data_9F8Y
# 
_entry.id   9F8Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F8Y         pdb_00009f8y 10.2210/pdb9f8y/pdb 
WWPDB D_1292137946 ?            ?                   
# 
_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       2025-05-21 
_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                        9F8Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-07 
_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              bruno.correia@epfl.ch 
_pdbx_contact_author.name_first         Bruno 
_pdbx_contact_author.name_last          Correia 
_pdbx_contact_author.name_mi            E 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7377-8636 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Castro, K.M.'  1 0000-0002-7753-6060 
'Correia, B.E.' 2 0000-0002-7377-8636 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Accurate single domain scaffolding of three non-overlapping protein epitopes using deep learning' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Castro, K.M.'   1 0000-0002-7753-6060 
primary 'Watson, J.L.'   2 ?                   
primary 'Wang, J.'       3 ?                   
primary 'Southern, J.'   4 ?                   
primary 'Ayardulabi, R.' 5 ?                   
primary 'Georgeon, S.'   6 ?                   
primary 'Rosset, S.'     7 ?                   
primary 'Baker, D.'      8 ?                   
primary 'Correia, B.E.'  9 0000-0002-7377-8636 
# 
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 'RSVF-multi-3.5 designed scaffold' 16847.234 4  ? ? ? ? 
2 water   nat water                              18.015    62 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGWHHHHHHENLYFQGASMKLVIARVKSPKVKRLSEEDIEKIKSALKSTNKAVVTIKDENGEEIEVEVRLLTLEEALKYI
NDLPISNDAKKLMSNNIHKALEPGRTVVFGPEGCEERDKNRGIIKTFSTDVKLDETYFFFRVEAEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGWHHHHHHENLYFQGASMKLVIARVKSPKVKRLSEEDIEKIKSALKSTNKAVVTIKDENGEEIEVEVRLLTLEEALKYI
NDLPISNDAKKLMSNNIHKALEPGRTVVFGPEGCEERDKNRGIIKTFSTDVKLDETYFFFRVEAEQ
;
_entity_poly.pdbx_strand_id                 D,A,B,C 
_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   MET n 
1 2   GLY n 
1 3   TRP n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  GLU n 
1 11  ASN n 
1 12  LEU n 
1 13  TYR n 
1 14  PHE n 
1 15  GLN n 
1 16  GLY n 
1 17  ALA n 
1 18  SER n 
1 19  MET n 
1 20  LYS n 
1 21  LEU n 
1 22  VAL n 
1 23  ILE n 
1 24  ALA n 
1 25  ARG n 
1 26  VAL n 
1 27  LYS n 
1 28  SER n 
1 29  PRO n 
1 30  LYS n 
1 31  VAL n 
1 32  LYS n 
1 33  ARG n 
1 34  LEU n 
1 35  SER n 
1 36  GLU n 
1 37  GLU n 
1 38  ASP n 
1 39  ILE n 
1 40  GLU n 
1 41  LYS n 
1 42  ILE n 
1 43  LYS n 
1 44  SER n 
1 45  ALA n 
1 46  LEU n 
1 47  LYS n 
1 48  SER n 
1 49  THR n 
1 50  ASN n 
1 51  LYS n 
1 52  ALA n 
1 53  VAL n 
1 54  VAL n 
1 55  THR n 
1 56  ILE n 
1 57  LYS n 
1 58  ASP n 
1 59  GLU n 
1 60  ASN n 
1 61  GLY n 
1 62  GLU n 
1 63  GLU n 
1 64  ILE n 
1 65  GLU n 
1 66  VAL n 
1 67  GLU n 
1 68  VAL n 
1 69  ARG n 
1 70  LEU n 
1 71  LEU n 
1 72  THR n 
1 73  LEU n 
1 74  GLU n 
1 75  GLU n 
1 76  ALA n 
1 77  LEU n 
1 78  LYS n 
1 79  TYR n 
1 80  ILE n 
1 81  ASN n 
1 82  ASP n 
1 83  LEU n 
1 84  PRO n 
1 85  ILE n 
1 86  SER n 
1 87  ASN n 
1 88  ASP n 
1 89  ALA n 
1 90  LYS n 
1 91  LYS n 
1 92  LEU n 
1 93  MET n 
1 94  SER n 
1 95  ASN n 
1 96  ASN n 
1 97  ILE n 
1 98  HIS n 
1 99  LYS n 
1 100 ALA n 
1 101 LEU n 
1 102 GLU n 
1 103 PRO n 
1 104 GLY n 
1 105 ARG n 
1 106 THR n 
1 107 VAL n 
1 108 VAL n 
1 109 PHE n 
1 110 GLY n 
1 111 PRO n 
1 112 GLU n 
1 113 GLY n 
1 114 CYS n 
1 115 GLU n 
1 116 GLU n 
1 117 ARG n 
1 118 ASP n 
1 119 LYS n 
1 120 ASN n 
1 121 ARG n 
1 122 GLY n 
1 123 ILE n 
1 124 ILE n 
1 125 LYS n 
1 126 THR n 
1 127 PHE n 
1 128 SER n 
1 129 THR n 
1 130 ASP n 
1 131 VAL n 
1 132 LYS n 
1 133 LEU n 
1 134 ASP n 
1 135 GLU n 
1 136 THR n 
1 137 TYR n 
1 138 PHE n 
1 139 PHE n 
1 140 PHE n 
1 141 ARG n 
1 142 VAL n 
1 143 GLU n 
1 144 ALA n 
1 145 GLU n 
1 146 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   146 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
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   MET 1   -17 ?   ?   ?   D . n 
A 1 2   GLY 2   -16 ?   ?   ?   D . n 
A 1 3   TRP 3   -15 ?   ?   ?   D . n 
A 1 4   HIS 4   -14 ?   ?   ?   D . n 
A 1 5   HIS 5   -13 ?   ?   ?   D . n 
A 1 6   HIS 6   -12 ?   ?   ?   D . n 
A 1 7   HIS 7   -11 ?   ?   ?   D . n 
A 1 8   HIS 8   -10 ?   ?   ?   D . n 
A 1 9   HIS 9   -9  ?   ?   ?   D . n 
A 1 10  GLU 10  -8  ?   ?   ?   D . n 
A 1 11  ASN 11  -7  ?   ?   ?   D . n 
A 1 12  LEU 12  -6  ?   ?   ?   D . n 
A 1 13  TYR 13  -5  ?   ?   ?   D . n 
A 1 14  PHE 14  -4  ?   ?   ?   D . n 
A 1 15  GLN 15  -3  ?   ?   ?   D . n 
A 1 16  GLY 16  -2  ?   ?   ?   D . n 
A 1 17  ALA 17  -1  ?   ?   ?   D . n 
A 1 18  SER 18  0   ?   ?   ?   D . n 
A 1 19  MET 19  1   1   MET MET D . n 
A 1 20  LYS 20  2   2   LYS LYS D . n 
A 1 21  LEU 21  3   3   LEU LEU D . n 
A 1 22  VAL 22  4   4   VAL VAL D . n 
A 1 23  ILE 23  5   5   ILE ILE D . n 
A 1 24  ALA 24  6   6   ALA ALA D . n 
A 1 25  ARG 25  7   7   ARG ARG D . n 
A 1 26  VAL 26  8   8   VAL VAL D . n 
A 1 27  LYS 27  9   9   LYS LYS D . n 
A 1 28  SER 28  10  10  SER SER D . n 
A 1 29  PRO 29  11  11  PRO PRO D . n 
A 1 30  LYS 30  12  12  LYS LYS D . n 
A 1 31  VAL 31  13  13  VAL VAL D . n 
A 1 32  LYS 32  14  14  LYS LYS D . n 
A 1 33  ARG 33  15  15  ARG ARG D . n 
A 1 34  LEU 34  16  16  LEU LEU D . n 
A 1 35  SER 35  17  17  SER SER D . n 
A 1 36  GLU 36  18  18  GLU GLU D . n 
A 1 37  GLU 37  19  19  GLU GLU D . n 
A 1 38  ASP 38  20  20  ASP ASP D . n 
A 1 39  ILE 39  21  21  ILE ILE D . n 
A 1 40  GLU 40  22  22  GLU GLU D . n 
A 1 41  LYS 41  23  23  LYS LYS D . n 
A 1 42  ILE 42  24  24  ILE ILE D . n 
A 1 43  LYS 43  25  25  LYS LYS D . n 
A 1 44  SER 44  26  26  SER SER D . n 
A 1 45  ALA 45  27  27  ALA ALA D . n 
A 1 46  LEU 46  28  28  LEU LEU D . n 
A 1 47  LYS 47  29  29  LYS LYS D . n 
A 1 48  SER 48  30  30  SER SER D . n 
A 1 49  THR 49  31  31  THR THR D . n 
A 1 50  ASN 50  32  32  ASN ASN D . n 
A 1 51  LYS 51  33  33  LYS LYS D . n 
A 1 52  ALA 52  34  34  ALA ALA D . n 
A 1 53  VAL 53  35  35  VAL VAL D . n 
A 1 54  VAL 54  36  36  VAL VAL D . n 
A 1 55  THR 55  37  37  THR THR D . n 
A 1 56  ILE 56  38  38  ILE ILE D . n 
A 1 57  LYS 57  39  39  LYS LYS D . n 
A 1 58  ASP 58  40  40  ASP ASP D . n 
A 1 59  GLU 59  41  41  GLU GLU D . n 
A 1 60  ASN 60  42  42  ASN ASN D . n 
A 1 61  GLY 61  43  43  GLY GLY D . n 
A 1 62  GLU 62  44  44  GLU GLU D . n 
A 1 63  GLU 63  45  45  GLU GLU D . n 
A 1 64  ILE 64  46  46  ILE ILE D . n 
A 1 65  GLU 65  47  47  GLU GLU D . n 
A 1 66  VAL 66  48  48  VAL VAL D . n 
A 1 67  GLU 67  49  49  GLU GLU D . n 
A 1 68  VAL 68  50  50  VAL VAL D . n 
A 1 69  ARG 69  51  51  ARG ARG D . n 
A 1 70  LEU 70  52  52  LEU LEU D . n 
A 1 71  LEU 71  53  53  LEU LEU D . n 
A 1 72  THR 72  54  54  THR THR D . n 
A 1 73  LEU 73  55  55  LEU LEU D . n 
A 1 74  GLU 74  56  56  GLU GLU D . n 
A 1 75  GLU 75  57  57  GLU GLU D . n 
A 1 76  ALA 76  58  58  ALA ALA D . n 
A 1 77  LEU 77  59  59  LEU LEU D . n 
A 1 78  LYS 78  60  60  LYS LYS D . n 
A 1 79  TYR 79  61  61  TYR TYR D . n 
A 1 80  ILE 80  62  62  ILE ILE D . n 
A 1 81  ASN 81  63  63  ASN ASN D . n 
A 1 82  ASP 82  64  64  ASP ASP D . n 
A 1 83  LEU 83  65  65  LEU LEU D . n 
A 1 84  PRO 84  66  66  PRO PRO D . n 
A 1 85  ILE 85  67  67  ILE ILE D . n 
A 1 86  SER 86  68  68  SER SER D . n 
A 1 87  ASN 87  69  69  ASN ASN D . n 
A 1 88  ASP 88  70  70  ASP ASP D . n 
A 1 89  ALA 89  71  71  ALA ALA D . n 
A 1 90  LYS 90  72  72  LYS LYS D . n 
A 1 91  LYS 91  73  73  LYS LYS D . n 
A 1 92  LEU 92  74  74  LEU LEU D . n 
A 1 93  MET 93  75  75  MET MET D . n 
A 1 94  SER 94  76  76  SER SER D . n 
A 1 95  ASN 95  77  77  ASN ASN D . n 
A 1 96  ASN 96  78  78  ASN ASN D . n 
A 1 97  ILE 97  79  79  ILE ILE D . n 
A 1 98  HIS 98  80  80  HIS HIS D . n 
A 1 99  LYS 99  81  81  LYS LYS D . n 
A 1 100 ALA 100 82  82  ALA ALA D . n 
A 1 101 LEU 101 83  83  LEU LEU D . n 
A 1 102 GLU 102 84  84  GLU GLU D . n 
A 1 103 PRO 103 85  85  PRO PRO D . n 
A 1 104 GLY 104 86  86  GLY GLY D . n 
A 1 105 ARG 105 87  87  ARG ARG D . n 
A 1 106 THR 106 88  88  THR THR D . n 
A 1 107 VAL 107 89  89  VAL VAL D . n 
A 1 108 VAL 108 90  90  VAL VAL D . n 
A 1 109 PHE 109 91  91  PHE PHE D . n 
A 1 110 GLY 110 92  92  GLY GLY D . n 
A 1 111 PRO 111 93  93  PRO PRO D . n 
A 1 112 GLU 112 94  94  GLU GLU D . n 
A 1 113 GLY 113 95  95  GLY GLY D . n 
A 1 114 CYS 114 96  96  CYS CYS D . n 
A 1 115 GLU 115 97  97  GLU GLU D . n 
A 1 116 GLU 116 98  98  GLU GLU D . n 
A 1 117 ARG 117 99  99  ARG ARG D . n 
A 1 118 ASP 118 100 100 ASP ASP D . n 
A 1 119 LYS 119 101 101 LYS LYS D . n 
A 1 120 ASN 120 102 ?   ?   ?   D . n 
A 1 121 ARG 121 103 ?   ?   ?   D . n 
A 1 122 GLY 122 104 104 GLY GLY D . n 
A 1 123 ILE 123 105 105 ILE ILE D . n 
A 1 124 ILE 124 106 106 ILE ILE D . n 
A 1 125 LYS 125 107 107 LYS LYS D . n 
A 1 126 THR 126 108 108 THR THR D . n 
A 1 127 PHE 127 109 109 PHE PHE D . n 
A 1 128 SER 128 110 110 SER SER D . n 
A 1 129 THR 129 111 111 THR THR D . n 
A 1 130 ASP 130 112 112 ASP ASP D . n 
A 1 131 VAL 131 113 113 VAL VAL D . n 
A 1 132 LYS 132 114 114 LYS LYS D . n 
A 1 133 LEU 133 115 115 LEU LEU D . n 
A 1 134 ASP 134 116 116 ASP ASP D . n 
A 1 135 GLU 135 117 117 GLU GLU D . n 
A 1 136 THR 136 118 118 THR THR D . n 
A 1 137 TYR 137 119 119 TYR TYR D . n 
A 1 138 PHE 138 120 120 PHE PHE D . n 
A 1 139 PHE 139 121 121 PHE PHE D . n 
A 1 140 PHE 140 122 122 PHE PHE D . n 
