1.00 84.15  ? 56  ARG A NH2  1 
ATOM   869  H H    . ARG A 1 56  ? 25.562 6.297   9.149   1.00 56.39  ? 56  ARG A H    1 
ATOM   870  H HA   . ARG A 1 56  ? 27.453 5.825   10.908  1.00 59.56  ? 56  ARG A HA   1 
ATOM   871  H HB2  . ARG A 1 56  ? 25.671 7.112   11.549  1.00 58.15  ? 56  ARG A HB2  1 
ATOM   872  H HB3  . ARG A 1 56  ? 24.632 6.016   11.056  1.00 58.15  ? 56  ARG A HB3  1 
ATOM   873  H HG2  . ARG A 1 56  ? 24.534 5.980   13.289  1.00 75.34  ? 56  ARG A HG2  1 
ATOM   874  H HG3  . ARG A 1 56  ? 25.350 4.676   12.888  1.00 75.34  ? 56  ARG A HG3  1 
ATOM   875  H HD2  . ARG A 1 56  ? 27.334 5.964   13.325  1.00 79.35  ? 56  ARG A HD2  1 
ATOM   876  H HD3  . ARG A 1 56  ? 26.375 7.017   14.030  1.00 79.35  ? 56  ARG A HD3  1 
ATOM   877  H HE   . ARG A 1 56  ? 27.070 4.612   15.049  1.00 96.22  ? 56  ARG A HE   1 
ATOM   878  H HH11 . ARG A 1 56  ? 24.981 7.144   15.608  1.00 94.24  ? 56  ARG A HH11 1 
ATOM   879  H HH12 . ARG A 1 56  ? 24.766 6.838   17.049  1.00 94.24  ? 56  ARG A HH12 1 
ATOM   880  H HH21 . ARG A 1 56  ? 26.788 4.251   17.253  1.00 101.06 ? 56  ARG A HH21 1 
ATOM   881  H HH22 . ARG A 1 56  ? 25.851 5.102   18.039  1.00 101.06 ? 56  ARG A HH22 1 
ATOM   882  N N    . LEU A 1 57  ? 25.578 3.328   10.198  1.00 43.75  ? 57  LEU A N    1 
ATOM   883  C CA   . LEU A 1 57  ? 25.546 1.867   10.278  1.00 43.77  ? 57  LEU A CA   1 
ATOM   884  C C    . LEU A 1 57  ? 26.798 1.255   9.671   1.00 44.74  ? 57  LEU A C    1 
ATOM   885  O O    . LEU A 1 57  ? 27.412 0.361   10.250  1.00 47.04  ? 57  LEU A O    1 
ATOM   886  C CB   . LEU A 1 57  ? 24.302 1.325   9.560   1.00 39.31  ? 57  LEU A CB   1 
ATOM   887  C CG   . LEU A 1 57  ? 22.979 1.784   10.173  1.00 39.17  ? 57  LEU A CG   1 
ATOM   888  C CD1  . LEU A 1 57  ? 21.791 1.274   9.402   1.00 41.04  ? 57  LEU A CD1  1 
ATOM   889  C CD2  . LEU A 1 57  ? 22.786 1.359   11.641  1.00 43.05  ? 57  LEU A CD2  1 
ATOM   890  H H    . LEU A 1 57  ? 24.931 3.683   9.757   1.00 52.57  ? 57  LEU A H    1 
ATOM   891  H HA   . LEU A 1 57  ? 25.498 1.613   11.212  1.00 52.60  ? 57  LEU A HA   1 
ATOM   892  H HB2  . LEU A 1 57  ? 24.320 1.625   8.638   1.00 47.25  ? 57  LEU A HB2  1 
ATOM   893  H HB3  . LEU A 1 57  ? 24.323 0.356   9.594   1.00 47.25  ? 57  LEU A HB3  1 
ATOM   894  H HG   . LEU A 1 57  ? 23.021 2.752   10.136  1.00 47.08  ? 57  LEU A HG   1 
ATOM   895  H HD11 . LEU A 1 57  ? 20.978 1.559   9.848   1.00 49.33  ? 57  LEU A HD11 1 
ATOM   896  H HD12 . LEU A 1 57  ? 21.819 1.637   8.502   1.00 49.33  ? 57  LEU A HD12 1 
ATOM   897  H HD13 . LEU A 1 57  ? 21.827 0.305   9.369   1.00 49.33  ? 57  LEU A HD13 1 
ATOM   898  H HD21 . LEU A 1 57  ? 21.873 1.547   11.907  1.00 51.73  ? 57  LEU A HD21 1 
ATOM   899  H HD22 . LEU A 1 57  ? 22.965 0.408   11.721  1.00 51.73  ? 57  LEU A HD22 1 
ATOM   900  H HD23 . LEU A 1 57  ? 23.403 1.859   12.198  1.00 51.73  ? 57  LEU A HD23 1 
ATOM   901  N N    . GLU A 1 58  ? 27.238 1.754   8.528   1.00 44.22  ? 58  GLU A N    1 
ATOM   902  C CA   . GLU A 1 58  ? 28.505 1.267   7.978   1.00 48.14  ? 58  GLU A CA   1 
ATOM   903  C C    . GLU A 1 58  ? 29.673 1.532   8.928   1.00 46.85  ? 58  GLU A C    1 
ATOM   904  O O    . GLU A 1 58  ? 30.554 0.691   9.091   1.00 46.76  ? 58  GLU A O    1 
ATOM   905  C CB   . GLU A 1 58  ? 28.700 1.968   6.628   1.00 49.90  ? 58  GLU A CB   1 
ATOM   906  C CG   . GLU A 1 58  ? 29.393 1.148   5.638   1.00 54.59  ? 58  GLU A CG   1 
ATOM   907  C CD   . GLU A 1 58  ? 29.245 1.731   4.238   1.00 61.67  ? 58  GLU A CD   1 
ATOM   908  O OE1  . GLU A 1 58  ? 28.386 2.659   4.038   1.00 61.03  ? 58  GLU A OE1  1 
ATOM   909  O OE2  . GLU A 1 58  ? 29.953 1.199   3.346   1.00 59.08  ? 58  GLU A OE2  1 
ATOM   910  H H    . GLU A 1 58  ? 26.840 2.357   8.061   1.00 53.14  ? 58  GLU A H    1 
ATOM   911  H HA   . GLU A 1 58  ? 28.482 0.306   7.847   1.00 57.85  ? 58  GLU A HA   1 
ATOM   912  H HB2  . GLU A 1 58  ? 27.830 2.198   6.266   1.00 59.95  ? 58  GLU A HB2  1 
ATOM   913  H HB3  . GLU A 1 58  ? 29.224 2.773   6.766   1.00 59.95  ? 58  GLU A HB3  1 
ATOM   914  H HG2  . GLU A 1 58  ? 30.338 1.110   5.855   1.00 65.59  ? 58  GLU A HG2  1 
ATOM   915  H HG3  . GLU A 1 58  ? 29.017 0.254   5.639   1.00 65.59  ? 58  GLU A HG3  1 
ATOM   916  N N    . LYS A 1 59  ? 29.714 2.711   9.532   1.00 50.16  ? 59  LYS A N    1 
ATOM   917  C CA   . LYS A 1 59  ? 30.799 3.075   10.454  1.00 53.21  ? 59  LYS A CA   1 
ATOM   918  C C    . LYS A 1 59  ? 30.874 2.122   11.636  1.00 51.88  ? 59  LYS A C    1 
ATOM   919  O O    . LYS A 1 59  ? 31.966 1.730   12.059  1.00 51.01  ? 59  LYS A O    1 
ATOM   920  C CB   . LYS A 1 59  ? 30.563 4.514   10.951  1.00 52.59  ? 59  LYS A CB   1 
ATOM   921  C CG   . LYS A 1 59  ? 31.414 4.936   12.080  1.00 59.58  ? 59  LYS A CG   1 
ATOM   922  C CD   . LYS A 1 59  ? 31.632 6.491   12.122  1.00 64.68  ? 59  LYS A CD   1 
ATOM   923  C CE   . LYS A 1 59  ? 30.278 7.260   12.159  1.00 69.20  ? 59  LYS A CE   1 
ATOM   924  N NZ   . LYS A 1 59  ? 29.434 6.939   13.380  1.00 77.93  ? 59  LYS A NZ   1 
ATOM   925  H H    . LYS A 1 59  ? 29.125 3.329   9.431   1.00 60.27  ? 59  LYS A H    1 
ATOM   926  H HA   . LYS A 1 59  ? 31.646 3.030   9.985   1.00 63.93  ? 59  LYS A HA   1 
ATOM   927  H HB2  . LYS A 1 59  ? 30.732 5.124   10.216  1.00 63.19  ? 59  LYS A HB2  1 
ATOM   928  H HB3  . LYS A 1 59  ? 29.640 4.591   11.239  1.00 63.19  ? 59  LYS A HB3  1 
ATOM   929  H HG2  . LYS A 1 59  ? 30.993 4.669   12.912  1.00 71.58  ? 59  LYS A HG2  1 
ATOM   930  H HG3  . LYS A 1 59  ? 32.283 4.513   11.997  1.00 71.58  ? 59  LYS A HG3  1 
ATOM   931  H HD2  . LYS A 1 59  ? 32.136 6.723   12.917  1.00 77.69  ? 59  LYS A HD2  1 
ATOM   932  H HD3  . LYS A 1 59  ? 32.118 6.769   11.329  1.00 77.69  ? 59  LYS A HD3  1 
ATOM   933  H HE2  . LYS A 1 59  ? 30.459 8.213   12.165  1.00 83.12  ? 59  LYS A HE2  1 
ATOM   934  H HE3  . LYS A 1 59  ? 29.762 7.025   11.372  1.00 83.12  ? 59  LYS A HE3  1 
ATOM   935  H HZ1  . LYS A 1 59  ? 28.694 7.433   13.377  1.00 93.59  ? 59  LYS A HZ1  1 
ATOM   936  H HZ2  . LYS A 1 59  ? 29.207 6.078   13.375  1.00 93.59  ? 59  LYS A HZ2  1 
ATOM   937  H HZ3  . LYS A 1 59  ? 29.894 7.112   14.122  1.00 93.59  ? 59  LYS A HZ3  1 
ATOM   938  N N    . ASP A 1 60  ? 29.715 1.712   12.159  1.00 52.03  ? 60  ASP A N    1 
ATOM   939  C CA   . ASP A 1 60  ? 29.607 0.725   13.224  1.00 55.25  ? 60  ASP A CA   1 
ATOM   940  C C    . ASP A 1 60  ? 29.741 -0.714  12.754  1.00 55.45  ? 60  ASP A C    1 
ATOM   941  O O    . ASP A 1 60  ? 29.653 -1.612  13.592  1.00 53.95  ? 60  ASP A O    1 
ATOM   942  C CB   . ASP A 1 60  ? 28.242 0.928   13.908  1.00 53.41  ? 60  ASP A CB   1 
ATOM   943  C CG   . ASP A 1 60  ? 28.139 2.284   14.642  1.00 60.56  ? 60  ASP A CG   1 
ATOM   944  O OD1  . ASP A 1 60  ? 29.154 2.992   14.829  1.00 61.81  ? 60  ASP A OD1  1 
ATOM   945  O OD2  . ASP A 1 60  ? 27.016 2.685   14.966  1.00 65.75  ? 60  ASP A OD2  1 
ATOM   946  H H    . ASP A 1 60  ? 28.949 2.005   11.900  1.00 62.51  ? 60  ASP A H    1 
ATOM   947  H HA   . ASP A 1 60  ? 30.322 0.862   13.865  1.00 66.38  ? 60  ASP A HA   1 
ATOM   948  H HB2  . ASP A 1 60  ? 27.544 0.897   13.235  1.00 64.16  ? 60  ASP A HB2  1 
ATOM   949  H HB3  . ASP A 1 60  ? 28.107 0.222   14.559  1.00 64.16  ? 60  ASP A HB3  1 
ATOM   950  N N    . GLY A 1 61  ? 30.016 -0.978  11.468  1.00 52.85  ? 61  GLY A N    1 
ATOM   951  C CA   . GLY A 1 61  ? 30.186 -2.352  11.012  1.00 49.96  ? 61  GLY A CA   1 
ATOM   952  C C    . GLY A 1 61  ? 28.918 -3.169  10.995  1.00 49.01  ? 61  GLY A C    1 
ATOM   953  O O    . GLY A 1 61  ? 28.971 -4.386  11.096  1.00 55.74  ? 61  GLY A O    1 
ATOM   954  H H    . GLY A 1 61  ? 30.106 -0.383  10.853  1.00 63.50  ? 61  GLY A H    1 
ATOM   955  H HA2  . GLY A 1 61  ? 30.543 -2.339  10.110  1.00 60.03  ? 61  GLY A HA2  1 
ATOM   956  H HA3  . GLY A 1 61  ? 30.819 -2.798  11.596  1.00 60.03  ? 61  GLY A HA3  1 
ATOM   957  N N    . ILE A 1 62  ? 27.762 -2.526  10.890  1.00 48.53  ? 62  ILE A N    1 
ATOM   958  C CA   . ILE A 1 62  ? 26.486 -3.239  10.843  1.00 49.64  ? 62  ILE A CA   1 
ATOM   959  C C    . ILE A 1 62  ? 25.966 -3.541  9.442   1.00 49.35  ? 62  ILE A C    1 
ATOM   960  O O    . ILE A 1 62  ? 25.165 -4.477  9.290   1.00 47.24  ? 62  ILE A O    1 
ATOM   961  C CB   . ILE A 1 62  ? 25.480 -2.390  11.635  1.00 48.78  ? 62  ILE A CB   1 
ATOM   962  C CG1  . ILE A 1 62  ? 25.777 -2.496  13.138  1.00 54.86  ? 62  ILE A CG1  1 
ATOM   963  C CG2  . ILE A 1 62  ? 24.049 -2.795  11.390  1.00 47.59  ? 62  ILE A CG2  1 
ATOM   964  C CD1  . ILE A 1 62  ? 25.208 -1.355  13.877  1.00 59.71  ? 62  ILE A CD1  1 
ATOM   965  H H    . ILE A 1 62  ? 27.685 -1.671  10.843  1.00 58.31  ? 62  ILE A H    1 
ATOM   966  H HA   . ILE A 1 62  ? 26.601 -4.116  11.240  1.00 59.65  ? 62  ILE A HA   1 
ATOM   967  H HB   . ILE A 1 62  ? 25.587 -1.477  11.326  1.00 58.61  ? 62  ILE A HB   1 
ATOM   968  H HG12 . ILE A 1 62  ? 25.385 -3.312  13.486  1.00 65.91  ? 62  ILE A HG12 1 
ATOM   969  H HG13 . ILE A 1 62  ? 26.737 -2.503  13.276  1.00 65.91  ? 62  ILE A HG13 1 
ATOM   970  H HG21 . ILE A 1 62  ? 23.481 -2.366  12.049  1.00 57.19  ? 62  ILE A HG21 1 
ATOM   971  H HG22 . ILE A 1 62  ? 23.790 -2.515  10.498  1.00 57.19  ? 62  ILE A HG22 1 
ATOM   972  H HG23 . ILE A 1 62  ? 23.975 -3.759  11.468  1.00 57.19  ? 62  ILE A HG23 1 
ATOM   973  H HD11 . ILE A 1 62  ? 25.507 -1.395  14.798  1.00 71.73  ? 62  ILE A HD11 1 
ATOM   974  H HD12 . ILE A 1 62  ? 25.511 -0.530  13.466  1.00 71.73  ? 62  ILE A HD12 1 
ATOM   975  H HD13 . ILE A 1 62  ? 24.240 -1.406  13.840  1.00 71.73  ? 62  ILE A HD13 1 
ATOM   976  N N    . ILE A 1 63  ? 26.358 -2.731  8.429   1.00 50.54  ? 63  ILE A N    1 
ATOM   977  C CA   . ILE A 1 63  ? 26.101 -2.971  7.010   1.00 40.81  ? 63  ILE A CA   1 
ATOM   978  C C    . ILE A 1 63  ? 27.383 -2.636  6.243   1.00 43.43  ? 63  ILE A C    1 
ATOM   979  O O    . ILE A 1 63  ? 28.300 -2.029  6.797   1.00 41.43  ? 63  ILE A O    1 
ATOM   980  C CB   . ILE A 1 63  ? 24.958 -2.105  6.470   1.00 40.35  ? 63  ILE A CB   1 
ATOM   981  C CG1  . ILE A 1 63  ? 25.418 -0.661  6.374   1.00 38.38  ? 63  ILE A CG1  1 
ATOM   982  C CG2  . ILE A 1 63  ? 23.734 -2.260  7.372   1.00 42.21  ? 63  ILE A CG2  1 
ATOM   983  C CD1  . ILE A 1 63  ? 24.384 0.288   5.775   1.00 35.77  ? 63  ILE A CD1  1 
ATOM   984  H H    . ILE A 1 63  ? 26.797 -2.003  8.558   1.00 60.73  ? 63  ILE A H    1 
ATOM   985  H HA   . ILE A 1 63  ? 25.873 -3.905  6.880   1.00 49.05  ? 63  ILE A HA   1 
ATOM   986  H HB   . ILE A 1 63  ? 24.708 -2.394  5.579   1.00 48.50  ? 63  ILE A HB   1 
ATOM   987  H HG12 . ILE A 1 63  ? 25.628 -0.343  7.266   1.00 46.13  ? 63  ILE A HG12 1 
ATOM   988  H HG13 . ILE A 1 63  ? 26.210 -0.625  5.815   1.00 46.13  ? 63  ILE A HG13 1 
ATOM   989  H HG21 . ILE A 1 63  ? 22.976 -1.826  6.952   1.00 50.73  ? 63  ILE A HG21 1 
ATOM   990  H HG22 . ILE A 1 63  ? 23.549 -3.205  7.493   1.00 50.73  ? 63  ILE A HG22 1 
ATOM   991  H HG23 . ILE A 1 63  ? 23.919 -1.847  8.229   1.00 50.73  ? 63  ILE A HG23 1 
ATOM   992  H HD11 . ILE A 1 63  ? 24.802 1.149   5.614   1.00 43.01  ? 63  ILE A HD11 1 
ATOM   993  H HD12 . ILE A 1 63  ? 24.060 -0.084  4.940   1.00 43.01  ? 63  ILE A HD12 1 
ATOM   994  H HD13 . ILE A 1 63  ? 23.649 0.389   6.400   1.00 43.01  ? 63  ILE A HD13 1 
ATOM   995  N N    . SER A 1 64  ? 27.410 -3.026  4.952   1.00 46.04  ? 64  SER A N    1 
ATOM   996  C CA   . SER A 1 64  ? 28.500 -2.712  4.016   1.00 43.90  ? 64  SER A CA   1 
ATOM   997  C C    . SER A 1 64  ? 27.885 -2.565  2.634   1.00 42.02  ? 64  SER A C    1 
ATOM   998  O O    . SER A 1 64  ? 26.687 -2.815  2.437   1.00 43.82  ? 64  SER A O    1 
ATOM   999  C CB   . SER A 1 64  ? 29.552 -3.791  3.944   1.00 47.60  ? 64  SER A CB   1 
ATOM   1000 O OG   . SER A 1 64  ? 29.114 -4.885  3.157   1.00 44.31  ? 64  SER A OG   1 
ATOM   1001 H H    . SER A 1 64  ? 26.785 -3.490  4.586   1.00 55.33  ? 64  SER A H    1 
ATOM   1002 H HA   . SER A 1 64  ? 28.921 -1.891  4.313   1.00 52.76  ? 64  SER A HA   1 
ATOM   1003 H HB2  . SER A 1 64  ? 30.355 -3.420  3.547   1.00 57.19  ? 64  SER A HB2  1 
ATOM   1004 H HB3  . SER A 1 64  ? 29.740 -4.105  4.842   1.00 57.19  ? 64  SER A HB3  1 
ATOM   1005 H HG   . SER A 1 64  ? 29.776 -5.325  2.883   1.00 53.25  ? 64  SER A HG   1 
ATOM   1006 N N    . SER A 1 65  ? 28.694 -2.086  1.685   1.00 45.62  ? 65  SER A N    1 
ATOM   1007 C CA   . SER A 1 65  ? 28.163 -1.832  0.344   1.00 46.59  ? 65  SER A CA   1 
ATOM   1008 C C    . SER A 1 65  ? 29.103 -2.352  -0.725  1.00 39.90  ? 65  SER A C    1 
ATOM   1009 O O    . SER A 1 65  ? 30.270 -2.637  -0.463  1.00 40.06  ? 65  SER A O    1 
ATOM   1010 C CB   . SER A 1 65  ? 27.958 -0.347  0.096   1.00 47.52  ? 65  SER A CB   1 
ATOM   1011 O OG   . SER A 1 65  ? 29.185 0.345   0.316   1.00 49.98  ? 65  SER A OG   1 
ATOM   1012 H H    . SER A 1 65  ? 29.529 -1.907  1.791   1.00 54.82  ? 65  SER A H    1 
ATOM   1013 H HA   . SER A 1 65  ? 27.322 -2.312  0.280   1.00 55.98  ? 65  SER A HA   1 
ATOM   1014 H HB2  . SER A 1 65  ? 27.671 -0.210  -0.820  1.00 57.10  ? 65  SER A HB2  1 
ATOM   1015 H HB3  . SER A 1 65  ? 27.285 -0.009  0.708   1.00 57.10  ? 65  SER A HB3  1 
ATOM   1016 H HG   . SER A 1 65  ? 29.456 0.209   1.099   1.00 60.05  ? 65  SER A HG   1 
ATOM   1017 N N    . TYR A 1 66  ? 28.599 -2.423  -1.958  1.00 44.93  ? 66  TYR A N    1 
ATOM   1018 C CA   . TYR A 1 66  ? 29.386 -2.940  -3.081  1.00 43.30  ? 66  TYR A CA   1 
ATOM   1019 C C    . TYR A 1 66  ? 28.607 -2.687  -4.369  1.00 49.72  ? 66  TYR A C    1 
ATOM   1020 O O    . TYR A 1 66  ? 27.409 -2.404  -4.325  1.00 47.42  ? 66  TYR A O    1 
ATOM   1021 C CB   . TYR A 1 66  ? 29.661 -4.417  -2.861  1.00 44.80  ? 66  TYR A CB   1 
ATOM   1022 C CG   . TYR A 1 66  ? 28.423 -5.264  -2.938  1.00 44.74  ? 66  TYR A CG   1 
ATOM   1023 C CD1  . TYR A 1 66  ? 27.999 -5.828  -4.133  1.00 45.28  ? 66  TYR A CD1  1 
ATOM   1024 C CD2  . TYR A 1 66  ? 27.636 -5.420  -1.860  1.00 39.74  ? 66  TYR A CD2  1 
ATOM   1025 C CE1  . TYR A 1 66  ? 26.820 -6.629  -4.211  1.00 40.68  ? 66  TYR A CE1  1 
ATOM   1026 C CE2  . TYR A 1 66  ? 26.486 -6.176  -1.924  1.00 44.53  ? 66  TYR A CE2  1 
ATOM   1027 C CZ   . TYR A 1 66  ? 26.089 -6.772  -3.105  1.00 43.80  ? 66  TYR A CZ   1 
ATOM   1028 O OH   . TYR A 1 66  ? 24.927 -7.542  -3.146  1.00 44.08  ? 66  TYR A OH   1 
ATOM   1029 H H    . TYR A 1 66  ? 27.803 -2.177  -2.171  1.00 54.00  ? 66  TYR A H    1 
ATOM   1030 H HA   . TYR A 1 66  ? 30.229 -2.468  -3.168  1.00 52.04  ? 66  TYR A HA   1 
ATOM   1031 H HB2  . TYR A 1 66  ? 30.278 -4.727  -3.542  1.00 53.84  ? 66  TYR A HB2  1 
ATOM   1032 H HB3  . TYR A 1 66  ? 30.050 -4.536  -1.981  1.00 53.84  ? 66  TYR A HB3  1 
ATOM   1033 H HD1  . TYR A 1 66  ? 28.497 -5.680  -4.904  1.00 54.41  ? 66  TYR A HD1  1 
ATOM   1034 H HD2  . TYR A 1 66  ? 27.871 -5.010  -1.058  1.00 47.76  ? 66  TYR A HD2  1 
ATOM   1035 H HE1  . TYR A 1 66  ? 26.570 -7.038  -5.008  1.00 48.89  ? 66  TYR A HE1  1 
ATOM   1036 H HE2  . TYR A 1 66  ? 25.969 -6.287  -1.159  1.00 53.51  ? 66  TYR A HE2  1 
ATOM   1037 H HH   . TYR A 1 66  ? 24.686 -7.740  -2.366  1.00 52.98  ? 66  TYR A HH   1 
ATOM   1038 N N    . TRP A 1 67  ? 29.271 -2.832  -5.535  1.00 55.41  ? 67  TRP A N    1 
ATOM   1039 C CA   . TRP A 1 67  ? 28.633 -2.482  -6.812  1.00 59.12  ? 67  TRP A CA   1 
ATOM   1040 C C    . TRP A 1 67  ? 28.065 -3.689  -7.542  1.00 60.93  ? 67  TRP A C    1 
ATOM   1041 O O    . TRP A 1 67  ? 28.674 -4.778  -7.534  1.00 53.98  ? 67  TRP A O    1 
ATOM   1042 C CB   . TRP A 1 67  ? 29.595 -1.735  -7.765  1.00 71.95  ? 67  TRP A CB   1 
ATOM   1043 C CG   . TRP A 1 67  ? 29.937 -0.363  -7.283  1.00 71.57  ? 67  TRP A CG   1 
ATOM   1044 C CD1  . TRP A 1 67  ? 31.034 -0.011  -6.571  1.00 70.40  ? 67  TRP A CD1  1 
ATOM   1045 C CD2  . TRP A 1 67  ? 29.135 0.816   -7.395  1.00 69.45  ? 67  TRP A CD2  1 
ATOM   1046 N NE1  . TRP A 1 67  ? 30.970 1.312   -6.222  1.00 72.11  ? 67  TRP A NE1  1 
ATOM   1047 C CE2  . TRP A 1 67  ? 29.821 1.847   -6.726  1.00 68.53  ? 67  TRP A CE2  1 
ATOM   1048 C CE3  . TRP A 1 67  ? 27.912 1.103   -7.998  1.00 73.94  ? 67  TRP A CE3  1 
ATOM   1049 C CZ2  . TRP A 1 67  ? 29.343 3.142   -6.659  1.00 71.54  ? 67  TRP A CZ2  1 
ATOM   1050 C CZ3  . TRP A 1 67  ? 27.424 2.401   -7.915  1.00 76.81  ? 67  TRP A CZ3  1 
ATOM   1051 C CH2  . TRP A 1 67  ? 28.134 3.397   -7.242  1.00 73.05  ? 67  TRP A CH2  1 
ATOM   1052 H H    . TRP A 1 67  ? 30.076 -3.125  -5.605  1.00 66.57  ? 67  TRP A H    1 
ATOM   1053 H HA   . TRP A 1 67  ? 27.892 -1.898  -6.588  1.00 71.02  ? 67  TRP A HA   1 
ATOM   1054 H HB2  . TRP A 1 67  ? 30.419 -2.240  -7.842  1.00 86.42  ? 67  TRP A HB2  1 
ATOM   1055 H HB3  . TRP A 1 67  ? 29.175 -1.651  -8.636  1.00 86.42  ? 67  TRP A HB3  1 
ATOM   1056 H HD1  . TRP A 1 67  ? 31.732 -0.585  -6.350  1.00 84.56  ? 67  TRP A HD1  1 
ATOM   1057 H HE1  . TRP A 1 67  ? 31.559 1.736   -5.761  1.00 86.61  ? 67  TRP A HE1  1 
ATOM   1058 H HE3  . TRP A 1 67  ? 27.435 0.442   -8.445  1.00 88.81  ? 67  TRP A HE3  1 
ATOM   1059 H HZ2  . TRP A 1 67  ? 29.825 3.813   -6.233  1.00 85.93  ? 67  TRP A HZ2  1 
ATOM   1060 H HZ3  . TRP A 1 67  ? 26.610 2.610   -8.314  1.00 92.26  ? 67  TRP A HZ3  1 
ATOM   1061 H HH2  . TRP A 1 67  ? 27.776 4.254   -7.190  1.00 87.74  ? 67  TRP A HH2  1 
ATOM   1062 N N    . GLY A 1 68  ? 26.918 -3.486  -8.216  1.00 60.46  ? 68  GLY A N    1 
ATOM   1063 C CA   . GLY A 1 68  ? 26.298 -4.491  -9.056  1.00 77.10  ? 68  GLY A CA   1 
ATOM   1064 C C    . GLY A 1 68  ? 26.709 -4.406  -10.530 1.00 94.29  ? 68  GLY A C    1 
ATOM   1065 O O    . GLY A 1 68  ? 27.793 -3.937  -10.873 1.00 93.57  ? 68  GLY A O    1 
ATOM   1066 H H    . GLY A 1 68  ? 26.478 -2.747  -8.193  1.00 72.63  ? 68  GLY A H    1 
ATOM   1067 H HA2  . GLY A 1 68  ? 26.541 -5.370  -8.727  1.00 92.60  ? 68  GLY A HA2  1 
ATOM   1068 H HA3  . GLY A 1 68  ? 25.334 -4.391  -9.007  1.00 92.60  ? 68  GLY A HA3  1 
ATOM   1069 N N    . ASP A 1 69  ? 25.838 -4.925  -11.403 1.00 99.10  ? 69  ASP A N    1 
ATOM   1070 C CA   . ASP A 1 69  ? 25.986 -4.708  -12.859 1.00 99.76  ? 69  ASP A CA   1 
ATOM   1071 C C    . ASP A 1 69  ? 24.933 -5.480  -13.666 1.00 99.41  ? 69  ASP A C    1 
ATOM   1072 O O    . ASP A 1 69  ? 23.791 -5.034  -13.815 1.00 98.21  ? 69  ASP A O    1 
ATOM   1073 C CB   . ASP A 1 69  ? 27.418 -5.058  -13.373 1.00 101.82 ? 69  ASP A CB   1 
ATOM   1074 C CG   . ASP A 1 69  ? 27.863 -6.514  -13.099 1.00 103.95 ? 69  ASP A CG   1 
ATOM   1075 O OD1  . ASP A 1 69  ? 27.071 -7.475  -13.294 1.00 98.90  ? 69  ASP A OD1  1 
ATOM   1076 O OD2  . ASP A 1 69  ? 29.062 -6.693  -12.746 1.00 103.85 ? 69  ASP A OD2  1 
ATOM   1077 H H    . ASP A 1 69  ? 25.156 -5.402  -11.186 1.00 118.99 ? 69  ASP A H    1 
ATOM   1078 H HA   . ASP A 1 69  ? 25.853 -3.760  -13.017 1.00 119.79 ? 69  ASP A HA   1 
ATOM   1079 H HB2  . ASP A 1 69  ? 27.443 -4.921  -14.333 1.00 122.26 ? 69  ASP A HB2  1 
ATOM   1080 H HB3  . ASP A 1 69  ? 28.055 -4.471  -12.937 1.00 122.26 ? 69  ASP A HB3  1 
ATOM   1081 N N    . ARG A 1 75  ? 25.287 0.866   -13.168 1.00 114.12 ? 75  ARG A N    1 
ATOM   1082 C CA   . ARG A 1 75  ? 25.876 0.132   -12.044 1.00 115.96 ? 75  ARG A CA   1 
ATOM   1083 C C    . ARG A 1 75  ? 25.350 0.755   -10.717 1.00 107.09 ? 75  ARG A C    1 
ATOM   1084 O O    . ARG A 1 75  ? 25.646 1.914   -10.413 1.00 107.36 ? 75  ARG A O    1 
ATOM   1085 C CB   . ARG A 1 75  ? 27.407 0.158   -12.184 1.00 116.01 ? 75  ARG A CB   1 
ATOM   1086 C CG   . ARG A 1 75  ? 28.111 -1.029  -11.524 1.00 116.73 ? 75  ARG A CG   1 
ATOM   1087 C CD   . ARG A 1 75  ? 29.642 -1.082  -11.718 1.00 120.06 ? 75  ARG A CD   1 
ATOM   1088 N NE   . ARG A 1 75  ? 30.193 -2.274  -11.068 1.00 126.95 ? 75  ARG A NE   1 
ATOM   1089 C CZ   . ARG A 1 75  ? 31.472 -2.473  -10.765 1.00 128.84 ? 75  ARG A CZ   1 
ATOM   1090 N NH1  . ARG A 1 75  ? 32.403 -1.581  -11.061 1.00 136.85 ? 75  ARG A NH1  1 
ATOM   1091 N NH2  . ARG A 1 75  ? 31.824 -3.598  -10.148 1.00 115.44 ? 75  ARG A NH2  1 
ATOM   1092 H HA   . ARG A 1 75  ? 25.630 -0.805  -12.026 1.00 139.23 ? 75  ARG A HA   1 
ATOM   1093 H HB2  . ARG A 1 75  ? 27.633 0.149   -13.127 1.00 139.29 ? 75  ARG A HB2  1 
ATOM   1094 H HB3  . ARG A 1 75  ? 27.743 0.968   -11.770 1.00 139.29 ? 75  ARG A HB3  1 
ATOM   1095 H HG2  . ARG A 1 75  ? 27.942 -0.994  -10.569 1.00 140.16 ? 75  ARG A HG2  1 
ATOM   1096 H HG3  . ARG A 1 75  ? 27.745 -1.847  -11.895 1.00 140.16 ? 75  ARG A HG3  1 
ATOM   1097 H HD2  . ARG A 1 75  ? 29.849 -1.121  -12.665 1.00 144.15 ? 75  ARG A HD2  1 
ATOM   1098 H HD3  . ARG A 1 75  ? 30.048 -0.296  -11.321 1.00 144.15 ? 75  ARG A HD3  1 
ATOM   1099 H HE   . ARG A 1 75  ? 29.641 -2.900  -10.864 1.00 152.42 ? 75  ARG A HE   1 
ATOM   1100 H HH11 . ARG A 1 75  ? 32.188 -0.851  -11.460 1.00 164.30 ? 75  ARG A HH11 1 
ATOM   1101 H HH12 . ARG A 1 75  ? 33.224 -1.732  -10.855 1.00 164.30 ? 75  ARG A HH12 1 
ATOM   1102 H HH21 . ARG A 1 75  ? 31.227 -4.185  -9.951  1.00 138.60 ? 75  ARG A HH21 1 
ATOM   1103 H HH22 . ARG A 1 75  ? 32.648 -3.738  -9.947  1.00 138.60 ? 75  ARG A HH22 1 
ATOM   1104 N N    . ARG A 1 76  ? 24.612 -0.021  -9.912  1.00 82.97  ? 76  ARG A N    1 
ATOM   1105 C CA   . ARG A 1 76  ? 24.010 0.491   -8.680  1.00 71.20  ? 76  ARG A CA   1 
ATOM   1106 C C    . ARG A 1 76  ? 24.831 0.109   -7.453  1.00 61.51  ? 76  ARG A C    1 
ATOM   1107 O O    . ARG A 1 76  ? 25.577 -0.862  -7.443  1.00 62.71  ? 76  ARG A O    1 
ATOM   1108 C CB   . ARG A 1 76  ? 22.564 -0.016  -8.498  1.00 64.57  ? 76  ARG A CB   1 
ATOM   1109 C CG   . ARG A 1 76  ? 21.566 0.879   -9.206  1.00 76.67  ? 76  ARG A CG   1 
ATOM   1110 C CD   . ARG A 1 76  ? 20.180 0.333   -9.417  1.00 78.45  ? 76  ARG A CD   1 
ATOM   1111 N NE   . ARG A 1 76  ? 19.418 1.229   -10.295 1.00 91.62  ? 76  ARG A NE   1 
ATOM   1112 C CZ   . ARG A 1 76  ? 18.350 0.864   -10.998 1.00 104.86 ? 76  ARG A CZ   1 
ATOM   1113 N NH1  . ARG A 1 76  ? 17.911 -0.387  -10.988 1.00 121.00 ? 76  ARG A NH1  1 
ATOM   1114 N NH2  . ARG A 1 76  ? 17.712 1.771   -11.736 1.00 103.74 ? 76  ARG A NH2  1 
ATOM   1115 H H    . ARG A 1 76  ? 24.446 -0.852  -10.062 1.00 99.65  ? 76  ARG A H    1 
ATOM   1116 H HA   . ARG A 1 76  ? 23.990 1.459   -8.746  1.00 85.52  ? 76  ARG A HA   1 
ATOM   1117 H HB2  . ARG A 1 76  ? 22.489 -0.910  -8.867  1.00 77.56  ? 76  ARG A HB2  1 
ATOM   1118 H HB3  . ARG A 1 76  ? 22.346 -0.029  -7.552  1.00 77.56  ? 76  ARG A HB3  1 
ATOM   1119 H HG2  . ARG A 1 76  ? 21.471 1.692   -8.685  1.00 92.08  ? 76  ARG A HG2  1 
ATOM   1120 H HG3  . ARG A 1 76  ? 21.922 1.087   -10.084 1.00 92.08  ? 76  ARG A HG3  1 
ATOM   1121 H HD2  . ARG A 1 76  ? 20.232 -0.541  -9.833  1.00 94.22  ? 76  ARG A HD2  1 
ATOM   1122 H HD3  . ARG A 1 76  ? 19.721 0.268   -8.564  1.00 94.22  ? 76  ARG A HD3  1 
ATOM   1123 H HE   . ARG A 1 76  ? 19.680 2.046   -10.359 1.00 110.02 ? 76  ARG A HE   1 
ATOM   1124 H HH11 . ARG A 1 76  ? 18.319 -0.982  -10.521 1.00 145.27 ? 76  ARG A HH11 1 
ATOM   1125 H HH12 . ARG A 1 76  ? 17.218 -0.603  -11.450 1.00 145.27 ? 76  ARG A HH12 1 
ATOM   1126 H HH21 . ARG A 1 76  ? 17.992 2.584   -11.755 1.00 124.57 ? 76  ARG A HH21 1 
ATOM   1127 H HH22 . ARG A 1 76  ? 17.020 1.544   -12.194 1.00 124.57 ? 76  ARG A HH22 1 
ATOM   1128 N N    . LYS A 1 77  ? 24.701 0.917   -6.417  1.00 54.49  ? 77  LYS A N    1 
ATOM   1129 C CA   . LYS A 1 77  ? 25.284 0.622   -5.111  1.00 49.66  ? 77  LYS A CA   1 
ATOM   1130 C C    . LYS A 1 77  ? 24.295 -0.210  -4.290  1.00 47.65  ? 77  LYS A C    1 
ATOM   1131 O O    . LYS A 1 77  ? 23.195 0.243   -3.987  1.00 46.57  ? 77  LYS A O    1 
ATOM   1132 C CB   . LYS A 1 77  ? 25.617 1.931   -4.413  1.00 43.89  ? 77  LYS A CB   1 
ATOM   1133 C CG   . LYS A 1 77  ? 26.548 1.806   -3.236  1.00 48.37  ? 77  LYS A CG   1 
ATOM   1134 C CD   . LYS A 1 77  ? 26.912 3.198   -2.686  1.00 57.13  ? 77  LYS A CD   1 
ATOM   1135 C CE   . LYS A 1 77  ? 27.976 3.191   -1.565  1.00 62.77  ? 77  LYS A CE   1 
ATOM   1136 N NZ   . LYS A 1 77  ? 29.359 2.961   -2.064  1.00 70.63  ? 77  LYS A NZ   1 
ATOM   1137 H H    . LYS A 1 77  ? 24.269 1.660   -6.440  1.00 65.46  ? 77  LYS A H    1 
ATOM   1138 H HA   . LYS A 1 77  ? 26.094 0.099   -5.207  1.00 59.68  ? 77  LYS A HA   1 
ATOM   1139 H HB2  . LYS A 1 77  ? 26.038 2.523   -5.055  1.00 52.74  ? 77  LYS A HB2  1 
ATOM   1140 H HB3  . LYS A 1 77  ? 24.792 2.326   -4.090  1.00 52.74  ? 77  LYS A HB3  1 
ATOM   1141 H HG2  . LYS A 1 77  ? 26.116 1.299   -2.532  1.00 58.12  ? 77  LYS A HG2  1 
ATOM   1142 H HG3  . LYS A 1 77  ? 27.364 1.360   -3.513  1.00 58.12  ? 77  LYS A HG3  1 
ATOM   1143 H HD2  . LYS A 1 77  ? 27.260 3.737   -3.414  1.00 68.64  ? 77  LYS A HD2  1 
ATOM   1144 H HD3  . LYS A 1 77  ? 26.110 3.607   -2.325  1.00 68.64  ? 77  LYS A HD3  1 
ATOM   1145 H HE2  . LYS A 1 77  ? 27.962 4.050   -1.113  1.00 75.40  ? 77  LYS A HE2  1 
ATOM   1146 H HE3  . LYS A 1 77  ? 27.765 2.483   -0.937  1.00 75.40  ? 77  LYS A HE3  1 
ATOM   1147 H HZ1  . LYS A 1 77  ? 29.928 2.930   -1.380  1.00 84.83  ? 77  LYS A HZ1  1 
ATOM   1148 H HZ2  . LYS A 1 77  ? 29.398 2.191   -2.508  1.00 84.83  ? 77  LYS A HZ2  1 
ATOM   1149 H HZ3  . LYS A 1 77  ? 29.599 3.622   -2.610  1.00 84.83  ? 77  LYS A HZ3  1 
ATOM   1150 N N    . TYR A 1 78  ? 24.691 -1.434  -3.922  1.00 44.47  ? 78  TYR A N    1 
ATOM   1151 C CA   . TYR A 1 78  ? 23.883 -2.369  -3.118  1.00 43.61  ? 78  TYR A CA   1 
ATOM   1152 C C    . TYR A 1 78  ? 24.352 -2.293  -1.667  1.00 38.57  ? 78  TYR A C    1 
ATOM   1153 O O    . TYR A 1 78  ? 25.513 -1.960  -1.392  1.00 42.27  ? 78  TYR A O    1 
ATOM   1154 C CB   . TYR A 1 78  ? 23.977 -3.830  -3.683  1.00 47.58  ? 78  TYR A CB   1 
ATOM   1155 C CG   . TYR A 1 78  ? 23.048 -4.061  -4.909  1.00 46.78  ? 78  TYR A CG   1 
ATOM   1156 C CD1  . TYR A 1 78  ? 23.425 -3.663  -6.169  1.00 53.60  ? 78  TYR A CD1  1 
ATOM   1157 C CD2  . TYR A 1 78  ? 21.748 -4.555  -4.747  1.00 47.79  ? 78  TYR A CD2  1 
ATOM   1158 C CE1  . TYR A 1 78  ? 22.566 -3.801  -7.267  1.00 58.10  ? 78  TYR A CE1  1 
ATOM   1159 C CE2  . TYR A 1 78  ? 20.871 -4.685  -5.816  1.00 50.23  ? 78  TYR A CE2  1 
ATOM   1160 C CZ   . TYR A 1 78  ? 21.295 -4.301  -7.084  1.00 59.33  ? 78  TYR A CZ   1 
ATOM   1161 O OH   . TYR A 1 78  ? 20.469 -4.419  -8.176  1.00 61.56  ? 78  TYR A OH   1 
ATOM   1162 H H    . TYR A 1 78  ? 25.457 -1.763  -4.133  1.00 53.44  ? 78  TYR A H    1 
ATOM   1163 H HA   . TYR A 1 78  ? 22.943 -2.131  -3.147  1.00 52.41  ? 78  TYR A HA   1 
ATOM   1164 H HB2  . TYR A 1 78  ? 24.890 -4.003  -3.961  1.00 57.18  ? 78  TYR A HB2  1 
ATOM   1165 H HB3  . TYR A 1 78  ? 23.718 -4.455  -2.988  1.00 57.18  ? 78  TYR A HB3  1 
ATOM   1166 H HD1  . TYR A 1 78  ? 24.269 -3.293  -6.296  1.00 64.39  ? 78  TYR A HD1  1 
ATOM   1167 H HD2  . TYR A 1 78  ? 21.463 -4.803  -3.898  1.00 57.42  ? 78  TYR A HD2  1 
ATOM   1168 H HE1  . TYR A 1 78  ? 22.853 -3.557  -8.117  1.00 69.80  ? 78  TYR A HE1  1 
ATOM   1169 H HE2  . TYR A 1 78  ? 20.014 -5.025  -5.687  1.00 60.36  ? 78  TYR A HE2  1 
ATOM   1170 H HH   . TYR A 1 78  ? 19.781 -4.855  -7.971  1.00 73.95  ? 78  TYR A HH   1 
ATOM   1171 N N    . TYR A 1 79  ? 23.415 -2.435  -0.724  1.00 44.10  ? 79  TYR A N    1 
ATOM   1172 C CA   . TYR A 1 79  ? 23.759 -2.440  0.708   1.00 40.74  ? 79  TYR A CA   1 
ATOM   1173 C C    . TYR A 1 79  ? 23.419 -3.819  1.246   1.00 39.46  ? 79  TYR A C    1 
ATOM   1174 O O    . TYR A 1 79  ? 22.460 -4.437  0.787   1.00 41.71  ? 79  TYR A O    1 
ATOM   1175 C CB   . TYR A 1 79  ? 23.039 -1.334  1.555   1.00 37.66  ? 79  TYR A CB   1 
ATOM   1176 C CG   . TYR A 1 79  ? 23.572 0.070   1.186   1.00 39.99  ? 79  TYR A CG   1 
ATOM   1177 C CD1  . TYR A 1 79  ? 23.039 0.766   0.136   1.00 38.99  ? 79  TYR A CD1  1 
ATOM   1178 C CD2  . TYR A 1 79  ? 24.658 0.633   1.836   1.00 43.55  ? 79  TYR A CD2  1 
ATOM   1179 C CE1  . TYR A 1 79  ? 23.519 2.033   -0.242  1.00 39.68  ? 79  TYR A CE1  1 
ATOM   1180 C CE2  . TYR A 1 79  ? 25.189 1.913   1.439   1.00 42.10  ? 79  TYR A CE2  1 
ATOM   1181 C CZ   . TYR A 1 79  ? 24.595 2.583   0.398   1.00 44.74  ? 79  TYR A CZ   1 
ATOM   1182 O OH   . TYR A 1 79  ? 25.040 3.819   -0.078  1.00 50.13  ? 79  TYR A OH   1 
ATOM   1183 H H    . TYR A 1 79  ? 22.576 -2.531  -0.886  1.00 53.00  ? 79  TYR A H    1 
ATOM   1184 H HA   . TYR A 1 79  ? 24.705 -2.249  0.811   1.00 48.96  ? 79  TYR A HA   1 
ATOM   1185 H HB2  . TYR A 1 79  ? 22.085 -1.360  1.377   1.00 45.28  ? 79  TYR A HB2  1 
ATOM   1186 H HB3  . TYR A 1 79  ? 23.204 -1.490  2.498   1.00 45.28  ? 79  TYR A HB3  1 
ATOM   1187 H HD1  . TYR A 1 79  ? 22.337 0.390   -0.344  1.00 46.86  ? 79  TYR A HD1  1 
ATOM   1188 H HD2  . TYR A 1 79  ? 25.053 0.176   2.543   1.00 52.33  ? 79  TYR A HD2  1 
ATOM   1189 H HE1  . TYR A 1 79  ? 23.103 2.499   -0.931  1.00 47.70  ? 79  TYR A HE1  1 
ATOM   1190 H HE2  . TYR A 1 79  ? 25.921 2.278   1.880   1.00 50.60  ? 79  TYR A HE2  1 
ATOM   1191 H HH   . TYR A 1 79  ? 25.684 4.091   0.387   1.00 60.23  ? 79  TYR A HH   1 
ATOM   1192 N N    . ARG A 1 80  ? 24.218 -4.289  2.207   1.00 40.77  ? 80  ARG A N    1 
ATOM   1193 C CA   . ARG A 1 80  ? 24.009 -5.591  2.795   1.00 39.70  ? 80  ARG A CA   1 
ATOM   1194 C C    . ARG A 1 80  ? 24.189 -5.581  4.308   1.00 38.51  ? 80  ARG A C    1 
ATOM   1195 O O    . ARG A 1 80  ? 25.006 -4.838  4.873   1.00 43.43  ? 80  ARG A O    1 
ATOM   1196 C CB   . ARG A 1 80  ? 25.021 -6.632  2.211   1.00 45.13  ? 80  ARG A CB   1 
ATOM   1197 C CG   . ARG A 1 80  ? 26.448 -6.367  2.667   1.00 42.45  ? 80  ARG A CG   1 
ATOM   1198 C CD   . ARG A 1 80  ? 27.377 -7.429  2.142   1.00 46.27  ? 80  ARG A CD   1 
ATOM   1199 N NE   . ARG A 1 80  ? 27.476 -8.583  3.015   1.00 43.12  ? 80  ARG A NE   1 
ATOM   1200 C CZ   . ARG A 1 80  ? 28.317 -8.628  4.025   1.00 47.73  ? 80  ARG A CZ   1 
ATOM   1201 N NH1  . ARG A 1 80  ? 29.089 -7.595  4.316   1.00 48.73  ? 80  ARG A NH1  1 
ATOM   1202 N NH2  . ARG A 1 80  ? 28.363 -9.717  4.792   1.00 48.28  ? 80  ARG A NH2  1 
ATOM   1203 H H    . ARG A 1 80  ? 24.890 -3.861  2.530   1.00 49.00  ? 80  ARG A H    1 
ATOM   1204 H HA   . ARG A 1 80  ? 23.091 -5.845  2.612   1.00 47.72  ? 80  ARG A HA   1 
ATOM   1205 H HB2  . ARG A 1 80  ? 24.769 -7.520  2.507   1.00 54.24  ? 80  ARG A HB2  1 
ATOM   1206 H HB3  . ARG A 1 80  ? 25.000 -6.586  1.242   1.00 54.24  ? 80  ARG A HB3  1 
ATOM   1207 H HG2  . ARG A 1 80  ? 26.742 -5.506  2.330   1.00 51.02  ? 80  ARG A HG2  1 
ATOM   1208 H HG3  . ARG A 1 80  ? 26.486 -6.375  3.636   1.00 51.02  ? 80  ARG A HG3  1 
ATOM   1209 H HD2  . ARG A 1 80  ? 27.052 -7.734  1.281   1.00 55.60  ? 80  ARG A HD2  1 
ATOM   1210 H HD3  . ARG A 1 80  ? 28.265 -7.051  2.047   1.00 55.60  ? 80  ARG A HD3  1 
ATOM   1211 H HE   . ARG A 1 80  ? 26.967 -9.260  2.867   1.00 51.82  ? 80  ARG A HE   1 
ATOM   1212 H HH11 . ARG A 1 80  ? 29.046 -6.879  3.841   1.00 58.56  ? 80  ARG A HH11 1 
ATOM   1213 H HH12 . ARG A 1 80  ? 29.635 -7.639  4.979   1.00 58.56  ? 80  ARG A HH12 1 
ATOM   1214 H HH21 . ARG A 1 80  ? 27.846 -10.383 4.625   1.00 58.01  ? 80  ARG A HH21 1 
ATOM   1215 H HH22 . ARG A 1 80  ? 28.911 -9.754  5.454   1.00 58.01  ? 80  ARG A HH22 1 
ATOM   1216 N N    . LEU A 1 81  ? 23.486 -6.492  4.961   1.00 46.63  ? 81  LEU A N    1 
ATOM   1217 C CA   . LEU A 1 81  ? 23.599 -6.659  6.411   1.00 42.63  ? 81  LEU A CA   1 
ATOM   1218 C C    . LEU A 1 81  ? 24.814 -7.548  6.643   1.00 44.76  ? 81  LEU A C    1 
ATOM   1219 O O    . LEU A 1 81  ? 24.900 -8.631  6.057   1.00 47.52  ? 81  LEU A O    1 
ATOM   1220 C CB   . LEU A 1 81  ? 22.303 -7.265  6.935   1.00 41.17  ? 81  LEU A CB   1 
ATOM   1221 C CG   . LEU A 1 81  ? 21.961 -7.159  8.407   1.00 50.35  ? 81  LEU A CG   1 
ATOM   1222 C CD1  . LEU A 1 81  ? 21.793 -5.745  8.936   1.00 48.32  ? 81  LEU A CD1  1 
ATOM   1223 C CD2  . LEU A 1 81  ? 20.668 -7.975  8.727   1.00 50.22  ? 81  LEU A CD2  1 
ATOM   1224 H H    . LEU A 1 81  ? 22.931 -7.034  4.590   1.00 56.04  ? 81  LEU A H    1 
ATOM   1225 H HA   . LEU A 1 81  ? 23.730 -5.825  6.889   1.00 51.24  ? 81  LEU A HA   1 
ATOM   1226 H HB2  . LEU A 1 81  ? 21.574 -6.840  6.457   1.00 49.48  ? 81  LEU A HB2  1 
ATOM   1227 H HB3  . LEU A 1 81  ? 22.326 -8.213  6.730   1.00 49.48  ? 81  LEU A HB3  1 
ATOM   1228 H HG   . LEU A 1 81  ? 22.731 -7.525  8.871   1.00 60.50  ? 81  LEU A HG   1 
ATOM   1229 H HD11 . LEU A 1 81  ? 21.575 -5.784  9.880   1.00 58.06  ? 81  LEU A HD11 1 
ATOM   1230 H HD12 . LEU A 1 81  ? 22.623 -5.259  8.808   1.00 58.06  ? 81  LEU A HD12 1 
ATOM   1231 H HD13 . LEU A 1 81  ? 21.076 -5.309  8.449   1.00 58.06  ? 81  LEU A HD13 1 
ATOM   1232 H HD21 . LEU A 1 81  ? 20.538 -7.995  9.688   1.00 60.34  ? 81  LEU A HD21 1 
ATOM   1233 H HD22 . LEU A 1 81  ? 19.911 -7.546  8.299   1.00 60.34  ? 81  LEU A HD22 1 
ATOM   1234 H HD23 . LEU A 1 81  ? 20.773 -8.878  8.389   1.00 60.34  ? 81  LEU A HD23 1 
ATOM   1235 N N    . THR A 1 82  ? 25.785 -7.080  7.443   1.00 45.06  ? 82  THR A N    1 
ATOM   1236 C CA   . THR A 1 82  ? 26.965 -7.885  7.751   1.00 47.97  ? 82  THR A CA   1 
ATOM   1237 C C    . THR A 1 82  ? 26.629 -8.935  8.794   1.00 49.68  ? 82  THR A C    1 
ATOM   1238 O O    . THR A 1 82  ? 25.590 -8.886  9.477   1.00 51.40  ? 82  THR A O    1 
ATOM   1239 C CB   . THR A 1 82  ? 28.119 -7.070  8.360   1.00 49.38  ? 82  THR A CB   1 
ATOM   1240 O OG1  . THR A 1 82  ? 27.650 -6.577  9.640   1.00 50.04  ? 82  THR A OG1  1 
ATOM   1241 C CG2  . THR A 1 82  ? 28.531 -5.862  7.484   1.00 46.22  ? 82  THR A CG2  1 
ATOM   1242 H H    . THR A 1 82  ? 25.779 -6.305  7.815   1.00 54.15  ? 82  THR A H    1 
ATOM   1243 H HA   . THR A 1 82  ? 27.246 -8.269  6.905   1.00 57.65  ? 82  THR A HA   1 
ATOM   1244 H HB   . THR A 1 82  ? 28.907 -7.630  8.440   1.00 59.34  ? 82  THR A HB   1 
ATOM   1245 H HG1  . THR A 1 82  ? 28.252 -6.123  10.010  1.00 60.12  ? 82  THR A HG1  1 
ATOM   1246 H HG21 . THR A 1 82  ? 29.294 -5.411  7.878   1.00 55.54  ? 82  THR A HG21 1 
ATOM   1247 H HG22 . THR A 1 82  ? 28.770 -6.164  6.593   1.00 55.54  ? 82  THR A HG22 1 
ATOM   1248 H HG23 . THR A 1 82  ? 27.795 -5.235  7.417   1.00 55.54  ? 82  THR A HG23 1 
ATOM   1249 N N    . GLU A 1 83  ? 27.604 -9.803  9.042   1.00 49.04  ? 83  GLU A N    1 
ATOM   1250 C CA   . GLU A 1 83  ? 27.412 -10.875 10.010  1.00 57.96  ? 83  GLU A CA   1 
ATOM   1251 C C    . GLU A 1 83  ? 27.147 -10.311 11.396  1.00 55.83  ? 83  GLU A C    1 
ATOM   1252 O O    . GLU A 1 83  ? 26.365 -10.870 12.167  1.00 60.45  ? 83  GLU A O    1 
ATOM   1253 C CB   . GLU A 1 83  ? 28.663 -11.762 9.977   1.00 65.86  ? 83  GLU A CB   1 
ATOM   1254 C CG   . GLU A 1 83  ? 28.742 -12.572 8.675   1.00 66.69  ? 83  GLU A CG   1 
ATOM   1255 C CD   . GLU A 1 83  ? 30.154 -13.042 8.339   1.00 75.86  ? 83  GLU A CD   1 
ATOM   1256 O OE1  . GLU A 1 83  ? 30.838 -13.637 9.215   1.00 79.28  ? 83  GLU A OE1  1 
ATOM   1257 O OE2  . GLU A 1 83  ? 30.588 -12.783 7.191   1.00 74.15  ? 83  GLU A OE2  1 
ATOM   1258 H H    . GLU A 1 83  ? 28.378 -9.793  8.668   1.00 58.92  ? 83  GLU A H    1 
ATOM   1259 H HA   . GLU A 1 83  ? 26.642 -11.419 9.782   1.00 69.63  ? 83  GLU A HA   1 
ATOM   1260 H HB2  . GLU A 1 83  ? 29.453 -11.204 10.039  1.00 79.11  ? 83  GLU A HB2  1 
ATOM   1261 H HB3  . GLU A 1 83  ? 28.635 -12.382 10.722  1.00 79.11  ? 83  GLU A HB3  1 
ATOM   1262 H HG2  . GLU A 1 83  ? 28.180 -13.357 8.759   1.00 80.10  ? 83  GLU A HG2  1 
ATOM   1263 H HG3  . GLU A 1 83  ? 28.431 -12.018 7.942   1.00 80.10  ? 83  GLU A HG3  1 
ATOM   1264 N N    . ILE A 1 84  ? 27.788 -9.193  11.735  1.00 61.85  ? 84  ILE A N    1 
ATOM   1265 C CA   . ILE A 1 84  ? 27.550 -8.558  13.030  1.00 63.96  ? 84  ILE A CA   1 
ATOM   1266 C C    . ILE A 1 84  ? 26.132 -8.031  13.125  1.00 63.19  ? 84  ILE A C    1 
ATOM   1267 O O    . ILE A 1 84  ? 25.498 -8.081  14.196  1.00 63.96  ? 84  ILE A O    1 
ATOM   1268 C CB   . ILE A 1 84  ? 28.562 -7.421  13.279  1.00 64.98  ? 84  ILE A CB   1 
ATOM   1269 C CG1  . ILE A 1 84  ? 29.993 -7.956  13.139  1.00 66.05  ? 84  ILE A CG1  1 
ATOM   1270 C CG2  . ILE A 1 84  ? 28.219 -6.795  14.622  1.00 70.59  ? 84  ILE A CG2  1 
ATOM   1271 C CD1  . ILE A 1 84  ? 31.031 -6.841  12.798  1.00 70.00  ? 84  ILE A CD1  1 
ATOM   1272 H H    . ILE A 1 84  ? 28.360 -8.786  11.238  1.00 74.30  ? 84  ILE A H    1 
ATOM   1273 H HA   . ILE A 1 84  ? 27.673 -9.239  13.710  1.00 76.83  ? 84  ILE A HA   1 
ATOM   1274 H HB   . ILE A 1 84  ? 28.507 -6.715  12.616  1.00 78.06  ? 84  ILE A HB   1 
ATOM   1275 H HG12 . ILE A 1 84  ? 30.259 -8.367  13.977  1.00 79.33  ? 84  ILE A HG12 1 
ATOM   1276 H HG13 . ILE A 1 84  ? 30.015 -8.613  12.426  1.00 79.33  ? 84  ILE A HG13 1 
ATOM   1277 H HG21 . ILE A 1 84  ? 28.914 -6.162  14.862  1.00 84.79  ? 84  ILE A HG21 1 
ATOM   1278 H HG22 . ILE A 1 84  ? 27.366 -6.338  14.549  1.00 84.79  ? 84  ILE A HG22 1 
ATOM   1279 H HG23 . ILE A 1 84  ? 28.163 -7.494  15.292  1.00 84.79  ? 84  ILE A HG23 1 
ATOM   1280 H HD11 . ILE A 1 84  ? 31.902 -7.249  12.669  1.00 84.08  ? 84  ILE A HD11 1 
ATOM   1281 H HD12 . ILE A 1 84  ? 30.754 -6.388  11.987  1.00 84.08  ? 84  ILE A HD12 1 
ATOM   1282 H HD13 . ILE A 1 84  ? 31.068 -6.209  13.533  1.00 84.08  ? 84  ILE A HD13 1 
ATOM   1283 N N    . GLY A 1 85  ? 25.623 -7.471  12.027  1.00 52.61  ? 85  GLY A N    1 
ATOM   1284 C CA   . GLY A 1 85  ? 24.302 -6.904  12.073  1.00 53.17  ? 85  GLY A CA   1 
ATOM   1285 C C    . GLY A 1 85  ? 23.244 -7.971  12.213  1.00 53.15  ? 85  GLY A C    1 
ATOM   1286 O O    . GLY A 1 85  ? 22.279 -7.807  12.963  1.00 56.67  ? 85  GLY A O    1 
ATOM   1287 H H    . GLY A 1 85  ? 26.021 -7.413  11.267  1.00 63.21  ? 85  GLY A H    1 
ATOM   1288 H HA2  . GLY A 1 85  ? 24.234 -6.301  12.830  1.00 63.89  ? 85  GLY A HA2  1 
ATOM   1289 H HA3  . GLY A 1 85  ? 24.134 -6.407  11.257  1.00 63.89  ? 85  GLY A HA3  1 
ATOM   1290 N N    . HIS A 1 86  ? 23.409 -9.096  11.521  1.00 54.53  ? 86  HIS A N    1 
ATOM   1291 C CA   . HIS A 1 86  ? 22.461 -10.173 11.780  1.00 54.93  ? 86  HIS A CA   1 
ATOM   1292 C C    . HIS A 1 86  ? 22.468 -10.537 13.255  1.00 58.50  ? 86  HIS A C    1 
ATOM   1293 O O    . HIS A 1 86  ? 21.424 -10.824 13.839  1.00 54.76  ? 86  HIS A O    1 
ATOM   1294 C CB   . HIS A 1 86  ? 22.804 -11.404 10.966  1.00 54.23  ? 86  HIS A CB   1 
ATOM   1295 C CG   . HIS A 1 86  ? 22.366 -11.334 9.546   1.00 51.30  ? 86  HIS A CG   1 
ATOM   1296 N ND1  . HIS A 1 86  ? 23.199 -10.928 8.533   1.00 46.53  ? 86  HIS A ND1  1 
ATOM   1297 C CD2  . HIS A 1 86  ? 21.183 -11.630 8.968   1.00 51.33  ? 86  HIS A CD2  1 
ATOM   1298 C CE1  . HIS A 1 86  ? 22.546 -10.975 7.389   1.00 51.22  ? 86  HIS A CE1  1 
ATOM   1299 N NE2  . HIS A 1 86  ? 21.316 -11.383 7.627   1.00 51.73  ? 86  HIS A NE2  1 
ATOM   1300 H H    . HIS A 1 86  ? 24.020 -9.251  10.937  1.00 65.51  ? 86  HIS A H    1 
ATOM   1301 H HA   . HIS A 1 86  ? 21.576 -9.877  11.514  1.00 65.99  ? 86  HIS A HA   1 
ATOM   1302 H HB2  . HIS A 1 86  ? 23.767 -11.522 10.971  1.00 65.15  ? 86  HIS A HB2  1 
ATOM   1303 H HB3  . HIS A 1 86  ? 22.373 -12.173 11.370  1.00 65.15  ? 86  HIS A HB3  1 
ATOM   1304 H HD2  . HIS A 1 86  ? 20.421 -11.944 9.398   1.00 61.68  ? 86  HIS A HD2  1 
ATOM   1305 H HE1  . HIS A 1 86  ? 22.895 -10.756 6.555   1.00 61.54  ? 86  HIS A HE1  1 
ATOM   1306 H HE2  . HIS A 1 86  ? 20.698 -11.479 7.037   1.00 62.15  ? 86  HIS A HE2  1 
ATOM   1307 N N    . GLU A 1 87  ? 23.641 -10.468 13.870  1.00 63.64  ? 87  GLU A N    1 
ATOM   1308 C CA   . GLU A 1 87  ? 23.796 -10.805 15.279  1.00 72.76  ? 87  GLU A CA   1 
ATOM   1309 C C    . GLU A 1 87  ? 23.107 -9.775  16.161  1.00 72.89  ? 87  GLU A C    1 
ATOM   1310 O O    . GLU A 1 87  ? 22.340 -10.124 17.072  1.00 69.79  ? 87  GLU A O    1 
ATOM   1311 C CB   . GLU A 1 87  ? 25.287 -10.899 15.585  1.00 69.79  ? 87  GLU A CB   1 
ATOM   1312 C CG   . GLU A 1 87  ? 25.609 -11.791 16.693  1.00 90.10  ? 87  GLU A CG   1 
ATOM   1313 C CD   . GLU A 1 87  ? 25.196 -13.209 16.349  1.00 95.90  ? 87  GLU A CD   1 
ATOM   1314 O OE1  . GLU A 1 87  ? 25.320 -13.565 15.150  1.00 85.15  ? 87  GLU A OE1  1 
ATOM   1315 O OE2  . GLU A 1 87  ? 24.732 -13.936 17.267  1.00 95.76  ? 87  GLU A OE2  1 
ATOM   1316 H H    . GLU A 1 87  ? 24.374 -10.225 13.491  1.00 76.44  ? 87  GLU A H    1 
ATOM   1317 H HA   . GLU A 1 87  ? 23.385 -11.663 15.470  1.00 87.39  ? 87  GLU A HA   1 
ATOM   1318 H HB2  . GLU A 1 87  ? 25.746 -11.230 14.797  1.00 83.82  ? 87  GLU A HB2  1 
ATOM   1319 H HB3  . GLU A 1 87  ? 25.614 -10.015 15.813  1.00 83.82  ? 87  GLU A HB3  1 
ATOM   1320 H HG2  . GLU A 1 87  ? 26.565 -11.775 16.858  1.00 108.20 ? 87  GLU A HG2  1 
ATOM   1321 H HG3  . GLU A 1 87  ? 25.130 -11.510 17.488  1.00 108.20 ? 87  GLU A HG3  1 
ATOM   1322 N N    . ASN A 1 88  ? 23.412 -8.490  15.942  1.00 66.48  ? 88  ASN A N    1 
ATOM   1323 C CA   . ASN A 1 88  ? 22.752 -7.441  16.698  1.00 64.64  ? 88  ASN A CA   1 
ATOM   1324 C C    . ASN A 1 88  ? 21.246 -7.543  16.570  1.00 66.46  ? 88  ASN A C    1 
ATOM   1325 O O    . ASN A 1 88  ? 20.530 -7.390  17.556  1.00 74.99  ? 88  ASN A O    1 
ATOM   1326 C CB   . ASN A 1 88  ? 23.221 -6.065  16.252  1.00 72.85  ? 88  ASN A CB   1 
ATOM   1327 C CG   . ASN A 1 88  ? 24.498 -5.644  16.935  1.00 81.14  ? 88  ASN A CG   1 
ATOM   1328 O OD1  . ASN A 1 88  ? 25.393 -6.453  17.143  1.00 85.66  ? 88  ASN A OD1  1 
ATOM   1329 N ND2  . ASN A 1 88  ? 24.581 -4.377  17.307  1.00 81.74  ? 88  ASN A ND2  1 
ATOM   1330 H H    . ASN A 1 88  ? 23.990 -8.211  15.369  1.00 79.85  ? 88  ASN A H    1 
ATOM   1331 H HA   . ASN A 1 88  ? 22.996 -7.544  17.632  1.00 77.65  ? 88  ASN A HA   1 
ATOM   1332 H HB2  . ASN A 1 88  ? 23.381 -6.079  15.296  1.00 87.49  ? 88  ASN A HB2  1 
ATOM   1333 H HB3  . ASN A 1 88  ? 22.536 -5.412  16.465  1.00 87.49  ? 88  ASN A HB3  1 
ATOM   1334 H HD21 . ASN A 1 88  ? 25.290 -4.090  17.700  1.00 98.16  ? 88  ASN A HD21 1 
ATOM   1335 H HD22 . ASN A 1 88  ? 23.926 -3.840  17.156  1.00 98.16  ? 88  ASN A HD22 1 
ATOM   1336 N N    . MET A 1 89  ? 20.743 -7.810  15.375  1.00 62.01  ? 89  MET A N    1 
ATOM   1337 C CA   . MET A 1 89  ? 19.300 -7.953  15.231  1.00 66.17  ? 89  MET A CA   1 
ATOM   1338 C C    . MET A 1 89  ? 18.760 -9.118  16.041  1.00 68.29  ? 89  MET A C    1 
ATOM   1339 O O    . MET A 1 89  ? 17.572 -9.140  16.395  1.00 66.25  ? 89  MET A O    1 
ATOM   1340 C CB   . MET A 1 89  ? 18.923 -8.120  13.776  1.00 65.49  ? 89  MET A CB   1 
ATOM   1341 C CG   . MET A 1 89  ? 19.335 -6.907  12.924  1.00 68.19  ? 89  MET A CG   1 
ATOM   1342 S SD   . MET A 1 89  ? 18.575 -5.346  13.515  1.00 75.27  ? 89  MET A SD   1 
ATOM   1343 C CE   . MET A 1 89  ? 16.927 -5.500  12.773  1.00 57.01  ? 89  MET A CE   1 
ATOM   1344 H H    . MET A 1 89  ? 21.199 -7.910  14.653  1.00 74.48  ? 89  MET A H    1 
ATOM   1345 H HA   . MET A 1 89  ? 18.892 -7.134  15.552  1.00 79.48  ? 89  MET A HA   1 
ATOM   1346 H HB2  . MET A 1 89  ? 19.369 -8.905  13.421  1.00 78.66  ? 89  MET A HB2  1 
ATOM   1347 H HB3  . MET A 1 89  ? 17.962 -8.226  13.708  1.00 78.66  ? 89  MET A HB3  1 
ATOM   1348 H HG2  . MET A 1 89  ? 20.299 -6.806  12.960  1.00 81.91  ? 89  MET A HG2  1 
ATOM   1349 H HG3  . MET A 1 89  ? 19.051 -7.052  12.007  1.00 81.91  ? 89  MET A HG3  1 
ATOM   1350 H HE1  . MET A 1 89  ? 16.398 -4.722  13.014  1.00 68.49  ? 89  MET A HE1  1 
ATOM   1351 H HE2  . MET A 1 89  ? 17.018 -5.553  11.809  1.00 68.49  ? 89  MET A HE2  1 
ATOM   1352 H HE3  . MET A 1 89  ? 16.503 -6.305  13.110  1.00 68.49  ? 89  MET A HE3  1 
ATOM   1353 N N    . ARG A 1 90  ? 19.577 -10.148 16.267  1.00 67.25  ? 90  ARG A N    1 
ATOM   1354 C CA   . ARG A 1 90  ? 19.099 -11.262 17.072  1.00 71.61  ? 90  ARG A CA   1 
ATOM   1355 C C    . ARG A 1 90  ? 19.074 -10.889 18.542  1.00 68.87  ? 90  ARG A C    1 
ATOM   1356 O O    . ARG A 1 90  ? 18.065 -11.106 19.221  1.00 68.14  ? 90  ARG A O    1 
ATOM   1357 C CB   . ARG A 1 90  ? 19.978 -12.479 16.865  1.00 76.08  ? 90  ARG A CB   1 
ATOM   1358 C CG   . ARG A 1 90  ? 19.395 -13.745 17.485  1.00 85.93  ? 90  ARG A CG   1 
ATOM   1359 C CD   . ARG A 1 90  ? 20.304 -14.910 17.203  1.00 86.27  ? 90  ARG A CD   1 
ATOM   1360 N NE   . ARG A 1 90  ? 21.653 -14.564 17.632  1.00 85.35  ? 90  ARG A NE   1 
ATOM   1361 C CZ   . ARG A 1 90  ? 22.070 -14.622 18.887  1.00 88.18  ? 90  ARG A CZ   1 
ATOM   1362 N NH1  . ARG A 1 90  ? 21.268 -15.017 19.862  1.00 83.43  ? 90  ARG A NH1  1 
ATOM   1363 N NH2  . ARG A 1 90  ? 23.310 -14.246 19.171  1.00 96.80  ? 90  ARG A NH2  1 
ATOM   1364 H H    . ARG A 1 90  ? 20.382 -10.220 15.974  1.00 80.78  ? 90  ARG A H    1 
ATOM   1365 H HA   . ARG A 1 90  ? 18.200 -11.489 16.787  1.00 86.02  ? 90  ARG A HA   1 
ATOM   1366 H HB2  . ARG A 1 90  ? 20.086 -12.632 15.914  1.00 91.38  ? 90  ARG A HB2  1 
ATOM   1367 H HB3  . ARG A 1 90  ? 20.843 -12.316 17.275  1.00 91.38  ? 90  ARG A HB3  1 
ATOM   1368 H HG2  . ARG A 1 90  ? 19.316 -13.634 18.445  1.00 103.20 ? 90  ARG A HG2  1 
ATOM   1369 H HG3  . ARG A 1 90  ? 18.524 -13.928 17.099  1.00 103.20 ? 90  ARG A HG3  1 
ATOM   1370 H HD2  . ARG A 1 90  ? 20.006 -15.690 17.695  1.00 103.61 ? 90  ARG A HD2  1 
ATOM   1371 H HD3  . ARG A 1 90  ? 20.314 -15.101 16.252  1.00 103.61 ? 90  ARG A HD3  1 
ATOM   1372 H HE   . ARG A 1 90  ? 22.213 -14.307 17.032  1.00 102.50 ? 90  ARG A HE   1 
ATOM   1373 H HH11 . ARG A 1 90  ? 20.457 -15.243 19.687  1.00 100.20 ? 90  ARG A HH11 1 
ATOM   1374 H HH12 . ARG A 1 90  ? 21.557 -15.048 20.672  1.00 100.20 ? 90  ARG A HH12 1 
ATOM   1375 H HH21 . ARG A 1 90  ? 23.830 -13.970 18.544  1.00 116.24 ? 90  ARG A HH21 1 
ATOM   1376 H HH22 . ARG A 1 90  ? 23.594 -14.278 19.982  1.00 116.24 ? 90  ARG A HH22 1 
ATOM   1377 N N    . LEU A 1 91  ? 20.187 -10.365 19.059  1.00 73.38  ? 91  LEU A N    1 
ATOM   1378 C CA   . LEU A 1 91  ? 20.209 -9.838  20.422  1.00 78.31  ? 91  LEU A CA   1 
ATOM   1379 C C    . LEU A 1 91  ? 19.097 -8.826  20.641  1.00 82.01  ? 91  LEU A C    1 
ATOM   1380 O O    . LEU A 1 91  ? 18.486 -8.783  21.711  1.00 88.16  ? 91  LEU A O    1 
ATOM   1381 C CB   . LEU A 1 91  ? 21.538 -9.174  20.725  1.00 75.62  ? 91  LEU A CB   1 
ATOM   1382 C CG   . LEU A 1 91  ? 22.718 -10.103 20.587  1.00 84.39  ? 91  LEU A CG   1 
ATOM   1383 C CD1  . LEU A 1 91  ? 23.895 -9.437  21.286  1.00 92.97  ? 91  LEU A CD1  1 
ATOM   1384 C CD2  . LEU A 1 91  ? 22.425 -11.499 21.201  1.00 86.80  ? 91  LEU A CD2  1 
ATOM   1385 H H    . LEU A 1 91  ? 20.938 -10.302 18.644  1.00 88.14  ? 91  LEU A H    1 
ATOM   1386 H HA   . LEU A 1 91  ? 20.091 -10.587 21.028  1.00 94.04  ? 91  LEU A HA   1 
ATOM   1387 H HB2  . LEU A 1 91  ? 21.666 -8.437  20.108  1.00 90.82  ? 91  LEU A HB2  1 
ATOM   1388 H HB3  . LEU A 1 91  ? 21.522 -8.845  21.637  1.00 90.82  ? 91  LEU A HB3  1 
ATOM   1389 H HG   . LEU A 1 91  ? 22.922 -10.262 19.652  1.00 101.34 ? 91  LEU A HG   1 
ATOM   1390 H HD11 . LEU A 1 91  ? 24.707 -9.632  20.793  1.00 111.64 ? 91  LEU A HD11 1 
ATOM   1391 H HD12 . LEU A 1 91  ? 23.746 -8.479  21.312  1.00 111.64 ? 91  LEU A HD12 1 
ATOM   1392 H HD13 . LEU A 1 91  ? 23.965 -9.785  22.189  1.00 111.64 ? 91  LEU A HD13 1 
ATOM   1393 H HD21 . LEU A 1 91  ? 23.261 -11.979 21.307  1.00 104.24 ? 91  LEU A HD21 1 
ATOM   1394 H HD22 . LEU A 1 91  ? 21.999 -11.381 22.064  1.00 104.24 ? 91  LEU A HD22 1 
ATOM   1395 H HD23 . LEU A 1 91  ? 21.836 -11.988 20.605  1.00 104.24 ? 91  LEU A HD23 1 
ATOM   1396 N N    . ARG A 1 92  ? 18.861 -7.953  19.686  1.00 73.05  ? 92  ARG A N    1 
ATOM   1397 C CA   . ARG A 1 92  ? 17.843 -6.945  19.922  1.00 78.08  ? 92  ARG A CA   1 
ATOM   1398 C C    . ARG A 1 92  ? 16.464 -7.567  20.001  1.00 76.29  ? 92  ARG A C    1 
ATOM   1399 O O    . ARG A 1 92  ? 15.655 -7.208  20.860  1.00 79.84  ? 92  ARG A O    1 
ATOM   1400 C CB   . ARG A 1 92  ? 17.905 -5.892  18.843  1.00 81.20  ? 92  ARG A CB   1 
ATOM   1401 C CG   . ARG A 1 92  ? 19.195 -5.107  18.922  1.00 80.64  ? 92  ARG A CG   1 
ATOM   1402 C CD   . ARG A 1 92  ? 19.148 -4.107  17.804  1.00 84.45  ? 92  ARG A CD   1 
ATOM   1403 N NE   . ARG A 1 92  ? 20.414 -3.419  17.647  1.00 77.67  ? 92  ARG A NE   1 