A 1 141 ARG 141 123 123 ARG ARG D . n 
A 1 142 VAL 142 124 124 VAL VAL D . n 
A 1 143 GLU 143 125 ?   ?   ?   D . n 
A 1 144 ALA 144 126 ?   ?   ?   D . n 
A 1 145 GLU 145 127 ?   ?   ?   D . n 
A 1 146 GLN 146 128 ?   ?   ?   D . n 
B 1 1   MET 1   -17 ?   ?   ?   A . n 
B 1 2   GLY 2   -16 ?   ?   ?   A . n 
B 1 3   TRP 3   -15 ?   ?   ?   A . n 
B 1 4   HIS 4   -14 ?   ?   ?   A . n 
B 1 5   HIS 5   -13 ?   ?   ?   A . n 
B 1 6   HIS 6   -12 ?   ?   ?   A . n 
B 1 7   HIS 7   -11 ?   ?   ?   A . n 
B 1 8   HIS 8   -10 ?   ?   ?   A . n 
B 1 9   HIS 9   -9  ?   ?   ?   A . n 
B 1 10  GLU 10  -8  ?   ?   ?   A . n 
B 1 11  ASN 11  -7  ?   ?   ?   A . n 
B 1 12  LEU 12  -6  ?   ?   ?   A . n 
B 1 13  TYR 13  -5  ?   ?   ?   A . n 
B 1 14  PHE 14  -4  ?   ?   ?   A . n 
B 1 15  GLN 15  -3  ?   ?   ?   A . n 
B 1 16  GLY 16  -2  ?   ?   ?   A . n 
B 1 17  ALA 17  -1  ?   ?   ?   A . n 
B 1 18  SER 18  0   ?   ?   ?   A . n 
B 1 19  MET 19  1   1   MET MET A . n 
B 1 20  LYS 20  2   2   LYS LYS A . n 
B 1 21  LEU 21  3   3   LEU LEU A . n 
B 1 22  VAL 22  4   4   VAL VAL A . n 
B 1 23  ILE 23  5   5   ILE ILE A . n 
B 1 24  ALA 24  6   6   ALA ALA A . n 
B 1 25  ARG 25  7   7   ARG ARG A . n 
B 1 26  VAL 26  8   8   VAL VAL A . n 
B 1 27  LYS 27  9   9   LYS LYS A . n 
B 1 28  SER 28  10  10  SER SER A . n 
B 1 29  PRO 29  11  11  PRO PRO A . n 
B 1 30  LYS 30  12  12  LYS LYS A . n 
B 1 31  VAL 31  13  13  VAL VAL A . n 
B 1 32  LYS 32  14  14  LYS LYS A . n 
B 1 33  ARG 33  15  15  ARG ARG A . n 
B 1 34  LEU 34  16  16  LEU LEU A . n 
B 1 35  SER 35  17  17  SER SER A . n 
B 1 36  GLU 36  18  18  GLU GLU A . n 
B 1 37  GLU 37  19  19  GLU GLU A . n 
B 1 38  ASP 38  20  20  ASP ASP A . n 
B 1 39  ILE 39  21  21  ILE ILE A . n 
B 1 40  GLU 40  22  22  GLU GLU A . n 
B 1 41  LYS 41  23  23  LYS LYS A . n 
B 1 42  ILE 42  24  24  ILE ILE A . n 
B 1 43  LYS 43  25  25  LYS LYS A . n 
B 1 44  SER 44  26  26  SER SER A . n 
B 1 45  ALA 45  27  27  ALA ALA A . n 
B 1 46  LEU 46  28  28  LEU LEU A . n 
B 1 47  LYS 47  29  29  LYS LYS A . n 
B 1 48  SER 48  30  30  SER SER A . n 
B 1 49  THR 49  31  31  THR THR A . n 
B 1 50  ASN 50  32  32  ASN ASN A . n 
B 1 51  LYS 51  33  33  LYS LYS A . n 
B 1 52  ALA 52  34  34  ALA ALA A . n 
B 1 53  VAL 53  35  35  VAL VAL A . n 
B 1 54  VAL 54  36  36  VAL VAL A . n 
B 1 55  THR 55  37  37  THR THR A . n 
B 1 56  ILE 56  38  38  ILE ILE A . n 
B 1 57  LYS 57  39  39  LYS LYS A . n 
B 1 58  ASP 58  40  40  ASP ASP A . n 
B 1 59  GLU 59  41  41  GLU GLU A . n 
B 1 60  ASN 60  42  ?   ?   ?   A . n 
B 1 61  GLY 61  43  ?   ?   ?   A . n 
B 1 62  GLU 62  44  44  GLU GLU A . n 
B 1 63  GLU 63  45  45  GLU GLU A . n 
B 1 64  ILE 64  46  46  ILE ILE A . n 
B 1 65  GLU 65  47  47  GLU GLU A . n 
B 1 66  VAL 66  48  48  VAL VAL A . n 
B 1 67  GLU 67  49  49  GLU GLU A . n 
B 1 68  VAL 68  50  50  VAL VAL A . n 
B 1 69  ARG 69  51  51  ARG ARG A . n 
B 1 70  LEU 70  52  52  LEU LEU A . n 
B 1 71  LEU 71  53  53  LEU LEU A . n 
B 1 72  THR 72  54  54  THR THR A . n 
B 1 73  LEU 73  55  55  LEU LEU A . n 
B 1 74  GLU 74  56  56  GLU GLU A . n 
B 1 75  GLU 75  57  57  GLU GLU A . n 
B 1 76  ALA 76  58  58  ALA ALA A . n 
B 1 77  LEU 77  59  59  LEU LEU A . n 
B 1 78  LYS 78  60  60  LYS LYS A . n 
B 1 79  TYR 79  61  61  TYR TYR A . n 
B 1 80  ILE 80  62  62  ILE ILE A . n 
B 1 81  ASN 81  63  63  ASN ASN A . n 
B 1 82  ASP 82  64  64  ASP ASP A . n 
B 1 83  LEU 83  65  65  LEU LEU A . n 
B 1 84  PRO 84  66  66  PRO PRO A . n 
B 1 85  ILE 85  67  67  ILE ILE A . n 
B 1 86  SER 86  68  68  SER SER A . n 
B 1 87  ASN 87  69  69  ASN ASN A . n 
B 1 88  ASP 88  70  70  ASP ASP A . n 
B 1 89  ALA 89  71  71  ALA ALA A . n 
B 1 90  LYS 90  72  72  LYS LYS A . n 
B 1 91  LYS 91  73  73  LYS LYS A . n 
B 1 92  LEU 92  74  74  LEU LEU A . n 
B 1 93  MET 93  75  75  MET MET A . n 
B 1 94  SER 94  76  76  SER SER A . n 
B 1 95  ASN 95  77  77  ASN ASN A . n 
B 1 96  ASN 96  78  78  ASN ASN A . n 
B 1 97  ILE 97  79  79  ILE ILE A . n 
B 1 98  HIS 98  80  80  HIS HIS A . n 
B 1 99  LYS 99  81  81  LYS LYS A . n 
B 1 100 ALA 100 82  82  ALA ALA A . n 
B 1 101 LEU 101 83  83  LEU LEU A . n 
B 1 102 GLU 102 84  84  GLU GLU A . n 
B 1 103 PRO 103 85  85  PRO PRO A . n 
B 1 104 GLY 104 86  86  GLY GLY A . n 
B 1 105 ARG 105 87  87  ARG ARG A . n 
B 1 106 THR 106 88  88  THR THR A . n 
B 1 107 VAL 107 89  89  VAL VAL A . n 
B 1 108 VAL 108 90  90  VAL VAL A . n 
B 1 109 PHE 109 91  91  PHE PHE A . n 
B 1 110 GLY 110 92  92  GLY GLY A . n 
B 1 111 PRO 111 93  93  PRO PRO A . n 
B 1 112 GLU 112 94  94  GLU GLU A . n 
B 1 113 GLY 113 95  95  GLY GLY A . n 
B 1 114 CYS 114 96  96  CYS CYS A . n 
B 1 115 GLU 115 97  97  GLU GLU A . n 
B 1 116 GLU 116 98  98  GLU GLU A . n 
B 1 117 ARG 117 99  99  ARG ARG A . n 
B 1 118 ASP 118 100 100 ASP ASP A . n 
B 1 119 LYS 119 101 101 LYS LYS A . n 
B 1 120 ASN 120 102 102 ASN ASN A . n 
B 1 121 ARG 121 103 103 ARG ARG A . n 
B 1 122 GLY 122 104 104 GLY GLY A . n 
B 1 123 ILE 123 105 105 ILE ILE A . n 
B 1 124 ILE 124 106 106 ILE ILE A . n 
B 1 125 LYS 125 107 107 LYS LYS A . n 
B 1 126 THR 126 108 108 THR THR A . n 
B 1 127 PHE 127 109 109 PHE PHE A . n 
B 1 128 SER 128 110 110 SER SER A . n 
B 1 129 THR 129 111 111 THR THR A . n 
B 1 130 ASP 130 112 112 ASP ASP A . n 
B 1 131 VAL 131 113 113 VAL VAL A . n 
B 1 132 LYS 132 114 114 LYS LYS A . n 
B 1 133 LEU 133 115 115 LEU LEU A . n 
B 1 134 ASP 134 116 116 ASP ASP A . n 
B 1 135 GLU 135 117 117 GLU GLU A . n 
B 1 136 THR 136 118 118 THR THR A . n 
B 1 137 TYR 137 119 119 TYR TYR A . n 
B 1 138 PHE 138 120 120 PHE PHE A . n 
B 1 139 PHE 139 121 121 PHE PHE A . n 
B 1 140 PHE 140 122 122 PHE PHE A . n 
B 1 141 ARG 141 123 123 ARG ARG A . n 
B 1 142 VAL 142 124 124 VAL VAL A . n 
B 1 143 GLU 143 125 ?   ?   ?   A . n 
B 1 144 ALA 144 126 ?   ?   ?   A . n 
B 1 145 GLU 145 127 ?   ?   ?   A . n 
B 1 146 GLN 146 128 ?   ?   ?   A . n 
C 1 1   MET 1   -17 ?   ?   ?   B . n 
C 1 2   GLY 2   -16 ?   ?   ?   B . n 
C 1 3   TRP 3   -15 ?   ?   ?   B . n 
C 1 4   HIS 4   -14 ?   ?   ?   B . n 
C 1 5   HIS 5   -13 ?   ?   ?   B . n 
C 1 6   HIS 6   -12 ?   ?   ?   B . n 
C 1 7   HIS 7   -11 ?   ?   ?   B . n 
C 1 8   HIS 8   -10 ?   ?   ?   B . n 
C 1 9   HIS 9   -9  ?   ?   ?   B . n 
C 1 10  GLU 10  -8  ?   ?   ?   B . n 
C 1 11  ASN 11  -7  ?   ?   ?   B . n 
C 1 12  LEU 12  -6  ?   ?   ?   B . n 
C 1 13  TYR 13  -5  ?   ?   ?   B . n 
C 1 14  PHE 14  -4  ?   ?   ?   B . n 
C 1 15  GLN 15  -3  ?   ?   ?   B . n 
C 1 16  GLY 16  -2  ?   ?   ?   B . n 
C 1 17  ALA 17  -1  ?   ?   ?   B . n 
C 1 18  SER 18  0   ?   ?   ?   B . n 
C 1 19  MET 19  1   1   MET MET B . n 
C 1 20  LYS 20  2   2   LYS LYS B . n 
C 1 21  LEU 21  3   3   LEU LEU B . n 
C 1 22  VAL 22  4   4   VAL VAL B . n 
C 1 23  ILE 23  5   5   ILE ILE B . n 
C 1 24  ALA 24  6   6   ALA ALA B . n 
C 1 25  ARG 25  7   7   ARG ARG B . n 
C 1 26  VAL 26  8   8   VAL VAL B . n 
C 1 27  LYS 27  9   9   LYS LYS B . n 
C 1 28  SER 28  10  10  SER SER B . n 
C 1 29  PRO 29  11  11  PRO PRO B . n 
C 1 30  LYS 30  12  12  LYS LYS B . n 
C 1 31  VAL 31  13  13  VAL VAL B . n 
C 1 32  LYS 32  14  14  LYS LYS B . n 
C 1 33  ARG 33  15  15  ARG ARG B . n 
C 1 34  LEU 34  16  16  LEU LEU B . n 
C 1 35  SER 35  17  17  SER SER B . n 
C 1 36  GLU 36  18  18  GLU GLU B . n 
C 1 37  GLU 37  19  19  GLU GLU B . n 
C 1 38  ASP 38  20  20  ASP ASP B . n 
C 1 39  ILE 39  21  21  ILE ILE B . n 
C 1 40  GLU 40  22  22  GLU GLU B . n 
C 1 41  LYS 41  23  23  LYS LYS B . n 
C 1 42  ILE 42  24  24  ILE ILE B . n 
C 1 43  LYS 43  25  25  LYS LYS B . n 
C 1 44  SER 44  26  26  SER SER B . n 
C 1 45  ALA 45  27  27  ALA ALA B . n 
C 1 46  LEU 46  28  28  LEU LEU B . n 
C 1 47  LYS 47  29  29  LYS LYS B . n 
C 1 48  SER 48  30  30  SER SER B . n 
C 1 49  THR 49  31  31  THR THR B . n 
C 1 50  ASN 50  32  32  ASN ASN B . n 
C 1 51  LYS 51  33  33  LYS LYS B . n 
C 1 52  ALA 52  34  34  ALA ALA B . n 
C 1 53  VAL 53  35  35  VAL VAL B . n 
C 1 54  VAL 54  36  36  VAL VAL B . n 
C 1 55  THR 55  37  37  THR THR B . n 
C 1 56  ILE 56  38  38  ILE ILE B . n 
C 1 57  LYS 57  39  39  LYS LYS B . n 
C 1 58  ASP 58  40  40  ASP ASP B . n 
C 1 59  GLU 59  41  41  GLU GLU B . n 
C 1 60  ASN 60  42  42  ASN ASN B . n 
C 1 61  GLY 61  43  43  GLY GLY B . n 
C 1 62  GLU 62  44  ?   ?   ?   B . n 
C 1 63  GLU 63  45  ?   ?   ?   B . n 
C 1 64  ILE 64  46  46  ILE ILE B . n 
C 1 65  GLU 65  47  47  GLU GLU B . n 
C 1 66  VAL 66  48  48  VAL VAL B . n 
C 1 67  GLU 67  49  49  GLU GLU B . n 
C 1 68  VAL 68  50  50  VAL VAL B . n 
C 1 69  ARG 69  51  51  ARG ARG B . n 
C 1 70  LEU 70  52  52  LEU LEU B . n 
C 1 71  LEU 71  53  53  LEU LEU B . n 
C 1 72  THR 72  54  54  THR THR B . n 
C 1 73  LEU 73  55  55  LEU LEU B . n 
C 1 74  GLU 74  56  56  GLU GLU B . n 
C 1 75  GLU 75  57  57  GLU GLU B . n 
C 1 76  ALA 76  58  58  ALA ALA B . n 
C 1 77  LEU 77  59  59  LEU LEU B . n 
C 1 78  LYS 78  60  60  LYS LYS B . n 
C 1 79  TYR 79  61  61  TYR TYR B . n 
C 1 80  ILE 80  62  62  ILE ILE B . n 
C 1 81  ASN 81  63  63  ASN ASN B . n 
C 1 82  ASP 82  64  64  ASP ASP B . n 
C 1 83  LEU 83  65  65  LEU LEU B . n 
C 1 84  PRO 84  66  66  PRO PRO B . n 
C 1 85  ILE 85  67  67  ILE ILE B . n 
C 1 86  SER 86  68  68  SER SER B . n 
C 1 87  ASN 87  69  69  ASN ASN B . n 
C 1 88  ASP 88  70  70  ASP ASP B . n 
C 1 89  ALA 89  71  71  ALA ALA B . n 
C 1 90  LYS 90  72  72  LYS LYS B . n 
C 1 91  LYS 91  73  73  LYS LYS B . n 
C 1 92  LEU 92  74  74  LEU LEU B . n 
C 1 93  MET 93  75  75  MET MET B . n 
C 1 94  SER 94  76  76  SER SER B . n 
C 1 95  ASN 95  77  77  ASN ASN B . n 