ATOM   1404 C CZ   . ARG A 1 92  ? 20.667 -2.595  16.651  1.00 83.96  ? 92  ARG A CZ   1 
ATOM   1405 N NH1  . ARG A 1 92  ? 19.762 -2.344  15.723  1.00 88.58  ? 92  ARG A NH1  1 
ATOM   1406 N NH2  . ARG A 1 92  ? 21.852 -2.003  16.590  1.00 93.26  ? 92  ARG A NH2  1 
ATOM   1407 H H    . ARG A 1 92  ? 19.256 -7.921  18.923  1.00 87.74  ? 92  ARG A H    1 
ATOM   1408 H HA   . ARG A 1 92  ? 18.017 -6.509  20.770  1.00 93.77  ? 92  ARG A HA   1 
ATOM   1409 H HB2  . ARG A 1 92  ? 17.858 -6.319  17.973  1.00 97.51  ? 92  ARG A HB2  1 
ATOM   1410 H HB3  . ARG A 1 92  ? 17.164 -5.276  18.951  1.00 97.51  ? 92  ARG A HB3  1 
ATOM   1411 H HG2  . ARG A 1 92  ? 19.261 -4.644  19.771  1.00 96.84  ? 92  ARG A HG2  1 
ATOM   1412 H HG3  . ARG A 1 92  ? 19.959 -5.693  18.803  1.00 96.84  ? 92  ARG A HG3  1 
ATOM   1413 H HD2  . ARG A 1 92  ? 18.945 -4.564  16.973  1.00 101.42 ? 92  ARG A HD2  1 
ATOM   1414 H HD3  . ARG A 1 92  ? 18.464 -3.446  17.994  1.00 101.42 ? 92  ARG A HD3  1 
ATOM   1415 H HE   . ARG A 1 92  ? 21.029 -3.555  18.233  1.00 93.28  ? 92  ARG A HE   1 
ATOM   1416 H HH11 . ARG A 1 92  ? 18.990 -2.721  15.763  1.00 106.37 ? 92  ARG A HH11 1 
ATOM   1417 H HH12 . ARG A 1 92  ? 19.944 -1.804  15.080  1.00 106.37 ? 92  ARG A HH12 1 
ATOM   1418 H HH21 . ARG A 1 92  ? 22.442 -2.159  17.196  1.00 111.99 ? 92  ARG A HH21 1 
ATOM   1419 H HH22 . ARG A 1 92  ? 22.031 -1.463  15.945  1.00 111.99 ? 92  ARG A HH22 1 
ATOM   1420 N N    . HIS A 1 93  ? 16.170 -8.508  19.132  1.00 72.49  ? 93  HIS A N    1 
ATOM   1421 C CA   . HIS A 1 93  ? 14.846 -9.110  19.189  1.00 79.05  ? 93  HIS A CA   1 
ATOM   1422 C C    . HIS A 1 93  ? 14.663 -9.957  20.450  1.00 80.19  ? 93  HIS A C    1 
ATOM   1423 O O    . HIS A 1 93  ? 13.531 -10.166 20.905  1.00 75.72  ? 93  HIS A O    1 
ATOM   1424 C CB   . HIS A 1 93  ? 14.617 -9.898  17.924  1.00 83.24  ? 93  HIS A CB   1 
ATOM   1425 C CG   . HIS A 1 93  ? 13.258 -10.480 17.828  1.00 82.27  ? 93  HIS A CG   1 
ATOM   1426 N ND1  . HIS A 1 93  ? 12.180 -9.758  17.364  1.00 87.80  ? 93  HIS A ND1  1 
ATOM   1427 C CD2  . HIS A 1 93  ? 12.804 -11.725 18.085  1.00 76.99  ? 93  HIS A CD2  1 
ATOM   1428 C CE1  . HIS A 1 93  ? 11.111 -10.535 17.372  1.00 100.50 ? 93  HIS A CE1  1 
ATOM   1429 N NE2  . HIS A 1 93  ? 11.463 -11.732 17.803  1.00 77.69  ? 93  HIS A NE2  1 
ATOM   1430 H H    . HIS A 1 93  ? 16.694 -8.810  18.520  1.00 87.06  ? 93  HIS A H    1 
ATOM   1431 H HA   . HIS A 1 93  ? 14.162 -8.423  19.231  1.00 94.94  ? 93  HIS A HA   1 
ATOM   1432 H HB2  . HIS A 1 93  ? 14.744 -9.311  17.162  1.00 99.96  ? 93  HIS A HB2  1 
ATOM   1433 H HB3  . HIS A 1 93  ? 15.256 -10.628 17.890  1.00 99.96  ? 93  HIS A HB3  1 
ATOM   1434 H HD2  . HIS A 1 93  ? 13.307 -12.443 18.395  1.00 92.46  ? 93  HIS A HD2  1 
ATOM   1435 H HE1  . HIS A 1 93  ? 10.253 -10.281 17.117  1.00 120.68 ? 93  HIS A HE1  1 
ATOM   1436 H HE2  . HIS A 1 93  ? 10.937 -12.406 17.893  1.00 93.31  ? 93  HIS A HE2  1 
ATOM   1437 N N    . GLU A 1 94  ? 15.755 -10.484 21.001  1.00 77.45  ? 94  GLU A N    1 
ATOM   1438 C CA   . GLU A 1 94  ? 15.650 -11.237 22.239  1.00 81.21  ? 94  GLU A CA   1 
ATOM   1439 C C    . GLU A 1 94  ? 15.530 -10.334 23.457  1.00 83.86  ? 94  GLU A C    1 
ATOM   1440 O O    . GLU A 1 94  ? 14.741 -10.610 24.369  1.00 83.58  ? 94  GLU A O    1 
ATOM   1441 C CB   . GLU A 1 94  ? 16.866 -12.128 22.425  1.00 71.90  ? 94  GLU A CB   1 
ATOM   1442 C CG   . GLU A 1 94  ? 16.958 -13.280 21.447  1.00 77.80  ? 94  GLU A CG   1 
ATOM   1443 C CD   . GLU A 1 94  ? 18.044 -14.241 21.861  1.00 81.15  ? 94  GLU A CD   1 
ATOM   1444 O OE1  . GLU A 1 94  ? 18.465 -14.163 23.050  1.00 88.28  ? 94  GLU A OE1  1 
ATOM   1445 O OE2  . GLU A 1 94  ? 18.460 -15.073 21.019  1.00 84.59  ? 94  GLU A OE2  1 
ATOM   1446 H H    . GLU A 1 94  ? 16.550 -10.420 20.681  1.00 93.01  ? 94  GLU A H    1 
ATOM   1447 H HA   . GLU A 1 94  ? 14.852 -11.784 22.170  1.00 97.53  ? 94  GLU A HA   1 
ATOM   1448 H HB2  . GLU A 1 94  ? 17.664 -11.587 22.317  1.00 86.36  ? 94  GLU A HB2  1 
ATOM   1449 H HB3  . GLU A 1 94  ? 16.839 -12.504 23.319  1.00 86.36  ? 94  GLU A HB3  1 
ATOM   1450 H HG2  . GLU A 1 94  ? 16.114 -13.757 21.427  1.00 93.43  ? 94  GLU A HG2  1 
ATOM   1451 H HG3  . GLU A 1 94  ? 17.167 -12.939 20.563  1.00 93.43  ? 94  GLU A HG3  1 
ATOM   1452 N N    . SER A 1 95  ? 16.385 -9.316  23.539  1.00 77.90  ? 95  SER A N    1 
ATOM   1453 C CA   . SER A 1 95  ? 16.254 -8.291  24.559  1.00 78.91  ? 95  SER A CA   1 
ATOM   1454 C C    . SER A 1 95  ? 14.794 -7.922  24.739  1.00 78.15  ? 95  SER A C    1 
ATOM   1455 O O    . SER A 1 95  ? 14.264 -8.012  25.854  1.00 81.63  ? 95  SER A O    1 
ATOM   1456 C CB   . SER A 1 95  ? 17.075 -7.053  24.178  1.00 81.84  ? 95  SER A CB   1 
ATOM   1457 O OG   . SER A 1 95  ? 18.328 -7.067  24.826  1.00 82.90  ? 95  SER A OG   1 
ATOM   1458 H H    . SER A 1 95  ? 17.053 -9.199  23.010  1.00 93.56  ? 95  SER A H    1 
ATOM   1459 H HA   . SER A 1 95  ? 16.608 -8.628  25.397  1.00 94.77  ? 95  SER A HA   1 
ATOM   1460 H HB2  . SER A 1 95  ? 17.215 -7.050  23.218  1.00 98.29  ? 95  SER A HB2  1 
ATOM   1461 H HB3  . SER A 1 95  ? 16.590 -6.257  24.445  1.00 98.29  ? 95  SER A HB3  1 
ATOM   1462 H HG   . SER A 1 95  ? 18.229 -7.250  25.640  1.00 99.56  ? 95  SER A HG   1 
ATOM   1463 N N    . TRP A 1 96  ? 14.134 -7.486  23.652  1.00 73.20  ? 96  TRP A N    1 
ATOM   1464 C CA   . TRP A 1 96  ? 12.779 -6.954  23.744  1.00 73.00  ? 96  TRP A CA   1 
ATOM   1465 C C    . TRP A 1 96  ? 11.746 -8.041  24.011  1.00 74.76  ? 96  TRP A C    1 
ATOM   1466 O O    . TRP A 1 96  ? 10.638 -7.740  24.493  1.00 69.23  ? 96  TRP A O    1 
ATOM   1467 C CB   . TRP A 1 96  ? 12.359 -6.190  22.469  1.00 73.72  ? 96  TRP A CB   1 
ATOM   1468 C CG   . TRP A 1 96  ? 12.802 -4.765  22.410  1.00 72.36  ? 96  TRP A CG   1 
ATOM   1469 C CD1  . TRP A 1 96  ? 13.821 -4.252  21.663  1.00 73.00  ? 96  TRP A CD1  1 
ATOM   1470 C CD2  . TRP A 1 96  ? 12.244 -3.660  23.136  1.00 69.37  ? 96  TRP A CD2  1 
ATOM   1471 N NE1  . TRP A 1 96  ? 13.930 -2.905  21.883  1.00 69.47  ? 96  TRP A NE1  1 
ATOM   1472 C CE2  . TRP A 1 96  ? 12.971 -2.519  22.781  1.00 68.82  ? 96  TRP A CE2  1 
ATOM   1473 C CE3  . TRP A 1 96  ? 11.201 -3.528  24.058  1.00 68.26  ? 96  TRP A CE3  1 
ATOM   1474 C CZ2  . TRP A 1 96  ? 12.705 -1.259  23.332  1.00 70.17  ? 96  TRP A CZ2  1 
ATOM   1475 C CZ3  . TRP A 1 96  ? 10.935 -2.273  24.601  1.00 68.60  ? 96  TRP A CZ3  1 
ATOM   1476 C CH2  . TRP A 1 96  ? 11.689 -1.165  24.242  1.00 64.17  ? 96  TRP A CH2  1 
ATOM   1477 H H    . TRP A 1 96  ? 14.454 -7.491  22.853  1.00 87.91  ? 96  TRP A H    1 
ATOM   1478 H HA   . TRP A 1 96  ? 12.784 -6.319  24.477  1.00 87.68  ? 96  TRP A HA   1 
ATOM   1479 H HB2  . TRP A 1 96  ? 12.737 -6.644  21.700  1.00 88.54  ? 96  TRP A HB2  1 
ATOM   1480 H HB3  . TRP A 1 96  ? 11.390 -6.195  22.413  1.00 88.54  ? 96  TRP A HB3  1 
ATOM   1481 H HD1  . TRP A 1 96  ? 14.362 -4.745  21.088  1.00 87.67  ? 96  TRP A HD1  1 
ATOM   1482 H HE1  . TRP A 1 96  ? 14.508 -2.384  21.516  1.00 83.44  ? 96  TRP A HE1  1 
ATOM   1483 H HE3  . TRP A 1 96  ? 10.694 -4.266  24.305  1.00 81.99  ? 96  TRP A HE3  1 
ATOM   1484 H HZ2  . TRP A 1 96  ? 13.202 -0.512  23.087  1.00 84.28  ? 96  TRP A HZ2  1 
ATOM   1485 H HZ3  . TRP A 1 96  ? 10.242 -2.177  25.214  1.00 82.39  ? 96  TRP A HZ3  1 
ATOM   1486 H HH2  . TRP A 1 96  ? 11.499 -0.340  24.628  1.00 77.08  ? 96  TRP A HH2  1 
ATOM   1487 N N    . SER A 1 97  ? 12.077 -9.298  23.731  1.00 77.90  ? 97  SER A N    1 
ATOM   1488 C CA   . SER A 1 97  ? 11.213 -10.378 24.176  1.00 78.66  ? 97  SER A CA   1 
ATOM   1489 C C    . SER A 1 97  ? 11.253 -10.517 25.695  1.00 75.61  ? 97  SER A C    1 
ATOM   1490 O O    . SER A 1 97  ? 10.202 -10.624 26.350  1.00 74.52  ? 97  SER A O    1 
ATOM   1491 C CB   . SER A 1 97  ? 11.629 -11.689 23.512  1.00 82.41  ? 97  SER A CB   1 
ATOM   1492 O OG   . SER A 1 97  ? 11.208 -11.701 22.161  1.00 83.41  ? 97  SER A OG   1 
ATOM   1493 H H    . SER A 1 97  ? 12.778 -9.544  23.297  1.00 93.56  ? 97  SER A H    1 
ATOM   1494 H HA   . SER A 1 97  ? 10.302 -10.180 23.910  1.00 94.47  ? 97  SER A HA   1 
ATOM   1495 H HB2  . SER A 1 97  ? 12.595 -11.772 23.545  1.00 98.97  ? 97  SER A HB2  1 
ATOM   1496 H HB3  . SER A 1 97  ? 11.216 -12.430 23.982  1.00 98.97  ? 97  SER A HB3  1 
ATOM   1497 H HG   . SER A 1 97  ? 11.578 -11.076 21.739  1.00 100.17 ? 97  SER A HG   1 
ATOM   1498 N N    . ARG A 1 98  ? 12.457 -10.520 26.285  1.00 75.09  ? 98  ARG A N    1 
ATOM   1499 C CA   . ARG A 1 98  ? 12.533 -10.614 27.745  1.00 79.66  ? 98  ARG A CA   1 
ATOM   1500 C C    . ARG A 1 98  ? 11.735 -9.492  28.383  1.00 76.81  ? 98  ARG A C    1 
ATOM   1501 O O    . ARG A 1 98  ? 11.056 -9.707  29.381  1.00 82.75  ? 98  ARG A O    1 
ATOM   1502 C CB   . ARG A 1 98  ? 13.993 -10.581 28.216  1.00 81.86  ? 98  ARG A CB   1 
ATOM   1503 C CG   . ARG A 1 98  ? 14.862 -11.638 27.512  1.00 94.07  ? 98  ARG A CG   1 
ATOM   1504 C CD   . ARG A 1 98  ? 16.253 -11.932 28.140  1.00 100.66 ? 98  ARG A CD   1 
ATOM   1505 N NE   . ARG A 1 98  ? 17.165 -10.792 28.022  1.00 98.69  ? 98  ARG A NE   1 
ATOM   1506 C CZ   . ARG A 1 98  ? 18.021 -10.615 27.022  1.00 97.22  ? 98  ARG A CZ   1 
ATOM   1507 N NH1  . ARG A 1 98  ? 18.112 -11.485 26.027  1.00 98.17  ? 98  ARG A NH1  1 
ATOM   1508 N NH2  . ARG A 1 98  ? 18.789 -9.524  27.011  1.00 99.22  ? 98  ARG A NH2  1 
ATOM   1509 H H    . ARG A 1 98  ? 13.213 -10.472 25.878  1.00 90.19  ? 98  ARG A H    1 
ATOM   1510 H HA   . ARG A 1 98  ? 12.166 -11.464 28.034  1.00 95.67  ? 98  ARG A HA   1 
ATOM   1511 H HB2  . ARG A 1 98  ? 14.368 -9.707  28.025  1.00 98.30  ? 98  ARG A HB2  1 
ATOM   1512 H HB3  . ARG A 1 98  ? 14.022 -10.753 29.170  1.00 98.30  ? 98  ARG A HB3  1 
ATOM   1513 H HG2  . ARG A 1 98  ? 14.372 -12.475 27.506  1.00 112.96 ? 98  ARG A HG2  1 
ATOM   1514 H HG3  . ARG A 1 98  ? 15.020 -11.341 26.602  1.00 112.96 ? 98  ARG A HG3  1 
ATOM   1515 H HD2  . ARG A 1 98  ? 16.141 -12.134 29.082  1.00 120.87 ? 98  ARG A HD2  1 
ATOM   1516 H HD3  . ARG A 1 98  ? 16.655 -12.689 27.684  1.00 120.87 ? 98  ARG A HD3  1 
ATOM   1517 H HE   . ARG A 1 98  ? 17.144 -10.196 28.642  1.00 118.50 ? 98  ARG A HE   1 
ATOM   1518 H HH11 . ARG A 1 98  ? 17.609 -12.182 26.018  1.00 117.89 ? 98  ARG A HH11 1 
ATOM   1519 H HH12 . ARG A 1 98  ? 18.673 -11.351 25.389  1.00 117.89 ? 98  ARG A HH12 1 
ATOM   1520 H HH21 . ARG A 1 98  ? 18.726 -8.947  27.646  1.00 119.14 ? 98  ARG A HH21 1 
ATOM   1521 H HH22 . ARG A 1 98  ? 19.348 -9.398  26.370  1.00 119.14 ? 98  ARG A HH22 1 
ATOM   1522 N N    . VAL A 1 99  ? 11.725 -8.314  27.771  1.00 73.62  ? 99  VAL A N    1 
ATOM   1523 C CA   . VAL A 1 99  ? 11.021 -7.191  28.376  1.00 80.92  ? 99  VAL A CA   1 
ATOM   1524 C C    . VAL A 1 99  ? 9.518  -7.440  28.399  1.00 82.62  ? 99  VAL A C    1 
ATOM   1525 O O    . VAL A 1 99  ? 8.833  -7.093  29.371  1.00 80.76  ? 99  VAL A O    1 
ATOM   1526 C CB   . VAL A 1 99  ? 11.384 -5.896  27.622  1.00 75.84  ? 99  VAL A CB   1 
ATOM   1527 C CG1  . VAL A 1 99  ? 10.452 -4.794  27.985  1.00 72.32  ? 99  VAL A CG1  1 
ATOM   1528 C CG2  . VAL A 1 99  ? 12.833 -5.486  27.914  1.00 72.88  ? 99  VAL A CG2  1 
ATOM   1529 H H    . VAL A 1 99  ? 12.110 -8.142  27.022  1.00 88.42  ? 99  VAL A H    1 
ATOM   1530 H HA   . VAL A 1 99  ? 11.306 -7.099  29.298  1.00 97.18  ? 99  VAL A HA   1 
ATOM   1531 H HB   . VAL A 1 99  ? 11.300 -6.062  26.670  1.00 91.08  ? 99  VAL A HB   1 
ATOM   1532 H HG11 . VAL A 1 99  ? 10.849 -3.947  27.728  1.00 86.87  ? 99  VAL A HG11 1 
ATOM   1533 H HG12 . VAL A 1 99  ? 9.613  -4.922  27.515  1.00 86.87  ? 99  VAL A HG12 1 
ATOM   1534 H HG13 . VAL A 1 99  ? 10.301 -4.811  28.943  1.00 86.87  ? 99  VAL A HG13 1 
ATOM   1535 H HG21 . VAL A 1 99  ? 13.059 -4.716  27.369  1.00 87.54  ? 99  VAL A HG21 1 
ATOM   1536 H HG22 . VAL A 1 99  ? 12.915 -5.261  28.854  1.00 87.54  ? 99  VAL A HG22 1 
ATOM   1537 H HG23 . VAL A 1 99  ? 13.420 -6.227  27.699  1.00 87.54  ? 99  VAL A HG23 1 
ATOM   1538 N N    . ASP A 1 100 ? 8.977  -8.016  27.322  1.00 79.33  ? 100 ASP A N    1 
ATOM   1539 C CA   . ASP A 1 100 ? 7.532  -8.189  27.242  1.00 83.43  ? 100 ASP A CA   1 
ATOM   1540 C C    . ASP A 1 100 ? 7.005  -9.213  28.222  1.00 87.53  ? 100 ASP A C    1 
ATOM   1541 O O    . ASP A 1 100 ? 5.864  -9.083  28.674  1.00 85.31  ? 100 ASP A O    1 
ATOM   1542 C CB   . ASP A 1 100 ? 7.119  -8.640  25.845  1.00 80.01  ? 100 ASP A CB   1 
ATOM   1543 C CG   . ASP A 1 100 ? 7.062  -7.514  24.870  1.00 76.88  ? 100 ASP A CG   1 
ATOM   1544 O OD1  . ASP A 1 100 ? 6.673  -6.405  25.285  1.00 78.51  ? 100 ASP A OD1  1 
ATOM   1545 O OD2  . ASP A 1 100 ? 7.404  -7.751  23.703  1.00 71.70  ? 100 ASP A OD2  1 
ATOM   1546 H H    . ASP A 1 100 ? 9.416  -8.306  26.642  1.00 95.28  ? 100 ASP A H    1 
ATOM   1547 H HA   . ASP A 1 100 ? 7.140  -7.325  27.442  1.00 100.19 ? 100 ASP A HA   1 
ATOM   1548 H HB2  . ASP A 1 100 ? 7.764  -9.287  25.519  1.00 96.08  ? 100 ASP A HB2  1 
ATOM   1549 H HB3  . ASP A 1 100 ? 6.238  -9.043  25.890  1.00 96.08  ? 100 ASP A HB3  1 
ATOM   1550 N N    . LYS A 1 101 ? 7.785  -10.260 28.521  1.00 88.63  ? 101 LYS A N    1 
ATOM   1551 C CA   . LYS A 1 101 ? 7.368  -11.199 29.553  1.00 102.73 ? 101 LYS A CA   1 
ATOM   1552 C C    . LYS A 1 101 ? 7.396  -10.519 30.911  1.00 97.50  ? 101 LYS A C    1 
ATOM   1553 O O    . LYS A 1 101 ? 6.397  -10.539 31.636  1.00 98.14  ? 101 LYS A O    1 
ATOM   1554 C CB   . LYS A 1 101 ? 8.261  -12.443 29.525  1.00 101.24 ? 101 LYS A CB   1 
ATOM   1555 C CG   . LYS A 1 101 ? 7.975  -13.493 30.548  1.00 117.81 ? 101 LYS A CG   1 
ATOM   1556 C CD   . LYS A 1 101 ? 6.588  -14.168 30.465  1.00 109.67 ? 101 LYS A CD   1 
ATOM   1557 C CE   . LYS A 1 101 ? 6.399  -15.139 31.659  1.00 110.75 ? 101 LYS A CE   1 
ATOM   1558 N NZ   . LYS A 1 101 ? 5.067  -15.856 31.737  1.00 106.12 ? 101 LYS A NZ   1 
ATOM   1559 H H    . LYS A 1 101 ? 8.539  -10.439 28.148  1.00 106.43 ? 101 LYS A H    1 
ATOM   1560 H HA   . LYS A 1 101 ? 6.462  -11.499 29.381  1.00 123.35 ? 101 LYS A HA   1 
ATOM   1561 H HB2  . LYS A 1 101 ? 8.167  -12.861 28.655  1.00 121.56 ? 101 LYS A HB2  1 
ATOM   1562 H HB3  . LYS A 1 101 ? 9.178  -12.158 29.658  1.00 121.56 ? 101 LYS A HB3  1 
ATOM   1563 H HG2  . LYS A 1 101 ? 8.639  -14.195 30.456  1.00 141.45 ? 101 LYS A HG2  1 
ATOM   1564 H HG3  . LYS A 1 101 ? 8.042  -13.087 31.426  1.00 141.45 ? 101 LYS A HG3  1 
ATOM   1565 H HD2  . LYS A 1 101 ? 5.893  -13.493 30.500  1.00 131.68 ? 101 LYS A HD2  1 
ATOM   1566 H HD3  . LYS A 1 101 ? 6.519  -14.673 29.640  1.00 131.68 ? 101 LYS A HD3  1 
ATOM   1567 H HE2  . LYS A 1 101 ? 7.087  -15.821 31.606  1.00 132.98 ? 101 LYS A HE2  1 
ATOM   1568 H HE3  . LYS A 1 101 ? 6.498  -14.631 32.480  1.00 132.98 ? 101 LYS A HE3  1 
ATOM   1569 H HZ1  . LYS A 1 101 ? 5.052  -16.395 32.445  1.00 127.42 ? 101 LYS A HZ1  1 
ATOM   1570 H HZ2  . LYS A 1 101 ? 4.407  -15.264 31.811  1.00 127.42 ? 101 LYS A HZ2  1 
ATOM   1571 H HZ3  . LYS A 1 101 ? 4.939  -16.341 31.002  1.00 127.42 ? 101 LYS A HZ3  1 
ATOM   1572 N N    . ILE A 1 102 ? 8.495  -9.814  31.222  1.00 89.85  ? 102 ILE A N    1 
ATOM   1573 C CA   . ILE A 1 102 ? 8.601  -9.094  32.491  1.00 98.06  ? 102 ILE A CA   1 
ATOM   1574 C C    . ILE A 1 102 ? 7.340  -8.288  32.738  1.00 102.99 ? 102 ILE A C    1 
ATOM   1575 O O    . ILE A 1 102 ? 6.841  -8.209  33.866  1.00 105.97 ? 102 ILE A O    1 
ATOM   1576 C CB   . ILE A 1 102 ? 9.840  -8.185  32.517  1.00 90.59  ? 102 ILE A CB   1 
ATOM   1577 C CG1  . ILE A 1 102 ? 11.099 -9.021  32.662  1.00 89.79  ? 102 ILE A CG1  1 
ATOM   1578 C CG2  . ILE A 1 102 ? 9.738  -7.140  33.625  1.00 84.31  ? 102 ILE A CG2  1 
ATOM   1579 C CD1  . ILE A 1 102 ? 12.332 -8.189  32.716  1.00 86.66  ? 102 ILE A CD1  1 
ATOM   1580 H H    . ILE A 1 102 ? 9.187  -9.740  30.717  1.00 107.89 ? 102 ILE A H    1 
ATOM   1581 H HA   . ILE A 1 102 ? 8.703  -9.751  33.197  1.00 117.75 ? 102 ILE A HA   1 
ATOM   1582 H HB   . ILE A 1 102 ? 9.883  -7.707  31.674  1.00 108.79 ? 102 ILE A HB   1 
ATOM   1583 H HG12 . ILE A 1 102 ? 11.046 -9.534  33.483  1.00 107.83 ? 102 ILE A HG12 1 
ATOM   1584 H HG13 . ILE A 1 102 ? 11.172 -9.618  31.901  1.00 107.83 ? 102 ILE A HG13 1 
ATOM   1585 H HG21 . ILE A 1 102 ? 10.590 -6.684  33.709  1.00 101.25 ? 102 ILE A HG21 1 
ATOM   1586 H HG22 . ILE A 1 102 ? 9.043  -6.503  33.396  1.00 101.25 ? 102 ILE A HG22 1 
ATOM   1587 H HG23 . ILE A 1 102 ? 9.518  -7.585  34.459  1.00 101.25 ? 102 ILE A HG23 1 
ATOM   1588 H HD11 . ILE A 1 102 ? 13.093 -8.735  32.464  1.00 104.07 ? 102 ILE A HD11 1 
ATOM   1589 H HD12 . ILE A 1 102 ? 12.239 -7.446  32.099  1.00 104.07 ? 102 ILE A HD12 1 
ATOM   1590 H HD13 . ILE A 1 102 ? 12.448 -7.856  33.620  1.00 104.07 ? 102 ILE A HD13 1 
ATOM   1591 N N    . ILE A 1 103 ? 6.843  -7.624  31.700  1.00 100.08 ? 103 ILE A N    1 
ATOM   1592 C CA   . ILE A 1 103 ? 5.639  -6.828  31.877  1.00 104.51 ? 103 ILE A CA   1 
ATOM   1593 C C    . ILE A 1 103 ? 4.440  -7.726  32.131  1.00 103.72 ? 103 ILE A C    1 
ATOM   1594 O O    . ILE A 1 103 ? 3.606  -7.443  32.995  1.00 110.27 ? 103 ILE A O    1 
ATOM   1595 C CB   . ILE A 1 103 ? 5.462  -5.908  30.668  1.00 94.45  ? 103 ILE A CB   1 
ATOM   1596 C CG1  . ILE A 1 103 ? 6.301  -4.655  30.915  1.00 94.52  ? 103 ILE A CG1  1 
ATOM   1597 C CG2  . ILE A 1 103 ? 4.034  -5.539  30.473  1.00 92.41  ? 103 ILE A CG2  1 
ATOM   1598 C CD1  . ILE A 1 103 ? 7.329  -4.392  29.852  1.00 84.07  ? 103 ILE A CD1  1 
ATOM   1599 H H    . ILE A 1 103 ? 7.175  -7.619  30.907  1.00 120.17 ? 103 ILE A H    1 
ATOM   1600 H HA   . ILE A 1 103 ? 5.729  -6.264  32.662  1.00 125.49 ? 103 ILE A HA   1 
ATOM   1601 H HB   . ILE A 1 103 ? 5.753  -6.368  29.865  1.00 113.41 ? 103 ILE A HB   1 
ATOM   1602 H HG12 . ILE A 1 103 ? 5.710  -3.887  30.951  1.00 113.50 ? 103 ILE A HG12 1 
ATOM   1603 H HG13 . ILE A 1 103 ? 6.768  -4.755  31.760  1.00 113.50 ? 103 ILE A HG13 1 
ATOM   1604 H HG21 . ILE A 1 103 ? 3.981  -4.806  29.841  1.00 110.98 ? 103 ILE A HG21 1 
ATOM   1605 H HG22 . ILE A 1 103 ? 3.553  -6.308  30.129  1.00 110.98 ? 103 ILE A HG22 1 
ATOM   1606 H HG23 . ILE A 1 103 ? 3.659  -5.268  31.326  1.00 110.98 ? 103 ILE A HG23 1 
ATOM   1607 H HD11 . ILE A 1 103 ? 7.656  -3.483  29.947  1.00 100.96 ? 103 ILE A HD11 1 
ATOM   1608 H HD12 . ILE A 1 103 ? 8.061  -5.019  29.958  1.00 100.96 ? 103 ILE A HD12 1 
ATOM   1609 H HD13 . ILE A 1 103 ? 6.919  -4.506  28.981  1.00 100.96 ? 103 ILE A HD13 1 
ATOM   1610 N N    . GLU A 1 104 ? 4.335  -8.824  31.403  1.00 92.26  ? 104 GLU A N    1 
ATOM   1611 C CA   . GLU A 1 104 ? 3.269  -9.785  31.648  1.00 98.89  ? 104 GLU A CA   1 
ATOM   1612 C C    . GLU A 1 104 ? 3.239  -10.216 33.101  1.00 105.31 ? 104 GLU A C    1 
ATOM   1613 O O    . GLU A 1 104 ? 2.171  -10.249 33.730  1.00 103.54 ? 104 GLU A O    1 
ATOM   1614 C CB   . GLU A 1 104 ? 3.483  -10.958 30.700  1.00 99.18  ? 104 GLU A CB   1 
ATOM   1615 C CG   . GLU A 1 104 ? 2.406  -11.993 30.670  1.00 102.27 ? 104 GLU A CG   1 
ATOM   1616 C CD   . GLU A 1 104 ? 2.720  -13.075 29.634  1.00 109.37 ? 104 GLU A CD   1 
ATOM   1617 O OE1  . GLU A 1 104 ? 3.138  -12.713 28.496  1.00 96.56  ? 104 GLU A OE1  1 
ATOM   1618 O OE2  . GLU A 1 104 ? 2.538  -14.274 29.961  1.00 110.53 ? 104 GLU A OE2  1 
ATOM   1619 H H    . GLU A 1 104 ? 4.866  -9.040  30.761  1.00 110.78 ? 104 GLU A H    1 
ATOM   1620 H HA   . GLU A 1 104 ? 2.398  -9.398  31.467  1.00 118.75 ? 104 GLU A HA   1 
ATOM   1621 H HB2  . GLU A 1 104 ? 3.566  -10.607 29.800  1.00 119.09 ? 104 GLU A HB2  1 
ATOM   1622 H HB3  . GLU A 1 104 ? 4.303  -11.408 30.957  1.00 119.09 ? 104 GLU A HB3  1 
ATOM   1623 H HG2  . GLU A 1 104 ? 2.336  -12.413 31.542  1.00 122.80 ? 104 GLU A HG2  1 
ATOM   1624 H HG3  . GLU A 1 104 ? 1.563  -11.576 30.434  1.00 122.80 ? 104 GLU A HG3  1 
ATOM   1625 N N    . ASN A 1 105 ? 4.412  -10.497 33.672  1.00 101.95 ? 105 ASN A N    1 
ATOM   1626 C CA   . ASN A 1 105 ? 4.458  -11.017 35.036  1.00 102.45 ? 105 ASN A CA   1 
ATOM   1627 C C    . ASN A 1 105 ? 4.112  -9.965  36.072  1.00 106.47 ? 105 ASN A C    1 
ATOM   1628 O O    . ASN A 1 105 ? 3.562  -10.304 37.132  1.00 112.50 ? 105 ASN A O    1 
ATOM   1629 C CB   . ASN A 1 105 ? 5.836  -11.595 35.322  1.00 102.51 ? 105 ASN A CB   1 
ATOM   1630 C CG   . ASN A 1 105 ? 6.158  -12.730 34.401  1.00 103.30 ? 105 ASN A CG   1 
ATOM   1631 O OD1  . ASN A 1 105 ? 5.287  -13.186 33.657  1.00 104.06 ? 105 ASN A OD1  1 
ATOM   1632 N ND2  . ASN A 1 105 ? 7.398  -13.202 34.431  1.00 104.80 ? 105 ASN A ND2  1 
ATOM   1633 H H    . ASN A 1 105 ? 5.180  -10.396 33.298  1.00 122.42 ? 105 ASN A H    1 
ATOM   1634 H HA   . ASN A 1 105 ? 3.802  -11.727 35.111  1.00 123.02 ? 105 ASN A HA   1 
ATOM   1635 H HB2  . ASN A 1 105 ? 6.506  -10.904 35.201  1.00 123.09 ? 105 ASN A HB2  1 
ATOM   1636 H HB3  . ASN A 1 105 ? 5.862  -11.925 36.234  1.00 123.09 ? 105 ASN A HB3  1 
ATOM   1637 H HD21 . ASN A 1 105 ? 7.623  -13.854 33.916  1.00 125.84 ? 105 ASN A HD21 1 
ATOM   1638 H HD22 . ASN A 1 105 ? 7.977  -12.857 34.964  1.00 125.84 ? 105 ASN A HD22 1 
ATOM   1639 N N    . LEU A 1 106 ? 4.439  -8.698  35.804  1.00 110.19 ? 106 LEU A N    1 
ATOM   1640 C CA   . LEU A 1 106 ? 4.084  -7.646  36.748  1.00 119.91 ? 106 LEU A CA   1 
ATOM   1641 C C    . LEU A 1 106 ? 2.584  -7.660  37.018  1.00 120.51 ? 106 LEU A C    1 
ATOM   1642 O O    . LEU A 1 106 ? 2.143  -7.540  38.168  1.00 119.46 ? 106 LEU A O    1 
ATOM   1643 C CB   . LEU A 1 106 ? 4.518  -6.281  36.210  1.00 107.29 ? 106 LEU A CB   1 
ATOM   1644 C CG   . LEU A 1 106 ? 5.996  -5.889  36.253  1.00 138.21 ? 106 LEU A CG   1 
ATOM   1645 C CD1  . LEU A 1 106 ? 6.251  -4.558  35.584  1.00 130.58 ? 106 LEU A CD1  1 
ATOM   1646 C CD2  . LEU A 1 106 ? 6.481  -5.822  37.677  1.00 170.65 ? 106 LEU A CD2  1 
ATOM   1647 H H    . LEU A 1 106 ? 4.855  -8.431  35.101  1.00 132.31 ? 106 LEU A H    1 
ATOM   1648 H HA   . LEU A 1 106 ? 4.553  -7.796  37.584  1.00 143.97 ? 106 LEU A HA   1 
ATOM   1649 H HB2  . LEU A 1 106 ? 4.254  -6.241  35.278  1.00 128.83 ? 106 LEU A HB2  1 
ATOM   1650 H HB3  . LEU A 1 106 ? 4.043  -5.605  36.719  1.00 128.83 ? 106 LEU A HB3  1 
ATOM   1651 H HG   . LEU A 1 106 ? 6.492  -6.568  35.770  1.00 165.93 ? 106 LEU A HG   1 
ATOM   1652 H HD11 . LEU A 1 106 ? 7.186  -4.325  35.691  1.00 156.78 ? 106 LEU A HD11 1 
ATOM   1653 H HD12 . LEU A 1 106 ? 6.035  -4.633  34.641  1.00 156.78 ? 106 LEU A HD12 1 
ATOM   1654 H HD13 . LEU A 1 106 ? 5.692  -3.883  35.999  1.00 156.78 ? 106 LEU A HD13 1 
ATOM   1655 H HD21 . LEU A 1 106 ? 7.386  -5.472  37.687  1.00 204.86 ? 106 LEU A HD21 1 
ATOM   1656 H HD22 . LEU A 1 106 ? 5.896  -5.237  38.183  1.00 204.86 ? 106 LEU A HD22 1 
ATOM   1657 H HD23 . LEU A 1 106 ? 6.467  -6.714  38.058  1.00 204.86 ? 106 LEU A HD23 1 
ATOM   1658 N N    . GLU A 1 107 ? 1.789  -7.840  35.959  1.00 116.98 ? 107 GLU A N    1 
ATOM   1659 C CA   . GLU A 1 107 ? 0.346  -7.969  36.119  1.00 117.48 ? 107 GLU A CA   1 
ATOM   1660 C C    . GLU A 1 107 ? 0.013  -9.249  36.859  1.00 118.96 ? 107 GLU A C    1 
ATOM   1661 O O    . GLU A 1 107 ? -0.919 -9.295  37.668  1.00 123.51 ? 107 GLU A O    1 
ATOM   1662 C CB   . GLU A 1 107 ? -0.329 -7.992  34.759  1.00 115.26 ? 107 GLU A CB   1 
ATOM   1663 C CG   . GLU A 1 107 ? 0.149  -6.922  33.847  1.00 109.77 ? 107 GLU A CG   1 
ATOM   1664 C CD   . GLU A 1 107 ? -0.531 -6.994  32.518  1.00 134.39 ? 107 GLU A CD   1 
ATOM   1665 O OE1  . GLU A 1 107 ? -1.313 -7.950  32.315  1.00 129.40 ? 107 GLU A OE1  1 
ATOM   1666 O OE2  . GLU A 1 107 ? -0.246 -6.129  31.665  1.00 147.36 ? 107 GLU A OE2  1 
ATOM   1667 H H    . GLU A 1 107 ? 2.061  -7.890  35.144  1.00 140.46 ? 107 GLU A H    1 
ATOM   1668 H HA   . GLU A 1 107 ? 0.015  -7.207  36.619  1.00 141.05 ? 107 GLU A HA   1 
ATOM   1669 H HB2  . GLU A 1 107 ? -0.151 -8.846  34.335  1.00 138.39 ? 107 GLU A HB2  1 
ATOM   1670 H HB3  . GLU A 1 107 ? -1.284 -7.874  34.881  1.00 138.39 ? 107 GLU A HB3  1 
ATOM   1671 H HG2  . GLU A 1 107 ? -0.041 -6.056  34.240  1.00 131.81 ? 107 GLU A HG2  1 
ATOM   1672 H HG3  . GLU A 1 107 ? 1.104  -7.021  33.707  1.00 131.81 ? 107 GLU A HG3  1 
ATOM   1673 N N    . ALA A 1 108 ? 0.780  -10.301 36.598  1.00 116.46 ? 108 ALA A N    1 
ATOM   1674 C CA   . ALA A 1 108 ? 0.546  -11.552 37.287  1.00 117.74 ? 108 ALA A CA   1 
ATOM   1675 C C    . ALA A 1 108 ? 0.874  -11.386 38.755  1.00 118.38 ? 108 ALA A C    1 
ATOM   1676 O O    . ALA A 1 108 ? 0.076  -11.746 39.627  1.00 125.58 ? 108 ALA A O    1 
ATOM   1677 C CB   . ALA A 1 108 ? 1.396  -12.652 36.661  1.00 128.54 ? 108 ALA A CB   1 
ATOM   1678 H H    . ALA A 1 108 ? 1.431  -10.312 36.035  1.00 139.84 ? 108 ALA A H    1 
ATOM   1679 H HA   . ALA A 1 108 ? -0.384 -11.815 37.200  1.00 141.37 ? 108 ALA A HA   1 
ATOM   1680 H HB1  . ALA A 1 108 ? 1.216  -13.489 37.117  1.00 154.32 ? 108 ALA A HB1  1 
ATOM   1681 H HB2  . ALA A 1 108 ? 1.167  -12.732 35.722  1.00 154.32 ? 108 ALA A HB2  1 
ATOM   1682 H HB3  . ALA A 1 108 ? 2.333  -12.419 36.754  1.00 154.32 ? 108 ALA A HB3  1 
ATOM   1683 N N    . ASN A 1 109 ? 2.038  -10.814 39.055  1.00 115.24 ? 109 ASN A N    1 
ATOM   1684 C CA   . ASN A 1 109 ? 2.392  -10.633 40.456  1.00 119.93 ? 109 ASN A CA   1 
ATOM   1685 C C    . ASN A 1 109 ? 1.382  -9.730  41.153  1.00 124.00 ? 109 ASN A C    1 
ATOM   1686 O O    . ASN A 1 109 ? 1.207  -9.817  42.375  1.00 121.95 ? 109 ASN A O    1 
ATOM   1687 C CB   . ASN A 1 109 ? 3.815  -10.101 40.544  1.00 122.74 ? 109 ASN A CB   1 
ATOM   1688 C CG   . ASN A 1 109 ? 4.845  -11.157 40.143  1.00 121.66 ? 109 ASN A CG   1 
ATOM   1689 O OD1  . ASN A 1 109 ? 4.533  -12.356 40.054  1.00 121.67 ? 109 ASN A OD1  1 
ATOM   1690 N ND2  . ASN A 1 109 ? 6.081  -10.719 39.920  1.00 118.81 ? 109 ASN A ND2  1 
ATOM   1691 H H    . ASN A 1 109 ? 2.618  -10.532 38.486  1.00 138.37 ? 109 ASN A H    1 
ATOM   1692 H HA   . ASN A 1 109 ? 2.382  -11.480 40.929  1.00 144.00 ? 109 ASN A HA   1 
ATOM   1693 H HB2  . ASN A 1 109 ? 3.910  -9.343  39.947  1.00 147.36 ? 109 ASN A HB2  1 
ATOM   1694 H HB3  . ASN A 1 109 ? 3.998  -9.830  41.457  1.00 147.36 ? 109 ASN A HB3  1 
ATOM   1695 H HD21 . ASN A 1 109 ? 6.699  -11.273 39.692  1.00 142.64 ? 109 ASN A HD21 1 
ATOM   1696 H HD22 . ASN A 1 109 ? 6.263  -9.883  40.005  1.00 142.64 ? 109 ASN A HD22 1 
ATOM   1697 N N    . LYS A 1 110 ? 0.710  -8.853  40.394  1.00 126.35 ? 110 LYS A N    1 
ATOM   1698 C CA   . LYS A 1 110 ? -0.400 -8.088  40.959  1.00 123.37 ? 110 LYS A CA   1 
ATOM   1699 C C    . LYS A 1 110 ? -1.594 -8.982  41.286  1.00 125.22 ? 110 LYS A C    1 
ATOM   1700 O O    . LYS A 1 110 ? -2.327 -8.710  42.238  1.00 129.03 ? 110 LYS A O    1 
ATOM   1701 C CB   . LYS A 1 110 ? -0.819 -6.981  40.000  1.00 123.61 ? 110 LYS A CB   1 
ATOM   1702 C CG   . LYS A 1 110 ? 0.048  -5.713  40.087  1.00 125.21 ? 110 LYS A CG   1 
ATOM   1703 C CD   . LYS A 1 110 ? 0.071  -5.086  41.500  1.00 120.76 ? 110 LYS A CD   1 
ATOM   1704 C CE   . LYS A 1 110 ? 0.866  -3.773  41.532  1.00 126.06 ? 110 LYS A CE   1 
ATOM   1705 N NZ   . LYS A 1 110 ? 2.264  -3.936  41.001  1.00 133.61 ? 110 LYS A NZ   1 
ATOM   1706 H H    . LYS A 1 110 ? 0.875  -8.689  39.566  1.00 151.69 ? 110 LYS A H    1 
ATOM   1707 H HA   . LYS A 1 110 ? -0.101 -7.673  41.783  1.00 148.13 ? 110 LYS A HA   1 
ATOM   1708 H HB2  . LYS A 1 110 ? -0.758 -7.318  39.092  1.00 148.40 ? 110 LYS A HB2  1 
ATOM   1709 H HB3  . LYS A 1 110 ? -1.734 -6.727  40.199  1.00 148.40 ? 110 LYS A HB3  1 
ATOM   1710 H HG2  . LYS A 1 110 ? 0.961  -5.939  39.847  1.00 150.33 ? 110 LYS A HG2  1 
ATOM   1711 H HG3  . LYS A 1 110 ? -0.302 -5.049  39.473  1.00 150.33 ? 110 LYS A HG3  1 
ATOM   1712 H HD2  . LYS A 1 110 ? -0.838 -4.897  41.781  1.00 144.99 ? 110 LYS A HD2  1 
ATOM   1713 H HD3  . LYS A 1 110 ? 0.486  -5.707  42.119  1.00 144.99 ? 110 LYS A HD3  1 
ATOM   1714 H HE2  . LYS A 1 110 ? 0.411  -3.114  40.985  1.00 151.35 ? 110 LYS A HE2  1 
ATOM   1715 H HE3  . LYS A 1 110 ? 0.926  -3.460  42.448  1.00 151.35 ? 110 LYS A HE3  1 
ATOM   1716 H HZ1  . LYS A 1 110 ? 2.689  -3.155  41.018  1.00 160.41 ? 110 LYS A HZ1  1 
ATOM   1717 H HZ2  . LYS A 1 110 ? 2.712  -4.520  41.501  1.00 160.41 ? 110 LYS A HZ2  1 
ATOM   1718 H HZ3  . LYS A 1 110 ? 2.238  -4.233  40.163  1.00 160.41 ? 110 LYS A HZ3  1 
ATOM   1719 N N    . LYS A 1 111 ? -1.805 -10.046 40.517  1.00 133.32 ? 111 LYS A N    1 
ATOM   1720 C CA   . LYS A 1 111 ? -2.878 -10.997 40.803  1.00 132.80 ? 111 LYS A CA   1 
ATOM   1721 C C    . LYS A 1 111 ? -2.270 -12.264 41.404  1.00 130.81 ? 111 LYS A C    1 
ATOM   1722 O O    . LYS A 1 111 ? -1.624 -12.209 42.459  1.00 132.05 ? 111 LYS A O    1 
ATOM   1723 C CB   . LYS A 1 111 ? -3.706 -11.316 39.542  1.00 133.30 ? 111 LYS A CB   1 
ATOM   1724 C CG   . LYS A 1 111 ? -4.636 -10.162 39.116  1.00 136.65 ? 111 LYS A CG   1 
ATOM   1725 C CD   . LYS A 1 111 ? -5.379 -10.418 37.813  1.00 134.67 ? 111 LYS A CD   1 
ATOM   1726 C CE   . LYS A 1 111 ? -4.495 -10.170 36.622  1.00 148.27 ? 111 LYS A CE   1 
ATOM   1727 N NZ   . LYS A 1 111 ? -5.234 -10.365 35.339  1.00 140.93 ? 111 LYS A NZ   1 
ATOM   1728 H H    . LYS A 1 111 ? -1.339 -10.241 39.821  1.00 160.06 ? 111 LYS A H    1 
ATOM   1729 H HA   . LYS A 1 111 ? -3.504 -10.613 41.437  1.00 159.43 ? 111 LYS A HA   1 
ATOM   1730 H HB2  . LYS A 1 111 ? -3.100 -11.498 38.807  1.00 160.04 ? 111 LYS A HB2  1 
ATOM   1731 H HB3  . LYS A 1 111 ? -4.257 -12.094 39.718  1.00 160.04 ? 111 LYS A HB3  1 
ATOM   1732 H HG2  . LYS A 1 111 ? -5.299 -10.022 39.810  1.00 164.05 ? 111 LYS A HG2  1 
ATOM   1733 H HG3  . LYS A 1 111 ? -4.104 -9.359  38.998  1.00 164.05 ? 111 LYS A HG3  1 
ATOM   1734 H HD2  . LYS A 1 111 ? -5.674 -11.342 37.788  1.00 161.68 ? 111 LYS A HD2  1 
ATOM   1735 H HD3  . LYS A 1 111 ? -6.143 -9.824  37.756  1.00 161.68 ? 111 LYS A HD3  1 
ATOM   1736 H HE2  . LYS A 1 111 ? -4.169 -9.257  36.650  1.00 178.00 ? 111 LYS A HE2  1 
ATOM   1737 H HE3  . LYS A 1 111 ? -3.749 -10.789 36.641  1.00 178.00 ? 111 LYS A HE3  1 
ATOM   1738 H HZ1  . LYS A 1 111 ? -4.834 -9.913  34.685  1.00 169.19 ? 111 LYS A HZ1  1 
ATOM   1739 H HZ2  . LYS A 1 111 ? -5.249 -11.229 35.125  1.00 169.19 ? 111 LYS A HZ2  1 
ATOM   1740 H HZ3  . LYS A 1 111 ? -6.071 -10.074 35.422  1.00 169.19 ? 111 LYS A HZ3  1 
ATOM   1741 N N    . ALA B 1 2   ? 28.804 -6.892  19.707  1.00 97.60  ? 2   ALA B N    1 
ATOM   1742 C CA   . ALA B 1 2   ? 27.419 -6.949  19.278  1.00 99.67  ? 2   ALA B CA   1 
ATOM   1743 C C    . ALA B 1 2   ? 26.453 -6.551  20.408  1.00 107.13 ? 2   ALA B C    1 
ATOM   1744 O O    . ALA B 1 2   ? 25.267 -6.903  20.385  1.00 108.37 ? 2   ALA B O    1 
ATOM   1745 C CB   . ALA B 1 2   ? 27.081 -8.357  18.758  1.00 96.30  ? 2   ALA B CB   1 
ATOM   1746 H HA   . ALA B 1 2   ? 27.296 -6.315  18.555  1.00 119.68 ? 2   ALA B HA   1 
ATOM   1747 H HB1  . ALA B 1 2   ? 26.159 -8.371  18.460  1.00 115.63 ? 2   ALA B HB1  1 
ATOM   1748 H HB2  . ALA B 1 2   ? 27.672 -8.571  18.019  1.00 115.63 ? 2   ALA B HB2  1 
ATOM   1749 H HB3  . ALA B 1 2   ? 27.206 -8.997  19.477  1.00 115.63 ? 2   ALA B HB3  1 
ATOM   1750 N N    . GLU B 1 3   ? 26.951 -5.803  21.385  1.00 105.34 ? 3   GLU B N    1 
ATOM   1751 C CA   . GLU B 1 3   ? 26.123 -5.430  22.527  1.00 104.21 ? 3   GLU B CA   1 
ATOM   1752 C C    . GLU B 1 3   ? 24.837 -4.741  22.066  1.00 99.54  ? 3   GLU B C    1 
ATOM   1753 O O    . GLU B 1 3   ? 24.769 -4.165  20.970  1.00 96.02  ? 3   GLU B O    1 
ATOM   1754 C CB   . GLU B 1 3   ? 26.899 -4.504  23.481  1.00 100.18 ? 3   GLU B CB   1 
ATOM   1755 C CG   . GLU B 1 3   ? 28.287 -5.006  23.884  1.00 105.35 ? 3   GLU B CG   1 
ATOM   1756 C CD   . GLU B 1 3   ? 29.082 -3.952  24.620  1.00 105.54 ? 3   GLU B CD   1 
ATOM   1757 O OE1  . GLU B 1 3   ? 28.476 -2.910  24.965  1.00 111.25 ? 3   GLU B OE1  1 
ATOM   1758 O OE2  . GLU B 1 3   ? 30.295 -4.150  24.859  1.00 110.71 ? 3   GLU B OE2  1 
ATOM   1759 H H    . GLU B 1 3   ? 27.756 -5.501  21.412  1.00 126.48 ? 3   GLU B H    1 
ATOM   1760 H HA   . GLU B 1 3   ? 25.881 -6.233  23.015  1.00 125.13 ? 3   GLU B HA   1 
ATOM   1761 H HB2  . GLU B 1 3   ? 27.015 -3.644  23.046  1.00 120.29 ? 3   GLU B HB2  1 
ATOM   1762 H HB3  . GLU B 1 3   ? 26.381 -4.397  24.294  1.00 120.29 ? 3   GLU B HB3  1 
ATOM   1763 H HG2  . GLU B 1 3   ? 28.191 -5.775  24.467  1.00 126.50 ? 3   GLU B HG2  1 
ATOM   1764 H HG3  . GLU B 1 3   ? 28.780 -5.255  23.086  1.00 126.50 ? 3   GLU B HG3  1 
ATOM   1765 N N    . ILE B 1 4   ? 23.802 -4.833  22.904  1.00 94.58  ? 4   ILE B N    1 
ATOM   1766 C CA   . ILE B 1 4   ? 22.584 -4.033  22.707  1.00 92.99  ? 4   ILE B CA   1 
ATOM   1767 C C    . ILE B 1 4   ? 22.950 -2.555  22.818  1.00 90.64  ? 4   ILE B C    1 
ATOM   1768 O O    . ILE B 1 4   ? 23.593 -2.148  23.805  1.00 87.28  ? 4   ILE B O    1 
ATOM   1769 C CB   . ILE B 1 4   ? 21.507 -4.400  23.745  1.00 88.55  ? 4   ILE B CB   1 
ATOM   1770 C CG1  . ILE B 1 4   ? 20.976 -5.825  23.582  1.00 90.31  ? 4   ILE B CG1  1 
ATOM   1771 C CG2  . ILE B 1 4   ? 20.303 -3.466  23.615  1.00 84.38  ? 4   ILE B CG2  1 
ATOM   1772 C CD1  . ILE B 1 4   ? 20.213 -6.059  22.301  1.00 86.13  ? 4   ILE B CD1  1 
ATOM   1773 H H    . ILE B 1 4   ? 23.775 -5.347  23.592  1.00 113.57 ? 4   ILE B H    1 
ATOM   1774 H HA   . ILE B 1 4   ? 22.225 -4.210  21.824  1.00 111.67 ? 4   ILE B HA   1 
ATOM   1775 H HB   . ILE B 1 4   ? 21.944 -4.318  24.607  1.00 106.34 ? 4   ILE B HB   1 
ATOM   1776 H HG12 . ILE B 1 4   ? 21.727 -6.439  23.593  1.00 108.46 ? 4   ILE B HG12 1 
ATOM   1777 H HG13 . ILE B 1 4   ? 20.378 -6.020  24.321  1.00 108.46 ? 4   ILE B HG13 1 
ATOM   1778 H HG21 . ILE B 1 4   ? 19.540 -3.871  24.056  1.00 101.34 ? 4   ILE B HG21 1 
ATOM   1779 H HG22 . ILE B 1 4   ? 20.516 -2.617  24.035  1.00 101.34 ? 4   ILE B HG22 1 
ATOM   1780 H HG23 . ILE B 1 4   ? 20.109 -3.330  22.675  1.00 101.34 ? 4   ILE B HG23 1 
ATOM   1781 H HD11 . ILE B 1 4   ? 19.898 -6.976  22.284  1.00 103.44 ? 4   ILE B HD11 1 
ATOM   1782 H HD12 . ILE B 1 4   ? 19.460 -5.449  22.267  1.00 103.44 ? 4   ILE B HD12 1 
ATOM   1783 H HD13 . ILE B 1 4   ? 20.803 -5.898  21.548  1.00 103.44 ? 4   ILE B HD13 1 
ATOM   1784 N N    . PRO B 1 5   ? 22.586 -1.719  21.855  1.00 89.91  ? 5   PRO B N    1 
ATOM   1785 C CA   . PRO B 1 5   ? 22.944 -0.303  21.945  1.00 94.94  ? 5   PRO B CA   1 
ATOM   1786 C C    . PRO B 1 5   ? 22.424 0.386   23.199  1.00 87.24  ? 5   PRO B C    1 
ATOM   1787 O O    . PRO B 1 5   ? 21.326 0.139   23.687  1.00 81.15  ? 5   PRO B O    1 
ATOM   1788 C CB   . PRO B 1 5   ? 22.326 0.307   20.682  1.00 86.45  ? 5   PRO B CB   1 
ATOM   1789 C CG   . PRO B 1 5   ? 21.424 -0.764  20.099  1.00 85.37  ? 5   PRO B CG   1 
ATOM   1790 C CD   . PRO B 1 5   ? 21.966 -2.067  20.566  1.00 89.64  ? 5   PRO B CD   1 
ATOM   1791 H HA   . PRO B 1 5   ? 23.911 -0.220  21.929  1.00 114.01 ? 5   PRO B HA   1 
ATOM   1792 H HB2  . PRO B 1 5   ? 21.814 1.096   20.918  1.00 103.82 ? 5   PRO B HB2  1 
ATOM   1793 H HB3  . PRO B 1 5   ? 23.029 0.543   20.056  1.00 103.82 ? 5   PRO B HB3  1 
ATOM   1794 H HG2  . PRO B 1 5   ? 20.518 -0.636  20.420  1.00 102.52 ? 5   PRO B HG2  1 
ATOM   1795 H HG3  . PRO B 1 5   ? 21.443 -0.713  19.131  1.00 102.52 ? 5   PRO B HG3  1 
ATOM   1796 H HD2  . PRO B 1 5   ? 21.255 -2.715  20.687  1.00 107.65 ? 5   PRO B HD2  1 
ATOM   1797 H HD3  . PRO B 1 5   ? 22.626 -2.411  19.944  1.00 107.65 ? 5   PRO B HD3  1 
ATOM   1798 N N    . LYS B 1 6   ? 23.221 1.324   23.677  1.00 92.28  ? 6   LYS B N    1 
ATOM   1799 C CA   . LYS B 1 6   ? 22.917 2.031   24.913  1.00 94.89  ? 6   LYS B CA   1 
ATOM   1800 C C    . LYS B 1 6   ? 21.564 2.731   24.849  1.00 92.76  ? 6   LYS B C    1 
ATOM   1801 O O    . LYS B 1 6   ? 20.847 2.800   25.854  1.00 90.40  ? 6   LYS B O    1 
ATOM   1802 C CB   . LYS B 1 6   ? 24.055 3.021   25.145  1.00 98.15  ? 6   LYS B CB   1 
ATOM   1803 C CG   . LYS B 1 6   ? 25.415 2.306   25.169  1.00 102.57 ? 6   LYS B CG   1 
ATOM   1804 C CD   . LYS B 1 6   ? 26.550 3.269   25.394  1.00 108.05 ? 6   LYS B CD   1 
ATOM   1805 C CE   . LYS B 1 6   ? 26.588 4.291   24.267  1.00 106.34 ? 6   LYS B CE   1 
ATOM   1806 N NZ   . LYS B 1 6   ? 27.866 5.052   24.273  1.00 116.02 ? 6   LYS B NZ   1 
ATOM   1807 H H    . LYS B 1 6   ? 23.955 1.575   23.305  1.00 110.82 ? 6   LYS B H    1 
ATOM   1808 H HA   . LYS B 1 6   ? 22.858 1.415   25.660  1.00 113.95 ? 6   LYS B HA   1 
ATOM   1809 H HB2  . LYS B 1 6   ? 24.065 3.675   24.428  1.00 117.86 ? 6   LYS B HB2  1 
ATOM   1810 H HB3  . LYS B 1 6   ? 23.926 3.465   25.998  1.00 117.86 ? 6   LYS B HB3  1 
ATOM   1811 H HG2  . LYS B 1 6   ? 25.422 1.656   25.889  1.00 123.16 ? 6   LYS B HG2  1 
ATOM   1812 H HG3  . LYS B 1 6   ? 25.558 1.861   24.319  1.00 123.16 ? 6   LYS B HG3  1 
ATOM   1813 H HD2  . LYS B 1 6   ? 26.423 3.735   26.234  1.00 129.74 ? 6   LYS B HD2  1 
ATOM   1814 H HD3  . LYS B 1 6   ? 27.391 2.786   25.406  1.00 129.74 ? 6   LYS B HD3  1 
ATOM   1815 H HE2  . LYS B 1 6   ? 26.508 3.835   23.415  1.00 127.69 ? 6   LYS B HE2  1 
ATOM   1816 H HE3  . LYS B 1 6   ? 25.857 4.919   24.377  1.00 127.69 ? 6   LYS B HE3  1 
ATOM   1817 H HZ1  . LYS B 1 6   ? 27.846 5.686   23.648  1.00 139.30 ? 6   LYS B HZ1  1 
ATOM   1818 H HZ2  . LYS B 1 6   ? 27.989 5.434   25.067  1.00 139.30 ? 6   LYS B HZ2  1 
ATOM   1819 H HZ3  . LYS B 1 6   ? 28.547 4.504   24.106  1.00 139.30 ? 6   LYS B HZ3  1 
ATOM   1820 N N    . GLU B 1 7   ? 21.198 3.250   23.674  1.00 94.35  ? 7   GLU B N    1 
ATOM   1821 C CA   . GLU B 1 7   ? 19.880 3.858   23.497  1.00 89.92  ? 7   GLU B CA   1 
ATOM   1822 C C    . GLU B 1 7   ? 18.764 2.830   23.621  1.00 84.98  ? 7   GLU B C    1 
ATOM   1823 O O    . GLU B 1 7   ? 17.634 3.186   23.989  1.00 81.55  ? 7   GLU B O    1 
ATOM   1824 C CB   . GLU B 1 7   ? 19.822 4.576   22.156  1.00 84.23  ? 7   GLU B CB   1 
ATOM   1825 C CG   . GLU B 1 7   ? 20.798 5.745   22.058  1.00 91.85  ? 7   GLU B CG   1 
ATOM   1826 C CD   . GLU B 1 7   ? 22.266 5.333   21.852  1.00 96.73  ? 7   GLU B CD   1 
ATOM   1827 O OE1  . GLU B 1 7   ? 22.525 4.316   21.160  1.00 99.07  ? 7   GLU B OE1  1 
ATOM   1828 O OE2  . GLU B 1 7   ? 23.169 6.056   22.352  1.00 95.91  ? 7   GLU B OE2  1 
ATOM   1829 H H    . GLU B 1 7   ? 21.690 3.263   22.970  1.00 113.30 ? 7   GLU B H    1 
ATOM   1830 H HA   . GLU B 1 7   ? 19.737 4.520   24.192  1.00 107.99 ? 7   GLU B HA   1 
ATOM   1831 H HB2  . GLU B 1 7   ? 20.040 3.946   21.452  1.00 101.16 ? 7   GLU B HB2  1 
ATOM   1832 H HB3  . GLU B 1 7   ? 18.926 4.924   22.025  1.00 101.16 ? 7   GLU B HB3  1 
ATOM   1833 H HG2  . GLU B 1 7   ? 20.542 6.301   21.306  1.00 110.30 ? 7   GLU B HG2  1 
ATOM   1834 H HG3  . GLU B 1 7   ? 20.751 6.258   22.880  1.00 110.30 ? 7   GLU B HG3  1 
ATOM   1835 N N    . MET B 1 8   ? 19.052 1.555   23.316  1.00 81.67  ? 8   MET B N    1 
ATOM   1836 C CA   . MET B 1 8   ? 18.007 0.536   23.386  1.00 85.31  ? 8   MET B CA   1 
ATOM   1837 C C    . MET B 1 8   ? 17.768 0.079   24.828  1.00 78.36  ? 8   MET B C    1 
ATOM   1838 O O    . MET B 1 8   ? 16.616 -0.016  25.262  1.00 73.21  ? 8   MET B O    1 
ATOM   1839 C CB   . MET B 1 8   ? 18.362 -0.665  22.493  1.00 85.00  ? 8   MET B CB   1 
ATOM   1840 C CG   . MET B 1 8   ? 17.227 -1.647  22.309  1.00 76.55  ? 8   MET B CG   1 
ATOM   1841 S SD   . MET B 1 8   ? 17.397 -2.836  20.965  1.00 71.95  ? 8   MET B SD   1 
ATOM   1842 C CE   . MET B 1 8   ? 17.473 -1.735  19.557  1.00 76.57  ? 8   MET B CE   1 
ATOM   1843 H H    . MET B 1 8   ? 19.825 1.266   23.074  1.00 98.08  ? 8   MET B H    1 
ATOM   1844 H HA   . MET B 1 8   ? 17.187 0.919   23.038  1.00 102.45 ? 8   MET B HA   1 
ATOM   1845 H HB2  . MET B 1 8   ? 18.615 -0.337  21.616  1.00 102.07 ? 8   MET B HB2  1 
ATOM   1846 H HB3  . MET B 1 8   ? 19.105 -1.143  22.895  1.00 102.07 ? 8   MET B HB3  1 
ATOM   1847 H HG2  . MET B 1 8   ? 17.135 -2.157  23.129  1.00 91.94  ? 8   MET B HG2  1 
ATOM   1848 H HG3  . MET B 1 8   ? 16.417 -1.141  22.139  1.00 91.94  ? 8   MET B HG3  1 
ATOM   1849 H HE1  . MET B 1 8   ? 17.028 -2.154  18.804  1.00 91.96  ? 8   MET B HE1  1 
ATOM   1850 H HE2  . MET B 1 8   ? 17.028 -0.903  19.783  1.00 91.96  ? 8   MET B HE2  1 
ATOM   1851 H HE3  . MET B 1 8   ? 18.402 -1.564  19.340  1.00 91.96  ? 8   MET B HE3  1 
ATOM   1852 N N    . LEU B 1 9   ? 18.833 -0.181  25.599  1.00 85.10  ? 9   LEU B N    1 
ATOM   1853 C CA   . LEU B 1 9   ? 18.647 -0.525  27.007  1.00 86.61  ? 9   LEU B CA   1 
ATOM   1854 C C    . LEU B 1 9   ? 17.938 0.606   27.753  1.00 81.91  ? 9   LEU B C    1 
ATOM   1855 O O    . LEU B 1 9   ? 17.063 0.356   28.593  1.00 77.33  ? 9   LEU B O    1 
ATOM   1856 C CB   . LEU B 1 9   ? 19.992 -0.822  27.680  1.00 84.61  ? 9   LEU B CB   1 
ATOM   1857 C CG   . LEU B 1 9   ? 20.810 -2.026  27.190  1.00 85.40  ? 9   LEU B CG   1 
ATOM   1858 C CD1  . LEU B 1 9   ? 22.170 -2.127  27.918  1.00 89.81  ? 9   LEU B CD1  1 
ATOM   1859 C CD2  . LEU B 1 9   ? 20.021 -3.357  27.314  1.00 82.76  ? 9   LEU B CD2  1 
ATOM   1860 H H    . LEU B 1 9   ? 19.651 -0.164  25.335  1.00 102.19 ? 9   LEU B H    1 
ATOM   1861 H HA   . LEU B 1 9   ? 18.105 -1.328  27.054  1.00 104.01 ? 9   LEU B HA   1 
ATOM   1862 H HB2  . LEU B 1 9   ? 20.556 -0.041  27.565  1.00 101.61 ? 9   LEU B HB2  1 
ATOM   1863 H HB3  . LEU B 1 9   ? 19.821 -0.971  28.623  1.00 101.61 ? 9   LEU B HB3  1 
ATOM   1864 H HG   . LEU B 1 9   ? 20.990 -1.884  26.247  1.00 102.56 ? 9   LEU B HG   1 
ATOM   1865 H HD11 . LEU B 1 9   ? 22.647 -2.905  27.589  1.00 107.85 ? 9   LEU B HD11 1 
ATOM   1866 H HD12 . LEU B 1 9   ? 22.684 -1.324  27.740  1.00 107.85 ? 9   LEU B HD12 1 
ATOM   1867 H HD13 . LEU B 1 9   ? 22.012 -2.214  28.871  1.00 107.85 ? 9   LEU B HD13 1 
ATOM   1868 H HD21 . LEU B 1 9   ? 20.601 -4.093  27.065  1.00 99.39  ? 9   LEU B HD21 1 
ATOM   1869 H HD22 . LEU B 1 9   ? 19.726 -3.464  28.232  1.00 99.39  ? 9   LEU B HD22 1 
ATOM   1870 H HD23 . LEU B 1 9   ? 19.253 -3.325  26.722  1.00 99.39  ? 9   LEU B HD23 1 
ATOM   1871 N N    . ARG B 1 10  ? 18.285 1.856   27.441  1.00 78.90  ? 10  ARG B N    1 
ATOM   1872 C CA   . ARG B 1 10  ? 17.585 2.992   28.029  1.00 79.20  ? 10  ARG B CA   1 
ATOM   1873 C C    . ARG B 1 10  ? 16.088 2.912   27.761  1.00 75.48  ? 10  ARG B C    1 
ATOM   1874 O O    . ARG B 1 10  ? 15.272 3.062   28.676  1.00 71.93  ? 10  ARG B O    1 
ATOM   1875 C CB   . ARG B 1 10  ? 18.170 4.285   27.460  1.00 88.58  ? 10  ARG B CB   1 
ATOM   1876 C CG   . ARG B 1 10  ? 17.530 5.587   27.934  1.00 83.15  ? 10  ARG B CG   1 
ATOM   1877 C CD   . ARG B 1 10  ? 17.774 5.892   29.393  1.00 88.56  ? 10  ARG B CD   1 
ATOM   1878 N NE   . ARG B 1 10  ? 17.894 7.329   29.660  1.00 107.96 ? 10  ARG B NE   1 
ATOM   1879 C CZ   . ARG B 1 10  ? 16.904 8.122   30.068  1.00 102.00 ? 10  ARG B CZ   1 
ATOM   1880 N NH1  . ARG B 1 10  ? 15.670 7.670   30.231  1.00 98.81  ? 10  ARG B NH1  1 
ATOM   1881 N NH2  . ARG B 1 10  ? 17.158 9.408   30.303  1.00 118.40 ? 10  ARG B NH2  1 
ATOM   1882 H H    . ARG B 1 10  ? 18.916 2.069   26.897  1.00 94.76  ? 10  ARG B H    1 
ATOM   1883 H HA   . ARG B 1 10  ? 17.713 2.988   28.991  1.00 95.12  ? 10  ARG B HA   1 
ATOM   1884 H HB2  . ARG B 1 10  ? 19.108 4.324   27.703  1.00 106.37 ? 10  ARG B HB2  1 
ATOM   1885 H HB3  . ARG B 1 10  ? 18.078 4.257   26.495  1.00 106.37 ? 10  ARG B HB3  1 
ATOM   1886 H HG2  . ARG B 1 10  ? 17.893 6.321   27.414  1.00 99.86  ? 10  ARG B HG2  1 
ATOM   1887 H HG3  . ARG B 1 10  ? 16.570 5.530   27.801  1.00 99.86  ? 10  ARG B HG3  1 
ATOM   1888 H HD2  . ARG B 1 10  ? 17.031 5.552   29.916  1.00 106.35 ? 10  ARG B HD2  1 
ATOM   1889 H HD3  . ARG B 1 10  ? 18.599 5.466   29.671  1.00 106.35 ? 10  ARG B HD3  1 
ATOM   1890 H HE   . ARG B 1 10  ? 18.667 7.689   29.544  1.00 129.63 ? 10  ARG B HE   1 
ATOM   1891 H HH11 . ARG B 1 10  ? 15.490 6.844   30.072  1.00 118.65 ? 10  ARG B HH11 1 
ATOM   1892 H HH12 . ARG B 1 10  ? 15.048 8.203   30.495  1.00 118.65 ? 10  ARG B HH12 1 
ATOM   1893 H HH21 . ARG B 1 10  ? 17.953 9.717   30.192  1.00 142.16 ? 10  ARG B HH21 1 
ATOM   1894 H HH22 . ARG B 1 10  ? 16.527 9.930   30.566  1.00 142.16 ? 10  ARG B HH22 1 
ATOM   1895 N N    . ALA B 1 11  ? 15.695 2.661   26.508  1.00 74.13  ? 11  ALA B N    1 
ATOM   1896 C CA   . ALA B 1 11  ? 14.268 2.611   26.196  1.00 70.28  ? 11  ALA B CA   1 
ATOM   1897 C C    . ALA B 1 11  ? 13.586 1.410   26.865  1.00 66.31  ? 11  ALA B C    1 
ATOM   1898 O O    . ALA B 1 11  ? 12.413 1.494   27.249  1.00 59.67  ? 11  ALA B O    1 
ATOM   1899 C CB   . ALA B 1 11  ? 14.070 2.572   24.685  1.00 80.23  ? 11  ALA B CB   1 
ATOM   1900 H H    . ALA B 1 11  ? 16.220 2.521   25.842  1.00 89.03  ? 11  ALA B H    1 
ATOM   1901 H HA   . ALA B 1 11  ? 13.845 3.415   26.536  1.00 84.41  ? 11  ALA B HA   1 
ATOM   1902 H HB1  . ALA B 1 11  ? 13.120 2.552   24.491  1.00 96.35  ? 11  ALA B HB1  1 
ATOM   1903 H HB2  . ALA B 1 11  ? 14.471 3.364   24.293  1.00 96.35  ? 11  ALA B HB2  1 
ATOM   1904 H HB3  . ALA B 1 11  ? 14.496 1.776   24.331  1.00 96.35  ? 11  ALA B HB3  1 
ATOM   1905 N N    . GLN B 1 12  ? 14.280 0.271   26.978  1.00 64.86  ? 12  GLN B N    1 
ATOM   1906 C CA   . GLN B 1 12  ? 13.649 -0.889  27.608  1.00 69.93  ? 12  GLN B CA   1 
ATOM   1907 C C    . GLN B 1 12  ? 13.352 -0.609  29.089  1.00 63.72  ? 12  GLN B C    1 
ATOM   1908 O O    . GLN B 1 12  ? 12.264 -0.906  29.583  1.00 58.77  ? 12  GLN B O    1 
ATOM   1909 C CB   . GLN B 1 12  ? 14.569 -2.114  27.480  1.00 74.11  ? 12  GLN B CB   1 
ATOM   1910 C CG   . GLN B 1 12  ? 14.751 -2.668  26.081  1.00 74.23  ? 12  GLN B CG   1 
ATOM   1911 C CD   . GLN B 1 12  ? 15.821 -3.776  25.954  1.00 68.61  ? 12  GLN B CD   1 
ATOM   1912 O OE1  . GLN B 1 12  ? 15.956 -4.370  24.900  1.00 73.82  ? 12  GLN B OE1  1 
ATOM   1913 N NE2  . GLN B 1 12  ? 16.546 -4.047  27.012  1.00 73.57  ? 12  GLN B NE2  1 
ATOM   1914 H H    . GLN B 1 12  ? 15.088 0.150   26.707  1.00 77.91  ? 12  GLN B H    1 
ATOM   1915 H HA   . GLN B 1 12  ? 12.814 -1.082  27.155  1.00 83.99  ? 12  GLN B HA   1 
ATOM   1916 H HB2  . GLN B 1 12  ? 15.448 -1.868  27.807  1.00 89.01  ? 12  GLN B HB2  1 
ATOM   1917 H HB3  . GLN B 1 12  ? 14.200 -2.827  28.024  1.00 89.01  ? 12  GLN B HB3  1 
ATOM   1918 H HG2  . GLN B 1 12  ? 13.907 -3.044  25.786  1.00 89.15  ? 12  GLN B HG2  1 
ATOM   1919 H HG3  . GLN B 1 12  ? 15.014 -1.942  25.494  1.00 89.15  ? 12  GLN B HG3  1 
ATOM   1920 H HE21 . GLN B 1 12  ? 16.418 -3.614  27.744  1.00 88.36  ? 12  GLN B HE21 1 
ATOM   1921 H HE22 . GLN B 1 12  ? 17.150 -4.659  26.974  1.00 88.36  ? 12  GLN B HE22 1 
ATOM   1922 N N    . THR B 1 13  ? 14.294 -0.000  29.791  1.00 63.20  ? 13  THR B N    1 
ATOM   1923 C CA   . THR B 1 13  ? 14.107 0.371   31.182  1.00 68.52  ? 13  THR B CA   1 
ATOM   1924 C C    . THR B 1 13  ? 13.039 1.445   31.353  1.00 70.28  ? 13  THR B C    1 
ATOM   1925 O O    . THR B 1 13  ? 12.238 1.377   32.299  1.00 71.86  ? 13  THR B O    1 
ATOM   1926 C CB   . THR B 1 13  ? 15.444 0.839   31.743  1.00 73.98  ? 13  THR B CB   1 
ATOM   1927 O OG1  . THR B 1 13  ? 16.401 -0.198  31.550  1.00 73.87  ? 13  THR B OG1  1 
ATOM   1928 C CG2  . THR B 1 13  ? 15.365 1.160   33.219  1.00 86.35  ? 13  THR B CG2  1 
ATOM   1929 H H    . THR B 1 13  ? 15.067 0.213   29.480  1.00 75.92  ? 13  THR B H    1 
ATOM   1930 H HA   . THR B 1 13  ? 13.805 -0.403  31.683  1.00 82.31  ? 13  THR B HA   1 
ATOM   1931 H HB   . THR B 1 13  ? 15.710 1.652   31.286  1.00 88.85  ? 13  THR B HB   1 
ATOM   1932 H HG1  . THR B 1 13  ? 16.566 -0.288  30.731  1.00 88.72  ? 13  THR B HG1  1 
ATOM   1933 H HG21 . THR B 1 13  ? 16.250 1.357   33.564  1.00 103.70 ? 13  THR B HG21 1 
ATOM   1934 H HG22 . THR B 1 13  ? 14.793 1.930   33.361  1.00 103.70 ? 13  THR B HG22 1 
ATOM   1935 H HG23 . THR B 1 13  ? 14.999 0.403   33.703  1.00 103.70 ? 13  THR B HG23 1 
ATOM   1936 N N    . ASN B 1 14  ? 13.020 2.457   30.495  1.00 69.46  ? 14  ASN B N    1 
ATOM   1937 C CA   . ASN B 1 14  ? 11.933 3.426   30.552  1.00 69.13  ? 14  ASN B CA   1 
ATOM   1938 C C    . ASN B 1 14  ? 10.615 2.734   30.365  1.00 68.12  ? 14  ASN B C    1 
ATOM   1939 O O    . ASN B 1 14  ? 9.650  3.018   31.035  1.00 66.42  ? 14  ASN B O    1 
ATOM   1940 C CB   . ASN B 1 14  ? 12.043 4.505   29.459  1.00 70.36  ? 14  ASN B CB   1 
ATOM   1941 C CG   . ASN B 1 14  ? 12.940 5.638   29.852  1.00 78.36  ? 14  ASN B CG   1 
ATOM   1942 O OD1  . ASN B 1 14  ? 14.106 5.447   30.203  1.00 78.18  ? 14  ASN B OD1  1 
ATOM   1943 N ND2  . ASN B 1 14  ? 12.415 6.843   29.747  1.00 82.84  ? 14  ASN B ND2  1 
ATOM   1944 H H    . ASN B 1 14  ? 13.610 2.601   29.886  1.00 83.43  ? 14  ASN B H    1 
ATOM   1945 H HA   . ASN B 1 14  ? 11.982 3.864   31.416  1.00 83.04  ? 14  ASN B HA   1 
ATOM   1946 H HB2  . ASN B 1 14  ? 12.403 4.103   28.653  1.00 84.51  ? 14  ASN B HB2  1 
ATOM   1947 H HB3  . ASN B 1 14  ? 11.161 4.869   29.283  1.00 84.51  ? 14  ASN B HB3  1 
ATOM   1948 H HD21 . ASN B 1 14  ? 12.880 7.535   29.958  1.00 99.49  ? 14  ASN B HD21 1 
ATOM   1949 H HD22 . ASN B 1 14  ? 11.607 6.937   29.468  1.00 99.49  ? 14  ASN B HD22 1 
HETATM 1950 O O    . HOX B 1 15  ? 7.642  0.536   30.771  1.00 72.54  ? 15  HOX B O    1 
HETATM 1951 C C    . HOX B 1 15  ? 8.782  0.430   30.316  1.00 69.69  ? 15  HOX B C    1 
HETATM 1952 N N    . HOX B 1 15  ? 10.557 1.865   29.371  1.00 66.77  ? 15  HOX B N    1 
HETATM 1953 C CA   . HOX B 1 15  ? 9.300  1.182   29.090  1.00 70.12  ? 15  HOX B CA   1 
HETATM 1954 C CB   . HOX B 1 15  ? 9.456  0.239   27.864  1.00 65.87  ? 15  HOX B CB   1 
HETATM 1955 C CG   . HOX B 1 15  ? 8.110  -0.294  27.562  1.00 65.88  ? 15  HOX B CG   1 
HETATM 1956 C CZ   . HOX B 1 15  ? 5.552  -1.267  27.025  1.00 69.65  ? 15  HOX B CZ   1 
HETATM 1957 N NZ   . HOX B 1 15  ? 4.272  -1.760  26.776  1.00 75.69  ? 15  HOX B NZ   1 
HETATM 1958 C CD1  . HOX B 1 15  ? 7.011  0.582   27.483  1.00 66.49  ? 15  HOX B CD1  1 
HETATM 1959 C CD2  . HOX B 1 15  ? 7.924  -1.660  27.371  1.00 67.10  ? 15  HOX B CD2  1 
HETATM 1960 C CE1  . HOX B 1 15  ? 5.743  0.122   27.205  1.00 67.83  ? 15  HOX B CE1  1 
HETATM 1961 C CE2  . HOX B 1 15  ? 6.658  -2.142  27.087  1.00 69.10  ? 15  HOX B CE2  1 
HETATM 1962 H HA   . HOX B 1 15  ? 8.456  1.912   28.895  1.00 84.22  ? 15  HOX B HA   1 
HETATM 1963 H HB   . HOX B 1 15  ? 10.173 -0.591  28.101  1.00 79.13  ? 15  HOX B HB   1 
HETATM 1964 H HBA  . HOX B 1 15  ? 9.870  0.805   26.989  1.00 79.13  ? 15  HOX B HBA  1 
HETATM 1965 H HNZ  . HOX B 1 15  ? 3.492  -1.144  26.715  1.00 90.90  ? 15  HOX B HNZ  1 
HETATM 1966 H HNZA . HOX B 1 15  ? 4.125  -2.742  26.675  1.00 90.90  ? 15  HOX B HNZA 1 
HETATM 1967 H HD1  . HOX B 1 15  ? 7.168  1.660   27.645  1.00 79.87  ? 15  HOX B HD1  1 
HETATM 1968 H HD2  . HOX B 1 15  ? 8.775  -2.354  27.444  1.00 80.60  ? 15  HOX B HD2  1 
HETATM 1969 H HE1  . HOX B 1 15  ? 4.900  0.825   27.127  1.00 81.47  ? 15  HOX B HE1  1 
HETATM 1970 H HE2  . HOX B 1 15  ? 6.519  -3.219  26.909  1.00 83.00  ? 15  HOX B HE2  1 
ATOM   1971 N N    . ILE B 1 16  ? 9.648  -0.371  30.902  1.00 68.61  ? 16  ILE B N    1 
ATOM   1972 C CA   . ILE B 1 16  ? 9.246  -1.191  32.033  1.00 72.80  ? 16  ILE B CA   1 
ATOM   1973 C C    . ILE B 1 16  ? 8.752  -0.302  33.155  1.00 72.54  ? 16  ILE B C    1 
ATOM   1974 O O    . ILE B 1 16  ? 7.711  -0.548  33.763  1.00 72.88  ? 16  ILE B O    1 
ATOM   1975 C CB   . ILE B 1 16  ? 10.392 -2.050  32.528  1.00 70.24  ? 16  ILE B CB   1 
ATOM   1976 C CG1  . ILE B 1 16  ? 10.536 -3.275  31.611  1.00 74.04  ? 16  ILE B CG1  1 
ATOM   1977 C CG2  . ILE B 1 16  ? 10.149 -2.460  33.957  1.00 83.32  ? 16  ILE B CG2  1 
ATOM   1978 C CD1  . ILE B 1 16  ? 11.871 -3.998  31.712  1.00 72.22  ? 16  ILE B CD1  1 
ATOM   1979 H H    . ILE B 1 16  ? 10.470 -0.460  30.668  1.00 82.41  ? 16  ILE B H    1 
ATOM   1980 H HA   . ILE B 1 16  ? 8.530  -1.780  31.747  1.00 87.44  ? 16  ILE B HA   1 
ATOM   1981 H HB   . ILE B 1 16  ? 11.219 -1.544  32.501  1.00 84.37  ? 16  ILE B HB   1 
ATOM   1982 H HG12 . ILE B 1 16  ? 9.842  -3.913  31.839  1.00 88.92  ? 16  ILE B HG12 1 
ATOM   1983 H HG13 . ILE B 1 16  ? 10.432 -2.985  30.692  1.00 88.92  ? 16  ILE B HG13 1 
ATOM   1984 H HG21 . ILE B 1 16  ? 10.721 -3.213  34.171  1.00 100.06 ? 16  ILE B HG21 1 
ATOM   1985 H HG22 . ILE B 1 16  ? 10.354 -1.712  34.539  1.00 100.06 ? 16  ILE B HG22 1 
ATOM   1986 H HG23 . ILE B 1 16  ? 9.217  -2.712  34.058  1.00 100.06 ? 16  ILE B HG23 1 
ATOM   1987 H HD11 . ILE B 1 16  ? 11.884 -4.728  31.073  1.00 86.74  ? 16  ILE B HD11 1 
ATOM   1988 H HD12 . ILE B 1 16  ? 12.585 -3.372  31.513  1.00 86.74  ? 16  ILE B HD12 1 
ATOM   1989 H HD13 . ILE B 1 16  ? 11.976 -4.345  32.612  1.00 86.74  ? 16  ILE B HD13 1 
ATOM   1990 N N    . LEU B 1 17  ? 9.508  0.756   33.409  1.00 71.57  ? 17  LEU B N    1 
ATOM   1991 C CA   . LEU B 1 17  ? 9.153  1.668   34.481  1.00 73.27  ? 17  LEU B CA   1 
ATOM   1992 C C    . LEU B 1 17  ? 7.799  2.324   34.249  1.00 80.87  ? 17  LEU B C    1 
ATOM   1993 O O    . LEU B 1 17  ? 6.998  2.430   35.179  1.00 82.57  ? 17  LEU B O    1 
ATOM   1994 C CB   . LEU B 1 17  ? 10.261 2.705   34.613  1.00 75.38  ? 17  LEU B CB   1 
ATOM   1995 C CG   . LEU B 1 17  ? 11.586 2.199   35.174  1.00 87.45  ? 17  LEU B CG   1 
ATOM   1996 C CD1  . LEU B 1 17  ? 12.666 3.276   35.062  1.00 89.10  ? 17  LEU B CD1  1 
ATOM   1997 C CD2  . LEU B 1 17  ? 11.484 1.731   36.661  1.00 90.28  ? 17  LEU B CD2  1 
ATOM   1998 H H    . LEU B 1 17  ? 10.223 0.965   32.980  1.00 85.96  ? 17  LEU B H    1 
ATOM   1999 H HA   . LEU B 1 17  ? 9.078  1.179   35.316  1.00 88.01  ? 17  LEU B HA   1 
ATOM   2000 H HB2  . LEU B 1 17  ? 10.442 3.068   33.732  1.00 90.53  ? 17  LEU B HB2  1 
ATOM   2001 H HB3  . LEU B 1 17  ? 9.948  3.407   35.204  1.00 90.53  ? 17  LEU B HB3  1 
ATOM   2002 H HG   . LEU B 1 17  ? 11.833 1.425   34.643  1.00 105.01 ? 17  LEU B HG   1 
ATOM   2003 H HD11 . LEU B 1 17  ? 13.507 2.914   35.383  1.00 107.00 ? 17  LEU B HD11 1 
ATOM   2004 H HD12 . LEU B 1 17  ? 12.753 3.540   34.133  1.00 107.00 ? 17  LEU B HD12 1 
ATOM   2005 H HD13 . LEU B 1 17  ? 12.408 4.040   35.601  1.00 107.00 ? 17  LEU B HD13 1 
ATOM   2006 H HD21 . LEU B 1 17  ? 12.378 1.595   37.011  1.00 108.42 ? 17  LEU B HD21 1 
ATOM   2007 H HD22 . LEU B 1 17  ? 11.027 2.413   37.176  1.00 108.42 ? 17  LEU B HD22 1 
ATOM   2008 H HD23 . LEU B 1 17  ? 10.985 0.899   36.697  1.00 108.42 ? 17  LEU B HD23 1 
ATOM   2009 N N    . LEU B 1 18  ? 7.514  2.799   33.043  1.00 76.17  ? 18  LEU B N    1 
ATOM   2010 C CA   . LEU B 1 18  ? 6.224  3.448   32.855  1.00 80.45  ? 18  LEU B CA   1 
ATOM   2011 C C    . LEU B 1 18  ? 5.064  2.470   32.985  1.00 79.97  ? 18  LEU B C    1 
ATOM   2012 O O    . LEU B 1 18  ? 3.932  2.882   33.286  1.00 81.12  ? 18  LEU B O    1 
ATOM   2013 C CB   . LEU B 1 18  ? 6.141  4.106   31.486  1.00 84.29  ? 18  LEU B CB   1 
ATOM   2014 C CG   . LEU B 1 18  ? 7.011  5.342   31.304  1.00 82.86  ? 18  LEU B CG   1 
ATOM   2015 C CD1  . LEU B 1 18  ? 7.085  5.707   29.821  1.00 77.45  ? 18  LEU B CD1  1 
ATOM   2016 C CD2  . LEU B 1 18  ? 6.494  6.483   32.123  1.00 85.25  ? 18  LEU B CD2  1 
ATOM   2017 H H    . LEU B 1 18  ? 8.023  2.760   32.351  1.00 91.49  ? 18  LEU B H    1 
ATOM   2018 H HA   . LEU B 1 18  ? 6.147  4.131   33.540  1.00 96.62  ? 18  LEU B HA   1 
ATOM   2019 H HB2  . LEU B 1 18  ? 6.414  3.458   30.818  1.00 101.23 ? 18  LEU B HB2  1 
ATOM   2020 H HB3  . LEU B 1 18  ? 5.221  4.373   31.331  1.00 101.23 ? 18  LEU B HB3  1 
ATOM   2021 H HG   . LEU B 1 18  ? 7.911  5.156   31.614  1.00 99.51  ? 18  LEU B HG   1 
ATOM   2022 H HD11 . LEU B 1 18  ? 7.608  6.518   29.721  1.00 93.02  ? 18  LEU B HD11 1 
ATOM   2023 H HD12 . LEU B 1 18  ? 7.507  4.980   29.337  1.00 93.02  ? 18  LEU B HD12 1 
ATOM   2024 H HD13 . LEU B 1 18  ? 6.186  5.851   29.485  1.00 93.02  ? 18  LEU B HD13 1 
ATOM   2025 H HD21 . LEU B 1 18  ? 7.004  7.280   31.911  1.00 102.38 ? 18  LEU B HD21 1 
ATOM   2026 H HD22 . LEU B 1 18  ? 5.558  6.624   31.913  1.00 102.38 ? 18  LEU B HD22 1 
ATOM   2027 H HD23 . LEU B 1 18  ? 6.593  6.267   33.063  1.00 102.38 ? 18  LEU B HD23 1 
ATOM   2028 N N    . MET B 1 19  ? 5.300  1.191   32.689  1.00 75.61  ? 19  MET B N    1 
ATOM   2029 C CA   . MET B 1 19  ? 4.231  0.216   32.816  1.00 81.30  ? 19  MET B CA   1 
ATOM   2030 C C    . MET B 1 19  ? 3.953  -0.048  34.288  1.00 86.48  ? 19  MET B C    1 
ATOM   2031 O O    . MET B 1 19  ? 2.798  -0.171  34.713  1.00 82.42  ? 19  MET B O    1 
ATOM   2032 C CB   . MET B 1 19  ? 4.625  -1.083  32.125  1.00 80.05  ? 19  MET B CB   1 
ATOM   2033 C CG   . MET B 1 19  ? 4.663  -1.054  30.597  1.00 80.29  ? 19  MET B CG   1 
ATOM   2034 S SD   . MET B 1 19  ? 3.058  -0.787  29.768  1.00 78.78  ? 19  MET B SD   1 
ATOM   2035 C CE   . MET B 1 19  ? 2.230  -2.316  30.275  1.00 76.80  ? 19  MET B CE   1 
ATOM   2036 H H    . MET B 1 19  ? 6.053  0.874   32.420  1.00 90.81  ? 19  MET B H    1 
ATOM   2037 H HA   . MET B 1 19  ? 3.434  0.555   32.380  1.00 97.64  ? 19  MET B HA   1 
ATOM   2038 H HB2  . MET B 1 19  ? 5.513  -1.329  32.427  1.00 96.13  ? 19  MET B HB2  1 
ATOM   2039 H HB3  . MET B 1 19  ? 3.986  -1.767  32.381  1.00 96.13  ? 19  MET B HB3  1 
ATOM   2040 H HG2  . MET B 1 19  ? 5.252  -0.334  30.321  1.00 96.43  ? 19  MET B HG2  1 
ATOM   2041 H HG3  . MET B 1 19  ? 5.009  -1.904  30.285  1.00 96.43  ? 19  MET B HG3  1 
ATOM   2042 H HE1  . MET B 1 19  ? 1.296  -2.269  30.016  1.00 92.24  ? 19  MET B HE1  1 
ATOM   2043 H HE2  . MET B 1 19  ? 2.658  -3.067  29.835  1.00 92.24  ? 19  MET B HE2  1 
ATOM   2044 H HE3  . MET B 1 19  ? 2.303  -2.410  31.237  1.00 92.24  ? 19  MET B HE3  1 
ATOM   2045 N N    . VAL B 1 20  ? 5.017  -0.086  35.083  1.00 84.32  ? 20  VAL B N    1 
ATOM   2046 C CA   . VAL B 1 20  ? 4.838  -0.162  36.522  1.00 89.49  ? 20  VAL B CA   1 
ATOM   2047 C C    . VAL B 1 20  ? 3.919  0.962   36.958  1.00 88.12  ? 20  VAL B C    1 
ATOM   2048 O O    . VAL B 1 20  ? 2.816  0.722   37.441  1.00 94.23  ? 20  VAL B O    1 
ATOM   2049 C CB   . VAL B 1 20  ? 6.206  -0.123  37.226  1.00 86.24  ? 20  VAL B CB   1 
ATOM   2050 C CG1  . VAL B 1 20  ? 6.093  0.096   38.717  1.00 85.64  ? 20  VAL B CG1  1 
ATOM   2051 C CG2  . VAL B 1 20  ? 6.945  -1.444  36.949  1.00 90.74  ? 20  VAL B CG2  1 
ATOM   2052 H H    . VAL B 1 20  ? 5.834  -0.069  34.818  1.00 101.26 ? 20  VAL B H    1 
ATOM   2053 H HA   . VAL B 1 20  ? 4.418  -1.001  36.769  1.00 107.46 ? 20  VAL B HA   1 
ATOM   2054 H HB   . VAL B 1 20  ? 6.705  0.631   36.874  1.00 103.57 ? 20  VAL B HB   1 
ATOM   2055 H HG11 . VAL B 1 20  ? 6.942  -0.123  39.133  1.00 102.85 ? 20  VAL B HG11 1 
ATOM   2056 H HG12 . VAL B 1 20  ? 5.873  1.025   38.884  1.00 102.85 ? 20  VAL B HG12 1 
ATOM   2057 H HG13 . VAL B 1 20  ? 5.395  -0.478  39.068  1.00 102.85 ? 20  VAL B HG13 1 
ATOM   2058 H HG21 . VAL B 1 20  ? 7.820  -1.409  37.365  1.00 108.97 ? 20  VAL B HG21 1 
ATOM   2059 H HG22 . VAL B 1 20  ? 6.431  -2.177  37.321  1.00 108.97 ? 20  VAL B HG22 1 
ATOM   2060 H HG23 . VAL B 1 20  ? 7.038  -1.558  35.990  1.00 108.97 ? 20  VAL B HG23 1 
ATOM   2061 N N    . LEU B 1 21  ? 4.270  2.203   36.639  1.00 82.62  ? 21  LEU B N    1 
ATOM   2062 C CA   . LEU B 1 21  ? 3.445  3.295   37.147  1.00 86.34  ? 21  LEU B CA   1 
ATOM   2063 C C    . LEU B 1 21  ? 2.016  3.226   36.617  1.00 89.93  ? 21  LEU B C    1 
ATOM   2064 O O    . LEU B 1 21  ? 1.081  3.666   37.298  1.00 91.44  ? 21  LEU B O    1 
ATOM   2065 C CB   . LEU B 1 21  ? 4.074  4.651   36.830  1.00 87.27  ? 21  LEU B CB   1 
ATOM   2066 C CG   . LEU B 1 21  ? 5.280  4.974   37.722  1.00 85.77  ? 21  LEU B CG   1 
ATOM   2067 C CD1  . LEU B 1 21  ? 5.751  6.406   37.480  1.00 84.06  ? 21  LEU B CD1  1 
ATOM   2068 C CD2  . LEU B 1 21  ? 5.019  4.767   39.221  1.00 87.27  ? 21  LEU B CD2  1 
ATOM   2069 H H    . LEU B 1 21  ? 4.944  2.430   36.156  1.00 99.22  ? 21  LEU B H    1 
ATOM   2070 H HA   . LEU B 1 21  ? 3.407  3.217   38.113  1.00 103.68 ? 21  LEU B HA   1 
ATOM   2071 H HB2  . LEU B 1 21  ? 4.375  4.650   35.908  1.00 104.80 ? 21  LEU B HB2  1 
ATOM   2072 H HB3  . LEU B 1 21  ? 3.409  5.345   36.961  1.00 104.80 ? 21  LEU B HB3  1 
ATOM   2073 H HG   . LEU B 1 21  ? 5.977  4.346   37.478  1.00 103.00 ? 21  LEU B HG   1 
ATOM   2074 H HD11 . LEU B 1 21  ? 6.540  6.574   38.018  1.00 100.95 ? 21  LEU B HD11 1 
ATOM   2075 H HD12 . LEU B 1 21  ? 5.963  6.513   36.539  1.00 100.95 ? 21  LEU B HD12 1 
ATOM   2076 H HD13 . LEU B 1 21  ? 5.042  7.018   37.731  1.00 100.95 ? 21  LEU B HD13 1 
ATOM   2077 H HD21 . LEU B 1 21  ? 5.704  5.231   39.728  1.00 104.80 ? 21  LEU B HD21 1 
ATOM   2078 H HD22 . LEU B 1 21  ? 4.145  5.124   39.443  1.00 104.80 ? 21  LEU B HD22 1 
ATOM   2079 H HD23 . LEU B 1 21  ? 5.048  3.817   39.419  1.00 104.80 ? 21  LEU B HD23 1 
ATOM   2080 N N    . LYS B 1 22  ? 1.819  2.673   35.418  1.00 89.95  ? 22  LYS B N    1 
ATOM   2081 C CA   . LYS B 1 22  ? 0.470  2.568   34.862  1.00 95.52  ? 22  LYS B CA   1 
ATOM   2082 C C    . LYS B 1 22  ? -0.409 1.630   35.683  1.00 97.82  ? 22  LYS B C    1 
ATOM   2083 O O    . LYS B 1 22  ? -1.633 1.829   35.754  1.00 96.44  ? 22  LYS B O    1 
ATOM   2084 C CB   . LYS B 1 22  ? 0.527  2.123   33.392  1.00 90.93  ? 22  LYS B CB   1 
ATOM   2085 C CG   . LYS B 1 22  ? -0.776 2.412   32.620  1.00 96.82  ? 22  LYS B CG   1 
ATOM   2086 C CD   . LYS B 1 22  ? -0.644 2.137   31.122  1.00 96.85  ? 22  LYS B CD   1 
ATOM   2087 C CE   . LYS B 1 22  ? -1.967 2.321   30.363  1.00 102.79 ? 22  LYS B CE   1 
ATOM   2088 N NZ   . LYS B 1 22  ? -2.955 1.231   30.629  1.00 113.28 ? 22  LYS B NZ   1 
ATOM   2089 H H    . LYS B 1 22  ? 2.440  2.355   34.914  1.00 108.01 ? 22  LYS B H    1 
ATOM   2090 H HA   . LYS B 1 22  ? 0.058  3.446   34.881  1.00 114.70 ? 22  LYS B HA   1 
ATOM   2091 H HB2  . LYS B 1 22  ? 1.248  2.597   32.949  1.00 109.19 ? 22  LYS B HB2  1 
ATOM   2092 H HB3  . LYS B 1 22  ? 0.687  1.167   33.359  1.00 109.19 ? 22  LYS B HB3  1 
ATOM   2093 H HG2  . LYS B 1 22  ? -1.483 1.847   32.968  1.00 116.26 ? 22  LYS B HG2  1 
ATOM   2094 H HG3  . LYS B 1 22  ? -1.012 3.346   32.734  1.00 116.26 ? 22  LYS B HG3  1 
ATOM   2095 H HD2  . LYS B 1 22  ? 0.005  2.751   30.744  1.00 116.30 ? 22  LYS B HD2  1 
ATOM   2096 H HD3  . LYS B 1 22  ? -0.350 1.222   30.993  1.00 116.30 ? 22  LYS B HD3  1 
ATOM   2097 H HE2  . LYS B 1 22  ? -2.370 3.161   30.633  1.00 123.42 ? 22  LYS B HE2  1 
ATOM   2098 H HE3  . LYS B 1 22  ? -1.784 2.332   29.411  1.00 123.42 ? 22  LYS B HE3  1 
ATOM   2099 H HZ1  . LYS B 1 22  ? -3.699 1.374   30.162  1.00 136.02 ? 22  LYS B HZ1  1 
ATOM   2100 H HZ2  . LYS B 1 22  ? -2.612 0.445   30.392  1.00 136.02 ? 22  LYS B HZ2  1 
ATOM   2101 H HZ3  . LYS B 1 22  ? -3.158 1.209   31.495  1.00 136.02 ? 22  LYS B HZ3  1 
ATOM   2102 N N    . GLN B 1 23  ? 0.184  0.637   36.334  1.00 102.00 ? 23  GLN B N    1 
ATOM   2103 C CA   . GLN B 1 23  ? -0.620 -0.232  37.184  1.00 102.55 ? 23  GLN B CA   1 
ATOM   2104 C C    . GLN B 1 23  ? -0.998 0.438   38.500  1.00 108.13 ? 23  GLN B C    1 
ATOM   2105 O O    . GLN B 1 23  ? -2.020 0.087   39.100  1.00 117.00 ? 23  GLN B O    1 
ATOM   2106 C CB   . GLN B 1 23  ? 0.138  -1.517  37.491  1.00 107.08 ? 23  GLN B CB   1 
ATOM   2107 C CG   . GLN B 1 23  ? 0.440  -2.378  36.298  1.00 106.51 ? 23  GLN B CG   1 
ATOM   2108 C CD   . GLN B 1 23  ? 1.329  -3.540  36.687  1.00 119.75 ? 23  GLN B CD   1 
ATOM   2109 O OE1  . GLN B 1 23  ? 1.461  -3.868  37.877  1.00 121.19 ? 23  GLN B OE1  1 
ATOM   2110 N NE2  . GLN B 1 23  ? 1.964  -4.162  35.694  1.00 113.68 ? 23  GLN B NE2  1 
ATOM   2111 H H    . GLN B 1 23  ? 1.023  0.450   36.303  1.00 122.48 ? 23  GLN B H    1 
ATOM   2112 H HA   . GLN B 1 23  ? -1.432 -0.453  36.703  1.00 123.14 ? 23  GLN B HA   1 
ATOM   2113 H HB2  . GLN B 1 23  ? 0.985  -1.282  37.902  1.00 128.58 ? 23  GLN B HB2  1 
ATOM   2114 H HB3  . GLN B 1 23  ? -0.393 -2.047  38.105  1.00 128.58 ? 23  GLN B HB3  1 
ATOM   2115 H HG2  . GLN B 1 23  ? -0.388 -2.730  35.935  1.00 127.90 ? 23  GLN B HG2  1 
ATOM   2116 H HG3  . GLN B 1 23  ? 0.899  -1.850  35.625  1.00 127.90 ? 23  GLN B HG3  1 
ATOM   2117 H HE21 . GLN B 1 23  ? 1.857  -3.897  34.882  1.00 136.50 ? 23  GLN B HE21 1 
ATOM   2118 H HE22 . GLN B 1 23  ? 2.480  -4.828  35.864  1.00 136.50 ? 23  GLN B HE22 1 
ATOM   2119 N N    . GLY B 1 24  ? -0.200 1.398   38.967  1.00 107.24 ? 24  GLY B N    1 
ATOM   2120 C CA   . GLY B 1 24  ? -0.502 2.098   40.200  1.00 108.87 ? 24  GLY B CA   1 
ATOM   2121 C C    . GLY B 1 24  ? 0.653  2.925   40.707  1.00 105.56 ? 24  GLY B C    1 
ATOM   2122 O O    . GLY B 1 24  ? 1.814  2.562   40.500  1.00 104.00 ? 24  GLY B O    1 
ATOM   2123 H H    . GLY B 1 24  ? 0.524  1.658   38.583  1.00 128.77 ? 24  GLY B H    1 
ATOM   2124 H HA2  . GLY B 1 24  ? -1.257 2.689   40.054  1.00 130.72 ? 24  GLY B HA2  1 
ATOM   2125 H HA3  . GLY B 1 24  ? -0.735 1.452   40.885  1.00 130.72 ? 24  GLY B HA3  1 
ATOM   2126 N N    . ASP B 1 25  ? 0.348  4.028   41.396  1.00 104.57 ? 25  ASP B N    1 
ATOM   2127 C CA   . ASP B 1 25  ? 1.361  4.827   42.067  1.00 103.62 ? 25  ASP B CA   1 
ATOM   2128 C C    . ASP B 1 25  ? 2.348  3.926   42.819  1.00 102.07 ? 25  ASP B C    1 
ATOM   2129 O O    . ASP B 1 25  ? 1.954  2.854   43.300  1.00 106.50 ? 25  ASP B O    1 
ATOM   2130 C CB   . ASP B 1 25  ? 0.731  5.803   43.071  1.00 104.48 ? 25  ASP B CB   1 
ATOM   2131 C CG   . ASP B 1 25  ? -0.397 6.655   42.487  1.00 100.36 ? 25  ASP B CG   1 
ATOM   2132 O OD1  . ASP B 1 25  ? -0.746 6.546   41.276  1.00 94.33  ? 25  ASP B OD1  1 
ATOM   2133 O OD2  . ASP B 1 25  ? -0.940 7.438   43.306  1.00 100.88 ? 25  ASP B OD2  1 
ATOM   2134 H H    . ASP B 1 25  ? -0.450 4.333   41.488  1.00 125.56 ? 25  ASP B H    1 
ATOM   2135 H HA   . ASP B 1 25  ? 1.831  5.339   41.391  1.00 124.42 ? 25  ASP B HA   1 
ATOM   2136 H HB2  . ASP B 1 25  ? 0.363  5.294   43.811  1.00 125.46 ? 25  ASP B HB2  1 
ATOM   2137 H HB3  . ASP B 1 25  ? 1.419  6.406   43.392  1.00 125.46 ? 25  ASP B HB3  1 
ATOM   2138 N N    . ASN B 1 26  ? 3.611  4.318   42.938  1.00 103.22 ? 26  ASN B N    1 
ATOM   2139 C CA   . ASN B 1 26  ? 4.592  3.462   43.587  1.00 106.86 ? 26  ASN B CA   1 
ATOM   2140 C C    . ASN B 1 26  ? 5.821  4.277   43.945  1.00 112.76 ? 26  ASN B C    1 
ATOM   2141 O O    . ASN B 1 26  ? 6.026  5.379   43.435  1.00 109.53 ? 26  ASN B O    1 
ATOM   2142 C CB   . ASN B 1 26  ? 4.972  2.266   42.702  1.00 96.52  ? 26  ASN B CB   1 
ATOM   2143 C CG   . ASN B 1 26  ? 5.628  1.140   43.482  1.00 99.40  ? 26  ASN B CG   1 
ATOM   2144 O OD1  . ASN B 1 26  ? 6.253  1.371   44.515  1.00 105.06 ? 26  ASN B OD1  1 
ATOM   2145 N ND2  . ASN B 1 26  ? 5.506  -0.084  42.982  1.00 105.87 ? 26  ASN B ND2  1 
ATOM   2146 H H    . ASN B 1 26  ? 3.921  5.068   42.655  1.00 123.94 ? 26  ASN B H    1 
ATOM   2147 H HA   . ASN B 1 26  ? 4.212  3.124   44.413  1.00 128.31 ? 26  ASN B HA   1 
ATOM   2148 H HB2  . ASN B 1 26  ? 4.170  1.915   42.285  1.00 115.90 ? 26  ASN B HB2  1 
ATOM   2149 H HB3  . ASN B 1 26  ? 5.597  2.563   42.022  1.00 115.90 ? 26  ASN B HB3  1 
ATOM   2150 H HD21 . ASN B 1 26  ? 5.861  -0.753  43.390  1.00 127.12 ? 26  ASN B HD21 1 
ATOM   2151 H HD22 . ASN B 1 26  ? 5.072  -0.208  42.250  1.00 127.12 ? 26  ASN B HD22 1 
ATOM   2152 N N    . TYR B 1 27  ? 6.618  3.720   44.864  1.00 122.65 ? 27  TYR B N    1 
ATOM   2153 C CA   . TYR B 1 27  ? 7.847  4.319   45.374  1.00 129.26 ? 27  TYR B CA   1 
ATOM   2154 C C    . TYR B 1 27  ? 9.027  3.429   44.994  1.00 126.62 ? 27  TYR B C    1 
ATOM   2155 O O    . TYR B 1 27  ? 8.858  2.263   44.620  1.00 122.54 ? 27  TYR B O    1 
ATOM   2156 C CB   . TYR B 1 27  ? 7.812  4.532   46.914  1.00 139.54 ? 27  TYR B CB   1 
ATOM   2157 C CG   . TYR B 1 27  ? 7.814  3.273   47.748  1.00 140.48 ? 27  TYR B CG   1 
ATOM   2158 C CD1  . TYR B 1 27  ? 6.684  2.490   47.854  1.00 136.98 ? 27  TYR B CD1  1 
ATOM   2159 C CD2  . TYR B 1 27  ? 8.945  2.892   48.470  1.00 145.30 ? 27  TYR B CD2  1 
ATOM   2160 C CE1  . TYR B 1 27  ? 6.686  1.345   48.638  1.00 143.67 ? 27  TYR B CE1  1 
ATOM   2161 C CE2  . TYR B 1 27  ? 8.959  1.749   49.220  1.00 148.19 ? 27  TYR B CE2  1 
ATOM   2162 C CZ   . TYR B 1 27  ? 7.825  0.976   49.312  1.00 143.70 ? 27  TYR B CZ   1 
ATOM   2163 O OH   . TYR B 1 27  ? 7.826  -0.167  50.085  1.00 130.26 ? 27  TYR B OH   1 
ATOM   2164 H H    . TYR B 1 27  ? 6.455  2.956   45.223  1.00 147.25 ? 27  TYR B H    1 
ATOM   2165 H HA   . TYR B 1 27  ? 7.965  5.194   44.973  1.00 155.19 ? 27  TYR B HA   1 
ATOM   2166 H HB2  . TYR B 1 27  ? 8.594  5.047   47.167  1.00 167.52 ? 27  TYR B HB2  1 
ATOM   2167 H HB3  . TYR B 1 27  ? 7.006  5.023   47.135  1.00 167.52 ? 27  TYR B HB3  1 
ATOM   2168 H HD1  . TYR B 1 27  ? 5.912  2.732   47.395  1.00 164.46 ? 27  TYR B HD1  1 
ATOM   2169 H HD2  . TYR B 1 27  ? 9.706  3.427   48.441  1.00 174.44 ? 27  TYR B HD2  1 
ATOM   2170 H HE1  . TYR B 1 27  ? 5.916  0.826   48.706  1.00 172.48 ? 27  TYR B HE1  1 
ATOM   2171 H HE2  . TYR B 1 27  ? 9.734  1.495   49.667  1.00 177.90 ? 27  TYR B HE2  1 
ATOM   2172 H HH   . TYR B 1 27  ? 8.609  -0.343  50.336  1.00 156.39 ? 27  TYR B HH   1 
ATOM   2173 N N    . VAL B 1 28  ? 10.232 3.987   45.100  1.00 127.71 ? 28  VAL B N    1 
ATOM   2174 C CA   . VAL B 1 28  ? 11.378 3.435   44.384  1.00 126.18 ? 28  VAL B CA   1 
ATOM   2175 C C    . VAL B 1 28  ? 11.643 1.994   44.812  1.00 124.71 ? 28  VAL B C    1 
ATOM   2176 O O    . VAL B 1 28  ? 11.664 1.086   43.987  1.00 120.24 ? 28  VAL B O    1 
ATOM   2177 C CB   . VAL B 1 28  ? 12.616 4.319   44.581  1.00 104.22 ? 28  VAL B CB   1 
ATOM   2178 C CG1  . VAL B 1 28  ? 13.825 3.619   44.075  1.00 100.53 ? 28  VAL B CG1  1 
ATOM   2179 C CG2  . VAL B 1 28  ? 12.434 5.636   43.881  1.00 100.31 ? 28  VAL B CG2  1 
ATOM   2180 H H    . VAL B 1 28  ? 10.411 4.680   45.576  1.00 153.33 ? 28  VAL B H    1 
ATOM   2181 H HA   . VAL B 1 28  ? 11.165 3.424   43.437  1.00 151.50 ? 28  VAL B HA   1 
ATOM   2182 H HB   . VAL B 1 28  ? 12.736 4.495   45.527  1.00 125.14 ? 28  VAL B HB   1 
ATOM   2183 H HG11 . VAL B 1 28  ? 14.531 4.270   43.936  1.00 120.72 ? 28  VAL B HG11 1 
ATOM   2184 H HG12 . VAL B 1 28  ? 14.106 2.961   44.730  1.00 120.72 ? 28  VAL B HG12 1 
ATOM   2185 H HG13 . VAL B 1 28  ? 13.609 3.181   43.237  1.00 120.72 ? 28  VAL B HG13 1 
ATOM   2186 H HG21 . VAL B 1 28  ? 13.299 5.958   43.585  1.00 120.45 ? 28  VAL B HG21 1 
ATOM   2187 H HG22 . VAL B 1 28  ? 11.848 5.510   43.118  1.00 120.45 ? 28  VAL B HG22 1 
ATOM   2188 H HG23 . VAL B 1 28  ? 12.039 6.270   44.500  1.00 120.45 ? 28  VAL B HG23 1 
ATOM   2189 N N    . TYR B 1 29  ? 11.824 1.776   46.125  1.00 129.58 ? 29  TYR B N    1 
ATOM   2190 C CA   . TYR B 1 29  ? 12.086 0.426   46.652  1.00 125.82 ? 29  TYR B CA   1 
ATOM   2191 C C    . TYR B 1 29  ? 10.982 -0.551  46.269  1.00 126.26 ? 29  TYR B C    1 
ATOM   2192 O O    . TYR B 1 29  ? 11.256 -1.725  45.988  1.00 115.70 ? 29  TYR B O    1 
ATOM   2193 C CB   . TYR B 1 29  ? 12.262 0.525   48.179  1.00 129.69 ? 29  TYR B CB   1 
ATOM   2194 C CG   . TYR B 1 29  ? 12.326 -0.731  49.036  1.00 126.69 ? 29  TYR B CG   1 
ATOM   2195 C CD1  . TYR B 1 29  ? 11.164 -1.400  49.451  1.00 117.59 ? 29  TYR B CD1  1 
ATOM   2196 C CD2  . TYR B 1 29  ? 13.552 -1.179  49.553  1.00 116.87 ? 29  TYR B CD2  1 
ATOM   2197 C CE1  . TYR B 1 29  ? 11.240 -2.523  50.310  1.00 115.53 ? 29  TYR B CE1  1 
ATOM   2198 C CE2  . TYR B 1 29  ? 13.632 -2.283  50.388  1.00 124.31 ? 29  TYR B CE2  1 
ATOM   2199 C CZ   . TYR B 1 29  ? 12.481 -2.950  50.764  1.00 118.00 ? 29  TYR B CZ   1 
ATOM   2200 O OH   . TYR B 1 29  ? 12.597 -4.048  51.602  1.00 123.73 ? 29  TYR B OH   1 
ATOM   2201 H H    . TYR B 1 29  ? 11.801 2.388   46.729  1.00 155.57 ? 29  TYR B H    1 
ATOM   2202 H HA   . TYR B 1 29  ? 12.905 0.072   46.271  1.00 151.06 ? 29  TYR B HA   1 
ATOM   2203 H HB2  . TYR B 1 29  ? 13.093 0.999   48.340  1.00 155.71 ? 29  TYR B HB2  1 
ATOM   2204 H HB3  . TYR B 1 29  ? 11.515 1.041   48.519  1.00 155.71 ? 29  TYR B HB3  1 
ATOM   2205 H HD1  . TYR B 1 29  ? 10.333 -1.102  49.158  1.00 141.18 ? 29  TYR B HD1  1 
ATOM   2206 H HD2  . TYR B 1 29  ? 14.332 -0.724  49.330  1.00 140.32 ? 29  TYR B HD2  1 
ATOM   2207 H HE1  . TYR B 1 29  ? 10.467 -2.971  50.567  1.00 138.72 ? 29  TYR B HE1  1 
ATOM   2208 H HE2  . TYR B 1 29  ? 14.460 -2.574  50.696  1.00 149.25 ? 29  TYR B HE2  1 
ATOM   2209 H HH   . TYR B 1 29  ? 13.397 -4.304  51.630  1.00 148.56 ? 29  TYR B HH   1 
ATOM   2210 N N    . GLY B 1 30  ? 9.730  -0.090  46.218  1.00 128.68 ? 30  GLY B N    1 
ATOM   2211 C CA   . GLY B 1 30  ? 8.657  -0.962  45.763  1.00 132.05 ? 30  GLY B CA   1 
ATOM   2212 C C    . GLY B 1 30  ? 8.748  -1.272  44.272  1.00 125.91 ? 30  GLY B C    1 
ATOM   2213 O O    . GLY B 1 30  ? 8.406  -2.368  43.835  1.00 117.04 ? 30  GLY B O    1 
ATOM   2214 H H    . GLY B 1 30  ? 9.484  0.705   46.436  1.00 154.49 ? 30  GLY B H    1 
ATOM   2215 H HA2  . GLY B 1 30  ? 8.696  -1.799  46.252  1.00 158.54 ? 30  GLY B HA2  1 
ATOM   2216 H HA3  . GLY B 1 30  ? 7.803  -0.535  45.935  1.00 158.54 ? 30  GLY B HA3  1 
ATOM   2217 N N    . ILE B 1 31  ? 9.183  -0.301  43.477  1.00 123.23 ? 31  ILE B N    1 
ATOM   2218 C CA   . ILE B 1 31  ? 9.389  -0.558  42.057  1.00 126.83 ? 31  ILE B CA   1 
ATOM   2219 C C    . ILE B 1 31  ? 10.517 -1.558  41.859  1.00 119.29 ? 31  ILE B C    1 
ATOM   2220 O O    . ILE B 1 31  ? 10.372 -2.544  41.131  1.00 110.21 ? 31  ILE B O    1 
ATOM   2221 C CB   . ILE B 1 31  ? 9.656  0.767   41.319  1.00 127.91 ? 31  ILE B CB   1 
ATOM   2222 C CG1  . ILE B 1 31  ? 8.431  1.664   41.445  1.00 120.53 ? 31  ILE B CG1  1 
ATOM   2223 C CG2  . ILE B 1 31  ? 10.039 0.505   39.904  1.00 127.53 ? 31  ILE B CG2  1 
ATOM   2224 C CD1  . ILE B 1 31  ? 8.609  3.019   40.842  1.00 116.39 ? 31  ILE B CD1  1 
ATOM   2225 H H    . ILE B 1 31  ? 9.363  0.501   43.730  1.00 147.95 ? 31  ILE B H    1 
ATOM   2226 H HA   . ILE B 1 31  ? 8.584  -0.951  41.685  1.00 152.27 ? 31  ILE B HA   1 
ATOM   2227 H HB   . ILE B 1 31  ? 10.405 1.230   41.726  1.00 153.57 ? 31  ILE B HB   1 
ATOM   2228 H HG12 . ILE B 1 31  ? 7.684  1.237   40.997  1.00 144.72 ? 31  ILE B HG12 1 
ATOM   2229 H HG13 . ILE B 1 31  ? 8.228  1.784   42.386  1.00 144.72 ? 31  ILE B HG13 1 
ATOM   2230 H HG21 . ILE B 1 31  ? 10.158 1.353   39.447  1.00 153.11 ? 31  ILE B HG21 1 
ATOM   2231 H HG22 . ILE B 1 31  ? 10.869 0.002   39.889  1.00 153.11 ? 31  ILE B HG22 1 
ATOM   2232 H HG23 . ILE B 1 31  ? 9.335  -0.006  39.475  1.00 153.11 ? 31  ILE B HG23 1 
ATOM   2233 H HD11 . ILE B 1 31  ? 7.942  3.619   41.211  1.00 139.75 ? 31  ILE B HD11 1 
ATOM   2234 H HD12 . ILE B 1 31  ? 9.499  3.344   41.052  1.00 139.75 ? 31  ILE B HD12 1 
ATOM   2235 H HD13 . ILE B 1 31  ? 8.499  2.953   39.880  1.00 139.75 ? 31  ILE B HD13 1 
ATOM   2236 N N    . ILE B 1 32  ? 11.660 -1.321  42.490  1.00 124.27 ? 32  ILE B N    1 
ATOM   2237 C CA   . ILE B 1 32  ? 12.768 -2.253  42.350  1.00 119.97 ? 32  ILE B CA   1 
ATOM   2238 C C    . ILE B 1 32  ? 12.318 -3.624  42.810  1.00 110.40 ? 32  ILE B C    1 
ATOM   2239 O O    . ILE B 1 32  ? 12.573 -4.642  42.164  1.00 110.55 ? 32  ILE B O    1 
ATOM   2240 C CB   . ILE B 1 32  ? 13.994 -1.745  43.125  1.00 114.66 ? 32  ILE B CB   1 
ATOM   2241 C CG1  . ILE B 1 32  ? 14.429 -0.408  42.521  1.00 110.99 ? 32  ILE B CG1  1 
ATOM   2242 C CG2  . ILE B 1 32  ? 15.084 -2.754  43.082  1.00 125.91 ? 32  ILE B CG2  1 
ATOM   2243 C CD1  . ILE B 1 32  ? 15.559 0.283   43.240  1.00 111.87 ? 32  ILE B CD1  1 
ATOM   2244 H H    . ILE B 1 32  ? 11.816 -0.642  42.995  1.00 149.20 ? 32  ILE B H    1 
ATOM   2245 H HA   . ILE B 1 32  ? 13.032 -2.315  41.419  1.00 144.04 ? 32  ILE B HA   1 
ATOM   2246 H HB   . ILE B 1 32  ? 13.770 -1.607  44.059  1.00 137.67 ? 32  ILE B HB   1 
ATOM   2247 H HG12 . ILE B 1 32  ? 14.719 -0.564  41.608  1.00 133.27 ? 32  ILE B HG12 1 
ATOM   2248 H HG13 . ILE B 1 32  ? 13.669 0.194   42.529  1.00 133.27 ? 32  ILE B HG13 1 
ATOM   2249 H HG21 . ILE B 1 32  ? 15.882 -2.375  43.483  1.00 151.17 ? 32  ILE B HG21 1 
ATOM   2250 H HG22 . ILE B 1 32  ? 14.806 -3.540  43.577  1.00 151.17 ? 32  ILE B HG22 1 
ATOM   2251 H HG23 . ILE B 1 32  ? 15.260 -2.990  42.158  1.00 151.17 ? 32  ILE B HG23 1 
ATOM   2252 H HD11 . ILE B 1 32  ? 15.627 1.195   42.918  1.00 134.32 ? 32  ILE B HD11 1 
ATOM   2253 H HD12 . ILE B 1 32  ? 15.375 0.280   44.192  1.00 134.32 ? 32  ILE B HD12 1 
ATOM   2254 H HD13 . ILE B 1 32  ? 16.385 -0.194  43.061  1.00 134.32 ? 32  ILE B HD13 1 
ATOM   2255 N N    . LYS B 1 33  ? 11.576 -3.654  43.906  1.00 96.03  ? 33  LYS B N    1 
ATOM   2256 C CA   . LYS B 1 33  ? 11.008 -4.897  44.396  1.00 104.11 ? 33  LYS B CA   1 
ATOM   2257 C C    . LYS B 1 33  ? 10.135 -5.531  43.332  1.00 100.90 ? 33  LYS B C    1 
ATOM   2258 O O    . LYS B 1 33  ? 10.379 -6.663  42.905  1.00 103.18 ? 33  LYS B O    1 
ATOM   2259 C CB   . LYS B 1 33  ? 10.212 -4.597  45.674  1.00 110.80 ? 33  LYS B CB   1 
ATOM   2260 C CG   . LYS B 1 33  ? 9.224  -5.657  46.113  1.00 109.88 ? 33  LYS B CG   1 
ATOM   2261 C CD   . LYS B 1 33  ? 8.389  -5.117  47.266  1.00 116.31 ? 33  LYS B CD   1 
ATOM   2262 C CE   . LYS B 1 33  ? 7.235  -6.042  47.593  1.00 123.71 ? 33  LYS B CE   1 
ATOM   2263 N NZ   . LYS B 1 33  ? 7.716  -7.412  47.923  1.00 132.26 ? 33  LYS B NZ   1 
ATOM   2264 H H    . LYS B 1 33  ? 11.385 -2.966  44.386  1.00 115.32 ? 33  LYS B H    1 
ATOM   2265 H HA   . LYS B 1 33  ? 11.710 -5.529  44.614  1.00 125.01 ? 33  LYS B HA   1 
ATOM   2266 H HB2  . LYS B 1 33  ? 10.843 -4.477  46.401  1.00 133.04 ? 33  LYS B HB2  1 
ATOM   2267 H HB3  . LYS B 1 33  ? 9.710  -3.780  45.532  1.00 133.04 ? 33  LYS B HB3  1 
ATOM   2268 H HG2  . LYS B 1 33  ? 8.635  -5.883  45.377  1.00 131.93 ? 33  LYS B HG2  1 
ATOM   2269 H HG3  . LYS B 1 33  ? 9.699  -6.448  46.413  1.00 131.93 ? 33  LYS B HG3  1 
ATOM   2270 H HD2  . LYS B 1 33  ? 8.947  -5.033  48.055  1.00 139.65 ? 33  LYS B HD2  1 
ATOM   2271 H HD3  . LYS B 1 33  ? 8.027  -4.251  47.022  1.00 139.65 ? 33  LYS B HD3  1 
ATOM   2272 H HE2  . LYS B 1 33  ? 6.752  -5.695  48.359  1.00 148.53 ? 33  LYS B HE2  1 
ATOM   2273 H HE3  . LYS B 1 33  ? 6.643  -6.102  46.827  1.00 148.53 ? 33  LYS B HE3  1 
ATOM   2274 H HZ1  . LYS B 1 33  ? 7.026  -7.938  48.120  1.00 158.78 ? 33  LYS B HZ1  1 
ATOM   2275 H HZ2  . LYS B 1 33  ? 8.152  -7.757  47.228  1.00 158.78 ? 33  LYS B HZ2  1 
ATOM   2276 H HZ3  . LYS B 1 33  ? 8.265  -7.382  48.622  1.00 158.78 ? 33  LYS B HZ3  1 
ATOM   2277 N N    . GLN B 1 34  ? 9.155  -4.783  42.830  1.00 102.86 ? 34  GLN B N    1 
ATOM   2278 C CA   . GLN B 1 34  ? 8.215  -5.359  41.876  1.00 105.58 ? 34  GLN B CA   1 
ATOM   2279 C C    . GLN B 1 34  ? 8.907  -5.827  40.604  1.00 107.83 ? 34  GLN B C    1 
ATOM   2280 O O    . GLN B 1 34  ? 8.467  -6.806  39.986  1.00 105.79 ? 34  GLN B O    1 
ATOM   2281 C CB   . GLN B 1 34  ? 7.127  -4.347  41.518  1.00 99.06  ? 34  GLN B CB   1 
ATOM   2282 C CG   . GLN B 1 34  ? 6.194  -4.057  42.653  1.00 105.79 ? 34  GLN B CG   1 
ATOM   2283 C CD   . GLN B 1 34  ? 5.029  -3.204  42.236  1.00 104.92 ? 34  GLN B CD   1 
ATOM   2284 O OE1  . GLN B 1 34  ? 4.815  -2.962  41.054  1.00 108.10 ? 34  GLN B OE1  1 
ATOM   2285 N NE2  . GLN B 1 34  ? 4.262  -2.740  43.210  1.00 121.41 ? 34  GLN B NE2  1 
ATOM   2286 H H    . GLN B 1 34  ? 9.016  -3.956  43.022  1.00 123.51 ? 34  GLN B H    1 
ATOM   2287 H HA   . GLN B 1 34  ? 7.797  -6.126  42.299  1.00 126.77 ? 34  GLN B HA   1 
ATOM   2288 H HB2  . GLN B 1 34  ? 7.547  -3.513  41.257  1.00 118.95 ? 34  GLN B HB2  1 
ATOM   2289 H HB3  . GLN B 1 34  ? 6.601  -4.699  40.782  1.00 118.95 ? 34  GLN B HB3  1 
ATOM   2290 H HG2  . GLN B 1 34  ? 5.845  -4.894  42.999  1.00 127.03 ? 34  GLN B HG2  1 
ATOM   2291 H HG3  . GLN B 1 34  ? 6.678  -3.587  43.349  1.00 127.03 ? 34  GLN B HG3  1 
ATOM   2292 H HE21 . GLN B 1 34  ? 4.444  -2.932  44.029  1.00 145.77 ? 34  GLN B HE21 1 
ATOM   2293 H HE22 . GLN B 1 34  ? 3.583  -2.247  43.025  1.00 145.77 ? 34  GLN B HE22 1 
ATOM   2294 N N    . VAL B 1 35  ? 9.967  -5.136  40.178  1.00 106.09 ? 35  VAL B N    1 
ATOM   2295 C CA   . VAL B 1 35  ? 10.608 -5.502  38.912  1.00 107.72 ? 35  VAL B CA   1 
ATOM   2296 C C    . VAL B 1 35  ? 11.380 -6.810  39.045  1.00 110.47 ? 35  VAL B C    1 
ATOM   2297 O O    . VAL B 1 35  ? 11.308 -7.683  38.167  1.00 108.91 ? 35  VAL B O    1 
ATOM   2298 C CB   . VAL B 1 35  ? 11.513 -4.351  38.430  1.00 100.56 ? 35  VAL B CB   1 
ATOM   2299 C CG1  . VAL B 1 35  ? 12.511 -4.816  37.410  1.00 88.15  ? 35  VAL B CG1  1 
ATOM   2300 C CG2  . VAL B 1 35  ? 10.639 -3.238  37.869  1.00 108.28 ? 35  VAL B CG2  1 
ATOM   2301 H H    . VAL B 1 35  ? 10.324 -4.470  40.589  1.00 127.39 ? 35  VAL B H    1 
ATOM   2302 H HA   . VAL B 1 35  ? 9.915  -5.645  38.248  1.00 129.34 ? 35  VAL B HA   1 
ATOM   2303 H HB   . VAL B 1 35  ? 12.025 -4.013  39.181  1.00 120.76 ? 35  VAL B HB   1 
ATOM   2304 H HG11 . VAL B 1 35  ? 12.883 -4.043  36.957  1.00 105.86 ? 35  VAL B HG11 1 
ATOM   2305 H HG12 . VAL B 1 35  ? 13.217 -5.307  37.859  1.00 105.86 ? 35  VAL B HG12 1 
ATOM   2306 H HG13 . VAL B 1 35  ? 12.064 -5.391  36.769  1.00 105.86 ? 35  VAL B HG13 1 
ATOM   2307 H HG21 . VAL B 1 35  ? 11.206 -2.506  37.580  1.00 130.02 ? 35  VAL B HG21 1 
ATOM   2308 H HG22 . VAL B 1 35  ? 10.134 -3.582  37.116  1.00 130.02 ? 35  VAL B HG22 1 
ATOM   2309 H HG23 . VAL B 1 35  ? 10.032 -2.933  38.562  1.00 130.02 ? 35  VAL B HG23 1 
ATOM   2310 N N    . LYS B 1 36  ? 12.092 -6.988  40.155  1.00 107.03 ? 36  LYS B N    1 
ATOM   2311 C CA   . LYS B 1 36  ? 12.933 -8.170  40.305  1.00 112.54 ? 36  LYS B CA   1 
ATOM   2312 C C    . LYS B 1 36  ? 12.095 -9.437  40.519  1.00 112.86 ? 36  LYS B C    1 
ATOM   2313 O O    . LYS B 1 36  ? 12.533 -10.538 40.161  1.00 114.63 ? 36  LYS B O    1 
ATOM   2314 C CB   . LYS B 1 36  ? 13.929 -7.890  41.434  1.00 112.42 ? 36  LYS B CB   1 
ATOM   2315 C CG   . LYS B 1 36  ? 15.167 -8.764  41.426  1.00 112.56 ? 36  LYS B CG   1 
ATOM   2316 C CD   . LYS B 1 36  ? 16.019 -8.513  42.654  1.00 115.05 ? 36  LYS B CD   1 
ATOM   2317 C CE   . LYS B 1 36  ? 17.161 -9.527  42.779  1.00 115.89 ? 36  LYS B CE   1 
ATOM   2318 N NZ   . LYS B 1 36  ? 17.837 -9.454  44.136  1.00 121.95 ? 36  LYS B NZ   1 
ATOM   2319 H H    . LYS B 1 36  ? 12.105 -6.449  40.824  1.00 128.51 ? 36  LYS B H    1 
ATOM   2320 H HA   . LYS B 1 36  ? 13.449 -8.347  39.503  1.00 135.13 ? 36  LYS B HA   1 
ATOM   2321 H HB2  . LYS B 1 36  ? 14.223 -6.969  41.364  1.00 134.98 ? 36  LYS B HB2  1 
ATOM   2322 H HB3  . LYS B 1 36  ? 13.480 -8.031  42.282  1.00 134.98 ? 36  LYS B HB3  1 
ATOM   2323 H HG2  . LYS B 1 36  ? 14.903 -9.698  41.422  1.00 135.15 ? 36  LYS B HG2  1 
ATOM   2324 H HG3  . LYS B 1 36  ? 15.697 -8.566  40.639  1.00 135.15 ? 36  LYS B HG3  1 
ATOM   2325 H HD2  . LYS B 1 36  ? 16.407 -7.626  42.596  1.00 138.14 ? 36  LYS B HD2  1 
ATOM   2326 H HD3  . LYS B 1 36  ? 15.465 -8.581  43.447  1.00 138.14 ? 36  LYS B HD3  1 
ATOM   2327 H HE2  . LYS B 1 36  ? 16.806 -10.423 42.665  1.00 139.15 ? 36  LYS B HE2  1 
ATOM   2328 H HE3  . LYS B 1 36  ? 17.827 -9.344  42.098  1.00 139.15 ? 36  LYS B HE3  1 
ATOM   2329 H HZ1  . LYS B 1 36  ? 18.499 -10.047 44.178  1.00 146.41 ? 36  LYS B HZ1  1 
ATOM   2330 H HZ2  . LYS B 1 36  ? 18.171 -8.639  44.266  1.00 146.41 ? 36  LYS B HZ2  1 
ATOM   2331 H HZ3  . LYS B 1 36  ? 17.249 -9.632  44.779  1.00 146.41 ? 36  LYS B HZ3  1 
ATOM   2332 N N    . GLU B 1 37  ? 10.896 -9.312  41.092  1.00 108.27 ? 37  GLU B N    1 
ATOM   2333 C CA   . GLU B 1 37  ? 10.036 -10.477 41.292  1.00 108.88 ? 37  GLU B CA   1 
ATOM   2334 C C    . GLU B 1 37  ? 9.468  -10.970 39.966  1.00 112.02 ? 37  GLU B C    1 
ATOM   2335 O O    . GLU B 1 37  ? 9.345  -12.184 39.748  1.00 108.56 ? 37  GLU B O    1 
ATOM   2336 C CB   . GLU B 1 37  ? 8.886  -10.110 42.220  1.00 109.77 ? 37  GLU B CB   1 
ATOM   2337 C CG   . GLU B 1 37  ? 9.305  -9.718  43.606  1.00 115.97 ? 37  GLU B CG   1 
ATOM   2338 C CD   . GLU B 1 37  ? 8.135  -9.200  44.427  1.00 119.79 ? 37  GLU B CD   1 
ATOM   2339 O OE1  . GLU B 1 37  ? 7.062  -8.928  43.837  1.00 115.76 ? 37  GLU B OE1  1 
ATOM   2340 O OE2  . GLU B 1 37  ? 8.314  -8.983  45.640  1.00 120.66 ? 37  GLU B OE2  1 
ATOM   2341 H H    . GLU B 1 37  ? 10.560 -8.571  41.371  1.00 130.00 ? 37  GLU B H    1 
ATOM   2342 H HA   . GLU B 1 37  ? 10.560 -11.187 41.695  1.00 130.73 ? 37  GLU B HA   1 
ATOM   2343 H HB2  . GLU B 1 37  ? 8.406  -9.359  41.836  1.00 131.80 ? 37  GLU B HB2  1 
ATOM   2344 H HB3  . GLU B 1 37  ? 8.295  -10.875 42.299  1.00 131.80 ? 37  GLU B HB3  1 
ATOM   2345 H HG2  . GLU B 1 37  ? 9.675  -10.492 44.059  1.00 139.25 ? 37  GLU B HG2  1 
ATOM   2346 H HG3  . GLU B 1 37  ? 9.972  -9.015  43.552  1.00 139.25 ? 37  GLU B HG3  1 
ATOM   2347 N N    . ALA B 1 38  ? 9.073  -10.026 39.087  1.00 110.84 ? 38  ALA B N    1 
ATOM   2348 C CA   . ALA B 1 38  ? 8.500  -10.340 37.783  1.00 106.12 ? 38  ALA B CA   1 
ATOM   2349 C C    . ALA B 1 38  ? 9.556  -10.801 36.792  1.00 111.40 ? 38  ALA B C    1 
ATOM   2350 O O    . ALA B 1 38  ? 9.214  -11.476 35.818  1.00 106.61 ? 38  ALA B O    1 
ATOM   2351 C CB   . ALA B 1 38  ? 7.765  -9.127  37.198  1.00 104.40 ? 38  ALA B CB   1 
ATOM   2352 H H    . ALA B 1 38  ? 9.132  -9.181  39.234  1.00 133.09 ? 38  ALA B H    1 
ATOM   2353 H HA   . ALA B 1 38  ? 7.848  -11.048 37.902  1.00 127.42 ? 38  ALA B HA   1 
ATOM   2354 H HB1  . ALA B 1 38  ? 7.455  -9.346  36.305  1.00 125.36 ? 38  ALA B HB1  1 
ATOM   2355 H HB2  . ALA B 1 38  ? 7.009  -8.912  37.766  1.00 125.36 ? 38  ALA B HB2  1 
ATOM   2356 H HB3  . ALA B 1 38  ? 8.376  -8.375  37.161  1.00 125.36 ? 38  ALA B HB3  1 
ATOM   2357 N N    . SER B 1 39  ? 10.819 -10.449 37.017  1.00 115.20 ? 39  SER B N    1 
ATOM   2358 C CA   . SER B 1 39  ? 11.908 -10.933 36.191  1.00 123.70 ? 39  SER B CA   1 
ATOM   2359 C C    . SER B 1 39  ? 12.627 -12.098 36.839  1.00 125.12 ? 39  SER B C    1 
ATOM   2360 O O    . SER B 1 39  ? 13.661 -12.535 36.329  1.00 132.04 ? 39  SER B O    1 
ATOM   2361 C CB   . SER B 1 39  ? 12.903 -9.814  35.929  1.00 123.22 ? 39  SER B CB   1 
ATOM   2362 O OG   . SER B 1 39  ? 13.621 -9.522  37.104  1.00 118.93 ? 39  SER B OG   1 
ATOM   2363 H H    . SER B 1 39  ? 11.068 -9.924  37.651  1.00 138.31 ? 39  SER B H    1 
ATOM   2364 H HA   . SER B 1 39  ? 11.549 -11.221 35.337  1.00 148.52 ? 39  SER B HA   1 
ATOM   2365 H HB2  . SER B 1 39  ? 13.523 -10.094 35.238  1.00 147.94 ? 39  SER B HB2  1 
ATOM   2366 H HB3  . SER B 1 39  ? 12.424 -9.021  35.644  1.00 147.94 ? 39  SER B HB3  1 
ATOM   2367 H HG   . SER B 1 39  ? 14.211 -8.945  36.945  1.00 142.79 ? 39  SER B HG   1 
ATOM   2368 N N    . ASN B 1 40  ? 12.100 -12.614 37.948  1.00 106.23 ? 40  ASN B N    1 
ATOM   2369 C CA   . ASN B 1 40  ? 12.721 -13.740 38.633  1.00 120.36 ? 40  ASN B CA   1 
ATOM   2370 C C    . ASN B 1 40  ? 14.202 -13.480 38.854  1.00 122.08 ? 40  ASN B C    1 
ATOM   2371 O O    . ASN B 1 40  ? 15.021 -14.405 38.794  1.00 116.37 ? 40  ASN B O    1 
ATOM   2372 C CB   . ASN B 1 40  ? 12.496 -15.024 37.847  1.00 116.16 ? 40  ASN B CB   1 
ATOM   2373 C CG   . ASN B 1 40  ? 11.031 -15.327 37.670  1.00 119.02 ? 40  ASN B CG   1 
ATOM   2374 O OD1  . ASN B 1 40  ? 10.258 -15.260 38.629  1.00 118.73 ? 40  ASN B OD1  1 
ATOM   2375 N ND2  . ASN B 1 40  ? 10.632 -15.663 36.449  1.00 123.61 ? 40  ASN B ND2  1 
ATOM   2376 H H    . ASN B 1 40  ? 11.381 -12.327 38.323  1.00 127.55 ? 40  ASN B H    1 
ATOM   2377 H HA   . ASN B 1 40  ? 12.316 -13.853 39.507  1.00 144.51 ? 40  ASN B HA   1 
ATOM   2378 H HB2  . ASN B 1 40  ? 12.896 -14.935 36.968  1.00 139.47 ? 40  ASN B HB2  1 
ATOM   2379 H HB3  . ASN B 1 40  ? 12.903 -15.765 38.323  1.00 139.47 ? 40  ASN B HB3  1 
ATOM   2380 H HD21 . ASN B 1 40  ? 9.804  -15.844 36.301  1.00 148.41 ? 40  ASN B HD21 1 
ATOM   2381 H HD22 . ASN B 1 40  ? 11.201 -15.700 35.805  1.00 148.41 ? 40  ASN B HD22 1 
ATOM   2382 N N    . GLY B 1 41  ? 14.551 -12.207 39.079  1.00 121.71 ? 41  GLY B N    1 
ATOM   2383 C CA   . GLY B 1 41  ? 15.887 -11.812 39.465  1.00 120.77 ? 41  GLY B CA   1 
ATOM   2384 C C    . GLY B 1 41  ? 16.850 -11.423 38.352  1.00 113.84 ? 41  GLY B C    1 
ATOM   2385 O O    . GLY B 1 41  ? 17.947 -10.941 38.667  1.00 106.38 ? 41  GLY B O    1 
ATOM   2386 H H    . GLY B 1 41  ? 14.008 -11.544 39.010  1.00 146.13 ? 41  GLY B H    1 
ATOM   2387 H HA2  . GLY B 1 41  ? 15.815 -11.048 40.059  1.00 145.00 ? 41  GLY B HA2  1 
ATOM   2388 H HA3  . GLY B 1 41  ? 16.292 -12.550 39.947  1.00 145.00 ? 41  GLY B HA3  1 
ATOM   2389 N N    . GLU B 1 42  ? 16.494 -11.579 37.065  1.00 104.80 ? 42  GLU B N    1 
ATOM   2390 C CA   . GLU B 1 42  ? 17.498 -11.285 36.044  1.00 100.75 ? 42  GLU B CA   1 
ATOM   2391 C C    . GLU B 1 42  ? 17.885 -9.801  36.049  1.00 100.12 ? 42  GLU B C    1 
ATOM   2392 O O    . GLU B 1 42  ? 19.013 -9.460  35.663  1.00 101.91 ? 42  GLU B O    1 
ATOM   2393 C CB   . GLU B 1 42  ? 17.053 -11.647 34.613  1.00 104.43 ? 42  GLU B CB   1 
ATOM   2394 C CG   . GLU B 1 42  ? 17.014 -13.132 34.167  1.00 108.65 ? 42  GLU B CG   1 
ATOM   2395 C CD   . GLU B 1 42  ? 16.626 -13.295 32.651  1.00 108.82 ? 42  GLU B CD   1 
ATOM   2396 O OE1  . GLU B 1 42  ? 16.561 -12.295 31.911  1.00 100.91 ? 42  GLU B OE1  1 
ATOM   2397 O OE2  . GLU B 1 42  ? 16.390 -14.426 32.183  1.00 106.43 ? 42  GLU B OE2  1 
ATOM   2398 H H    . GLU B 1 42  ? 15.725 -11.838 36.781  1.00 125.83 ? 42  GLU B H    1 
ATOM   2399 H HA   . GLU B 1 42  ? 18.257 -11.848 36.260  1.00 120.98 ? 42  GLU B HA   1 
ATOM   2400 H HB2  . GLU B 1 42  ? 16.152 -11.307 34.497  1.00 125.39 ? 42  GLU B HB2  1 
ATOM   2401 H HB3  . GLU B 1 42  ? 17.658 -11.198 34.002  1.00 125.39 ? 42  GLU B HB3  1 
ATOM   2402 H HG2  . GLU B 1 42  ? 17.891 -13.525 34.297  1.00 130.46 ? 42  GLU B HG2  1 
ATOM   2403 H HG3  . GLU B 1 42  ? 16.356 -13.605 34.699  1.00 130.46 ? 42  GLU B HG3  1 
ATOM   2404 N N    . MET B 1 43  ? 16.951 -8.909  36.436  1.00 111.14 ? 43  MET B N    1 
ATOM   2405 C CA   . MET B 1 43  ? 17.106 -7.459  36.284  1.00 113.05 ? 43  MET B CA   1 
ATOM   2406 C C    . MET B 1 43  ? 16.936 -6.773  37.629  1.00 110.14 ? 43  MET B C    1 
ATOM   2407 O O    . MET B 1 43  ? 15.826 -6.722  38.172  1.00 109.44 ? 43  MET B O    1 
ATOM   2408 C CB   . MET B 1 43  ? 16.089 -6.891  35.304  1.00 117.17 ? 43  MET B CB   1 
ATOM   2409 C CG   . MET B 1 43  ? 16.274 -5.439  35.007  1.00 112.80 ? 43  MET B CG   1 
ATOM   2410 S SD   . MET B 1 43  ? 15.054 -5.002  33.768  1.00 93.18  ? 43  MET B SD   1 
ATOM   2411 C CE   . MET B 1 43  ? 15.561 -3.301  33.418  1.00 93.10  ? 43  MET B CE   1 
ATOM   2412 H H    . MET B 1 43  ? 16.203 -9.132  36.797  1.00 133.45 ? 43  MET B H    1 
ATOM   2413 H HA   . MET B 1 43  ? 18.004 -7.304  35.953  1.00 135.74 ? 43  MET B HA   1 
ATOM   2414 H HB2  . MET B 1 43  ? 16.162 -7.374  34.466  1.00 140.68 ? 43  MET B HB2  1 
ATOM   2415 H HB3  . MET B 1 43  ? 15.201 -7.005  35.676  1.00 140.68 ? 43  MET B HB3  1 
ATOM   2416 H HG2  . MET B 1 43  ? 16.129 -4.909  35.806  1.00 135.44 ? 43  MET B HG2  1 
ATOM   2417 H HG3  . MET B 1 43  ? 17.164 -5.275  34.657  1.00 135.44 ? 43  MET B HG3  1 
ATOM   2418 H HE1  . MET B 1 43  ? 15.288 -3.069  32.517  1.00 111.80 ? 43  MET B HE1  1 
ATOM   2419 H HE2  . MET B 1 43  ? 15.134 -2.707  34.056  1.00 111.80 ? 43  MET B HE2  1 
ATOM   2420 H HE3  . MET B 1 43  ? 16.525 -3.235  33.499  1.00 111.80 ? 43  MET B HE3  1 
ATOM   2421 N N    . GLU B 1 44  ? 18.028 -6.242  38.155  1.00 107.46 ? 44  GLU B N    1 
ATOM   2422 C CA   . GLU B 1 44  ? 18.060 -5.590  39.462  1.00 107.05 ? 44  GLU B CA   1 
ATOM   2423 C C    . GLU B 1 44  ? 18.487 -4.148  39.236  1.00 105.79 ? 44  GLU B C    1 
ATOM   2424 O O    . GLU B 1 44  ? 19.681 -3.863  39.116  1.00 109.54 ? 44  GLU B O    1 
ATOM   2425 C CB   . GLU B 1 44  ? 19.000 -6.341  40.388  1.00 94.87  ? 44  GLU B CB   1 
ATOM   2426 C CG   . GLU B 1 44  ? 18.730 -6.137  41.858  1.00 101.29 ? 44  GLU B CG   1 
ATOM   2427 C CD   . GLU B 1 44  ? 19.438 -7.165  42.726  1.00 105.00 ? 44  GLU B CD   1 
ATOM   2428 O OE1  . GLU B 1 44  ? 20.175 -8.021  42.156  1.00 99.58  ? 44  GLU B OE1  1 
ATOM   2429 O OE2  . GLU B 1 44  ? 19.224 -7.140  43.970  1.00 107.42 ? 44  GLU B OE2  1 
ATOM   2430 H H    . GLU B 1 44  ? 18.793 -6.245  37.762  1.00 129.03 ? 44  GLU B H    1 
ATOM   2431 H HA   . GLU B 1 44  ? 17.179 -5.577  39.869  1.00 128.54 ? 44  GLU B HA   1 
ATOM   2432 H HB2  . GLU B 1 44  ? 18.920 -7.290  40.205  1.00 113.92 ? 44  GLU B HB2  1 
ATOM   2433 H HB3  . GLU B 1 44  ? 19.907 -6.045  40.213  1.00 113.92 ? 44  GLU B HB3  1 
ATOM   2434 H HG2  . GLU B 1 44  ? 19.042 -5.256  42.119  1.00 121.63 ? 44  GLU B HG2  1 
ATOM   2435 H HG3  . GLU B 1 44  ? 17.776 -6.212  42.019  1.00 121.63 ? 44  GLU B HG3  1 
ATOM   2436 N N    . LEU B 1 45  ? 17.513 -3.244  39.207  1.00 119.75 ? 45  LEU B N    1 
ATOM   2437 C CA   . LEU B 1 45  ? 17.750 -1.849  38.879  1.00 122.30 ? 45  LEU B CA   1 
ATOM   2438 C C    . LEU B 1 45  ? 18.439 -1.156  40.043  1.00 117.71 ? 45  LEU B C    1 
ATOM   2439 O O    . LEU B 1 45  ? 18.285 -1.548  41.199  1.00 121.56 ? 45  LEU B O    1 
ATOM   2440 C CB   . LEU B 1 45  ? 16.421 -1.162  38.592  1.00 126.95 ? 45  LEU B CB   1 
ATOM   2441 C CG   . LEU B 1 45  ? 15.505 -1.818  37.564  1.00 121.78 ? 45  LEU B CG   1 
ATOM   2442 C CD1  . LEU B 1 45  ? 14.116 -1.232  37.649  1.00 138.09 ? 45  LEU B CD1  1 
ATOM   2443 C CD2  . LEU B 1 45  ? 16.048 -1.616  36.201  1.00 111.88 ? 45  LEU B CD2  1 
ATOM   2444 H H    . LEU B 1 45  ? 16.689 -3.419  39.377  1.00 143.78 ? 45  LEU B H    1 
ATOM   2445 H HA   . LEU B 1 45  ? 18.316 -1.779  38.095  1.00 146.83 ? 45  LEU B HA   1 
ATOM   2446 H HB2  . LEU B 1 45  ? 15.923 -1.115  39.423  1.00 152.42 ? 45  LEU B HB2  1 
ATOM   2447 H HB3  . LEU B 1 45  ? 16.612 -0.267  38.269  1.00 152.42 ? 45  LEU B HB3  1 
ATOM   2448 H HG   . LEU B 1 45  ? 15.452 -2.769  37.745  1.00 146.22 ? 45  LEU B HG   1 
ATOM   2449 H HD11 . LEU B 1 45  ? 13.563 -1.630  36.959  1.00 165.78 ? 45  LEU B HD11 1 
ATOM   2450 H HD12 . LEU B 1 45  ? 13.744 -1.428  38.524  1.00 165.78 ? 45  LEU B HD12 1 
ATOM   2451 H HD13 . LEU B 1 45  ? 14.169 -0.273  37.519  1.00 165.78 ? 45  LEU B HD13 1 
ATOM   2452 H HD21 . LEU B 1 45  ? 15.313 -1.463  35.587  1.00 134.34 ? 45  LEU B HD21 1 
ATOM   2453 H HD22 . LEU B 1 45  ? 16.640 -0.847  36.207  1.00 134.34 ? 45  LEU B HD22 1 
ATOM   2454 H HD23 . LEU B 1 45  ? 16.539 -2.409  35.936  1.00 134.34 ? 45  LEU B HD23 1 
ATOM   2455 N N    . ASN B 1 46  ? 19.172 -0.089  39.736  1.00 102.34 ? 46  ASN B N    1 
ATOM   2456 C CA   . ASN B 1 46  ? 19.911 0.677   40.739  1.00 103.66 ? 46  ASN B CA   1 
ATOM   2457 C C    . ASN B 1 46  ? 19.206 1.996   41.055  1.00 105.90 ? 46  ASN B C    1 
ATOM   2458 O O    . ASN B 1 46  ? 18.706 2.672   40.150  1.00 106.21 ? 46  ASN B O    1 
ATOM   2459 C CB   . ASN B 1 46  ? 21.338 0.923   40.216  1.00 100.92 ? 46  ASN B CB   1 
ATOM   2460 C CG   . ASN B 1 46  ? 22.240 1.641   41.221  1.00 102.04 ? 46  ASN B CG   1 
ATOM   2461 O OD1  . ASN B 1 46  ? 21.816 2.005   42.314  1.00 101.04 ? 46  ASN B OD1  1 
ATOM   2462 N ND2  . ASN B 1 46  ? 23.505 1.844   40.841  1.00 104.57 ? 46  ASN B ND2  1 
ATOM   2463 H H    . ASN B 1 46  ? 19.259 0.218   38.938  1.00 122.89 ? 46  ASN B H    1 
ATOM   2464 H HA   . ASN B 1 46  ? 19.952 0.192   41.578  1.00 124.47 ? 46  ASN B HA   1 
ATOM   2465 H HB2  . ASN B 1 46  ? 21.747 0.069   40.007  1.00 121.18 ? 46  ASN B HB2  1 
ATOM   2466 H HB3  . ASN B 1 46  ? 21.289 1.471   39.417  1.00 121.18 ? 46  ASN B HB3  1 
ATOM   2467 H HD21 . ASN B 1 46  ? 24.054 2.243   41.369  1.00 125.57 ? 46  ASN B HD21 1 
ATOM   2468 H HD22 . ASN B 1 46  ? 23.771 1.576   40.068  1.00 125.57 ? 46  ASN B HD22 1 
ATOM   2469 N N    . GLU B 1 47  ? 19.183 2.347   42.361  1.00 102.29 ? 47  GLU B N    1 
ATOM   2470 C CA   . GLU B 1 47  ? 18.536 3.576   42.837  1.00 97.84  ? 47  GLU B CA   1 
ATOM   2471 C C    . GLU B 1 47  ? 18.988 4.803   42.065  1.00 102.90 ? 47  GLU B C    1 
ATOM   2472 O O    . GLU B 1 47  ? 18.168 5.627   41.635  1.00 105.00 ? 47  GLU B O    1 
ATOM   2473 C CB   . GLU B 1 47  ? 18.823 3.831   44.316  1.00 99.01  ? 47  GLU B CB   1 
ATOM   2474 C CG   . GLU B 1 47  ? 17.682 3.469   45.257  1.00 99.11  ? 47  GLU B CG   1 
ATOM   2475 C CD   . GLU B 1 47  ? 17.842 4.012   46.693  1.00 99.91  ? 47  GLU B CD   1 