C 1 96  ASN 96  78  78  ASN ASN B . n 
C 1 97  ILE 97  79  79  ILE ILE B . n 
C 1 98  HIS 98  80  80  HIS HIS B . n 
C 1 99  LYS 99  81  81  LYS LYS B . n 
C 1 100 ALA 100 82  82  ALA ALA B . n 
C 1 101 LEU 101 83  83  LEU LEU B . n 
C 1 102 GLU 102 84  84  GLU GLU B . n 
C 1 103 PRO 103 85  85  PRO PRO B . n 
C 1 104 GLY 104 86  86  GLY GLY B . n 
C 1 105 ARG 105 87  87  ARG ARG B . n 
C 1 106 THR 106 88  88  THR THR B . n 
C 1 107 VAL 107 89  89  VAL VAL B . n 
C 1 108 VAL 108 90  90  VAL VAL B . n 
C 1 109 PHE 109 91  91  PHE PHE B . n 
C 1 110 GLY 110 92  92  GLY GLY B . n 
C 1 111 PRO 111 93  93  PRO PRO B . n 
C 1 112 GLU 112 94  94  GLU GLU B . n 
C 1 113 GLY 113 95  95  GLY GLY B . n 
C 1 114 CYS 114 96  96  CYS CYS B . n 
C 1 115 GLU 115 97  97  GLU GLU B . n 
C 1 116 GLU 116 98  98  GLU GLU B . n 
C 1 117 ARG 117 99  99  ARG ARG B . n 
C 1 118 ASP 118 100 100 ASP ASP B . n 
C 1 119 LYS 119 101 101 LYS LYS B . n 
C 1 120 ASN 120 102 102 ASN ASN B . n 
C 1 121 ARG 121 103 103 ARG ARG B . n 
C 1 122 GLY 122 104 104 GLY GLY B . n 
C 1 123 ILE 123 105 105 ILE ILE B . n 
C 1 124 ILE 124 106 106 ILE ILE B . n 
C 1 125 LYS 125 107 107 LYS LYS B . n 
C 1 126 THR 126 108 108 THR THR B . n 
C 1 127 PHE 127 109 109 PHE PHE B . n 
C 1 128 SER 128 110 110 SER SER B . n 
C 1 129 THR 129 111 111 THR THR B . n 
C 1 130 ASP 130 112 112 ASP ASP B . n 
C 1 131 VAL 131 113 113 VAL VAL B . n 
C 1 132 LYS 132 114 114 LYS LYS B . n 
C 1 133 LEU 133 115 115 LEU LEU B . n 
C 1 134 ASP 134 116 116 ASP ASP B . n 
C 1 135 GLU 135 117 117 GLU GLU B . n 
C 1 136 THR 136 118 118 THR THR B . n 
C 1 137 TYR 137 119 119 TYR TYR B . n 
C 1 138 PHE 138 120 120 PHE PHE B . n 
C 1 139 PHE 139 121 121 PHE PHE B . n 
C 1 140 PHE 140 122 122 PHE PHE B . n 
C 1 141 ARG 141 123 123 ARG ARG B . n 
C 1 142 VAL 142 124 124 VAL VAL B . n 
C 1 143 GLU 143 125 ?   ?   ?   B . n 
C 1 144 ALA 144 126 ?   ?   ?   B . n 
C 1 145 GLU 145 127 ?   ?   ?   B . n 
C 1 146 GLN 146 128 ?   ?   ?   B . n 
D 1 1   MET 1   -17 ?   ?   ?   C . n 
D 1 2   GLY 2   -16 ?   ?   ?   C . n 
D 1 3   TRP 3   -15 ?   ?   ?   C . n 
D 1 4   HIS 4   -14 ?   ?   ?   C . n 
D 1 5   HIS 5   -13 ?   ?   ?   C . n 
D 1 6   HIS 6   -12 ?   ?   ?   C . n 
D 1 7   HIS 7   -11 ?   ?   ?   C . n 
D 1 8   HIS 8   -10 ?   ?   ?   C . n 
D 1 9   HIS 9   -9  ?   ?   ?   C . n 
D 1 10  GLU 10  -8  ?   ?   ?   C . n 
D 1 11  ASN 11  -7  ?   ?   ?   C . n 
D 1 12  LEU 12  -6  ?   ?   ?   C . n 
D 1 13  TYR 13  -5  ?   ?   ?   C . n 
D 1 14  PHE 14  -4  ?   ?   ?   C . n 
D 1 15  GLN 15  -3  ?   ?   ?   C . n 
D 1 16  GLY 16  -2  ?   ?   ?   C . n 
D 1 17  ALA 17  -1  ?   ?   ?   C . n 
D 1 18  SER 18  0   0   SER SER C . n 
D 1 19  MET 19  1   1   MET MET C . n 
D 1 20  LYS 20  2   2   LYS LYS C . n 
D 1 21  LEU 21  3   3   LEU LEU C . n 
D 1 22  VAL 22  4   4   VAL VAL C . n 
D 1 23  ILE 23  5   5   ILE ILE C . n 
D 1 24  ALA 24  6   6   ALA ALA C . n 
D 1 25  ARG 25  7   7   ARG ARG C . n 
D 1 26  VAL 26  8   8   VAL VAL C . n 
D 1 27  LYS 27  9   9   LYS LYS C . n 
D 1 28  SER 28  10  10  SER SER C . n 
D 1 29  PRO 29  11  11  PRO PRO C . n 
D 1 30  LYS 30  12  12  LYS LYS C . n 
D 1 31  VAL 31  13  13  VAL VAL C . n 
D 1 32  LYS 32  14  14  LYS LYS C . n 
D 1 33  ARG 33  15  15  ARG ARG C . n 
D 1 34  LEU 34  16  16  LEU LEU C . n 
D 1 35  SER 35  17  17  SER SER C . n 
D 1 36  GLU 36  18  18  GLU GLU C . n 
D 1 37  GLU 37  19  19  GLU GLU C . n 
D 1 38  ASP 38  20  20  ASP ASP C . n 
D 1 39  ILE 39  21  21  ILE ILE C . n 
D 1 40  GLU 40  22  22  GLU GLU C . n 
D 1 41  LYS 41  23  23  LYS LYS C . n 
D 1 42  ILE 42  24  24  ILE ILE C . n 
D 1 43  LYS 43  25  25  LYS LYS C . n 
D 1 44  SER 44  26  26  SER SER C . n 
D 1 45  ALA 45  27  27  ALA ALA C . n 
D 1 46  LEU 46  28  28  LEU LEU C . n 
D 1 47  LYS 47  29  29  LYS LYS C . n 
D 1 48  SER 48  30  30  SER SER C . n 
D 1 49  THR 49  31  31  THR THR C . n 
D 1 50  ASN 50  32  32  ASN ASN C . n 
D 1 51  LYS 51  33  33  LYS LYS C . n 
D 1 52  ALA 52  34  34  ALA ALA C . n 
D 1 53  VAL 53  35  35  VAL VAL C . n 
D 1 54  VAL 54  36  36  VAL VAL C . n 
D 1 55  THR 55  37  37  THR THR C . n 
D 1 56  ILE 56  38  38  ILE ILE C . n 
D 1 57  LYS 57  39  39  LYS LYS C . n 
D 1 58  ASP 58  40  40  ASP ASP C . n 
D 1 59  GLU 59  41  41  GLU GLU C . n 
D 1 60  ASN 60  42  42  ASN ASN C . n 
D 1 61  GLY 61  43  43  GLY GLY C . n 
D 1 62  GLU 62  44  44  GLU GLU C . n 
D 1 63  GLU 63  45  45  GLU GLU C . n 
D 1 64  ILE 64  46  46  ILE ILE C . n 
D 1 65  GLU 65  47  47  GLU GLU C . n 
D 1 66  VAL 66  48  48  VAL VAL C . n 
D 1 67  GLU 67  49  49  GLU GLU C . n 
D 1 68  VAL 68  50  50  VAL VAL C . n 
D 1 69  ARG 69  51  51  ARG ARG C . n 
D 1 70  LEU 70  52  52  LEU LEU C . n 
D 1 71  LEU 71  53  53  LEU LEU C . n 
D 1 72  THR 72  54  54  THR THR C . n 
D 1 73  LEU 73  55  55  LEU LEU C . n 
D 1 74  GLU 74  56  56  GLU GLU C . n 
D 1 75  GLU 75  57  57  GLU GLU C . n 
D 1 76  ALA 76  58  58  ALA ALA C . n 
D 1 77  LEU 77  59  59  LEU LEU C . n 
D 1 78  LYS 78  60  60  LYS LYS C . n 
D 1 79  TYR 79  61  61  TYR TYR C . n 
D 1 80  ILE 80  62  62  ILE ILE C . n 
D 1 81  ASN 81  63  63  ASN ASN C . n 
D 1 82  ASP 82  64  64  ASP ASP C . n 
D 1 83  LEU 83  65  65  LEU LEU C . n 
D 1 84  PRO 84  66  66  PRO PRO C . n 
D 1 85  ILE 85  67  67  ILE ILE C . n 
D 1 86  SER 86  68  68  SER SER C . n 
D 1 87  ASN 87  69  69  ASN ASN C . n 
D 1 88  ASP 88  70  70  ASP ASP C . n 
D 1 89  ALA 89  71  71  ALA ALA C . n 
D 1 90  LYS 90  72  72  LYS LYS C . n 
D 1 91  LYS 91  73  73  LYS LYS C . n 
D 1 92  LEU 92  74  74  LEU LEU C . n 
D 1 93  MET 93  75  75  MET MET C . n 
D 1 94  SER 94  76  76  SER SER C . n 
D 1 95  ASN 95  77  77  ASN ASN C . n 
D 1 96  ASN 96  78  78  ASN ASN C . n 
D 1 97  ILE 97  79  79  ILE ILE C . n 
D 1 98  HIS 98  80  80  HIS HIS C . n 
D 1 99  LYS 99  81  81  LYS LYS C . n 
D 1 100 ALA 100 82  82  ALA ALA C . n 
D 1 101 LEU 101 83  83  LEU LEU C . n 
D 1 102 GLU 102 84  84  GLU GLU C . n 
D 1 103 PRO 103 85  85  PRO PRO C . n 
D 1 104 GLY 104 86  86  GLY GLY C . n 
D 1 105 ARG 105 87  87  ARG ARG C . n 
D 1 106 THR 106 88  88  THR THR C . n 
D 1 107 VAL 107 89  89  VAL VAL C . n 
D 1 108 VAL 108 90  90  VAL VAL C . n 
D 1 109 PHE 109 91  91  PHE PHE C . n 
D 1 110 GLY 110 92  92  GLY GLY C . n 
D 1 111 PRO 111 93  93  PRO PRO C . n 
D 1 112 GLU 112 94  94  GLU GLU C . n 
D 1 113 GLY 113 95  95  GLY GLY C . n 
D 1 114 CYS 114 96  96  CYS CYS C . n 
D 1 115 GLU 115 97  97  GLU GLU C . n 
D 1 116 GLU 116 98  98  GLU GLU C . n 
D 1 117 ARG 117 99  99  ARG ARG C . n 
D 1 118 ASP 118 100 100 ASP ASP C . n 
D 1 119 LYS 119 101 101 LYS LYS C . n 
D 1 120 ASN 120 102 102 ASN ASN C . n 
D 1 121 ARG 121 103 103 ARG ARG C . n 
D 1 122 GLY 122 104 104 GLY GLY C . n 
D 1 123 ILE 123 105 105 ILE ILE C . n 
D 1 124 ILE 124 106 106 ILE ILE C . n 
D 1 125 LYS 125 107 107 LYS LYS C . n 
D 1 126 THR 126 108 108 THR THR C . n 
D 1 127 PHE 127 109 109 PHE PHE C . n 
D 1 128 SER 128 110 110 SER SER C . n 
D 1 129 THR 129 111 111 THR THR C . n 
D 1 130 ASP 130 112 112 ASP ASP C . n 
D 1 131 VAL 131 113 113 VAL VAL C . n 
D 1 132 LYS 132 114 114 LYS LYS C . n 
D 1 133 LEU 133 115 115 LEU LEU C . n 
D 1 134 ASP 134 116 116 ASP ASP C . n 
D 1 135 GLU 135 117 117 GLU GLU C . n 
D 1 136 THR 136 118 118 THR THR C . n 
D 1 137 TYR 137 119 119 TYR TYR C . n 
D 1 138 PHE 138 120 120 PHE PHE C . n 
D 1 139 PHE 139 121 121 PHE PHE C . n 
D 1 140 PHE 140 122 122 PHE PHE C . n 
D 1 141 ARG 141 123 123 ARG ARG C . n 
D 1 142 VAL 142 124 124 VAL VAL C . n 
D 1 143 GLU 143 125 ?   ?   ?   C . n 
D 1 144 ALA 144 126 ?   ?   ?   C . n 
D 1 145 GLU 145 127 ?   ?   ?   C . n 
D 1 146 GLN 146 128 ?   ?   ?   C . n 
# 
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 
E 2 HOH 1  201 1  HOH HOH D . 
E 2 HOH 2  202 68 HOH HOH D . 
E 2 HOH 3  203 54 HOH HOH D . 
E 2 HOH 4  204 34 HOH HOH D . 
E 2 HOH 5  205 72 HOH HOH D . 
E 2 HOH 6  206 5  HOH HOH D . 
E 2 HOH 7  207 71 HOH HOH D . 
E 2 HOH 8  208 19 HOH HOH D . 
E 2 HOH 9  209 58 HOH HOH D . 
E 2 HOH 10 210 67 HOH HOH D . 
E 2 HOH 11 211 52 HOH HOH D . 
E 2 HOH 12 212 73 HOH HOH D . 
E 2 HOH 13 213 69 HOH HOH D . 
E 2 HOH 14 214 41 HOH HOH D . 
E 2 HOH 15 215 12 HOH HOH D . 
E 2 HOH 16 216 63 HOH HOH D . 
E 2 HOH 17 217 64 HOH HOH D . 
E 2 HOH 18 218 18 HOH HOH D . 
E 2 HOH 19 219 65 HOH HOH D . 
F 2 HOH 1  201 3  HOH HOH A . 
F 2 HOH 2  202 37 HOH HOH A . 
F 2 HOH 3  203 33 HOH HOH A . 
F 2 HOH 4  204 6  HOH HOH A . 
F 2 HOH 5  205 32 HOH HOH A . 
F 2 HOH 6  206 24 HOH HOH A . 
F 2 HOH 7  207 28 HOH HOH A . 
F 2 HOH 8  208 11 HOH HOH A . 
F 2 HOH 9  209 17 HOH HOH A . 
F 2 HOH 10 210 4  HOH HOH A . 
F 2 HOH 11 211 39 HOH HOH A . 
F 2 HOH 12 212 74 HOH HOH A . 
F 2 HOH 13 213 76 HOH HOH A . 
G 2 HOH 1  201 13 HOH HOH B . 
G 2 HOH 2  202 38 HOH HOH B . 
G 2 HOH 3  203 7  HOH HOH B . 
G 2 HOH 4  204 26 HOH HOH B . 
G 2 HOH 5  205 21 HOH HOH B . 
G 2 HOH 6  206 57 HOH HOH B . 
G 2 HOH 7  207 31 HOH HOH B . 
G 2 HOH 8  208 29 HOH HOH B . 
G 2 HOH 9  209 77 HOH HOH B . 
G 2 HOH 10 210 66 HOH HOH B . 
G 2 HOH 11 211 46 HOH HOH B . 
G 2 HOH 12 212 16 HOH HOH B . 
G 2 HOH 13 213 44 HOH HOH B . 
G 2 HOH 14 214 61 HOH HOH B . 
G 2 HOH 15 215 45 HOH HOH B . 
G 2 HOH 16 216 48 HOH HOH B . 
H 2 HOH 1  201 23 HOH HOH C . 
H 2 HOH 2  202 8  HOH HOH C . 
H 2 HOH 3  203 25 HOH HOH C . 
H 2 HOH 4  204 53 HOH HOH C . 
H 2 HOH 5  205 62 HOH HOH C . 
H 2 HOH 6  206 42 HOH HOH C . 
H 2 HOH 7  207 35 HOH HOH C . 
H 2 HOH 8  208 22 HOH HOH C . 
H 2 HOH 9  209 15 HOH HOH C . 
H 2 HOH 10 210 27 HOH HOH C . 
H 2 HOH 11 211 30 HOH HOH C . 
H 2 HOH 12 212 75 HOH HOH C . 
H 2 HOH 13 213 10 HOH HOH C . 