ATOM   2476 O OE1  . GLU B 1 47  ? 18.795 3.620   47.410  1.00 98.54  ? 47  GLU B OE1  1 
ATOM   2477 O OE2  . GLU B 1 47  ? 17.007 4.860   47.106  1.00 101.58 ? 47  GLU B OE2  1 
ATOM   2478 H H    . GLU B 1 47  ? 19.539 1.883   42.992  1.00 122.83 ? 47  GLU B H    1 
ATOM   2479 H HA   . GLU B 1 47  ? 17.584 3.436   42.713  1.00 117.48 ? 47  GLU B HA   1 
ATOM   2480 H HB2  . GLU B 1 47  ? 19.594 3.303   44.576  1.00 118.89 ? 47  GLU B HB2  1 
ATOM   2481 H HB3  . GLU B 1 47  ? 19.011 4.775   44.435  1.00 118.89 ? 47  GLU B HB3  1 
ATOM   2482 H HG2  . GLU B 1 47  ? 16.857 3.831   44.897  1.00 119.00 ? 47  GLU B HG2  1 
ATOM   2483 H HG3  . GLU B 1 47  ? 17.623 2.502   45.314  1.00 119.00 ? 47  GLU B HG3  1 
ATOM   2484 N N    . ALA B 1 48  ? 20.311 4.978   41.951  1.00 107.60 ? 48  ALA B N    1 
ATOM   2485 C CA   . ALA B 1 48  ? 20.854 6.165   41.297  1.00 106.17 ? 48  ALA B CA   1 
ATOM   2486 C C    . ALA B 1 48  ? 20.410 6.240   39.841  1.00 98.40  ? 48  ALA B C    1 
ATOM   2487 O O    . ALA B 1 48  ? 20.006 7.302   39.358  1.00 99.72  ? 48  ALA B O    1 
ATOM   2488 C CB   . ALA B 1 48  ? 22.380 6.148   41.386  1.00 106.17 ? 48  ALA B CB   1 
ATOM   2489 H H    . ALA B 1 48  ? 20.906 4.429   42.241  1.00 129.19 ? 48  ALA B H    1 
ATOM   2490 H HA   . ALA B 1 48  ? 20.529 6.956   41.755  1.00 127.48 ? 48  ALA B HA   1 
ATOM   2491 H HB1  . ALA B 1 48  ? 22.730 6.948   40.964  1.00 127.48 ? 48  ALA B HB1  1 
ATOM   2492 H HB2  . ALA B 1 48  ? 22.642 6.126   42.320  1.00 127.48 ? 48  ALA B HB2  1 
ATOM   2493 H HB3  . ALA B 1 48  ? 22.714 5.360   40.930  1.00 127.48 ? 48  ALA B HB3  1 
ATOM   2494 N N    . THR B 1 49  ? 20.430 5.117   39.143  1.00 113.50 ? 49  THR B N    1 
ATOM   2495 C CA   . THR B 1 49  ? 19.913 5.122   37.789  1.00 128.52 ? 49  THR B CA   1 
ATOM   2496 C C    . THR B 1 49  ? 18.415 5.390   37.786  1.00 119.08 ? 49  THR B C    1 
ATOM   2497 O O    . THR B 1 49  ? 17.912 6.127   36.936  1.00 123.63 ? 49  THR B O    1 
ATOM   2498 C CB   . THR B 1 49  ? 20.240 3.803   37.121  1.00 120.35 ? 49  THR B CB   1 
ATOM   2499 O OG1  . THR B 1 49  ? 21.517 3.352   37.567  1.00 123.31 ? 49  THR B OG1  1 
ATOM   2500 C CG2  . THR B 1 49  ? 20.300 4.026   35.641  1.00 99.65  ? 49  THR B CG2  1 
ATOM   2501 H H    . THR B 1 49  ? 20.728 4.360   39.422  1.00 136.28 ? 49  THR B H    1 
ATOM   2502 H HA   . THR B 1 49  ? 20.339 5.826   37.276  1.00 154.31 ? 49  THR B HA   1 
ATOM   2503 H HB   . THR B 1 49  ? 19.570 3.134   37.331  1.00 144.49 ? 49  THR B HB   1 
ATOM   2504 H HG1  . THR B 1 49  ? 21.656 2.570   37.295  1.00 148.05 ? 49  THR B HG1  1 
ATOM   2505 H HG21 . THR B 1 49  ? 20.463 3.185   35.185  1.00 119.65 ? 49  THR B HG21 1 
ATOM   2506 H HG22 . THR B 1 49  ? 19.461 4.396   35.327  1.00 119.65 ? 49  THR B HG22 1 
ATOM   2507 H HG23 . THR B 1 49  ? 21.017 4.644   35.427  1.00 119.65 ? 49  THR B HG23 1 
ATOM   2508 N N    . LEU B 1 50  ? 17.682 4.806   38.730  1.00 118.85 ? 50  LEU B N    1 
ATOM   2509 C CA   . LEU B 1 50  ? 16.236 5.027   38.791  1.00 112.78 ? 50  LEU B CA   1 
ATOM   2510 C C    . LEU B 1 50  ? 15.916 6.474   39.139  1.00 108.80 ? 50  LEU B C    1 
ATOM   2511 O O    . LEU B 1 50  ? 15.076 7.106   38.491  1.00 109.49 ? 50  LEU B O    1 
ATOM   2512 C CB   . LEU B 1 50  ? 15.623 4.068   39.809  1.00 105.27 ? 50  LEU B CB   1 
ATOM   2513 C CG   . LEU B 1 50  ? 14.147 3.739   39.662  1.00 99.23  ? 50  LEU B CG   1 
ATOM   2514 C CD1  . LEU B 1 50  ? 13.841 2.294   40.017  1.00 92.80  ? 50  LEU B CD1  1 
ATOM   2515 C CD2  . LEU B 1 50  ? 13.369 4.647   40.562  1.00 101.01 ? 50  LEU B CD2  1 
ATOM   2516 H H    . LEU B 1 50  ? 17.991 4.285   39.341  1.00 142.70 ? 50  LEU B H    1 
ATOM   2517 H HA   . LEU B 1 50  ? 15.844 4.843   37.923  1.00 135.42 ? 50  LEU B HA   1 
ATOM   2518 H HB2  . LEU B 1 50  ? 16.104 3.227   39.752  1.00 126.40 ? 50  LEU B HB2  1 
ATOM   2519 H HB3  . LEU B 1 50  ? 15.737 4.457   40.690  1.00 126.40 ? 50  LEU B HB3  1 
ATOM   2520 H HG   . LEU B 1 50  ? 13.888 3.864   38.735  1.00 119.16 ? 50  LEU B HG   1 
ATOM   2521 H HD11 . LEU B 1 50  ? 12.884 2.150   39.955  1.00 111.44 ? 50  LEU B HD11 1 
ATOM   2522 H HD12 . LEU B 1 50  ? 14.304 1.711   39.395  1.00 111.44 ? 50  LEU B HD12 1 
ATOM   2523 H HD13 . LEU B 1 50  ? 14.144 2.120   40.921  1.00 111.44 ? 50  LEU B HD13 1 
ATOM   2524 H HD21 . LEU B 1 50  ? 12.459 4.318   40.632  1.00 121.30 ? 50  LEU B HD21 1 
ATOM   2525 H HD22 . LEU B 1 50  ? 13.785 4.656   41.438  1.00 121.30 ? 50  LEU B HD22 1 
ATOM   2526 H HD23 . LEU B 1 50  ? 13.370 5.541   40.186  1.00 121.30 ? 50  LEU B HD23 1 
ATOM   2527 N N    . TYR B 1 51  ? 16.592 7.030   40.144  1.00 98.72  ? 51  TYR B N    1 
ATOM   2528 C CA   . TYR B 1 51  ? 16.330 8.420   40.501  1.00 99.79  ? 51  TYR B CA   1 
ATOM   2529 C C    . TYR B 1 51  ? 16.772 9.356   39.381  1.00 97.15  ? 51  TYR B C    1 
ATOM   2530 O O    . TYR B 1 51  ? 16.150 10.400  39.149  1.00 97.39  ? 51  TYR B O    1 
ATOM   2531 C CB   . TYR B 1 51  ? 17.063 8.808   41.776  1.00 101.00 ? 51  TYR B CB   1 
ATOM   2532 C CG   . TYR B 1 51  ? 16.533 8.221   43.051  1.00 103.35 ? 51  TYR B CG   1 
ATOM   2533 C CD1  . TYR B 1 51  ? 15.226 8.439   43.452  1.00 104.70 ? 51  TYR B CD1  1 
ATOM   2534 C CD2  . TYR B 1 51  ? 17.356 7.487   43.881  1.00 104.10 ? 51  TYR B CD2  1 
ATOM   2535 C CE1  . TYR B 1 51  ? 14.755 7.929   44.643  1.00 101.83 ? 51  TYR B CE1  1 
ATOM   2536 C CE2  . TYR B 1 51  ? 16.895 6.974   45.060  1.00 102.47 ? 51  TYR B CE2  1 
ATOM   2537 C CZ   . TYR B 1 51  ? 15.592 7.194   45.430  1.00 103.79 ? 51  TYR B CZ   1 
ATOM   2538 O OH   . TYR B 1 51  ? 15.155 6.673   46.625  1.00 110.28 ? 51  TYR B OH   1 
ATOM   2539 H H    . TYR B 1 51  ? 17.189 6.635   40.621  1.00 118.54 ? 51  TYR B H    1 
ATOM   2540 H HA   . TYR B 1 51  ? 15.376 8.510   40.655  1.00 119.83 ? 51  TYR B HA   1 
ATOM   2541 H HB2  . TYR B 1 51  ? 17.987 8.523   41.692  1.00 121.28 ? 51  TYR B HB2  1 
ATOM   2542 H HB3  . TYR B 1 51  ? 17.021 9.773   41.867  1.00 121.28 ? 51  TYR B HB3  1 
ATOM   2543 H HD1  . TYR B 1 51  ? 14.658 8.936   42.910  1.00 125.72 ? 51  TYR B HD1  1 
ATOM   2544 H HD2  . TYR B 1 51  ? 18.240 7.339   43.633  1.00 125.00 ? 51  TYR B HD2  1 
ATOM   2545 H HE1  . TYR B 1 51  ? 13.877 8.084   44.907  1.00 122.27 ? 51  TYR B HE1  1 
ATOM   2546 H HE2  . TYR B 1 51  ? 17.461 6.480   45.608  1.00 123.04 ? 51  TYR B HE2  1 
ATOM   2547 H HH   . TYR B 1 51  ? 15.774 6.241   46.994  1.00 132.41 ? 51  TYR B HH   1 
ATOM   2548 N N    . THR B 1 52  ? 17.891 9.034   38.740  1.00 110.46 ? 52  THR B N    1 
ATOM   2549 C CA   . THR B 1 52  ? 18.300 9.783   37.560  1.00 118.65 ? 52  THR B CA   1 
ATOM   2550 C C    . THR B 1 52  ? 17.202 9.769   36.511  1.00 119.01 ? 52  THR B C    1 
ATOM   2551 O O    . THR B 1 52  ? 16.796 10.816  36.003  1.00 117.79 ? 52  THR B O    1 
ATOM   2552 C CB   . THR B 1 52  ? 19.592 9.192   37.005  1.00 123.58 ? 52  THR B CB   1 
ATOM   2553 O OG1  . THR B 1 52  ? 20.625 9.349   37.985  1.00 134.38 ? 52  THR B OG1  1 
ATOM   2554 C CG2  . THR B 1 52  ? 19.984 9.857   35.706  1.00 107.41 ? 52  THR B CG2  1 
ATOM   2555 H H    . THR B 1 52  ? 18.423 8.397   38.964  1.00 132.62 ? 52  THR B H    1 
ATOM   2556 H HA   . THR B 1 52  ? 18.470 10.706  37.804  1.00 142.46 ? 52  THR B HA   1 
ATOM   2557 H HB   . THR B 1 52  ? 19.471 8.250   36.810  1.00 148.38 ? 52  THR B HB   1 
ATOM   2558 H HG1  . THR B 1 52  ? 20.422 8.930   38.685  1.00 161.33 ? 52  THR B HG1  1 
ATOM   2559 H HG21 . THR B 1 52  ? 20.893 9.613   35.470  1.00 128.97 ? 52  THR B HG21 1 
ATOM   2560 H HG22 . THR B 1 52  ? 19.387 9.574   34.996  1.00 128.97 ? 52  THR B HG22 1 
ATOM   2561 H HG23 . THR B 1 52  ? 19.930 10.821  35.798  1.00 128.97 ? 52  THR B HG23 1 
ATOM   2562 N N    . ILE B 1 53  ? 16.695 8.592   36.186  1.00 119.62 ? 53  ILE B N    1 
ATOM   2563 C CA   . ILE B 1 53  ? 15.700 8.487   35.131  1.00 120.30 ? 53  ILE B CA   1 
ATOM   2564 C C    . ILE B 1 53  ? 14.422 9.218   35.500  1.00 112.65 ? 53  ILE B C    1 
ATOM   2565 O O    . ILE B 1 53  ? 13.848 9.940   34.679  1.00 110.10 ? 53  ILE B O    1 
ATOM   2566 C CB   . ILE B 1 53  ? 15.428 7.009   34.830  1.00 120.97 ? 53  ILE B CB   1 
ATOM   2567 C CG1  . ILE B 1 53  ? 16.681 6.368   34.268  1.00 122.67 ? 53  ILE B CG1  1 
ATOM   2568 C CG2  . ILE B 1 53  ? 14.271 6.900   33.897  1.00 112.88 ? 53  ILE B CG2  1 
ATOM   2569 C CD1  . ILE B 1 53  ? 16.610 4.874   34.298  1.00 127.29 ? 53  ILE B CD1  1 
ATOM   2570 H H    . ILE B 1 53  ? 16.906 7.845   36.557  1.00 143.62 ? 53  ILE B H    1 
ATOM   2571 H HA   . ILE B 1 53  ? 16.055 8.913   34.335  1.00 144.44 ? 53  ILE B HA   1 
ATOM   2572 H HB   . ILE B 1 53  ? 15.198 6.535   35.644  1.00 145.24 ? 53  ILE B HB   1 
ATOM   2573 H HG12 . ILE B 1 53  ? 16.795 6.647   33.346  1.00 147.28 ? 53  ILE B HG12 1 
ATOM   2574 H HG13 . ILE B 1 53  ? 17.445 6.646   34.796  1.00 147.28 ? 53  ILE B HG13 1 
ATOM   2575 H HG21 . ILE B 1 53  ? 14.261 6.012   33.508  1.00 135.53 ? 53  ILE B HG21 1 
ATOM   2576 H HG22 . ILE B 1 53  ? 13.451 7.053   34.392  1.00 135.53 ? 53  ILE B HG22 1 
ATOM   2577 H HG23 . ILE B 1 53  ? 14.365 7.567   33.198  1.00 135.53 ? 53  ILE B HG23 1 
ATOM   2578 H HD11 . ILE B 1 53  ? 17.491 4.512   34.114  1.00 152.82 ? 53  ILE B HD11 1 
ATOM   2579 H HD12 . ILE B 1 53  ? 16.313 4.589   35.177  1.00 152.82 ? 53  ILE B HD12 1 
ATOM   2580 H HD13 . ILE B 1 53  ? 15.981 4.574   33.623  1.00 152.82 ? 53  ILE B HD13 1 
ATOM   2581 N N    . PHE B 1 54  ? 13.951 9.044   36.739  1.00 112.93 ? 54  PHE B N    1 
ATOM   2582 C CA   . PHE B 1 54  ? 12.663 9.619   37.106  1.00 104.55 ? 54  PHE B CA   1 
ATOM   2583 C C    . PHE B 1 54  ? 12.696 11.136  37.070  1.00 102.94 ? 54  PHE B C    1 
ATOM   2584 O O    . PHE B 1 54  ? 11.653 11.785  36.904  1.00 101.16 ? 54  PHE B O    1 
ATOM   2585 C CB   . PHE B 1 54  ? 12.253 9.202   38.507  1.00 99.90  ? 54  PHE B CB   1 
ATOM   2586 C CG   . PHE B 1 54  ? 11.664 7.836   38.598  1.00 99.03  ? 54  PHE B CG   1 
ATOM   2587 C CD1  . PHE B 1 54  ? 11.542 7.021   37.493  1.00 103.18 ? 54  PHE B CD1  1 
ATOM   2588 C CD2  . PHE B 1 54  ? 11.177 7.382   39.805  1.00 99.16  ? 54  PHE B CD2  1 
ATOM   2589 C CE1  . PHE B 1 54  ? 10.970 5.756   37.605  1.00 99.00  ? 54  PHE B CE1  1 
ATOM   2590 C CE2  . PHE B 1 54  ? 10.596 6.139   39.923  1.00 99.18  ? 54  PHE B CE2  1 
ATOM   2591 C CZ   . PHE B 1 54  ? 10.493 5.325   38.837  1.00 98.49  ? 54  PHE B CZ   1 
ATOM   2592 H H    . PHE B 1 54  ? 14.348 8.610   37.365  1.00 135.59 ? 54  PHE B H    1 
ATOM   2593 H HA   . PHE B 1 54  ? 12.012 9.282   36.471  1.00 125.54 ? 54  PHE B HA   1 
ATOM   2594 H HB2  . PHE B 1 54  ? 13.037 9.221   39.077  1.00 119.96 ? 54  PHE B HB2  1 
ATOM   2595 H HB3  . PHE B 1 54  ? 11.589 9.829   38.834  1.00 119.96 ? 54  PHE B HB3  1 
ATOM   2596 H HD1  . PHE B 1 54  ? 11.844 7.318   36.665  1.00 123.90 ? 54  PHE B HD1  1 
ATOM   2597 H HD2  . PHE B 1 54  ? 11.241 7.927   40.556  1.00 119.07 ? 54  PHE B HD2  1 
ATOM   2598 H HE1  . PHE B 1 54  ? 10.907 5.204   36.860  1.00 118.88 ? 54  PHE B HE1  1 
ATOM   2599 H HE2  . PHE B 1 54  ? 10.274 5.854   40.747  1.00 119.09 ? 54  PHE B HE2  1 
ATOM   2600 H HZ   . PHE B 1 54  ? 10.105 4.484   38.918  1.00 118.26 ? 54  PHE B HZ   1 
ATOM   2601 N N    . LYS B 1 55  ? 13.876 11.719  37.278  1.00 103.97 ? 55  LYS B N    1 
ATOM   2602 C CA   . LYS B 1 55  ? 14.003 13.175  37.218  1.00 101.45 ? 55  LYS B CA   1 
ATOM   2603 C C    . LYS B 1 55  ? 13.661 13.683  35.815  1.00 102.15 ? 55  LYS B C    1 
ATOM   2604 O O    . LYS B 1 55  ? 12.908 14.656  35.665  1.00 98.89  ? 55  LYS B O    1 
ATOM   2605 C CB   . LYS B 1 55  ? 15.409 13.555  37.687  1.00 101.00 ? 55  LYS B CB   1 
ATOM   2606 C CG   . LYS B 1 55  ? 15.608 15.026  38.018  1.00 105.54 ? 55  LYS B CG   1 
ATOM   2607 C CD   . LYS B 1 55  ? 17.068 15.293  38.375  1.00 106.19 ? 55  LYS B CD   1 
ATOM   2608 C CE   . LYS B 1 55  ? 17.253 16.737  38.745  1.00 103.38 ? 55  LYS B CE   1 
ATOM   2609 N NZ   . LYS B 1 55  ? 16.398 17.071  39.918  1.00 104.32 ? 55  LYS B NZ   1 
ATOM   2610 H H    . LYS B 1 55  ? 14.607 11.302  37.454  1.00 124.84 ? 55  LYS B H    1 
ATOM   2611 H HA   . LYS B 1 55  ? 13.381 13.616  37.817  1.00 121.81 ? 55  LYS B HA   1 
ATOM   2612 H HB2  . LYS B 1 55  ? 15.612 13.047  38.488  1.00 121.28 ? 55  LYS B HB2  1 
ATOM   2613 H HB3  . LYS B 1 55  ? 16.038 13.329  36.983  1.00 121.28 ? 55  LYS B HB3  1 
ATOM   2614 H HG2  . LYS B 1 55  ? 15.373 15.569  37.249  1.00 126.72 ? 55  LYS B HG2  1 
ATOM   2615 H HG3  . LYS B 1 55  ? 15.054 15.268  38.777  1.00 126.72 ? 55  LYS B HG3  1 
ATOM   2616 H HD2  . LYS B 1 55  ? 17.325 14.743  39.132  1.00 127.51 ? 55  LYS B HD2  1 
ATOM   2617 H HD3  . LYS B 1 55  ? 17.633 15.092  37.613  1.00 127.51 ? 55  LYS B HD3  1 
ATOM   2618 H HE2  . LYS B 1 55  ? 18.181 16.899  38.979  1.00 124.13 ? 55  LYS B HE2  1 
ATOM   2619 H HE3  . LYS B 1 55  ? 16.996 17.302  38.000  1.00 124.13 ? 55  LYS B HE3  1 
ATOM   2620 H HZ1  . LYS B 1 55  ? 16.584 17.892  40.207  1.00 125.27 ? 55  LYS B HZ1  1 
ATOM   2621 H HZ2  . LYS B 1 55  ? 15.539 17.035  39.688  1.00 125.27 ? 55  LYS B HZ2  1 
ATOM   2622 H HZ3  . LYS B 1 55  ? 16.545 16.493  40.578  1.00 125.27 ? 55  LYS B HZ3  1 
ATOM   2623 N N    . ARG B 1 56  ? 14.151 12.996  34.772  1.00 103.30 ? 56  ARG B N    1 
ATOM   2624 C CA   . ARG B 1 56  ? 13.844 13.406  33.403  1.00 104.30 ? 56  ARG B CA   1 
ATOM   2625 C C    . ARG B 1 56  ? 12.351 13.282  33.128  1.00 104.91 ? 56  ARG B C    1 
ATOM   2626 O O    . ARG B 1 56  ? 11.750 14.155  32.485  1.00 104.38 ? 56  ARG B O    1 
ATOM   2627 C CB   . ARG B 1 56  ? 14.649 12.561  32.401  1.00 110.50 ? 56  ARG B CB   1 
ATOM   2628 C CG   . ARG B 1 56  ? 14.190 12.666  30.931  1.00 102.01 ? 56  ARG B CG   1 
ATOM   2629 C CD   . ARG B 1 56  ? 14.461 14.048  30.306  1.00 101.32 ? 56  ARG B CD   1 
ATOM   2630 N NE   . ARG B 1 56  ? 13.713 14.279  29.065  1.00 103.74 ? 56  ARG B NE   1 
ATOM   2631 C CZ   . ARG B 1 56  ? 14.152 14.021  27.832  1.00 108.99 ? 56  ARG B CZ   1 
ATOM   2632 N NH1  . ARG B 1 56  ? 15.342 13.477  27.609  1.00 100.53 ? 56  ARG B NH1  1 
ATOM   2633 N NH2  . ARG B 1 56  ? 13.369 14.309  26.794  1.00 104.26 ? 56  ARG B NH2  1 
ATOM   2634 H H    . ARG B 1 56  ? 14.655 12.301  34.833  1.00 124.03 ? 56  ARG B H    1 
ATOM   2635 H HA   . ARG B 1 56  ? 14.104 14.333  33.283  1.00 125.24 ? 56  ARG B HA   1 
ATOM   2636 H HB2  . ARG B 1 56  ? 15.576 12.846  32.436  1.00 132.68 ? 56  ARG B HB2  1 
ATOM   2637 H HB3  . ARG B 1 56  ? 14.578 11.629  32.660  1.00 132.68 ? 56  ARG B HB3  1 
ATOM   2638 H HG2  . ARG B 1 56  ? 14.665 12.004  30.406  1.00 122.49 ? 56  ARG B HG2  1 
ATOM   2639 H HG3  . ARG B 1 56  ? 13.235 12.502  30.888  1.00 122.49 ? 56  ARG B HG3  1 
ATOM   2640 H HD2  . ARG B 1 56  ? 14.205 14.735  30.940  1.00 121.66 ? 56  ARG B HD2  1 
ATOM   2641 H HD3  . ARG B 1 56  ? 15.406 14.120  30.101  1.00 121.66 ? 56  ARG B HD3  1 
ATOM   2642 H HE   . ARG B 1 56  ? 12.923 14.609  29.139  1.00 124.57 ? 56  ARG B HE   1 
ATOM   2643 H HH11 . ARG B 1 56  ? 15.855 13.280  28.271  1.00 120.72 ? 56  ARG B HH11 1 
ATOM   2644 H HH12 . ARG B 1 56  ? 15.600 13.322  26.804  1.00 120.72 ? 56  ARG B HH12 1 
ATOM   2645 H HH21 . ARG B 1 56  ? 12.593 14.655  26.925  1.00 125.19 ? 56  ARG B HH21 1 
ATOM   2646 H HH22 . ARG B 1 56  ? 13.639 14.148  25.994  1.00 125.19 ? 56  ARG B HH22 1 
ATOM   2647 N N    . LEU B 1 57  ? 11.742 12.187  33.579  1.00 102.90 ? 57  LEU B N    1 
ATOM   2648 C CA   . LEU B 1 57  ? 10.310 12.006  33.379  1.00 105.93 ? 57  LEU B CA   1 
ATOM   2649 C C    . LEU B 1 57  ? 9.485  13.061  34.109  1.00 109.34 ? 57  LEU B C    1 
ATOM   2650 O O    . LEU B 1 57  ? 8.498  13.558  33.557  1.00 112.94 ? 57  LEU B O    1 
ATOM   2651 C CB   . LEU B 1 57  ? 9.894  10.604  33.807  1.00 103.53 ? 57  LEU B CB   1 
ATOM   2652 C CG   . LEU B 1 57  ? 10.544 9.511   32.968  1.00 99.14  ? 57  LEU B CG   1 
ATOM   2653 C CD1  . LEU B 1 57  ? 10.153 8.144   33.462  1.00 99.53  ? 57  LEU B CD1  1 
ATOM   2654 C CD2  . LEU B 1 57  ? 10.153 9.639   31.521  1.00 87.06  ? 57  LEU B CD2  1 
ATOM   2655 H H    . LEU B 1 57  ? 12.130 11.544  33.998  1.00 123.55 ? 57  LEU B H    1 
ATOM   2656 H HA   . LEU B 1 57  ? 10.123 12.101  32.432  1.00 127.19 ? 57  LEU B HA   1 
ATOM   2657 H HB2  . LEU B 1 57  ? 10.155 10.467  34.732  1.00 124.32 ? 57  LEU B HB2  1 
ATOM   2658 H HB3  . LEU B 1 57  ? 8.932  10.520  33.718  1.00 124.32 ? 57  LEU B HB3  1 
ATOM   2659 H HG   . LEU B 1 57  ? 11.505 9.611   33.046  1.00 119.04 ? 57  LEU B HG   1 
ATOM   2660 H HD11 . LEU B 1 57  ? 10.615 7.473   32.935  1.00 119.52 ? 57  LEU B HD11 1 
ATOM   2661 H HD12 . LEU B 1 57  ? 10.404 8.061   34.395  1.00 119.52 ? 57  LEU B HD12 1 
ATOM   2662 H HD13 . LEU B 1 57  ? 9.193  8.036   33.367  1.00 119.52 ? 57  LEU B HD13 1 
ATOM   2663 H HD21 . LEU B 1 57  ? 10.335 8.800   31.069  1.00 104.54 ? 57  LEU B HD21 1 
ATOM   2664 H HD22 . LEU B 1 57  ? 9.207  9.845   31.466  1.00 104.54 ? 57  LEU B HD22 1 
ATOM   2665 H HD23 . LEU B 1 57  ? 10.671 10.352  31.115  1.00 104.54 ? 57  LEU B HD23 1 
ATOM   2666 N N    . GLU B 1 58  ? 9.823  13.391  35.361  1.00 104.79 ? 58  GLU B N    1 
ATOM   2667 C CA   . GLU B 1 58  ? 9.087  14.484  35.996  1.00 113.86 ? 58  GLU B CA   1 
ATOM   2668 C C    . GLU B 1 58  ? 9.281  15.779  35.211  1.00 110.40 ? 58  GLU B C    1 
ATOM   2669 O O    . GLU B 1 58  ? 8.331  16.537  34.979  1.00 110.28 ? 58  GLU B O    1 
ATOM   2670 C CB   . GLU B 1 58  ? 9.497  14.698  37.463  1.00 118.50 ? 58  GLU B CB   1 
ATOM   2671 C CG   . GLU B 1 58  ? 8.373  15.449  38.256  1.00 119.51 ? 58  GLU B CG   1 
ATOM   2672 C CD   . GLU B 1 58  ? 8.584  15.629  39.781  1.00 112.38 ? 58  GLU B CD   1 
ATOM   2673 O OE1  . GLU B 1 58  ? 9.431  14.942  40.402  1.00 98.07  ? 58  GLU B OE1  1 
ATOM   2674 O OE2  . GLU B 1 58  ? 7.902  16.535  40.329  1.00 98.29  ? 58  GLU B OE2  1 
ATOM   2675 H H    . GLU B 1 58  ? 10.437 13.019  35.834  1.00 125.82 ? 58  GLU B H    1 
ATOM   2676 H HA   . GLU B 1 58  ? 8.149  14.235  36.006  1.00 136.71 ? 58  GLU B HA   1 
ATOM   2677 H HB2  . GLU B 1 58  ? 9.650  13.838  37.884  1.00 142.28 ? 58  GLU B HB2  1 
ATOM   2678 H HB3  . GLU B 1 58  ? 10.307 15.232  37.496  1.00 142.28 ? 58  GLU B HB3  1 
ATOM   2679 H HG2  . GLU B 1 58  ? 8.282  16.338  37.877  1.00 143.49 ? 58  GLU B HG2  1 
ATOM   2680 H HG3  . GLU B 1 58  ? 7.546  14.954  38.143  1.00 143.49 ? 58  GLU B HG3  1 
ATOM   2681 N N    . LYS B 1 59  ? 10.517 16.033  34.777  1.00 99.61  ? 59  LYS B N    1 
ATOM   2682 C CA   . LYS B 1 59  ? 10.827 17.255  34.038  1.00 102.74 ? 59  LYS B CA   1 
ATOM   2683 C C    . LYS B 1 59  ? 10.004 17.349  32.758  1.00 96.52  ? 59  LYS B C    1 
ATOM   2684 O O    . LYS B 1 59  ? 9.534  18.432  32.399  1.00 97.57  ? 59  LYS B O    1 
ATOM   2685 C CB   . LYS B 1 59  ? 12.335 17.286  33.768  1.00 105.25 ? 59  LYS B CB   1 
ATOM   2686 C CG   . LYS B 1 59  ? 12.840 18.376  32.853  1.00 103.07 ? 59  LYS B CG   1 
ATOM   2687 C CD   . LYS B 1 59  ? 14.275 18.792  33.232  1.00 103.59 ? 59  LYS B CD   1 
ATOM   2688 C CE   . LYS B 1 59  ? 15.259 17.632  33.296  1.00 103.74 ? 59  LYS B CE   1 
ATOM   2689 N NZ   . LYS B 1 59  ? 15.419 16.894  32.019  1.00 106.72 ? 59  LYS B NZ   1 
ATOM   2690 H H    . LYS B 1 59  ? 11.193 15.515  34.897  1.00 119.61 ? 59  LYS B H    1 
ATOM   2691 H HA   . LYS B 1 59  ? 10.601 18.040  34.562  1.00 123.36 ? 59  LYS B HA   1 
ATOM   2692 H HB2  . LYS B 1 59  ? 12.790 17.397  34.618  1.00 126.37 ? 59  LYS B HB2  1 
ATOM   2693 H HB3  . LYS B 1 59  ? 12.586 16.440  33.366  1.00 126.37 ? 59  LYS B HB3  1 
ATOM   2694 H HG2  . LYS B 1 59  ? 12.845 18.054  31.938  1.00 123.76 ? 59  LYS B HG2  1 
ATOM   2695 H HG3  . LYS B 1 59  ? 12.265 19.154  32.928  1.00 123.76 ? 59  LYS B HG3  1 
ATOM   2696 H HD2  . LYS B 1 59  ? 14.603 19.420  32.569  1.00 124.39 ? 59  LYS B HD2  1 
ATOM   2697 H HD3  . LYS B 1 59  ? 14.257 19.212  34.106  1.00 124.39 ? 59  LYS B HD3  1 
ATOM   2698 H HE2  . LYS B 1 59  ? 16.131 17.978  33.546  1.00 124.57 ? 59  LYS B HE2  1 
ATOM   2699 H HE3  . LYS B 1 59  ? 14.950 17.000  33.964  1.00 124.57 ? 59  LYS B HE3  1 
ATOM   2700 H HZ1  . LYS B 1 59  ? 15.866 16.138  32.158  1.00 128.14 ? 59  LYS B HZ1  1 
ATOM   2701 H HZ2  . LYS B 1 59  ? 14.620 16.699  31.678  1.00 128.14 ? 59  LYS B HZ2  1 
ATOM   2702 H HZ3  . LYS B 1 59  ? 15.868 17.392  31.434  1.00 128.14 ? 59  LYS B HZ3  1 
ATOM   2703 N N    . ASP B 1 60  ? 9.799  16.236  32.077  1.00 102.52 ? 60  ASP B N    1 
ATOM   2704 C CA   . ASP B 1 60  ? 8.942  16.192  30.907  1.00 110.49 ? 60  ASP B CA   1 
ATOM   2705 C C    . ASP B 1 60  ? 7.465  16.026  31.220  1.00 114.76 ? 60  ASP B C    1 
ATOM   2706 O O    . ASP B 1 60  ? 6.689  15.806  30.291  1.00 117.43 ? 60  ASP B O    1 
ATOM   2707 C CB   . ASP B 1 60  ? 9.410  15.078  29.986  1.00 106.82 ? 60  ASP B CB   1 
ATOM   2708 C CG   . ASP B 1 60  ? 10.780 15.327  29.496  1.00 107.05 ? 60  ASP B CG   1 
ATOM   2709 O OD1  . ASP B 1 60  ? 11.310 16.390  29.852  1.00 109.62 ? 60  ASP B OD1  1 
ATOM   2710 O OD2  . ASP B 1 60  ? 11.313 14.519  28.718  1.00 106.78 ? 60  ASP B OD2  1 
ATOM   2711 H H    . ASP B 1 60  ? 10.152 15.478  32.277  1.00 123.11 ? 60  ASP B H    1 
ATOM   2712 H HA   . ASP B 1 60  ? 9.026  17.038  30.439  1.00 132.67 ? 60  ASP B HA   1 
ATOM   2713 H HB2  . ASP B 1 60  ? 9.406  14.237  30.471  1.00 128.26 ? 60  ASP B HB2  1 
ATOM   2714 H HB3  . ASP B 1 60  ? 8.816  15.022  29.221  1.00 128.26 ? 60  ASP B HB3  1 
ATOM   2715 N N    . GLY B 1 61  ? 7.058  16.063  32.485  1.00 117.30 ? 61  GLY B N    1 
ATOM   2716 C CA   . GLY B 1 61  ? 5.647  16.023  32.822  1.00 115.10 ? 61  GLY B CA   1 
ATOM   2717 C C    . GLY B 1 61  ? 4.943  14.727  32.514  1.00 109.55 ? 61  GLY B C    1 
ATOM   2718 O O    . GLY B 1 61  ? 3.715  14.693  32.428  1.00 107.42 ? 61  GLY B O    1 
ATOM   2719 H H    . GLY B 1 61  ? 7.582  16.112  33.165  1.00 140.83 ? 61  GLY B H    1 
ATOM   2720 H HA2  . GLY B 1 61  ? 5.553  16.188  33.774  1.00 138.19 ? 61  GLY B HA2  1 
ATOM   2721 H HA3  . GLY B 1 61  ? 5.193  16.727  32.333  1.00 138.19 ? 61  GLY B HA3  1 
ATOM   2722 N N    . ILE B 1 62  ? 5.684  13.646  32.364  1.00 112.11 ? 62  ILE B N    1 
ATOM   2723 C CA   . ILE B 1 62  ? 5.057  12.356  32.113  1.00 114.18 ? 62  ILE B CA   1 
ATOM   2724 C C    . ILE B 1 62  ? 4.721  11.688  33.441  1.00 107.31 ? 62  ILE B C    1 
ATOM   2725 O O    . ILE B 1 62  ? 3.757  10.922  33.528  1.00 102.37 ? 62  ILE B O    1 
ATOM   2726 C CB   . ILE B 1 62  ? 5.964  11.476  31.224  1.00 110.67 ? 62  ILE B CB   1 
ATOM   2727 C CG1  . ILE B 1 62  ? 5.905  11.927  29.739  1.00 111.70 ? 62  ILE B CG1  1 
ATOM   2728 C CG2  . ILE B 1 62  ? 5.567  10.028  31.325  1.00 107.40 ? 62  ILE B CG2  1 
ATOM   2729 C CD1  . ILE B 1 62  ? 7.072  11.449  28.885  1.00 90.89  ? 62  ILE B CD1  1 
ATOM   2730 H H    . ILE B 1 62  ? 6.543  13.628  32.403  1.00 134.61 ? 62  ILE B H    1 
ATOM   2731 H HA   . ILE B 1 62  ? 4.232  12.471  31.615  1.00 137.10 ? 62  ILE B HA   1 
ATOM   2732 H HB   . ILE B 1 62  ? 6.872  11.583  31.546  1.00 132.89 ? 62  ILE B HB   1 
ATOM   2733 H HG12 . ILE B 1 62  ? 5.091  11.579  29.343  1.00 134.11 ? 62  ILE B HG12 1 
ATOM   2734 H HG13 . ILE B 1 62  ? 5.900  12.896  29.712  1.00 134.11 ? 62  ILE B HG13 1 
ATOM   2735 H HG21 . ILE B 1 62  ? 5.978  9.537   30.597  1.00 128.96 ? 62  ILE B HG21 1 
ATOM   2736 H HG22 . ILE B 1 62  ? 5.871  9.676   32.176  1.00 128.96 ? 62  ILE B HG22 1 
ATOM   2737 H HG23 . ILE B 1 62  ? 4.601  9.961   31.266  1.00 128.96 ? 62  ILE B HG23 1 
ATOM   2738 H HD11 . ILE B 1 62  ? 7.000  11.847  28.003  1.00 109.15 ? 62  ILE B HD11 1 
ATOM   2739 H HD12 . ILE B 1 62  ? 7.903  11.722  29.304  1.00 109.15 ? 62  ILE B HD12 1 
ATOM   2740 H HD13 . ILE B 1 62  ? 7.038  10.483  28.815  1.00 109.15 ? 62  ILE B HD13 1 
ATOM   2741 N N    . ILE B 1 63  ? 5.460  12.008  34.499  1.00 107.34 ? 63  ILE B N    1 
ATOM   2742 C CA   . ILE B 1 63  ? 5.103  11.593  35.843  1.00 108.19 ? 63  ILE B CA   1 
ATOM   2743 C C    . ILE B 1 63  ? 5.246  12.792  36.775  1.00 101.90 ? 63  ILE B C    1 
ATOM   2744 O O    . ILE B 1 63  ? 5.822  13.823  36.438  1.00 102.73 ? 63  ILE B O    1 
ATOM   2745 C CB   . ILE B 1 63  ? 5.963  10.415  36.355  1.00 106.14 ? 63  ILE B CB   1 
ATOM   2746 C CG1  . ILE B 1 63  ? 7.370  10.906  36.675  1.00 104.83 ? 63  ILE B CG1  1 
ATOM   2747 C CG2  . ILE B 1 63  ? 5.965  9.275   35.346  1.00 100.35 ? 63  ILE B CG2  1 
ATOM   2748 C CD1  . ILE B 1 63  ? 8.262  9.856   37.321  1.00 101.59 ? 63  ILE B CD1  1 
ATOM   2749 H H    . ILE B 1 63  ? 6.183  12.472  34.458  1.00 128.89 ? 63  ILE B H    1 
ATOM   2750 H HA   . ILE B 1 63  ? 4.175  11.310  35.841  1.00 129.91 ? 63  ILE B HA   1 
ATOM   2751 H HB   . ILE B 1 63  ? 5.577  10.067  37.175  1.00 127.44 ? 63  ILE B HB   1 
ATOM   2752 H HG12 . ILE B 1 63  ? 7.796  11.187  35.849  1.00 125.88 ? 63  ILE B HG12 1 
ATOM   2753 H HG13 . ILE B 1 63  ? 7.306  11.656  37.287  1.00 125.88 ? 63  ILE B HG13 1 
ATOM   2754 H HG21 . ILE B 1 63  ? 6.429  8.515   35.729  1.00 120.50 ? 63  ILE B HG21 1 
ATOM   2755 H HG22 . ILE B 1 63  ? 5.048  9.034   35.140  1.00 120.50 ? 63  ILE B HG22 1 
ATOM   2756 H HG23 . ILE B 1 63  ? 6.419  9.568   34.540  1.00 120.50 ? 63  ILE B HG23 1 
ATOM   2757 H HD11 . ILE B 1 63  ? 9.082  10.279  37.621  1.00 121.99 ? 63  ILE B HD11 1 
ATOM   2758 H HD12 . ILE B 1 63  ? 7.795  9.467   38.077  1.00 121.99 ? 63  ILE B HD12 1 
ATOM   2759 H HD13 . ILE B 1 63  ? 8.464  9.168   36.668  1.00 121.99 ? 63  ILE B HD13 1 
ATOM   2760 N N    . SER B 1 64  ? 4.748  12.608  37.985  1.00 105.46 ? 64  SER B N    1 
ATOM   2761 C CA   . SER B 1 64  ? 4.828  13.585  39.057  1.00 102.25 ? 64  SER B CA   1 
ATOM   2762 C C    . SER B 1 64  ? 4.907  12.804  40.365  1.00 100.32 ? 64  SER B C    1 
ATOM   2763 O O    . SER B 1 64  ? 4.793  11.570  40.371  1.00 104.87 ? 64  SER B O    1 
ATOM   2764 C CB   . SER B 1 64  ? 3.646  14.538  38.948  1.00 105.22 ? 64  SER B CB   1 
ATOM   2765 O OG   . SER B 1 64  ? 2.452  13.861  39.273  1.00 105.55 ? 64  SER B OG   1 
ATOM   2766 H H    . SER B 1 64  ? 4.338  11.890  38.223  1.00 126.62 ? 64  SER B H    1 
ATOM   2767 H HA   . SER B 1 64  ? 5.628  14.132  39.023  1.00 122.77 ? 64  SER B HA   1 
ATOM   2768 H HB2  . SER B 1 64  ? 3.773  15.276  39.565  1.00 126.34 ? 64  SER B HB2  1 
ATOM   2769 H HB3  . SER B 1 64  ? 3.586  14.872  38.039  1.00 126.34 ? 64  SER B HB3  1 
ATOM   2770 H HG   . SER B 1 64  ? 1.809  14.401  39.279  1.00 126.73 ? 64  SER B HG   1 
ATOM   2771 N N    . SER B 1 65  ? 5.152  13.511  41.477  1.00 101.43 ? 65  SER B N    1 
ATOM   2772 C CA   . SER B 1 65  ? 5.358  12.849  42.766  1.00 103.17 ? 65  SER B CA   1 
ATOM   2773 C C    . SER B 1 65  ? 4.554  13.517  43.872  1.00 111.62 ? 65  SER B C    1 
ATOM   2774 O O    . SER B 1 65  ? 4.037  14.623  43.726  1.00 116.40 ? 65  SER B O    1 
ATOM   2775 C CB   . SER B 1 65  ? 6.850  12.811  43.138  1.00 101.37 ? 65  SER B CB   1 
ATOM   2776 O OG   . SER B 1 65  ? 7.456  14.092  43.069  1.00 101.89 ? 65  SER B OG   1 
ATOM   2777 H H    . SER B 1 65  ? 5.203  14.369  41.505  1.00 121.80 ? 65  SER B H    1 
ATOM   2778 H HA   . SER B 1 65  ? 5.025  11.941  42.692  1.00 123.88 ? 65  SER B HA   1 
ATOM   2779 H HB2  . SER B 1 65  ? 6.934  12.477  44.045  1.00 121.73 ? 65  SER B HB2  1 
ATOM   2780 H HB3  . SER B 1 65  ? 7.308  12.218  42.523  1.00 121.73 ? 65  SER B HB3  1 
ATOM   2781 H HG   . SER B 1 65  ? 8.281  14.028  43.212  1.00 122.35 ? 65  SER B HG   1 
ATOM   2782 N N    . TYR B 1 66  ? 4.453  12.825  45.001  1.00 121.68 ? 66  TYR B N    1 
ATOM   2783 C CA   . TYR B 1 66  ? 3.719  13.301  46.170  1.00 122.84 ? 66  TYR B CA   1 
ATOM   2784 C C    . TYR B 1 66  ? 4.114  12.422  47.361  1.00 126.91 ? 66  TYR B C    1 
ATOM   2785 O O    . TYR B 1 66  ? 4.701  11.350  47.203  1.00 130.93 ? 66  TYR B O    1 
ATOM   2786 C CB   . TYR B 1 66  ? 2.205  13.267  45.948  1.00 118.75 ? 66  TYR B CB   1 
ATOM   2787 C CG   . TYR B 1 66  ? 1.628  11.877  45.879  1.00 117.72 ? 66  TYR B CG   1 
ATOM   2788 C CD1  . TYR B 1 66  ? 1.329  11.184  47.036  1.00 125.31 ? 66  TYR B CD1  1 
ATOM   2789 C CD2  . TYR B 1 66  ? 1.324  11.287  44.680  1.00 114.89 ? 66  TYR B CD2  1 
ATOM   2790 C CE1  . TYR B 1 66  ? 0.800  9.920   47.000  1.00 122.98 ? 66  TYR B CE1  1 
ATOM   2791 C CE2  . TYR B 1 66  ? 0.766  10.025  44.633  1.00 110.84 ? 66  TYR B CE2  1 
ATOM   2792 C CZ   . TYR B 1 66  ? 0.512  9.350   45.803  1.00 113.94 ? 66  TYR B CZ   1 
ATOM   2793 O OH   . TYR B 1 66  ? -0.039 8.089   45.797  1.00 101.16 ? 66  TYR B OH   1 
ATOM   2794 H H    . TYR B 1 66  ? 4.811  12.052  45.120  1.00 146.10 ? 66  TYR B H    1 
ATOM   2795 H HA   . TYR B 1 66  ? 3.976  14.217  46.357  1.00 147.49 ? 66  TYR B HA   1 
ATOM   2796 H HB2  . TYR B 1 66  ? 1.772  13.730  46.683  1.00 142.58 ? 66  TYR B HB2  1 
ATOM   2797 H HB3  . TYR B 1 66  ? 2.003  13.712  45.110  1.00 142.58 ? 66  TYR B HB3  1 
ATOM   2798 H HD1  . TYR B 1 66  ? 1.491  11.584  47.859  1.00 150.45 ? 66  TYR B HD1  1 
ATOM   2799 H HD2  . TYR B 1 66  ? 1.495  11.743  43.887  1.00 137.94 ? 66  TYR B HD2  1 
ATOM   2800 H HE1  . TYR B 1 66  ? 0.640  9.457   47.790  1.00 147.66 ? 66  TYR B HE1  1 
ATOM   2801 H HE2  . TYR B 1 66  ? 0.564  9.634   43.814  1.00 133.08 ? 66  TYR B HE2  1 
ATOM   2802 H HH   . TYR B 1 66  ? -0.288 7.888   45.020  1.00 121.47 ? 66  TYR B HH   1 
ATOM   2803 N N    . TRP B 1 67  ? 3.788  12.895  48.565  1.00 128.40 ? 67  TRP B N    1 
ATOM   2804 C CA   . TRP B 1 67  ? 4.203  12.254  49.805  1.00 122.62 ? 67  TRP B CA   1 
ATOM   2805 C C    . TRP B 1 67  ? 3.069  11.476  50.458  1.00 118.19 ? 67  TRP B C    1 
ATOM   2806 O O    . TRP B 1 67  ? 1.900  11.854  50.363  1.00 120.76 ? 67  TRP B O    1 
ATOM   2807 C CB   . TRP B 1 67  ? 4.754  13.320  50.758  1.00 121.60 ? 67  TRP B CB   1 
ATOM   2808 C CG   . TRP B 1 67  ? 6.082  13.876  50.275  1.00 122.28 ? 67  TRP B CG   1 
ATOM   2809 C CD1  . TRP B 1 67  ? 6.276  14.961  49.452  1.00 122.52 ? 67  TRP B CD1  1 
ATOM   2810 C CD2  . TRP B 1 67  ? 7.398  13.382  50.600  1.00 123.11 ? 67  TRP B CD2  1 
ATOM   2811 N NE1  . TRP B 1 67  ? 7.627  15.151  49.227  1.00 118.13 ? 67  TRP B NE1  1 
ATOM   2812 C CE2  . TRP B 1 67  ? 8.335  14.207  49.928  1.00 119.07 ? 67  TRP B CE2  1 
ATOM   2813 C CE3  . TRP B 1 67  ? 7.874  12.307  51.370  1.00 123.72 ? 67  TRP B CE3  1 
ATOM   2814 C CZ2  . TRP B 1 67  ? 9.723  13.994  50.018  1.00 120.91 ? 67  TRP B CZ2  1 
ATOM   2815 C CZ3  . TRP B 1 67  ? 9.253  12.100  51.461  1.00 123.04 ? 67  TRP B CZ3  1 
ATOM   2816 C CH2  . TRP B 1 67  ? 10.159 12.943  50.793  1.00 122.18 ? 67  TRP B CH2  1 
ATOM   2817 H H    . TRP B 1 67  ? 3.316  13.603  48.688  1.00 154.16 ? 67  TRP B H    1 
ATOM   2818 H HA   . TRP B 1 67  ? 4.893  11.600  49.619  1.00 147.22 ? 67  TRP B HA   1 
ATOM   2819 H HB2  . TRP B 1 67  ? 4.121  14.053  50.819  1.00 145.99 ? 67  TRP B HB2  1 
ATOM   2820 H HB3  . TRP B 1 67  ? 4.889  12.926  51.634  1.00 145.99 ? 67  TRP B HB3  1 
ATOM   2821 H HD1  . TRP B 1 67  ? 5.597  15.490  49.099  1.00 147.10 ? 67  TRP B HD1  1 
ATOM   2822 H HE1  . TRP B 1 67  ? 7.969  15.763  48.728  1.00 141.83 ? 67  TRP B HE1  1 
ATOM   2823 H HE3  . TRP B 1 67  ? 7.281  11.743  51.811  1.00 148.54 ? 67  TRP B HE3  1 
ATOM   2824 H HZ2  . TRP B 1 67  ? 10.325 14.544  49.570  1.00 145.17 ? 67  TRP B HZ2  1 
ATOM   2825 H HZ3  . TRP B 1 67  ? 9.577  11.393  51.972  1.00 147.72 ? 67  TRP B HZ3  1 
ATOM   2826 H HH2  . TRP B 1 67  ? 11.072 12.786  50.876  1.00 146.69 ? 67  TRP B HH2  1 
ATOM   2827 N N    . GLY B 1 68  ? 3.435  10.365  51.110  1.00 121.95 ? 68  GLY B N    1 
ATOM   2828 C CA   . GLY B 1 68  ? 2.499  9.557   51.880  1.00 125.33 ? 68  GLY B CA   1 
ATOM   2829 C C    . GLY B 1 68  ? 2.445  9.897   53.361  1.00 134.13 ? 68  GLY B C    1 
ATOM   2830 O O    . GLY B 1 68  ? 1.403  9.774   54.036  1.00 159.18 ? 68  GLY B O    1 
ATOM   2831 H H    . GLY B 1 68  ? 4.237  10.056  51.118  1.00 146.42 ? 68  GLY B H    1 
ATOM   2832 H HA2  . GLY B 1 68  ? 1.609  9.678   51.515  1.00 150.48 ? 68  GLY B HA2  1 
ATOM   2833 H HA3  . GLY B 1 68  ? 2.751  8.624   51.798  1.00 150.48 ? 68  GLY B HA3  1 
ATOM   2834 N N    . ARG B 1 75  ? 5.488  10.044  55.091  1.00 140.35 ? 75  ARG B N    1 
ATOM   2835 C CA   . ARG B 1 75  ? 6.264  8.829   55.262  1.00 140.52 ? 75  ARG B CA   1 
ATOM   2836 C C    . ARG B 1 75  ? 7.101  8.399   54.061  1.00 138.42 ? 75  ARG B C    1 
ATOM   2837 O O    . ARG B 1 75  ? 8.324  8.431   54.150  1.00 136.53 ? 75  ARG B O    1 
ATOM   2838 C CB   . ARG B 1 75  ? 5.335  7.686   55.622  1.00 142.49 ? 75  ARG B CB   1 
ATOM   2839 C CG   . ARG B 1 75  ? 6.043  6.536   56.194  1.00 142.66 ? 75  ARG B CG   1 
ATOM   2840 C CD   . ARG B 1 75  ? 5.058  5.449   56.377  1.00 142.14 ? 75  ARG B CD   1 
ATOM   2841 N NE   . ARG B 1 75  ? 5.720  4.242   56.828  1.00 147.59 ? 75  ARG B NE   1 
ATOM   2842 C CZ   . ARG B 1 75  ? 5.220  3.024   56.682  1.00 152.25 ? 75  ARG B CZ   1 
ATOM   2843 N NH1  . ARG B 1 75  ? 4.037  2.827   56.109  1.00 157.80 ? 75  ARG B NH1  1 
ATOM   2844 N NH2  . ARG B 1 75  ? 5.911  1.981   57.144  1.00 148.87 ? 75  ARG B NH2  1 
ATOM   2845 H HA   . ARG B 1 75  ? 6.900  9.020   55.969  1.00 168.70 ? 75  ARG B HA   1 
ATOM   2846 H HB2  . ARG B 1 75  ? 4.691  7.998   56.277  1.00 171.06 ? 75  ARG B HB2  1 
ATOM   2847 H HB3  . ARG B 1 75  ? 4.877  7.389   54.821  1.00 171.06 ? 75  ARG B HB3  1 
ATOM   2848 H HG2  . ARG B 1 75  ? 6.742  6.238   55.590  1.00 171.27 ? 75  ARG B HG2  1 
ATOM   2849 H HG3  . ARG B 1 75  ? 6.426  6.771   57.054  1.00 171.27 ? 75  ARG B HG3  1 
ATOM   2850 H HD2  . ARG B 1 75  ? 4.403  5.711   57.043  1.00 170.64 ? 75  ARG B HD2  1 
ATOM   2851 H HD3  . ARG B 1 75  ? 4.616  5.264   55.533  1.00 170.64 ? 75  ARG B HD3  1 
ATOM   2852 H HE   . ARG B 1 75  ? 6.485  4.321   57.214  1.00 177.19 ? 75  ARG B HE   1 
ATOM   2853 H HH11 . ARG B 1 75  ? 3.580  3.497   55.824  1.00 189.44 ? 75  ARG B HH11 1 
ATOM   2854 H HH12 . ARG B 1 75  ? 3.728  2.029   56.023  1.00 189.44 ? 75  ARG B HH12 1 
ATOM   2855 H HH21 . ARG B 1 75  ? 6.669  2.105   57.530  1.00 178.73 ? 75  ARG B HH21 1 
ATOM   2856 H HH22 . ARG B 1 75  ? 5.597  1.185   57.056  1.00 178.73 ? 75  ARG B HH22 1 
ATOM   2857 N N    . ARG B 1 76  ? 6.456  7.901   52.992  1.00 142.38 ? 76  ARG B N    1 
ATOM   2858 C CA   . ARG B 1 76  ? 7.129  7.501   51.762  1.00 135.65 ? 76  ARG B CA   1 
ATOM   2859 C C    . ARG B 1 76  ? 6.758  8.425   50.602  1.00 130.00 ? 76  ARG B C    1 
ATOM   2860 O O    . ARG B 1 76  ? 5.645  8.956   50.549  1.00 130.06 ? 76  ARG B O    1 
ATOM   2861 C CB   . ARG B 1 76  ? 6.772  6.067   51.354  1.00 135.05 ? 76  ARG B CB   1 
ATOM   2862 C CG   . ARG B 1 76  ? 7.581  4.992   52.048  1.00 145.92 ? 76  ARG B CG   1 
ATOM   2863 C CD   . ARG B 1 76  ? 7.003  3.609   51.782  1.00 147.23 ? 76  ARG B CD   1 
ATOM   2864 N NE   . ARG B 1 76  ? 7.706  2.576   52.536  1.00 158.15 ? 76  ARG B NE   1 
ATOM   2865 C CZ   . ARG B 1 76  ? 7.259  1.340   52.725  1.00 161.45 ? 76  ARG B CZ   1 
ATOM   2866 N NH1  . ARG B 1 76  ? 6.088  0.947   52.249  1.00 164.44 ? 76  ARG B NH1  1 
ATOM   2867 N NH2  . ARG B 1 76  ? 8.019  0.472   53.391  1.00 166.32 ? 76  ARG B NH2  1 
ATOM   2868 H H    . ARG B 1 76  ? 5.605  7.786   52.963  1.00 170.93 ? 76  ARG B H    1 
ATOM   2869 H HA   . ARG B 1 76  ? 8.084  7.560   51.921  1.00 162.86 ? 76  ARG B HA   1 
ATOM   2870 H HB2  . ARG B 1 76  ? 5.838  5.910   51.564  1.00 162.14 ? 76  ARG B HB2  1 
ATOM   2871 H HB3  . ARG B 1 76  ? 6.919  5.972   50.400  1.00 162.14 ? 76  ARG B HB3  1 
ATOM   2872 H HG2  . ARG B 1 76  ? 8.493  5.011   51.717  1.00 175.18 ? 76  ARG B HG2  1 
ATOM   2873 H HG3  . ARG B 1 76  ? 7.572  5.149   53.005  1.00 175.18 ? 76  ARG B HG3  1 
ATOM   2874 H HD2  . ARG B 1 76  ? 6.070  3.596   52.046  1.00 176.76 ? 76  ARG B HD2  1 
ATOM   2875 H HD3  . ARG B 1 76  ? 7.084  3.404   50.837  1.00 176.76 ? 76  ARG B HD3  1 
ATOM   2876 H HE   . ARG B 1 76  ? 8.465  2.782   52.882  1.00 189.86 ? 76  ARG B HE   1 
ATOM   2877 H HH11 . ARG B 1 76  ? 5.598  1.497   51.805  1.00 197.40 ? 76  ARG B HH11 1 
ATOM   2878 H HH12 . ARG B 1 76  ? 5.818  0.142   52.384  1.00 197.40 ? 76  ARG B HH12 1 
ATOM   2879 H HH21 . ARG B 1 76  ? 8.787  0.714   53.691  1.00 199.67 ? 76  ARG B HH21 1 
ATOM   2880 H HH22 . ARG B 1 76  ? 7.741  -0.332  53.521  1.00 199.67 ? 76  ARG B HH22 1 
ATOM   2881 N N    . LYS B 1 77  ? 7.672  8.543   49.632  1.00 136.50 ? 77  LYS B N    1 
ATOM   2882 C CA   . LYS B 1 77  ? 7.456  9.340   48.421  1.00 143.58 ? 77  LYS B CA   1 
ATOM   2883 C C    . LYS B 1 77  ? 6.892  8.480   47.297  1.00 147.23 ? 77  LYS B C    1 
ATOM   2884 O O    . LYS B 1 77  ? 7.492  7.469   46.929  1.00 145.21 ? 77  LYS B O    1 
ATOM   2885 C CB   . LYS B 1 77  ? 8.748  10.000  47.946  1.00 147.73 ? 77  LYS B CB   1 
ATOM   2886 C CG   . LYS B 1 77  ? 8.536  11.056  46.859  1.00 130.22 ? 77  LYS B CG   1 
ATOM   2887 C CD   . LYS B 1 77  ? 9.833  11.752  46.467  1.00 104.90 ? 77  LYS B CD   1 
ATOM   2888 C CE   . LYS B 1 77  ? 9.573  12.946  45.565  1.00 116.14 ? 77  LYS B CE   1 
ATOM   2889 N NZ   . LYS B 1 77  ? 10.783 13.387  44.823  1.00 121.28 ? 77  LYS B NZ   1 
ATOM   2890 H H    . LYS B 1 77  ? 8.442  8.162   49.654  1.00 163.88 ? 77  LYS B H    1 
ATOM   2891 H HA   . LYS B 1 77  ? 6.808  10.027  48.643  1.00 172.37 ? 77  LYS B HA   1 
ATOM   2892 H HB2  . LYS B 1 77  ? 9.173  10.435  48.702  1.00 177.36 ? 77  LYS B HB2  1 
ATOM   2893 H HB3  . LYS B 1 77  ? 9.333  9.316   47.584  1.00 177.36 ? 77  LYS B HB3  1 
ATOM   2894 H HG2  . LYS B 1 77  ? 8.173  10.629  46.067  1.00 156.34 ? 77  LYS B HG2  1 
ATOM   2895 H HG3  . LYS B 1 77  ? 7.920  11.730  47.185  1.00 156.34 ? 77  LYS B HG3  1 
ATOM   2896 H HD2  . LYS B 1 77  ? 10.283 12.067  47.266  1.00 125.96 ? 77  LYS B HD2  1 
ATOM   2897 H HD3  . LYS B 1 77  ? 10.402 11.128  45.990  1.00 125.96 ? 77  LYS B HD3  1 
ATOM   2898 H HE2  . LYS B 1 77  ? 8.894  12.707  44.914  1.00 139.45 ? 77  LYS B HE2  1 
ATOM   2899 H HE3  . LYS B 1 77  ? 9.267  13.690  46.106  1.00 139.45 ? 77  LYS B HE3  1 
ATOM   2900 H HZ1  . LYS B 1 77  ? 10.577 14.060  44.278  1.00 145.62 ? 77  LYS B HZ1  1 
ATOM   2901 H HZ2  . LYS B 1 77  ? 11.408 13.659  45.395  1.00 145.62 ? 77  LYS B HZ2  1 
ATOM   2902 H HZ3  . LYS B 1 77  ? 11.107 12.713  44.340  1.00 145.62 ? 77  LYS B HZ3  1 
ATOM   2903 N N    . TYR B 1 78  ? 5.738  8.853   46.779  1.00 141.20 ? 78  TYR B N    1 
ATOM   2904 C CA   . TYR B 1 78  ? 5.090  8.115   45.702  1.00 139.20 ? 78  TYR B CA   1 
ATOM   2905 C C    . TYR B 1 78  ? 5.186  8.864   44.373  1.00 128.47 ? 78  TYR B C    1 
ATOM   2906 O O    . TYR B 1 78  ? 5.254  10.097  44.331  1.00 122.14 ? 78  TYR B O    1 
ATOM   2907 C CB   . TYR B 1 78  ? 3.643  7.809   46.093  1.00 134.17 ? 78  TYR B CB   1 
ATOM   2908 C CG   . TYR B 1 78  ? 3.617  6.702   47.115  1.00 136.69 ? 78  TYR B CG   1 
ATOM   2909 C CD1  . TYR B 1 78  ? 3.892  6.975   48.448  1.00 146.61 ? 78  TYR B CD1  1 
ATOM   2910 C CD2  . TYR B 1 78  ? 3.344  5.397   46.758  1.00 133.32 ? 78  TYR B CD2  1 
ATOM   2911 C CE1  . TYR B 1 78  ? 3.903  5.979   49.409  1.00 128.57 ? 78  TYR B CE1  1 
ATOM   2912 C CE2  . TYR B 1 78  ? 3.339  4.386   47.717  1.00 139.53 ? 78  TYR B CE2  1 
ATOM   2913 C CZ   . TYR B 1 78  ? 3.619  4.687   49.041  1.00 132.01 ? 78  TYR B CZ   1 
ATOM   2914 O OH   . TYR B 1 78  ? 3.631  3.713   50.011  1.00 128.46 ? 78  TYR B OH   1 
ATOM   2915 H H    . TYR B 1 78  ? 5.298  9.545   47.037  1.00 169.51 ? 78  TYR B H    1 
ATOM   2916 H HA   . TYR B 1 78  ? 5.543  7.272   45.545  1.00 167.12 ? 78  TYR B HA   1 
ATOM   2917 H HB2  . TYR B 1 78  ? 3.234  8.600   46.477  1.00 161.08 ? 78  TYR B HB2  1 
ATOM   2918 H HB3  . TYR B 1 78  ? 3.145  7.525   45.311  1.00 161.08 ? 78  TYR B HB3  1 
ATOM   2919 H HD1  . TYR B 1 78  ? 4.074  7.850   48.702  1.00 176.01 ? 78  TYR B HD1  1 
ATOM   2920 H HD2  . TYR B 1 78  ? 3.160  5.192   45.870  1.00 160.06 ? 78  TYR B HD2  1 
ATOM   2921 H HE1  . TYR B 1 78  ? 4.100  6.182   50.294  1.00 154.36 ? 78  TYR B HE1  1 
ATOM   2922 H HE2  . TYR B 1 78  ? 3.149  3.510   47.468  1.00 167.52 ? 78  TYR B HE2  1 
ATOM   2923 H HH   . TYR B 1 78  ? 3.316  2.997   49.703  1.00 154.23 ? 78  TYR B HH   1 
ATOM   2924 N N    . TYR B 1 79  ? 5.266  8.083   43.280  1.00 124.95 ? 79  TYR B N    1 
ATOM   2925 C CA   . TYR B 1 79  ? 5.244  8.587   41.911  1.00 110.65 ? 79  TYR B CA   1 
ATOM   2926 C C    . TYR B 1 79  ? 4.001  8.049   41.205  1.00 96.93  ? 79  TYR B C    1 
ATOM   2927 O O    . TYR B 1 79  ? 3.564  6.924   41.457  1.00 95.28  ? 79  TYR B O    1 
ATOM   2928 C CB   . TYR B 1 79  ? 6.504  8.169   41.124  1.00 106.03 ? 79  TYR B CB   1 
ATOM   2929 C CG   . TYR B 1 79  ? 7.820  8.748   41.632  1.00 106.16 ? 79  TYR B CG   1 
ATOM   2930 C CD1  . TYR B 1 79  ? 8.547  8.098   42.621  1.00 114.08 ? 79  TYR B CD1  1 
ATOM   2931 C CD2  . TYR B 1 79  ? 8.338  9.931   41.125  1.00 98.93  ? 79  TYR B CD2  1 
ATOM   2932 C CE1  . TYR B 1 79  ? 9.753  8.614   43.095  1.00 109.54 ? 79  TYR B CE1  1 
ATOM   2933 C CE2  . TYR B 1 79  ? 9.546  10.460  41.603  1.00 91.89  ? 79  TYR B CE2  1 
ATOM   2934 C CZ   . TYR B 1 79  ? 10.246 9.794   42.586  1.00 97.49  ? 79  TYR B CZ   1 
ATOM   2935 O OH   . TYR B 1 79  ? 11.436 10.305  43.059  1.00 105.14 ? 79  TYR B OH   1 
ATOM   2936 H H    . TYR B 1 79  ? 5.336  7.227   43.317  1.00 150.02 ? 79  TYR B H    1 
ATOM   2937 H HA   . TYR B 1 79  ? 5.213  9.557   41.922  1.00 132.86 ? 79  TYR B HA   1 
ATOM   2938 H HB2  . TYR B 1 79  ? 6.580  7.203   41.162  1.00 127.31 ? 79  TYR B HB2  1 
ATOM   2939 H HB3  . TYR B 1 79  ? 6.398  8.458   40.204  1.00 127.31 ? 79  TYR B HB3  1 
ATOM   2940 H HD1  . TYR B 1 79  ? 8.222  7.302   42.975  1.00 136.98 ? 79  TYR B HD1  1 
ATOM   2941 H HD2  . TYR B 1 79  ? 7.876  10.382  40.456  1.00 118.80 ? 79  TYR B HD2  1 
ATOM   2942 H HE1  . TYR B 1 79  ? 10.225 8.160   43.756  1.00 131.52 ? 79  TYR B HE1  1 
ATOM   2943 H HE2  . TYR B 1 79  ? 9.874  11.259  41.258  1.00 110.34 ? 79  TYR B HE2  1 
ATOM   2944 H HH   . TYR B 1 79  ? 11.556 11.080  42.759  1.00 126.24 ? 79  TYR B HH   1 
ATOM   2945 N N    . ARG B 1 80  ? 3.431  8.860   40.318  1.00 100.64 ? 80  ARG B N    1 
ATOM   2946 C CA   . ARG B 1 80  ? 2.239  8.490   39.568  1.00 102.60 ? 80  ARG B CA   1 
ATOM   2947 C C    . ARG B 1 80  ? 2.404  8.986   38.140  1.00 98.09  ? 80  ARG B C    1 
ATOM   2948 O O    . ARG B 1 80  ? 3.230  9.857   37.855  1.00 93.11  ? 80  ARG B O    1 
ATOM   2949 C CB   . ARG B 1 80  ? 0.969  9.065   40.186  1.00 96.20  ? 80  ARG B CB   1 
ATOM   2950 C CG   . ARG B 1 80  ? 0.842  10.548  40.007  1.00 95.70  ? 80  ARG B CG   1 
ATOM   2951 C CD   . ARG B 1 80  ? -0.429 11.022  40.668  1.00 103.67 ? 80  ARG B CD   1 
ATOM   2952 N NE   . ARG B 1 80  ? -1.584 10.953  39.794  1.00 114.03 ? 80  ARG B NE   1 
ATOM   2953 C CZ   . ARG B 1 80  ? -1.919 11.899  38.923  1.00 112.37 ? 80  ARG B CZ   1 
ATOM   2954 N NH1  . ARG B 1 80  ? -1.182 12.991  38.770  1.00 118.02 ? 80  ARG B NH1  1 
ATOM   2955 N NH2  . ARG B 1 80  ? -3.032 11.756  38.203  1.00 108.07 ? 80  ARG B NH2  1 
ATOM   2956 H H    . ARG B 1 80  ? 3.723  9.647   40.130  1.00 120.85 ? 80  ARG B H    1 
ATOM   2957 H HA   . ARG B 1 80  ? 2.146  7.525   39.558  1.00 123.20 ? 80  ARG B HA   1 
ATOM   2958 H HB2  . ARG B 1 80  ? 0.200  8.647   39.767  1.00 115.52 ? 80  ARG B HB2  1 
ATOM   2959 H HB3  . ARG B 1 80  ? 0.971  8.878   41.137  1.00 115.52 ? 80  ARG B HB3  1 
ATOM   2960 H HG2  . ARG B 1 80  ? 1.596  10.996  40.420  1.00 114.92 ? 80  ARG B HG2  1 
ATOM   2961 H HG3  . ARG B 1 80  ? 0.804  10.764  39.062  1.00 114.92 ? 80  ARG B HG3  1 
ATOM   2962 H HD2  . ARG B 1 80  ? -0.607 10.466  41.443  1.00 124.48 ? 80  ARG B HD2  1 
ATOM   2963 H HD3  . ARG B 1 80  ? -0.316 11.945  40.942  1.00 124.48 ? 80  ARG B HD3  1 
ATOM   2964 H HE   . ARG B 1 80  ? -2.085 10.255  39.842  1.00 136.91 ? 80  ARG B HE   1 
ATOM   2965 H HH11 . ARG B 1 80  ? -0.470 13.098  39.240  1.00 141.70 ? 80  ARG B HH11 1 
ATOM   2966 H HH12 . ARG B 1 80  ? -1.416 13.591  38.201  1.00 141.70 ? 80  ARG B HH12 1 
ATOM   2967 H HH21 . ARG B 1 80  ? -3.523 11.057  38.305  1.00 129.77 ? 80  ARG B HH21 1 
ATOM   2968 H HH22 . ARG B 1 80  ? -3.259 12.362  37.636  1.00 129.77 ? 80  ARG B HH22 1 
ATOM   2969 N N    . LEU B 1 81  ? 1.640  8.371   37.231  1.00 103.30 ? 81  LEU B N    1 
ATOM   2970 C CA   . LEU B 1 81  ? 1.592  8.734   35.804  1.00 98.76  ? 81  LEU B CA   1 
ATOM   2971 C C    . LEU B 1 81  ? 0.534  9.799   35.510  1.00 95.99  ? 81  LEU B C    1 
ATOM   2972 O O    . LEU B 1 81  ? -0.639 9.627   35.859  1.00 92.67  ? 81  LEU B O    1 
ATOM   2973 C CB   . LEU B 1 81  ? 1.314  7.451   35.020  1.00 86.28  ? 81  LEU B CB   1 
ATOM   2974 C CG   . LEU B 1 81  ? 1.582  7.337   33.535  1.00 93.22  ? 81  LEU B CG   1 
ATOM   2975 C CD1  . LEU B 1 81  ? 3.055  7.567   33.284  1.00 96.21  ? 81  LEU B CD1  1 
ATOM   2976 C CD2  . LEU B 1 81  ? 1.169  5.967   33.009  1.00 93.99  ? 81  LEU B CD2  1 
ATOM   2977 H H    . LEU B 1 81  ? 1.119  7.714   37.421  1.00 124.04 ? 81  LEU B H    1 
ATOM   2978 H HA   . LEU B 1 81  ? 2.432  9.133   35.529  1.00 118.59 ? 81  LEU B HA   1 
ATOM   2979 H HB2  . LEU B 1 81  ? 1.845  6.752   35.434  1.00 103.61 ? 81  LEU B HB2  1 
ATOM   2980 H HB3  . LEU B 1 81  ? 0.370  7.258   35.128  1.00 103.61 ? 81  LEU B HB3  1 
ATOM   2981 H HG   . LEU B 1 81  ? 1.062  8.002   33.058  1.00 111.94 ? 81  LEU B HG   1 
ATOM   2982 H HD11 . LEU B 1 81  ? 3.242  7.417   32.344  1.00 115.53 ? 81  LEU B HD11 1 
ATOM   2983 H HD12 . LEU B 1 81  ? 3.277  8.480   33.524  1.00 115.53 ? 81  LEU B HD12 1 
ATOM   2984 H HD13 . LEU B 1 81  ? 3.568  6.948   33.826  1.00 115.53 ? 81  LEU B HD13 1 
ATOM   2985 H HD21 . LEU B 1 81  ? 1.333  5.934   32.053  1.00 112.87 ? 81  LEU B HD21 1 
ATOM   2986 H HD22 . LEU B 1 81  ? 1.692  5.285   33.458  1.00 112.87 ? 81  LEU B HD22 1 
ATOM   2987 H HD23 . LEU B 1 81  ? 0.225  5.832   33.187  1.00 112.87 ? 81  LEU B HD23 1 
ATOM   2988 N N    . THR B 1 82  ? 0.960  10.908  34.874  1.00 98.11  ? 82  THR B N    1 
ATOM   2989 C CA   . THR B 1 82  ? 0.062  11.998  34.512  1.00 100.57 ? 82  THR B CA   1 
ATOM   2990 C C    . THR B 1 82  ? -0.774 11.635  33.291  1.00 100.15 ? 82  THR B C    1 
ATOM   2991 O O    . THR B 1 82  ? -0.597 10.572  32.701  1.00 98.61  ? 82  THR B O    1 
ATOM   2992 C CB   . THR B 1 82  ? 0.804  13.290  34.147  1.00 103.99 ? 82  THR B CB   1 
ATOM   2993 O OG1  . THR B 1 82  ? 1.559  13.095  32.940  1.00 97.47  ? 82  THR B OG1  1 
ATOM   2994 C CG2  . THR B 1 82  ? 1.711  13.718  35.253  1.00 96.27  ? 82  THR B CG2  1 
ATOM   2995 H H    . THR B 1 82  ? 1.777  11.045  34.642  1.00 117.80 ? 82  THR B H    1 
ATOM   2996 H HA   . THR B 1 82  ? -0.492 12.150  35.294  1.00 120.77 ? 82  THR B HA   1 
ATOM   2997 H HB   . THR B 1 82  ? 0.159  14.000  34.006  1.00 124.87 ? 82  THR B HB   1 
ATOM   2998 H HG1  . THR B 1 82  ? 2.000  13.787  32.762  1.00 117.04 ? 82  THR B HG1  1 
ATOM   2999 H HG21 . THR B 1 82  ? 2.072  14.599  35.065  1.00 115.60 ? 82  THR B HG21 1 
ATOM   3000 H HG22 . THR B 1 82  ? 1.222  13.750  36.090  1.00 115.60 ? 82  THR B HG22 1 
ATOM   3001 H HG23 . THR B 1 82  ? 2.446  13.090  35.342  1.00 115.60 ? 82  THR B HG23 1 
ATOM   3002 N N    . GLU B 1 83  ? -1.713 12.527  32.920  1.00 101.24 ? 83  GLU B N    1 
ATOM   3003 C CA   . GLU B 1 83  ? -2.440 12.329  31.667  1.00 103.24 ? 83  GLU B CA   1 
ATOM   3004 C C    . GLU B 1 83  ? -1.514 12.452  30.467  1.00 94.99  ? 83  GLU B C    1 
ATOM   3005 O O    . GLU B 1 83  ? -1.697 11.767  29.466  1.00 95.10  ? 83  GLU B O    1 
ATOM   3006 C CB   . GLU B 1 83  ? -3.587 13.319  31.465  1.00 103.08 ? 83  GLU B CB   1 
ATOM   3007 C CG   . GLU B 1 83  ? -4.842 13.038  32.194  1.00 104.18 ? 83  GLU B CG   1 
ATOM   3008 C CD   . GLU B 1 83  ? -5.759 14.236  32.131  1.00 113.36 ? 83  GLU B CD   1 
ATOM   3009 O OE1  . GLU B 1 83  ? -5.940 14.764  31.004  1.00 113.14 ? 83  GLU B OE1  1 
ATOM   3010 O OE2  . GLU B 1 83  ? -6.288 14.641  33.191  1.00 116.01 ? 83  GLU B OE2  1 