H 2 HOH 14 214 59 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 D MET 1   ? CE  ? A MET 19  CE  
2   1 Y 1 D LYS 12  ? CG  ? A LYS 30  CG  
3   1 Y 1 D LYS 12  ? CD  ? A LYS 30  CD  
4   1 Y 1 D LYS 12  ? CE  ? A LYS 30  CE  
5   1 Y 1 D LYS 12  ? NZ  ? A LYS 30  NZ  
6   1 Y 1 D LYS 25  ? CE  ? A LYS 43  CE  
7   1 Y 1 D LYS 25  ? NZ  ? A LYS 43  NZ  
8   1 Y 1 D LYS 29  ? CG  ? A LYS 47  CG  
9   1 Y 1 D LYS 29  ? CD  ? A LYS 47  CD  
10  1 Y 1 D LYS 29  ? CE  ? A LYS 47  CE  
11  1 Y 1 D LYS 29  ? NZ  ? A LYS 47  NZ  
12  1 Y 1 D LYS 33  ? CE  ? A LYS 51  CE  
13  1 Y 1 D LYS 33  ? NZ  ? A LYS 51  NZ  
14  1 Y 1 D LYS 39  ? CG  ? A LYS 57  CG  
15  1 Y 1 D LYS 39  ? CD  ? A LYS 57  CD  
16  1 Y 1 D LYS 39  ? CE  ? A LYS 57  CE  
17  1 Y 1 D LYS 39  ? NZ  ? A LYS 57  NZ  
18  1 Y 1 D GLU 41  ? CG  ? A GLU 59  CG  
19  1 Y 1 D GLU 41  ? CD  ? A GLU 59  CD  
20  1 Y 1 D GLU 41  ? OE1 ? A GLU 59  OE1 
21  1 Y 1 D GLU 41  ? OE2 ? A GLU 59  OE2 
22  1 Y 1 D ASN 42  ? CG  ? A ASN 60  CG  
23  1 Y 1 D ASN 42  ? OD1 ? A ASN 60  OD1 
24  1 Y 1 D ASN 42  ? ND2 ? A ASN 60  ND2 
25  1 Y 1 D GLU 44  ? CG  ? A GLU 62  CG  
26  1 Y 1 D GLU 44  ? CD  ? A GLU 62  CD  
27  1 Y 1 D GLU 44  ? OE1 ? A GLU 62  OE1 
28  1 Y 1 D GLU 44  ? OE2 ? A GLU 62  OE2 
29  1 Y 1 D LYS 73  ? CD  ? A LYS 91  CD  
30  1 Y 1 D LYS 73  ? CE  ? A LYS 91  CE  
31  1 Y 1 D LYS 73  ? NZ  ? A LYS 91  NZ  
32  1 Y 1 D GLU 84  ? CD  ? A GLU 102 CD  
33  1 Y 1 D GLU 84  ? OE1 ? A GLU 102 OE1 
34  1 Y 1 D GLU 84  ? OE2 ? A GLU 102 OE2 
35  1 Y 1 D GLU 94  ? CD  ? A GLU 112 CD  
36  1 Y 1 D GLU 94  ? OE1 ? A GLU 112 OE1 
37  1 Y 1 D GLU 94  ? OE2 ? A GLU 112 OE2 
38  1 Y 1 D ILE 105 ? CG1 ? A ILE 123 CG1 
39  1 Y 1 D ILE 105 ? CG2 ? A ILE 123 CG2 
40  1 Y 1 D ILE 105 ? CD1 ? A ILE 123 CD1 
41  1 Y 1 D ILE 106 ? CG1 ? A ILE 124 CG1 
42  1 Y 1 D ILE 106 ? CG2 ? A ILE 124 CG2 
43  1 Y 1 D ILE 106 ? CD1 ? A ILE 124 CD1 
44  1 Y 1 D PHE 109 ? CG  ? A PHE 127 CG  
45  1 Y 1 D PHE 109 ? CD1 ? A PHE 127 CD1 
46  1 Y 1 D PHE 109 ? CD2 ? A PHE 127 CD2 
47  1 Y 1 D PHE 109 ? CE1 ? A PHE 127 CE1 
48  1 Y 1 D PHE 109 ? CE2 ? A PHE 127 CE2 
49  1 Y 1 D PHE 109 ? CZ  ? A PHE 127 CZ  
50  1 Y 1 A MET 1   ? CE  ? B MET 19  CE  
51  1 Y 1 A LYS 12  ? CG  ? B LYS 30  CG  
52  1 Y 1 A LYS 12  ? CD  ? B LYS 30  CD  
53  1 Y 1 A LYS 12  ? CE  ? B LYS 30  CE  
54  1 Y 1 A LYS 12  ? NZ  ? B LYS 30  NZ  
55  1 Y 1 A LYS 14  ? CE  ? B LYS 32  CE  
56  1 Y 1 A LYS 14  ? NZ  ? B LYS 32  NZ  
57  1 Y 1 A ARG 15  ? CG  ? B ARG 33  CG  
58  1 Y 1 A ARG 15  ? CD  ? B ARG 33  CD  
59  1 Y 1 A ARG 15  ? NE  ? B ARG 33  NE  
60  1 Y 1 A ARG 15  ? CZ  ? B ARG 33  CZ  
61  1 Y 1 A ARG 15  ? NH1 ? B ARG 33  NH1 
62  1 Y 1 A ARG 15  ? NH2 ? B ARG 33  NH2 
63  1 Y 1 A GLU 18  ? CG  ? B GLU 36  CG  
64  1 Y 1 A GLU 18  ? CD  ? B GLU 36  CD  
65  1 Y 1 A GLU 18  ? OE1 ? B GLU 36  OE1 
66  1 Y 1 A GLU 18  ? OE2 ? B GLU 36  OE2 
67  1 Y 1 A LYS 25  ? CE  ? B LYS 43  CE  
68  1 Y 1 A LYS 25  ? NZ  ? B LYS 43  NZ  
69  1 Y 1 A LYS 29  ? CD  ? B LYS 47  CD  
70  1 Y 1 A LYS 29  ? CE  ? B LYS 47  CE  
71  1 Y 1 A LYS 29  ? NZ  ? B LYS 47  NZ  
72  1 Y 1 A LYS 39  ? CG  ? B LYS 57  CG  
73  1 Y 1 A LYS 39  ? CD  ? B LYS 57  CD  
74  1 Y 1 A LYS 39  ? CE  ? B LYS 57  CE  
75  1 Y 1 A LYS 39  ? NZ  ? B LYS 57  NZ  
76  1 Y 1 A GLU 44  ? CG  ? B GLU 62  CG  
77  1 Y 1 A GLU 44  ? CD  ? B GLU 62  CD  
78  1 Y 1 A GLU 44  ? OE1 ? B GLU 62  OE1 
79  1 Y 1 A GLU 44  ? OE2 ? B GLU 62  OE2 
80  1 Y 1 A GLU 45  ? CG  ? B GLU 63  CG  
81  1 Y 1 A GLU 45  ? CD  ? B GLU 63  CD  
82  1 Y 1 A GLU 45  ? OE1 ? B GLU 63  OE1 
83  1 Y 1 A GLU 45  ? OE2 ? B GLU 63  OE2 
84  1 Y 1 A LYS 73  ? CD  ? B LYS 91  CD  
85  1 Y 1 A LYS 73  ? CE  ? B LYS 91  CE  
86  1 Y 1 A LYS 73  ? NZ  ? B LYS 91  NZ  
87  1 Y 1 A GLU 84  ? CD  ? B GLU 102 CD  
88  1 Y 1 A GLU 84  ? OE1 ? B GLU 102 OE1 
89  1 Y 1 A GLU 84  ? OE2 ? B GLU 102 OE2 
90  1 Y 1 A GLU 94  ? CD  ? B GLU 112 CD  
91  1 Y 1 A GLU 94  ? OE1 ? B GLU 112 OE1 
92  1 Y 1 A GLU 94  ? OE2 ? B GLU 112 OE2 
93  1 Y 1 A LYS 101 ? CG  ? B LYS 119 CG  
94  1 Y 1 A LYS 101 ? CD  ? B LYS 119 CD  
95  1 Y 1 A LYS 101 ? CE  ? B LYS 119 CE  
96  1 Y 1 A LYS 101 ? NZ  ? B LYS 119 NZ  
97  1 Y 1 A ARG 103 ? CG  ? B ARG 121 CG  
98  1 Y 1 A ARG 103 ? CD  ? B ARG 121 CD  
99  1 Y 1 A ARG 103 ? NE  ? B ARG 121 NE  
100 1 Y 1 A ARG 103 ? CZ  ? B ARG 121 CZ  
101 1 Y 1 A ARG 103 ? NH1 ? B ARG 121 NH1 
102 1 Y 1 A ARG 103 ? NH2 ? B ARG 121 NH2 
103 1 Y 1 A LYS 107 ? NZ  ? B LYS 125 NZ  
104 1 Y 1 A LYS 114 ? CG  ? B LYS 132 CG  
105 1 Y 1 A LYS 114 ? CD  ? B LYS 132 CD  
106 1 Y 1 A LYS 114 ? CE  ? B LYS 132 CE  
107 1 Y 1 A LYS 114 ? NZ  ? B LYS 132 NZ  
108 1 Y 1 B MET 1   ? CE  ? C MET 19  CE  
109 1 Y 1 B LYS 12  ? CG  ? C LYS 30  CG  
110 1 Y 1 B LYS 12  ? CD  ? C LYS 30  CD  
111 1 Y 1 B LYS 12  ? CE  ? C LYS 30  CE  
112 1 Y 1 B LYS 12  ? NZ  ? C LYS 30  NZ  
113 1 Y 1 B VAL 13  ? CG1 ? C VAL 31  CG1 
114 1 Y 1 B VAL 13  ? CG2 ? C VAL 31  CG2 
115 1 Y 1 B LYS 14  ? CG  ? C LYS 32  CG  
116 1 Y 1 B LYS 14  ? CD  ? C LYS 32  CD  
117 1 Y 1 B LYS 14  ? CE  ? C LYS 32  CE  
118 1 Y 1 B LYS 14  ? NZ  ? C LYS 32  NZ  
119 1 Y 1 B ARG 15  ? CG  ? C ARG 33  CG  
120 1 Y 1 B ARG 15  ? CD  ? C ARG 33  CD  
121 1 Y 1 B ARG 15  ? NE  ? C ARG 33  NE  
122 1 Y 1 B ARG 15  ? CZ  ? C ARG 33  CZ  
123 1 Y 1 B ARG 15  ? NH1 ? C ARG 33  NH1 
124 1 Y 1 B ARG 15  ? NH2 ? C ARG 33  NH2 
125 1 Y 1 B GLU 18  ? CG  ? C GLU 36  CG  
126 1 Y 1 B GLU 18  ? CD  ? C GLU 36  CD  
127 1 Y 1 B GLU 18  ? OE1 ? C GLU 36  OE1 
128 1 Y 1 B GLU 18  ? OE2 ? C GLU 36  OE2 
129 1 Y 1 B ASP 20  ? CG  ? C ASP 38  CG  
130 1 Y 1 B ASP 20  ? OD1 ? C ASP 38  OD1 
131 1 Y 1 B ASP 20  ? OD2 ? C ASP 38  OD2 
132 1 Y 1 B LYS 23  ? CE  ? C LYS 41  CE  
133 1 Y 1 B LYS 23  ? NZ  ? C LYS 41  NZ  
134 1 Y 1 B LYS 25  ? CG  ? C LYS 43  CG  
135 1 Y 1 B LYS 25  ? CD  ? C LYS 43  CD  
136 1 Y 1 B LYS 25  ? CE  ? C LYS 43  CE  
137 1 Y 1 B LYS 25  ? NZ  ? C LYS 43  NZ  
138 1 Y 1 B LYS 29  ? CG  ? C LYS 47  CG  
139 1 Y 1 B LYS 29  ? CD  ? C LYS 47  CD  
140 1 Y 1 B LYS 29  ? CE  ? C LYS 47  CE  
141 1 Y 1 B LYS 29  ? NZ  ? C LYS 47  NZ  
142 1 Y 1 B LYS 39  ? CG  ? C LYS 57  CG  
143 1 Y 1 B LYS 39  ? CD  ? C LYS 57  CD  
144 1 Y 1 B LYS 39  ? CE  ? C LYS 57  CE  
145 1 Y 1 B LYS 39  ? NZ  ? C LYS 57  NZ  
146 1 Y 1 B ASP 40  ? CG  ? C ASP 58  CG  
147 1 Y 1 B ASP 40  ? OD1 ? C ASP 58  OD1 
148 1 Y 1 B ASP 40  ? OD2 ? C ASP 58  OD2 
149 1 Y 1 B GLU 41  ? CG  ? C GLU 59  CG  
150 1 Y 1 B GLU 41  ? CD  ? C GLU 59  CD  
151 1 Y 1 B GLU 41  ? OE1 ? C GLU 59  OE1 
152 1 Y 1 B GLU 41  ? OE2 ? C GLU 59  OE2 
153 1 Y 1 B ASN 42  ? CG  ? C ASN 60  CG  
154 1 Y 1 B ASN 42  ? OD1 ? C ASN 60  OD1 
155 1 Y 1 B ASN 42  ? ND2 ? C ASN 60  ND2 
156 1 Y 1 B ILE 46  ? CD1 ? C ILE 64  CD1 
157 1 Y 1 B GLU 47  ? CG  ? C GLU 65  CG  
158 1 Y 1 B GLU 47  ? CD  ? C GLU 65  CD  
159 1 Y 1 B GLU 47  ? OE1 ? C GLU 65  OE1 
160 1 Y 1 B GLU 47  ? OE2 ? C GLU 65  OE2 
161 1 Y 1 B VAL 48  ? CG1 ? C VAL 66  CG1 
162 1 Y 1 B VAL 48  ? CG2 ? C VAL 66  CG2 
163 1 Y 1 B GLU 94  ? CG  ? C GLU 112 CG  
164 1 Y 1 B GLU 94  ? CD  ? C GLU 112 CD  
165 1 Y 1 B GLU 94  ? OE1 ? C GLU 112 OE1 
166 1 Y 1 B GLU 94  ? OE2 ? C GLU 112 OE2 
167 1 Y 1 B LYS 101 ? CD  ? C LYS 119 CD  
168 1 Y 1 B LYS 101 ? CE  ? C LYS 119 CE  
169 1 Y 1 B LYS 101 ? NZ  ? C LYS 119 NZ  
170 1 Y 1 B ILE 105 ? CD1 ? C ILE 123 CD1 
171 1 Y 1 B PHE 109 ? CD1 ? C PHE 127 CD1 
172 1 Y 1 B PHE 109 ? CD2 ? C PHE 127 CD2 
173 1 Y 1 B PHE 109 ? CE1 ? C PHE 127 CE1 
174 1 Y 1 B PHE 109 ? CE2 ? C PHE 127 CE2 
175 1 Y 1 B PHE 109 ? CZ  ? C PHE 127 CZ  
176 1 Y 1 B ASP 112 ? CG  ? C ASP 130 CG  
177 1 Y 1 B ASP 112 ? OD1 ? C ASP 130 OD1 
178 1 Y 1 B ASP 112 ? OD2 ? C ASP 130 OD2 
179 1 Y 1 C MET 1   ? CE  ? D MET 19  CE  
180 1 Y 1 C LYS 12  ? CG  ? D LYS 30  CG  
181 1 Y 1 C LYS 12  ? CD  ? D LYS 30  CD  
182 1 Y 1 C LYS 12  ? CE  ? D LYS 30  CE  
183 1 Y 1 C LYS 12  ? NZ  ? D LYS 30  NZ  
184 1 Y 1 C LYS 14  ? CG  ? D LYS 32  CG  
185 1 Y 1 C LYS 14  ? CD  ? D LYS 32  CD  
186 1 Y 1 C LYS 14  ? CE  ? D LYS 32  CE  
187 1 Y 1 C LYS 14  ? NZ  ? D LYS 32  NZ  
188 1 Y 1 C ARG 15  ? CG  ? D ARG 33  CG  
189 1 Y 1 C ARG 15  ? CD  ? D ARG 33  CD  
190 1 Y 1 C ARG 15  ? NE  ? D ARG 33  NE  
191 1 Y 1 C ARG 15  ? CZ  ? D ARG 33  CZ  
192 1 Y 1 C ARG 15  ? NH1 ? D ARG 33  NH1 
193 1 Y 1 C ARG 15  ? NH2 ? D ARG 33  NH2 
194 1 Y 1 C GLU 18  ? CG  ? D GLU 36  CG  
195 1 Y 1 C GLU 18  ? CD  ? D GLU 36  CD  
196 1 Y 1 C GLU 18  ? OE1 ? D GLU 36  OE1 
197 1 Y 1 C GLU 18  ? OE2 ? D GLU 36  OE2 
198 1 Y 1 C GLU 19  ? CG  ? D GLU 37  CG  
199 1 Y 1 C GLU 19  ? CD  ? D GLU 37  CD  
200 1 Y 1 C GLU 19  ? OE1 ? D GLU 37  OE1 
201 1 Y 1 C GLU 19  ? OE2 ? D GLU 37  OE2 
202 1 Y 1 C LYS 23  ? CD  ? D LYS 41  CD  
203 1 Y 1 C LYS 23  ? CE  ? D LYS 41  CE  
204 1 Y 1 C LYS 23  ? NZ  ? D LYS 41  NZ  
205 1 Y 1 C LYS 25  ? CD  ? D LYS 43  CD  
206 1 Y 1 C LYS 25  ? CE  ? D LYS 43  CE  
207 1 Y 1 C LYS 25  ? NZ  ? D LYS 43  NZ  
208 1 Y 1 C LYS 29  ? CG  ? D LYS 47  CG  
209 1 Y 1 C LYS 29  ? CD  ? D LYS 47  CD  
210 1 Y 1 C LYS 29  ? CE  ? D LYS 47  CE  
211 1 Y 1 C LYS 29  ? NZ  ? D LYS 47  NZ  
212 1 Y 1 C LYS 39  ? CG  ? D LYS 57  CG  
213 1 Y 1 C LYS 39  ? CD  ? D LYS 57  CD  
214 1 Y 1 C LYS 39  ? CE  ? D LYS 57  CE  
215 1 Y 1 C LYS 39  ? NZ  ? D LYS 57  NZ  
216 1 Y 1 C ASP 40  ? CG  ? D ASP 58  CG  
217 1 Y 1 C ASP 40  ? OD1 ? D ASP 58  OD1 
218 1 Y 1 C ASP 40  ? OD2 ? D ASP 58  OD2 
219 1 Y 1 C GLU 41  ? CG  ? D GLU 59  CG  
220 1 Y 1 C GLU 41  ? CD  ? D GLU 59  CD  
221 1 Y 1 C GLU 41  ? OE1 ? D GLU 59  OE1 
222 1 Y 1 C GLU 41  ? OE2 ? D GLU 59  OE2 
223 1 Y 1 C ASN 42  ? CG  ? D ASN 60  CG  
224 1 Y 1 C ASN 42  ? OD1 ? D ASN 60  OD1 
225 1 Y 1 C ASN 42  ? ND2 ? D ASN 60  ND2 
226 1 Y 1 C GLU 94  ? CD  ? D GLU 112 CD  
227 1 Y 1 C GLU 94  ? OE1 ? D GLU 112 OE1 
228 1 Y 1 C GLU 94  ? OE2 ? D GLU 112 OE2 
229 1 Y 1 C LYS 101 ? CG  ? D LYS 119 CG  
230 1 Y 1 C LYS 101 ? CD  ? D LYS 119 CD  
231 1 Y 1 C LYS 101 ? CE  ? D LYS 119 CE  
232 1 Y 1 C LYS 101 ? NZ  ? D LYS 119 NZ  
233 1 Y 1 C ILE 105 ? CG1 ? D ILE 123 CG1 
234 1 Y 1 C ILE 105 ? CG2 ? D ILE 123 CG2 
235 1 Y 1 C ILE 105 ? CD1 ? D ILE 123 CD1 
236 1 Y 1 C LYS 107 ? CG  ? D LYS 125 CG  
237 1 Y 1 C LYS 107 ? CD  ? D LYS 125 CD  
238 1 Y 1 C LYS 107 ? CE  ? D LYS 125 CE  
239 1 Y 1 C LYS 107 ? NZ  ? D LYS 125 NZ  
240 1 Y 1 C ASP 112 ? CG  ? D ASP 130 CG  
241 1 Y 1 C ASP 112 ? OD1 ? D ASP 130 OD1 
242 1 Y 1 C ASP 112 ? OD2 ? D ASP 130 OD2 
243 1 Y 1 C VAL 124 ? CG1 ? D VAL 142 CG1 
244 1 Y 1 C VAL 124 ? CG2 ? D VAL 142 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F8Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.843 
_cell.length_a_esd                 ? 
_cell.length_b                     106.432 
_cell.length_b_esd                 ? 
_cell.length_c                     113.589 
_cell.length_c_esd                 ? 
_cell.volume                       566308.657 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9F8Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F8Y 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.45 
_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              ? 
_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    '0.2 M calcium acetate, Tris pH 7.5, and 25 % (v/v) PEG 2000 MME' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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 PILATUS3 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         2023-06-17 
_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   0.96 
_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        0.96 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          54.11 
_reflns.entry_id                                       9F8Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.3 
_reflns.d_resolution_low                               77.67 
_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                                     135054 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.26 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.17 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.3 
_reflns_shell.d_res_low                                     2.382 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2558 
_reflns_shell.percent_possible_obs                          ? 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.77 
_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                                  0.77 
_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                               66.97 
_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                                 9F8Y 
_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                            2.30 
_refine.ls_d_res_low                             77.67 
_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                     25880 
_refine.ls_number_reflns_R_free                  1364 
_refine.ls_number_reflns_R_work                  24516 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.26 
_refine.ls_percent_reflns_R_free                 5.27 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2615 
_refine.ls_R_factor_R_free                       0.2834 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2603 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.2443 
_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                            0.3831 
_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.details                          ? 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        77.67 
_refine_hist.number_atoms_solvent             62 
_refine_hist.number_atoms_total               3747 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3685 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0086  ? 3724 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2024  ? 5033 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0804  ? 622  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0126  ? 640  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.0748 ? 1373 ? f_dihedral_angle_d ? ? 
# 
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' 2.30 2.38  . . 135 2416 99.96  . . . . 0.3444 . . . . . . . . . . . 0.3925 
'X-RAY DIFFRACTION' 2.38 2.48  . . 131 2448 100.00 . . . . 0.3381 . . . . . . . . . . . 0.3798 
'X-RAY DIFFRACTION' 2.48 2.59  . . 135 2427 99.96  . . . . 0.3419 . . . . . . . . . . . 0.3881 
'X-RAY DIFFRACTION' 2.59 2.72  . . 143 2414 99.65  . . . . 0.2993 . . . . . . . . . . . 0.3241 
'X-RAY DIFFRACTION' 2.72 2.90  . . 144 2429 99.88  . . . . 0.2966 . . . . . . . . . . . 0.3297 
'X-RAY DIFFRACTION' 2.90 3.12  . . 121 2466 99.92  . . . . 0.3064 . . . . . . . . . . . 0.2940 
'X-RAY DIFFRACTION' 3.12 3.43  . . 143 2372 98.24  . . . . 0.2801 . . . . . . . . . . . 0.3199 
'X-RAY DIFFRACTION' 3.44 3.93  . . 142 2406 98.26  . . . . 0.2500 . . . . . . . . . . . 0.3027 
'X-RAY DIFFRACTION' 3.93 4.95  . . 119 2505 99.73  . . . . 0.2121 . . . . . . . . . . . 0.2294 
'X-RAY DIFFRACTION' 4.95 77.67 . . 151 2633 99.50  . . . . 0.2439 . . . . . . . . . . . 0.2443 
# 
_struct.entry_id                     9F8Y 
_struct.title                        'Crystal structure of a designed three-motif Respiratory Syncytial Virus immunogen' 
_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        9F8Y 
_struct_keywords.text            'Designed immunogen, Specific Binding, RSV F protein, DE NOVO PROTEIN' 
_struct_keywords.pdbx_keywords   'DE NOVO 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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9F8Y 
_struct_ref.pdbx_db_accession          9F8Y 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
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 9F8Y D 1 ? 146 ? 9F8Y -17 ? 128 ? -17 128 
2 1 9F8Y A 1 ? 146 ? 9F8Y -17 ? 128 ? -17 128 
3 1 9F8Y B 1 ? 146 ? 9F8Y -17 ? 128 ? -17 128 
4 1 9F8Y C 1 ? 146 ? 9F8Y -17 ? 128 ? -17 128 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E 
2 1 B,F 
3 1 C,G 
4 1 D,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            2 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_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 SER A 35  ? LEU A 46  ? SER D 17  LEU D 28  1 ? 12 
HELX_P HELX_P2  AA2 LEU A 73  ? ASP A 82  ? LEU D 55  ASP D 64  1 ? 10 
HELX_P HELX_P3  AA3 SER A 86  ? ILE A 97  ? SER D 68  ILE D 79  1 ? 12 
HELX_P HELX_P4  AA4 HIS A 98  ? GLU A 102 ? HIS D 80  GLU D 84  5 ? 5  
HELX_P HELX_P5  AA5 SER B 35  ? LEU B 46  ? SER A 17  LEU A 28  1 ? 12 
HELX_P HELX_P6  AA6 LEU B 73  ? ASP B 82  ? LEU A 55  ASP A 64  1 ? 10 
HELX_P HELX_P7  AA7 SER B 86  ? ILE B 97  ? SER A 68  ILE A 79  1 ? 12 
HELX_P HELX_P8  AA8 HIS B 98  ? GLU B 102 ? HIS A 80  GLU A 84  5 ? 5  
HELX_P HELX_P9  AA9 SER C 35  ? LEU C 46  ? SER B 17  LEU B 28  1 ? 12 
HELX_P HELX_P10 AB1 LEU C 73  ? LEU C 83  ? LEU B 55  LEU B 65  1 ? 11 
HELX_P HELX_P11 AB2 SER C 86  ? ASN C 95  ? SER B 68  ASN B 77  1 ? 10 
HELX_P HELX_P12 AB3 ASN C 96  ? GLU C 102 ? ASN B 78  GLU B 84  5 ? 7  
HELX_P HELX_P13 AB4 SER D 35  ? LEU D 46  ? SER C 17  LEU C 28  1 ? 12 
HELX_P HELX_P14 AB5 GLU D 59  ? GLY D 61  ? GLU C 41  GLY C 43  5 ? 3  
HELX_P HELX_P15 AB6 LEU D 73  ? LEU D 83  ? LEU C 55  LEU C 65  1 ? 11 
HELX_P HELX_P16 AB7 SER D 86  ? ILE D 97  ? SER C 68  ILE C 79  1 ? 12 
HELX_P HELX_P17 AB8 HIS D 98  ? GLU D 102 ? HIS C 80  GLU C 84  5 ? 5  
HELX_P HELX_P18 AB9 ASN D 120 ? GLY D 122 ? ASN C 102 GLY C 104 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 14 ? 
AA2 ? 7  ? 