ATOM   3011 H H    . GLU B 1 83  ? -1.935 13.228  33.365  1.00 121.57 ? 83  GLU B H    1 
ATOM   3012 H HA   . GLU B 1 83  ? -2.824 11.440  31.730  1.00 123.96 ? 83  GLU B HA   1 
ATOM   3013 H HB2  . GLU B 1 83  ? -3.282 14.194  31.751  1.00 123.77 ? 83  GLU B HB2  1 
ATOM   3014 H HB3  . GLU B 1 83  ? -3.805 13.336  30.520  1.00 123.77 ? 83  GLU B HB3  1 
ATOM   3015 H HG2  . GLU B 1 83  ? -5.292 12.281  31.788  1.00 125.10 ? 83  GLU B HG2  1 
ATOM   3016 H HG3  . GLU B 1 83  ? -4.644 12.848  33.124  1.00 125.10 ? 83  GLU B HG3  1 
ATOM   3017 N N    . ILE B 1 84  ? -0.543 13.363  30.548  1.00 107.97 ? 84  ILE B N    1 
ATOM   3018 C CA   . ILE B 1 84  ? 0.435  13.511  29.492  1.00 118.70 ? 84  ILE B CA   1 
ATOM   3019 C C    . ILE B 1 84  ? 1.128  12.178  29.282  1.00 117.12 ? 84  ILE B C    1 
ATOM   3020 O O    . ILE B 1 84  ? 1.397  11.759  28.148  1.00 113.37 ? 84  ILE B O    1 
ATOM   3021 C CB   . ILE B 1 84  ? 1.439  14.616  29.876  1.00 127.49 ? 84  ILE B CB   1 
ATOM   3022 C CG1  . ILE B 1 84  ? 0.702  15.890  30.294  1.00 124.27 ? 84  ILE B CG1  1 
ATOM   3023 C CG2  . ILE B 1 84  ? 2.393  14.856  28.705  1.00 163.60 ? 84  ILE B CG2  1 
ATOM   3024 C CD1  . ILE B 1 84  ? 1.505  16.822  31.242  1.00 123.34 ? 84  ILE B CD1  1 
ATOM   3025 H H    . ILE B 1 84  ? -0.435 13.905  31.207  1.00 129.64 ? 84  ILE B H    1 
ATOM   3026 H HA   . ILE B 1 84  ? 0.002  13.773  28.665  1.00 142.52 ? 84  ILE B HA   1 
ATOM   3027 H HB   . ILE B 1 84  ? 1.961  14.332  30.642  1.00 153.06 ? 84  ILE B HB   1 
ATOM   3028 H HG12 . ILE B 1 84  ? 0.488  16.398  29.496  1.00 149.20 ? 84  ILE B HG12 1 
ATOM   3029 H HG13 . ILE B 1 84  ? -0.114 15.637  30.755  1.00 149.20 ? 84  ILE B HG13 1 
ATOM   3030 H HG21 . ILE B 1 84  ? 2.968  15.608  28.916  1.00 196.40 ? 84  ILE B HG21 1 
ATOM   3031 H HG22 . ILE B 1 84  ? 2.928  14.059  28.565  1.00 196.40 ? 84  ILE B HG22 1 
ATOM   3032 H HG23 . ILE B 1 84  ? 1.873  15.050  27.909  1.00 196.40 ? 84  ILE B HG23 1 
ATOM   3033 H HD11 . ILE B 1 84  ? 0.947  17.574  31.494  1.00 148.09 ? 84  ILE B HD11 1 
ATOM   3034 H HD12 . ILE B 1 84  ? 1.763  16.323  32.033  1.00 148.09 ? 84  ILE B HD12 1 
ATOM   3035 H HD13 . ILE B 1 84  ? 2.296  17.139  30.778  1.00 148.09 ? 84  ILE B HD13 1 
ATOM   3036 N N    . GLY B 1 85  ? 1.387  11.479  30.397  1.00 110.60 ? 85  GLY B N    1 
ATOM   3037 C CA   . GLY B 1 85  ? 2.050  10.185  30.318  1.00 109.17 ? 85  GLY B CA   1 
ATOM   3038 C C    . GLY B 1 85  ? 1.148  9.060   29.835  1.00 96.10  ? 85  GLY B C    1 
ATOM   3039 O O    . GLY B 1 85  ? 1.617  8.111   29.223  1.00 92.76  ? 85  GLY B O    1 
ATOM   3040 H H    . GLY B 1 85  ? 1.191  11.733  31.195  1.00 132.80 ? 85  GLY B H    1 
ATOM   3041 H HA2  . GLY B 1 85  ? 2.799  10.251  29.705  1.00 131.08 ? 85  GLY B HA2  1 
ATOM   3042 H HA3  . GLY B 1 85  ? 2.381  9.946   31.198  1.00 131.08 ? 85  GLY B HA3  1 
ATOM   3043 N N    . HIS B 1 86  ? -0.140 9.093   30.201  1.00 100.86 ? 86  HIS B N    1 
ATOM   3044 C CA   . HIS B 1 86  ? -1.102 8.111   29.685  1.00 98.84  ? 86  HIS B CA   1 
ATOM   3045 C C    . HIS B 1 86  ? -1.294 8.199   28.180  1.00 97.31  ? 86  HIS B C    1 
ATOM   3046 O O    . HIS B 1 86  ? -1.613 7.180   27.538  1.00 84.41  ? 86  HIS B O    1 
ATOM   3047 C CB   . HIS B 1 86  ? -2.453 8.272   30.382  1.00 89.32  ? 86  HIS B CB   1 
ATOM   3048 C CG   . HIS B 1 86  ? -2.478 7.637   31.729  1.00 96.12  ? 86  HIS B CG   1 
ATOM   3049 N ND1  . HIS B 1 86  ? -2.217 8.335   32.896  1.00 82.39  ? 86  HIS B ND1  1 
ATOM   3050 C CD2  . HIS B 1 86  ? -2.663 6.353   32.094  1.00 92.62  ? 86  HIS B CD2  1 
ATOM   3051 C CE1  . HIS B 1 86  ? -2.251 7.505   33.912  1.00 89.72  ? 86  HIS B CE1  1 
ATOM   3052 N NE2  . HIS B 1 86  ? -2.529 6.296   33.459  1.00 87.95  ? 86  HIS B NE2  1 
ATOM   3053 H H    . HIS B 1 86  ? -0.481 9.669   30.742  1.00 121.11 ? 86  HIS B H    1 
ATOM   3054 H HA   . HIS B 1 86  ? -0.749 7.230   29.886  1.00 118.69 ? 86  HIS B HA   1 
ATOM   3055 H HB2  . HIS B 1 86  ? -2.642 9.217   30.490  1.00 107.26 ? 86  HIS B HB2  1 
ATOM   3056 H HB3  . HIS B 1 86  ? -3.141 7.856   29.839  1.00 107.26 ? 86  HIS B HB3  1 
ATOM   3057 H HD1  . HIS B 1 86  ? -2.058 9.178   32.947  1.00 98.94  ? 86  HIS B HD1  1 
ATOM   3058 H HD2  . HIS B 1 86  ? -2.847 5.639   31.527  1.00 111.22 ? 86  HIS B HD2  1 
ATOM   3059 H HE1  . HIS B 1 86  ? -2.104 7.730   34.802  1.00 107.75 ? 86  HIS B HE1  1 
ATOM   3060 N N    . GLU B 1 87  ? -1.202 9.418   27.611  1.00 97.05  ? 87  GLU B N    1 
ATOM   3061 C CA   . GLU B 1 87  ? -1.320 9.612   26.164  1.00 89.80  ? 87  GLU B CA   1 
ATOM   3062 C C    . GLU B 1 87  ? -0.134 9.000   25.444  1.00 87.43  ? 87  GLU B C    1 
ATOM   3063 O O    . GLU B 1 87  ? -0.301 8.123   24.596  1.00 87.41  ? 87  GLU B O    1 
ATOM   3064 C CB   . GLU B 1 87  ? -1.410 11.110  25.837  1.00 89.14  ? 87  GLU B CB   1 
ATOM   3065 C CG   . GLU B 1 87  ? -1.923 11.489  24.462  1.00 94.26  ? 87  GLU B CG   1 
ATOM   3066 C CD   . GLU B 1 87  ? -3.358 11.106  24.213  1.00 101.70 ? 87  GLU B CD   1 
ATOM   3067 O OE1  . GLU B 1 87  ? -4.174 11.221  25.156  1.00 109.48 ? 87  GLU B OE1  1 
ATOM   3068 O OE2  . GLU B 1 87  ? -3.664 10.676  23.065  1.00 101.20 ? 87  GLU B OE2  1 
ATOM   3069 H H    . GLU B 1 87  ? -1.071 10.148  28.047  1.00 116.54 ? 87  GLU B H    1 
ATOM   3070 H HA   . GLU B 1 87  ? -2.133 9.182   25.858  1.00 107.84 ? 87  GLU B HA   1 
ATOM   3071 H HB2  . GLU B 1 87  ? -2.005 11.521  26.483  1.00 107.05 ? 87  GLU B HB2  1 
ATOM   3072 H HB3  . GLU B 1 87  ? -0.520 11.487  25.918  1.00 107.05 ? 87  GLU B HB3  1 
ATOM   3073 H HG2  . GLU B 1 87  ? -1.854 12.452  24.359  1.00 113.19 ? 87  GLU B HG2  1 
ATOM   3074 H HG3  . GLU B 1 87  ? -1.380 11.044  23.793  1.00 113.19 ? 87  GLU B HG3  1 
ATOM   3075 N N    . ASN B 1 88  ? 1.079  9.396   25.828  1.00 93.21  ? 88  ASN B N    1 
ATOM   3076 C CA   . ASN B 1 88  ? 2.273  8.856   25.191  1.00 92.37  ? 88  ASN B CA   1 
ATOM   3077 C C    . ASN B 1 88  ? 2.256  7.333   25.187  1.00 92.71  ? 88  ASN B C    1 
ATOM   3078 O O    . ASN B 1 88  ? 2.649  6.696   24.202  1.00 95.11  ? 88  ASN B O    1 
ATOM   3079 C CB   . ASN B 1 88  ? 3.514  9.353   25.920  1.00 91.51  ? 88  ASN B CB   1 
ATOM   3080 C CG   . ASN B 1 88  ? 3.812  10.783  25.615  1.00 91.58  ? 88  ASN B CG   1 
ATOM   3081 O OD1  . ASN B 1 88  ? 2.903  11.623  25.582  1.00 92.53  ? 88  ASN B OD1  1 
ATOM   3082 N ND2  . ASN B 1 88  ? 5.085  11.082  25.357  1.00 92.08  ? 88  ASN B ND2  1 
ATOM   3083 H H    . ASN B 1 88  ? 1.235  9.971   26.449  1.00 111.93 ? 88  ASN B H    1 
ATOM   3084 H HA   . ASN B 1 88  ? 2.305  9.166   24.272  1.00 110.92 ? 88  ASN B HA   1 
ATOM   3085 H HB2  . ASN B 1 88  ? 3.375  9.271   26.877  1.00 109.89 ? 88  ASN B HB2  1 
ATOM   3086 H HB3  . ASN B 1 88  ? 4.278  8.820   25.648  1.00 109.89 ? 88  ASN B HB3  1 
ATOM   3087 H HD21 . ASN B 1 88  ? 5.309  11.892  25.176  1.00 110.57 ? 88  ASN B HD21 1 
ATOM   3088 H HD22 . ASN B 1 88  ? 5.683  10.464  25.373  1.00 110.57 ? 88  ASN B HD22 1 
ATOM   3089 N N    . MET B 1 89  ? 1.814  6.723   26.275  1.00 89.32  ? 89  MET B N    1 
ATOM   3090 C CA   . MET B 1 89  ? 1.803  5.266   26.293  1.00 95.12  ? 89  MET B CA   1 
ATOM   3091 C C    . MET B 1 89  ? 0.912  4.731   25.194  1.00 87.62  ? 89  MET B C    1 
ATOM   3092 O O    . MET B 1 89  ? 1.229  3.701   24.577  1.00 84.83  ? 89  MET B O    1 
ATOM   3093 C CB   . MET B 1 89  ? 1.330  4.748   27.657  1.00 94.71  ? 89  MET B CB   1 
ATOM   3094 C CG   . MET B 1 89  ? 2.241  5.088   28.821  1.00 101.22 ? 89  MET B CG   1 
ATOM   3095 S SD   . MET B 1 89  ? 3.862  4.285   28.748  1.00 99.55  ? 89  MET B SD   1 
ATOM   3096 C CE   . MET B 1 89  ? 3.438  2.724   29.564  1.00 93.28  ? 89  MET B CE   1 
ATOM   3097 H H    . MET B 1 89  ? 1.528  7.110   26.987  1.00 107.26 ? 89  MET B H    1 
ATOM   3098 H HA   . MET B 1 89  ? 2.709  4.945   26.164  1.00 114.22 ? 89  MET B HA   1 
ATOM   3099 H HB2  . MET B 1 89  ? 0.460  5.131   27.847  1.00 113.73 ? 89  MET B HB2  1 
ATOM   3100 H HB3  . MET B 1 89  ? 1.265  3.781   27.613  1.00 113.73 ? 89  MET B HB3  1 
ATOM   3101 H HG2  . MET B 1 89  ? 2.388  6.047   28.831  1.00 121.54 ? 89  MET B HG2  1 
ATOM   3102 H HG3  . MET B 1 89  ? 1.811  4.810   29.645  1.00 121.54 ? 89  MET B HG3  1 
ATOM   3103 H HE1  . MET B 1 89  ? 4.228  2.162   29.601  1.00 112.02 ? 89  MET B HE1  1 
ATOM   3104 H HE2  . MET B 1 89  ? 3.124  2.913   30.462  1.00 112.02 ? 89  MET B HE2  1 
ATOM   3105 H HE3  . MET B 1 89  ? 2.740  2.282   29.056  1.00 112.02 ? 89  MET B HE3  1 
ATOM   3106 N N    . ARG B 1 90  ? -0.186 5.432   24.900  1.00 88.17  ? 90  ARG B N    1 
ATOM   3107 C CA   . ARG B 1 90  ? -1.045 4.998   23.811  1.00 93.63  ? 90  ARG B CA   1 
ATOM   3108 C C    . ARG B 1 90  ? -0.405 5.334   22.483  1.00 85.95  ? 90  ARG B C    1 
ATOM   3109 O O    . ARG B 1 90  ? -0.294 4.471   21.615  1.00 84.25  ? 90  ARG B O    1 
ATOM   3110 C CB   . ARG B 1 90  ? -2.431 5.642   23.894  1.00 99.13  ? 90  ARG B CB   1 
ATOM   3111 C CG   . ARG B 1 90  ? -3.444 5.066   22.891  1.00 100.34 ? 90  ARG B CG   1 
ATOM   3112 C CD   . ARG B 1 90  ? -4.827 5.634   23.017  1.00 102.79 ? 90  ARG B CD   1 
ATOM   3113 N NE   . ARG B 1 90  ? -4.883 7.087   22.964  1.00 90.84  ? 90  ARG B NE   1 
ATOM   3114 C CZ   . ARG B 1 90  ? -4.900 7.793   21.848  1.00 92.94  ? 90  ARG B CZ   1 
ATOM   3115 N NH1  . ARG B 1 90  ? -4.868 7.206   20.663  1.00 105.08 ? 90  ARG B NH1  1 
ATOM   3116 N NH2  . ARG B 1 90  ? -4.984 9.115   21.920  1.00 99.62  ? 90  ARG B NH2  1 
ATOM   3117 H H    . ARG B 1 90  ? -0.445 6.143   25.308  1.00 105.88 ? 90  ARG B H    1 
ATOM   3118 H HA   . ARG B 1 90  ? -1.173 4.039   23.887  1.00 112.44 ? 90  ARG B HA   1 
ATOM   3119 H HB2  . ARG B 1 90  ? -2.786 5.504   24.786  1.00 119.03 ? 90  ARG B HB2  1 
ATOM   3120 H HB3  . ARG B 1 90  ? -2.344 6.591   23.714  1.00 119.03 ? 90  ARG B HB3  1 
ATOM   3121 H HG2  . ARG B 1 90  ? -3.132 5.252   21.992  1.00 120.49 ? 90  ARG B HG2  1 
ATOM   3122 H HG3  . ARG B 1 90  ? -3.507 4.108   23.029  1.00 120.49 ? 90  ARG B HG3  1 
ATOM   3123 H HD2  . ARG B 1 90  ? -5.370 5.292   22.290  1.00 123.42 ? 90  ARG B HD2  1 
ATOM   3124 H HD3  . ARG B 1 90  ? -5.199 5.357   23.869  1.00 123.42 ? 90  ARG B HD3  1 
ATOM   3125 H HE   . ARG B 1 90  ? -4.908 7.515   23.710  1.00 109.08 ? 90  ARG B HE   1 
ATOM   3126 H HH11 . ARG B 1 90  ? -4.836 6.348   20.609  1.00 126.17 ? 90  ARG B HH11 1 
ATOM   3127 H HH12 . ARG B 1 90  ? -4.879 7.682   19.947  1.00 126.17 ? 90  ARG B HH12 1 
ATOM   3128 H HH21 . ARG B 1 90  ? -5.027 9.502   22.686  1.00 119.63 ? 90  ARG B HH21 1 
ATOM   3129 H HH22 . ARG B 1 90  ? -4.995 9.585   21.199  1.00 119.63 ? 90  ARG B HH22 1 
ATOM   3130 N N    . LEU B 1 91  ? 0.032  6.588   22.313  1.00 88.75  ? 91  LEU B N    1 
ATOM   3131 C CA   . LEU B 1 91  ? 0.721  6.978   21.085  1.00 95.32  ? 91  LEU B CA   1 
ATOM   3132 C C    . LEU B 1 91  ? 1.858  6.002   20.762  1.00 91.23  ? 91  LEU B C    1 
ATOM   3133 O O    . LEU B 1 91  ? 1.976  5.519   19.635  1.00 87.92  ? 91  LEU B O    1 
ATOM   3134 C CB   . LEU B 1 91  ? 1.275  8.411   21.192  1.00 96.84  ? 91  LEU B CB   1 
ATOM   3135 C CG   . LEU B 1 91  ? 0.457  9.677   21.470  1.00 95.66  ? 91  LEU B CG   1 
ATOM   3136 C CD1  . LEU B 1 91  ? 1.278  10.952  21.092  1.00 87.20  ? 91  LEU B CD1  1 
ATOM   3137 C CD2  . LEU B 1 91  ? -0.884 9.690   20.775  1.00 93.15  ? 91  LEU B CD2  1 
ATOM   3138 H H    . LEU B 1 91  ? -0.059 7.221   22.888  1.00 106.58 ? 91  LEU B H    1 
ATOM   3139 H HA   . LEU B 1 91  ? 0.074  6.964   20.362  1.00 114.46 ? 91  LEU B HA   1 
ATOM   3140 H HB2  . LEU B 1 91  ? 1.932  8.386   21.905  1.00 116.29 ? 91  LEU B HB2  1 
ATOM   3141 H HB3  . LEU B 1 91  ? 1.712  8.587   20.344  1.00 116.29 ? 91  LEU B HB3  1 
ATOM   3142 H HG   . LEU B 1 91  ? 0.267  9.688   22.421  1.00 114.87 ? 91  LEU B HG   1 
ATOM   3143 H HD11 . LEU B 1 91  ? 0.738  11.739  21.265  1.00 104.71 ? 91  LEU B HD11 1 
ATOM   3144 H HD12 . LEU B 1 91  ? 2.084  10.980  21.632  1.00 104.71 ? 91  LEU B HD12 1 
ATOM   3145 H HD13 . LEU B 1 91  ? 1.511  10.910  20.152  1.00 104.71 ? 91  LEU B HD13 1 
ATOM   3146 H HD21 . LEU B 1 91  ? -1.351 10.508  21.005  1.00 111.86 ? 91  LEU B HD21 1 
ATOM   3147 H HD22 . LEU B 1 91  ? -0.743 9.647   19.817  1.00 111.86 ? 91  LEU B HD22 1 
ATOM   3148 H HD23 . LEU B 1 91  ? -1.399 8.922   21.068  1.00 111.86 ? 91  LEU B HD23 1 
ATOM   3149 N N    . ARG B 1 92  ? 2.685  5.664   21.748  1.00 90.49  ? 92  ARG B N    1 
ATOM   3150 C CA   . ARG B 1 92  ? 3.806  4.774   21.477  1.00 87.27  ? 92  ARG B CA   1 
ATOM   3151 C C    . ARG B 1 92  ? 3.325  3.403   21.058  1.00 79.44  ? 92  ARG B C    1 
ATOM   3152 O O    . ARG B 1 92  ? 3.866  2.801   20.110  1.00 73.28  ? 92  ARG B O    1 
ATOM   3153 C CB   . ARG B 1 92  ? 4.706  4.652   22.695  1.00 94.26  ? 92  ARG B CB   1 
ATOM   3154 C CG   . ARG B 1 92  ? 5.396  5.951   22.987  1.00 96.30  ? 92  ARG B CG   1 
ATOM   3155 C CD   . ARG B 1 92  ? 6.244  5.901   24.221  1.00 97.74  ? 92  ARG B CD   1 
ATOM   3156 N NE   . ARG B 1 92  ? 6.723  7.244   24.522  1.00 101.99 ? 92  ARG B NE   1 
ATOM   3157 C CZ   . ARG B 1 92  ? 7.362  7.587   25.630  1.00 98.40  ? 92  ARG B CZ   1 
ATOM   3158 N NH1  . ARG B 1 92  ? 7.611  6.705   26.585  1.00 98.17  ? 92  ARG B NH1  1 
ATOM   3159 N NH2  . ARG B 1 92  ? 7.761  8.849   25.782  1.00 108.53 ? 92  ARG B NH2  1 
ATOM   3160 H H    . ARG B 1 92  ? 2.620  5.929   22.564  1.00 108.66 ? 92  ARG B H    1 
ATOM   3161 H HA   . ARG B 1 92  ? 4.328  5.159   20.756  1.00 104.81 ? 92  ARG B HA   1 
ATOM   3162 H HB2  . ARG B 1 92  ? 4.172  4.407   23.467  1.00 113.19 ? 92  ARG B HB2  1 
ATOM   3163 H HB3  . ARG B 1 92  ? 5.382  3.976   22.531  1.00 113.19 ? 92  ARG B HB3  1 
ATOM   3164 H HG2  . ARG B 1 92  ? 5.970  6.178   22.239  1.00 115.64 ? 92  ARG B HG2  1 
ATOM   3165 H HG3  . ARG B 1 92  ? 4.727  6.642   23.112  1.00 115.64 ? 92  ARG B HG3  1 
ATOM   3166 H HD2  . ARG B 1 92  ? 5.719  5.578   24.970  1.00 117.37 ? 92  ARG B HD2  1 
ATOM   3167 H HD3  . ARG B 1 92  ? 7.006  5.319   24.075  1.00 117.37 ? 92  ARG B HD3  1 
ATOM   3168 H HE   . ARG B 1 92  ? 6.581  7.859   23.937  1.00 122.47 ? 92  ARG B HE   1 
ATOM   3169 H HH11 . ARG B 1 92  ? 7.357  5.888   26.494  1.00 117.88 ? 92  ARG B HH11 1 
ATOM   3170 H HH12 . ARG B 1 92  ? 8.028  6.948   27.298  1.00 117.88 ? 92  ARG B HH12 1 
ATOM   3171 H HH21 . ARG B 1 92  ? 7.603  9.427   25.166  1.00 130.31 ? 92  ARG B HH21 1 
ATOM   3172 H HH22 . ARG B 1 92  ? 8.177  9.085   26.497  1.00 130.31 ? 92  ARG B HH22 1 
ATOM   3173 N N    . HIS B 1 93  ? 2.276  2.925   21.716  1.00 79.10  ? 93  HIS B N    1 
ATOM   3174 C CA   . HIS B 1 93  ? 1.780  1.594   21.419  1.00 79.03  ? 93  HIS B CA   1 
ATOM   3175 C C    . HIS B 1 93  ? 1.186  1.484   20.018  1.00 74.94  ? 93  HIS B C    1 
ATOM   3176 O O    . HIS B 1 93  ? 1.326  0.441   19.368  1.00 68.42  ? 93  HIS B O    1 
ATOM   3177 C CB   . HIS B 1 93  ? 0.709  1.222   22.407  1.00 81.32  ? 93  HIS B CB   1 
ATOM   3178 C CG   . HIS B 1 93  ? 0.153  -0.137  22.168  1.00 77.98  ? 93  HIS B CG   1 
ATOM   3179 N ND1  . HIS B 1 93  ? 0.657  -1.262  22.782  1.00 80.51  ? 93  HIS B ND1  1 
ATOM   3180 C CD2  . HIS B 1 93  ? -0.810 -0.558  21.308  1.00 76.95  ? 93  HIS B CD2  1 
ATOM   3181 C CE1  . HIS B 1 93  ? -0.019 -2.321  22.355  1.00 83.47  ? 93  HIS B CE1  1 
ATOM   3182 N NE2  . HIS B 1 93  ? -0.903 -1.921  21.455  1.00 81.26  ? 93  HIS B NE2  1 
ATOM   3183 H H    . HIS B 1 93  ? 1.843  3.345   22.329  1.00 95.00  ? 93  HIS B H    1 
ATOM   3184 H HA   . HIS B 1 93  ? 2.534  0.988   21.485  1.00 94.91  ? 93  HIS B HA   1 
ATOM   3185 H HB2  . HIS B 1 93  ? 1.084  1.239   23.302  1.00 97.66  ? 93  HIS B HB2  1 
ATOM   3186 H HB3  . HIS B 1 93  ? -0.018 1.860   22.340  1.00 97.66  ? 93  HIS B HB3  1 
ATOM   3187 H HD2  . HIS B 1 93  ? -1.309 -0.027  20.731  1.00 92.42  ? 93  HIS B HD2  1 
ATOM   3188 H HE1  . HIS B 1 93  ? 0.107  -3.197  22.640  1.00 100.24 ? 93  HIS B HE1  1 
ATOM   3189 H HE2  . HIS B 1 93  ? -1.449 -2.432  21.031  1.00 97.59  ? 93  HIS B HE2  1 
ATOM   3190 N N    . GLU B 1 94  ? 0.533  2.542   19.535  1.00 74.44  ? 94  GLU B N    1 
ATOM   3191 C CA   . GLU B 1 94  ? -0.087 2.498   18.214  1.00 76.53  ? 94  GLU B CA   1 
ATOM   3192 C C    . GLU B 1 94  ? 0.962  2.635   17.133  1.00 68.94  ? 94  GLU B C    1 
ATOM   3193 O O    . GLU B 1 94  ? 0.908  1.914   16.132  1.00 67.43  ? 94  GLU B O    1 
ATOM   3194 C CB   . GLU B 1 94  ? -1.148 3.589   18.100  1.00 78.47  ? 94  GLU B CB   1 
ATOM   3195 C CG   . GLU B 1 94  ? -2.340 3.327   19.022  1.00 83.85  ? 94  GLU B CG   1 
ATOM   3196 C CD   . GLU B 1 94  ? -3.481 4.325   18.871  1.00 81.30  ? 94  GLU B CD   1 
ATOM   3197 O OE1  . GLU B 1 94  ? -3.554 5.024   17.836  1.00 81.96  ? 94  GLU B OE1  1 
ATOM   3198 O OE2  . GLU B 1 94  ? -4.287 4.428   19.817  1.00 84.96  ? 94  GLU B OE2  1 
ATOM   3199 H H    . GLU B 1 94  ? 0.437  3.290   19.948  1.00 89.40  ? 94  GLU B H    1 
ATOM   3200 H HA   . GLU B 1 94  ? -0.539 1.648   18.089  1.00 91.91  ? 94  GLU B HA   1 
ATOM   3201 H HB2  . GLU B 1 94  ? -0.756 4.442   18.345  1.00 94.24  ? 94  GLU B HB2  1 
ATOM   3202 H HB3  . GLU B 1 94  ? -1.473 3.624   17.186  1.00 94.24  ? 94  GLU B HB3  1 
ATOM   3203 H HG2  . GLU B 1 94  ? -2.694 2.445   18.828  1.00 100.70 ? 94  GLU B HG2  1 
ATOM   3204 H HG3  . GLU B 1 94  ? -2.035 3.367   19.942  1.00 100.70 ? 94  GLU B HG3  1 
ATOM   3205 N N    . SER B 1 95  ? 1.906  3.559   17.322  1.00 69.16  ? 95  SER B N    1 
ATOM   3206 C CA   . SER B 1 95  ? 3.118  3.630   16.505  1.00 69.59  ? 95  SER B CA   1 
ATOM   3207 C C    . SER B 1 95  ? 3.724  2.263   16.233  1.00 68.20  ? 95  SER B C    1 
ATOM   3208 O O    . SER B 1 95  ? 3.956  1.875   15.078  1.00 68.14  ? 95  SER B O    1 
ATOM   3209 C CB   . SER B 1 95  ? 4.163  4.481   17.229  1.00 72.87  ? 95  SER B CB   1 
ATOM   3210 O OG   . SER B 1 95  ? 4.148  5.801   16.743  1.00 85.85  ? 95  SER B OG   1 
ATOM   3211 H H    . SER B 1 95  ? 1.869  4.167   17.929  1.00 83.07  ? 95  SER B H    1 
ATOM   3212 H HA   . SER B 1 95  ? 2.873  4.035   15.658  1.00 83.58  ? 95  SER B HA   1 
ATOM   3213 H HB2  . SER B 1 95  ? 3.962  4.490   18.177  1.00 87.53  ? 95  SER B HB2  1 
ATOM   3214 H HB3  . SER B 1 95  ? 5.041  4.098   17.080  1.00 87.53  ? 95  SER B HB3  1 
ATOM   3215 H HG   . SER B 1 95  ? 4.750  6.252   17.117  1.00 103.10 ? 95  SER B HG   1 
ATOM   3216 N N    . TRP B 1 96  ? 4.065  1.553   17.292  1.00 67.04  ? 96  TRP B N    1 
ATOM   3217 C CA   . TRP B 1 96  ? 4.733  0.276   17.134  1.00 62.51  ? 96  TRP B CA   1 
ATOM   3218 C C    . TRP B 1 96  ? 3.786  -0.787  16.609  1.00 65.07  ? 96  TRP B C    1 
ATOM   3219 O O    . TRP B 1 96  ? 4.264  -1.835  16.162  1.00 65.59  ? 96  TRP B O    1 
ATOM   3220 C CB   . TRP B 1 96  ? 5.365  -0.136  18.463  1.00 64.55  ? 96  TRP B CB   1 
ATOM   3221 C CG   . TRP B 1 96  ? 6.693  0.567   18.671  1.00 64.43  ? 96  TRP B CG   1 
ATOM   3222 C CD1  . TRP B 1 96  ? 6.943  1.652   19.474  1.00 70.05  ? 96  TRP B CD1  1 
ATOM   3223 C CD2  . TRP B 1 96  ? 7.933  0.226   18.065  1.00 62.30  ? 96  TRP B CD2  1 
ATOM   3224 N NE1  . TRP B 1 96  ? 8.267  2.017   19.382  1.00 63.83  ? 96  TRP B NE1  1 
ATOM   3225 C CE2  . TRP B 1 96  ? 8.897  1.154   18.526  1.00 62.74  ? 96  TRP B CE2  1 
ATOM   3226 C CE3  . TRP B 1 96  ? 8.323  -0.755  17.147  1.00 63.66  ? 96  TRP B CE3  1 
ATOM   3227 C CZ2  . TRP B 1 96  ? 10.228 1.119   18.109  1.00 60.25  ? 96  TRP B CZ2  1 
ATOM   3228 C CZ3  . TRP B 1 96  ? 9.655  -0.770  16.723  1.00 59.88  ? 96  TRP B CZ3  1 
ATOM   3229 C CH2  . TRP B 1 96  ? 10.579 0.170   17.201  1.00 54.19  ? 96  TRP B CH2  1 
ATOM   3230 H H    . TRP B 1 96  ? 3.922  1.786   18.108  1.00 80.52  ? 96  TRP B H    1 
ATOM   3231 H HA   . TRP B 1 96  ? 5.457  0.351   16.492  1.00 75.10  ? 96  TRP B HA   1 
ATOM   3232 H HB2  . TRP B 1 96  ? 4.772  0.106   19.192  1.00 77.54  ? 96  TRP B HB2  1 
ATOM   3233 H HB3  . TRP B 1 96  ? 5.520  -1.093  18.465  1.00 77.54  ? 96  TRP B HB3  1 
ATOM   3234 H HD1  . TRP B 1 96  ? 6.309  2.079   20.004  1.00 84.14  ? 96  TRP B HD1  1 
ATOM   3235 H HE1  . TRP B 1 96  ? 8.636  2.676   19.793  1.00 76.67  ? 96  TRP B HE1  1 
ATOM   3236 H HE3  . TRP B 1 96  ? 7.714  -1.381  16.827  1.00 76.47  ? 96  TRP B HE3  1 
ATOM   3237 H HZ2  . TRP B 1 96  ? 10.853 1.722   18.441  1.00 72.38  ? 96  TRP B HZ2  1 
ATOM   3238 H HZ3  . TRP B 1 96  ? 9.934  -1.414  16.113  1.00 71.94  ? 96  TRP B HZ3  1 
ATOM   3239 H HH2  . TRP B 1 96  ? 11.454 0.144   16.889  1.00 65.10  ? 96  TRP B HH2  1 
ATOM   3240 N N    . SER B 1 97  ? 2.460  -0.583  16.707  1.00 64.35  ? 97  SER B N    1 
ATOM   3241 C CA   . SER B 1 97  ? 1.552  -1.428  15.940  1.00 69.90  ? 97  SER B CA   1 
ATOM   3242 C C    . SER B 1 97  ? 1.695  -1.158  14.434  1.00 65.02  ? 97  SER B C    1 
ATOM   3243 O O    . SER B 1 97  ? 1.767  -2.095  13.634  1.00 68.25  ? 97  SER B O    1 
ATOM   3244 C CB   . SER B 1 97  ? 0.103  -1.213  16.374  1.00 71.56  ? 97  SER B CB   1 
ATOM   3245 O OG   . SER B 1 97  ? -0.171 -1.917  17.590  1.00 71.32  ? 97  SER B OG   1 
ATOM   3246 H H    . SER B 1 97  ? 2.083  0.018   17.194  1.00 77.29  ? 97  SER B H    1 
ATOM   3247 H HA   . SER B 1 97  ? 1.780  -2.353  16.120  1.00 83.96  ? 97  SER B HA   1 
ATOM   3248 H HB2  . SER B 1 97  ? -0.047 -0.265  16.517  1.00 85.95  ? 97  SER B HB2  1 
ATOM   3249 H HB3  . SER B 1 97  ? -0.487 -1.541  15.678  1.00 85.95  ? 97  SER B HB3  1 
ATOM   3250 H HG   . SER B 1 97  ? 0.391  -1.706  18.177  1.00 85.67  ? 97  SER B HG   1 
ATOM   3251 N N    . ARG B 1 98  ? 1.723  0.119   14.036  1.00 60.82  ? 98  ARG B N    1 
ATOM   3252 C CA   . ARG B 1 98  ? 1.822  0.438   12.615  1.00 70.34  ? 98  ARG B CA   1 
ATOM   3253 C C    . ARG B 1 98  ? 3.117  -0.117  12.013  1.00 62.91  ? 98  ARG B C    1 
ATOM   3254 O O    . ARG B 1 98  ? 3.135  -0.524  10.863  1.00 60.63  ? 98  ARG B O    1 
ATOM   3255 C CB   . ARG B 1 98  ? 1.747  1.952   12.381  1.00 68.98  ? 98  ARG B CB   1 
ATOM   3256 C CG   . ARG B 1 98  ? 0.627  2.693   13.154  1.00 70.97  ? 98  ARG B CG   1 
ATOM   3257 C CD   . ARG B 1 98  ? 0.278  4.027   12.462  1.00 67.46  ? 98  ARG B CD   1 
ATOM   3258 N NE   . ARG B 1 98  ? 1.438  4.914   12.365  1.00 69.57  ? 98  ARG B NE   1 
ATOM   3259 C CZ   . ARG B 1 98  ? 1.716  5.879   13.225  1.00 75.37  ? 98  ARG B CZ   1 
ATOM   3260 N NH1  . ARG B 1 98  ? 0.927  6.128   14.266  1.00 68.14  ? 98  ARG B NH1  1 
ATOM   3261 N NH2  . ARG B 1 98  ? 2.802  6.623   13.028  1.00 76.16  ? 98  ARG B NH2  1 
ATOM   3262 H H    . ARG B 1 98  ? 1.686  0.801   14.558  1.00 73.06  ? 98  ARG B H    1 
ATOM   3263 H HA   . ARG B 1 98  ? 1.065  0.031   12.165  1.00 84.48  ? 98  ARG B HA   1 
ATOM   3264 H HB2  . ARG B 1 98  ? 2.592  2.344   12.651  1.00 82.86  ? 98  ARG B HB2  1 
ATOM   3265 H HB3  . ARG B 1 98  ? 1.597  2.107   11.435  1.00 82.86  ? 98  ARG B HB3  1 
ATOM   3266 H HG2  . ARG B 1 98  ? -0.170 2.141   13.178  1.00 85.24  ? 98  ARG B HG2  1 
ATOM   3267 H HG3  . ARG B 1 98  ? 0.927  2.883   14.057  1.00 85.24  ? 98  ARG B HG3  1 
ATOM   3268 H HD2  . ARG B 1 98  ? -0.041 3.847   11.564  1.00 81.03  ? 98  ARG B HD2  1 
ATOM   3269 H HD3  . ARG B 1 98  ? -0.409 4.482   12.974  1.00 81.03  ? 98  ARG B HD3  1 
ATOM   3270 H HE   . ARG B 1 98  ? 1.975  4.800   11.704  1.00 83.56  ? 98  ARG B HE   1 
ATOM   3271 H HH11 . ARG B 1 98  ? 0.219  5.657   14.392  1.00 81.85  ? 98  ARG B HH11 1 
ATOM   3272 H HH12 . ARG B 1 98  ? 1.125  6.761   14.815  1.00 81.85  ? 98  ARG B HH12 1 
ATOM   3273 H HH21 . ARG B 1 98  ? 3.310  6.472   12.351  1.00 91.47  ? 98  ARG B HH21 1 
ATOM   3274 H HH22 . ARG B 1 98  ? 2.996  7.254   13.579  1.00 91.47  ? 98  ARG B HH22 1 
ATOM   3275 N N    . VAL B 1 99  ? 4.206  -0.104  12.794  1.00 61.83  ? 99  VAL B N    1 
ATOM   3276 C CA   . VAL B 1 99  ? 5.512  -0.585  12.362  1.00 57.34  ? 99  VAL B CA   1 
ATOM   3277 C C    . VAL B 1 99  ? 5.517  -2.101  12.169  1.00 58.80  ? 99  VAL B C    1 
ATOM   3278 O O    . VAL B 1 99  ? 6.087  -2.616  11.202  1.00 55.81  ? 99  VAL B O    1 
ATOM   3279 C CB   . VAL B 1 99  ? 6.575  -0.141  13.391  1.00 54.05  ? 99  VAL B CB   1 
ATOM   3280 C CG1  . VAL B 1 99  ? 7.839  -0.911  13.157  1.00 55.98  ? 99  VAL B CG1  1 
ATOM   3281 C CG2  . VAL B 1 99  ? 6.817  1.360   13.324  1.00 50.54  ? 99  VAL B CG2  1 
ATOM   3282 H H    . VAL B 1 99  ? 4.210  0.189   13.603  1.00 74.28  ? 99  VAL B H    1 
ATOM   3283 H HA   . VAL B 1 99  ? 5.716  -0.193  11.499  1.00 68.88  ? 99  VAL B HA   1 
ATOM   3284 H HB   . VAL B 1 99  ? 6.257  -0.329  14.288  1.00 64.94  ? 99  VAL B HB   1 
ATOM   3285 H HG11 . VAL B 1 99  ? 8.572  -0.458  13.603  1.00 67.25  ? 99  VAL B HG11 1 
ATOM   3286 H HG12 . VAL B 1 99  ? 7.735  -1.805  13.518  1.00 67.25  ? 99  VAL B HG12 1 
ATOM   3287 H HG13 . VAL B 1 99  ? 8.009  -0.956  12.204  1.00 67.25  ? 99  VAL B HG13 1 
ATOM   3288 H HG21 . VAL B 1 99  ? 7.474  1.604   13.994  1.00 60.26  ? 99  VAL B HG21 1 
ATOM   3289 H HG22 . VAL B 1 99  ? 7.145  1.587   12.440  1.00 60.26  ? 99  VAL B HG22 1 
ATOM   3290 H HG23 . VAL B 1 99  ? 5.981  1.822   13.495  1.00 60.26  ? 99  VAL B HG23 1 
ATOM   3291 N N    . ASP B 1 100 ? 4.913  -2.848  13.073  1.00 57.68  ? 100 ASP B N    1 
ATOM   3292 C CA   . ASP B 1 100 ? 4.992  -4.294  12.920  1.00 62.14  ? 100 ASP B CA   1 
ATOM   3293 C C    . ASP B 1 100 ? 4.177  -4.751  11.716  1.00 63.14  ? 100 ASP B C    1 
ATOM   3294 O O    . ASP B 1 100 ? 4.455  -5.800  11.101  1.00 59.27  ? 100 ASP B O    1 
ATOM   3295 C CB   . ASP B 1 100 ? 4.516  -4.976  14.192  1.00 64.47  ? 100 ASP B CB   1 
ATOM   3296 C CG   . ASP B 1 100 ? 5.526  -4.824  15.342  1.00 73.83  ? 100 ASP B CG   1 
ATOM   3297 O OD1  . ASP B 1 100 ? 6.754  -4.766  15.061  1.00 72.25  ? 100 ASP B OD1  1 
ATOM   3298 O OD2  . ASP B 1 100 ? 5.075  -4.764  16.514  1.00 71.56  ? 100 ASP B OD2  1 
ATOM   3299 H H    . ASP B 1 100 ? 4.471  -2.562  13.753  1.00 69.30  ? 100 ASP B H    1 
ATOM   3300 H HA   . ASP B 1 100 ? 5.915  -4.559  12.778  1.00 74.65  ? 100 ASP B HA   1 
ATOM   3301 H HB2  . ASP B 1 100 ? 3.676  -4.579  14.471  1.00 77.44  ? 100 ASP B HB2  1 
ATOM   3302 H HB3  . ASP B 1 100 ? 4.394  -5.923  14.019  1.00 77.44  ? 100 ASP B HB3  1 
ATOM   3303 N N    . LYS B 1 101 ? 3.137  -4.002  11.384  1.00 63.35  ? 101 LYS B N    1 
ATOM   3304 C CA   . LYS B 1 101 ? 2.387  -4.331  10.182  1.00 68.58  ? 101 LYS B CA   1 
ATOM   3305 C C    . LYS B 1 101 ? 3.237  -4.028  8.951   1.00 65.57  ? 101 LYS B C    1 
ATOM   3306 O O    . LYS B 1 101 ? 3.297  -4.835  8.015   1.00 66.56  ? 101 LYS B O    1 
ATOM   3307 C CB   . LYS B 1 101 ? 1.033  -3.605  10.209  1.00 68.88  ? 101 LYS B CB   1 
ATOM   3308 C CG   . LYS B 1 101 ? 0.107  -3.890  9.012   1.00 75.55  ? 101 LYS B CG   1 
ATOM   3309 C CD   . LYS B 1 101 ? -0.349 -5.370  8.901   1.00 78.46  ? 101 LYS B CD   1 
ATOM   3310 C CE   . LYS B 1 101 ? -1.150 -5.632  7.587   1.00 83.72  ? 101 LYS B CE   1 
ATOM   3311 N NZ   . LYS B 1 101 ? -1.630 -7.058  7.401   1.00 78.54  ? 101 LYS B NZ   1 
ATOM   3312 H H    . LYS B 1 101 ? 2.853  -3.319  11.823  1.00 76.09  ? 101 LYS B H    1 
ATOM   3313 H HA   . LYS B 1 101 ? 2.169  -5.275  10.142  1.00 82.38  ? 101 LYS B HA   1 
ATOM   3314 H HB2  . LYS B 1 101 ? 0.559  -3.872  11.011  1.00 82.73  ? 101 LYS B HB2  1 
ATOM   3315 H HB3  . LYS B 1 101 ? 1.199  -2.649  10.224  1.00 82.73  ? 101 LYS B HB3  1 
ATOM   3316 H HG2  . LYS B 1 101 ? -0.690 -3.343  9.098   1.00 90.73  ? 101 LYS B HG2  1 
ATOM   3317 H HG3  . LYS B 1 101 ? 0.576  -3.665  8.194   1.00 90.73  ? 101 LYS B HG3  1 
ATOM   3318 H HD2  . LYS B 1 101 ? 0.431  -5.946  8.902   1.00 94.24  ? 101 LYS B HD2  1 
ATOM   3319 H HD3  . LYS B 1 101 ? -0.922 -5.586  9.654   1.00 94.24  ? 101 LYS B HD3  1 
ATOM   3320 H HE2  . LYS B 1 101 ? -1.933 -5.060  7.584   1.00 100.55 ? 101 LYS B HE2  1 
ATOM   3321 H HE3  . LYS B 1 101 ? -0.580 -5.417  6.832   1.00 100.55 ? 101 LYS B HE3  1 
ATOM   3322 H HZ1  . LYS B 1 101 ? -2.080 -7.131  6.637   1.00 94.33  ? 101 LYS B HZ1  1 
ATOM   3323 H HZ2  . LYS B 1 101 ? -0.934 -7.613  7.381   1.00 94.33  ? 101 LYS B HZ2  1 
ATOM   3324 H HZ3  . LYS B 1 101 ? -2.164 -7.290  8.075   1.00 94.33  ? 101 LYS B HZ3  1 
ATOM   3325 N N    . ILE B 1 102 ? 3.934  -2.902  8.940   1.00 55.63  ? 102 ILE B N    1 
ATOM   3326 C CA   . ILE B 1 102 ? 4.859  -2.642  7.828   1.00 56.08  ? 102 ILE B CA   1 
ATOM   3327 C C    . ILE B 1 102 ? 5.784  -3.833  7.616   1.00 53.62  ? 102 ILE B C    1 
ATOM   3328 O O    . ILE B 1 102 ? 5.915  -4.344  6.510   1.00 53.93  ? 102 ILE B O    1 
ATOM   3329 C CB   . ILE B 1 102 ? 5.666  -1.364  8.087   1.00 53.96  ? 102 ILE B CB   1 
ATOM   3330 C CG1  . ILE B 1 102 ? 4.737  -0.156  8.011   1.00 53.58  ? 102 ILE B CG1  1 
ATOM   3331 C CG2  . ILE B 1 102 ? 6.770  -1.288  7.081   1.00 52.31  ? 102 ILE B CG2  1 
ATOM   3332 C CD1  . ILE B 1 102 ? 5.479  1.162   8.226   1.00 52.00  ? 102 ILE B CD1  1 
ATOM   3333 H H    . ILE B 1 102 ? 3.897  -2.287  9.540   1.00 66.84  ? 102 ILE B H    1 
ATOM   3334 H HA   . ILE B 1 102 ? 4.334  -2.514  7.022   1.00 67.37  ? 102 ILE B HA   1 
ATOM   3335 H HB   . ILE B 1 102 ? 6.058  -1.376  8.974   1.00 64.83  ? 102 ILE B HB   1 
ATOM   3336 H HG12 . ILE B 1 102 ? 4.322  -0.129  7.135   1.00 64.37  ? 102 ILE B HG12 1 
ATOM   3337 H HG13 . ILE B 1 102 ? 4.057  -0.235  8.698   1.00 64.37  ? 102 ILE B HG13 1 
ATOM   3338 H HG21 . ILE B 1 102 ? 7.163  -0.402  7.109   1.00 62.85  ? 102 ILE B HG21 1 
ATOM   3339 H HG22 . ILE B 1 102 ? 7.441  -1.954  7.298   1.00 62.85  ? 102 ILE B HG22 1 
ATOM   3340 H HG23 . ILE B 1 102 ? 6.406  -1.461  6.198   1.00 62.85  ? 102 ILE B HG23 1 
ATOM   3341 H HD11 . ILE B 1 102 ? 4.843  1.842   8.499   1.00 62.01  ? 102 ILE B HD11 1 
ATOM   3342 H HD12 . ILE B 1 102 ? 6.148  1.039   8.918   1.00 62.01  ? 102 ILE B HD12 1 
ATOM   3343 H HD13 . ILE B 1 102 ? 5.907  1.423   7.396   1.00 62.01  ? 102 ILE B HD13 1 
ATOM   3344 N N    . ILE B 1 103 ? 6.368  -4.350  8.690   1.00 56.75  ? 103 ILE B N    1 
ATOM   3345 C CA   . ILE B 1 103 ? 7.273  -5.497  8.574   1.00 58.56  ? 103 ILE B CA   1 
ATOM   3346 C C    . ILE B 1 103 ? 6.504  -6.728  8.132   1.00 60.83  ? 103 ILE B C    1 
ATOM   3347 O O    . ILE B 1 103 ? 6.936  -7.481  7.243   1.00 58.48  ? 103 ILE B O    1 
ATOM   3348 C CB   . ILE B 1 103 ? 7.982  -5.741  9.918   1.00 55.88  ? 103 ILE B CB   1 
ATOM   3349 C CG1  . ILE B 1 103 ? 9.193  -4.827  10.012  1.00 55.03  ? 103 ILE B CG1  1 
ATOM   3350 C CG2  . ILE B 1 103 ? 8.417  -7.165  10.026  1.00 58.76  ? 103 ILE B CG2  1 
ATOM   3351 C CD1  . ILE B 1 103 ? 8.971  -3.636  10.847  1.00 57.23  ? 103 ILE B CD1  1 
ATOM   3352 H H    . ILE B 1 103 ? 6.261  -4.061  9.493   1.00 68.17  ? 103 ILE B H    1 
ATOM   3353 H HA   . ILE B 1 103 ? 7.945  -5.298  7.903   1.00 70.35  ? 103 ILE B HA   1 
ATOM   3354 H HB   . ILE B 1 103 ? 7.366  -5.549  10.642  1.00 67.13  ? 103 ILE B HB   1 
ATOM   3355 H HG12 . ILE B 1 103 ? 9.931  -5.325  10.396  1.00 66.11  ? 103 ILE B HG12 1 
ATOM   3356 H HG13 . ILE B 1 103 ? 9.426  -4.525  9.120   1.00 66.11  ? 103 ILE B HG13 1 
ATOM   3357 H HG21 . ILE B 1 103 ? 9.063  -7.245  10.744  1.00 70.59  ? 103 ILE B HG21 1 
ATOM   3358 H HG22 . ILE B 1 103 ? 7.642  -7.718  10.215  1.00 70.59  ? 103 ILE B HG22 1 
ATOM   3359 H HG23 . ILE B 1 103 ? 8.820  -7.437  9.187   1.00 70.59  ? 103 ILE B HG23 1 
ATOM   3360 H HD11 . ILE B 1 103 ? 9.804  -3.145  10.924  1.00 68.75  ? 103 ILE B HD11 1 
ATOM   3361 H HD12 . ILE B 1 103 ? 8.296  -3.079  10.429  1.00 68.75  ? 103 ILE B HD12 1 
ATOM   3362 H HD13 . ILE B 1 103 ? 8.670  -3.918  11.725  1.00 68.75  ? 103 ILE B HD13 1 
ATOM   3363 N N    . GLU B 1 104 ? 5.326  -6.935  8.707   1.00 60.94  ? 104 GLU B N    1 
ATOM   3364 C CA   . GLU B 1 104 ? 4.469  -8.019  8.239   1.00 64.16  ? 104 GLU B CA   1 
ATOM   3365 C C    . GLU B 1 104 ? 4.294  -7.962  6.709   1.00 64.84  ? 104 GLU B C    1 
ATOM   3366 O O    . GLU B 1 104 ? 4.479  -8.957  6.006   1.00 66.86  ? 104 GLU B O    1 
ATOM   3367 C CB   . GLU B 1 104 ? 3.167  -7.886  9.010   1.00 64.54  ? 104 GLU B CB   1 
ATOM   3368 C CG   . GLU B 1 104 ? 2.160  -8.963  8.856   1.00 76.76  ? 104 GLU B CG   1 
ATOM   3369 C CD   . GLU B 1 104 ? 0.900  -8.651  9.670   1.00 84.39  ? 104 GLU B CD   1 
ATOM   3370 O OE1  . GLU B 1 104 ? 1.024  -8.255  10.873  1.00 81.75  ? 104 GLU B OE1  1 
ATOM   3371 O OE2  . GLU B 1 104 ? -0.213 -8.752  9.090   1.00 85.95  ? 104 GLU B OE2  1 
ATOM   3372 H H    . GLU B 1 104 ? 5.004  -6.472  9.357   1.00 73.21  ? 104 GLU B H    1 
ATOM   3373 H HA   . GLU B 1 104 ? 4.844  -8.896  8.413   1.00 77.07  ? 104 GLU B HA   1 
ATOM   3374 H HB2  . GLU B 1 104 ? 3.385  -7.841  9.954   1.00 77.53  ? 104 GLU B HB2  1 
ATOM   3375 H HB3  . GLU B 1 104 ? 2.739  -7.062  8.729   1.00 77.53  ? 104 GLU B HB3  1 
ATOM   3376 H HG2  . GLU B 1 104 ? 1.911  -9.043  7.922   1.00 92.19  ? 104 GLU B HG2  1 
ATOM   3377 H HG3  . GLU B 1 104 ? 2.531  -9.802  9.173   1.00 92.19  ? 104 GLU B HG3  1 
ATOM   3378 N N    . ASN B 1 105 ? 4.029  -6.782  6.163   1.00 60.94  ? 105 ASN B N    1 
ATOM   3379 C CA   . ASN B 1 105 ? 3.825  -6.704  4.725   1.00 59.75  ? 105 ASN B CA   1 
ATOM   3380 C C    . ASN B 1 105 ? 5.116  -6.881  3.936   1.00 65.17  ? 105 ASN B C    1 
ATOM   3381 O O    . ASN B 1 105 ? 5.081  -7.376  2.803   1.00 69.21  ? 105 ASN B O    1 
ATOM   3382 C CB   . ASN B 1 105 ? 3.199  -5.362  4.351   1.00 61.98  ? 105 ASN B CB   1 
ATOM   3383 C CG   . ASN B 1 105 ? 1.759  -5.207  4.842   1.00 68.20  ? 105 ASN B CG   1 
ATOM   3384 O OD1  . ASN B 1 105 ? 1.117  -6.173  5.281   1.00 71.41  ? 105 ASN B OD1  1 
ATOM   3385 N ND2  . ASN B 1 105 ? 1.245  -3.978  4.767   1.00 60.10  ? 105 ASN B ND2  1 
ATOM   3386 H H    . ASN B 1 105 ? 3.964  -6.037  6.587   1.00 73.20  ? 105 ASN B H    1 
ATOM   3387 H HA   . ASN B 1 105 ? 3.219  -7.421  4.481   1.00 71.78  ? 105 ASN B HA   1 
ATOM   3388 H HB2  . ASN B 1 105 ? 3.725  -4.649  4.745   1.00 74.46  ? 105 ASN B HB2  1 
ATOM   3389 H HB3  . ASN B 1 105 ? 3.194  -5.276  3.385   1.00 74.46  ? 105 ASN B HB3  1 
ATOM   3390 H HD21 . ASN B 1 105 ? 0.439  -3.832  5.029   1.00 72.20  ? 105 ASN B HD21 1 
ATOM   3391 H HD22 . ASN B 1 105 ? 1.720  -3.332  4.456   1.00 72.20  ? 105 ASN B HD22 1 
ATOM   3392 N N    . LEU B 1 106 ? 6.250  -6.426  4.477   1.00 58.28  ? 106 LEU B N    1 
ATOM   3393 C CA   . LEU B 1 106 ? 7.502  -6.610  3.772   1.00 59.46  ? 106 LEU B CA   1 
ATOM   3394 C C    . LEU B 1 106 ? 7.779  -8.079  3.516   1.00 64.93  ? 106 LEU B C    1 
ATOM   3395 O O    . LEU B 1 106 ? 8.270  -8.444  2.437   1.00 66.35  ? 106 LEU B O    1 
ATOM   3396 C CB   . LEU B 1 106 ? 8.643  -5.982  4.560   1.00 58.21  ? 106 LEU B CB   1 
ATOM   3397 C CG   . LEU B 1 106 ? 8.798  -4.468  4.517   1.00 58.19  ? 106 LEU B CG   1 
ATOM   3398 C CD1  . LEU B 1 106 ? 9.859  -4.142  5.561   1.00 52.48  ? 106 LEU B CD1  1 
ATOM   3399 C CD2  . LEU B 1 106 ? 9.197  -3.889  3.171   1.00 52.76  ? 106 LEU B CD2  1 
ATOM   3400 H H    . LEU B 1 106 ? 6.313  -6.019  5.232   1.00 70.01  ? 106 LEU B H    1 
ATOM   3401 H HA   . LEU B 1 106 ? 7.445  -6.161  2.914   1.00 71.43  ? 106 LEU B HA   1 
ATOM   3402 H HB2  . LEU B 1 106 ? 8.523  -6.222  5.492   1.00 69.93  ? 106 LEU B HB2  1 
ATOM   3403 H HB3  . LEU B 1 106 ? 9.473  -6.356  4.225   1.00 69.93  ? 106 LEU B HB3  1 
ATOM   3404 H HG   . LEU B 1 106 ? 7.938  -4.055  4.691   1.00 69.91  ? 106 LEU B HG   1 
ATOM   3405 H HD11 . LEU B 1 106 ? 10.031 -3.188  5.548   1.00 63.06  ? 106 LEU B HD11 1 
ATOM   3406 H HD12 . LEU B 1 106 ? 9.534  -4.408  6.435   1.00 63.06  ? 106 LEU B HD12 1 
ATOM   3407 H HD13 . LEU B 1 106 ? 10.671 -4.628  5.348   1.00 63.06  ? 106 LEU B HD13 1 
ATOM   3408 H HD21 . LEU B 1 106 ? 9.368  -2.940  3.274   1.00 62.92  ? 106 LEU B HD21 1 
ATOM   3409 H HD22 . LEU B 1 106 ? 9.999  -4.338  2.860   1.00 62.92  ? 106 LEU B HD22 1 
ATOM   3410 H HD23 . LEU B 1 106 ? 8.474  -4.030  2.540   1.00 62.92  ? 106 LEU B HD23 1 
ATOM   3411 N N    . GLU B 1 107 ? 7.490  -8.936  4.508   1.00 66.08  ? 107 GLU B N    1 
ATOM   3412 C CA   . GLU B 1 107 ? 7.661  -10.383 4.342   1.00 70.59  ? 107 GLU B CA   1 
ATOM   3413 C C    . GLU B 1 107 ? 6.696  -10.966 3.325   1.00 75.67  ? 107 GLU B C    1 
ATOM   3414 O O    . GLU B 1 107 ? 7.038  -11.919 2.618   1.00 84.04  ? 107 GLU B O    1 
ATOM   3415 C CB   . GLU B 1 107 ? 7.498  -11.084 5.700   1.00 74.68  ? 107 GLU B CB   1 
ATOM   3416 C CG   . GLU B 1 107 ? 8.387  -10.475 6.827   1.00 73.14  ? 107 GLU B CG   1 
ATOM   3417 C CD   . GLU B 1 107 ? 8.295  -11.190 8.204   1.00 75.36  ? 107 GLU B CD   1 
ATOM   3418 O OE1  . GLU B 1 107 ? 7.420  -12.081 8.362   1.00 84.16  ? 107 GLU B OE1  1 
ATOM   3419 O OE2  . GLU B 1 107 ? 9.156  -10.880 9.106   1.00 69.52  ? 107 GLU B OE2  1 
ATOM   3420 H H    . GLU B 1 107 ? 7.195  -8.705  5.282   1.00 79.37  ? 107 GLU B H    1 
ATOM   3421 H HA   . GLU B 1 107 ? 8.558  -10.547 4.011   1.00 84.79  ? 107 GLU B HA   1 
ATOM   3422 H HB2  . GLU B 1 107 ? 6.573  -11.011 5.980   1.00 89.70  ? 107 GLU B HB2  1 
ATOM   3423 H HB3  . GLU B 1 107 ? 7.742  -12.017 5.601   1.00 89.70  ? 107 GLU B HB3  1 
ATOM   3424 H HG2  . GLU B 1 107 ? 9.313  -10.515 6.541   1.00 87.85  ? 107 GLU B HG2  1 
ATOM   3425 H HG3  . GLU B 1 107 ? 8.121  -9.552  6.962   1.00 87.85  ? 107 GLU B HG3  1 
ATOM   3426 N N    . ALA B 1 108 ? 5.476  -10.451 3.259   1.00 74.27  ? 108 ALA B N    1 
ATOM   3427 C CA   . ALA B 1 108 ? 4.528  -10.974 2.274   1.00 76.58  ? 108 ALA B CA   1 
ATOM   3428 C C    . ALA B 1 108 ? 4.835  -10.510 0.861   1.00 81.90  ? 108 ALA B C    1 
ATOM   3429 O O    . ALA B 1 108 ? 4.769  -11.298 -0.084  1.00 86.76  ? 108 ALA B O    1 
ATOM   3430 C CB   . ALA B 1 108 ? 3.087  -10.587 2.619   1.00 74.80  ? 108 ALA B CB   1 
ATOM   3431 H H    . ALA B 1 108 ? 5.177  -9.816  3.755   1.00 89.20  ? 108 ALA B H    1 
ATOM   3432 H HA   . ALA B 1 108 ? 4.607  -11.940 2.309   1.00 91.97  ? 108 ALA B HA   1 
ATOM   3433 H HB1  . ALA B 1 108 ? 2.489  -10.978 1.964   1.00 89.83  ? 108 ALA B HB1  1 
ATOM   3434 H HB2  . ALA B 1 108 ? 2.873  -10.922 3.504   1.00 89.83  ? 108 ALA B HB2  1 
ATOM   3435 H HB3  . ALA B 1 108 ? 3.007  -9.620  2.604   1.00 89.83  ? 108 ALA B HB3  1 
ATOM   3436 N N    . ASN B 1 109 ? 5.121  -9.226  0.682   1.00 76.11  ? 109 ASN B N    1 
ATOM   3437 C CA   . ASN B 1 109 ? 5.355  -8.722  -0.662  1.00 80.92  ? 109 ASN B CA   1 
ATOM   3438 C C    . ASN B 1 109 ? 6.493  -9.452  -1.356  1.00 87.85  ? 109 ASN B C    1 
ATOM   3439 O O    . ASN B 1 109 ? 6.494  -9.542  -2.592  1.00 92.45  ? 109 ASN B O    1 
ATOM   3440 C CB   . ASN B 1 109 ? 5.630  -7.224  -0.619  1.00 76.46  ? 109 ASN B CB   1 
ATOM   3441 C CG   . ASN B 1 109 ? 4.377  -6.419  -0.341  1.00 75.97  ? 109 ASN B CG   1 
ATOM   3442 O OD1  . ASN B 1 109 ? 3.252  -6.920  -0.470  1.00 79.91  ? 109 ASN B OD1  1 
ATOM   3443 N ND2  . ASN B 1 109 ? 4.554  -5.183  0.069   1.00 63.13  ? 109 ASN B ND2  1 
ATOM   3444 H H    . ASN B 1 109 ? 5.184  -8.639  1.308   1.00 91.41  ? 109 ASN B H    1 
ATOM   3445 H HA   . ASN B 1 109 ? 4.554  -8.857  -1.192  1.00 97.18  ? 109 ASN B HA   1 
ATOM   3446 H HB2  . ASN B 1 109 ? 6.271  -7.038  0.085   1.00 91.83  ? 109 ASN B HB2  1 
ATOM   3447 H HB3  . ASN B 1 109 ? 5.987  -6.941  -1.475  1.00 91.83  ? 109 ASN B HB3  1 
ATOM   3448 H HD21 . ASN B 1 109 ? 3.874  -4.685  0.240   1.00 75.84  ? 109 ASN B HD21 1 
ATOM   3449 H HD22 . ASN B 1 109 ? 5.350  -4.873  0.166   1.00 75.84  ? 109 ASN B HD22 1 
ATOM   3450 N N    . LYS B 1 110 ? 7.412  -10.045 -0.591  1.00 93.91  ? 110 LYS B N    1 
ATOM   3451 C CA   . LYS B 1 110 ? 8.485  -10.812 -1.212  1.00 96.55  ? 110 LYS B CA   1 
ATOM   3452 C C    . LYS B 1 110 ? 7.931  -11.967 -2.043  1.00 103.34 ? 110 LYS B C    1 
ATOM   3453 O O    . LYS B 1 110 ? 8.525  -12.338 -3.061  1.00 101.66 ? 110 LYS B O    1 
ATOM   3454 C CB   . LYS B 1 110 ? 9.452  -11.318 -0.138  1.00 93.12  ? 110 LYS B CB   1 
ATOM   3455 C CG   . LYS B 1 110 ? 10.517 -10.307 0.273   1.00 91.33  ? 110 LYS B CG   1 
ATOM   3456 C CD   . LYS B 1 110 ? 11.403 -9.820  -0.933  1.00 92.68  ? 110 LYS B CD   1 
ATOM   3457 C CE   . LYS B 1 110 ? 12.539 -8.838  -0.546  1.00 85.38  ? 110 LYS B CE   1 
ATOM   3458 N NZ   . LYS B 1 110 ? 12.128 -7.555  0.197   1.00 87.61  ? 110 LYS B NZ   1 
ATOM   3459 H H    . LYS B 1 110 ? 7.435  -10.019 0.268   1.00 112.77 ? 110 LYS B H    1 
ATOM   3460 H HA   . LYS B 1 110 ? 8.988  -10.236 -1.809  1.00 115.94 ? 110 LYS B HA   1 
ATOM   3461 H HB2  . LYS B 1 110 ? 8.942  -11.546 0.655   1.00 111.82 ? 110 LYS B HB2  1 
ATOM   3462 H HB3  . LYS B 1 110 ? 9.907  -12.104 -0.477  1.00 111.82 ? 110 LYS B HB3  1 
ATOM   3463 H HG2  . LYS B 1 110 ? 10.082 -9.530  0.657   1.00 109.67 ? 110 LYS B HG2  1 
ATOM   3464 H HG3  . LYS B 1 110 ? 11.104 -10.716 0.928   1.00 109.67 ? 110 LYS B HG3  1 
ATOM   3465 H HD2  . LYS B 1 110 ? 11.815 -10.594 -1.346  1.00 111.29 ? 110 LYS B HD2  1 
ATOM   3466 H HD3  . LYS B 1 110 ? 10.831 -9.367  -1.572  1.00 111.29 ? 110 LYS B HD3  1 
ATOM   3467 H HE2  . LYS B 1 110 ? 13.161 -9.310  0.030   1.00 102.53 ? 110 LYS B HE2  1 
ATOM   3468 H HE3  . LYS B 1 110 ? 12.986 -8.561  -1.361  1.00 102.53 ? 110 LYS B HE3  1 
ATOM   3469 H HZ1  . LYS B 1 110 ? 12.849 -7.069  0.387   1.00 105.21 ? 110 LYS B HZ1  1 
ATOM   3470 H HZ2  . LYS B 1 110 ? 11.579 -7.071  -0.310  1.00 105.21 ? 110 LYS B HZ2  1 
ATOM   3471 H HZ3  . LYS B 1 110 ? 11.712 -7.762  0.956   1.00 105.21 ? 110 LYS B HZ3  1 
ATOM   3472 N N    . LYS B 1 111 ? 6.786  -12.512 -1.647  1.00 103.91 ? 111 LYS B N    1 
ATOM   3473 C CA   . LYS B 1 111 ? 6.112  -13.598 -2.349  1.00 102.52 ? 111 LYS B CA   1 
ATOM   3474 C C    . LYS B 1 111 ? 4.847  -13.128 -3.055  1.00 92.11  ? 111 LYS B C    1 
ATOM   3475 O O    . LYS B 1 111 ? 4.909  -12.685 -4.197  1.00 90.90  ? 111 LYS B O    1 
ATOM   3476 C CB   . LYS B 1 111 ? 5.801  -14.693 -1.325  1.00 107.79 ? 111 LYS B CB   1 
ATOM   3477 C CG   . LYS B 1 111 ? 7.065  -15.382 -0.801  1.00 106.94 ? 111 LYS B CG   1 
ATOM   3478 C CD   . LYS B 1 111 ? 6.785  -16.275 0.385   1.00 109.64 ? 111 LYS B CD   1 
ATOM   3479 C CE   . LYS B 1 111 ? 6.653  -15.427 1.640   1.00 106.22 ? 111 LYS B CE   1 
ATOM   3480 N NZ   . LYS B 1 111 ? 6.448  -16.269 2.865   1.00 124.13 ? 111 LYS B NZ   1 
ATOM   3481 H H    . LYS B 1 111 ? 6.361  -12.260 -0.943  1.00 124.77 ? 111 LYS B H    1 
ATOM   3482 H HA   . LYS B 1 111 ? 6.682  -13.957 -3.048  1.00 123.11 ? 111 LYS B HA   1 
ATOM   3483 H HB2  . LYS B 1 111 ? 5.338  -14.298 -0.570  1.00 129.43 ? 111 LYS B HB2  1 
ATOM   3484 H HB3  . LYS B 1 111 ? 5.241  -15.367 -1.742  1.00 129.43 ? 111 LYS B HB3  1 
ATOM   3485 H HG2  . LYS B 1 111 ? 7.445  -15.928 -1.506  1.00 128.40 ? 111 LYS B HG2  1 
ATOM   3486 H HG3  . LYS B 1 111 ? 7.704  -14.706 -0.524  1.00 128.40 ? 111 LYS B HG3  1 
ATOM   3487 H HD2  . LYS B 1 111 ? 5.956  -16.758 0.244   1.00 131.65 ? 111 LYS B HD2  1 
ATOM   3488 H HD3  . LYS B 1 111 ? 7.517  -16.901 0.505   1.00 131.65 ? 111 LYS B HD3  1 
ATOM   3489 H HE2  . LYS B 1 111 ? 7.463  -14.907 1.762   1.00 127.54 ? 111 LYS B HE2  1 
ATOM   3490 H HE3  . LYS B 1 111 ? 5.890  -14.836 1.547   1.00 127.54 ? 111 LYS B HE3  1 
ATOM   3491 H HZ1  . LYS B 1 111 ? 6.389  -15.749 3.585   1.00 149.04 ? 111 LYS B HZ1  1 
ATOM   3492 H HZ2  . LYS B 1 111 ? 5.698  -16.741 2.787   1.00 149.04 ? 111 LYS B HZ2  1 
ATOM   3493 H HZ3  . LYS B 1 111 ? 7.132  -16.828 2.967   1.00 149.04 ? 111 LYS B HZ3  1 
HETATM 3494 O O    . HOH C 2 .   ? 34.043 2.001   11.797  1.00 52.99  ? 201 HOH A O    1 
HETATM 3495 O O    . HOH C 2 .   ? 30.500 -2.105  7.576   1.00 54.62  ? 202 HOH A O    1 
HETATM 3496 O O    . HOH C 2 .   ? 15.822 -6.244  0.800   1.00 50.87  ? 203 HOH A O    1 
HETATM 3497 O O    . HOH C 2 .   ? 25.796 -10.070 0.049   1.00 46.59  ? 204 HOH A O    1 
HETATM 3498 O O    . HOH C 2 .   ? 30.399 -4.594  -12.482 1.00 142.36 ? 205 HOH A O    1 
HETATM 3499 O O    . HOH C 2 .   ? 31.223 -0.919  2.842   1.00 53.64  ? 206 HOH A O    1 
HETATM 3500 O O    . HOH C 2 .   ? 0.790  1.319   8.568   1.00 66.62  ? 207 HOH A O    1 
HETATM 3501 O O    . HOH C 2 .   ? 30.730 -4.717  1.172   1.00 44.81  ? 208 HOH A O    1 
HETATM 3502 O O    . HOH C 2 .   ? 29.924 -9.895  6.824   1.00 55.48  ? 209 HOH A O    1 
HETATM 3503 O O    . HOH C 2 .   ? 21.394 -7.857  3.392   1.00 42.17  ? 210 HOH A O    1 
HETATM 3504 O O    . HOH C 2 .   ? 7.010  -3.835  -0.166  1.00 57.05  ? 211 HOH A O    1 
HETATM 3505 O O    . HOH C 2 .   ? 9.653  4.961   1.511   1.00 45.14  ? 212 HOH A O    1 
HETATM 3506 O O    . HOH C 2 .   ? 17.050 -2.434  15.463  1.00 62.34  ? 213 HOH A O    1 
HETATM 3507 O O    . HOH C 2 .   ? 30.493 5.362   6.787   1.00 55.26  ? 214 HOH A O    1 
HETATM 3508 O O    . HOH C 2 .   ? 21.944 2.763   -3.687  1.00 43.21  ? 215 HOH A O    1 
HETATM 3509 O O    . HOH C 2 .   ? 30.406 -9.169  9.245   1.00 58.22  ? 216 HOH A O    1 
HETATM 3510 O O    . HOH C 2 .   ? 19.543 3.736   -5.385  1.00 57.72  ? 217 HOH A O    1 
HETATM 3511 O O    . HOH C 2 .   ? 32.307 -3.370  -5.224  1.00 54.77  ? 218 HOH A O    1 
HETATM 3512 O O    . HOH C 2 .   ? 0.546  -0.393  7.004   1.00 58.12  ? 219 HOH A O    1 
HETATM 3513 O O    . HOH D 2 .   ? 4.868  5.183   12.478  1.00 62.33  ? 201 HOH B O    1 
HETATM 3514 O O    . HOH D 2 .   ? 8.899  -6.418  0.131   1.00 68.72  ? 202 HOH B O    1 
HETATM 3515 O O    . HOH D 2 .   ? 3.769  4.558   9.859   1.00 60.59  ? 203 HOH B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ILE A 4   ? 1.4383 1.3853 1.5499 0.0260  0.0953  -0.1344 4   ILE A N   
2    C CA  . ILE A 4   ? 1.5171 1.4650 1.6059 0.0089  0.0744  -0.1303 4   ILE A CA  
3    C C   . ILE A 4   ? 1.4590 1.3808 1.5422 0.0003  0.0721  -0.1347 4   ILE A C   
4    O O   . ILE A 4   ? 1.3877 1.2935 1.4892 0.0126  0.0784  -0.1275 4   ILE A O   
5    C CB  . ILE A 4   ? 1.4960 1.4665 1.5931 0.0181  0.0584  -0.1113 4   ILE A CB  
6    C CG1 . ILE A 4   ? 1.4480 1.4510 1.5503 0.0192  0.0601  -0.1127 4   ILE A CG1 
7    C CG2 . ILE A 4   ? 1.3136 1.2794 1.3916 0.0042  0.0401  -0.1051 4   ILE A CG2 
8    C CD1 . ILE A 4   ? 1.3707 1.3732 1.4460 -0.0026 0.0606  -0.1230 4   ILE A CD1 
19   N N   . PRO A 5   ? 1.8061 1.7266 1.8639 -0.0206 0.0639  -0.1463 5   PRO A N   
20   C CA  . PRO A 5   ? 1.7286 1.6352 1.7846 -0.0315 0.0602  -0.1545 5   PRO A CA  
21   C C   . PRO A 5   ? 1.4484 1.3542 1.5180 -0.0231 0.0475  -0.1363 5   PRO A C   
22   O O   . PRO A 5   ? 1.3435 1.2640 1.4120 -0.0158 0.0341  -0.1189 5   PRO A O   
23   C CB  . PRO A 5   ? 1.6989 1.6203 1.7224 -0.0515 0.0472  -0.1650 5   PRO A CB  
24   C CG  . PRO A 5   ? 1.7189 1.6546 1.7251 -0.0495 0.0439  -0.1559 5   PRO A CG  
25   C CD  . PRO A 5   ? 1.6543 1.5877 1.6835 -0.0348 0.0605  -0.1540 5   PRO A CD  
33   N N   . LYS A 6   ? 1.2224 1.1090 1.3059 -0.0259 0.0553  -0.1427 6   LYS A N   
34   C CA  . LYS A 6   ? 1.2073 1.0902 1.3044 -0.0187 0.0473  -0.1269 6   LYS A CA  
35   C C   . LYS A 6   ? 1.1303 1.0349 1.2152 -0.0272 0.0227  -0.1201 6   LYS A C   
36   O O   . LYS A 6   ? 1.0715 0.9797 1.1640 -0.0185 0.0137  -0.1030 6   LYS A O   
37   C CB  . LYS A 6   ? 1.2570 1.1133 1.3706 -0.0244 0.0637  -0.1379 6   LYS A CB  
38   C CG  . LYS A 6   ? 1.2615 1.0860 1.3900 -0.0124 0.0935  -0.1407 6   LYS A CG  
39   C CD  . LYS A 6   ? 1.3641 1.1563 1.5094 -0.0186 0.1127  -0.1481 6   LYS A CD  
40   C CE  . LYS A 6   ? 1.4278 1.2260 1.5697 -0.0499 0.1112  -0.1791 6   LYS A CE  
41   N NZ  . LYS A 6   ? 1.4334 1.1936 1.5956 -0.0589 0.1406  -0.1930 6   LYS A NZ  
55   N N   . GLU A 7   ? 1.1244 1.0440 1.1899 -0.0430 0.0129  -0.1328 7   GLU A N   
56   C CA  . GLU A 7   ? 1.0799 1.0200 1.1342 -0.0460 -0.0089 -0.1225 7   GLU A CA  
57   C C   . GLU A 7   ? 0.9892 0.9341 1.0353 -0.0350 -0.0155 -0.1021 7   GLU A C   
58   O O   . GLU A 7   ? 0.9047 0.8560 0.9521 -0.0312 -0.0275 -0.0879 7   GLU A O   
59   C CB  . GLU A 7   ? 1.1178 1.0781 1.1478 -0.0608 -0.0183 -0.1367 7   GLU A CB  
60   C CG  . GLU A 7   ? 1.2147 1.1779 1.2515 -0.0779 -0.0112 -0.1647 7   GLU A CG  
61   C CD  . GLU A 7   ? 1.2882 1.2314 1.3240 -0.0840 0.0127  -0.1849 7   GLU A CD  
62   O OE1 . GLU A 7   ? 1.2219 1.1655 1.2382 -0.0811 0.0163  -0.1828 7   GLU A OE1 