AA3 ? 7  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA1 12 13 ? anti-parallel 
AA1 13 14 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA3 5  6  ? anti-parallel 
AA3 6  7  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  LYS A 51  ? LYS A 57  ? LYS D 33  LYS D 39  
AA1 2  GLU A 63  ? THR A 72  ? GLU D 45  THR D 54  
AA1 3  LYS A 20  ? VAL A 26  ? LYS D 2   VAL D 8   
AA1 4  THR A 136 ? ARG A 141 ? THR D 118 ARG D 123 
AA1 5  ARG A 105 ? PHE A 109 ? ARG D 87  PHE D 91  
AA1 6  GLY A 113 ? ASP A 118 ? GLY D 95  ASP D 100 
AA1 7  LYS A 125 ? SER A 128 ? LYS D 107 SER D 110 
AA1 8  GLY B 122 ? PHE B 127 ? GLY A 104 PHE A 109 
AA1 9  CYS B 114 ? ASP B 118 ? CYS A 96  ASP A 100 
AA1 10 ARG B 105 ? PHE B 109 ? ARG A 87  PHE A 91  
AA1 11 THR B 136 ? ARG B 141 ? THR A 118 ARG A 123 
AA1 12 LYS B 20  ? VAL B 26  ? LYS A 2   VAL A 8   
AA1 13 GLU B 63  ? THR B 72  ? GLU A 45  THR A 54  
AA1 14 LYS B 51  ? LYS B 57  ? LYS A 33  LYS A 39  
AA2 1  LYS C 51  ? THR C 55  ? LYS B 33  THR B 37  
AA2 2  GLU C 65  ? THR C 72  ? GLU B 47  THR B 54  
AA2 3  LYS C 20  ? VAL C 26  ? LYS B 2   VAL B 8   
AA2 4  THR C 136 ? ARG C 141 ? THR B 118 ARG B 123 
AA2 5  ARG C 105 ? GLY C 110 ? ARG B 87  GLY B 92  
AA2 6  GLY C 113 ? ASP C 118 ? GLY B 95  ASP B 100 
AA2 7  ILE C 123 ? PHE C 127 ? ILE B 105 PHE B 109 
AA3 1  LYS D 51  ? LYS D 57  ? LYS C 33  LYS C 39  
AA3 2  GLU D 63  ? THR D 72  ? GLU C 45  THR C 54  
AA3 3  LYS D 20  ? VAL D 26  ? LYS C 2   VAL C 8   
AA3 4  THR D 136 ? ARG D 141 ? THR C 118 ARG C 123 
AA3 5  ARG D 105 ? GLY D 110 ? ARG C 87  GLY C 92  
AA3 6  GLY D 113 ? ASP D 118 ? GLY C 95  ASP C 100 
AA3 7  ILE D 123 ? SER D 128 ? ILE C 105 SER C 110 
# 
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 ILE A 56  ? N ILE D 38  O ILE A 64  ? O ILE D 46  
AA1 2  3  O LEU A 71  ? O LEU D 53  N LEU A 21  ? N LEU D 3   
AA1 3  4  N VAL A 26  ? N VAL D 8   O THR A 136 ? O THR D 118 
AA1 4  5  O TYR A 137 ? O TYR D 119 N PHE A 109 ? N PHE D 91  
AA1 5  6  N THR A 106 ? N THR D 88  O ARG A 117 ? O ARG D 99  
AA1 6  7  N GLU A 116 ? N GLU D 98  O LYS A 125 ? O LYS D 107 
AA1 7  8  N SER A 128 ? N SER D 110 O ILE B 124 ? O ILE A 106 
AA1 8  9  O GLY B 122 ? O GLY A 104 N ASP B 118 ? N ASP A 100 
AA1 9  10 O GLU B 115 ? O GLU A 97  N VAL B 108 ? N VAL A 90  
AA1 10 11 N PHE B 109 ? N PHE A 91  O TYR B 137 ? O TYR A 119 
AA1 11 12 O PHE B 140 ? O PHE A 122 N VAL B 22  ? N VAL A 4   
AA1 12 13 N LEU B 21  ? N LEU A 3   O LEU B 71  ? O LEU A 53  
AA1 13 14 O ILE B 64  ? O ILE A 46  N ILE B 56  ? N ILE A 38  
AA2 1  2  N ALA C 52  ? N ALA B 34  O VAL C 68  ? O VAL B 50  
AA2 2  3  O LEU C 71  ? O LEU B 53  N LEU C 21  ? N LEU B 3   
AA2 3  4  N VAL C 26  ? N VAL B 8   O THR C 136 ? O THR B 118 
AA2 4  5  O PHE C 139 ? O PHE B 121 N VAL C 107 ? N VAL B 89  
AA2 5  6  N THR C 106 ? N THR B 88  O ARG C 117 ? O ARG B 99  
AA2 6  7  N GLU C 116 ? N GLU B 98  O LYS C 125 ? O LYS B 107 
AA3 1  2  N ALA D 52  ? N ALA C 34  O VAL D 68  ? O VAL C 50  
AA3 2  3  O LEU D 71  ? O LEU C 53  N LEU D 21  ? N LEU C 3   
AA3 3  4  N VAL D 22  ? N VAL C 4   O PHE D 140 ? O PHE C 122 
AA3 4  5  O TYR D 137 ? O TYR C 119 N PHE D 109 ? N PHE C 91  
AA3 5  6  N THR D 106 ? N THR C 88  O ARG D 117 ? O ARG C 99  
AA3 6  7  N ASP D 118 ? N ASP C 100 O ILE D 123 ? O ILE C 105 
# 
_pdbx_entry_details.entry_id                   9F8Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE D 106 ? ? -134.35 -34.37  
2 1 ILE A 106 ? ? -124.81 -53.40  
3 1 LYS B 33  ? ? -164.52 116.97  
4 1 GLU B 41  ? ? 67.03   -28.75  
5 1 ARG B 103 ? ? -110.85 -154.33 
6 1 LYS B 114 ? ? 72.05   32.49   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 D MET -17 ? A MET 1   
2  1 Y 1 D GLY -16 ? A GLY 2   
3  1 Y 1 D TRP -15 ? A TRP 3   
4  1 Y 1 D HIS -14 ? A HIS 4   
5  1 Y 1 D HIS -13 ? A HIS 5   
6  1 Y 1 D HIS -12 ? A HIS 6   
7  1 Y 1 D HIS -11 ? A HIS 7   
8  1 Y 1 D HIS -10 ? A HIS 8   
9  1 Y 1 D HIS -9  ? A HIS 9   
10 1 Y 1 D GLU -8  ? A GLU 10  
11 1 Y 1 D ASN -7  ? A ASN 11  
12 1 Y 1 D LEU -6  ? A LEU 12  
13 1 Y 1 D TYR -5  ? A TYR 13  
14 1 Y 1 D PHE -4  ? A PHE 14  
15 1 Y 1 D GLN -3  ? A GLN 15  
16 1 Y 1 D GLY -2  ? A GLY 16  
17 1 Y 1 D ALA -1  ? A ALA 17  
18 1 Y 1 D SER 0   ? A SER 18  
19 1 Y 1 D ASN 102 ? A ASN 120 
20 1 Y 1 D ARG 103 ? A ARG 121 
21 1 Y 1 D GLU 125 ? A GLU 143 
22 1 Y 1 D ALA 126 ? A ALA 144 
23 1 Y 1 D GLU 127 ? A GLU 145 
24 1 Y 1 D GLN 128 ? A GLN 146 
25 1 Y 1 A MET -17 ? B MET 1   
26 1 Y 1 A GLY -16 ? B GLY 2   
27 1 Y 1 A TRP -15 ? B TRP 3   
28 1 Y 1 A HIS -14 ? B HIS 4   
29 1 Y 1 A HIS -13 ? B HIS 5   
30 1 Y 1 A HIS -12 ? B HIS 6   
31 1 Y 1 A HIS -11 ? B HIS 7   
32 1 Y 1 A HIS -10 ? B HIS 8   
33 1 Y 1 A HIS -9  ? B HIS 9   
34 1 Y 1 A GLU -8  ? B GLU 10  
35 1 Y 1 A ASN -7  ? B ASN 11  
36 1 Y 1 A LEU -6  ? B LEU 12  
37 1 Y 1 A TYR -5  ? B TYR 13  
38 1 Y 1 A PHE -4  ? B PHE 14  
39 1 Y 1 A GLN -3  ? B GLN 15  
40 1 Y 1 A GLY -2  ? B GLY 16  
41 1 Y 1 A ALA -1  ? B ALA 17  
42 1 Y 1 A SER 0   ? B SER 18  
43 1 Y 1 A ASN 42  ? B ASN 60  
44 1 Y 1 A GLY 43  ? B GLY 61  
45 1 Y 1 A GLU 125 ? B GLU 143 
46 1 Y 1 A ALA 126 ? B ALA 144 
47 1 Y 1 A GLU 127 ? B GLU 145 
48 1 Y 1 A GLN 128 ? B GLN 146 
49 1 Y 1 B MET -17 ? C MET 1   
50 1 Y 1 B GLY -16 ? C GLY 2   
51 1 Y 1 B TRP -15 ? C TRP 3   
52 1 Y 1 B HIS -14 ? C HIS 4   
53 1 Y 1 B HIS -13 ? C HIS 5   
54 1 Y 1 B HIS -12 ? C HIS 6   
55 1 Y 1 B HIS -11 ? C HIS 7   
56 1 Y 1 B HIS -10 ? C HIS 8   
57 1 Y 1 B HIS -9  ? C HIS 9   
58 1 Y 1 B GLU -8  ? C GLU 10  
59 1 Y 1 B ASN -7  ? C ASN 11  
60 1 Y 1 B LEU -6  ? C LEU 12  
61 1 Y 1 B TYR -5  ? C TYR 13  
62 1 Y 1 B PHE -4  ? C PHE 14  
63 1 Y 1 B GLN -3  ? C GLN 15  
64 1 Y 1 B GLY -2  ? C GLY 16  
65 1 Y 1 B ALA -1  ? C ALA 17  
66 1 Y 1 B SER 0   ? C SER 18  
67 1 Y 1 B GLU 44  ? C GLU 62  
68 1 Y 1 B GLU 45  ? C GLU 63  
69 1 Y 1 B GLU 125 ? C GLU 143 
70 1 Y 1 B ALA 126 ? C ALA 144 
71 1 Y 1 B GLU 127 ? C GLU 145 
72 1 Y 1 B GLN 128 ? C GLN 146 
73 1 Y 1 C MET -17 ? D MET 1   
74 1 Y 1 C GLY -16 ? D GLY 2   
75 1 Y 1 C TRP -15 ? D TRP 3   
76 1 Y 1 C HIS -14 ? D HIS 4   
77 1 Y 1 C HIS -13 ? D HIS 5   
78 1 Y 1 C HIS -12 ? D HIS 6   
79 1 Y 1 C HIS -11 ? D HIS 7   
80 1 Y 1 C HIS -10 ? D HIS 8   
81 1 Y 1 C HIS -9  ? D HIS 9   
82 1 Y 1 C GLU -8  ? D GLU 10  
83 1 Y 1 C ASN -7  ? D ASN 11  
84 1 Y 1 C LEU -6  ? D LEU 12  
85 1 Y 1 C TYR -5  ? D TYR 13  
86 1 Y 1 C PHE -4  ? D PHE 14  
87 1 Y 1 C GLN -3  ? D GLN 15  
88 1 Y 1 C GLY -2  ? D GLY 16  
89 1 Y 1 C ALA -1  ? D ALA 17  
90 1 Y 1 C GLU 125 ? D GLU 143 
91 1 Y 1 C ALA 126 ? D ALA 144 
92 1 Y 1 C GLU 127 ? D GLU 145 
93 1 Y 1 C GLN 128 ? D GLN 146 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland      ? 1 
'European Research Council (ERC)'   'European Union' ? 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9F8Y 
_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]   0.021348 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009396 
_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]   0.008804 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . MET A 1 19  ? -9.72400  20.80000 24.30700  1.000 106.58000 ? 1   MET D N   1 
ATOM   2    C CA  . MET A 1 19  ? -8.84800  21.74800 23.57300  1.000 89.52000  ? 1   MET D CA  1 
ATOM   3    C C   . MET A 1 19  ? -7.93600  20.94200 22.64800  1.000 84.43000  ? 1   MET D C   1 
ATOM   4    O O   . MET A 1 19  ? -7.13300  20.14900 23.15300  1.000 81.18000  ? 1   MET D O   1 
ATOM   5    C CB  . MET A 1 19  ? -8.00800  22.57600 24.54500  1.000 83.67000  ? 1   MET D CB  1 
ATOM   6    C CG  . MET A 1 19  ? -7.24600  23.69400 23.89000  1.000 86.44000  ? 1   MET D CG  1 
ATOM   7    S SD  . MET A 1 19  ? -6.50300  24.74200 25.15100  1.000 103.46000 ? 1   MET D SD  1 
ATOM   8    N N   . LYS A 1 20  ? -8.08100  21.13300 21.34500  1.000 57.03000  ? 2   LYS D N   1 
ATOM   9    C CA  . LYS A 1 20  ? -7.29100  20.35500 20.40300  1.000 66.04000  ? 2   LYS D CA  1 
ATOM   10   C C   . LYS A 1 20  ? -6.52200  21.26700 19.45800  1.000 58.95000  ? 2   LYS D C   1 
ATOM   11   O O   . LYS A 1 20  ? -6.98400  22.35400 19.09700  1.000 66.44000  ? 2   LYS D O   1 
ATOM   12   C CB  . LYS A 1 20  ? -8.16900  19.39600 19.58700  1.000 53.96000  ? 2   LYS D CB  1 
ATOM   13   C CG  . LYS A 1 20  ? -8.76200  18.25900 20.40000  1.000 66.11000  ? 2   LYS D CG  1 
ATOM   14   C CD  . LYS A 1 20  ? -9.30800  17.16300 19.50100  1.000 62.46000  ? 2   LYS D CD  1 
ATOM   15   C CE  . LYS A 1 20  ? -9.72500  15.94800 20.31400  1.000 50.05000  ? 2   LYS D CE  1 
ATOM   16   N NZ  . LYS A 1 20  ? -10.12700 14.80600 19.44700  1.000 78.94000  ? 2   LYS D NZ  1 
ATOM   17   N N   . LEU A 1 21  ? -5.34000  20.80700 19.05500  1.000 54.36000  ? 3   LEU D N   1 
ATOM   18   C CA  . LEU A 1 21  ? -4.49400  21.58900 18.12500  1.000 42.20000  ? 3   LEU D CA  1 
ATOM   19   C C   . LEU A 1 21  ? -4.44900  20.86100 16.78500  1.000 50.66000  ? 3   LEU D C   1 
ATOM   20   O O   . LEU A 1 21  ? -4.72500  19.64900 16.76000  1.000 41.89000  ? 3   LEU D O   1 
ATOM   21   C CB  . LEU A 1 21  ? -3.07700  21.66300 18.69500  1.000 51.69000  ? 3   LEU D CB  1 
ATOM   22   C CG  . LEU A 1 21  ? -2.85200  22.64700 19.83800  1.000 63.95000  ? 3   LEU D CG  1 
ATOM   23   C CD1 . LEU A 1 21  ? -1.44200  22.49900 20.38800  1.000 61.00000  ? 3   LEU D CD1 1 
ATOM   24   C CD2 . LEU A 1 21  ? -3.08000  24.06900 19.36200  1.000 68.03000  ? 3   LEU D CD2 1 
ATOM   25   N N   . VAL A 1 22  ? -4.10600  21.58000 15.72000  1.000 52.46000  ? 4   VAL D N   1 
ATOM   26   C CA  . VAL A 1 22  ? -3.91500  20.90400 14.40900  1.000 48.13000  ? 4   VAL D CA  1 
ATOM   27   C C   . VAL A 1 22  ? -2.41200  20.89800 14.13600  1.000 52.92000  ? 4   VAL D C   1 
ATOM   28   O O   . VAL A 1 22  ? -1.79000  21.96800 14.25800  1.000 41.58000  ? 4   VAL D O   1 
ATOM   29   C CB  . VAL A 1 22  ? -4.69300  21.59300 13.27600  1.000 56.59000  ? 4   VAL D CB  1 
ATOM   30   C CG1 . VAL A 1 22  ? -4.45200  20.90700 11.94100  1.000 52.48000  ? 4   VAL D CG1 1 
ATOM   31   C CG2 . VAL A 1 22  ? -6.18000  21.67100 13.57800  1.000 58.46000  ? 4   VAL D CG2 1 
ATOM   32   N N   . ILE A 1 23  ? -1.85100  19.72800 13.83600  1.000 40.87000  ? 5   ILE D N   1 
ATOM   33   C CA  . ILE A 1 23  ? -0.41100  19.66500 13.46300  1.000 41.66000  ? 5   ILE D CA  1 
ATOM   34   C C   . ILE A 1 23  ? -0.32800  19.39100 11.95900  1.000 50.53000  ? 5   ILE D C   1 
ATOM   35   O O   . ILE A 1 23  ? -0.75500  18.30800 11.53500  1.000 44.75000  ? 5   ILE D O   1 
ATOM   36   C CB  . ILE A 1 23  ? 0.35200   18.62100 14.30000  1.000 61.67000  ? 5   ILE D CB  1 
ATOM   37   C CG1 . ILE A 1 23  ? 0.01100   18.71600 15.78900  1.000 54.72000  ? 5   ILE D CG1 1 
ATOM   38   C CG2 . ILE A 1 23  ? 1.84700   18.73700 14.05400  1.000 48.16000  ? 5   ILE D CG2 1 
ATOM   39   C CD1 . ILE A 1 23  ? 0.48700   19.98700 16.44900  1.000 72.07000  ? 5   ILE D CD1 1 
ATOM   40   N N   . ALA A 1 24  ? 0.18900   20.35100 11.19500  1.000 41.57000  ? 6   ALA D N   1 
ATOM   41   C CA  . ALA A 1 24  ? 0.31700   20.21800 9.74900   1.000 48.66000  ? 6   ALA D CA  1 
ATOM   42   C C   . ALA A 1 24  ? 1.79100   20.02800 9.41100   1.000 53.78000  ? 6   ALA D C   1 
ATOM   43   O O   . ALA A 1 24  ? 2.58400   20.97000 9.51500   1.000 47.96000  ? 6   ALA D O   1 
ATOM   44   C CB  . ALA A 1 24  ? -0.26100  21.43700 9.03400   1.000 43.11000  ? 6   ALA D CB  1 
ATOM   45   N N   . ARG A 1 25  ? 2.15900   18.79900 9.03600   1.000 55.40000  ? 7   ARG D N   1 
ATOM   46   C CA  . ARG A 1 25  ? 3.54700   18.48900 8.61200   1.000 42.63000  ? 7   ARG D CA  1 
ATOM   47   C C   . ARG A 1 25  ? 3.61300   18.59600 7.09300   1.000 46.05000  ? 7   ARG D C   1 
ATOM   48   O O   . ARG A 1 25  ? 3.12400   17.70200 6.40400   1.000 45.44000  ? 7   ARG D O   1 
ATOM   49   C CB  . ARG A 1 25  ? 4.00100   17.10700 9.08500   1.000 46.57000  ? 7   ARG D CB  1 
ATOM   50   C CG  . ARG A 1 25  ? 5.35400   16.64900 8.56400   1.000 37.09000  ? 7   ARG D CG  1 
ATOM   51   C CD  . ARG A 1 25  ? 5.57100   15.20700 8.97600   1.000 44.07000  ? 7   ARG D CD  1 
ATOM   52   N NE  . ARG A 1 25  ? 6.86400   14.67100 8.58800   1.000 51.63000  ? 7   ARG D NE  1 
ATOM   53   C CZ  . ARG A 1 25  ? 7.28300   13.44400 8.86400   1.000 57.15000  ? 7   ARG D CZ  1 
ATOM   54   N NH1 . ARG A 1 25  ? 6.59600   12.68200 9.69200   1.000 56.84000  ? 7   ARG D NH1 1 
ATOM   55   N NH2 . ARG A 1 25  ? 8.39300   12.98500 8.31300   1.000 49.76000  ? 7   ARG D NH2 1 
ATOM   56   N N   . VAL A 1 26  ? 4.19800   19.67800 6.62100   1.000 54.95000  ? 8   VAL D N   1 
ATOM   57   C CA  . VAL A 1 26  ? 4.36500   19.91300 5.19100   1.000 61.25000  ? 8   VAL D CA  1 
ATOM   58   C C   . VAL A 1 26  ? 5.70600   19.33200 4.76200   1.000 49.87000  ? 8   VAL D C   1 
ATOM   59   O O   . VAL A 1 26  ? 6.76200   19.77100 5.23100   1.000 52.17000  ? 8   VAL D O   1 
ATOM   60   C CB  . VAL A 1 26  ? 4.27800   21.41000 4.86000   1.000 47.81000  ? 8   VAL D CB  1 
ATOM   61   C CG1 . VAL A 1 26  ? 4.47600   21.63700 3.37200   1.000 54.03000  ? 8   VAL D CG1 1 
ATOM   62   C CG2 . VAL A 1 26  ? 2.94300   21.97700 5.32000   1.000 52.39000  ? 8   VAL D CG2 1 
ATOM   63   N N   . LYS A 1 27  ? 5.66700   18.34700 3.86400   1.000 54.80000  ? 9   LYS D N   1 
ATOM   64   C CA  . LYS A 1 27  ? 6.87400   17.64700 3.42200   1.000 71.00000  ? 9   LYS D CA  1 
ATOM   65   C C   . LYS A 1 27  ? 7.54600   18.43800 2.29800   1.000 62.68000  ? 9   LYS D C   1 
ATOM   66   O O   . LYS A 1 27  ? 7.60200   18.02600 1.13700   1.000 64.00000  ? 9   LYS D O   1 
ATOM   67   C CB  . LYS A 1 27  ? 6.53300   16.23100 2.98000   1.000 69.53000  ? 9   LYS D CB  1 
ATOM   68   C CG  . LYS A 1 27  ? 5.52400   15.53500 3.87400   1.000 66.87000  ? 9   LYS D CG  1 
ATOM   69   C CD  . LYS A 1 27  ? 6.03700   14.19000 4.34500   1.000 75.61000  ? 9   LYS D CD  1 
ATOM   70   C CE  . LYS A 1 27  ? 4.92400   13.38700 4.98800   1.000 72.16000  ? 9   LYS D CE  1 
ATOM   71   N NZ  . LYS A 1 27  ? 5.41400   12.09500 5.53800   1.000 93.96000  ? 9   LYS D NZ  1 
ATOM   72   N N   . SER A 1 28  ? 8.07200   19.60700 2.67200   1.000 55.22000  ? 10  SER D N   1 
ATOM   73   C CA  . SER A 1 28  ? 8.75100   20.47100 1.71900   1.000 71.51000  ? 10  SER D CA  1 
ATOM   74   C C   . SER A 1 28  ? 9.67800   21.40900 2.47700   1.000 80.58000  ? 10  SER D C   1 
ATOM   75   O O   . SER A 1 28  ? 9.27400   21.93400 3.52300   1.000 61.93000  ? 10  SER D O   1 
ATOM   76   C CB  . SER A 1 28  ? 7.75600   21.28500 0.88400   1.000 77.04000  ? 10  SER D CB  1 
ATOM   77   O OG  . SER A 1 28  ? 8.43200   22.17600 0.01200   1.000 75.98000  ? 10  SER D OG  1 
ATOM   78   N N   . PRO A 1 29  ? 10.89600  21.63500 1.99500   1.000 83.10000  ? 11  PRO D N   1 
ATOM   79   C CA  . PRO A 1 29  ? 11.78600  22.60800 2.64200   1.000 81.83000  ? 11  PRO D CA  1 
ATOM   80   C C   . PRO A 1 29  ? 11.53100  24.04700 2.22700   1.000 90.10000  ? 11  PRO D C   1 
ATOM   81   O O   . PRO A 1 29  ? 12.17800  24.95100 2.76800   1.000 87.56000  ? 11  PRO D O   1 
ATOM   82   C CB  . PRO A 1 29  ? 13.17400  22.14800 2.18000   1.000 77.73000  ? 11  PRO D CB  1 
ATOM   83   C CG  . PRO A 1 29  ? 12.92300  21.58800 0.81900   1.000 91.93000  ? 11  PRO D CG  1 
ATOM   84   C CD  . PRO A 1 29  ? 11.56100  20.93400 0.88300   1.000 78.32000  ? 11  PRO D CD  1 
ATOM   85   N N   . LYS A 1 30  ? 10.61200  24.28900 1.29000   1.000 90.52000  ? 12  LYS D N   1 
ATOM   86   C CA  . LYS A 1 30  ? 10.37200  25.62600 0.75200   1.000 89.20000  ? 12  LYS D CA  1 
ATOM   87   C C   . LYS A 1 30  ? 8.86900   25.91300 0.71900   1.000 85.32000  ? 12  LYS D C   1 
ATOM   88   O O   . LYS A 1 30  ? 8.27200   26.12900 -0.33500  1.000 101.07000 ? 12  LYS D O   1 
ATOM   89   C CB  . LYS A 1 30  ? 10.98600  25.77700 -0.63700  1.000 90.75000  ? 12  LYS D CB  1 
ATOM   90   N N   . VAL A 1 31  ? 8.24000   25.92300 1.89400   1.000 81.03000  ? 13  VAL D N   1 
ATOM   91   C CA  . VAL A 1 31  ? 6.80400   26.31800 1.99400   1.000 75.34000  ? 13  VAL D CA  1 
ATOM   92   C C   . VAL A 1 31  ? 6.72200   27.15300 3.26900   1.000 72.07000  ? 13  VAL D C   1 
ATOM   93   O O   . VAL A 1 31  ? 6.85300   26.56700 4.35300   1.000 85.34000  ? 13  VAL D O   1 
ATOM   94   C CB  . VAL A 1 31  ? 5.84300   25.11500 2.02800   1.000 84.90000  ? 13  VAL D CB  1 
ATOM   95   C CG1 . VAL A 1 31  ? 4.47700   25.49600 2.57600   1.000 66.78000  ? 13  VAL D CG1 1 
ATOM   96   C CG2 . VAL A 1 31  ? 5.70300   24.45700 0.66500   1.000 76.81000  ? 13  VAL D CG2 1 
ATOM   97   N N   . LYS A 1 32  ? 6.55700   28.46800 3.14100   1.000 63.99000  ? 14  LYS D N   1 
ATOM   98   C CA  . LYS A 1 32  ? 6.62200   29.34000 4.34400   1.000 82.56000  ? 14  LYS D CA  1 
ATOM   99   C C   . LYS A 1 32  ? 5.26000   29.45200 5.02900   1.000 79.92000  ? 14  LYS D C   1 
ATOM   100  O O   . LYS A 1 32  ? 5.24200   29.59000 6.26200   1.000 85.38000  ? 14  LYS D O   1 
ATOM   101  C CB  . LYS A 1 32  ? 7.13700   30.73000 3.95500   1.000 82.47000  ? 14  LYS D CB  1 
ATOM   102  C CG  . LYS A 1 32  ? 7.53000   31.62400 5.12300   1.000 88.84000  ? 14  LYS D CG  1 
ATOM   103  C CD  . LYS A 1 32  ? 7.97200   33.00700 4.70500   1.000 93.20000  ? 14  LYS D CD  1 
ATOM   104  C CE  . LYS A 1 32  ? 8.41800   33.85800 5.87500   1.000 91.82000  ? 14  LYS D CE  1 
ATOM   105  N NZ  . LYS A 1 32  ? 8.87500   35.19800 5.43900   1.000 80.21000  ? 14  LYS D NZ  1 
ATOM   106  N N   . ARG A 1 33  ? 4.16600   29.38100 4.27400   1.000 64.29000  ? 15  ARG D N   1 
ATOM   107  C CA  . ARG A 1 33  ? 2.85400   29.62400 4.92000   1.000 67.89000  ? 15  ARG D CA  1 
ATOM   108  C C   . ARG A 1 33  ? 1.76200   28.76900 4.28500   1.000 65.28000  ? 15  ARG D C   1 
ATOM   109  O O   . ARG A 1 33  ? 2.01000   28.18700 3.21600   1.000 78.80000  ? 15  ARG D O   1 
ATOM   110  C CB  . ARG A 1 33  ? 2.51100   31.11000 4.78800   1.000 90.90000  ? 15  ARG D CB  1 
ATOM   111  C CG  . ARG A 1 33  ? 1.56000   31.63400 5.85400   1.000 107.35000 ? 15  ARG D CG  1 
ATOM   112  C CD  . ARG A 1 33  ? 1.49600   33.14900 5.85000   1.000 115.68000 ? 15  ARG D CD  1 
ATOM   113  N NE  . ARG A 1 33  ? 0.74900   33.67000 6.98500   1.000 130.30000 ? 15  ARG D NE  1 
ATOM   114  C CZ  . ARG A 1 33  ? 1.24400   34.50200 7.89300   1.000 132.65000 ? 15  ARG D CZ  1 
ATOM   115  N NH1 . ARG A 1 33  ? 2.47000   34.97600 7.75800   1.000 135.92000 ? 15  ARG D NH1 1 
ATOM   116  N NH2 . ARG A 1 33  ? 0.51000   34.85700 8.93200   1.000 129.49000 ? 15  ARG D NH2 1 
ATOM   117  N N   . LEU A 1 34  ? 0.60100   28.70300 4.93400   1.000 75.35000  ? 16  LEU D N   1 
ATOM   118  C CA  . LEU A 1 34  ? -0.55200  27.95200 4.37900   1.000 80.32000  ? 16  LEU D CA  1 
ATOM   119  C C   . LEU A 1 34  ? -1.63500  28.94900 3.96900   1.000 71.49000  ? 16  LEU D C   1 
ATOM   120  O O   . LEU A 1 34  ? -1.97600  29.81800 4.78400   1.000 76.69000  ? 16  LEU D O   1 
ATOM   121  C CB  . LEU A 1 34  ? -1.06700  26.97400 5.43700   1.000 68.58000  ? 16  LEU D CB  1 
ATOM   122  C CG  . LEU A 1 34  ? -0.12300  25.82700 5.78800   1.000 77.86000  ? 16  LEU D CG  1 
ATOM   123  C CD1 . LEU A 1 34  ? -0.72700  24.94200 6.86500   1.000 65.03000  ? 16  LEU D CD1 1 
ATOM   124  C CD2 . LEU A 1 34  ? 0.20300   25.00800 4.55000   1.000 75.29000  ? 16  LEU D CD2 1 
ATOM   125  N N   . SER A 1 35  ? -2.12900  28.83300 2.74200   1.000 65.38000  ? 17  SER D N   1 
ATOM   126  C CA  . SER A 1 35  ? -3.23900  29.70600 2.29200   1.000 94.86000  ? 17  SER D CA  1 
ATOM   127  C C   . SER A 1 35  ? -4.50800  29.31400 3.04900   1.000 90.59000  ? 17  SER D C   1 
ATOM   128  O O   . SER A 1 35  ? -4.58600  28.17400 3.52700   1.000 85.11000  ? 17  SER D O   1 
ATOM   129  C CB  . SER A 1 35  ? -3.44900  29.60000 0.80800   1.000 90.19000  ? 17  SER D CB  1 
ATOM   130  O OG  . SER A 1 35  ? -4.24800  28.47200 0.48900   1.000 94.03000  ? 17  SER D OG  1 
ATOM   131  N N   . GLU A 1 36  ? -5.46100  30.23500 3.14300   1.000 88.62000  ? 18  GLU D N   1 
ATOM   132  C CA  . GLU A 1 36  ? -6.73100  29.93000 3.84400   1.000 95.17000  ? 18  GLU D CA  1 
ATOM   133  C C   . GLU A 1 36  ? -7.40300  28.77200 3.10300   1.000 92.75000  ? 18  GLU D C   1 
ATOM   134  O O   . GLU A 1 36  ? -8.04500  27.94200 3.76400   1.000 95.67000  ? 18  GLU D O   1 
ATOM   135  C CB  . GLU A 1 36  ? -7.60600  31.18100 3.93300   1.000 96.16000  ? 18  GLU D CB  1 
ATOM   136  C CG  . GLU A 1 36  ? -8.65800  31.08600 5.01800   1.000 96.42000  ? 18  GLU D CG  1 
ATOM   137  C CD  . GLU A 1 36  ? -8.08100  30.76500 6.38500   1.000 94.48000  ? 18  GLU D CD  1 
ATOM   138  O OE1 . GLU A 1 36  ? -7.24500  31.55300 6.86700   1.000 89.07000  ? 18  GLU D OE1 1 
ATOM   139  O OE2 . GLU A 1 36  ? -8.46500  29.73000 6.96100   1.000 89.64000  ? 18  GLU D OE2 1 
ATOM   140  N N   . GLU A 1 37  ? -7.24000  28.71200 1.78300   1.000 89.12000  ? 19  GLU D N   1 
ATOM   141  C CA  . GLU A 1 37  ? -7.78200  27.56600 1.01200   1.000 96.36000  ? 19  GLU D CA  1 
ATOM   142  C C   . GLU A 1 37  ? -7.12100  26.28100 1.52100   1.000 93.58000  ? 19  GLU D C   1 
ATOM   143  O O   . GLU A 1 37  ? -7.84300  25.29800 1.74600   1.000 88.05000  ? 19  GLU D O   1 
ATOM   144  C CB  . GLU A 1 37  ? -7.52600  27.79900 -0.47800  1.000 93.86000  ? 19  GLU D CB  1 
ATOM   145  C CG  . GLU A 1 37  ? -7.81200  26.59100 -1.34800  1.000 98.12000  ? 19  GLU D CG  1 
ATOM   146  C CD  . GLU A 1 37  ? -7.56600  26.83700 -2.82600  1.000 102.86000 ? 19  GLU D CD  1 
ATOM   147  O OE1 . GLU A 1 37  ? -7.18500  27.97100 -3.17700  1.000 102.43000 ? 19  GLU D OE1 1 
ATOM   148  O OE2 . GLU A 1 37  ? -7.75300  25.89700 -3.62100  1.000 99.38000  ? 19  GLU D OE2 1 
ATOM   149  N N   . ASP A 1 38  ? -5.80100  26.30300 1.71500   1.000 97.29000  ? 20  ASP D N   1 
ATOM   150  C CA  . ASP A 1 38  ? -5.06900  25.12100 2.24000   1.000 92.18000  ? 20  ASP D CA  1 
ATOM   151  C C   . ASP A 1 38  ? -5.61000  24.77500 3.62800   1.000 87.60000  ? 20  ASP D C   1 
ATOM   152  O O   . ASP A 1 38  ? -5.89900  23.59400 3.86900   1.000 72.44000  ? 20  ASP D O   1 
ATOM   153  C CB  . ASP A 1 38  ? -3.56500  25.39000 2.29900   1.000 85.40000  ? 20  ASP D CB  1 