63   O OE2 . GLU A 7   ? 1.3190 1.2428 1.3753 -0.0912 0.0310  -0.2024 7   GLU A OE2 
70   N N   . MET A 8   ? 0.9862 0.9288 1.0274 -0.0307 -0.0052 -0.1025 8   MET A N   
71   C CA  . MET A 8   ? 0.9579 0.9081 0.9919 -0.0256 -0.0080 -0.0893 8   MET A CA  
72   C C   . MET A 8   ? 0.8450 0.7963 0.9005 -0.0135 -0.0076 -0.0772 8   MET A C   
73   O O   . MET A 8   ? 0.7636 0.7204 0.8173 -0.0126 -0.0143 -0.0663 8   MET A O   
74   C CB  . MET A 8   ? 0.9996 0.9532 1.0233 -0.0281 0.0041  -0.0978 8   MET A CB  
75   C CG  . MET A 8   ? 1.0772 1.0389 1.0899 -0.0295 0.0044  -0.0892 8   MET A CG  
76   S SD  . MET A 8   ? 1.0850 1.0499 1.0768 -0.0388 0.0190  -0.1015 8   MET A SD  
77   C CE  . MET A 8   ? 1.2810 1.2402 1.2394 -0.0496 0.0113  -0.1071 8   MET A CE  
87   N N   . LEU A 9   ? 0.9061 0.8516 0.9802 -0.0036 0.0021  -0.0787 9   LEU A N   
88   C CA  . LEU A 9   ? 0.8658 0.8161 0.9559 0.0097  0.0015  -0.0657 9   LEU A CA  
89   C C   . LEU A 9   ? 0.8307 0.7747 0.9242 0.0075  -0.0078 -0.0577 9   LEU A C   
90   O O   . LEU A 9   ? 0.7962 0.7490 0.8937 0.0125  -0.0123 -0.0475 9   LEU A O   
91   C CB  . LEU A 9   ? 0.9514 0.8934 1.0576 0.0247  0.0158  -0.0648 9   LEU A CB  
92   C CG  . LEU A 9   ? 1.0724 1.0266 1.1814 0.0311  0.0260  -0.0711 9   LEU A CG  
93   C CD1 . LEU A 9   ? 1.1272 1.0685 1.2536 0.0507  0.0433  -0.0673 9   LEU A CD1 
94   C CD2 . LEU A 9   ? 1.0260 1.0139 1.1360 0.0337  0.0193  -0.0666 9   LEU A CD2 
106  N N   . ARG A 10  ? 0.8103 0.7422 0.9045 -0.0007 -0.0092 -0.0648 10  ARG A N   
107  C CA  . ARG A 10  ? 0.7302 0.6614 0.8302 -0.0042 -0.0182 -0.0594 10  ARG A CA  
108  C C   . ARG A 10  ? 0.7300 0.6732 0.8180 -0.0074 -0.0305 -0.0519 10  ARG A C   
109  O O   . ARG A 10  ? 0.6127 0.5573 0.7068 -0.0038 -0.0342 -0.0418 10  ARG A O   
110  C CB  . ARG A 10  ? 0.8372 0.7631 0.9426 -0.0155 -0.0175 -0.0736 10  ARG A CB  
111  C CG  . ARG A 10  ? 0.9142 0.8452 1.0324 -0.0200 -0.0256 -0.0717 10  ARG A CG  
112  C CD  . ARG A 10  ? 1.0627 0.9781 1.1980 -0.0114 -0.0155 -0.0618 10  ARG A CD  
113  N NE  . ARG A 10  ? 1.1298 1.0397 1.2839 -0.0192 -0.0107 -0.0688 10  ARG A NE  
114  C CZ  . ARG A 10  ? 1.0476 0.9687 1.2125 -0.0211 -0.0191 -0.0643 10  ARG A CZ  
115  N NH1 . ARG A 10  ? 0.8208 0.7555 0.9785 -0.0153 -0.0321 -0.0522 10  ARG A NH1 
116  N NH2 . ARG A 10  ? 1.2580 1.1745 1.4434 -0.0294 -0.0109 -0.0729 10  ARG A NH2 
130  N N   . ALA A 11  ? 0.7078 0.6568 0.7769 -0.0135 -0.0337 -0.0558 11  ALA A N   
131  C CA  . ALA A 11  ? 0.6536 0.6063 0.7091 -0.0144 -0.0405 -0.0455 11  ALA A CA  
132  C C   . ALA A 11  ? 0.6114 0.5637 0.6700 -0.0111 -0.0342 -0.0388 11  ALA A C   
133  O O   . ALA A 11  ? 0.5856 0.5347 0.6448 -0.0104 -0.0358 -0.0298 11  ALA A O   
134  C CB  . ALA A 11  ? 0.8082 0.7645 0.8382 -0.0203 -0.0420 -0.0487 11  ALA A CB  
140  N N   . GLN A 12  ? 0.6202 0.5787 0.6829 -0.0092 -0.0260 -0.0444 12  GLN A N   
141  C CA  . GLN A 12  ? 0.6091 0.5783 0.6764 -0.0088 -0.0207 -0.0427 12  GLN A CA  
142  C C   . GLN A 12  ? 0.5314 0.5043 0.6129 -0.0031 -0.0231 -0.0367 12  GLN A C   
143  O O   . GLN A 12  ? 0.5179 0.4954 0.5999 -0.0072 -0.0208 -0.0355 12  GLN A O   
144  C CB  . GLN A 12  ? 0.6572 0.6426 0.7294 -0.0059 -0.0132 -0.0511 12  GLN A CB  
145  C CG  . GLN A 12  ? 0.7397 0.7237 0.7963 -0.0146 -0.0067 -0.0587 12  GLN A CG  
146  C CD  . GLN A 12  ? 0.7919 0.7924 0.8576 -0.0103 0.0021  -0.0685 12  GLN A CD  
147  O OE1 . GLN A 12  ? 0.8691 0.8719 0.9242 -0.0184 0.0102  -0.0762 12  GLN A OE1 
148  N NE2 . GLN A 12  ? 0.7729 0.7817 0.8567 0.0038  0.0026  -0.0669 12  GLN A NE2 
157  N N   . THR A 13  ? 0.5322 0.5019 0.6244 0.0054  -0.0243 -0.0343 13  THR A N   
158  C CA  . THR A 13  ? 0.5605 0.5310 0.6624 0.0111  -0.0249 -0.0274 13  THR A CA  
159  C C   . THR A 13  ? 0.5751 0.5345 0.6778 0.0054  -0.0291 -0.0233 13  THR A C   
160  O O   . THR A 13  ? 0.4816 0.4447 0.5881 0.0055  -0.0274 -0.0201 13  THR A O   
161  C CB  . THR A 13  ? 0.6047 0.5645 0.7157 0.0206  -0.0208 -0.0245 13  THR A CB  
162  O OG1 . THR A 13  ? 0.6262 0.5926 0.7383 0.0294  -0.0144 -0.0265 13  THR A OG1 
163  C CG2 . THR A 13  ? 0.5922 0.5517 0.7094 0.0283  -0.0183 -0.0151 13  THR A CG2 
171  N N   . ASN A 14  ? 0.5761 0.5258 0.6771 0.0017  -0.0344 -0.0237 14  ASN A N   
172  C CA  . ASN A 14  ? 0.5508 0.4956 0.6556 0.0002  -0.0389 -0.0179 14  ASN A CA  
173  C C   . ASN A 14  ? 0.5387 0.4805 0.6341 -0.0027 -0.0345 -0.0142 14  ASN A C   
174  O O   . ASN A 14  ? 0.5283 0.4653 0.6303 -0.0025 -0.0307 -0.0103 14  ASN A O   
175  C CB  . ASN A 14  ? 0.5706 0.5172 0.6738 -0.0016 -0.0475 -0.0191 14  ASN A CB  
176  C CG  . ASN A 14  ? 0.6449 0.5929 0.7639 -0.0028 -0.0486 -0.0257 14  ASN A CG  
177  O OD1 . ASN A 14  ? 0.6876 0.6300 0.8087 -0.0029 -0.0415 -0.0320 14  ASN A OD1 
178  N ND2 . ASN A 14  ? 0.6657 0.6205 0.7986 -0.0032 -0.0543 -0.0245 14  ASN A ND2 
185  O O   . HOX A 15  ? 0.5286 0.4582 0.6103 -0.0224 -0.0022 -0.0212 15  HOX A O   
186  C C   . HOX A 15  ? 0.5282 0.4689 0.6089 -0.0173 -0.0125 -0.0214 15  HOX A C   
187  N N   . HOX A 15  ? 0.5315 0.4737 0.6119 -0.0068 -0.0314 -0.0170 15  HOX A N   
188  C CA  . HOX A 15  ? 0.5276 0.4615 0.5990 -0.0123 -0.0215 -0.0152 15  HOX A CA  
189  C CB  . HOX A 15  ? 0.5168 0.4516 0.5712 -0.0183 -0.0159 -0.0200 15  HOX A CB  
190  C CG  . HOX A 15  ? 0.5175 0.4387 0.5622 -0.0267 -0.0005 -0.0195 15  HOX A CG  
191  C CZ  . HOX A 15  ? 0.5656 0.4503 0.5949 -0.0470 0.0396  -0.0224 15  HOX A CZ  
192  N NZ  . HOX A 15  ? 0.6434 0.5030 0.6655 -0.0585 0.0644  -0.0242 15  HOX A NZ  
193  C CD1 . HOX A 15  ? 0.5720 0.4700 0.6105 -0.0234 0.0050  -0.0068 15  HOX A CD1 
194  C CD2 . HOX A 15  ? 0.6109 0.5432 0.6551 -0.0376 0.0111  -0.0324 15  HOX A CD2 
195  C CE1 . HOX A 15  ? 0.5835 0.4602 0.6135 -0.0316 0.0254  -0.0061 15  HOX A CE1 
196  C CE2 . HOX A 15  ? 0.5761 0.4938 0.6138 -0.0496 0.0304  -0.0360 15  HOX A CE2 
206  N N   . ILE A 16  ? 0.4611 0.4229 0.5480 -0.0157 -0.0146 -0.0285 16  ILE A N   
207  C CA  . ILE A 16  ? 0.5276 0.5093 0.6199 -0.0206 -0.0086 -0.0370 16  ILE A CA  
208  C C   . ILE A 16  ? 0.4703 0.4460 0.5698 -0.0187 -0.0081 -0.0331 16  ILE A C   
209  O O   . ILE A 16  ? 0.5096 0.4859 0.6102 -0.0277 0.0015  -0.0399 16  ILE A O   
210  C CB  . ILE A 16  ? 0.5199 0.5314 0.6166 -0.0132 -0.0132 -0.0408 16  ILE A CB  
211  C CG1 . ILE A 16  ? 0.4878 0.5138 0.5816 -0.0188 -0.0089 -0.0501 16  ILE A CG1 
212  C CG2 . ILE A 16  ? 0.5140 0.5544 0.6155 -0.0125 -0.0124 -0.0455 16  ILE A CG2 
213  C CD1 . ILE A 16  ? 0.5326 0.5823 0.6326 -0.0067 -0.0129 -0.0507 16  ILE A CD1 
225  N N   . LEU A 17  ? 0.4840 0.4519 0.5891 -0.0087 -0.0158 -0.0242 17  LEU A N   
226  C CA  . LEU A 17  ? 0.5008 0.4623 0.6142 -0.0064 -0.0141 -0.0201 17  LEU A CA  
227  C C   . LEU A 17  ? 0.5118 0.4540 0.6286 -0.0110 -0.0078 -0.0182 17  LEU A C   
228  O O   . LEU A 17  ? 0.4445 0.3842 0.5654 -0.0154 0.0012  -0.0217 17  LEU A O   
229  C CB  . LEU A 17  ? 0.4452 0.3995 0.5665 0.0024  -0.0203 -0.0130 17  LEU A CB  
230  C CG  . LEU A 17  ? 0.4990 0.4655 0.6175 0.0104  -0.0205 -0.0117 17  LEU A CG  
231  C CD1 . LEU A 17  ? 0.4967 0.4478 0.6239 0.0162  -0.0203 -0.0068 17  LEU A CD1 
232  C CD2 . LEU A 17  ? 0.4778 0.4610 0.5923 0.0130  -0.0161 -0.0110 17  LEU A CD2 
244  N N   . LEU A 18  ? 0.5278 0.4565 0.6421 -0.0087 -0.0111 -0.0119 18  LEU A N   
245  C CA  . LEU A 18  ? 0.5096 0.4190 0.6270 -0.0075 -0.0038 -0.0052 18  LEU A CA  
246  C C   . LEU A 18  ? 0.5349 0.4335 0.6448 -0.0181 0.0136  -0.0122 18  LEU A C   
247  O O   . LEU A 18  ? 0.5433 0.4231 0.6593 -0.0187 0.0268  -0.0102 18  LEU A O   
248  C CB  . LEU A 18  ? 0.5863 0.4899 0.6985 0.0004  -0.0124 0.0059  18  LEU A CB  
249  C CG  . LEU A 18  ? 0.5159 0.4322 0.6416 0.0079  -0.0269 0.0092  18  LEU A CG  
250  C CD1 . LEU A 18  ? 0.5687 0.4913 0.6847 0.0131  -0.0382 0.0154  18  LEU A CD1 
251  C CD2 . LEU A 18  ? 0.5328 0.4451 0.6789 0.0136  -0.0229 0.0142  18  LEU A CD2 
263  N N   . MET A 19  ? 0.4936 0.4038 0.5932 -0.0274 0.0166  -0.0224 19  MET A N   
264  C CA  . MET A 19  ? 0.5322 0.4348 0.6279 -0.0423 0.0366  -0.0345 19  MET A CA  
265  C C   . MET A 19  ? 0.5443 0.4635 0.6480 -0.0520 0.0438  -0.0496 19  MET A C   
266  O O   . MET A 19  ? 0.6057 0.5101 0.7115 -0.0641 0.0638  -0.0596 19  MET A O   
267  C CB  . MET A 19  ? 0.5820 0.4962 0.6675 -0.0514 0.0395  -0.0433 19  MET A CB  
268  C CG  . MET A 19  ? 0.6047 0.4934 0.6754 -0.0466 0.0420  -0.0299 19  MET A CG  
269  S SD  . MET A 19  ? 0.6779 0.5209 0.7425 -0.0489 0.0674  -0.0210 19  MET A SD  
270  C CE  . MET A 19  ? 0.6477 0.4942 0.7137 -0.0763 0.0940  -0.0477 19  MET A CE  
280  N N   . VAL A 20  ? 0.5062 0.4553 0.6125 -0.0470 0.0302  -0.0517 20  VAL A N   
281  C CA  . VAL A 20  ? 0.4677 0.4351 0.5767 -0.0534 0.0351  -0.0629 20  VAL A CA  
282  C C   . VAL A 20  ? 0.5162 0.4549 0.6332 -0.0525 0.0460  -0.0587 20  VAL A C   
283  O O   . VAL A 20  ? 0.5295 0.4672 0.6476 -0.0655 0.0624  -0.0733 20  VAL A O   
284  C CB  . VAL A 20  ? 0.4345 0.4308 0.5417 -0.0410 0.0189  -0.0567 20  VAL A CB  
285  C CG1 . VAL A 20  ? 0.5134 0.5239 0.6189 -0.0434 0.0231  -0.0622 20  VAL A CG1 
286  C CG2 . VAL A 20  ? 0.4367 0.4692 0.5390 -0.0409 0.0115  -0.0635 20  VAL A CG2 
296  N N   . LEU A 21  ? 0.4786 0.3991 0.6035 -0.0373 0.0372  -0.0409 21  LEU A N   
297  C CA  . LEU A 21  ? 0.4827 0.3815 0.6205 -0.0334 0.0468  -0.0360 21  LEU A CA  
298  C C   . LEU A 21  ? 0.5710 0.4386 0.7109 -0.0382 0.0672  -0.0369 21  LEU A C   
299  O O   . LEU A 21  ? 0.5811 0.4320 0.7304 -0.0414 0.0847  -0.0417 21  LEU A O   
300  C CB  . LEU A 21  ? 0.4425 0.3367 0.5926 -0.0174 0.0331  -0.0194 21  LEU A CB  
301  C CG  . LEU A 21  ? 0.4907 0.4035 0.6430 -0.0132 0.0217  -0.0181 21  LEU A CG  
302  C CD1 . LEU A 21  ? 0.4769 0.3859 0.6471 -0.0023 0.0126  -0.0073 21  LEU A CD1 
303  C CD2 . LEU A 21  ? 0.4674 0.3891 0.6168 -0.0202 0.0325  -0.0278 21  LEU A CD2 
315  N N   . LYS A 22  ? 0.6034 0.4595 0.7340 -0.0387 0.0689  -0.0324 22  LYS A N   
316  C CA  . LYS A 22  ? 0.5887 0.4084 0.7177 -0.0427 0.0935  -0.0313 22  LYS A CA  
317  C C   . LYS A 22  ? 0.6489 0.4662 0.7776 -0.0658 0.1181  -0.0567 22  LYS A C   
318  O O   . LYS A 22  ? 0.6737 0.4554 0.8077 -0.0703 0.1453  -0.0593 22  LYS A O   
319  C CB  . LYS A 22  ? 0.6743 0.4847 0.7880 -0.0406 0.0913  -0.0221 22  LYS A CB  
320  C CG  . LYS A 22  ? 0.7340 0.4984 0.8416 -0.0365 0.1160  -0.0096 22  LYS A CG  
321  C CD  . LYS A 22  ? 0.7664 0.5272 0.8534 -0.0333 0.1104  0.0013  22  LYS A CD  
322  C CE  . LYS A 22  ? 0.9651 0.6776 1.0393 -0.0297 0.1384  0.0155  22  LYS A CE  
323  N NZ  . LYS A 22  ? 1.0537 0.7454 1.1279 -0.0559 0.1720  -0.0079 22  LYS A NZ  
337  N N   . GLN A 23  ? 0.7167 0.5741 0.8400 -0.0803 0.1103  -0.0765 23  GLN A N   
338  C CA  . GLN A 23  ? 0.6721 0.5408 0.7952 -0.1049 0.1310  -0.1057 23  GLN A CA  
339  C C   . GLN A 23  ? 0.6835 0.5532 0.8136 -0.1069 0.1384  -0.1132 23  GLN A C   
340  O O   . GLN A 23  ? 0.6522 0.5184 0.7833 -0.1282 0.1631  -0.1381 23  GLN A O   
341  C CB  . GLN A 23  ? 0.6793 0.6019 0.7948 -0.1170 0.1178  -0.1237 23  GLN A CB  
342  C CG  . GLN A 23  ? 0.7835 0.7058 0.8944 -0.1214 0.1182  -0.1238 23  GLN A CG  
343  C CD  . GLN A 23  ? 0.8267 0.8066 0.9352 -0.1290 0.1039  -0.1393 23  GLN A CD  
344  O OE1 . GLN A 23  ? 0.8563 0.8796 0.9646 -0.1351 0.0976  -0.1542 23  GLN A OE1 
345  N NE2 . GLN A 23  ? 0.9206 0.9053 1.0265 -0.1269 0.0984  -0.1349 23  GLN A NE2 
354  N N   . GLY A 24  ? 0.6651 0.5419 0.7996 -0.0881 0.1196  -0.0959 24  GLY A N   
355  C CA  . GLY A 24  ? 0.6237 0.4982 0.7650 -0.0893 0.1288  -0.1015 24  GLY A CA  
356  C C   . GLY A 24  ? 0.5516 0.4429 0.6952 -0.0715 0.1061  -0.0844 24  GLY A C   
357  O O   . GLY A 24  ? 0.5427 0.4595 0.6777 -0.0648 0.0848  -0.0772 24  GLY A O   
361  N N   . ASP A 25  ? 0.5723 0.4475 0.7295 -0.0642 0.1136  -0.0786 25  ASP A N   
362  C CA  . ASP A 25  ? 0.4898 0.3802 0.6499 -0.0527 0.0990  -0.0676 25  ASP A CA  
363  C C   . ASP A 25  ? 0.5472 0.4750 0.6849 -0.0598 0.0899  -0.0765 25  ASP A C   
364  O O   . ASP A 25  ? 0.5601 0.5063 0.6844 -0.0763 0.0994  -0.0967 25  ASP A O   
365  C CB  . ASP A 25  ? 0.5242 0.3973 0.7011 -0.0510 0.1158  -0.0689 25  ASP A CB  
366  C CG  . ASP A 25  ? 0.5438 0.3833 0.7449 -0.0406 0.1278  -0.0591 25  ASP A CG  
367  O OD1 . ASP A 25  ? 0.5609 0.3881 0.7614 -0.0348 0.1235  -0.0500 25  ASP A OD1 
368  O OD2 . ASP A 25  ? 0.5474 0.3731 0.7676 -0.0367 0.1435  -0.0598 25  ASP A OD2 
373  N N   . ASN A 26  ? 0.5130 0.4541 0.6471 -0.0469 0.0729  -0.0618 26  ASN A N   
374  C CA  . ASN A 26  ? 0.5161 0.4924 0.6278 -0.0464 0.0629  -0.0632 26  ASN A CA  
375  C C   . ASN A 26  ? 0.5052 0.4784 0.6174 -0.0307 0.0543  -0.0443 26  ASN A C   
376  O O   . ASN A 26  ? 0.5463 0.4962 0.6779 -0.0235 0.0527  -0.0340 26  ASN A O   
377  C CB  . ASN A 26  ? 0.5553 0.5510 0.6599 -0.0475 0.0513  -0.0661 26  ASN A CB  
378  C CG  . ASN A 26  ? 0.5356 0.5793 0.6193 -0.0527 0.0465  -0.0773 26  ASN A CG  
379  O OD1 . ASN A 26  ? 0.4839 0.5467 0.5536 -0.0478 0.0457  -0.0739 26  ASN A OD1 
380  N ND2 . ASN A 26  ? 0.6002 0.6672 0.6822 -0.0607 0.0425  -0.0892 26  ASN A ND2 
387  N N   . TYR A 27  ? 0.5557 0.5542 0.6464 -0.0259 0.0508  -0.0405 27  TYR A N   
388  C CA  . TYR A 27  ? 0.5578 0.5488 0.6443 -0.0115 0.0490  -0.0222 27  TYR A CA  
389  C C   . TYR A 27  ? 0.5279 0.5357 0.6033 0.0019  0.0354  -0.0108 27  TYR A C   
390  O O   . TYR A 27  ? 0.5757 0.6115 0.6434 -0.0007 0.0271  -0.0189 27  TYR A O   
391  C CB  . TYR A 27  ? 0.6244 0.6247 0.6912 -0.0122 0.0610  -0.0214 27  TYR A CB  
392  C CG  . TYR A 27  ? 0.7266 0.7719 0.7617 -0.0131 0.0574  -0.0274 27  TYR A CG  
393  C CD1 . TYR A 27  ? 0.7745 0.8440 0.8049 -0.0314 0.0608  -0.0520 27  TYR A CD1 
394  C CD2 . TYR A 27  ? 0.7651 0.8313 0.7751 0.0046  0.0518  -0.0093 27  TYR A CD2 
395  C CE1 . TYR A 27  ? 0.7678 0.8894 0.7713 -0.0347 0.0559  -0.0618 27  TYR A CE1 
396  C CE2 . TYR A 27  ? 0.7893 0.9081 0.7712 0.0062  0.0452  -0.0145 27  TYR A CE2 
397  C CZ  . TYR A 27  ? 0.7833 0.9331 0.7629 -0.0148 0.0461  -0.0424 27  TYR A CZ  
398  O OH  . TYR A 27  ? 0.8761 1.0881 0.8299 -0.0165 0.0386  -0.0525 27  TYR A OH  
408  N N   . VAL A 28  ? 0.5243 0.5140 0.6016 0.0154  0.0360  0.0065  28  VAL A N   
409  C CA  . VAL A 28  ? 0.4794 0.4702 0.5558 0.0289  0.0269  0.0175  28  VAL A CA  
410  C C   . VAL A 28  ? 0.5153 0.5466 0.5686 0.0398  0.0196  0.0216  28  VAL A C   
411  O O   . VAL A 28  ? 0.4204 0.4707 0.4771 0.0406  0.0094  0.0162  28  VAL A O   
412  C CB  . VAL A 28  ? 0.5218 0.4807 0.6044 0.0386  0.0360  0.0326  28  VAL A CB  
413  C CG1 . VAL A 28  ? 0.5863 0.5441 0.6632 0.0552  0.0329  0.0454  28  VAL A CG1 
414  C CG2 . VAL A 28  ? 0.5390 0.4728 0.6505 0.0273  0.0371  0.0243  28  VAL A CG2 
424  N N   . TYR A 29  ? 0.5849 0.6341 0.6149 0.0482  0.0249  0.0305  29  TYR A N   
425  C CA  . TYR A 29  ? 0.6396 0.7409 0.6477 0.0598  0.0154  0.0335  29  TYR A CA  
426  C C   . TYR A 29  ? 0.6102 0.7506 0.6228 0.0410  0.0066  0.0072  29  TYR A C   
427  O O   . TYR A 29  ? 0.5137 0.6987 0.5226 0.0474  -0.0046 0.0041  29  TYR A O   
428  C CB  . TYR A 29  ? 0.9567 1.0766 0.9336 0.0701  0.0226  0.0460  29  TYR A CB  
429  C CG  . TYR A 29  ? 1.2620 1.4532 1.2131 0.0793  0.0105  0.0446  29  TYR A CG  
430  C CD1 . TYR A 29  ? 1.2491 1.4860 1.1946 0.0567  0.0061  0.0158  29  TYR A CD1 
431  C CD2 . TYR A 29  ? 1.4467 1.6627 1.3803 0.1109  0.0052  0.0710  29  TYR A CD2 
432  C CE1 . TYR A 29  ? 1.3657 1.6785 1.2905 0.0623  -0.0063 0.0098  29  TYR A CE1 
433  C CE2 . TYR A 29  ? 1.4929 1.7859 1.4051 0.1217  -0.0086 0.0699  29  TYR A CE2 
434  C CZ  . TYR A 29  ? 1.6317 1.9765 1.5400 0.0958  -0.0156 0.0376  29  TYR A CZ  
435  O OH  . TYR A 29  ? 1.7426 2.1730 1.6319 0.1037  -0.0303 0.0321  29  TYR A OH  
445  N N   . GLY A 30  ? 0.5052 0.6305 0.5277 0.0176  0.0141  -0.0129 30  GLY A N   
446  C CA  . GLY A 30  ? 0.5401 0.6944 0.5678 -0.0026 0.0119  -0.0392 30  GLY A CA  
447  C C   . GLY A 30  ? 0.4984 0.6425 0.5451 -0.0045 0.0054  -0.0426 30  GLY A C   
448  O O   . GLY A 30  ? 0.4735 0.6552 0.5214 -0.0118 -0.0001 -0.0571 30  GLY A O   
452  N N   . ILE A 31  ? 0.4523 0.5500 0.5136 0.0014  0.0063  -0.0302 31  ILE A N   
453  C CA  . ILE A 31  ? 0.4528 0.5388 0.5278 0.0009  0.0005  -0.0312 31  ILE A CA  
454  C C   . ILE A 31  ? 0.5355 0.6532 0.6053 0.0170  -0.0096 -0.0232 31  ILE A C   
455  O O   . ILE A 31  ? 0.4910 0.6294 0.5665 0.0128  -0.0144 -0.0329 31  ILE A O   
456  C CB  . ILE A 31  ? 0.3947 0.4328 0.4837 0.0050  0.0022  -0.0198 31  ILE A CB  
457  C CG1 . ILE A 31  ? 0.4844 0.4984 0.5817 -0.0070 0.0125  -0.0263 31  ILE A CG1 
458  C CG2 . ILE A 31  ? 0.4968 0.5235 0.5951 0.0045  -0.0036 -0.0205 31  ILE A CG2 
459  C CD1 . ILE A 31  ? 0.4563 0.4346 0.5713 -0.0037 0.0136  -0.0176 31  ILE A CD1 
471  N N   . ILE A 32  ? 0.4429 0.5614 0.5031 0.0377  -0.0105 -0.0035 32  ILE A N   
472  C CA  . ILE A 32  ? 0.4460 0.5898 0.5038 0.0584  -0.0175 0.0080  32  ILE A CA  
473  C C   . ILE A 32  ? 0.4255 0.6350 0.4776 0.0560  -0.0258 -0.0052 32  ILE A C   
474  O O   . ILE A 32  ? 0.4281 0.6644 0.4900 0.0588  -0.0319 -0.0110 32  ILE A O   
475  C CB  . ILE A 32  ? 0.4683 0.5958 0.5143 0.0829  -0.0117 0.0343  32  ILE A CB  
476  C CG1 . ILE A 32  ? 0.4431 0.5085 0.5014 0.0795  -0.0018 0.0406  32  ILE A CG1 
477  C CG2 . ILE A 32  ? 0.4501 0.6106 0.4920 0.1087  -0.0169 0.0484  32  ILE A CG2 
478  C CD1 . ILE A 32  ? 0.4928 0.5317 0.5410 0.0989  0.0109  0.0641  32  ILE A CD1 
490  N N   . LYS A 33  ? 0.4583 0.6980 0.4959 0.0476  -0.0250 -0.0141 33  LYS A N   
491  C CA  . LYS A 33  ? 0.4659 0.7778 0.4982 0.0416  -0.0329 -0.0316 33  LYS A CA  
492  C C   . LYS A 33  ? 0.4311 0.7519 0.4822 0.0164  -0.0314 -0.0592 33  LYS A C   
493  O O   . LYS A 33  ? 0.4997 0.8713 0.5591 0.0184  -0.0391 -0.0685 33  LYS A O   
494  C CB  . LYS A 33  ? 0.5517 0.8883 0.5628 0.0323  -0.0294 -0.0397 33  LYS A CB  
495  C CG  . LYS A 33  ? 0.5891 0.9996 0.5968 0.0120  -0.0339 -0.0711 33  LYS A CG  
496  C CD  . LYS A 33  ? 0.6765 1.1082 0.6607 -0.0016 -0.0275 -0.0837 33  LYS A CD  
497  C CE  . LYS A 33  ? 0.6672 1.1675 0.6521 -0.0296 -0.0282 -0.1229 33  LYS A CE  
498  N NZ  . LYS A 33  ? 0.7136 1.2963 0.7001 -0.0123 -0.0474 -0.1210 33  LYS A NZ  
512  N N   . GLN A 34  ? 0.4262 0.6999 0.4845 -0.0066 -0.0197 -0.0721 34  GLN A N   
513  C CA  . GLN A 34  ? 0.4667 0.7430 0.5391 -0.0312 -0.0131 -0.0971 34  GLN A CA  
514  C C   . GLN A 34  ? 0.4970 0.7642 0.5822 -0.0226 -0.0178 -0.0902 34  GLN A C   
515  O O   . GLN A 34  ? 0.5375 0.8308 0.6327 -0.0371 -0.0151 -0.1095 34  GLN A O   
516  C CB  . GLN A 34  ? 0.5179 0.7365 0.5951 -0.0509 0.0028  -0.1052 34  GLN A CB  
517  C CG  . GLN A 34  ? 0.6288 0.8524 0.6977 -0.0668 0.0138  -0.1204 34  GLN A CG  
518  C CD  . GLN A 34  ? 0.6806 0.8479 0.7585 -0.0856 0.0338  -0.1300 34  GLN A CD  
519  O OE1 . GLN A 34  ? 0.6884 0.8185 0.7768 -0.0882 0.0392  -0.1266 34  GLN A OE1 
520  N NE2 . GLN A 34  ? 0.8110 0.9742 0.8832 -0.0977 0.0465  -0.1419 34  GLN A NE2 
529  N N   . VAL A 35  ? 0.4598 0.6863 0.5454 -0.0025 -0.0216 -0.0658 35  VAL A N   
530  C CA  . VAL A 35  ? 0.4237 0.6390 0.5195 0.0050  -0.0243 -0.0607 35  VAL A CA  
531  C C   . VAL A 35  ? 0.4555 0.7288 0.5557 0.0210  -0.0329 -0.0596 35  VAL A C   
532  O O   . VAL A 35  ? 0.4637 0.7542 0.5758 0.0177  -0.0329 -0.0690 35  VAL A O   
533  C CB  . VAL A 35  ? 0.4874 0.6485 0.5829 0.0193  -0.0242 -0.0395 35  VAL A CB  
534  C CG1 . VAL A 35  ? 0.4737 0.6307 0.5768 0.0310  -0.0266 -0.0337 35  VAL A CG1 
535  C CG2 . VAL A 35  ? 0.4556 0.5674 0.5526 0.0029  -0.0170 -0.0429 35  VAL A CG2 
545  N N   . LYS A 36  ? 0.5230 0.8285 0.6134 0.0411  -0.0397 -0.0463 36  LYS A N   
546  C CA  . LYS A 36  ? 0.4262 0.7932 0.5214 0.0629  -0.0489 -0.0408 36  LYS A CA  
547  C C   . LYS A 36  ? 0.4628 0.9035 0.5668 0.0448  -0.0533 -0.0695 36  LYS A C   
548  O O   . LYS A 36  ? 0.5030 0.9944 0.6218 0.0552  -0.0592 -0.0734 36  LYS A O   
549  C CB  . LYS A 36  ? 0.4827 0.8662 0.5606 0.0910  -0.0536 -0.0161 36  LYS A CB  
550  C CG  . LYS A 36  ? 0.6174 1.0551 0.7014 0.1237  -0.0619 -0.0011 36  LYS A CG  
551  C CD  . LYS A 36  ? 0.6707 1.1322 0.7318 0.1528  -0.0658 0.0251  36  LYS A CD  
552  C CE  . LYS A 36  ? 0.8179 1.3486 0.8846 0.1892  -0.0755 0.0412  36  LYS A CE  
553  N NZ  . LYS A 36  ? 0.7544 1.3195 0.7931 0.2167  -0.0805 0.0661  36  LYS A NZ  
567  N N   . GLU A 37  ? 0.5150 0.9659 0.6121 0.0174  -0.0487 -0.0917 37  GLU A N   
568  C CA  . GLU A 37  ? 0.4749 0.9924 0.5827 -0.0072 -0.0483 -0.1257 37  GLU A CA  
569  C C   . GLU A 37  ? 0.4583 0.9527 0.5849 -0.0302 -0.0366 -0.1449 37  GLU A C   
570  O O   . GLU A 37  ? 0.4597 1.0119 0.6035 -0.0413 -0.0368 -0.1673 37  GLU A O   
571  C CB  . GLU A 37  ? 0.4906 1.0174 0.5864 -0.0342 -0.0409 -0.1482 37  GLU A CB  
572  C CG  . GLU A 37  ? 0.5544 1.1263 0.6294 -0.0202 -0.0511 -0.1402 37  GLU A CG  
573  C CD  . GLU A 37  ? 0.6557 1.2300 0.7201 -0.0526 -0.0392 -0.1683 37  GLU A CD  
574  O OE1 . GLU A 37  ? 0.6737 1.1891 0.7462 -0.0796 -0.0205 -0.1840 37  GLU A OE1 
575  O OE2 . GLU A 37  ? 0.7348 1.3735 0.7826 -0.0509 -0.0474 -0.1755 37  GLU A OE2 
582  N N   . ALA A 38  ? 0.4586 0.8720 0.5818 -0.0385 -0.0252 -0.1374 38  ALA A N   
583  C CA  . ALA A 38  ? 0.5045 0.8910 0.6393 -0.0592 -0.0118 -0.1522 38  ALA A CA  
584  C C   . ALA A 38  ? 0.4582 0.8523 0.6044 -0.0420 -0.0171 -0.1423 38  ALA A C   
585  O O   . ALA A 38  ? 0.5761 0.9716 0.7334 -0.0591 -0.0066 -0.1587 38  ALA A O   
586  C CB  . ALA A 38  ? 0.4756 0.7775 0.6007 -0.0686 0.0006  -0.1433 38  ALA A CB  
592  N N   . SER A 39  ? 0.3882 0.7816 0.5319 -0.0095 -0.0291 -0.1161 39  SER A N   
593  C CA  . SER A 39  ? 0.3682 0.7698 0.5244 0.0086  -0.0315 -0.1076 39  SER A CA  
594  C C   . SER A 39  ? 0.4343 0.9176 0.6046 0.0292  -0.0423 -0.1081 39  SER A C   
595  O O   . SER A 39  ? 0.4727 0.9606 0.6529 0.0540  -0.0443 -0.0938 39  SER A O   
596  C CB  . SER A 39  ? 0.4485 0.7894 0.5953 0.0310  -0.0325 -0.0797 39  SER A CB  
597  O OG  . SER A 39  ? 0.4605 0.8121 0.5996 0.0569  -0.0405 -0.0588 39  SER A OG  
603  N N   . ASN A 40  ? 0.4604 1.0099 0.6311 0.0227  -0.0494 -0.1222 40  ASN A N   
604  C CA  . ASN A 40  ? 0.3977 1.0399 0.5821 0.0438  -0.0625 -0.1230 40  ASN A CA  
605  C C   . ASN A 40  ? 0.3627 0.9969 0.5424 0.0898  -0.0703 -0.0852 40  ASN A C   
606  O O   . ASN A 40  ? 0.3931 1.0826 0.5902 0.1163  -0.0767 -0.0778 40  ASN A O   
607  C CB  . ASN A 40  ? 0.3945 1.0878 0.6084 0.0288  -0.0578 -0.1500 40  ASN A CB  
608  C CG  . ASN A 40  ? 0.4064 1.1057 0.6249 -0.0190 -0.0446 -0.1890 40  ASN A CG  
609  O OD1 . ASN A 40  ? 0.4517 1.1814 0.6615 -0.0372 -0.0462 -0.2061 40  ASN A OD1 
610  N ND2 . ASN A 40  ? 0.3908 1.0506 0.6188 -0.0396 -0.0281 -0.2017 40  ASN A ND2 
617  N N   . GLY A 41  ? 0.4226 0.9894 0.5797 0.0999  -0.0676 -0.0614 41  GLY A N   
618  C CA  . GLY A 41  ? 0.4225 0.9741 0.5712 0.1412  -0.0699 -0.0253 41  GLY A CA  
619  C C   . GLY A 41  ? 0.5036 0.9882 0.6602 0.1534  -0.0584 -0.0110 41  GLY A C   
620  O O   . GLY A 41  ? 0.6345 1.0905 0.7848 0.1851  -0.0539 0.0181  41  GLY A O   
624  N N   . GLU A 42  ? 0.5147 0.9730 0.6833 0.1283  -0.0510 -0.0313 42  GLU A N   
625  C CA  . GLU A 42  ? 0.5617 0.9649 0.7374 0.1364  -0.0398 -0.0233 42  GLU A CA  
626  C C   . GLU A 42  ? 0.6044 0.9253 0.7623 0.1349  -0.0326 -0.0084 42  GLU A C   
627  O O   . GLU A 42  ? 0.6523 0.9305 0.8117 0.1528  -0.0230 0.0069  42  GLU A O   
628  C CB  . GLU A 42  ? 0.5299 0.9297 0.7168 0.1068  -0.0336 -0.0500 42  GLU A CB  
629  C CG  . GLU A 42  ? 0.5098 0.9888 0.7218 0.1051  -0.0358 -0.0694 42  GLU A CG  
630  C CD  . GLU A 42  ? 0.6685 1.1338 0.8873 0.0712  -0.0247 -0.0961 42  GLU A CD  
631  O OE1 . GLU A 42  ? 0.7439 1.1390 0.9462 0.0540  -0.0165 -0.0959 42  GLU A OE1 
632  O OE2 . GLU A 42  ? 0.6514 1.1794 0.8919 0.0625  -0.0234 -0.1169 42  GLU A OE2 
639  N N   . MET A 43  ? 0.5208 0.8188 0.6645 0.1124  -0.0349 -0.0148 43  MET A N   
640  C CA  . MET A 43  ? 0.5131 0.7402 0.6453 0.1072  -0.0285 -0.0052 43  MET A CA  
641  C C   . MET A 43  ? 0.5072 0.7354 0.6249 0.1133  -0.0316 0.0071  43  MET A C   
642  O O   . MET A 43  ? 0.4890 0.7310 0.6000 0.0937  -0.0357 -0.0051 43  MET A O   
643  C CB  . MET A 43  ? 0.5439 0.7371 0.6736 0.0765  -0.0262 -0.0224 43  MET A CB  
644  C CG  . MET A 43  ? 0.5898 0.7213 0.7114 0.0711  -0.0221 -0.0147 43  MET A CG  
645  S SD  . MET A 43  ? 0.6005 0.7035 0.7180 0.0416  -0.0209 -0.0307 43  MET A SD  
646  C CE  . MET A 43  ? 0.6807 0.7304 0.7938 0.0421  -0.0196 -0.0201 43  MET A CE  
656  N N   . GLU A 44  ? 0.5901 0.7991 0.7026 0.1398  -0.0260 0.0310  44  GLU A N   
657  C CA  . GLU A 44  ? 0.6356 0.8396 0.7313 0.1500  -0.0250 0.0476  44  GLU A CA  
658  C C   . GLU A 44  ? 0.5872 0.7183 0.6801 0.1490  -0.0115 0.0583  44  GLU A C   
659  O O   . GLU A 44  ? 0.6346 0.7355 0.7305 0.1692  0.0009  0.0743  44  GLU A O   
660  C CB  . GLU A 44  ? 0.6404 0.8889 0.7303 0.1852  -0.0271 0.0693  44  GLU A CB  
661  C CG  . GLU A 44  ? 0.7844 1.0533 0.8507 0.1917  -0.0305 0.0815  44  GLU A CG  
662  C CD  . GLU A 44  ? 1.0135 1.3467 1.0700 0.2280  -0.0373 0.1028  44  GLU A CD  
663  O OE1 . GLU A 44  ? 1.0550 1.4170 1.1277 0.2494  -0.0390 0.1083  44  GLU A OE1 
664  O OE2 . GLU A 44  ? 0.9970 1.3532 1.0291 0.2369  -0.0402 0.1151  44  GLU A OE2 
671  N N   . LEU A 45  ? 0.5667 0.6709 0.6565 0.1245  -0.0119 0.0474  45  LEU A N   
672  C CA  . LEU A 45  ? 0.5477 0.5928 0.6398 0.1189  -0.0006 0.0522  45  LEU A CA  
673  C C   . LEU A 45  ? 0.6113 0.6385 0.6911 0.1339  0.0103  0.0725  45  LEU A C   
674  O O   . LEU A 45  ? 0.6298 0.6900 0.6942 0.1428  0.0061  0.0808  45  LEU A O   
675  C CB  . LEU A 45  ? 0.5663 0.5959 0.6627 0.0910  -0.0053 0.0349  45  LEU A CB  
676  C CG  . LEU A 45  ? 0.5811 0.6218 0.6851 0.0767  -0.0127 0.0177  45  LEU A CG  
677  C CD1 . LEU A 45  ? 0.5376 0.5674 0.6428 0.0539  -0.0164 0.0051  45  LEU A CD1 
678  C CD2 . LEU A 45  ? 0.5347 0.5457 0.6467 0.0798  -0.0066 0.0176  45  LEU A CD2 
690  N N   . ASN A 46  ? 0.6688 0.6449 0.7539 0.1359  0.0261  0.0795  46  ASN A N   
691  C CA  . ASN A 46  ? 0.7024 0.6516 0.7762 0.1472  0.0419  0.0984  46  ASN A CA  
692  C C   . ASN A 46  ? 0.6824 0.6029 0.7635 0.1223  0.0456  0.0863  46  ASN A C   
693  O O   . ASN A 46  ? 0.6510 0.5636 0.7480 0.1017  0.0390  0.0672  46  ASN A O   
694  C CB  . ASN A 46  ? 0.7591 0.6700 0.8348 0.1694  0.0637  0.1164  46  ASN A CB  
695  C CG  . ASN A 46  ? 0.8758 0.7285 0.9608 0.1564  0.0848  0.1134  46  ASN A CG  
696  O OD1 . ASN A 46  ? 0.8604 0.6882 0.9344 0.1633  0.1018  0.1293  46  ASN A OD1 
697  N ND2 . ASN A 46  ? 0.8807 0.7135 0.9858 0.1357  0.0852  0.0913  46  ASN A ND2 
704  N N   . GLU A 47  ? 0.6879 0.6005 0.7559 0.1258  0.0550  0.0982  47  GLU A N   
705  C CA  . GLU A 47  ? 0.6725 0.5641 0.7488 0.1050  0.0604  0.0882  47  GLU A CA  
706  C C   . GLU A 47  ? 0.6323 0.4890 0.7340 0.0884  0.0676  0.0740  47  GLU A C   
707  O O   . GLU A 47  ? 0.6109 0.4711 0.7281 0.0686  0.0593  0.0572  47  GLU A O   
708  C CB  . GLU A 47  ? 0.7159 0.5878 0.7747 0.1164  0.0799  0.1080  47  GLU A CB  
709  C CG  . GLU A 47  ? 0.7487 0.6537 0.7863 0.1170  0.0731  0.1111  47  GLU A CG  
710  C CD  . GLU A 47  ? 0.8128 0.6937 0.8318 0.1256  0.0946  0.1296  47  GLU A CD  
711  O OE1 . GLU A 47  ? 0.8329 0.6992 0.8353 0.1503  0.1079  0.1542  47  GLU A OE1 
712  O OE2 . GLU A 47  ? 0.8389 0.7159 0.8589 0.1093  0.0995  0.1209  47  GLU A OE2 
719  N N   . ALA A 48  ? 0.6172 0.4403 0.7232 0.0974  0.0857  0.0813  48  ALA A N   
720  C CA  . ALA A 48  ? 0.5930 0.3842 0.7226 0.0795  0.0970  0.0651  48  ALA A CA  
721  C C   . ALA A 48  ? 0.6425 0.4532 0.7859 0.0645  0.0774  0.0437  48  ALA A C   
722  O O   . ALA A 48  ? 0.6772 0.4847 0.8396 0.0444  0.0749  0.0257  48  ALA A O   
723  C CB  . ALA A 48  ? 0.6305 0.3790 0.7604 0.0920  0.1248  0.0753  48  ALA A CB  
729  N N   . THR A 49  ? 0.6629 0.4972 0.7972 0.0743  0.0638  0.0452  49  THR A N   
730  C CA  . THR A 49  ? 0.6235 0.4744 0.7667 0.0596  0.0470  0.0263  49  THR A CA  
731  C C   . THR A 49  ? 0.5365 0.4074 0.6838 0.0449  0.0312  0.0178  49  THR A C   
732  O O   . THR A 49  ? 0.5641 0.4372 0.7238 0.0299  0.0236  0.0034  49  THR A O   
733  C CB  . THR A 49  ? 0.6208 0.4946 0.7546 0.0708  0.0374  0.0283  49  THR A CB  
734  O OG1 . THR A 49  ? 0.7129 0.5729 0.8418 0.0927  0.0533  0.0433  49  THR A OG1 
735  C CG2 . THR A 49  ? 0.7354 0.6104 0.8764 0.0572  0.0304  0.0101  49  THR A CG2 
743  N N   . LEU A 50  ? 0.5191 0.4056 0.6562 0.0495  0.0275  0.0263  50  LEU A N   
744  C CA  . LEU A 50  ? 0.4937 0.3943 0.6365 0.0366  0.0168  0.0181  50  LEU A CA  
745  C C   . LEU A 50  ? 0.5138 0.3988 0.6758 0.0258  0.0233  0.0122  50  LEU A C   
746  O O   . LEU A 50  ? 0.4997 0.3934 0.6750 0.0157  0.0139  0.0029  50  LEU A O   
747  C CB  . LEU A 50  ? 0.4886 0.4077 0.6169 0.0408  0.0158  0.0242  50  LEU A CB  
748  C CG  . LEU A 50  ? 0.5049 0.4526 0.6238 0.0390  0.0038  0.0182  50  LEU A CG  
749  C CD1 . LEU A 50  ? 0.5357 0.4955 0.6460 0.0525  0.0024  0.0239  50  LEU A CD1 
750  C CD2 . LEU A 50  ? 0.5342 0.5019 0.6424 0.0361  0.0042  0.0166  50  LEU A CD2 
762  N N   . TYR A 51  ? 0.5350 0.3987 0.6995 0.0288  0.0409  0.0186  51  TYR A N   
763  C CA  . TYR A 51  ? 0.5230 0.3775 0.7097 0.0162  0.0488  0.0105  51  TYR A CA  
764  C C   . TYR A 51  ? 0.5266 0.3829 0.7344 0.0036  0.0439  -0.0063 51  TYR A C   
765  O O   . TYR A 51  ? 0.5524 0.4247 0.7808 -0.0070 0.0362  -0.0171 51  TYR A O   
766  C CB  . TYR A 51  ? 0.5534 0.3804 0.7369 0.0204  0.0735  0.0207  51  TYR A CB  
767  C CG  . TYR A 51  ? 0.5610 0.3932 0.7217 0.0312  0.0777  0.0361  51  TYR A CG  
768  C CD1 . TYR A 51  ? 0.6397 0.4905 0.8028 0.0248  0.0706  0.0316  51  TYR A CD1 
769  C CD2 . TYR A 51  ? 0.5907 0.4098 0.7270 0.0485  0.0904  0.0551  51  TYR A CD2 
770  C CE1 . TYR A 51  ? 0.6508 0.5092 0.7894 0.0324  0.0759  0.0424  51  TYR A CE1 
771  C CE2 . TYR A 51  ? 0.6955 0.5258 0.8075 0.0585  0.0931  0.0686  51  TYR A CE2 
772  C CZ  . TYR A 51  ? 0.6634 0.5142 0.7754 0.0490  0.0858  0.0607  51  TYR A CZ  
773  O OH  . TYR A 51  ? 0.8187 0.6813 0.9013 0.0592  0.0913  0.0737  51  TYR A OH  
783  N N   . THR A 52  ? 0.5385 0.3828 0.7415 0.0053  0.0483  -0.0094 52  THR A N   
784  C CA  . THR A 52  ? 0.4933 0.3446 0.7111 -0.0084 0.0427  -0.0285 52  THR A CA  
785  C C   . THR A 52  ? 0.4854 0.3687 0.7024 -0.0113 0.0177  -0.0334 52  THR A C   
786  O O   . THR A 52  ? 0.4915 0.3950 0.7262 -0.0219 0.0085  -0.0455 52  THR A O   
787  C CB  . THR A 52  ? 0.5651 0.3981 0.7719 -0.0034 0.0517  -0.0298 52  THR A CB  
788  O OG1 . THR A 52  ? 0.6034 0.4001 0.8109 0.0021  0.0794  -0.0225 52  THR A OG1 
789  C CG2 . THR A 52  ? 0.5707 0.4142 0.7876 -0.0193 0.0459  -0.0525 52  THR A CG2 
797  N N   . ILE A 53  ? 0.4729 0.3630 0.6693 -0.0010 0.0078  -0.0235 53  ILE A N   
798  C CA  . ILE A 53  ? 0.4850 0.3974 0.6772 -0.0029 -0.0109 -0.0257 53  ILE A CA  
799  C C   . ILE A 53  ? 0.4684 0.3923 0.6741 -0.0042 -0.0158 -0.0230 53  ILE A C   
800  O O   . ILE A 53  ? 0.4566 0.3989 0.6715 -0.0071 -0.0277 -0.0271 53  ILE A O   
801  C CB  . ILE A 53  ? 0.5242 0.4395 0.6941 0.0055  -0.0153 -0.0178 53  ILE A CB  
802  C CG1 . ILE A 53  ? 0.5966 0.5049 0.7576 0.0077  -0.0110 -0.0221 53  ILE A CG1 
803  C CG2 . ILE A 53  ? 0.5451 0.4746 0.7087 0.0038  -0.0280 -0.0170 53  ILE A CG2 
804  C CD1 . ILE A 53  ? 0.5929 0.5088 0.7373 0.0173  -0.0121 -0.0152 53  ILE A CD1 
816  N N   . PHE A 54  ? 0.4440 0.3593 0.6502 -0.0002 -0.0061 -0.0151 54  PHE A N   
817  C CA  . PHE A 54  ? 0.4579 0.3820 0.6775 -0.0006 -0.0077 -0.0132 54  PHE A CA  
818  C C   . PHE A 54  ? 0.4399 0.3743 0.6894 -0.0076 -0.0068 -0.0219 54  PHE A C   
819  O O   . PHE A 54  ? 0.4414 0.3923 0.7077 -0.0059 -0.0132 -0.0218 54  PHE A O   
820  C CB  . PHE A 54  ? 0.4600 0.3742 0.6709 0.0031  0.0044  -0.0057 54  PHE A CB  
821  C CG  . PHE A 54  ? 0.4898 0.4079 0.6776 0.0072  0.0011  -0.0013 54  PHE A CG  
822  C CD1 . PHE A 54  ? 0.4562 0.3811 0.6347 0.0074  -0.0095 -0.0029 54  PHE A CD1 
823  C CD2 . PHE A 54  ? 0.4546 0.3723 0.6294 0.0092  0.0103  0.0024  54  PHE A CD2 
824  C CE1 . PHE A 54  ? 0.4533 0.3836 0.6148 0.0075  -0.0094 -0.0027 54  PHE A CE1 
825  C CE2 . PHE A 54  ? 0.4677 0.3963 0.6250 0.0092  0.0079  0.0013  54  PHE A CE2 
826  C CZ  . PHE A 54  ? 0.4622 0.3967 0.6149 0.0074  -0.0012 -0.0023 54  PHE A CZ  
836  N N   . LYS A 55  ? 0.4364 0.3626 0.6957 -0.0154 0.0032  -0.0306 55  LYS A N   
837  C CA  . LYS A 55  ? 0.4488 0.3916 0.7408 -0.0259 0.0052  -0.0439 55  LYS A CA  
838  C C   . LYS A 55  ? 0.4994 0.4780 0.8023 -0.0274 -0.0158 -0.0519 55  LYS A C   
839  O O   . LYS A 55  ? 0.5511 0.5582 0.8799 -0.0273 -0.0228 -0.0555 55  LYS A O   
840  C CB  . LYS A 55  ? 0.5292 0.4537 0.8292 -0.0377 0.0233  -0.0557 55  LYS A CB  
841  C CG  . LYS A 55  ? 0.5118 0.4568 0.8514 -0.0539 0.0300  -0.0750 55  LYS A CG  
842  C CD  . LYS A 55  ? 0.5596 0.4830 0.9077 -0.0705 0.0519  -0.0922 55  LYS A CD  
843  C CE  . LYS A 55  ? 0.6219 0.5707 1.0119 -0.0901 0.0599  -0.1153 55  LYS A CE  
844  N NZ  . LYS A 55  ? 0.7284 0.6701 1.1332 -0.0868 0.0738  -0.1056 55  LYS A NZ  
858  N N   . ARG A 56  ? 0.5068 0.4866 0.7895 -0.0277 -0.0254 -0.0544 56  ARG A N   
859  C CA  . ARG A 56  ? 0.5288 0.5425 0.8122 -0.0283 -0.0453 -0.0605 56  ARG A CA  
860  C C   . ARG A 56  ? 0.5262 0.5516 0.8023 -0.0130 -0.0583 -0.0435 56  ARG A C   
861  O O   . ARG A 56  ? 0.5326 0.5920 0.8245 -0.0082 -0.0714 -0.0430 56  ARG A O   
862  C CB  . ARG A 56  ? 0.5257 0.5292 0.7838 -0.0326 -0.0467 -0.0665 56  ARG A CB  
863  C CG  . ARG A 56  ? 0.7022 0.7344 0.9462 -0.0309 -0.0662 -0.0684 56  ARG A CG  
864  C CD  . ARG A 56  ? 0.7232 0.7988 0.9881 -0.0425 -0.0767 -0.0880 56  ARG A CD  
865  N NE  . ARG A 56  ? 0.8941 1.0062 1.1438 -0.0354 -0.0987 -0.0837 56  ARG A NE  
866  C CZ  . ARG A 56  ? 0.8828 1.0040 1.1075 -0.0411 -0.1056 -0.0923 56  ARG A CZ  
867  N NH1 . ARG A 56  ? 0.8914 0.9853 1.1048 -0.0535 -0.0916 -0.1062 56  ARG A NH1 
868  N NH2 . ARG A 56  ? 0.9428 1.1018 1.1528 -0.0330 -0.1256 -0.0860 56  ARG A NH2 
882  N N   . LEU A 57  ? 0.4700 0.4684 0.7237 -0.0047 -0.0528 -0.0293 57  LEU A N   
883  C CA  . LEU A 57  ? 0.4719 0.4719 0.7192 0.0079  -0.0581 -0.0144 57  LEU A CA  
884  C C   . LEU A 57  ? 0.4702 0.4824 0.7473 0.0137  -0.0552 -0.0109 57  LEU A C   
885  O O   . LEU A 57  ? 0.4900 0.5213 0.7759 0.0253  -0.0641 -0.0023 57  LEU A O   
886  C CB  . LEU A 57  ? 0.4332 0.4040 0.6565 0.0102  -0.0480 -0.0063 57  LEU A CB  
887  C CG  . LEU A 57  ? 0.4429 0.4057 0.6397 0.0068  -0.0502 -0.0088 57  LEU A CG  
888  C CD1 . LEU A 57  ? 0.4785 0.4236 0.6573 0.0077  -0.0409 -0.0043 57  LEU A CD1 
889  C CD2 . LEU A 57  ? 0.4928 0.4680 0.6748 0.0096  -0.0627 -0.0061 57  LEU A CD2 
901  N N   . GLU A 58  ? 0.4614 0.4638 0.7548 0.0074  -0.0415 -0.0166 58  GLU A N   
902  C CA  . GLU A 58  ? 0.4954 0.5123 0.8213 0.0116  -0.0369 -0.0162 58  GLU A CA  
903  C C   . GLU A 58  ? 0.4541 0.5161 0.8099 0.0116  -0.0511 -0.0246 58  GLU A C   
904  O O   . GLU A 58  ? 0.4371 0.5238 0.8157 0.0241  -0.0566 -0.0179 58  GLU A O   
905  C CB  . GLU A 58  ? 0.5217 0.5189 0.8552 0.0020  -0.0176 -0.0223 58  GLU A CB  
906  C CG  . GLU A 58  ? 0.5767 0.5702 0.9275 0.0070  -0.0055 -0.0181 58  GLU A CG  
907  C CD  . GLU A 58  ? 0.6774 0.6454 1.0204 -0.0012 0.0149  -0.0206 58  GLU A CD  
908  O OE1 . GLU A 58  ? 0.6832 0.6334 1.0022 -0.0067 0.0187  -0.0208 58  GLU A OE1 
909  O OE2 . GLU A 58  ? 0.6398 0.6059 0.9991 -0.0001 0.0279  -0.0205 58  GLU A OE2 
916  N N   . LYS A 59  ? 0.4906 0.5668 0.8487 -0.0023 -0.0557 -0.0407 59  LYS A N   
917  C CA  . LYS A 59  ? 0.5021 0.6306 0.8890 -0.0070 -0.0697 -0.0550 59  LYS A CA  
918  C C   . LYS A 59  ? 0.4771 0.6391 0.8552 0.0101  -0.0922 -0.0426 59  LYS A C   
919  O O   . LYS A 59  ? 0.4402 0.6508 0.8470 0.0190  -0.1044 -0.0427 59  LYS A O   
920  C CB  . LYS A 59  ? 0.4952 0.6248 0.8784 -0.0284 -0.0668 -0.0775 59  LYS A CB  
921  C CG  . LYS A 59  ? 0.5574 0.7446 0.9619 -0.0377 -0.0827 -0.0974 59  LYS A CG  
922  C CD  . LYS A 59  ? 0.6178 0.8028 1.0369 -0.0660 -0.0675 -0.1281 59  LYS A CD  
923  C CE  . LYS A 59  ? 0.7050 0.8373 1.0871 -0.0723 -0.0547 -0.1280 59  LYS A CE  
924  N NZ  . LYS A 59  ? 0.8230 0.9664 1.1715 -0.0661 -0.0735 -0.1238 59  LYS A NZ  
938  N N   . ASP A 60  ? 0.5003 0.6380 0.8385 0.0167  -0.0965 -0.0300 60  ASP A N   
939  C CA  . ASP A 60  ? 0.5408 0.6975 0.8611 0.0349  -0.1128 -0.0127 60  ASP A CA  
940  C C   . ASP A 60  ? 0.5485 0.6873 0.8709 0.0570  -0.1062 0.0117  60  ASP A C   
941  O O   . ASP A 60  ? 0.5323 0.6792 0.8383 0.0753  -0.1152 0.0304  60  ASP A O   
942  C CB  . ASP A 60  ? 0.5404 0.6717 0.8170 0.0298  -0.1143 -0.0112 60  ASP A CB  
943  C CG  . ASP A 60  ? 0.6254 0.7770 0.8984 0.0098  -0.1204 -0.0358 60  ASP A CG  
944  O OD1 . ASP A 60  ? 0.6184 0.8096 0.9206 -0.0007 -0.1260 -0.0549 60  ASP A OD1 
945  O OD2 . ASP A 60  ? 0.7096 0.8355 0.9531 0.0027  -0.1162 -0.0389 60  ASP A OD2 
950  N N   . GLY A 61  ? 0.5171 0.6319 0.8591 0.0564  -0.0886 0.0122  61  GLY A N   
951  C CA  . GLY A 61  ? 0.4854 0.5808 0.8320 0.0755  -0.0780 0.0318  61  GLY A CA  
952  C C   . GLY A 61  ? 0.5018 0.5501 0.8103 0.0788  -0.0673 0.0449  61  GLY A C   
953  O O   . GLY A 61  ? 0.5931 0.6260 0.8987 0.0963  -0.0596 0.0631  61  GLY A O   
957  N N   . ILE A 62  ? 0.5123 0.5380 0.7934 0.0624  -0.0645 0.0354  62  ILE A N   
958  C CA  . ILE A 62  ? 0.5503 0.5375 0.7985 0.0616  -0.0534 0.0430  62  ILE A CA  
959  C C   . ILE A 62  ? 0.5577 0.5125 0.8049 0.0524  -0.0329 0.0371  62  ILE A C   
960  O O   . ILE A 62  ? 0.5464 0.4730 0.7755 0.0527  -0.0197 0.0424  62  ILE A O   
961  C CB  . ILE A 62  ? 0.5477 0.5373 0.7683 0.0506  -0.0633 0.0354  62  ILE A CB  
962  C CG1 . ILE A 62  ? 0.6192 0.6363 0.8289 0.0610  -0.0808 0.0440  62  ILE A CG1 
963  C CG2 . ILE A 62  ? 0.5533 0.5095 0.7454 0.0438  -0.0509 0.0360  62  ILE A CG2 
964  C CD1 . ILE A 62  ? 0.6818 0.7120 0.8750 0.0475  -0.0912 0.0298  62  ILE A CD1 
976  N N   . ILE A 63  ? 0.5656 0.5251 0.8296 0.0425  -0.0284 0.0249  63  ILE A N   
977  C CA  . ILE A 63  ? 0.4498 0.3875 0.7135 0.0350  -0.0100 0.0191  63  ILE A CA  
978  C C   . ILE A 63  ? 0.4678 0.4181 0.7641 0.0352  -0.0046 0.0142  63  ILE A C   
979  O O   . ILE A 63  ? 0.4259 0.4036 0.7447 0.0377  -0.0159 0.0121  63  ILE A O   
980  C CB  . ILE A 63  ? 0.4544 0.3838 0.6950 0.0220  -0.0082 0.0101  63  ILE A CB  
981  C CG1 . ILE A 63  ? 0.4212 0.3642 0.6727 0.0165  -0.0138 0.0031  63  ILE A CG1 
982  C CG2 . ILE A 63  ? 0.4885 0.4129 0.7023 0.0209  -0.0147 0.0125  63  ILE A CG2 
983  C CD1 . ILE A 63  ? 0.3984 0.3319 0.6290 0.0092  -0.0097 -0.0014 63  ILE A CD1 
995  N N   . SER A 64  ? 0.5061 0.4390 0.8043 0.0303  0.0139  0.0099  64  SER A N   
996  C CA  . SER A 64  ? 0.4678 0.4074 0.7928 0.0278  0.0244  0.0039  64  SER A CA  
997  C C   . SER A 64  ? 0.4570 0.3776 0.7620 0.0162  0.0407  -0.0033 64  SER A C   
998  O O   . SER A 64  ? 0.4938 0.4023 0.7689 0.0113  0.0422  -0.0044 64  SER A O   
999  C CB  . SER A 64  ? 0.5035 0.4463 0.8586 0.0403  0.0334  0.0090  64  SER A CB  
1000 O OG  . SER A 64  ? 0.4753 0.3894 0.8189 0.0391  0.0535  0.0084  64  SER A OG  
1006 N N   . SER A 65  ? 0.4967 0.4193 0.8172 0.0114  0.0525  -0.0088 65  SER A N   
1007 C CA  . SER A 65  ? 0.5214 0.4305 0.8181 0.0018  0.0672  -0.0138 65  SER A CA  
1008 C C   . SER A 65  ? 0.4325 0.3367 0.7468 -0.0006 0.0881  -0.0194 65  SER A C   
1009 O O   . SER A 65  ? 0.4193 0.3326 0.7701 0.0054  0.0911  -0.0196 65  SER A O   
1010 C CB  . SER A 65  ? 0.5369 0.4470 0.8216 -0.0032 0.0650  -0.0131 65  SER A CB  
1011 O OG  . SER A 65  ? 0.5540 0.4735 0.8715 -0.0046 0.0671  -0.0160 65  SER A OG  
1017 N N   . TYR A 66  ? 0.5082 0.4025 0.7965 -0.0091 0.1025  -0.0248 66  TYR A N   
1018 C CA  . TYR A 66  ? 0.4862 0.3740 0.7851 -0.0137 0.1256  -0.0325 66  TYR A CA  
1019 C C   . TYR A 66  ? 0.5820 0.4665 0.8405 -0.0238 0.1363  -0.0374 66  TYR A C   
1020 O O   . TYR A 66  ? 0.5617 0.4517 0.7883 -0.0251 0.1251  -0.0351 66  TYR A O   
1021 C CB  . TYR A 66  ? 0.5019 0.3811 0.8192 -0.0092 0.1351  -0.0365 66  TYR A CB  
1022 C CG  . TYR A 66  ? 0.5147 0.3833 0.8019 -0.0154 0.1375  -0.0422 66  TYR A CG  
1023 C CD1 . TYR A 66  ? 0.5310 0.3930 0.7963 -0.0288 0.1569  -0.0568 66  TYR A CD1 
1024 C CD2 . TYR A 66  ? 0.4541 0.3228 0.7328 -0.0107 0.1212  -0.0357 66  TYR A CD2 
1025 C CE1 . TYR A 66  ? 0.4825 0.3403 0.7228 -0.0389 0.1608  -0.0675 66  TYR A CE1 
1026 C CE2 . TYR A 66  ? 0.5257 0.3864 0.7797 -0.0193 0.1259  -0.0436 66  TYR A CE2 
1027 C CZ  . TYR A 66  ? 0.5236 0.3802 0.7602 -0.0342 0.1457  -0.0606 66  TYR A CZ  
1028 O OH  . TYR A 66  ? 0.5353 0.3890 0.7507 -0.0465 0.1518  -0.0734 66  TYR A OH  
1038 N N   . TRP A 67  ? 0.6555 0.5352 0.9146 -0.0303 0.1582  -0.0446 67  TRP A N   
1039 C CA  . TRP A 67  ? 0.7156 0.5982 0.9323 -0.0385 0.1679  -0.0475 67  TRP A CA  
1040 C C   . TRP A 67  ? 0.7445 0.6289 0.9417 -0.0491 0.1803  -0.0639 67  TRP A C   
1041 O O   . TRP A 67  ? 0.6520 0.5249 0.8743 -0.0520 0.1956  -0.0749 67  TRP A O   
1042 C CB  . TRP A 67  ? 0.8796 0.7562 1.0982 -0.0414 0.1870  -0.0454 67  TRP A CB  
1043 C CG  . TRP A 67  ? 0.8729 0.7458 1.1009 -0.0357 0.1801  -0.0320 67  TRP A CG  
1044 C CD1 . TRP A 67  ? 0.8434 0.7155 1.1159 -0.0341 0.1805  -0.0322 67  TRP A CD1 
1045 C CD2 . TRP A 67  ? 0.8577 0.7287 1.0523 -0.0309 0.1729  -0.0181 67  TRP A CD2 
1046 N NE1 . TRP A 67  ? 0.8681 0.7350 1.1368 -0.0325 0.1758  -0.0227 67  TRP A NE1 
1047 C CE2 . TRP A 67  ? 0.8403 0.7021 1.0613 -0.0290 0.1726  -0.0122 67  TRP A CE2 
1048 C CE3 . TRP A 67  ? 0.9278 0.8070 1.0745 -0.0271 0.1675  -0.0105 67  TRP A CE3 
1049 C CZ2 . TRP A 67  ? 0.8889 0.7397 1.0897 -0.0237 0.1716  0.0014  67  TRP A CZ2 
1050 C CZ3 . TRP A 67  ? 0.9730 0.8456 1.1000 -0.0174 0.1634  0.0068  67  TRP A CZ3 
1051 C CH2 . TRP A 67  ? 0.9227 0.7766 1.0764 -0.0159 0.1672  0.0128  67  TRP A CH2 
1062 N N   . GLY A 68  ? 0.7475 0.6488 0.9010 -0.0548 0.1757  -0.0669 68  GLY A N   
1063 C CA  . GLY A 68  ? 0.9625 0.8743 1.0927 -0.0696 0.1882  -0.0875 68  GLY A CA  
1064 C C   . GLY A 68  ? 1.1863 1.1040 1.2924 -0.0788 0.2092  -0.0959 68  GLY A C   
1065 O O   . GLY A 68  ? 1.1773 1.0808 1.2972 -0.0752 0.2221  -0.0888 68  GLY A O   
1069 N N   . ASP A 69  ? 1.2510 1.1929 1.3213 -0.0927 0.2141  -0.1138 69  ASP A N   
1070 C CA  . ASP A 69  ? 1.2664 1.2239 1.3002 -0.1009 0.2301  -0.1204 69  ASP A CA  
1071 C C   . ASP A 69  ? 1.2619 1.2556 1.2596 -0.1197 0.2333  -0.1469 69  ASP A C   
1072 O O   . ASP A 69  ? 1.2446 1.2771 1.2098 -0.1168 0.2134  -0.1431 69  ASP A O   
1073 C CB  . ASP A 69  ? 1.2938 1.2231 1.3516 -0.1061 0.2595  -0.1274 69  ASP A CB  
1074 C CG  . ASP A 69  ? 1.3161 1.2238 1.4096 -0.1175 0.2795  -0.1512 69  ASP A CG  
1075 O OD1 . ASP A 69  ? 1.2531 1.1712 1.3333 -0.1334 0.2852  -0.1750 69  ASP A OD1 
1076 O OD2 . ASP A 69  ? 1.3094 1.1902 1.4461 -0.1105 0.2927  -0.1470 69  ASP A OD2 
1081 N N   . ARG A 75  ? 1.4751 1.4368 1.4241 -0.0302 0.1930  -0.0076 75  ARG A N   
1082 C CA  . ARG A 75  ? 1.4872 1.4289 1.4898 -0.0390 0.1902  -0.0225 75  ARG A CA  
1083 C C   . ARG A 75  ? 1.3701 1.3067 1.3920 -0.0264 0.1677  -0.0093 75  ARG A C   
1084 O O   . ARG A 75  ? 1.3787 1.2954 1.4050 -0.0149 0.1690  0.0101  75  ARG A O   
1085 C CB  . ARG A 75  ? 1.4878 1.3978 1.5222 -0.0451 0.2137  -0.0251 75  ARG A CB  
1086 C CG  . ARG A 75  ? 1.4842 1.3846 1.5666 -0.0553 0.2177  -0.0455 75  ARG A CG  
1087 C CD  . ARG A 75  ? 1.5213 1.3998 1.6405 -0.0600 0.2412  -0.0500 75  ARG A CD  
1088 N NE  . ARG A 75  ? 1.5953 1.4689 1.7593 -0.0641 0.2437  -0.0661 75  ARG A NE  
1089 C CZ  . ARG A 75  ? 1.6069 1.4692 1.8192 -0.0635 0.2562  -0.0699 75  ARG A CZ  
1090 N NH1 . ARG A 75  ? 1.7065 1.5611 1.9322 -0.0635 0.2694  -0.0632 75  ARG A NH1 
1091 N NH2 . ARG A 75  ? 1.4258 1.2853 1.6749 -0.0620 0.2572  -0.0802 75  ARG A NH2 
1104 N N   . ARG A 76  ? 1.0557 1.0070 1.0899 -0.0303 0.1508  -0.0214 76  ARG A N   
1105 C CA  . ARG A 76  ? 0.9026 0.8523 0.9505 -0.0198 0.1303  -0.0112 76  ARG A CA  
1106 C C   . ARG A 76  ? 0.7720 0.6984 0.8667 -0.0229 0.1278  -0.0164 76  ARG A C   
1107 O O   . ARG A 76  ? 0.7823 0.7001 0.9002 -0.0322 0.1381  -0.0300 76  ARG A O   
1108 C CB  . ARG A 76  ? 0.8132 0.7974 0.8428 -0.0211 0.1129  -0.0196 76  ARG A CB  
1109 C CG  . ARG A 76  ? 0.9699 0.9840 0.9593 -0.0070 0.1050  -0.0043 76  ARG A CG  
1110 C CD  . ARG A 76  ? 0.9830 1.0465 0.9515 -0.0106 0.0907  -0.0168 76  ARG A CD  
1111 N NE  . ARG A 76  ? 1.1514 1.2495 1.0803 0.0072  0.0847  0.0013  76  ARG A NE  
1112 C CZ  . ARG A 76  ? 1.3090 1.4650 1.2100 0.0050  0.0750  -0.0092 76  ARG A CZ  
1113 N NH1 . ARG A 76  ? 1.5021 1.6848 1.4104 -0.0185 0.0736  -0.0415 76  ARG A NH1 
1114 N NH2 . ARG A 76  ? 1.2955 1.4853 1.1610 0.0273  0.0682  0.0129  76  ARG A NH2 
1128 N N   . LYS A 77  ? 0.6814 0.5995 0.7894 -0.0136 0.1148  -0.0049 77  LYS A N   
1129 C CA  . LYS A 77  ? 0.6112 0.5177 0.7581 -0.0146 0.1068  -0.0088 77  LYS A CA  
1130 C C   . LYS A 77  ? 0.5823 0.5010 0.7274 -0.0159 0.0913  -0.0157 77  LYS A C   
1131 O O   . LYS A 77  ? 0.5706 0.5018 0.6972 -0.0106 0.0786  -0.0106 77  LYS A O   
1132 C CB  . LYS A 77  ? 0.5381 0.4318 0.6976 -0.0073 0.1029  0.0030  77  LYS A CB  
1133 C CG  . LYS A 77  ? 0.5828 0.4714 0.7835 -0.0096 0.0971  -0.0022 77  LYS A CG  
1134 C CD  . LYS A 77  ? 0.6937 0.5712 0.9059 -0.0075 0.0978  0.0038  77  LYS A CD  
1135 C CE  . LYS A 77  ? 0.7489 0.6321 1.0040 -0.0120 0.0917  -0.0049 77  LYS A CE  
1136 N NZ  . LYS A 77  ? 0.8378 0.7224 1.1235 -0.0183 0.1071  -0.0120 77  LYS A NZ  
1150 N N   . TYR A 78  ? 0.5369 0.4502 0.7024 -0.0221 0.0952  -0.0266 78  TYR A N   
1151 C CA  . TYR A 78  ? 0.5249 0.4416 0.6904 -0.0249 0.0869  -0.0333 78  TYR A CA  
1152 C C   . TYR A 78  ? 0.4555 0.3626 0.6473 -0.0169 0.0749  -0.0254 78  TYR A C   
1153 O O   . TYR A 78  ? 0.4957 0.3968 0.7133 -0.0122 0.0763  -0.0208 78  TYR A O   
1154 C CB  . TYR A 78  ? 0.5764 0.4873 0.7443 -0.0364 0.1047  -0.0498 78  TYR A CB  
1155 C CG  . TYR A 78  ? 0.5700 0.5025 0.7048 -0.0486 0.1119  -0.0638 78  TYR A CG  
1156 C CD1 . TYR A 78  ? 0.6591 0.5995 0.7779 -0.0513 0.1227  -0.0653 78  TYR A CD1 
1157 C CD2 . TYR A 78  ? 0.5822 0.5331 0.7004 -0.0571 0.1064  -0.0751 78  TYR A CD2 
1158 C CE1 . TYR A 78  ? 0.7178 0.6874 0.8025 -0.0610 0.1261  -0.0775 78  TYR A CE1 
1159 C CE2 . TYR A 78  ? 0.6119 0.5953 0.7014 -0.0684 0.1094  -0.0899 78  TYR A CE2 
1160 C CZ  . TYR A 78  ? 0.7295 0.7241 0.8008 -0.0695 0.1181  -0.0905 78  TYR A CZ  
1161 O OH  . TYR A 78  ? 0.7550 0.7896 0.7945 -0.0797 0.1196  -0.1050 78  TYR A OH  
1171 N N   . TYR A 79  ? 0.5268 0.4381 0.7106 -0.0155 0.0621  -0.0241 79  TYR A N   
1172 C CA  . TYR A 79  ? 0.4800 0.3859 0.6820 -0.0081 0.0500  -0.0169 79  TYR A CA  
1173 C C   . TYR A 79  ? 0.4670 0.3626 0.6698 -0.0100 0.0552  -0.0203 79  TYR A C   
1174 O O   . TYR A 79  ? 0.5011 0.3977 0.6861 -0.0196 0.0629  -0.0302 79  TYR A O   
1175 C CB  . TYR A 79  ? 0.4418 0.3560 0.6333 -0.0039 0.0333  -0.0108 79  TYR A CB  
1176 C CG  . TYR A 79  ? 0.4697 0.3844 0.6653 -0.0010 0.0334  -0.0061 79  TYR A CG  
1177 C CD1 . TYR A 79  ? 0.4629 0.3806 0.6379 -0.0005 0.0396  -0.0037 79  TYR A CD1 
1178 C CD2 . TYR A 79  ? 0.5069 0.4202 0.7275 0.0009  0.0302  -0.0046 79  TYR A CD2 
1179 C CE1 . TYR A 79  ? 0.4739 0.3835 0.6504 0.0030  0.0456  0.0030  79  TYR A CE1 
1180 C CE2 . TYR A 79  ? 0.4883 0.3967 0.7148 -0.0001 0.0369  -0.0032 79  TYR A CE2 
1181 C CZ  . TYR A 79  ? 0.5317 0.4334 0.7348 0.0014  0.0463  0.0020  79  TYR A CZ  
1182 O OH  . TYR A 79  ? 0.6039 0.4925 0.8081 0.0018  0.0585  0.0065  79  TYR A OH  
1192 N N   . ARG A 80  ? 0.4793 0.3668 0.7030 -0.0006 0.0523  -0.0121 80  ARG A N   
1193 C CA  . ARG A 80  ? 0.4713 0.3416 0.6956 0.0017  0.0610  -0.0101 80  ARG A CA  
1194 C C   . ARG A 80  ? 0.4542 0.3260 0.6831 0.0144  0.0460  0.0039  80  ARG A C   
1195 O O   . ARG A 80  ? 0.5058 0.3943 0.7502 0.0231  0.0313  0.0108  80  ARG A O   
1196 C CB  . ARG A 80  ? 0.5383 0.3919 0.7846 0.0053  0.0819  -0.0113 80  ARG A CB  
1197 C CG  . ARG A 80  ? 0.4903 0.3540 0.7686 0.0212  0.0745  0.0002  80  ARG A CG  
1198 C CD  . ARG A 80  ? 0.5357 0.3837 0.8384 0.0278  0.0967  0.0001  80  ARG A CD  
1199 N NE  . ARG A 80  ? 0.5002 0.3286 0.8095 0.0426  0.1043  0.0132  80  ARG A NE  
1200 C CZ  . ARG A 80  ? 0.5471 0.3893 0.8771 0.0640  0.0917  0.0309  80  ARG A CZ  
1201 N NH1 . ARG A 80  ? 0.5417 0.4200 0.8900 0.0687  0.0708  0.0327  80  ARG A NH1 
1202 N NH2 . ARG A 80  ? 0.5605 0.3819 0.8919 0.0810  0.1009  0.0471  80  ARG A NH2 
1216 N N   . LEU A 81  ? 0.5670 0.4221 0.7827 0.0146  0.0524  0.0072  81  LEU A N   
1217 C CA  . LEU A 81  ? 0.5173 0.3718 0.7307 0.0278  0.0409  0.0228  81  LEU A CA  
1218 C C   . LEU A 81  ? 0.5397 0.3846 0.7764 0.0458  0.0493  0.0367  81  LEU A C   
1219 O O   . LEU A 81  ? 0.5817 0.3999 0.8240 0.0454  0.0734  0.0351  81  LEU A O   
1220 C CB  . LEU A 81  ? 0.5132 0.3503 0.7008 0.0200  0.0488  0.0212  81  LEU A CB  
1221 C CG  . LEU A 81  ? 0.6339 0.4730 0.8061 0.0283  0.0360  0.0341  81  LEU A CG  
1222 C CD1 . LEU A 81  ? 0.6003 0.4687 0.7671 0.0268  0.0115  0.0314  81  LEU A CD1 
1223 C CD2 . LEU A 81  ? 0.6479 0.4632 0.7970 0.0173  0.0527  0.0301  81  LEU A CD2 
1235 N N   . THR A 82  ? 0.5296 0.3998 0.7826 0.0614  0.0307  0.0486  82  THR A N   
1236 C CA  . THR A 82  ? 0.5577 0.4291 0.8360 0.0835  0.0354  0.0646  82  THR A CA  
1237 C C   . THR A 82  ? 0.5925 0.4414 0.8538 0.0992  0.0420  0.0848  82  THR A C   
1238 O O   . THR A 82  ? 0.6278 0.4668 0.8584 0.0923  0.0385  0.0861  82  THR A O   
1239 C CB  . THR A 82  ? 0.5519 0.4694 0.8550 0.0956  0.0113  0.0695  82  THR A CB  
1240 O OG1 . THR A 82  ? 0.5618 0.4970 0.8425 0.0977  -0.0098 0.0756  82  THR A OG1 
1241 C CG2 . THR A 82  ? 0.4989 0.4379 0.8193 0.0796  0.0060  0.0504  82  THR A CG2 
1249 N N   . GLU A 83  ? 0.5786 0.4238 0.8608 0.1239  0.0503  0.1034  83  GLU A N   
1250 C CA  . GLU A 83  ? 0.7060 0.5247 0.9716 0.1443  0.0609  0.1285  83  GLU A CA  
1251 C C   . GLU A 83  ? 0.6778 0.5246 0.9190 0.1517  0.0338  0.1407  83  GLU A C   
1252 O O   . GLU A 83  ? 0.7558 0.5754 0.9656 0.1551  0.0421  0.1536  83  GLU A O   
1253 C CB  . GLU A 83  ? 0.7958 0.6129 1.0936 0.1749  0.0727  0.1488  83  GLU A CB  
1254 C CG  . GLU A 83  ? 0.8143 0.5895 1.1299 0.1665  0.1087  0.1364  83  GLU A CG  
1255 C CD  . GLU A 83  ? 0.9119 0.6993 1.2713 0.1924  0.1168  0.1478  83  GLU A CD  
1256 O OE1 . GLU A 83  ? 0.9498 0.7479 1.3146 0.2245  0.1131  0.1757  83  GLU A OE1 
1257 O OE2 . GLU A 83  ? 0.8803 0.6731 1.2640 0.1787  0.1254  0.1272  83  GLU A OE2 
1264 N N   . ILE A 84  ? 0.7315 0.6325 0.9862 0.1520  0.0036  0.1346  84  ILE A N   
1265 C CA  . ILE A 84  ? 0.7556 0.6881 0.9865 0.1549  -0.0221 0.1406  84  ILE A CA  
1266 C C   . ILE A 84  ? 0.7640 0.6763 0.9609 0.1295  -0.0208 0.1252  84  ILE A C   
1267 O O   . ILE A 84  ? 0.7852 0.6953 0.9499 0.1321  -0.0267 0.1348  84  ILE A O   
1268 C CB  . ILE A 84  ? 0.7385 0.7352 0.9954 0.1550  -0.0511 0.1300  84  ILE A CB  
1269 C CG1 . ILE A 84  ? 0.7290 0.7543 1.0261 0.1809  -0.0524 0.1436  84  ILE A CG1 
1270 C CG2 . ILE A 84  ? 0.8088 0.8364 1.0369 0.1543  -0.0748 0.1319  84  ILE A CG2 
1271 C CD1 . ILE A 84  ? 0.7470 0.8291 1.0837 0.1713  -0.0707 0.1223  84  ILE A CD1 
1283 N N   . GLY A 85  ? 0.6312 0.5331 0.8345 0.1058  -0.0136 0.1018  85  GLY A N   
1284 C CA  . GLY A 85  ? 0.6510 0.5420 0.8273 0.0846  -0.0137 0.0874  85  GLY A CA  
1285 C C   . GLY A 85  ? 0.6734 0.5216 0.8245 0.0812  0.0092  0.0934  85  GLY A C   
1286 O O   . GLY A 85  ? 0.7287 0.5722 0.8522 0.0740  0.0070  0.0927  85  GLY A O   
1290 N N   . HIS A 86  ? 0.6987 0.5134 0.8597 0.0850  0.0348  0.0977  86  HIS A N   
1291 C CA  . HIS A 86  ? 0.7261 0.4969 0.8641 0.0806  0.0611  0.1027  86  HIS A CA  
1292 C C   . HIS A 86  ? 0.7811 0.5472 0.8946 0.0997  0.0562  0.1288  86  HIS A C   
1293 O O   . HIS A 86  ? 0.7505 0.4946 0.8355 0.0907  0.0672  0.1295  86  HIS A O   
1294 C CB  . HIS A 86  ? 0.7250 0.4565 0.8788 0.0841  0.0934  0.1049  86  HIS A CB  
1295 C CG  . HIS A 86  ? 0.6859 0.4127 0.8507 0.0590  0.1070  0.0762  86  HIS A CG  
1296 N ND1 . HIS A 86  ? 0.6104 0.3561 0.8014 0.0586  0.1019  0.0666  86  HIS A ND1 
1297 C CD2 . HIS A 86  ? 0.6960 0.4062 0.8483 0.0331  0.1256  0.0542  86  HIS A CD2 
1298 C CE1 . HIS A 86  ? 0.6721 0.4119 0.8621 0.0348  0.1163  0.0417  86  HIS A CE1 
1299 N NE2 . HIS A 86  ? 0.6917 0.4141 0.8596 0.0188  0.1293  0.0327  86  HIS A NE2 
1307 N N   . GLU A 87  ? 0.8337 0.6264 0.9577 0.1259  0.0387  0.1493  87  GLU A N   
1308 C CA  . GLU A 87  ? 0.9564 0.7534 1.0546 0.1487  0.0310  0.1774  87  GLU A CA  
1309 C C   . GLU A 87  ? 0.9575 0.7835 1.0287 0.1355  0.0081  0.1678  87  GLU A C   
1310 O O   . GLU A 87  ? 0.9365 0.7429 0.9722 0.1362  0.0159  0.1789  87  GLU A O   
1311 C CB  . GLU A 87  ? 0.8987 0.7321 1.0207 0.1800  0.0143  0.1982  87  GLU A CB  
1312 C CG  . GLU A 87  ? 1.1663 0.9905 1.2666 0.2127  0.0187  0.2355  87  GLU A CG  
1313 C CD  . GLU A 87  ? 1.2665 1.0175 1.3597 0.2197  0.0625  0.2511  87  GLU A CD  
1314 O OE1 . GLU A 87  ? 1.1293 0.8547 1.2513 0.2094  0.0834  0.2358  87  GLU A OE1 
1315 O OE2 . GLU A 87  ? 1.2877 1.0056 1.3451 0.2335  0.0780  0.2766  87  GLU A OE2 
1322 N N   . ASN A 88  ? 0.8556 0.7268 0.9433 0.1238  -0.0177 0.1472  88  ASN A N   
1323 C CA  . ASN A 88  ? 0.8317 0.7271 0.8972 0.1095  -0.0356 0.1341  88  ASN A CA  
1324 C C   . ASN A 88  ? 0.8738 0.7346 0.9167 0.0884  -0.0171 0.1220  88  ASN A C   
1325 O O   . ASN A 88  ? 0.9923 0.8527 1.0043 0.0849  -0.0192 0.1244  88  ASN A O   
1326 C CB  . ASN A 88  ? 0.9137 0.8499 1.0042 0.0967  -0.0568 0.1105  88  ASN A CB  
1327 C CG  . ASN A 88  ? 0.9971 0.9847 1.1011 0.1118  -0.0815 0.1166  88  ASN A CG  
1328 O OD1 . ASN A 88  ? 1.0481 1.0446 1.1619 0.1359  -0.0825 0.1382  88  ASN A OD1 
1329 N ND2 . ASN A 88  ? 0.9918 1.0160 1.0979 0.0979  -0.1003 0.0966  88  ASN A ND2 
1336 N N   . MET A 89  ? 0.8206 0.6569 0.8785 0.0737  0.0013  0.1075  89  MET A N   
1337 C CA  . MET A 89  ? 0.8867 0.6998 0.9275 0.0532  0.0186  0.0936  89  MET A CA  
1338 C C   . MET A 89  ? 0.9359 0.7104 0.9486 0.0584  0.0417  0.1111  89  MET A C   
1339 O O   . MET A 89  ? 0.9207 0.6832 0.9133 0.0428  0.0528  0.1020  89  MET A O   
1340 C CB  . MET A 89  ? 0.8749 0.6768 0.9365 0.0369  0.0337  0.0740  89  MET A CB  
1341 C CG  . MET A 89  ? 0.8904 0.7259 0.9747 0.0315  0.0144  0.0582  89  MET A CG  
1342 S SD  . MET A 89  ? 0.9735 0.8403 1.0462 0.0216  -0.0067 0.0445  89  MET A SD  
1343 C CE  . MET A 89  ? 0.7471 0.6054 0.8136 0.0008  0.0107  0.0250  89  MET A CE  
1353 N N   . ARG A 90  ? 0.9305 0.6818 0.9431 0.0804  0.0535  0.1365  90  ARG A N   
1354 C CA  . ARG A 90  ? 1.0102 0.7177 0.9931 0.0879  0.0798  0.1574  90  ARG A CA  
1355 C C   . ARG A 90  ? 0.9806 0.7073 0.9288 0.1005  0.0625  0.1752  90  ARG A C   
1356 O O   . ARG A 90  ? 0.9888 0.6939 0.9064 0.0903  0.0772  0.1757  90  ARG A O   
1357 C CB  . ARG A 90  ? 1.0751 0.7475 1.0681 0.1116  0.1014  0.1825  90  ARG A CB  
1358 C CG  . ARG A 90  ? 1.2297 0.8417 1.1936 0.1171  0.1396  0.2032  90  ARG A CG  
1359 C CD  . ARG A 90  ? 1.2423 0.8156 1.2201 0.1431  0.1642  0.2286  90  ARG A CD  
1360 N NE  . ARG A 90  ? 1.2125 0.8296 1.2008 0.1773  0.1328  0.2529  90  ARG A NE  
1361 C CZ  . ARG A 90  ? 1.2524 0.8855 1.2125 0.2063  0.1185  0.2860  90  ARG A CZ  
1362 N NH1 . ARG A 90  ? 1.2171 0.8197 1.1333 0.2066  0.1344  0.3017  90  ARG A NH1 
1363 N NH2 . ARG A 90  ? 1.3386 1.0247 1.3146 0.2344  0.0873  0.3021  90  ARG A NH2 
1377 N N   . LEU A 91  ? 1.0222 0.7918 0.9743 0.1217  0.0326  0.1885  91  LEU A N   
1378 C CA  . LEU A 91  ? 1.0852 0.8860 1.0040 0.1303  0.0115  0.1993  91  LEU A CA  
1379 C C   . LEU A 91  ? 1.1320 0.9459 1.0381 0.1021  0.0049  0.1711  91  LEU A C   
1380 O O   . LEU A 91  ? 1.2232 1.0347 1.0918 0.1004  0.0067  0.1773  91  LEU A O   
1381 C CB  . LEU A 91  ? 1.0261 0.8864 0.9609 0.1484  -0.0231 0.2047  91  LEU A CB  
1382 C CG  . LEU A 91  ? 1.1322 0.9906 1.0836 0.1810  -0.0198 0.2341  91  LEU A CG  
1383 C CD1 . LEU A 91  ? 1.2147 1.1450 1.1727 0.1993  -0.0569 0.2404  91  LEU A CD1 
1384 C CD2 . LEU A 91  ? 1.1919 0.9962 1.1099 0.2030  0.0104  0.2707  91  LEU A CD2 
1396 N N   . ARG A 92  ? 1.0034 0.8334 0.9389 0.0820  -0.0029 0.1416  92  ARG A N   
1397 C CA  . ARG A 92  ? 1.0654 0.9096 0.9915 0.0600  -0.0087 0.1174  92  ARG A CA  
1398 C C   . ARG A 92  ? 1.0618 0.8682 0.9688 0.0448  0.0198  0.1129  92  ARG A C   
1399 O O   . ARG A 92  ? 1.1142 0.9240 0.9953 0.0359  0.0211  0.1077  92  ARG A O   
1400 C CB  . ARG A 92  ? 1.0858 0.9527 1.0467 0.0462  -0.0206 0.0914  92  ARG A CB  
1401 C CG  . ARG A 92  ? 1.0593 0.9664 1.0382 0.0562  -0.0469 0.0908  92  ARG A CG  
1402 C CD  . ARG A 92  ? 1.0933 1.0121 1.1033 0.0420  -0.0517 0.0671  92  ARG A CD  
1403 N NE  . ARG A 92  ? 0.9883 0.9403 1.0226 0.0479  -0.0706 0.0635  92  ARG A NE  
1404 C CZ  . ARG A 92  ? 1.0559 1.0160 1.1182 0.0390  -0.0732 0.0473  92  ARG A CZ  
1405 N NH1 . ARG A 92  ? 1.1187 1.0605 1.1863 0.0272  -0.0611 0.0357  92  ARG A NH1 
1406 N NH2 . ARG A 92  ? 1.1560 1.1461 1.2412 0.0424  -0.0875 0.0428  92  ARG A NH2 
1420 N N   . HIS A 93  ? 1.0207 0.7925 0.9411 0.0395  0.0448  0.1123  93  HIS A N   
1421 C CA  . HIS A 93  ? 1.1189 0.8593 1.0254 0.0209  0.0741  0.1034  93  HIS A CA  
1422 C C   . HIS A 93  ? 1.1578 0.8658 1.0232 0.0314  0.0923  0.1292  93  HIS A C   
1423 O O   . HIS A 93  ? 1.1135 0.8038 0.9597 0.0153  0.1126  0.1215  93  HIS A O   
1424 C CB  . HIS A 93  ? 1.1717 0.8871 1.1038 0.0092  0.0978  0.0915  93  HIS A CB  
1425 C CG  . HIS A 93  ? 1.1694 0.8611 1.0952 -0.0149 0.1285  0.0748  93  HIS A CG  
1426 N ND1 . HIS A 93  ? 1.2252 0.9467 1.1642 -0.0371 0.1244  0.0449  93  HIS A ND1 
1427 C CD2 . HIS A 93  ? 1.1238 0.7666 1.0348 -0.0207 0.1659  0.0825  93  HIS A CD2 
1428 C CE1 . HIS A 93  ? 1.3953 1.0938 1.3295 -0.0573 0.1560  0.0326  93  HIS A CE1 
1429 N NE2 . HIS A 93  ? 1.1293 0.7767 1.0461 -0.0496 0.1833  0.0539  93  HIS A NE2 
1437 N N   . GLU A 94  ? 1.1300 0.8307 0.9820 0.0594  0.0873  0.1611  94  GLU A N   
1438 C CA  . GLU A 94  ? 1.2021 0.8741 1.0095 0.0744  0.1033  0.1911  94  GLU A CA  
1439 C C   . GLU A 94  ? 1.2340 0.9436 1.0087 0.0763  0.0793  0.1922  94  GLU A C   
1440 O O   . GLU A 94  ? 1.2501 0.9388 0.9867 0.0712  0.0967  0.1993  94  GLU A O   
1441 C CB  . GLU A 94  ? 1.0910 0.7467 0.8942 0.1090  0.1060  0.2287  94  GLU A CB  
1442 C CG  . GLU A 94  ? 1.1752 0.7788 1.0019 0.1097  0.1404  0.2330  94  GLU A CG  
1443 C CD  . GLU A 94  ? 1.2288 0.8092 1.0454 0.1490  0.1491  0.2764  94  GLU A CD  
1444 O OE1 . GLU A 94  ? 1.3244 0.9242 1.1056 0.1741  0.1333  0.3057  94  GLU A OE1 
1445 O OE2 . GLU A 94  ? 1.2756 0.8205 1.1181 0.1557  0.1724  0.2813  94  GLU A OE2 
1452 N N   . SER A 95  ? 1.1362 0.9000 0.9236 0.0840  0.0420  0.1859  95  SER A N   
1453 C CA  . SER A 95  ? 1.1438 0.9483 0.9062 0.0794  0.0193  0.1768  95  SER A CA  
1454 C C   . SER A 95  ? 1.1426 0.9331 0.8935 0.0522  0.0362  0.1532  95  SER A C   
1455 O O   . SER A 95  ? 1.2029 0.9869 0.9116 0.0511  0.0445  0.1612  95  SER A O   
1456 C CB  . SER A 95  ? 1.1520 1.0116 0.9461 0.0771  -0.0155 0.1562  95  SER A CB  
1457 O OG  . SER A 95  ? 1.1562 1.0526 0.9410 0.1012  -0.0390 0.1763  95  SER A OG  
1463 N N   . TRP A 96  ? 1.0677 0.8577 0.8556 0.0312  0.0413  0.1242  96  TRP A N   
1464 C CA  . TRP A 96  ? 1.0658 0.8561 0.8519 0.0072  0.0529  0.0987  96  TRP A CA  
1465 C C   . TRP A 96  ? 1.1099 0.8553 0.8754 -0.0028 0.0903  0.1048  96  TRP A C   
1466 O O   . TRP A 96  ? 1.0438 0.7899 0.7969 -0.0199 0.1027  0.0892  96  TRP A O   
1467 C CB  . TRP A 96  ? 1.0535 0.8624 0.8852 -0.0083 0.0470  0.0689  96  TRP A CB  
1468 C CG  . TRP A 96  ? 1.0173 0.8672 0.8649 -0.0082 0.0185  0.0531  96  TRP A CG  
1469 C CD1 . TRP A 96  ? 1.0093 0.8791 0.8851 -0.0006 -0.0014 0.0509  96  TRP A CD1 
1470 C CD2 . TRP A 96  ? 0.9756 0.8477 0.8125 -0.0175 0.0114  0.0356  96  TRP A CD2 
1471 N NE1 . TRP A 96  ? 0.9520 0.8523 0.8351 -0.0054 -0.0189 0.0333  96  TRP A NE1 
1472 C CE2 . TRP A 96  ? 0.9512 0.8526 0.8110 -0.0154 -0.0112 0.0234  96  TRP A CE2 
1473 C CE3 . TRP A 96  ? 0.9716 0.8394 0.7824 -0.0282 0.0251  0.0280  96  TRP A CE3 
1474 C CZ2 . TRP A 96  ? 0.9619 0.8851 0.8191 -0.0236 -0.0191 0.0036  96  TRP A CZ2 
1475 C CZ3 . TRP A 96  ? 0.9684 0.8611 0.7768 -0.0353 0.0153  0.0084  96  TRP A CZ3 
1476 C CH2 . TRP A 96  ? 0.8961 0.8146 0.7275 -0.0329 -0.0058 -0.0036 96  TRP A CH2 
1487 N N   . SER A 97  ? 1.1642 0.8688 0.9269 0.0067  0.1121  0.1260  97  SER A N   
1488 C CA  . SER A 97  ? 1.1988 0.8541 0.9360 -0.0020 0.1523  0.1350  97  SER A CA  
1489 C C   . SER A 97  ? 1.1816 0.8278 0.8633 0.0112  0.1554  0.1608  97  SER A C   
1490 O O   . SER A 97  ? 1.1814 0.8115 0.8387 -0.0048 0.1781  0.1541  97  SER A O   
1491 C CB  . SER A 97  ? 1.2587 0.8661 1.0065 0.0058  0.1793  0.1519  97  SER A CB  
1492 O OG  . SER A 97  ? 1.2550 0.8666 1.0475 -0.0152 0.1866  0.1218  97  SER A OG  
1498 N N   . ARG A 98  ? 1.1773 0.8382 0.8376 0.0406  0.1328  0.1903  98  ARG A N   
1499 C CA  . ARG A 98  ? 1.2543 0.9154 0.8568 0.0549  0.1325  0.2156  98  ARG A CA  
1500 C C   . ARG A 98  ? 1.2113 0.9065 0.8006 0.0339  0.1213  0.1877  98  ARG A C   
1501 O O   . ARG A 98  ? 1.3070 0.9847 0.8525 0.0290  0.1404  0.1951  98  ARG A O   
1502 C CB  . ARG A 98  ? 1.2763 0.9695 0.8643 0.0894  0.1015  0.2458  98  ARG A CB  
1503 C CG  . ARG A 98  ? 1.4345 1.0968 1.0428 0.1135  0.1122  0.2731  98  ARG A CG  
1504 C CD  . ARG A 98  ? 1.5159 1.2046 1.1041 0.1549  0.0894  0.3131  98  ARG A CD  
1505 N NE  . ARG A 98  ? 1.4574 1.2211 1.0712 0.1577  0.0425  0.2954  98  ARG A NE  
1506 C CZ  . ARG A 98  ? 1.4152 1.1998 1.0790 0.1634  0.0261  0.2872  98  ARG A CZ  
1507 N NH1 . ARG A 98  ? 1.4325 1.1714 1.1263 0.1675  0.0505  0.2943  98  ARG A NH1 
1508 N NH2 . ARG A 98  ? 1.4111 1.2629 1.0958 0.1621  -0.0129 0.2686  98  ARG A NH2 
1522 N N   . VAL A 99  ? 1.1437 0.8820 0.7715 0.0203  0.0957  0.1547  99  VAL A N   
1523 C CA  . VAL A 99  ? 1.2291 0.9980 0.8474 0.0026  0.0870  0.1279  99  VAL A CA  
1524 C C   . VAL A 99  ? 1.2604 1.0013 0.8776 -0.0215 0.1214  0.1107  99  VAL A C   
1525 O O   . VAL A 99  ? 1.2461 0.9910 0.8315 -0.0313 0.1300  0.1036  99  VAL A O   
1526 C CB  . VAL A 99  ? 1.1349 0.9486 0.7980 -0.0041 0.0569  0.0988  99  VAL A CB  
1527 C CG1 . VAL A 99  ? 1.0830 0.9174 0.7475 -0.0241 0.0571  0.0678  99  VAL A CG1 
1528 C CG2 . VAL A 99  ? 1.0864 0.9377 0.7451 0.0154  0.0232  0.1106  99  VAL A CG2 
1538 N N   . ASP A 100 ? 1.2145 0.9316 0.8682 -0.0333 0.1418  0.1005  100 ASP A N   
1539 C CA  . ASP A 100 ? 1.2684 0.9710 0.9305 -0.0589 0.1727  0.0781  100 ASP A CA  
1540 C C   . ASP A 100 ? 1.3515 1.0077 0.9664 -0.0616 0.2097  0.0980  100 ASP A C   
1541 O O   . ASP A 100 ? 1.3266 0.9806 0.9340 -0.0818 0.2314  0.0803  100 ASP A O   
1542 C CB  . ASP A 100 ? 1.2112 0.9062 0.9225 -0.0724 0.1858  0.0604  100 ASP A CB  
1543 C CG  . ASP A 100 ? 1.1405 0.8824 0.8983 -0.0774 0.1589  0.0329  100 ASP A CG  
1544 O OD1 . ASP A 100 ? 1.1501 0.9241 0.9087 -0.0814 0.1449  0.0167  100 ASP A OD1 
1545 O OD2 . ASP A 100 ? 1.0630 0.8069 0.8545 -0.0768 0.1543  0.0284  100 ASP A OD2 
1550 N N   . LYS A 101 ? 1.3885 1.0055 0.9736 -0.0411 0.2208  0.1353  101 LYS A N   
1551 C CA  . LYS A 101 ? 1.6009 1.1690 1.1332 -0.0394 0.2577  0.1605  101 LYS A CA  
1552 C C   . LYS A 101 ? 1.5436 1.1363 1.0246 -0.0325 0.2432  0.1685  101 LYS A C   
1553 O O   . LYS A 101 ? 1.5649 1.1440 1.0198 -0.0497 0.2691  0.1600  101 LYS A O   
1554 C CB  . LYS A 101 ? 1.6049 1.1238 1.1178 -0.0134 0.2736  0.2026  101 LYS A CB  
1555 C CG  . LYS A 101 ? 1.8538 1.3136 1.3089 -0.0055 0.3148  0.2367  101 LYS A CG  
1556 C CD  . LYS A 101 ? 1.7652 1.1772 1.2245 -0.0389 0.3685  0.2172  101 LYS A CD  
1557 C CE  . LYS A 101 ? 1.8224 1.1720 1.2138 -0.0277 0.4108  0.2569  101 LYS A CE  
1558 N NZ  . LYS A 101 ? 1.7723 1.0841 1.1756 -0.0594 0.4596  0.2331  101 LYS A NZ  
1572 N N   . ILE A 102 ? 1.4357 1.0716 0.9064 -0.0112 0.2014  0.1787  102 ILE A N   
1573 C CA  . ILE A 102 ? 1.5452 1.2134 0.9674 -0.0069 0.1847  0.1812  102 ILE A CA  
1574 C C   . ILE A 102 ? 1.6005 1.2823 1.0302 -0.0371 0.1965  0.1430  102 ILE A C   
1575 O O   . ILE A 102 ? 1.6559 1.3339 1.0367 -0.0426 0.2105  0.1459  102 ILE A O   
1576 C CB  . ILE A 102 ? 1.4283 1.1553 0.8583 0.0099  0.1357  0.1799  102 ILE A CB  
1577 C CG1 . ILE A 102 ? 1.4272 1.1484 0.8361 0.0448  0.1248  0.2237  102 ILE A CG1 
1578 C CG2 . ILE A 102 ? 1.3461 1.1165 0.7406 0.0024  0.1185  0.1637  102 ILE A CG2 
1579 C CD1 . ILE A 102 ? 1.3629 1.1479 0.7819 0.0596  0.0782  0.2206  102 ILE A CD1 
1591 N N   . ILE A 103 ? 1.5367 1.2387 1.0270 -0.0550 0.1899  0.1074  103 ILE A N   
1592 C CA  . ILE A 103 ? 1.5826 1.3016 1.0867 -0.0799 0.2011  0.0718  103 ILE A CA  
1593 C C   . ILE A 103 ? 1.5908 1.2679 1.0823 -0.0979 0.2481  0.0710  103 ILE A C   
1594 O O   . ILE A 103 ? 1.6819 1.3600 1.1478 -0.1118 0.2661  0.0593  103 ILE A O   
1595 C CB  . ILE A 103 ? 1.4212 1.1747 0.9926 -0.0887 0.1817  0.0391  103 ILE A CB  
1596 C CG1 . ILE A 103 ? 1.4076 1.2044 0.9794 -0.0796 0.1439  0.0300  103 ILE A CG1 
1597 C CG2 . ILE A 103 ? 1.3833 1.1447 0.9833 -0.1122 0.2037  0.0068  103 ILE A CG2 
1598 C CD1 . ILE A 103 ? 1.2563 1.0705 0.8675 -0.0669 0.1150  0.0320  103 ILE A CD1 
1610 N N   . GLU A 104 ? 1.4523 1.0911 0.9619 -0.1000 0.2716  0.0814  104 GLU A N   
1611 C CA  . GLU A 104 ? 1.5553 1.1494 1.0529 -0.1195 0.3213  0.0804  104 GLU A CA  
1612 C C   . GLU A 104 ? 1.6718 1.2342 1.0952 -0.1123 0.3427  0.1088  104 GLU A C   
1613 O O   . GLU A 104 ? 1.6586 1.2100 1.0655 -0.1330 0.3740  0.0951  104 GLU A O   
1614 C CB  . GLU A 104 ? 1.5645 1.1175 1.0862 -0.1192 0.3422  0.0916  104 GLU A CB  
1615 C CG  . GLU A 104 ? 1.6184 1.1251 1.1421 -0.1445 0.3967  0.0833  104 GLU A CG  
1616 C CD  . GLU A 104 ? 1.7118 1.1800 1.2638 -0.1457 0.4163  0.0893  104 GLU A CD  
1617 O OE1 . GLU A 104 ? 1.5225 1.0236 1.1229 -0.1435 0.3881  0.0736  104 GLU A OE1 
1618 O OE2 . GLU A 104 ? 1.7572 1.1601 1.2822 -0.1496 0.4628  0.1090  104 GLU A OE2 
1625 N N   . ASN A 105 ? 1.6478 1.2010 1.0250 -0.0821 0.3251  0.1485  105 ASN A N   
1626 C CA  . ASN A 105 ? 1.6902 1.2129 0.9898 -0.0705 0.3457  0.1823  105 ASN A CA  
1627 C C   . ASN A 105 ? 1.7385 1.3020 1.0050 -0.0788 0.3322  0.1650  105 ASN A C   
1628 O O   . ASN A 105 ? 1.8422 1.3797 1.0525 -0.0840 0.3623  0.1772  105 ASN A O   
1629 C CB  . ASN A 105 ? 1.7072 1.2189 0.9689 -0.0317 0.3276  0.2310  105 ASN A CB  
1630 C CG  . ASN A 105 ? 1.7246 1.1863 1.0140 -0.0225 0.3488  0.2504  105 ASN A CG  
1631 O OD1 . ASN A 105 ? 1.7315 1.1622 1.0601 -0.0483 0.3821  0.2276  105 ASN A OD1 
1632 N ND2 . ASN A 105 ? 1.7513 1.2077 1.0229 0.0136  0.3313  0.2904  105 ASN A ND2 
1639 N N   . LEU A 106 ? 1.7551 1.3787 1.0531 -0.0805 0.2906  0.1367  106 LEU A N   
1640 C CA  . LEU A 106 ? 1.8748 1.5355 1.1458 -0.0913 0.2813  0.1147  106 LEU A CA  
1641 C C   . LEU A 106 ? 1.8869 1.5290 1.1627 -0.1206 0.3228  0.0890  106 LEU A C   
1642 O O   . LEU A 106 ? 1.8927 1.5310 1.1151 -0.1275 0.3403  0.0900  106 LEU A O   
1643 C CB  . LEU A 106 ? 1.6799 1.3990 0.9978 -0.0933 0.2390  0.0823  106 LEU A CB  
1644 C CG  . LEU A 106 ? 2.0625 1.8181 1.3706 -0.0696 0.1944  0.0974  106 LEU A CG  
1645 C CD1 . LEU A 106 ? 1.9321 1.7347 1.2947 -0.0772 0.1629  0.0608  106 LEU A CD1 
1646 C CD2 . LEU A 106 ? 2.4932 2.2660 1.7247 -0.0589 0.1865  0.1160  106 LEU A CD2 
1658 N N   . GLU A 107 ? 1.8238 1.4577 1.1633 -0.1385 0.3399  0.0651  107 GLU A N   
1659 C CA  . GLU A 107 ? 1.8300 1.4510 1.1826 -0.1669 0.3814  0.0396  107 GLU A CA  
1660 C C   . GLU A 107 ? 1.8879 1.4468 1.1853 -0.1700 0.4284  0.0692  107 GLU A C   
1661 O O   . GLU A 107 ? 1.9589 1.5049 1.2291 -0.1882 0.4625  0.0595  107 GLU A O   
1662 C CB  . GLU A 107 ? 1.7708 1.4046 1.2041 -0.1832 0.3868  0.0096  107 GLU A CB  
1663 C CG  . GLU A 107 ? 1.6667 1.3511 1.1531 -0.1746 0.3425  -0.0101 107 GLU A CG  
1664 C CD  . GLU A 107 ? 1.9484 1.6497 1.5080 -0.1885 0.3477  -0.0367 107 GLU A CD  
1665 O OE1 . GLU A 107 ? 1.8909 1.5653 1.4604 -0.2067 0.3856  -0.0413 107 GLU A OE1 
1666 O OE2 . GLU A 107 ? 2.0841 1.8254 1.6894 -0.1813 0.3151  -0.0524 107 GLU A OE2 
1673 N N   . ALA A 108 ? 1.8761 1.3929 1.1561 -0.1515 0.4338  0.1066  108 ALA A N   
1674 C CA  . ALA A 108 ? 1.9302 1.3827 1.1607 -0.1494 0.4786  0.1389  108 ALA A CA  
1675 C C   . ALA A 108 ? 1.9612 1.4192 1.1174 -0.1323 0.4707  0.1645  108 ALA A C   
1676 O O   . ALA A 108 ? 2.0651 1.5056 1.2008 -0.1423 0.4985  0.1637  108 ALA A O   
1677 C CB  . ALA A 108 ? 2.0775 1.4895 1.3168 -0.1271 0.4797  0.1726  108 ALA A CB  
1683 N N   . ASN A 109 ? 1.9254 1.4127 1.0406 -0.1073 0.4317  0.1851  109 ASN A N   
1684 C CA  . ASN A 109 ? 2.0022 1.5075 1.0473 -0.0915 0.4201  0.2070  109 ASN A CA  
1685 C C   . ASN A 109 ? 2.0469 1.5797 1.0847 -0.1190 0.4304  0.1685  109 ASN A C   
1686 O O   . ASN A 109 ? 2.0368 1.5730 1.0236 -0.1154 0.4381  0.1810  109 ASN A O   
1687 C CB  . ASN A 109 ? 2.0337 1.5806 1.0492 -0.0622 0.3705  0.2269  109 ASN A CB  
1688 C CG  . ASN A 109 ? 2.0291 1.5488 1.0444 -0.0282 0.3634  0.2736  109 ASN A CG  
1689 O OD1 . ASN A 109 ? 2.0422 1.5101 1.0705 -0.0245 0.3959  0.2944  109 ASN A OD1 
1690 N ND2 . ASN A 109 ? 1.9773 1.5417 0.9950 -0.0036 0.3163  0.2845  109 ASN A ND2 
1697 N N   . LYS A 110 ? 2.0499 1.6071 1.1435 -0.1452 0.4296  0.1213  110 LYS A N   
1698 C CA  . LYS A 110 ? 2.0023 1.5819 1.1034 -0.1714 0.4458  0.0825  110 LYS A CA  
1699 C C   . LYS A 110 ? 2.0336 1.5752 1.1489 -0.1875 0.4909  0.0805  110 LYS A C   
1700 O O   . LYS A 110 ? 2.0863 1.6351 1.1813 -0.1994 0.5067  0.0674  110 LYS A O   
1701 C CB  . LYS A 110 ? 1.9634 1.5886 1.1444 -0.1874 0.4264  0.0343  110 LYS A CB  
1702 C CG  . LYS A 110 ? 1.9638 1.6449 1.1488 -0.1757 0.3763  0.0200  110 LYS A CG  
1703 C CD  . LYS A 110 ? 1.9240 1.6242 1.0401 -0.1793 0.3765  0.0150  110 LYS A CD  
1704 C CE  . LYS A 110 ? 1.9684 1.7249 1.0965 -0.1740 0.3315  -0.0079 110 LYS A CE  
1705 N NZ  . LYS A 110 ? 2.0572 1.8290 1.1904 -0.1487 0.2898  0.0173  110 LYS A NZ  
1719 N N   . LYS A 111 ? 2.1380 1.6389 1.2888 -0.1894 0.5125  0.0906  111 LYS A N   
1720 C CA  . LYS A 111 ? 2.1405 1.6010 1.3041 -0.2056 0.5559  0.0872  111 LYS A CA  
1721 C C   . LYS A 111 ? 2.1502 1.5579 1.2623 -0.1814 0.5697  0.1381  111 LYS A C   
1722 O O   . LYS A 111 ? 2.1863 1.5994 1.2315 -0.1600 0.5569  0.1698  111 LYS A O   
1723 C CB  . LYS A 111 ? 2.1211 1.5772 1.3667 -0.2295 0.5739  0.0536  111 LYS A CB  
1724 C CG  . LYS A 111 ? 2.1260 1.6377 1.4283 -0.2542 0.5681  0.0018  111 LYS A CG  
1725 C CD  . LYS A 111 ? 2.0694 1.5929 1.4544 -0.2748 0.5785  -0.0313 111 LYS A CD  
1726 C CE  . LYS A 111 ? 2.2261 1.7681 1.6395 -0.2641 0.5502  -0.0284 111 LYS A CE  
1727 N NZ  . LYS A 111 ? 2.0985 1.6631 1.5929 -0.2844 0.5572  -0.0632 111 LYS A NZ  
1741 N N   . ALA B 2   ? 1.1924 1.1825 1.3333 0.0328  -0.1923 -0.3754 2   ALA B N   
1742 C CA  . ALA B 2   ? 1.2336 1.1947 1.3588 0.0132  -0.1790 -0.3406 2   ALA B CA  
1743 C C   . ALA B 2   ? 1.3518 1.2705 1.4482 0.0112  -0.1741 -0.3060 2   ALA B C   
1744 O O   . ALA B 2   ? 1.3847 1.2718 1.4613 0.0014  -0.1694 -0.2770 2   ALA B O   
1745 C CB  . ALA B 2   ? 1.2037 1.1361 1.3190 0.0216  -0.1945 -0.3427 2   ALA B CB  
1750 N N   . GLU B 3   ? 1.3280 1.2515 1.4229 0.0199  -0.1751 -0.3105 3   GLU B N   
1751 C CA  . GLU B 3   ? 1.3343 1.2238 1.4014 0.0223  -0.1722 -0.2816 3   GLU B CA  
1752 C C   . GLU B 3   ? 1.2776 1.1660 1.3386 -0.0017 -0.1502 -0.2509 3   GLU B C   
1753 O O   . GLU B 3   ? 1.2170 1.1345 1.2970 -0.0206 -0.1351 -0.2535 3   GLU B O   
1754 C CB  . GLU B 3   ? 1.2768 1.1811 1.3484 0.0331  -0.1744 -0.2955 3   GLU B CB  
1755 C CG  . GLU B 3   ? 1.3337 1.2527 1.4164 0.0577  -0.1955 -0.3315 3   GLU B CG  
1756 C CD  . GLU B 3   ? 1.3237 1.2684 1.4179 0.0625  -0.1951 -0.3490 3   GLU B CD  
1757 O OE1 . GLU B 3   ? 1.4001 1.3393 1.4875 0.0498  -0.1811 -0.3303 3   GLU B OE1 
1758 O OE2 . GLU B 3   ? 1.3751 1.3463 1.4851 0.0797  -0.2099 -0.3827 3   GLU B OE2 
1765 N N   . ILE B 4   ? 1.2346 1.0918 1.2671 0.0001  -0.1489 -0.2217 4   ILE B N   
1766 C CA  . ILE B 4   ? 1.2157 1.0772 1.2403 -0.0168 -0.1294 -0.1945 4   ILE B CA  
1767 C C   . ILE B 4   ? 1.1751 1.0584 1.2104 -0.0197 -0.1188 -0.2019 4   ILE B C   
1768 O O   . ILE B 4   ? 1.1346 1.0150 1.1665 -0.0049 -0.1269 -0.2130 4   ILE B O   
1769 C CB  . ILE B 4   ? 1.1798 1.0128 1.1719 -0.0121 -0.1312 -0.1651 4   ILE B CB  
1770 C CG1 . ILE B 4   ? 1.2162 1.0213 1.1940 -0.0166 -0.1404 -0.1527 4   ILE B CG1 
1771 C CG2 . ILE B 4   ? 1.1248 0.9715 1.1098 -0.0247 -0.1122 -0.1417 4   ILE B CG2 
1772 C CD1 . ILE B 4   ? 1.1552 0.9728 1.1446 -0.0384 -0.1292 -0.1450 4   ILE B CD1 
1784 N N   . PRO B 5   ? 1.1560 1.0581 1.2019 -0.0379 -0.1024 -0.1969 5   PRO B N   
1785 C CA  . PRO B 5   ? 1.2142 1.1270 1.2660 -0.0426 -0.0942 -0.2030 5   PRO B CA  
1786 C C   . PRO B 5   ? 1.1303 1.0250 1.1596 -0.0291 -0.0957 -0.1902 5   PRO B C   
1787 O O   . PRO B 5   ? 1.0645 0.9468 1.0720 -0.0234 -0.0938 -0.1673 5   PRO B O   
1788 C CB  . PRO B 5   ? 1.1008 1.0265 1.1574 -0.0633 -0.0772 -0.1914 5   PRO B CB  
1789 C CG  . PRO B 5   ? 1.0894 1.0133 1.1409 -0.0673 -0.0758 -0.1767 5   PRO B CG  
1790 C CD  . PRO B 5   ? 1.1465 1.0598 1.1997 -0.0549 -0.0925 -0.1885 5   PRO B CD  
1798 N N   . LYS B 6   ? 1.1909 1.0887 1.2267 -0.0256 -0.0985 -0.2067 6   LYS B N   
1799 C CA  . LYS B 6   ? 1.2354 1.1184 1.2517 -0.0096 -0.1026 -0.2013 6   LYS B CA  
1800 C C   . LYS B 6   ? 1.2181 1.0925 1.2138 -0.0113 -0.0913 -0.1759 6   LYS B C   
1801 O O   . LYS B 6   ? 1.1984 1.0648 1.1716 0.0051  -0.0943 -0.1632 6   LYS B O   
1802 C CB  . LYS B 6   ? 1.2695 1.1590 1.3009 -0.0118 -0.1066 -0.2266 6   LYS B CB  
1803 C CG  . LYS B 6   ? 1.3113 1.2201 1.3657 -0.0085 -0.1183 -0.2553 6   LYS B CG  
1804 C CD  . LYS B 6   ? 1.3701 1.2930 1.4425 -0.0143 -0.1218 -0.2820 6   LYS B CD  
1805 C CE  . LYS B 6   ? 1.3426 1.2715 1.4263 -0.0442 -0.1066 -0.2801 6   LYS B CE  
1806 N NZ  . LYS B 6   ? 1.4508 1.3999 1.5574 -0.0582 -0.1094 -0.3086 6   LYS B NZ  
1820 N N   . GLU B 7   ? 1.2346 1.1140 1.2362 -0.0294 -0.0787 -0.1689 7   GLU B N   
1821 C CA  . GLU B 7   ? 1.1869 1.0613 1.1685 -0.0282 -0.0692 -0.1464 7   GLU B CA  
1822 C C   . GLU B 7   ? 1.1258 1.0078 1.0952 -0.0242 -0.0670 -0.1257 7   GLU B C   
1823 O O   . GLU B 7   ? 1.0880 0.9729 1.0376 -0.0155 -0.0626 -0.1086 7   GLU B O   
1824 C CB  . GLU B 7   ? 1.1118 0.9884 1.1002 -0.0476 -0.0578 -0.1440 7   GLU B CB  
1825 C CG  . GLU B 7   ? 1.2100 1.0747 1.2051 -0.0565 -0.0589 -0.1603 7   GLU B CG  
1826 C CD  . GLU B 7   ? 1.2571 1.1380 1.2803 -0.0686 -0.0634 -0.1852 7   GLU B CD  
1827 O OE1 . GLU B 7   ? 1.2741 1.1763 1.3136 -0.0763 -0.0616 -0.1892 7   GLU B OE1 
1828 O OE2 . GLU B 7   ? 1.2466 1.1215 1.2761 -0.0705 -0.0693 -0.2029 7   GLU B OE2 
1835 N N   . MET B 8   ? 1.0788 0.9651 1.0592 -0.0308 -0.0708 -0.1280 8   MET B N   
1836 C CA  . MET B 8   ? 1.1279 1.0172 1.0964 -0.0325 -0.0692 -0.1079 8   MET B CA  
1837 C C   . MET B 8   ? 1.0501 0.9297 0.9975 -0.0163 -0.0781 -0.0994 8   MET B C   
1838 O O   . MET B 8   ? 0.9884 0.8764 0.9170 -0.0143 -0.0730 -0.0786 8   MET B O   
1839 C CB  . MET B 8   ? 1.1182 1.0085 1.1028 -0.0457 -0.0722 -0.1137 8   MET B CB  
1840 C CG  . MET B 8   ? 1.0142 0.9060 0.9885 -0.0545 -0.0696 -0.0932 8   MET B CG  
1841 S SD  . MET B 8   ? 0.9489 0.8429 0.9419 -0.0716 -0.0717 -0.1006 8   MET B SD  
1842 C CE  . MET B 8   ? 0.9925 0.9132 1.0035 -0.0826 -0.0571 -0.1081 8   MET B CE  
1852 N N   . LEU B 9   ? 1.1393 1.0058 1.0882 -0.0040 -0.0912 -0.1154 9   LEU B N   
1853 C CA  . LEU B 9   ? 1.1695 1.0267 1.0945 0.0133  -0.0999 -0.1068 9   LEU B CA  
1854 C C   . LEU B 9   ? 1.1118 0.9803 1.0201 0.0259  -0.0943 -0.0989 9   LEU B C   
1855 O O   . LEU B 9   ? 1.0594 0.9347 0.9442 0.0334  -0.0932 -0.0803 9   LEU B O   
1856 C CB  . LEU B 9   ? 1.1470 0.9910 1.0767 0.0283  -0.1162 -0.1292 9   LEU B CB  
1857 C CG  . LEU B 9   ? 1.1573 0.9888 1.0989 0.0249  -0.1272 -0.1414 9   LEU B CG  
1858 C CD1 . LEU B 9   ? 1.2134 1.0394 1.1598 0.0448  -0.1443 -0.1677 9   LEU B CD1 
1859 C CD2 . LEU B 9   ? 1.1375 0.9489 1.0581 0.0193  -0.1308 -0.1181 9   LEU B CD2 
1871 N N   . ARG B 10  ? 1.0696 0.9403 0.9881 0.0277  -0.0911 -0.1128 10  ARG B N   
1872 C CA  . ARG B 10  ? 1.0769 0.9540 0.9784 0.0419  -0.0879 -0.1080 10  ARG B CA  
1873 C C   . ARG B 10  ? 1.0279 0.9248 0.9152 0.0384  -0.0765 -0.0839 10  ARG B C   
1874 O O   . ARG B 10  ? 0.9850 0.8972 0.8507 0.0533  -0.0760 -0.0727 10  ARG B O   
1875 C CB  . ARG B 10  ? 1.1950 1.0619 1.1088 0.0386  -0.0868 -0.1251 10  ARG B CB  
1876 C CG  . ARG B 10  ? 1.1334 0.9974 1.0285 0.0550  -0.0865 -0.1241 10  ARG B CG  
1877 C CD  . ARG B 10  ? 1.2074 1.0699 1.0878 0.0797  -0.0981 -0.1338 10  ARG B CD  
1878 N NE  . ARG B 10  ? 1.4610 1.3074 1.3338 0.0919  -0.1035 -0.1477 10  ARG B NE  
1879 C CZ  . ARG B 10  ? 1.3916 1.2422 1.2417 0.1113  -0.1035 -0.1416 10  ARG B CZ  
1880 N NH1 . ARG B 10  ? 1.3470 1.2259 1.1815 0.1193  -0.0963 -0.1214 10  ARG B NH1 
1881 N NH2 . ARG B 10  ? 1.6099 1.4366 1.4523 0.1228  -0.1119 -0.1575 10  ARG B NH2 
1895 N N   . ALA B 11  ? 1.0047 0.9077 0.9042 0.0191  -0.0671 -0.0768 11  ALA B N   
1896 C CA  . ALA B 11  ? 0.9512 0.8794 0.8397 0.0156  -0.0566 -0.0565 11  ALA B CA  
1897 C C   . ALA B 11  ? 0.9005 0.8427 0.7762 0.0114  -0.0564 -0.0382 11  ALA B C   
1898 O O   . ALA B 11  ? 0.8120 0.7833 0.6718 0.0156  -0.0499 -0.0226 11  ALA B O   
1899 C CB  . ALA B 11  ? 1.0704 1.0029 0.9750 -0.0036 -0.0479 -0.0549 11  ALA B CB  
1905 N N   . GLN B 12  ? 0.8870 0.8095 0.7679 0.0022  -0.0639 -0.0395 12  GLN B N   
1906 C CA  . GLN B 12  ? 0.9557 0.8819 0.8195 -0.0052 -0.0650 -0.0195 12  GLN B CA  
1907 C C   . GLN B 12  ? 0.8821 0.8193 0.7198 0.0144  -0.0680 -0.0118 12  GLN B C   
1908 O O   . GLN B 12  ? 0.8164 0.7804 0.6361 0.0103  -0.0612 0.0086  12  GLN B O   
1909 C CB  . GLN B 12  ? 1.0179 0.9101 0.8877 -0.0142 -0.0766 -0.0248 12  GLN B CB  
1910 C CG  . GLN B 12  ? 1.0141 0.8996 0.9067 -0.0338 -0.0748 -0.0310 12  GLN B CG  
1911 C CD  . GLN B 12  ? 0.9524 0.8033 0.8510 -0.0357 -0.0898 -0.0431 12  GLN B CD  
1912 O OE1 . GLN B 12  ? 1.0148 0.8605 0.9294 -0.0497 -0.0905 -0.0491 12  GLN B OE1 
1913 N NE2 . GLN B 12  ? 1.0271 0.8564 0.9118 -0.0191 -0.1028 -0.0481 12  GLN B NE2 
1922 N N   . THR B 13  ? 0.8810 0.8033 0.7171 0.0352  -0.0776 -0.0293 13  THR B N   
1923 C CA  . THR B 13  ? 0.9525 0.8870 0.7642 0.0574  -0.0817 -0.0262 13  THR B CA  
1924 C C   . THR B 13  ? 0.9656 0.9369 0.7679 0.0696  -0.0725 -0.0221 13  THR B C   
1925 O O   . THR B 13  ? 0.9834 0.9842 0.7625 0.0790  -0.0697 -0.0083 13  THR B O   
1926 C CB  . THR B 13  ? 1.0277 0.9386 0.8445 0.0765  -0.0954 -0.0509 13  THR B CB  
1927 O OG1 . THR B 13  ? 1.0332 0.9151 0.8583 0.0684  -0.1052 -0.0566 13  THR B OG1 
1928 C CG2 . THR B 13  ? 1.1892 1.1117 0.9802 0.1017  -0.1019 -0.0504 13  THR B CG2 
1936 N N   . ASN B 14  ? 0.9505 0.9214 0.7675 0.0714  -0.0687 -0.0344 14  ASN B N   
1937 C CA  . ASN B 14  ? 0.9392 0.9426 0.7449 0.0856  -0.0620 -0.0311 14  ASN B CA  
1938 C C   . ASN B 14  ? 0.9153 0.9593 0.7137 0.0717  -0.0502 -0.0080 14  ASN B C   
1939 O O   . ASN B 14  ? 0.8859 0.9710 0.6666 0.0849  -0.0460 0.0000  14  ASN B O   
1940 C CB  . ASN B 14  ? 0.9552 0.9442 0.7740 0.0862  -0.0602 -0.0439 14  ASN B CB  
1941 C CG  . ASN B 14  ? 1.0665 1.0264 0.8845 0.1049  -0.0710 -0.0663 14  ASN B CG  
1942 O OD1 . ASN B 14  ? 1.0697 1.0044 0.8965 0.1035  -0.0797 -0.0794 14  ASN B OD1 
1943 N ND2 . ASN B 14  ? 1.1263 1.0880 0.9334 0.1224  -0.0719 -0.0724 14  ASN B ND2 
1950 O O   . HOX B 15  ? 0.9434 1.0958 0.7169 0.0266  -0.0244 0.0517  15  HOX B O   
1951 C C   . HOX B 15  ? 0.9202 1.0203 0.7073 0.0240  -0.0328 0.0396  15  HOX B C   
1952 N N   . HOX B 15  ? 0.8954 0.9322 0.7093 0.0443  -0.0449 0.0007  15  HOX B N   
1953 C CA  . HOX B 15  ? 0.9258 1.0024 0.7360 0.0263  -0.0338 0.0213  15  HOX B CA  
1954 C CB  . HOX B 15  ? 0.8713 0.9298 0.7018 -0.0039 -0.0310 0.0254  15  HOX B CB  
1955 C CG  . HOX B 15  ? 0.8572 0.9608 0.6853 -0.0222 -0.0199 0.0436  15  HOX B CG  
1956 C CZ  . HOX B 15  ? 0.8725 1.0742 0.6995 -0.0602 0.0012  0.0746  15  HOX B CZ  
1957 N NZ  . HOX B 15  ? 0.9303 1.1871 0.7585 -0.0815 0.0117  0.0885  15  HOX B NZ  
1958 C CD1 . HOX B 15  ? 0.8497 1.0041 0.6727 -0.0088 -0.0116 0.0446  15  HOX B CD1 
1959 C CD2 . HOX B 15  ? 0.8746 0.9706 0.7044 -0.0520 -0.0191 0.0584  15  HOX B CD2 
1960 C CE1 . HOX B 15  ? 0.8493 1.0555 0.6722 -0.0255 -0.0012 0.0589  15  HOX B CE1 
1961 C CE2 . HOX B 15  ? 0.8850 1.0264 0.7142 -0.0727 -0.0087 0.0743  15  HOX B CE2 
1971 N N   . ILE B 16  ? 0.9210 0.9842 0.7015 0.0195  -0.0419 0.0420  16  ILE B N   
1972 C CA  . ILE B 16  ? 0.9785 1.0550 0.7326 0.0141  -0.0418 0.0627  16  ILE B CA  
1973 C C   . ILE B 16  ? 0.9678 1.0868 0.7015 0.0421  -0.0400 0.0611  16  ILE B C   
1974 O O   . ILE B 16  ? 0.9619 1.1300 0.6774 0.0370  -0.0312 0.0794  16  ILE B O   
1975 C CB  . ILE B 16  ? 0.9669 0.9893 0.7127 0.0127  -0.0556 0.0622  16  ILE B CB  
1976 C CG1 . ILE B 16  ? 1.0226 1.0111 0.7794 -0.0184 -0.0574 0.0707  16  ILE B CG1 
1977 C CG2 . ILE B 16  ? 1.1399 1.1744 0.8514 0.0197  -0.0578 0.0795  16  ILE B CG2 
1978 C CD1 . ILE B 16  ? 1.0197 0.9481 0.7760 -0.0148 -0.0743 0.0608  16  ILE B CD1 
1990 N N   . LEU B 17  ? 0.9598 1.0624 0.6971 0.0713  -0.0488 0.0377  17  LEU B N   
1991 C CA  . LEU B 17  ? 0.9761 1.1140 0.6941 0.1027  -0.0504 0.0310  17  LEU B CA  
1992 C C   . LEU B 17  ? 1.0528 1.2516 0.7682 0.1094  -0.0391 0.0344  17  LEU B C   
1993 O O   . LEU B 17  ? 1.0638 1.3155 0.7580 0.1218  -0.0347 0.0425  17  LEU B O   
1994 C CB  . LEU B 17  ? 1.0123 1.1137 0.7381 0.1290  -0.0634 0.0023  17  LEU B CB  
1995 C CG  . LEU B 17  ? 1.1805 1.2369 0.9051 0.1318  -0.0766 -0.0056 17  LEU B CG  
1996 C CD1 . LEU B 17  ? 1.2072 1.2316 0.9466 0.1510  -0.0881 -0.0364 17  LEU B CD1 
1997 C CD2 . LEU B 17  ? 1.2208 1.2959 0.9137 0.1455  -0.0808 0.0060  17  LEU B CD2 
2009 N N   . LEU B 18  ? 0.9874 1.1846 0.7223 0.1040  -0.0348 0.0273  18  LEU B N   
2010 C CA  . LEU B 18  ? 1.0229 1.2805 0.7533 0.1156  -0.0263 0.0281  18  LEU B CA  
2011 C C   . LEU B 18  ? 0.9993 1.3158 0.7235 0.0904  -0.0127 0.0528  18  LEU B C   
2012 O O   . LEU B 18  ? 0.9942 1.3794 0.7087 0.1031  -0.0056 0.0547  18  LEU B O   
2013 C CB  . LEU B 18  ? 1.0706 1.3122 0.8198 0.1148  -0.0252 0.0172  18  LEU B CB  
2014 C CG  . LEU B 18  ? 1.0680 1.2611 0.8193 0.1401  -0.0373 -0.0068 18  LEU B CG  
2015 C CD1 . LEU B 18  ? 1.0024 1.1696 0.7710 0.1290  -0.0351 -0.0115 18  LEU B CD1 
2016 C CD2 . LEU B 18  ? 1.0957 1.3174 0.8261 0.1797  -0.0435 -0.0200 18  LEU B CD2 
2028 N N   . MET B 19  ? 0.9501 1.2421 0.6806 0.0540  -0.0095 0.0705  19  MET B N   
2029 C CA  . MET B 19  ? 1.0078 1.3499 0.7314 0.0241  0.0028  0.0952  19  MET B CA  
2030 C C   . MET B 19  ? 1.0718 1.4484 0.7658 0.0304  0.0044  0.1089  19  MET B C   
2031 O O   . MET B 19  ? 0.9993 1.4500 0.6822 0.0234  0.0159  0.1219  19  MET B O   
2032 C CB  . MET B 19  ? 1.0038 1.2990 0.7386 -0.0159 0.0025  0.1091  19  MET B CB  
2033 C CG  . MET B 19  ? 1.0035 1.2801 0.7671 -0.0293 0.0039  0.0996  19  MET B CG  
2034 S SD  . MET B 19  ? 0.9530 1.3116 0.7285 -0.0392 0.0187  0.1030  19  MET B SD  
2035 C CE  . MET B 19  ? 0.9212 1.3119 0.6850 -0.0855 0.0280  0.1341  19  MET B CE  
2045 N N   . VAL B 20  ? 1.0648 1.3933 0.7455 0.0452  -0.0073 0.1046  20  VAL B N   
2046 C CA  . VAL B 20  ? 1.1298 1.4908 0.7795 0.0584  -0.0073 0.1146  20  VAL B CA  
2047 C C   . VAL B 20  ? 1.0890 1.5269 0.7321 0.0902  -0.0021 0.1022  20  VAL B C   
2048 O O   . VAL B 20  ? 1.1461 1.6588 0.7755 0.0816  0.0100  0.1175  20  VAL B O   
2049 C CB  . VAL B 20  ? 1.1132 1.4113 0.7524 0.0786  -0.0234 0.1040  20  VAL B CB  
2050 C CG1 . VAL B 20  ? 1.1042 1.4384 0.7113 0.1029  -0.0255 0.1075  20  VAL B CG1 
2051 C CG2 . VAL B 20  ? 1.1923 1.4245 0.8309 0.0472  -0.0289 0.1198  20  VAL B CG2 
2061 N N   . LEU B 21  ? 1.0205 1.4438 0.6749 0.1249  -0.0109 0.0737  21  LEU B N   
2062 C CA  . LEU B 21  ? 1.0488 1.5394 0.6922 0.1615  -0.0099 0.0589  21  LEU B CA  
2063 C C   . LEU B 21  ? 1.0659 1.6353 0.7155 0.1491  0.0048  0.0677  21  LEU B C   
2064 O O   . LEU B 21  ? 1.0631 1.7133 0.6979 0.1701  0.0097  0.0646  21  LEU B O   
2065 C CB  . LEU B 21  ? 1.0717 1.5212 0.7231 0.1993  -0.0243 0.0270  21  LEU B CB  
2066 C CG  . LEU B 21  ? 1.0728 1.4724 0.7136 0.2216  -0.0395 0.0127  21  LEU B CG  
2067 C CD1 . LEU B 21  ? 1.0609 1.4262 0.7067 0.2574  -0.0538 -0.0192 21  LEU B CD1 
2068 C CD2 . LEU B 21  ? 1.0852 1.5340 0.6965 0.2375  -0.0392 0.0197  21  LEU B CD2 
2080 N N   . LYS B 22  ? 1.0642 1.6177 0.7357 0.1164  0.0114  0.0765  22  LYS B N   
2081 C CA  . LYS B 22  ? 1.1060 1.7376 0.7858 0.1031  0.0248  0.0831  22  LYS B CA  
2082 C C   . LYS B 22  ? 1.1160 1.8205 0.7803 0.0754  0.0388  0.1087  22  LYS B C   
2083 O O   . LYS B 22  ? 1.0676 1.8659 0.7309 0.0781  0.0494  0.1090  22  LYS B O   
2084 C CB  . LYS B 22  ? 1.0509 1.6463 0.7576 0.0731  0.0277  0.0862  22  LYS B CB  
2085 C CG  . LYS B 22  ? 1.0961 1.7678 0.8148 0.0725  0.0373  0.0824  22  LYS B CG  
2086 C CD  . LYS B 22  ? 1.1008 1.7340 0.8450 0.0498  0.0380  0.0812  22  LYS B CD  
2087 C CE  . LYS B 22  ? 1.1454 1.8590 0.9011 0.0479  0.0471  0.0778  22  LYS B CE  
2088 N NZ  . LYS B 22  ? 1.2532 2.0401 1.0111 0.0074  0.0619  0.0990  22  LYS B NZ  
2102 N N   . GLN B 23  ? 1.1867 1.8523 0.8366 0.0497  0.0386  0.1300  23  GLN B N   
2103 C CA  . GLN B 23  ? 1.1790 1.9092 0.8084 0.0210  0.0517  0.1573  23  GLN B CA  
2104 C C   . GLN B 23  ? 1.2352 2.0350 0.8384 0.0566  0.0527  0.1513  23  GLN B C   
2105 O O   . GLN B 23  ? 1.3223 2.2115 0.9116 0.0411  0.0668  0.1674  23  GLN B O   
2106 C CB  . GLN B 23  ? 1.2649 1.9234 0.8803 -0.0161 0.0489  0.1837  23  GLN B CB  
2107 C CG  . GLN B 23  ? 1.2715 1.8668 0.9088 -0.0547 0.0477  0.1917  23  GLN B CG  
2108 C CD  . GLN B 23  ? 1.4726 1.9863 1.0912 -0.0807 0.0397  0.2129  23  GLN B CD  
2109 O OE1 . GLN B 23  ? 1.5003 2.0179 1.0864 -0.0791 0.0389  0.2291  23  GLN B OE1 
2110 N NE2 . GLN B 23  ? 1.4146 1.8535 1.0514 -0.1018 0.0323  0.2119  23  GLN B NE2 
2119 N N   . GLY B 24  ? 1.2380 2.0025 0.8342 0.1032  0.0380  0.1274  24  GLY B N   
2120 C CA  . GLY B 24  ? 1.2457 2.0736 0.8172 0.1422  0.0364  0.1170  24  GLY B CA  
2121 C C   . GLY B 24  ? 1.2276 1.9916 0.7915 0.1852  0.0172  0.0928  24  GLY B C   
2122 O O   . GLY B 24  ? 1.2368 1.9091 0.8057 0.1751  0.0074  0.0944  24  GLY B O   
2126 N N   . ASP B 25  ? 1.2023 2.0171 0.7539 0.2338  0.0108  0.0684  25  ASP B N   
2127 C CA  . ASP B 25  ? 1.2104 1.9752 0.7513 0.2753  -0.0079 0.0442  25  ASP B CA  
2128 C C   . ASP B 25  ? 1.2141 1.9258 0.7385 0.2574  -0.0116 0.0628  25  ASP B C   
2129 O O   . ASP B 25  ? 1.2654 2.0086 0.7725 0.2247  0.0009  0.0944  25  ASP B O   
2130 C CB  . ASP B 25  ? 1.2015 2.0471 0.7213 0.3249  -0.0122 0.0226  25  ASP B CB  
2131 C CG  . ASP B 25  ? 1.1235 2.0366 0.6531 0.3483  -0.0095 0.0039  25  ASP B CG  
2132 O OD1 . ASP B 25  ? 1.0435 1.9441 0.5964 0.3268  -0.0038 0.0078  25  ASP B OD1 
2133 O OD2 . ASP B 25  ? 1.1112 2.0819 0.6398 0.3872  -0.0140 -0.0158 25  ASP B OD2 
2138 N N   . ASN B 26  ? 1.2541 1.8863 0.7815 0.2770  -0.0290 0.0442  26  ASN B N   
2139 C CA  . ASN B 26  ? 1.3228 1.9028 0.8348 0.2635  -0.0348 0.0591  26  ASN B CA  
2140 C C   . ASN B 26  ? 1.4163 1.9374 0.9306 0.2998  -0.0557 0.0279  26  ASN B C   
2141 O O   . ASN B 26  ? 1.3762 1.8770 0.9084 0.3246  -0.0653 -0.0018 26  ASN B O   
2142 C CB  . ASN B 26  ? 1.2072 1.7264 0.7335 0.2145  -0.0297 0.0837  26  ASN B CB  
2143 C CG  . ASN B 26  ? 1.2646 1.7470 0.7650 0.1968  -0.0331 0.1077  26  ASN B CG  
2144 O OD1 . ASN B 26  ? 1.3458 1.8210 0.8251 0.2251  -0.0443 0.0988  26  ASN B OD1 
2145 N ND2 . ASN B 26  ? 1.3558 1.8108 0.8561 0.1514  -0.0254 0.1373  26  ASN B ND2 
2152 N N   . TYR B 27  ? 1.5574 2.0519 1.0508 0.3024  -0.0635 0.0352  27  TYR B N   
2153 C CA  . TYR B 27  ? 1.6579 2.1024 1.1511 0.3341  -0.0837 0.0070  27  TYR B CA  
2154 C C   . TYR B 27  ? 1.6484 2.0112 1.1512 0.3094  -0.0910 0.0153  27  TYR B C   
2155 O O   . TYR B 27  ? 1.6029 1.9504 1.1026 0.2718  -0.0816 0.0458  27  TYR B O   
2156 C CB  . TYR B 27  ? 1.7839 2.2764 1.2415 0.3683  -0.0899 0.0023  27  TYR B CB  
2157 C CG  . TYR B 27  ? 1.8036 2.3063 1.2278 0.3481  -0.0837 0.0375  27  TYR B CG  
2158 C CD1 . TYR B 27  ? 1.7459 2.3067 1.1521 0.3185  -0.0641 0.0730  27  TYR B CD1 
2159 C CD2 . TYR B 27  ? 1.8860 2.3411 1.2938 0.3593  -0.0987 0.0349  27  TYR B CD2 
2160 C CE1 . TYR B 27  ? 1.8418 2.4051 1.2119 0.2974  -0.0592 0.1080  27  TYR B CE1 
2161 C CE2 . TYR B 27  ? 1.9342 2.3903 1.3060 0.3424  -0.0950 0.0685  27  TYR B CE2 
2162 C CZ  . TYR B 27  ? 1.8671 2.3743 1.2183 0.3104  -0.0752 0.1065  27  TYR B CZ  
2163 O OH  . TYR B 27  ? 1.7124 2.2148 1.0221 0.2908  -0.0721 0.1432  27  TYR B OH  
2173 N N   . VAL B 28  ? 1.6755 1.9871 1.1897 0.3312  -0.1089 -0.0138 28  VAL B N   
2174 C CA  . VAL B 28  ? 1.6741 1.9107 1.2097 0.3109  -0.1168 -0.0166 28  VAL B CA  
2175 C C   . VAL B 28  ? 1.6700 1.8863 1.1822 0.2893  -0.1161 0.0139  28  VAL B C   
2176 O O   . VAL B 28  ? 1.6211 1.8041 1.1435 0.2551  -0.1104 0.0330  28  VAL B O   
2177 C CB  . VAL B 28  ? 1.4041 1.6016 0.9543 0.3388  -0.1364 -0.0551 28  VAL B CB  
2178 C CG1 . VAL B 28  ? 1.3726 1.5071 0.9401 0.3209  -0.1449 -0.0578 28  VAL B CG1 
2179 C CG2 . VAL B 28  ? 1.3471 1.5432 0.9212 0.3508  -0.1380 -0.0818 28  VAL B CG2 
2189 N N   . TYR B 29  ? 1.7372 1.9718 1.2144 0.3106  -0.1230 0.0189  29  TYR B N   
2190 C CA  . TYR B 29  ? 1.7083 1.9178 1.1544 0.2936  -0.1249 0.0496  29  TYR B CA  
2191 C C   . TYR B 29  ? 1.7119 1.9400 1.1453 0.2522  -0.1061 0.0906  29  TYR B C   
2192 O O   . TYR B 29  ? 1.5977 1.7770 1.0215 0.2239  -0.1077 0.1142  29  TYR B O   
2193 C CB  . TYR B 29  ? 1.7607 2.0002 1.1668 0.3267  -0.1336 0.0487  29  TYR B CB  
2194 C CG  . TYR B 29  ? 1.7428 1.9690 1.1020 0.3161  -0.1353 0.0841  29  TYR B CG  
2195 C CD1 . TYR B 29  ? 1.6235 1.8952 0.9490 0.2921  -0.1180 0.1243  29  TYR B CD1 
2196 C CD2 . TYR B 29  ? 1.6409 1.8142 0.9853 0.3336  -0.1555 0.0760  29  TYR B CD2 
2197 C CE1 . TYR B 29  ? 1.6200 1.8741 0.8956 0.2818  -0.1206 0.1593  29  TYR B CE1 
2198 C CE2 . TYR B 29  ? 1.7575 1.9129 1.0527 0.3282  -0.1597 0.1085  29  TYR B CE2 
2199 C CZ  . TYR B 29  ? 1.6775 1.8694 0.9367 0.3014  -0.1423 0.1514  29  TYR B CZ  
2200 O OH  . TYR B 29  ? 1.7768 1.9427 0.9818 0.2942  -0.1475 0.1861  29  TYR B OH  
2210 N N   . GLY B 30  ? 1.7190 2.0172 1.1529 0.2478  -0.0894 0.0978  30  GLY B N   
2211 C CA  . GLY B 30  ? 1.7560 2.0780 1.1834 0.2049  -0.0710 0.1336  30  GLY B CA  
2212 C C   . GLY B 30  ? 1.6810 1.9574 1.1458 0.1740  -0.0679 0.1327  30  GLY B C   
2213 O O   . GLY B 30  ? 1.5772 1.8335 1.0362 0.1344  -0.0607 0.1616  30  GLY B O   
2217 N N   . ILE B 31  ? 1.6402 1.9000 1.1418 0.1908  -0.0735 0.0996  31  ILE B N   
2218 C CA  . ILE B 31  ? 1.6888 1.9049 1.2251 0.1644  -0.0716 0.0965  31  ILE B CA  
2219 C C   . ILE B 31  ? 1.6195 1.7581 1.1548 0.1509  -0.0845 0.1011  31  ILE B C   
2220 O O   . ILE B 31  ? 1.5130 1.6216 1.0529 0.1164  -0.0806 0.1203  31  ILE B O   
2221 C CB  . ILE B 31  ? 1.6919 1.9059 1.2623 0.1864  -0.0754 0.0612  31  ILE B CB  
2222 C CG1 . ILE B 31  ? 1.5743 1.8631 1.1422 0.2009  -0.0642 0.0576  31  ILE B CG1 
2223 C CG2 . ILE B 31  ? 1.6916 1.8586 1.2952 0.1614  -0.0748 0.0568  31  ILE B CG2 
2224 C CD1 . ILE B 31  ? 1.5159 1.7983 1.1081 0.2258  -0.0701 0.0247  31  ILE B CD1 
2236 N N   . ILE B 32  ? 1.6953 1.8015 1.2248 0.1794  -0.1016 0.0813  32  ILE B N   
2237 C CA  . ILE B 32  ? 1.6646 1.7018 1.1919 0.1725  -0.1163 0.0820  32  ILE B CA  
2238 C C   . ILE B 32  ? 1.5612 1.5837 1.0498 0.1470  -0.1137 0.1218  32  ILE B C   
2239 O O   . ILE B 32  ? 1.5797 1.5507 1.0700 0.1214  -0.1178 0.1344  32  ILE B O   
2240 C CB  . ILE B 32  ? 1.6050 1.6228 1.1289 0.2103  -0.1354 0.0533  32  ILE B CB  
2241 C CG1 . ILE B 32  ? 1.5430 1.5675 1.1067 0.2273  -0.1377 0.0151  32  ILE B CG1 
2242 C CG2 . ILE B 32  ? 1.7707 1.7251 1.2881 0.2076  -0.1518 0.0536  32  ILE B CG2 
2243 C CD1 . ILE B 32  ? 1.5569 1.5710 1.1227 0.2624  -0.1555 -0.0176 32  ILE B CD1 
2255 N N   . LYS B 33  ? 1.3759 1.4452 0.8278 0.1520  -0.1066 0.1426  33  LYS B N   
2256 C CA  . LYS B 33  ? 1.4950 1.5554 0.9054 0.1229  -0.1018 0.1849  33  LYS B CA  
2257 C C   . LYS B 33  ? 1.4493 1.5092 0.8751 0.0769  -0.0875 0.2058  33  LYS B C   
2258 O O   . LYS B 33  ? 1.5016 1.5004 0.9185 0.0497  -0.0939 0.2235  33  LYS B O   
2259 C CB  . LYS B 33  ? 1.5686 1.6995 0.9418 0.1351  -0.0922 0.2012  33  LYS B CB  
2260 C CG  . LYS B 33  ? 1.5645 1.7131 0.8972 0.0967  -0.0793 0.2483  33  LYS B CG  
2261 C CD  . LYS B 33  ? 1.6256 1.8637 0.9299 0.1120  -0.0671 0.2576  33  LYS B CD  
2262 C CE  . LYS B 33  ? 1.7190 1.9928 0.9887 0.0672  -0.0494 0.3041  33  LYS B CE  
2263 N NZ  . LYS B 33  ? 1.8686 2.0611 1.0954 0.0426  -0.0603 0.3381  33  LYS B NZ  
2277 N N   . GLN B 34  ? 1.4441 1.5692 0.8948 0.0704  -0.0703 0.2002  34  GLN B N   
2278 C CA  . GLN B 34  ? 1.4700 1.6066 0.9349 0.0268  -0.0559 0.2196  34  GLN B CA  
2279 C C   . GLN B 34  ? 1.5115 1.5785 1.0073 0.0113  -0.0649 0.2080  34  GLN B C   
2280 O O   . GLN B 34  ? 1.4936 1.5376 0.9884 -0.0280 -0.0607 0.2294  34  GLN B O   
2281 C CB  . GLN B 34  ? 1.3511 1.5730 0.8399 0.0306  -0.0385 0.2091  34  GLN B CB  
2282 C CG  . GLN B 34  ? 1.4189 1.7231 0.8776 0.0385  -0.0266 0.2238  34  GLN B CG  
2283 C CD  . GLN B 34  ? 1.3716 1.7626 0.8523 0.0408  -0.0104 0.2142  34  GLN B CD  
2284 O OE1 . GLN B 34  ? 1.4017 1.7885 0.9173 0.0304  -0.0067 0.2021  34  GLN B OE1 
2285 N NE2 . GLN B 34  ? 1.5602 2.0337 1.0190 0.0568  -0.0013 0.2184  34  GLN B NE2 
2294 N N   . VAL B 35  ? 1.4903 1.5265 1.0141 0.0400  -0.0771 0.1734  35  VAL B N   
2295 C CA  . VAL B 35  ? 1.5185 1.5002 1.0741 0.0264  -0.0842 0.1597  35  VAL B CA  
2296 C C   . VAL B 35  ? 1.5863 1.4920 1.1190 0.0154  -0.1008 0.1725  35  VAL B C   
2297 O O   . VAL B 35  ? 1.5764 1.4442 1.1176 -0.0136 -0.1025 0.1812  35  VAL B O   
2298 C CB  . VAL B 35  ? 1.4178 1.3945 1.0088 0.0571  -0.0912 0.1197  35  VAL B CB  
2299 C CG1 . VAL B 35  ? 1.2719 1.1893 0.8884 0.0499  -0.1027 0.1034  35  VAL B CG1 
2300 C CG2 . VAL B 35  ? 1.4877 1.5233 1.1033 0.0595  -0.0758 0.1095  35  VAL B CG2 
2310 N N   . LYS B 36  ? 1.5612 1.4432 1.0621 0.0398  -0.1147 0.1736  36  LYS B N   
2311 C CA  . LYS B 36  ? 1.6651 1.4696 1.1414 0.0372  -0.1345 0.1820  36  LYS B CA  
2312 C C   . LYS B 36  ? 1.6901 1.4708 1.1273 -0.0021 -0.1307 0.2254  36  LYS B C   
2313 O O   . LYS B 36  ? 1.7409 1.4497 1.1649 -0.0164 -0.1454 0.2339  36  LYS B O   
2314 C CB  . LYS B 36  ? 1.6754 1.4670 1.1290 0.0785  -0.1511 0.1681  36  LYS B CB  
2315 C CG  . LYS B 36  ? 1.7072 1.4213 1.1482 0.0917  -0.1766 0.1590  36  LYS B CG  
2316 C CD  . LYS B 36  ? 1.7491 1.4591 1.1631 0.1325  -0.1924 0.1478  36  LYS B CD  
2317 C CE  . LYS B 36  ? 1.7928 1.4260 1.1847 0.1479  -0.2198 0.1426  36  LYS B CE  
2318 N NZ  . LYS B 36  ? 1.8834 1.5127 1.2372 0.1864  -0.2358 0.1391  36  LYS B NZ  
2332 N N   . GLU B 37  ? 1.6189 1.4587 1.0361 -0.0205 -0.1120 0.2523  37  GLU B N   
2333 C CA  . GLU B 37  ? 1.6445 1.4673 1.0249 -0.0644 -0.1063 0.2951  37  GLU B CA  
2334 C C   . GLU B 37  ? 1.6780 1.4897 1.0884 -0.1043 -0.0991 0.2982  37  GLU B C   
2335 O O   . GLU B 37  ? 1.6617 1.4137 1.0493 -0.1375 -0.1066 0.3220  37  GLU B O   
2336 C CB  . GLU B 37  ? 1.6363 1.5419 0.9925 -0.0740 -0.0859 0.3196  37  GLU B CB  
2337 C CG  . GLU B 37  ? 1.7213 1.6434 1.0418 -0.0376 -0.0921 0.3205  37  GLU B CG  
2338 C CD  . GLU B 37  ? 1.7428 1.7625 1.0460 -0.0432 -0.0704 0.3384  37  GLU B CD  
2339 O OE1 . GLU B 37  ? 1.6627 1.7450 0.9908 -0.0686 -0.0508 0.3421  37  GLU B OE1 
2340 O OE2 . GLU B 37  ? 1.7589 1.7994 1.0263 -0.0177 -0.0736 0.3445  37  GLU B OE2 
2347 N N   . ALA B 38  ? 1.6280 1.4966 1.0870 -0.1014 -0.0853 0.2747  38  ALA B N   
2348 C CA  . ALA B 38  ? 1.5568 1.4270 1.0482 -0.1351 -0.0775 0.2736  38  ALA B CA  
2349 C C   . ALA B 38  ? 1.6414 1.4363 1.1549 -0.1297 -0.0960 0.2511  38  ALA B C   
2350 O O   . ALA B 38  ? 1.5833 1.3561 1.1113 -0.1612 -0.0956 0.2554  38  ALA B O   
2351 C CB  . ALA B 38  ? 1.4933 1.4485 1.0250 -0.1282 -0.0584 0.2551  38  ALA B CB  
2357 N N   . SER B 39  ? 1.6995 1.4604 1.2170 -0.0905 -0.1124 0.2255  39  SER B N   
2358 C CA  . SER B 39  ? 1.8232 1.5181 1.3587 -0.0821 -0.1315 0.2026  39  SER B CA  
2359 C C   . SER B 39  ? 1.8830 1.4966 1.3746 -0.0777 -0.1550 0.2160  39  SER B C   
2360 O O   . SER B 39  ? 1.9861 1.5439 1.4870 -0.0629 -0.1748 0.1944  39  SER B O   
2361 C CB  . SER B 39  ? 1.7997 1.5118 1.3704 -0.0433 -0.1356 0.1626  39  SER B CB  
2362 O OG  . SER B 39  ? 1.7557 1.4612 1.3019 -0.0098 -0.1465 0.1575  39  SER B OG  
2368 N N   . ASN B 40  ? 1.6624 1.2694 1.1043 -0.0895 -0.1537 0.2511  40  ASN B N   
2369 C CA  . ASN B 40  ? 1.8861 1.4096 1.2775 -0.0851 -0.1772 0.2682  40  ASN B CA  
2370 C C   . ASN B 40  ? 1.9171 1.4078 1.3136 -0.0358 -0.1996 0.2344  40  ASN B C   
2371 O O   . ASN B 40  ? 1.8778 1.2902 1.2533 -0.0258 -0.2247 0.2305  40  ASN B O   
2372 C CB  . ASN B 40  ? 1.8596 1.3132 1.2409 -0.1217 -0.1876 0.2831  40  ASN B CB  
2373 C CG  . ASN B 40  ? 1.8858 1.3747 1.2618 -0.1740 -0.1661 0.3163  40  ASN B CG  
2374 O OD1 . ASN B 40  ? 1.8804 1.4067 1.2242 -0.1887 -0.1525 0.3470  40  ASN B OD1 
2375 N ND2 . ASN B 40  ? 1.9354 1.4184 1.3430 -0.2027 -0.1627 0.3094  40  ASN B ND2 
2382 N N   . GLY B 41  ? 1.8825 1.4339 1.3079 -0.0045 -0.1916 0.2075  41  GLY B N   
2383 C CA  . GLY B 41  ? 1.8739 1.4102 1.3045 0.0412  -0.2102 0.1754  41  GLY B CA  
2384 C C   . GLY B 41  ? 1.7701 1.3026 1.2528 0.0569  -0.2180 0.1322  41  GLY B C   
2385 O O   . GLY B 41  ? 1.6715 1.2058 1.1645 0.0934  -0.2310 0.1020  41  GLY B O   
2389 N N   . GLU B 42  ? 1.6441 1.1771 1.1607 0.0304  -0.2099 0.1268  42  GLU B N   
2390 C CA  . GLU B 42  ? 1.5789 1.1084 1.1407 0.0459  -0.2184 0.0863  42  GLU B CA  
2391 C C   . GLU B 42  ? 1.5379 1.1293 1.1368 0.0679  -0.2076 0.0572  42  GLU B C   
2392 O O   . GLU B 42  ? 1.5516 1.1418 1.1785 0.0898  -0.2184 0.0219  42  GLU B O   
2393 C CB  . GLU B 42  ? 1.6167 1.1418 1.2093 0.0153  -0.2111 0.0837  42  GLU B CB  
2394 C CG  . GLU B 42  ? 1.7018 1.1547 1.2717 -0.0039 -0.2280 0.0971  42  GLU B CG  
2395 C CD  . GLU B 42  ? 1.6882 1.1495 1.2970 -0.0307 -0.2199 0.0868  42  GLU B CD  
2396 O OE1 . GLU B 42  ? 1.5545 1.0726 1.2070 -0.0306 -0.2035 0.0675  42  GLU B OE1 
2397 O OE2 . GLU B 42  ? 1.6803 1.0891 1.2743 -0.0515 -0.2310 0.0978  42  GLU B OE2 
2404 N N   . MET B 43  ? 1.6588 1.3052 1.2588 0.0611  -0.1868 0.0703  43  MET B N   
2405 C CA  . MET B 43  ? 1.6535 1.3539 1.2880 0.0764  -0.1756 0.0451  43  MET B CA  
2406 C C   . MET B 43  ? 1.6146 1.3461 1.2243 0.0989  -0.1735 0.0504  43  MET B C   
2407 O O   . MET B 43  ? 1.6035 1.3644 1.1902 0.0871  -0.1600 0.0778  43  MET B O   
2408 C CB  . MET B 43  ? 1.6828 1.4235 1.3455 0.0510  -0.1536 0.0502  43  MET B CB  
2409 C CG  . MET B 43  ? 1.6024 1.3856 1.2978 0.0654  -0.1445 0.0246  43  MET B CG  
2410 S SD  . MET B 43  ? 1.3328 1.1534 1.0542 0.0363  -0.1221 0.0336  43  MET B SD  
2411 C CE  . MET B 43  ? 1.3109 1.1617 1.0649 0.0573  -0.1174 0.0009  43  MET B CE  
2421 N N   . GLU B 44  ? 1.5791 1.3096 1.1943 0.1313  -0.1869 0.0225  44  GLU B N   
2422 C CA  . GLU B 44  ? 1.5726 1.3302 1.1648 0.1582  -0.1890 0.0213  44  GLU B CA  
2423 C C   . GLU B 44  ? 1.5319 1.3262 1.1614 0.1745  -0.1850 -0.0130 44  GLU B C   
2424 O O   . GLU B 44  ? 1.5762 1.3592 1.2268 0.1920  -0.1984 -0.0450 44  GLU B O   
2425 C CB  . GLU B 44  ? 1.4422 1.1605 1.0018 0.1829  -0.2121 0.0189  44  GLU B CB  
2426 C CG  . GLU B 44  ? 1.5305 1.2694 1.0489 0.2041  -0.2140 0.0329  44  GLU B CG  
2427 C CD  . GLU B 44  ? 1.6080 1.2988 1.0828 0.2233  -0.2365 0.0415  44  GLU B CD  
2428 O OE1 . GLU B 44  ? 1.5553 1.1948 1.0336 0.2223  -0.2523 0.0336  44  GLU B OE1 
2429 O OE2 . GLU B 44  ? 1.6477 1.3519 1.0817 0.2404  -0.2391 0.0567  44  GLU B OE2 
2436 N N   . LEU B 45  ? 1.6921 1.5301 1.3277 0.1691  -0.1677 -0.0068 45  LEU B N   
2437 C CA  . LEU B 45  ? 1.7048 1.5697 1.3722 0.1805  -0.1636 -0.0357 45  LEU B CA  
2438 C C   . LEU B 45  ? 1.6466 1.5228 1.3031 0.2150  -0.1763 -0.0571 45  LEU B C   
2439 O O   . LEU B 45  ? 1.7059 1.5872 1.3257 0.2306  -0.1821 -0.0431 45  LEU B O   
2440 C CB  . LEU B 45  ? 1.7495 1.6550 1.4190 0.1690  -0.1442 -0.0216 45  LEU B CB  
2441 C CG  . LEU B 45  ? 1.6816 1.5874 1.3583 0.1350  -0.1300 0.0020  45  LEU B CG  
2442 C CD1 . LEU B 45  ? 1.8737 1.8302 1.5428 0.1304  -0.1130 0.0176  45  LEU B CD1 
2443 C CD2 . LEU B 45  ? 1.5496 1.4365 1.2649 0.1215  -0.1292 -0.0169 45  LEU B CD2 
2455 N N   . ASN B 46  ? 1.4400 1.3213 1.1272 0.2256  -0.1805 -0.0908 46  ASN B N   
2456 C CA  . ASN B 46  ? 1.4545 1.3466 1.1376 0.2569  -0.1940 -0.1172 46  ASN B CA  
2457 C C   . ASN B 46  ? 1.4719 1.3971 1.1546 0.2687  -0.1866 -0.1245 46  ASN B C   
2458 O O   . ASN B 46  ? 1.4672 1.3978 1.1705 0.2538  -0.1751 -0.1261 46  ASN B O   
2459 C CB  . ASN B 46  ? 1.4142 1.2880 1.1322 0.2589  -0.2066 -0.1532 46  ASN B CB  
2460 C CG  . ASN B 46  ? 1.4250 1.3096 1.1423 0.2893  -0.2228 -0.1845 46  ASN B CG  
2461 O OD1 . ASN B 46  ? 1.4148 1.3190 1.1051 0.3116  -0.2255 -0.1809 46  ASN B OD1 
2462 N ND2 . ASN B 46  ? 1.4495 1.3261 1.1978 0.2899  -0.2340 -0.2174 46  ASN B ND2 
2469 N N   . GLU B 47  ? 1.4279 1.3743 1.0844 0.2983  -0.1949 -0.1300 47  GLU B N   
2470 C CA  . GLU B 47  ? 1.3626 1.3413 1.0134 0.3168  -0.1917 -0.1402 47  GLU B CA  
2471 C C   . GLU B 47  ? 1.4194 1.3855 1.1049 0.3137  -0.1938 -0.1707 47  GLU B C   
2472 O O   . GLU B 47  ? 1.4408 1.4187 1.1300 0.3113  -0.1846 -0.1694 47  GLU B O   
2473 C CB  . GLU B 47  ? 1.3798 1.3790 1.0033 0.3525  -0.2054 -0.1523 47  GLU B CB  
2474 C CG  . GLU B 47  ? 1.3818 1.4203 0.9635 0.3631  -0.1972 -0.1232 47  GLU B CG  
2475 C CD  . GLU B 47  ? 1.3907 1.4593 0.9461 0.4026  -0.2098 -0.1395 47  GLU B CD  
2476 O OE1 . GLU B 47  ? 1.3815 1.4366 0.9261 0.4195  -0.2255 -0.1504 47  GLU B OE1 
2477 O OE2 . GLU B 47  ? 1.4022 1.5104 0.9470 0.4195  -0.2052 -0.1437 47  GLU B OE2 
2484 N N   . ALA B 48  ? 1.4787 1.4221 1.1873 0.3154  -0.2072 -0.1998 48  ALA B N   
2485 C CA  . ALA B 48  ? 1.4552 1.3843 1.1945 0.3092  -0.2103 -0.2291 48  ALA B CA  
2486 C C   . ALA B 48  ? 1.3545 1.2694 1.1150 0.2775  -0.1949 -0.2164 48  ALA B C   
2487 O O   . ALA B 48  ? 1.3704 1.2804 1.1380 0.2743  -0.1907 -0.2234 48  ALA B O   
2488 C CB  . ALA B 48  ? 1.4521 1.3673 1.2144 0.3110  -0.2259 -0.2607 48  ALA B CB  
2494 N N   . THR B 49  ? 1.5462 1.4527 1.3135 0.2557  -0.1875 -0.1974 49  THR B N   
2495 C CA  . THR B 49  ? 1.7335 1.6317 1.5181 0.2273  -0.1727 -0.1841 49  THR B CA  
2496 C C   . THR B 49  ? 1.6134 1.5331 1.3779 0.2294  -0.1597 -0.1603 49  THR B C   
2497 O O   . THR B 49  ? 1.6688 1.5855 1.4433 0.2194  -0.1514 -0.1600 49  THR B O   
2498 C CB  . THR B 49  ? 1.6308 1.5168 1.4251 0.2066  -0.1698 -0.1711 49  THR B CB  
2499 O OG1 . THR B 49  ? 1.6691 1.5453 1.4708 0.2164  -0.1854 -0.1917 49  THR B OG1 
2500 C CG2 . THR B 49  ? 1.3626 1.2377 1.1858 0.1788  -0.1596 -0.1729 49  THR B CG2 
2508 N N   . LEU B 50  ? 1.6123 1.5566 1.3468 0.2427  -0.1581 -0.1404 50  LEU B N   
2509 C CA  . LEU B 50  ? 1.5307 1.5078 1.2467 0.2453  -0.1454 -0.1195 50  LEU B CA  
2510 C C   . LEU B 50  ? 1.4780 1.4670 1.1890 0.2702  -0.1499 -0.1394 50  LEU B C   
2511 O O   . LEU B 50  ? 1.4830 1.4810 1.1961 0.2674  -0.1416 -0.1354 50  LEU B O   
2512 C CB  . LEU B 50  ? 1.4371 1.4419 1.1208 0.2517  -0.1428 -0.0943 50  LEU B CB  
2513 C CG  . LEU B 50  ? 1.3528 1.3964 1.0212 0.2402  -0.1261 -0.0648 50  LEU B CG  
2514 C CD1 . LEU B 50  ? 1.2772 1.3243 0.9246 0.2224  -0.1212 -0.0333 50  LEU B CD1 
2515 C CD2 . LEU B 50  ? 1.3673 1.4561 1.0146 0.2699  -0.1260 -0.0705 50  LEU B CD2 
2527 N N   . TYR B 51  ? 1.3535 1.3404 1.0569 0.2964  -0.1650 -0.1629 51  TYR B N   
2528 C CA  . TYR B 51  ? 1.3677 1.3594 1.0645 0.3219  -0.1727 -0.1849 51  TYR B CA  
2529 C C   . TYR B 51  ? 1.3393 1.2908 1.0612 0.3070  -0.1744 -0.2022 51  TYR B C   
2530 O O   . TYR B 51  ? 1.3456 1.2940 1.0609 0.3185  -0.1754 -0.2093 51  TYR B O   
2531 C CB  . TYR B 51  ? 1.3856 1.3808 1.0711 0.3518  -0.1904 -0.2097 51  TYR B CB  
2532 C CG  . TYR B 51  ? 1.4118 1.4503 1.0647 0.3745  -0.1907 -0.1960 51  TYR B CG  
2533 C CD1 . TYR B 51  ? 1.4218 1.5058 1.0505 0.3901  -0.1823 -0.1819 51  TYR B CD1 
2534 C CD2 . TYR B 51  ? 1.4245 1.4618 1.0689 0.3822  -0.2001 -0.1983 51  TYR B CD2 
2535 C CE1 . TYR B 51  ? 1.3808 1.5102 0.9779 0.4092  -0.1816 -0.1689 51  TYR B CE1 
2536 C CE2 . TYR B 51  ? 1.4026 1.4777 1.0129 0.4025  -0.2006 -0.1840 51  TYR B CE2 
2537 C CZ  . TYR B 51  ? 1.4116 1.5336 0.9985 0.4141  -0.1903 -0.1684 51  TYR B CZ  
2538 O OH  . TYR B 51  ? 1.4914 1.6561 1.0426 0.4321  -0.1897 -0.1531 51  TYR B OH  
2548 N N   . THR B 52  ? 1.5092 1.4300 1.2576 0.2834  -0.1765 -0.2108 52  THR B N   
2549 C CA  . THR B 52  ? 1.6171 1.5028 1.3884 0.2619  -0.1750 -0.2218 52  THR B CA  
2550 C C   . THR B 52  ? 1.6209 1.5110 1.3901 0.2475  -0.1594 -0.1984 52  THR B C   
2551 O O   . THR B 52  ? 1.6124 1.4852 1.3780 0.2506  -0.1600 -0.2040 52  THR B O   
2552 C CB  . THR B 52  ? 1.6761 1.5431 1.4764 0.2368  -0.1766 -0.2313 52  THR B CB  
2553 O OG1 . THR B 52  ? 1.8122 1.6784 1.6152 0.2528  -0.1929 -0.2575 52  THR B OG1 
2554 C CG2 . THR B 52  ? 1.4737 1.3108 1.2967 0.2094  -0.1719 -0.2384 52  THR B CG2 
2562 N N   . ILE B 53  ? 1.6214 1.5327 1.3909 0.2325  -0.1468 -0.1726 53  ILE B N   
2563 C CA  . ILE B 53  ? 1.6268 1.5464 1.3978 0.2166  -0.1322 -0.1519 53  ILE B CA  
2564 C C   . ILE B 53  ? 1.5288 1.4758 1.2756 0.2412  -0.1304 -0.1470 53  ILE B C   
2565 O O   . ILE B 53  ? 1.4994 1.4380 1.2458 0.2400  -0.1266 -0.1460 53  ILE B O   
2566 C CB  . ILE B 53  ? 1.6281 1.5651 1.4032 0.1953  -0.1212 -0.1270 53  ILE B CB  
2567 C CG1 . ILE B 53  ? 1.6507 1.5596 1.4507 0.1737  -0.1245 -0.1355 53  ILE B CG1 
2568 C CG2 . ILE B 53  ? 1.5197 1.4748 1.2944 0.1820  -0.1069 -0.1068 53  ILE B CG2 
2569 C CD1 . ILE B 53  ? 1.7071 1.6240 1.5053 0.1601  -0.1204 -0.1158 53  ILE B CD1 
2581 N N   . PHE B 54  ? 1.5278 1.5107 1.2524 0.2658  -0.1337 -0.1445 54  PHE B N   
2582 C CA  . PHE B 54  ? 1.4160 1.4384 1.1180 0.2906  -0.1311 -0.1403 54  PHE B CA  
2583 C C   . PHE B 54  ? 1.4069 1.4025 1.1020 0.3151  -0.1441 -0.1655 54  PHE B C   
2584 O O   . PHE B 54  ? 1.3826 1.3983 1.0629 0.3335  -0.1429 -0.1647 54  PHE B O   
2585 C CB  . PHE B 54  ? 1.3492 1.4191 1.0275 0.3131  -0.1328 -0.1352 54  PHE B CB  
2586 C CG  . PHE B 54  ? 1.3277 1.4344 1.0006 0.2924  -0.1183 -0.1041 54  PHE B CG  
2587 C CD1 . PHE B 54  ? 1.3782 1.4736 1.0686 0.2573  -0.1062 -0.0849 54  PHE B CD1 
2588 C CD2 . PHE B 54  ? 1.3222 1.4758 0.9697 0.3076  -0.1170 -0.0936 54  PHE B CD2 
2589 C CE1 . PHE B 54  ? 1.3180 1.4424 1.0012 0.2363  -0.0945 -0.0563 54  PHE B CE1 
2590 C CE2 . PHE B 54  ? 1.3152 1.4994 0.9537 0.2850  -0.1039 -0.0626 54  PHE B CE2 
2591 C CZ  . PHE B 54  ? 1.3063 1.4733 0.9625 0.2489  -0.0933 -0.0443 54  PHE B CZ  
2601 N N   . LYS B 55  ? 1.4318 1.3828 1.1357 0.3170  -0.1582 -0.1894 55  LYS B N   
2602 C CA  . LYS B 55  ? 1.4152 1.3282 1.1111 0.3360  -0.1728 -0.2139 55  LYS B CA  
2603 C C   . LYS B 55  ? 1.4329 1.3139 1.1342 0.3184  -0.1667 -0.2062 55  LYS B C   
2604 O O   . LYS B 55  ? 1.4010 1.2737 1.0828 0.3411  -0.1731 -0.2123 55  LYS B O   
2605 C CB  . LYS B 55  ? 1.4186 1.2928 1.1263 0.3337  -0.1880 -0.2401 55  LYS B CB  
2606 C CG  . LYS B 55  ? 1.4933 1.3287 1.1879 0.3573  -0.2076 -0.2692 55  LYS B CG  
2607 C CD  . LYS B 55  ? 1.5073 1.3083 1.2192 0.3468  -0.2209 -0.2948 55  LYS B CD  
2608 C CE  . LYS B 55  ? 1.4906 1.2491 1.1882 0.3680  -0.2420 -0.3244 55  LYS B CE  
2609 N NZ  . LYS B 55  ? 1.5004 1.2948 1.1687 0.4156  -0.2521 -0.3339 55  LYS B NZ  
2623 N N   . ARG B 56  ? 1.4447 1.3103 1.1698 0.2806  -0.1549 -0.1925 56  ARG B N   
2624 C CA  . ARG B 56  ? 1.4651 1.3037 1.1941 0.2627  -0.1481 -0.1834 56  ARG B CA  
2625 C C   . ARG B 56  ? 1.4641 1.3448 1.1771 0.2769  -0.1387 -0.1655 56  ARG B C   
2626 O O   . ARG B 56  ? 1.4683 1.3302 1.1673 0.2875  -0.1417 -0.1665 56  ARG B O   
2627 C CB  . ARG B 56  ? 1.5382 1.3639 1.2965 0.2212  -0.1367 -0.1732 56  ARG B CB  
2628 C CG  . ARG B 56  ? 1.4335 1.2464 1.1959 0.2005  -0.1256 -0.1579 56  ARG B CG  
2629 C CD  . ARG B 56  ? 1.4474 1.2030 1.1991 0.2004  -0.1348 -0.1693 56  ARG B CD  
2630 N NE  . ARG B 56  ? 1.4831 1.2313 1.2273 0.1922  -0.1262 -0.1532 56  ARG B NE  
2631 C CZ  . ARG B 56  ? 1.5496 1.2816 1.3100 0.1589  -0.1160 -0.1436 56  ARG B CZ  
2632 N NH1 . ARG B 56  ? 1.4357 1.1609 1.2232 0.1292  -0.1123 -0.1488 56  ARG B NH1 
2633 N NH2 . ARG B 56  ? 1.4953 1.2225 1.2437 0.1574  -0.1100 -0.1296 56  ARG B NH2 
2647 N N   . LEU B 57  ? 1.4194 1.3570 1.1332 0.2758  -0.1277 -0.1487 57  LEU B N   
2648 C CA  . LEU B 57  ? 1.4447 1.4340 1.1460 0.2865  -0.1178 -0.1329 57  LEU B CA  
2649 C C   . LEU B 57  ? 1.4906 1.4998 1.1639 0.3310  -0.1294 -0.1477 57  LEU B C   
2650 O O   . LEU B 57  ? 1.5351 1.5599 1.1964 0.3452  -0.1280 -0.1450 57  LEU B O   
2651 C CB  . LEU B 57  ? 1.3943 1.4386 1.1010 0.2717  -0.1043 -0.1118 57  LEU B CB  
2652 C CG  . LEU B 57  ? 1.3366 1.3617 1.0685 0.2307  -0.0943 -0.0975 57  LEU B CG  
2653 C CD1 . LEU B 57  ? 1.3274 1.3954 1.0591 0.2162  -0.0841 -0.0765 57  LEU B CD1 
2654 C CD2 . LEU B 57  ? 1.1836 1.1979 0.9262 0.2126  -0.0859 -0.0892 57  LEU B CD2 
2666 N N   . GLU B 58  ? 1.4354 1.4495 1.0966 0.3565  -0.1417 -0.1647 58  GLU B N   
2667 C CA  . GLU B 58  ? 1.5545 1.5835 1.1882 0.4022  -0.1554 -0.1832 58  GLU B CA  
2668 C C   . GLU B 58  ? 1.5368 1.4965 1.1616 0.4115  -0.1695 -0.1988 58  GLU B C   
2669 O O   . GLU B 58  ? 1.5393 1.5076 1.1432 0.4404  -0.1757 -0.2041 58  GLU B O   
2670 C CB  . GLU B 58  ? 1.6130 1.6552 1.2344 0.4299  -0.1685 -0.2024 58  GLU B CB  
2671 C CG  . GLU B 58  ? 1.6188 1.7114 1.2107 0.4800  -0.1779 -0.2168 58  GLU B CG  
2672 C CD  . GLU B 58  ? 1.5240 1.6458 1.1000 0.5127  -0.1901 -0.2359 58  GLU B CD  
2673 O OE1 . GLU B 58  ? 1.3401 1.4603 0.9257 0.4974  -0.1883 -0.2330 58  GLU B OE1 
2674 O OE2 . GLU B 58  ? 1.3461 1.4903 0.8981 0.5575  -0.2036 -0.2564 58  GLU B OE2 
2681 N N   . LYS B 59  ? 1.4182 1.3089 1.0575 0.3864  -0.1751 -0.2060 59  LYS B N   
2682 C CA  . LYS B 59  ? 1.4865 1.3021 1.1149 0.3883  -0.1886 -0.2184 59  LYS B CA  
2683 C C   . LYS B 59  ? 1.4105 1.2235 1.0334 0.3809  -0.1795 -0.2007 59  LYS B C   
2684 O O   . LYS B 59  ? 1.4445 1.2208 1.0418 0.4047  -0.1926 -0.2093 59  LYS B O   
2685 C CB  . LYS B 59  ? 1.5307 1.2874 1.1808 0.3531  -0.1915 -0.2258 59  LYS B CB  
2686 C CG  . LYS B 59  ? 1.5327 1.2082 1.1752 0.3397  -0.2015 -0.2327 59  LYS B CG  
2687 C CD  . LYS B 59  ? 1.5517 1.1773 1.2071 0.3217  -0.2134 -0.2537 59  LYS B CD  
2688 C CE  . LYS B 59  ? 1.5323 1.1858 1.2237 0.2879  -0.2004 -0.2487 59  LYS B CE  
2689 N NZ  . LYS B 59  ? 1.5617 1.2187 1.2743 0.2487  -0.1813 -0.2262 59  LYS B NZ  
2703 N N   . ASP B 60  ? 1.4671 1.3170 1.1113 0.3505  -0.1589 -0.1771 60  ASP B N   
2704 C CA  . ASP B 60  ? 1.5657 1.4259 1.2064 0.3444  -0.1492 -0.1605 60  ASP B CA  
2705 C C   . ASP B 60  ? 1.5996 1.5351 1.2256 0.3752  -0.1451 -0.1557 60  ASP B C   
2706 O O   . ASP B 60  ? 1.6255 1.5841 1.2523 0.3690  -0.1354 -0.1416 60  ASP B O   
2707 C CB  . ASP B 60  ? 1.5072 1.3733 1.1783 0.2976  -0.1304 -0.1403 60  ASP B CB  
2708 C CG  . ASP B 60  ? 1.5275 1.3273 1.2128 0.2679  -0.1337 -0.1461 60  ASP B CG  
2709 O OD1 . ASP B 60  ? 1.5822 1.3297 1.2529 0.2813  -0.1503 -0.1644 60  ASP B OD1 
2710 O OD2 . ASP B 60  ? 1.5157 1.3157 1.2256 0.2314  -0.1207 -0.1339 60  ASP B OD2 
2715 N N   . GLY B 61  ? 1.6202 1.6021 1.2345 0.4063  -0.1511 -0.1670 61  GLY B N   
2716 C CA  . GLY B 61  ? 1.5710 1.6319 1.1702 0.4375  -0.1480 -0.1657 61  GLY B CA  
2717 C C   . GLY B 61  ? 1.4696 1.6052 1.0877 0.4108  -0.1251 -0.1410 61  GLY B C   
2718 O O   . GLY B 61  ? 1.4233 1.6254 1.0328 0.4289  -0.1200 -0.1378 61  GLY B O   
2722 N N   . ILE B 62  ? 1.4962 1.6240 1.1395 0.3684  -0.1122 -0.1250 62  ILE B N   
2723 C CA  . ILE B 62  ? 1.4959 1.6869 1.1556 0.3400  -0.0921 -0.1015 62  ILE B CA  
2724 C C   . ILE B 62  ? 1.3890 1.6451 1.0431 0.3469  -0.0873 -0.0973 62  ILE B C   
2725 O O   . ILE B 62  ? 1.3014 1.6306 0.9575 0.3374  -0.0734 -0.0817 62  ILE B O   
2726 C CB  . ILE B 62  ? 1.4566 1.6052 1.1433 0.2924  -0.0823 -0.0867 62  ILE B CB  
2727 C CG1 . ILE B 62  ? 1.4804 1.5917 1.1719 0.2819  -0.0812 -0.0843 62  ILE B CG1 
2728 C CG2 . ILE B 62  ? 1.3924 1.5949 1.0936 0.2624  -0.0655 -0.0647 62  ILE B CG2 
2729 C CD1 . ILE B 62  ? 1.2278 1.2833 0.9424 0.2428  -0.0767 -0.0783 62  ILE B CD1 
2741 N N   . ILE B 63  ? 1.3999 1.6337 1.0448 0.3638  -0.0989 -0.1113 63  ILE B N   
2742 C CA  . ILE B 63  ? 1.3942 1.6903 1.0264 0.3786  -0.0969 -0.1099 63  ILE B CA  
2743 C C   . ILE B 63  ? 1.3254 1.6112 0.9350 0.4263  -0.1167 -0.1387 63  ILE B C   
2744 O O   . ILE B 63  ? 1.3597 1.5781 0.9653 0.4412  -0.1326 -0.1583 63  ILE B O   
2745 C CB  . ILE B 63  ? 1.3683 1.6530 1.0115 0.3469  -0.0902 -0.0946 63  ILE B CB  
2746 C CG1 . ILE B 63  ? 1.3751 1.5866 1.0215 0.3524  -0.1059 -0.1136 63  ILE B CG1 
2747 C CG2 . ILE B 63  ? 1.2896 1.5685 0.9549 0.3004  -0.0744 -0.0698 63  ILE B CG2 
2748 C CD1 . ILE B 63  ? 1.3353 1.5365 0.9882 0.3311  -0.1036 -0.1036 63  ILE B CD1 
2760 N N   . SER B 64  ? 1.3535 1.7063 0.9471 0.4480  -0.1159 -0.1407 64  SER B N   
2761 C CA  . SER B 64  ? 1.3189 1.6761 0.8899 0.4951  -0.1345 -0.1686 64  SER B CA  
2762 C C   . SER B 64  ? 1.2793 1.6906 0.8416 0.4953  -0.1287 -0.1605 64  SER B C   
2763 O O   . SER B 64  ? 1.3238 1.7660 0.8947 0.4594  -0.1109 -0.1320 64  SER B O   
2764 C CB  . SER B 64  ? 1.3483 1.7490 0.9006 0.5375  -0.1418 -0.1849 64  SER B CB  
2765 O OG  . SER B 64  ? 1.3186 1.8248 0.8669 0.5374  -0.1252 -0.1697 64  SER B OG  
2771 N N   . SER B 65  ? 1.2980 1.7151 0.8410 0.5350  -0.1451 -0.1853 65  SER B N   
2772 C CA  . SER B 65  ? 1.3090 1.7708 0.8400 0.5381  -0.1420 -0.1791 65  SER B CA  
2773 C C   . SER B 65  ? 1.4001 1.9374 0.9035 0.5890  -0.1503 -0.1995 65  SER B C   
2774 O O   . SER B 65  ? 1.4629 2.0035 0.9561 0.6275  -0.1639 -0.2249 65  SER B O   
2775 C CB  . SER B 65  ? 1.3086 1.6964 0.8467 0.5302  -0.1544 -0.1892 65  SER B CB  
2776 O OG  . SER B 65  ? 1.3365 1.6617 0.8733 0.5579  -0.1771 -0.2234 65  SER B OG  
2782 N N   . TYR B 66  ? 1.5121 2.1105 1.0008 0.5904  -0.1430 -0.1882 66  TYR B N   
2783 C CA  . TYR B 66  ? 1.5037 2.1789 0.9848 0.6295  -0.1444 -0.2021 66  TYR B CA  
2784 C C   . TYR B 66  ? 1.5476 2.2533 1.0213 0.6182  -0.1366 -0.1855 66  TYR B C   
2785 O O   . TYR B 66  ? 1.6094 2.2909 1.0744 0.5814  -0.1292 -0.1599 66  TYR B O   
2786 C CB  . TYR B 66  ? 1.4175 2.1817 0.9127 0.6307  -0.1272 -0.1911 66  TYR B CB  
2787 C CG  . TYR B 66  ? 1.3830 2.2075 0.8822 0.5834  -0.1005 -0.1505 66  TYR B CG  
2788 C CD1 . TYR B 66  ? 1.4579 2.3487 0.9547 0.5752  -0.0879 -0.1332 66  TYR B CD1 
2789 C CD2 . TYR B 66  ? 1.3480 2.1647 0.8525 0.5471  -0.0886 -0.1298 66  TYR B CD2 
2790 C CE1 . TYR B 66  ? 1.4123 2.3513 0.9092 0.5290  -0.0651 -0.0952 66  TYR B CE1 
2791 C CE2 . TYR B 66  ? 1.2779 2.1474 0.7860 0.5021  -0.0653 -0.0934 66  TYR B CE2 
2792 C CZ  . TYR B 66  ? 1.2994 2.2270 0.8027 0.4922  -0.0542 -0.0759 66  TYR B CZ  
2793 O OH  . TYR B 66  ? 1.1222 2.0957 0.6256 0.4442  -0.0324 -0.0385 66  TYR B OH  
2803 N N   . TRP B 67  ? 1.5485 2.3063 1.0238 0.6524  -0.1399 -0.2004 67  TRP B N   
2804 C CA  . TRP B 67  ? 1.4701 2.2535 0.9353 0.6501  -0.1359 -0.1897 67  TRP B CA  
2805 C C   . TRP B 67  ? 1.3791 2.2653 0.8462 0.6348  -0.1122 -0.1611 67  TRP B C   
2806 O O   . TRP B 67  ? 1.3837 2.3391 0.8657 0.6467  -0.1044 -0.1644 67  TRP B O   
2807 C CB  . TRP B 67  ? 1.4627 2.2299 0.9275 0.6988  -0.1578 -0.2278 67  TRP B CB  
2808 C CG  . TRP B 67  ? 1.5076 2.1695 0.9688 0.7042  -0.1817 -0.2527 67  TRP B CG  
2809 C CD1 . TRP B 67  ? 1.5295 2.1302 0.9954 0.7215  -0.2004 -0.2805 67  TRP B CD1 
2810 C CD2 . TRP B 67  ? 1.5396 2.1463 0.9917 0.6913  -0.1910 -0.2527 67  TRP B CD2 
2811 N NE1 . TRP B 67  ? 1.5045 2.0172 0.9666 0.7153  -0.2193 -0.2973 67  TRP B NE1 
2812 C CE2 . TRP B 67  ? 1.5165 2.0350 0.9725 0.6986  -0.2142 -0.2824 67  TRP B CE2 
2813 C CE3 . TRP B 67  ? 1.5462 2.1681 0.9864 0.6736  -0.1829 -0.2301 67  TRP B CE3 
2814 C CZ2 . TRP B 67  ? 1.5621 2.0161 1.0159 0.6885  -0.2287 -0.2928 67  TRP B CZ2 
2815 C CZ3 . TRP B 67  ? 1.5617 2.1162 0.9971 0.6682  -0.1987 -0.2400 67  TRP B CZ3 
2816 C CH2 . TRP B 67  ? 1.5738 2.0497 1.0188 0.6756  -0.2211 -0.2724 67  TRP B CH2 
2827 N N   . GLY B 68  ? 1.4295 2.3237 0.8803 0.6071  -0.1020 -0.1327 68  GLY B N   
2828 C CA  . GLY B 68  ? 1.4436 2.4279 0.8906 0.5883  -0.0811 -0.1035 68  GLY B CA  
2829 C C   . GLY B 68  ? 1.5391 2.5762 0.9812 0.6227  -0.0852 -0.1164 68  GLY B C   
2830 O O   . GLY B 68  ? 1.8229 2.9546 1.2705 0.6252  -0.0722 -0.1070 68  GLY B O   
2834 N N   . ARG B 75  ? 1.6747 2.5774 1.0804 0.6653  -0.1245 -0.1496 75  ARG B N   
2835 C CA  . ARG B 75  ? 1.6984 2.5610 1.0796 0.6325  -0.1212 -0.1192 75  ARG B CA  
2836 C C   . ARG B 75  ? 1.7017 2.4762 1.0814 0.6041  -0.1281 -0.1120 75  ARG B C   
2837 O O   . ARG B 75  ? 1.7012 2.4106 1.0757 0.6131  -0.1459 -0.1270 75  ARG B O   
2838 C CB  . ARG B 75  ? 1.7073 2.6342 1.0724 0.5960  -0.0970 -0.0741 75  ARG B CB  
2839 C CG  . ARG B 75  ? 1.7308 2.6258 1.0639 0.5731  -0.0960 -0.0444 75  ARG B CG  
2840 C CD  . ARG B 75  ? 1.7116 2.6610 1.0280 0.5312  -0.0726 0.0012  75  ARG B CD  
2841 N NE  . ARG B 75  ? 1.8074 2.7137 1.0867 0.5052  -0.0726 0.0348  75  ARG B NE  
2842 C CZ  . ARG B 75  ? 1.8724 2.7832 1.1290 0.4564  -0.0562 0.0810  75  ARG B CZ  
2843 N NH1 . ARG B 75  ? 1.9204 2.8839 1.1914 0.4257  -0.0369 0.0984  75  ARG B NH1 
2844 N NH2 . ARG B 75  ? 1.8593 2.7197 1.0775 0.4384  -0.0603 0.1098  75  ARG B NH2 
2857 N N   . ARG B 76  ? 1.7493 2.5268 1.1336 0.5685  -0.1140 -0.0879 76  ARG B N   
2858 C CA  . ARG B 76  ? 1.6890 2.3910 1.0741 0.5417  -0.1196 -0.0807 76  ARG B CA  
2859 C C   . ARG B 76  ? 1.6142 2.3026 1.0227 0.5489  -0.1232 -0.1028 76  ARG B C   
2860 O O   . ARG B 76  ? 1.5903 2.3394 1.0121 0.5593  -0.1134 -0.1077 76  ARG B O   
2861 C CB  . ARG B 76  ? 1.6856 2.3916 1.0541 0.4913  -0.1014 -0.0324 76  ARG B CB  
2862 C CG  . ARG B 76  ? 1.8444 2.5167 1.1832 0.4777  -0.1053 -0.0083 76  ARG B CG  
2863 C CD  . ARG B 76  ? 1.8641 2.5469 1.1831 0.4276  -0.0861 0.0421  76  ARG B CD  
2864 N NE  . ARG B 76  ? 2.0257 2.6733 1.3100 0.4172  -0.0911 0.0674  76  ARG B NE  
2865 C CZ  . ARG B 76  ? 2.0742 2.7287 1.3313 0.3772  -0.0769 0.1132  76  ARG B CZ  
2866 N NH1 . ARG B 76  ? 2.0942 2.7957 1.3580 0.3403  -0.0551 0.1385  76  ARG B NH1 
2867 N NH2 . ARG B 76  ? 2.1628 2.7718 1.3849 0.3734  -0.0859 0.1334  76  ARG B NH2 
2881 N N   . LYS B 77  ? 1.7200 2.3263 1.1401 0.5387  -0.1356 -0.1135 77  LYS B N   
2882 C CA  . LYS B 77  ? 1.8108 2.3847 1.2598 0.5367  -0.1376 -0.1303 77  LYS B CA  
2883 C C   . LYS B 77  ? 1.8523 2.4235 1.3183 0.4889  -0.1172 -0.0971 77  LYS B C   
2884 O O   . LYS B 77  ? 1.8392 2.3643 1.3137 0.4516  -0.1117 -0.0740 77  LYS B O   
2885 C CB  . LYS B 77  ? 1.8868 2.3673 1.3591 0.5417  -0.1571 -0.1593 77  LYS B CB  
2886 C CG  . LYS B 77  ? 1.6695 2.1151 1.1632 0.5477  -0.1628 -0.1805 77  LYS B CG  
2887 C CD  . LYS B 77  ? 1.3718 1.7283 0.8857 0.5494  -0.1818 -0.2088 77  LYS B CD  
2888 C CE  . LYS B 77  ? 1.5222 1.8433 1.0474 0.5610  -0.1903 -0.2306 77  LYS B CE  
2889 N NZ  . LYS B 77  ? 1.6092 1.8401 1.1589 0.5436  -0.2020 -0.2470 77  LYS B NZ  
2903 N N   . TYR B 78  ? 1.7573 2.3802 1.2273 0.4919  -0.1074 -0.0962 78  TYR B N   
2904 C CA  . TYR B 78  ? 1.7242 2.3538 1.2111 0.4490  -0.0886 -0.0680 78  TYR B CA  
2905 C C   . TYR B 78  ? 1.5966 2.1731 1.1116 0.4476  -0.0940 -0.0851 78  TYR B C   
2906 O O   . TYR B 78  ? 1.5215 2.0826 1.0367 0.4849  -0.1095 -0.1174 78  TYR B O   
2907 C CB  . TYR B 78  ? 1.6295 2.3688 1.0995 0.4476  -0.0709 -0.0503 78  TYR B CB  
2908 C CG  . TYR B 78  ? 1.6579 2.4340 1.1015 0.4279  -0.0606 -0.0199 78  TYR B CG  
2909 C CD1 . TYR B 78  ? 1.7815 2.5791 1.2099 0.4579  -0.0682 -0.0311 78  TYR B CD1 
2910 C CD2 . TYR B 78  ? 1.6148 2.3917 1.0589 0.3755  -0.0430 0.0199  78  TYR B CD2 
2911 C CE1 . TYR B 78  ? 1.5520 2.3734 0.9596 0.4382  -0.0588 -0.0020 78  TYR B CE1 
2912 C CE2 . TYR B 78  ? 1.6955 2.4969 1.1093 0.3564  -0.0351 0.0503  78  TYR B CE2 
2913 C CZ  . TYR B 78  ? 1.5990 2.4215 0.9951 0.3879  -0.0428 0.0396  78  TYR B CZ  
2914 O OH  . TYR B 78  ? 1.5577 2.3952 0.9280 0.3678  -0.0351 0.0698  78  TYR B OH  
2924 N N   . TYR B 79  ? 1.5566 2.0977 1.0932 0.4033  -0.0827 -0.0629 79  TYR B N   
2925 C CA  . TYR B 79  ? 1.3815 1.8797 0.9431 0.3944  -0.0836 -0.0715 79  TYR B CA  
2926 C C   . TYR B 79  ? 1.1857 1.7433 0.7537 0.3698  -0.0645 -0.0493 79  TYR B C   
2927 O O   . TYR B 79  ? 1.1534 1.7512 0.7158 0.3388  -0.0493 -0.0202 79  TYR B O   
2928 C CB  . TYR B 79  ? 1.3461 1.7518 0.9307 0.3641  -0.0879 -0.0687 79  TYR B CB  
2929 C CG  . TYR B 79  ? 1.3681 1.7126 0.9530 0.3842  -0.1073 -0.0941 79  TYR B CG  
2930 C CD1 . TYR B 79  ? 1.4745 1.8128 1.0474 0.3837  -0.1117 -0.0890 79  TYR B CD1 
2931 C CD2 . TYR B 79  ? 1.2903 1.5828 0.8859 0.4023  -0.1217 -0.1227 79  TYR B CD2 
2932 C CE1 . TYR B 79  ? 1.4326 1.7216 1.0077 0.4021  -0.1300 -0.1146 79  TYR B CE1 
2933 C CE2 . TYR B 79  ? 1.2178 1.4582 0.8154 0.4169  -0.1395 -0.1472 79  TYR B CE2 
2934 C CZ  . TYR B 79  ? 1.2908 1.5333 0.8800 0.4173  -0.1434 -0.1443 79  TYR B CZ  
2935 O OH  . TYR B 79  ? 1.4014 1.5989 0.9945 0.4318  -0.1614 -0.1708 79  TYR B OH  
2945 N N   . ARG B 80  ? 1.2282 1.7897 0.8061 0.3833  -0.0664 -0.0632 80  ARG B N   
2946 C CA  . ARG B 80  ? 1.2303 1.8514 0.8166 0.3645  -0.0504 -0.0476 80  ARG B CA  
2947 C C   . ARG B 80  ? 1.1854 1.7493 0.7924 0.3582  -0.0543 -0.0560 80  ARG B C   
2948 O O   . ARG B 80  ? 1.1455 1.6371 0.7550 0.3764  -0.0700 -0.0768 80  ARG B O   
2949 C CB  . ARG B 80  ? 1.1214 1.8443 0.6896 0.3999  -0.0481 -0.0584 80  ARG B CB  
2950 C CG  . ARG B 80  ? 1.1222 1.8303 0.6835 0.4512  -0.0666 -0.0932 80  ARG B CG  
2951 C CD  . ARG B 80  ? 1.1929 2.0104 0.7357 0.4888  -0.0650 -0.1055 80  ARG B CD  
2952 N NE  . ARG B 80  ? 1.3003 2.1772 0.8549 0.4812  -0.0539 -0.1000 80  ARG B NE  
2953 C CZ  . ARG B 80  ? 1.2857 2.1418 0.8422 0.5086  -0.0651 -0.1199 80  ARG B CZ  
2954 N NH1 . ARG B 80  ? 1.3890 2.1598 0.9355 0.5416  -0.0875 -0.1448 80  ARG B NH1 
2955 N NH2 . ARG B 80  ? 1.2045 2.1220 0.7798 0.4999  -0.0539 -0.1138 80  ARG B NH2 
2969 N N   . LEU B 81  ? 1.2359 1.8318 0.8572 0.3285  -0.0395 -0.0382 81  LEU B N   
2970 C CA  . LEU B 81  ? 1.1855 1.7422 0.8247 0.3206  -0.0405 -0.0426 81  LEU B CA  
2971 C C   . LEU B 81  ? 1.1376 1.7427 0.7670 0.3601  -0.0457 -0.0613 81  LEU B C   
2972 O O   . LEU B 81  ? 1.0658 1.7668 0.6886 0.3678  -0.0364 -0.0577 81  LEU B O   
2973 C CB  . LEU B 81  ? 1.0167 1.5858 0.6756 0.2690  -0.0232 -0.0152 81  LEU B CB  
2974 C CG  . LEU B 81  ? 1.1144 1.6319 0.7957 0.2451  -0.0214 -0.0123 81  LEU B CG  
2975 C CD1 . LEU B 81  ? 1.1828 1.6012 0.8715 0.2412  -0.0329 -0.0208 81  LEU B CD1 
2976 C CD2 . LEU B 81  ? 1.1100 1.6538 0.8075 0.1961  -0.0050 0.0136  81  LEU B CD2 
2988 N N   . THR B 82  ? 1.1874 1.7261 0.8141 0.3851  -0.0614 -0.0816 82  THR B N   
2989 C CA  . THR B 82  ? 1.2140 1.7805 0.8268 0.4270  -0.0708 -0.1010 82  THR B CA  
2990 C C   . THR B 82  ? 1.1930 1.7922 0.8201 0.4071  -0.0590 -0.0890 82  THR B C   
2991 O O   . THR B 82  ? 1.1680 1.7621 0.8168 0.3600  -0.0443 -0.0668 82  THR B O   
2992 C CB  . THR B 82  ? 1.2928 1.7649 0.8935 0.4564  -0.0928 -0.1237 82  THR B CB  
2993 O OG1 . THR B 82  ? 1.2301 1.6248 0.8485 0.4216  -0.0900 -0.1128 82  THR B OG1 
2994 C CG2 . THR B 82  ? 1.2122 1.6446 0.8011 0.4750  -0.1066 -0.1390 82  THR B CG2 
3002 N N   . GLU B 83  ? 1.1995 1.8341 0.8130 0.4462  -0.0672 -0.1056 83  GLU B N   
3003 C CA  . GLU B 83  ? 1.2129 1.8712 0.8385 0.4326  -0.0593 -0.0978 83  GLU B CA  
3004 C C   . GLU B 83  ? 1.1397 1.6944 0.7751 0.4096  -0.0630 -0.0918 83  GLU B C   
3005 O O   . GLU B 83  ? 1.1325 1.6936 0.7871 0.3758  -0.0509 -0.0765 83  GLU B O   
3006 C CB  . GLU B 83  ? 1.1994 1.9116 0.8055 0.4842  -0.0703 -0.1191 83  GLU B CB  
3007 C CG  . GLU B 83  ? 1.1704 2.0140 0.7741 0.5000  -0.0615 -0.1232 83  GLU B CG  
3008 C CD  . GLU B 83  ? 1.2808 2.1595 0.8668 0.5612  -0.0783 -0.1507 83  GLU B CD  
3009 O OE1 . GLU B 83  ? 1.2933 2.1361 0.8693 0.5752  -0.0874 -0.1565 83  GLU B OE1 
3010 O OE2 . GLU B 83  ? 1.2932 2.2279 0.8868 0.5922  -0.0823 -0.1645 83  GLU B OE2 
3017 N N   . ILE B 84  ? 1.3394 1.8019 0.9609 0.4281  -0.0801 -0.1051 84  ILE B N   
3018 C CA  . ILE B 84  ? 1.5047 1.8710 1.1344 0.4037  -0.0830 -0.0994 84  ILE B CA  
3019 C C   . ILE B 84  ? 1.4776 1.8354 1.1372 0.3484  -0.0660 -0.0778 84  ILE B C   
3020 O O   . ILE B 84  ? 1.4343 1.7630 1.1102 0.3176  -0.0587 -0.0662 84  ILE B O   
3021 C CB  . ILE B 84  ? 1.6525 1.9280 1.2634 0.4270  -0.1033 -0.1173 84  ILE B CB  
3022 C CG1 . ILE B 84  ? 1.6195 1.9052 1.1968 0.4866  -0.1232 -0.1412 84  ILE B CG1 
3023 C CG2 . ILE B 84  ? 2.1389 2.3208 1.7563 0.4003  -0.1055 -0.1111 84  ILE B CG2 
3024 C CD1 . ILE B 84  ? 1.6351 1.8587 1.1927 0.5146  -0.1439 -0.1627 84  ILE B CD1 
3036 N N   . GLY B 85  ? 1.3842 1.7697 1.0486 0.3377  -0.0606 -0.0727 85  GLY B N   
3037 C CA  . GLY B 85  ? 1.3622 1.7355 1.0501 0.2893  -0.0476 -0.0531 85  GLY B CA  
3038 C C   . GLY B 85  ? 1.1689 1.6097 0.8729 0.2579  -0.0299 -0.0337 85  GLY B C   
3039 O O   . GLY B 85  ? 1.1281 1.5442 0.8521 0.2176  -0.0214 -0.0191 85  GLY B O   
3043 N N   . HIS B 86  ? 1.2018 1.7330 0.8974 0.2749  -0.0246 -0.0344 86  HIS B N   
3044 C CA  . HIS B 86  ? 1.1474 1.7492 0.8590 0.2439  -0.0082 -0.0181 86  HIS B CA  
3045 C C   . HIS B 86  ? 1.1301 1.7124 0.8548 0.2333  -0.0068 -0.0178 86  HIS B C   
3046 O O   . HIS B 86  ? 0.9516 1.5593 0.6962 0.1948  0.0057  -0.0029 86  HIS B O   
3047 C CB  . HIS B 86  ? 0.9940 1.7056 0.6941 0.2673  -0.0035 -0.0229 86  HIS B CB  
3048 C CG  . HIS B 86  ? 1.0683 1.8228 0.7609 0.2576  0.0032  -0.0128 86  HIS B CG  
3049 N ND1 . HIS B 86  ? 0.9014 1.6566 0.5723 0.2948  -0.0071 -0.0266 86  HIS B ND1 
3050 C CD2 . HIS B 86  ? 1.0091 1.7997 0.7104 0.2138  0.0183  0.0107  86  HIS B CD2 
3051 C CE1 . HIS B 86  ? 0.9828 1.7772 0.6491 0.2749  0.0023  -0.0112 86  HIS B CE1 
3052 N NE2 . HIS B 86  ? 0.9481 1.7624 0.6311 0.2250  0.0177  0.0127  86  HIS B NE2 
3060 N N   . GLU B 87  ? 1.1451 1.6865 0.8559 0.2684  -0.0202 -0.0342 87  GLU B N   
3061 C CA  . GLU B 87  ? 1.0592 1.5758 0.7770 0.2619  -0.0203 -0.0336 87  GLU B CA  
3062 C C   . GLU B 87  ? 1.0483 1.4887 0.7849 0.2220  -0.0166 -0.0228 87  GLU B C   
3063 O O   . GLU B 87  ? 1.0363 1.4915 0.7932 0.1885  -0.0061 -0.0114 87  GLU B O   
3064 C CB  . GLU B 87  ? 1.0726 1.5509 0.7635 0.3099  -0.0377 -0.0519 87  GLU B CB  
3065 C CG  . GLU B 87  ? 1.1395 1.6144 0.8275 0.3166  -0.0395 -0.0528 87  GLU B CG  
3066 C CD  . GLU B 87  ? 1.1962 1.7772 0.8907 0.3221  -0.0312 -0.0531 87  GLU B CD  
3067 O OE1 . GLU B 87  ? 1.2720 1.9289 0.9586 0.3463  -0.0315 -0.0616 87  GLU B OE1 
3068 O OE2 . GLU B 87  ? 1.1812 1.7743 0.8896 0.3015  -0.0242 -0.0458 87  GLU B OE2 
3075 N N   . ASN B 88  ? 1.1488 1.5128 0.8801 0.2245  -0.0255 -0.0279 88  ASN B N   
3076 C CA  . ASN B 88  ? 1.1541 1.4517 0.9037 0.1894  -0.0228 -0.0209 88  ASN B CA  
3077 C C   . ASN B 88  ? 1.1406 1.4681 0.9137 0.1474  -0.0096 -0.0048 88  ASN B C   
3078 O O   . ASN B 88  ? 1.1726 1.4770 0.9641 0.1177  -0.0044 0.0017  88  ASN B O   
3079 C CB  . ASN B 88  ? 1.1678 1.3986 0.9106 0.1971  -0.0335 -0.0302 88  ASN B CB  
3080 C CG  . ASN B 88  ? 1.1940 1.3698 0.9160 0.2267  -0.0476 -0.0446 88  ASN B CG  
3081 O OD1 . ASN B 88  ? 1.2052 1.4043 0.9061 0.2610  -0.0543 -0.0522 88  ASN B OD1 
3082 N ND2 . ASN B 88  ? 1.2235 1.3252 0.9499 0.2133  -0.0531 -0.0489 88  ASN B ND2 
3089 N N   . MET B 89  ? 1.0821 1.4588 0.8527 0.1442  -0.0049 0.0019  89  MET B N   
3090 C CA  . MET B 89  ? 1.1438 1.5386 0.9317 0.1026  0.0057  0.0189  89  MET B CA  
3091 C C   . MET B 89  ? 1.0295 1.4673 0.8324 0.0816  0.0151  0.0258  89  MET B C   
3092 O O   . MET B 89  ? 0.9939 1.4139 0.8152 0.0454  0.0201  0.0351  89  MET B O   
3093 C CB  . MET B 89  ? 1.1253 1.5709 0.9023 0.1018  0.0100  0.0279  89  MET B CB  
3094 C CG  . MET B 89  ? 1.2255 1.6322 0.9880 0.1199  0.0007  0.0219  89  MET B CG  
3095 S SD  . MET B 89  ? 1.2291 1.5490 1.0044 0.0920  -0.0043 0.0258  89  MET B SD  
3096 C CE  . MET B 89  ? 1.1386 1.4953 0.9104 0.0583  0.0050  0.0506  89  MET B CE  
3106 N N   . ARG B 90  ? 1.0203 1.5142 0.8154 0.1060  0.0159  0.0188  90  ARG B N   
3107 C CA  . ARG B 90  ? 1.0697 1.6085 0.8794 0.0889  0.0236  0.0224  90  ARG B CA  
3108 C C   . ARG B 90  ? 0.9899 1.4691 0.8066 0.0865  0.0193  0.0174  90  ARG B C   
3109 O O   . ARG B 90  ? 0.9636 1.4376 0.8000 0.0541  0.0250  0.0238  90  ARG B O   
3110 C CB  . ARG B 90  ? 1.1144 1.7386 0.9134 0.1189  0.0246  0.0142  90  ARG B CB  
3111 C CG  . ARG B 90  ? 1.1029 1.7905 0.9193 0.0989  0.0333  0.0171  90  ARG B CG  
3112 C CD  . ARG B 90  ? 1.1049 1.8879 0.9127 0.1289  0.0342  0.0069  90  ARG B CD  
3113 N NE  . ARG B 90  ? 0.9683 1.7321 0.7510 0.1835  0.0203  -0.0103 90  ARG B NE  
3114 C CZ  . ARG B 90  ? 1.0074 1.7407 0.7831 0.2034  0.0126  -0.0183 90  ARG B CZ  
3115 N NH1 . ARG B 90  ? 1.1579 1.8829 0.9517 0.1749  0.0181  -0.0123 90  ARG B NH1 
3116 N NH2 . ARG B 90  ? 1.1091 1.8197 0.8565 0.2539  -0.0020 -0.0330 90  ARG B NH2 
3130 N N   . LEU B 91  ? 1.0469 1.4793 0.8458 0.1199  0.0087  0.0059  91  LEU B N   
3131 C CA  . LEU B 91  ? 1.1493 1.5217 0.9506 0.1159  0.0051  0.0031  91  LEU B CA  
3132 C C   . LEU B 91  ? 1.1061 1.4308 0.9294 0.0769  0.0090  0.0097  91  LEU B C   
3133 O O   . LEU B 91  ? 1.0613 1.3798 0.8995 0.0553  0.0133  0.0123  91  LEU B O   
3134 C CB  . LEU B 91  ? 1.1971 1.5096 0.9729 0.1508  -0.0080 -0.0078 91  LEU B CB  
3135 C CG  . LEU B 91  ? 1.1861 1.5162 0.9322 0.1990  -0.0186 -0.0190 91  LEU B CG  
3136 C CD1 . LEU B 91  ? 1.1161 1.3584 0.8386 0.2195  -0.0322 -0.0264 91  LEU B CD1 
3137 C CD2 . LEU B 91  ? 1.1317 1.5321 0.8756 0.2118  -0.0154 -0.0198 91  LEU B CD2 
3149 N N   . ARG B 92  ? 1.1062 1.4008 0.9311 0.0693  0.0067  0.0109  92  ARG B N   
3150 C CA  . ARG B 92  ? 1.0743 1.3236 0.9181 0.0379  0.0078  0.0139  92  ARG B CA  
3151 C C   . ARG B 92  ? 0.9572 1.2410 0.8201 0.0043  0.0160  0.0240  92  ARG B C   
3152 O O   . ARG B 92  ? 0.8817 1.1409 0.7616 -0.0185 0.0171  0.0234  92  ARG B O   
3153 C CB  . ARG B 92  ? 1.1753 1.3914 1.0147 0.0401  0.0021  0.0122  92  ARG B CB  
3154 C CG  . ARG B 92  ? 1.2214 1.3924 1.0454 0.0676  -0.0075 -0.0003 92  ARG B CG  
3155 C CD  . ARG B 92  ? 1.2500 1.3943 1.0696 0.0730  -0.0142 -0.0048 92  ARG B CD  
3156 N NE  . ARG B 92  ? 1.3217 1.4282 1.1252 0.1007  -0.0245 -0.0186 92  ARG B NE  
3157 C CZ  . ARG B 92  ? 1.2864 1.3712 1.0813 0.1151  -0.0331 -0.0273 92  ARG B CZ  
3158 N NH1 . ARG B 92  ? 1.2779 1.3756 1.0765 0.1070  -0.0324 -0.0226 92  ARG B NH1 
3159 N NH2 . ARG B 92  ? 1.4323 1.4789 1.2124 0.1382  -0.0436 -0.0411 92  ARG B NH2 
3173 N N   . HIS B 93  ? 0.9340 1.2775 0.7940 0.0004  0.0214  0.0323  93  HIS B N   
3174 C CA  . HIS B 93  ? 0.9175 1.2913 0.7939 -0.0356 0.0283  0.0428  93  HIS B CA  
3175 C C   . HIS B 93  ? 0.8523 1.2523 0.7426 -0.0453 0.0323  0.0396  93  HIS B C   
3176 O O   . HIS B 93  ? 0.7665 1.1588 0.6744 -0.0764 0.0341  0.0427  93  HIS B O   
3177 C CB  . HIS B 93  ? 0.9273 1.3668 0.7957 -0.0396 0.0345  0.0530  93  HIS B CB  
3178 C CG  . HIS B 93  ? 0.8706 1.3389 0.7534 -0.0809 0.0411  0.0652  93  HIS B CG  
3179 N ND1 . HIS B 93  ? 0.9136 1.3495 0.7962 -0.1096 0.0397  0.0775  93  HIS B ND1 
3180 C CD2 . HIS B 93  ? 0.8356 1.3556 0.7326 -0.0991 0.0473  0.0659  93  HIS B CD2 
3181 C CE1 . HIS B 93  ? 0.9375 1.4018 0.8320 -0.1456 0.0448  0.0865  93  HIS B CE1 
3182 N NE2 . HIS B 93  ? 0.8880 1.4059 0.7935 -0.1408 0.0499  0.0787  93  HIS B NE2 
3190 N N   . GLU B 94  ? 0.8397 1.2683 0.7204 -0.0170 0.0321  0.0322  94  GLU B N   
3191 C CA  . GLU B 94  ? 0.8530 1.3110 0.7438 -0.0221 0.0351  0.0285  94  GLU B CA  
3192 C C   . GLU B 94  ? 0.7752 1.1719 0.6723 -0.0273 0.0316  0.0233  94  GLU B C   
3193 O O   . GLU B 94  ? 0.7477 1.1521 0.6621 -0.0498 0.0343  0.0225  94  GLU B O   
3194 C CB  . GLU B 94  ? 0.8661 1.3751 0.7403 0.0141  0.0340  0.0219  94  GLU B CB  
3195 C CG  . GLU B 94  ? 0.9074 1.4987 0.7799 0.0158  0.0394  0.0251  94  GLU B CG  
3196 C CD  . GLU B 94  ? 0.8592 1.5131 0.7169 0.0543  0.0372  0.0150  94  GLU B CD  
3197 O OE1 . GLU B 94  ? 0.8745 1.5147 0.7250 0.0744  0.0321  0.0075  94  GLU B OE1 
3198 O OE2 . GLU B 94  ? 0.8867 1.6042 0.7374 0.0666  0.0396  0.0142  94  GLU B OE2 
3205 N N   . SER B 95  ? 0.8017 1.1411 0.6850 -0.0076 0.0255  0.0188  95  SER B N   
3206 C CA  . SER B 95  ? 0.8247 1.1048 0.7145 -0.0175 0.0231  0.0145  95  SER B CA  
3207 C C   . SER B 95  ? 0.8031 1.0708 0.7174 -0.0524 0.0249  0.0153  95  SER B C   
3208 O O   . SER B 95  ? 0.7992 1.0632 0.7265 -0.0670 0.0264  0.0115  95  SER B O   
3209 C CB  . SER B 95  ? 0.8900 1.1129 0.7660 -0.0015 0.0164  0.0103  95  SER B CB  
3210 O OG  . SER B 95  ? 1.0686 1.2697 0.9236 0.0235  0.0124  0.0067  95  SER B OG  
3216 N N   . TRP B 96  ? 0.7910 1.0473 0.7088 -0.0635 0.0230  0.0194  96  TRP B N   
3217 C CA  . TRP B 96  ? 0.7354 0.9685 0.6713 -0.0924 0.0211  0.0191  96  TRP B CA  
3218 C C   . TRP B 96  ? 0.7493 1.0246 0.6985 -0.1169 0.0250  0.0238  96  TRP B C   
3219 O O   . TRP B 96  ? 0.7578 1.0122 0.7220 -0.1402 0.0217  0.0210  96  TRP B O   
3220 C CB  . TRP B 96  ? 0.7729 0.9767 0.7030 -0.0941 0.0160  0.0229  96  TRP B CB  
3221 C CG  . TRP B 96  ? 0.7896 0.9419 0.7165 -0.0797 0.0099  0.0129  96  TRP B CG  
3222 C CD1 . TRP B 96  ? 0.8709 1.0094 0.7814 -0.0550 0.0071  0.0103  96  TRP B CD1 
3223 C CD2 . TRP B 96  ? 0.7711 0.8837 0.7123 -0.0901 0.0054  0.0021  96  TRP B CD2 
3224 N NE1 . TRP B 96  ? 0.8062 0.8980 0.7211 -0.0525 0.0017  -0.0008 96  TRP B NE1 
3225 C CE2 . TRP B 96  ? 0.7903 0.8692 0.7244 -0.0736 0.0012  -0.0060 96  TRP B CE2 
3226 C CE3 . TRP B 96  ? 0.7845 0.8902 0.7442 -0.1109 0.0039  -0.0036 96  TRP B CE3 
3227 C CZ2 . TRP B 96  ? 0.7660 0.8109 0.7125 -0.0795 -0.0031 -0.0190 96  TRP B CZ2 
3228 C CZ3 . TRP B 96  ? 0.7442 0.8160 0.7150 -0.1128 -0.0010 -0.0175 96  TRP B CZ3 
3229 C CH2 . TRP B 96  ? 0.6830 0.7281 0.6478 -0.0982 -0.0036 -0.0247 96  TRP B CH2 
3240 N N   . SER B 97  ? 0.7218 1.0572 0.6659 -0.1125 0.0308  0.0294  97  SER B N   
3241 C CA  . SER B 97  ? 0.7720 1.1524 0.7314 -0.1359 0.0347  0.0303  97  SER B CA  
3242 C C   . SER B 97  ? 0.7074 1.0871 0.6761 -0.1326 0.0345  0.0196  97  SER B C   
3243 O O   . SER B 97  ? 0.7426 1.1218 0.7287 -0.1561 0.0331  0.0150  97  SER B O   
3244 C CB  . SER B 97  ? 0.7701 1.2253 0.7236 -0.1311 0.0412  0.0362  97  SER B CB  
3245 O OG  . SER B 97  ? 0.7646 1.2315 0.7139 -0.1485 0.0430  0.0484  97  SER B OG  
3251 N N   . ARG B 98  ? 0.6594 1.0374 0.6140 -0.1030 0.0350  0.0155  98  ARG B N   
3252 C CA  . ARG B 98  ? 0.7786 1.1572 0.7367 -0.0990 0.0354  0.0080  98  ARG B CA  
3253 C C   . ARG B 98  ? 0.6966 1.0254 0.6682 -0.1158 0.0322  0.0012  98  ARG B C   
3254 O O   . ARG B 98  ? 0.6602 0.9998 0.6437 -0.1263 0.0326  -0.0057 98  ARG B O   
3255 C CB  . ARG B 98  ? 0.7722 1.1430 0.7059 -0.0643 0.0346  0.0074  98  ARG B CB  
3256 C CG  . ARG B 98  ? 0.7890 1.2027 0.7047 -0.0381 0.0347  0.0107  98  ARG B CG  
3257 C CD  . ARG B 98  ? 0.7531 1.1662 0.6440 -0.0039 0.0315  0.0080  98  ARG B CD  
3258 N NE  . ARG B 98  ? 0.8096 1.1500 0.6838 0.0069  0.0272  0.0084  98  ARG B NE  
3259 C CZ  . ARG B 98  ? 0.9016 1.2080 0.7541 0.0302  0.0216  0.0089  98  ARG B CZ  
3260 N NH1 . ARG B 98  ? 0.8020 1.1419 0.6453 0.0496  0.0194  0.0084  98  ARG B NH1 
3261 N NH2 . ARG B 98  ? 0.9379 1.1782 0.7775 0.0335  0.0178  0.0089  98  ARG B NH2 
3275 N N   . VAL B 99  ? 0.7003 0.9792 0.6698 -0.1159 0.0285  0.0012  99  VAL B N   
3276 C CA  . VAL B 99  ? 0.6534 0.8897 0.6355 -0.1283 0.0245  -0.0078 99  VAL B CA  
3277 C C   . VAL B 99  ? 0.6644 0.9035 0.6664 -0.1550 0.0203  -0.0120 99  VAL B C   
3278 O O   . VAL B 99  ? 0.6246 0.8554 0.6405 -0.1651 0.0176  -0.0233 99  VAL B O   
3279 C CB  . VAL B 99  ? 0.6300 0.8196 0.6041 -0.1190 0.0204  -0.0082 99  VAL B CB  
3280 C CG1 . VAL B 99  ? 0.6604 0.8160 0.6505 -0.1331 0.0148  -0.0193 99  VAL B CG1 
3281 C CG2 . VAL B 99  ? 0.5971 0.7710 0.5523 -0.0961 0.0223  -0.0075 99  VAL B CG2 
3291 N N   . ASP B 100 ? 0.6470 0.8958 0.6488 -0.1673 0.0188  -0.0034 100 ASP B N   
3292 C CA  . ASP B 100 ? 0.7023 0.9403 0.7186 -0.1939 0.0121  -0.0068 100 ASP B CA  
3293 C C   . ASP B 100 ? 0.6967 0.9756 0.7267 -0.2074 0.0141  -0.0129 100 ASP B C   
3294 O O   . ASP B 100 ? 0.6474 0.9130 0.6917 -0.2257 0.0068  -0.0228 100 ASP B O   
3295 C CB  . ASP B 100 ? 0.7355 0.9705 0.7437 -0.2075 0.0102  0.0072  100 ASP B CB  
3296 C CG  . ASP B 100 ? 0.8741 1.0609 0.8702 -0.1962 0.0049  0.0102  100 ASP B CG  
3297 O OD1 . ASP B 100 ? 0.8654 1.0127 0.8668 -0.1885 -0.0013 -0.0022 100 ASP B OD1 
3298 O OD2 . ASP B 100 ? 0.8477 1.0420 0.8294 -0.1950 0.0069  0.0239  100 ASP B OD2 
3303 N N   . LYS B 101 ? 0.6840 1.0139 0.7090 -0.1968 0.0221  -0.0090 101 LYS B N   
3304 C CA  . LYS B 101 ? 0.7316 1.1049 0.7693 -0.2060 0.0235  -0.0170 101 LYS B CA  
3305 C C   . LYS B 101 ? 0.6972 1.0542 0.7398 -0.1967 0.0220  -0.0303 101 LYS B C   
3306 O O   . LYS B 101 ? 0.7022 1.0663 0.7604 -0.2111 0.0177  -0.0424 101 LYS B O   
3307 C CB  . LYS B 101 ? 0.7168 1.1539 0.7465 -0.1937 0.0312  -0.0107 101 LYS B CB  
3308 C CG  . LYS B 101 ? 0.7784 1.2712 0.8208 -0.2010 0.0324  -0.0198 101 LYS B CG  
3309 C CD  . LYS B 101 ? 0.8039 1.3105 0.8668 -0.2384 0.0279  -0.0238 101 LYS B CD  
3310 C CE  . LYS B 101 ? 0.8474 1.4087 0.9250 -0.2445 0.0276  -0.0371 101 LYS B CE  
3311 N NZ  . LYS B 101 ? 0.7711 1.3444 0.8689 -0.2831 0.0216  -0.0433 101 LYS B NZ  
3325 N N   . ILE B 102 ? 0.5836 0.9179 0.6123 -0.1744 0.0251  -0.0288 102 ILE B N   
3326 C CA  . ILE B 102 ? 0.5933 0.9121 0.6254 -0.1699 0.0249  -0.0398 102 ILE B CA  
3327 C C   . ILE B 102 ? 0.5649 0.8565 0.6159 -0.1879 0.0166  -0.0534 102 ILE B C   
3328 O O   . ILE B 102 ? 0.5598 0.8662 0.6233 -0.1949 0.0142  -0.0666 102 ILE B O   
3329 C CB  . ILE B 102 ? 0.5833 0.8698 0.5971 -0.1503 0.0283  -0.0349 102 ILE B CB  
3330 C CG1 . ILE B 102 ? 0.5780 0.8882 0.5694 -0.1284 0.0336  -0.0246 102 ILE B CG1 
3331 C CG2 . ILE B 102 ? 0.5658 0.8365 0.5853 -0.1530 0.0285  -0.0460 102 ILE B CG2 
3332 C CD1 . ILE B 102 ? 0.5785 0.8493 0.5479 -0.1103 0.0350  -0.0193 102 ILE B CD1 
3344 N N   . ILE B 103 ? 0.6168 0.8703 0.6690 -0.1940 0.0105  -0.0515 103 ILE B N   
3345 C CA  . ILE B 103 ? 0.6453 0.8676 0.7120 -0.2065 -0.0006 -0.0658 103 ILE B CA  
3346 C C   . ILE B 103 ? 0.6645 0.9032 0.7437 -0.2272 -0.0073 -0.0713 103 ILE B C   
3347 O O   . ILE B 103 ? 0.6311 0.8668 0.7240 -0.2337 -0.0152 -0.0891 103 ILE B O   
3348 C CB  . ILE B 103 ? 0.6288 0.8054 0.6890 -0.2053 -0.0071 -0.0610 103 ILE B CB  
3349 C CG1 . ILE B 103 ? 0.6263 0.7816 0.6828 -0.1888 -0.0049 -0.0666 103 ILE B CG1 
3350 C CG2 . ILE B 103 ? 0.6725 0.8178 0.7422 -0.2198 -0.0216 -0.0714 103 ILE B CG2 
3351 C CD1 . ILE B 103 ? 0.6607 0.8140 0.6997 -0.1745 0.0027  -0.0521 103 ILE B CD1 
3363 N N   . GLU B 104 ? 0.6601 0.9205 0.7349 -0.2384 -0.0046 -0.0576 104 GLU B N   
3364 C CA  . GLU B 104 ? 0.6898 0.9713 0.7767 -0.2621 -0.0100 -0.0623 104 GLU B CA  
3365 C C   . GLU B 104 ? 0.6817 1.0005 0.7813 -0.2590 -0.0090 -0.0788 104 GLU B C   
3366 O O   . GLU B 104 ? 0.7052 1.0168 0.8184 -0.2719 -0.0194 -0.0953 104 GLU B O   
3367 C CB  . GLU B 104 ? 0.6850 1.0025 0.7648 -0.2720 -0.0026 -0.0443 104 GLU B CB  
3368 C CG  . GLU B 104 ? 0.8284 1.1697 0.9186 -0.3025 -0.0068 -0.0445 104 GLU B CG  
3369 C CD  . GLU B 104 ? 0.9113 1.3011 0.9942 -0.3105 0.0033  -0.0268 104 GLU B CD  
3370 O OE1 . GLU B 104 ? 0.8882 1.2626 0.9554 -0.3035 0.0072  -0.0112 104 GLU B OE1 
3371 O OE2 . GLU B 104 ? 0.9076 1.3573 1.0008 -0.3216 0.0073  -0.0301 104 GLU B OE2 
3378 N N   . ASN B 105 ? 0.6230 0.9771 0.7152 -0.2394 0.0019  -0.0758 105 ASN B N   
3379 C CA  . ASN B 105 ? 0.5929 0.9844 0.6931 -0.2352 0.0031  -0.0896 105 ASN B CA  
3380 C C   . ASN B 105 ? 0.6674 1.0347 0.7742 -0.2295 -0.0019 -0.1068 105 ASN B C   
3381 O O   . ASN B 105 ? 0.7067 1.0976 0.8253 -0.2331 -0.0061 -0.1236 105 ASN B O   
3382 C CB  . ASN B 105 ? 0.6133 1.0438 0.6979 -0.2135 0.0146  -0.0800 105 ASN B CB  
3383 C CG  . ASN B 105 ? 0.6782 1.1539 0.7593 -0.2158 0.0190  -0.0691 105 ASN B CG  
3384 O OD1 . ASN B 105 ? 0.7109 1.1983 0.8041 -0.2392 0.0148  -0.0691 105 ASN B OD1 
3385 N ND2 . ASN B 105 ? 0.5730 1.0747 0.6359 -0.1915 0.0266  -0.0603 105 ASN B ND2 
3392 N N   . LEU B 106 ? 0.5955 0.9234 0.6954 -0.2195 -0.0011 -0.1044 106 LEU B N   
3393 C CA  . LEU B 106 ? 0.6125 0.9264 0.7204 -0.2150 -0.0053 -0.1225 106 LEU B CA  
3394 C C   . LEU B 106 ? 0.6808 0.9800 0.8062 -0.2283 -0.0210 -0.1427 106 LEU B C   
3395 O O   . LEU B 106 ? 0.6899 1.0052 0.8261 -0.2258 -0.0255 -0.1633 106 LEU B O   
3396 C CB  . LEU B 106 ? 0.6118 0.8880 0.7118 -0.2053 -0.0032 -0.1179 106 LEU B CB  
3397 C CG  . LEU B 106 ? 0.6157 0.8976 0.6979 -0.1910 0.0100  -0.1044 106 LEU B CG  
3398 C CD1 . LEU B 106 ? 0.5585 0.7986 0.6370 -0.1866 0.0084  -0.1023 106 LEU B CD1 
3399 C CD2 . LEU B 106 ? 0.5386 0.8475 0.6184 -0.1856 0.0169  -0.1116 106 LEU B CD2 
3411 N N   . GLU B 107 ? 0.7061 0.9725 0.8320 -0.2420 -0.0306 -0.1372 107 GLU B N   
3412 C CA  . GLU B 107 ? 0.7680 1.0087 0.9055 -0.2556 -0.0487 -0.1549 107 GLU B CA  
3413 C C   . GLU B 107 ? 0.8157 1.0946 0.9647 -0.2685 -0.0520 -0.1656 107 GLU B C   
3414 O O   . GLU B 107 ? 0.9207 1.1912 1.0813 -0.2724 -0.0664 -0.1890 107 GLU B O   
3415 C CB  . GLU B 107 ? 0.8391 1.0308 0.9677 -0.2694 -0.0576 -0.1413 107 GLU B CB  
3416 C CG  . GLU B 107 ? 0.8355 0.9920 0.9515 -0.2552 -0.0547 -0.1303 107 GLU B CG  
3417 C CD  . GLU B 107 ? 0.8848 0.9909 0.9878 -0.2668 -0.0643 -0.1159 107 GLU B CD  
3418 O OE1 . GLU B 107 ? 0.9991 1.0980 1.1007 -0.2898 -0.0709 -0.1097 107 GLU B OE1 
3419 O OE2 . GLU B 107 ? 0.8250 0.8981 0.9182 -0.2535 -0.0659 -0.1116 107 GLU B OE2 
3426 N N   . ALA B 108 ? 0.7845 1.1068 0.9306 -0.2743 -0.0407 -0.1512 108 ALA B N   
3427 C CA  . ALA B 108 ? 0.7952 1.1608 0.9537 -0.2864 -0.0440 -0.1633 108 ALA B CA  
3428 C C   . ALA B 108 ? 0.8473 1.2536 1.0109 -0.2691 -0.0401 -0.1802 108 ALA B C   
3429 O O   . ALA B 108 ? 0.8992 1.3210 1.0762 -0.2746 -0.0505 -0.2027 108 ALA B O   
3430 C CB  . ALA B 108 ? 0.7591 1.1685 0.9143 -0.2967 -0.0337 -0.1453 108 ALA B CB  
3436 N N   . ASN B 109 ? 0.7721 1.1966 0.9230 -0.2488 -0.0256 -0.1694 109 ASN B N   
3437 C CA  . ASN B 109 ? 0.8198 1.2843 0.9703 -0.2341 -0.0204 -0.1813 109 ASN B CA  
3438 C C   . ASN B 109 ? 0.9077 1.3597 1.0704 -0.2316 -0.0312 -0.2076 109 ASN B C   
3439 O O   . ASN B 109 ? 0.9510 1.4426 1.1191 -0.2256 -0.0320 -0.2246 109 ASN B O   
3440 C CB  . ASN B 109 ? 0.7684 1.2388 0.8979 -0.2153 -0.0046 -0.1627 109 ASN B CB  
3441 C CG  . ASN B 109 ? 0.7572 1.2563 0.8730 -0.2099 0.0045  -0.1430 109 ASN B CG  
3442 O OD1 . ASN B 109 ? 0.7932 1.3257 0.9175 -0.2196 0.0012  -0.1458 109 ASN B OD1 
3443 N ND2 . ASN B 109 ? 0.6058 1.0928 0.7002 -0.1944 0.0148  -0.1245 109 ASN B ND2 
3450 N N   . LYS B 110 ? 1.0001 1.4012 1.1669 -0.2347 -0.0411 -0.2134 110 LYS B N   
3451 C CA  . LYS B 110 ? 1.0325 1.4247 1.2113 -0.2290 -0.0541 -0.2423 110 LYS B CA  
3452 C C   . LYS B 110 ? 1.1082 1.5166 1.3016 -0.2380 -0.0695 -0.2662 110 LYS B C   
3453 O O   . LYS B 110 ? 1.0767 1.5070 1.2791 -0.2283 -0.0765 -0.2928 110 LYS B O   
3454 C CB  . LYS B 110 ? 1.0089 1.3415 1.1877 -0.2285 -0.0651 -0.2448 110 LYS B CB  
3455 C CG  . LYS B 110 ? 0.9913 1.3167 1.1621 -0.2149 -0.0537 -0.2364 110 LYS B CG  
3456 C CD  . LYS B 110 ? 0.9923 1.3615 1.1676 -0.2020 -0.0467 -0.2539 110 LYS B CD  
3457 C CE  . LYS B 110 ? 0.9039 1.2674 1.0726 -0.1937 -0.0356 -0.2471 110 LYS B CE  
3458 N NZ  . LYS B 110 ? 0.9422 1.2942 1.0924 -0.1951 -0.0191 -0.2144 110 LYS B NZ  
3472 N N   . LYS B 111 ? 1.1167 1.5189 1.3124 -0.2573 -0.0746 -0.2581 111 LYS B N   
3473 C CA  . LYS B 111 ? 1.0903 1.5055 1.2997 -0.2710 -0.0899 -0.2794 111 LYS B CA  
3474 C C   . LYS B 111 ? 0.9361 1.4159 1.1477 -0.2753 -0.0792 -0.2739 111 LYS B C   
3475 O O   . LYS B 111 ? 0.9038 1.4331 1.1167 -0.2601 -0.0736 -0.2857 111 LYS B O   
3476 C CB  . LYS B 111 ? 1.1768 1.5322 1.3867 -0.2947 -0.1059 -0.2753 111 LYS B CB  
3477 C CG  . LYS B 111 ? 1.1890 1.4785 1.3957 -0.2867 -0.1227 -0.2879 111 LYS B CG  
3478 C CD  . LYS B 111 ? 1.2485 1.4705 1.4468 -0.3089 -0.1364 -0.2755 111 LYS B CD  
3479 C CE  . LYS B 111 ? 1.2141 1.4241 1.3977 -0.3110 -0.1198 -0.2409 111 LYS B CE  
3480 N NZ  . LYS B 111 ? 1.4672 1.6111 1.6382 -0.3324 -0.1321 -0.2258 111 LYS B NZ  
# 