ATOM   154  C CG  . ASP A 1 38  ? -2.97300  25.83200 0.97400   1.000 92.74000  ? 20  ASP D CG  1 
ATOM   155  O OD1 . ASP A 1 38  ? -3.71000  25.82300 -0.02800  1.000 106.45000 ? 20  ASP D OD1 1 
ATOM   156  O OD2 . ASP A 1 38  ? -1.78900  26.21300 0.96300   1.000 93.07000  ? 20  ASP D OD2 1 
ATOM   157  N N   . ILE A 1 39  ? -5.76600  25.78200 4.48600   1.000 81.12000  ? 21  ILE D N   1 
ATOM   158  C CA  . ILE A 1 39  ? -6.25200  25.55100 5.87400   1.000 72.91000  ? 21  ILE D CA  1 
ATOM   159  C C   . ILE A 1 39  ? -7.61700  24.86800 5.81100   1.000 84.78000  ? 21  ILE D C   1 
ATOM   160  O O   . ILE A 1 39  ? -7.82100  23.89400 6.55300   1.000 82.97000  ? 21  ILE D O   1 
ATOM   161  C CB  . ILE A 1 39  ? -6.30000  26.88600 6.63700   1.000 68.96000  ? 21  ILE D CB  1 
ATOM   162  C CG1 . ILE A 1 39  ? -4.89600  27.47400 6.80400   1.000 76.92000  ? 21  ILE D CG1 1 
ATOM   163  C CG2 . ILE A 1 39  ? -7.00600  26.72800 7.97300   1.000 78.62000  ? 21  ILE D CG2 1 
ATOM   164  C CD1 . ILE A 1 39  ? -4.85900  28.79200 7.53700   1.000 76.29000  ? 21  ILE D CD1 1 
ATOM   165  N N   . GLU A 1 40  ? -8.50800  25.35000 4.94700   1.000 88.28000  ? 22  GLU D N   1 
ATOM   166  C CA  . GLU A 1 40  ? -9.87900  24.78100 4.89200   1.000 91.32000  ? 22  GLU D CA  1 
ATOM   167  C C   . GLU A 1 40  ? -9.78500  23.33500 4.41300   1.000 79.49000  ? 22  GLU D C   1 
ATOM   168  O O   . GLU A 1 40  ? -10.53000 22.49400 4.93400   1.000 85.95000  ? 22  GLU D O   1 
ATOM   169  C CB  . GLU A 1 40  ? -10.78900 25.59700 3.97100   1.000 101.03000 ? 22  GLU D CB  1 
ATOM   170  C CG  . GLU A 1 40  ? -11.01700 27.02100 4.44200   1.000 101.60000 ? 22  GLU D CG  1 
ATOM   171  C CD  . GLU A 1 40  ? -11.43300 27.16200 5.89600   1.000 103.00000 ? 22  GLU D CD  1 
ATOM   172  O OE1 . GLU A 1 40  ? -12.46700 26.58100 6.27600   1.000 84.71000  ? 22  GLU D OE1 1 
ATOM   173  O OE2 . GLU A 1 40  ? -10.72700 27.86400 6.64200   1.000 103.86000 ? 22  GLU D OE2 1 
ATOM   174  N N   . LYS A 1 41  ? -8.89700  23.07100 3.45700   1.000 81.98000  ? 23  LYS D N   1 
ATOM   175  C CA  . LYS A 1 41  ? -8.70400  21.67700 2.97900   1.000 90.67000  ? 23  LYS D CA  1 
ATOM   176  C C   . LYS A 1 41  ? -8.25600  20.81900 4.16800   1.000 87.09000  ? 23  LYS D C   1 
ATOM   177  O O   . LYS A 1 41  ? -8.77400  19.69900 4.30800   1.000 83.38000  ? 23  LYS D O   1 
ATOM   178  C CB  . LYS A 1 41  ? -7.71500  21.63400 1.81000   1.000 76.33000  ? 23  LYS D CB  1 
ATOM   179  C CG  . LYS A 1 41  ? -7.24100  20.24200 1.41900   1.000 80.32000  ? 23  LYS D CG  1 
ATOM   180  C CD  . LYS A 1 41  ? -7.18900  20.01200 -0.07500  1.000 91.41000  ? 23  LYS D CD  1 
ATOM   181  C CE  . LYS A 1 41  ? -6.32200  21.01400 -0.80600  1.000 96.25000  ? 23  LYS D CE  1 
ATOM   182  N NZ  . LYS A 1 41  ? -6.13400  20.63700 -2.22700  1.000 70.45000  ? 23  LYS D NZ  1 
ATOM   183  N N   . ILE A 1 42  ? -7.36000  21.34500 5.00500   1.000 78.18000  ? 24  ILE D N   1 
ATOM   184  C CA  . ILE A 1 42  ? -6.88700  20.60400 6.21100   1.000 77.82000  ? 24  ILE D CA  1 
ATOM   185  C C   . ILE A 1 42  ? -8.05700  20.43300 7.18200   1.000 73.16000  ? 24  ILE D C   1 
ATOM   186  O O   . ILE A 1 42  ? -8.29800  19.29700 7.61400   1.000 65.96000  ? 24  ILE D O   1 
ATOM   187  C CB  . ILE A 1 42  ? -5.70500  21.34500 6.86500   1.000 62.67000  ? 24  ILE D CB  1 
ATOM   188  C CG1 . ILE A 1 42  ? -4.47500  21.35500 5.95500   1.000 62.78000  ? 24  ILE D CG1 1 
ATOM   189  C CG2 . ILE A 1 42  ? -5.39100  20.76700 8.23500   1.000 66.62000  ? 24  ILE D CG2 1 
ATOM   190  C CD1 . ILE A 1 42  ? -3.33800  22.19500 6.47600   1.000 68.68000  ? 24  ILE D CD1 1 
ATOM   191  N N   . LYS A 1 43  ? -8.77600  21.51500 7.47500   1.000 77.73000  ? 25  LYS D N   1 
ATOM   192  C CA  . LYS A 1 43  ? -9.86800  21.45300 8.48000   1.000 68.70000  ? 25  LYS D CA  1 
ATOM   193  C C   . LYS A 1 43  ? -10.98200 20.52700 7.98700   1.000 81.03000  ? 25  LYS D C   1 
ATOM   194  O O   . LYS A 1 43  ? -11.61200 19.86800 8.83000   1.000 91.88000  ? 25  LYS D O   1 
ATOM   195  C CB  . LYS A 1 43  ? -10.39500 22.86000 8.76500   1.000 78.07000  ? 25  LYS D CB  1 
ATOM   196  C CG  . LYS A 1 43  ? -9.39900  23.80500 9.42200   1.000 76.76000  ? 25  LYS D CG  1 
ATOM   197  C CD  . LYS A 1 43  ? -9.99500  25.15600 9.74900   1.000 92.22000  ? 25  LYS D CD  1 
ATOM   198  N N   . SER A 1 44  ? -11.21500 20.48600 6.67900   1.000 73.40000  ? 26  SER D N   1 
ATOM   199  C CA  . SER A 1 44  ? -12.31900 19.65600 6.14300   1.000 78.01000  ? 26  SER D CA  1 
ATOM   200  C C   . SER A 1 44  ? -11.96000 18.17900 6.28400   1.000 81.90000  ? 26  SER D C   1 
ATOM   201  O O   . SER A 1 44  ? -12.84400 17.38900 6.66100   1.000 84.64000  ? 26  SER D O   1 
ATOM   202  C CB  . SER A 1 44  ? -12.61700 20.00600 4.71300   1.000 81.62000  ? 26  SER D CB  1 
ATOM   203  O OG  . SER A 1 44  ? -13.55200 19.09700 4.15500   1.000 84.60000  ? 26  SER D OG  1 
ATOM   204  N N   . ALA A 1 45  ? -10.70800 17.82500 6.00000   1.000 73.41000  ? 27  ALA D N   1 
ATOM   205  C CA  . ALA A 1 45  ? -10.31700 16.40000 6.03300   1.000 70.88000  ? 27  ALA D CA  1 
ATOM   206  C C   . ALA A 1 45  ? -10.22300 15.87100 7.46800   1.000 72.42000  ? 27  ALA D C   1 
ATOM   207  O O   . ALA A 1 45  ? -10.07100 14.66100 7.61900   1.000 67.79000  ? 27  ALA D O   1 
ATOM   208  C CB  . ALA A 1 45  ? -9.01300  16.24600 5.31400   1.000 74.40000  ? 27  ALA D CB  1 
ATOM   209  N N   . LEU A 1 46  ? -10.29000 16.75500 8.46700   1.000 72.38000  ? 28  LEU D N   1 
ATOM   210  C CA  . LEU A 1 46  ? -10.11900 16.33200 9.88300   1.000 73.17000  ? 28  LEU D CA  1 
ATOM   211  C C   . LEU A 1 46  ? -11.47700 16.32200 10.59000  1.000 77.83000  ? 28  LEU D C   1 
ATOM   212  O O   . LEU A 1 46  ? -11.49300 16.37500 11.83200  1.000 87.89000  ? 28  LEU D O   1 
ATOM   213  C CB  . LEU A 1 46  ? -9.13900  17.28800 10.56900  1.000 71.30000  ? 28  LEU D CB  1 
ATOM   214  C CG  . LEU A 1 46  ? -7.67000  17.09800 10.19500  1.000 63.56000  ? 28  LEU D CG  1 
ATOM   215  C CD1 . LEU A 1 46  ? -6.77600  17.96500 11.06600  1.000 66.07000  ? 28  LEU D CD1 1 
ATOM   216  C CD2 . LEU A 1 46  ? -7.26700  15.63700 10.31400  1.000 63.42000  ? 28  LEU D CD2 1 
ATOM   217  N N   . LYS A 1 47  ? -12.56700 16.25000 9.82700   1.000 79.78000  ? 29  LYS D N   1 
ATOM   218  C CA  . LYS A 1 47  ? -13.92100 16.16800 10.42700  1.000 75.87000  ? 29  LYS D CA  1 
ATOM   219  C C   . LYS A 1 47  ? -14.26600 14.70000 10.67700  1.000 78.97000  ? 29  LYS D C   1 
ATOM   220  O O   . LYS A 1 47  ? -14.77900 14.39000 11.76300  1.000 87.07000  ? 29  LYS D O   1 
ATOM   221  C CB  . LYS A 1 47  ? -14.93500 16.80200 9.47700   1.000 83.65000  ? 29  LYS D CB  1 
ATOM   222  N N   . SER A 1 48  ? -13.97800 13.83500 9.70900   1.000 78.89000  ? 30  SER D N   1 
ATOM   223  C CA  . SER A 1 48  ? -14.31700 12.39600 9.83000   1.000 94.22000  ? 30  SER D CA  1 
ATOM   224  C C   . SER A 1 48  ? -13.17900 11.64000 10.51400  1.000 95.26000  ? 30  SER D C   1 
ATOM   225  O O   . SER A 1 48  ? -13.40300 10.49100 10.93200  1.000 82.15000  ? 30  SER D O   1 
ATOM   226  C CB  . SER A 1 48  ? -14.59200 11.80900 8.47500   1.000 96.10000  ? 30  SER D CB  1 
ATOM   227  O OG  . SER A 1 48  ? -14.57500 10.39000 8.52700   1.000 99.39000  ? 30  SER D OG  1 
ATOM   228  N N   . THR A 1 49  ? -12.00700 12.26500 10.60600  1.000 86.40000  ? 31  THR D N   1 
ATOM   229  C CA  . THR A 1 49  ? -10.83300 11.56700 11.18500  1.000 84.91000  ? 31  THR D CA  1 
ATOM   230  C C   . THR A 1 49  ? -9.94400  12.57200 11.91100  1.000 71.59000  ? 31  THR D C   1 
ATOM   231  O O   . THR A 1 49  ? -10.11300 13.77500 11.68800  1.000 84.66000  ? 31  THR D O   1 
ATOM   232  C CB  . THR A 1 49  ? -10.06700 10.80500 10.09700  1.000 88.25000  ? 31  THR D CB  1 
ATOM   233  O OG1 . THR A 1 49  ? -8.88600  10.25100 10.67700  1.000 86.84000  ? 31  THR D OG1 1 
ATOM   234  C CG2 . THR A 1 49  ? -9.70100  11.68000 8.91800   1.000 81.85000  ? 31  THR D CG2 1 
ATOM   235  N N   . ASN A 1 50  ? -9.04700  12.08200 12.76400  1.000 77.99000  ? 32  ASN D N   1 
ATOM   236  C CA  . ASN A 1 50  ? -8.08800  12.97300 13.46500  1.000 77.78000  ? 32  ASN D CA  1 
ATOM   237  C C   . ASN A 1 50  ? -6.70700  12.76600 12.84100  1.000 72.22000  ? 32  ASN D C   1 
ATOM   238  O O   . ASN A 1 50  ? -5.72900  13.29600 13.39100  1.000 65.44000  ? 32  ASN D O   1 
ATOM   239  C CB  . ASN A 1 50  ? -8.10700  12.72700 14.97300  1.000 73.89000  ? 32  ASN D CB  1 
ATOM   240  C CG  . ASN A 1 50  ? -9.29700  13.36800 15.65300  1.000 79.72000  ? 32  ASN D CG  1 
ATOM   241  O OD1 . ASN A 1 50  ? -10.09300 14.04800 15.01100  1.000 82.13000  ? 32  ASN D OD1 1 
ATOM   242  N ND2 . ASN A 1 50  ? -9.41900  13.16700 16.95400  1.000 78.66000  ? 32  ASN D ND2 1 
ATOM   243  N N   . LYS A 1 51  ? -6.64800  12.01900 11.73600  1.000 64.99000  ? 33  LYS D N   1 
ATOM   244  C CA  . LYS A 1 51  ? -5.36700  11.77500 11.02400  1.000 67.29000  ? 33  LYS D CA  1 
ATOM   245  C C   . LYS A 1 51  ? -5.66600  11.68300 9.52700   1.000 78.66000  ? 33  LYS D C   1 
ATOM   246  O O   . LYS A 1 51  ? -6.41400  10.77100 9.13400   1.000 78.24000  ? 33  LYS D O   1 
ATOM   247  C CB  . LYS A 1 51  ? -4.70400  10.48700 11.51800  1.000 60.91000  ? 33  LYS D CB  1 
ATOM   248  C CG  . LYS A 1 51  ? -3.43000  10.08800 10.78800  1.000 62.00000  ? 33  LYS D CG  1 
ATOM   249  C CD  . LYS A 1 51  ? -2.90000  8.74000  11.22300  1.000 83.70000  ? 33  LYS D CD  1 
ATOM   250  N N   . ALA A 1 52  ? -5.10700  12.59800 8.73400   1.000 73.00000  ? 34  ALA D N   1 
ATOM   251  C CA  . ALA A 1 52  ? -5.35200  12.60000 7.27900   1.000 75.77000  ? 34  ALA D CA  1 
ATOM   252  C C   . ALA A 1 52  ? -4.13500  13.09600 6.50000   1.000 78.38000  ? 34  ALA D C   1 
ATOM   253  O O   . ALA A 1 52  ? -3.19700  13.60800 7.11300   1.000 69.59000  ? 34  ALA D O   1 
ATOM   254  C CB  . ALA A 1 52  ? -6.55200  13.44900 6.98000   1.000 73.51000  ? 34  ALA D CB  1 
ATOM   255  N N   . VAL A 1 53  ? -4.17700  12.94000 5.18300   1.000 73.82000  ? 35  VAL D N   1 
ATOM   256  C CA  . VAL A 1 53  ? -3.08500  13.38400 4.32300   1.000 64.03000  ? 35  VAL D CA  1 
ATOM   257  C C   . VAL A 1 53  ? -3.69100  14.18900 3.18300   1.000 71.97000  ? 35  VAL D C   1 
ATOM   258  O O   . VAL A 1 53  ? -4.54000  13.67700 2.44200   1.000 87.71000  ? 35  VAL D O   1 
ATOM   259  C CB  . VAL A 1 53  ? -2.26100  12.20600 3.77700   1.000 73.39000  ? 35  VAL D CB  1 
ATOM   260  C CG1 . VAL A 1 53  ? -1.23600  12.69800 2.77200   1.000 67.37000  ? 35  VAL D CG1 1 
ATOM   261  C CG2 . VAL A 1 53  ? -1.58100  11.45500 4.91300   1.000 69.12000  ? 35  VAL D CG2 1 
ATOM   262  N N   . VAL A 1 54  ? -3.26300  15.44100 3.04100   1.000 59.88000  ? 36  VAL D N   1 
ATOM   263  C CA  . VAL A 1 54  ? -3.77300  16.33300 2.00900   1.000 61.67000  ? 36  VAL D CA  1 
ATOM   264  C C   . VAL A 1 54  ? -2.61900  16.74200 1.09800   1.000 75.89000  ? 36  VAL D C   1 
ATOM   265  O O   . VAL A 1 54  ? -1.44500  16.55100 1.41600   1.000 71.32000  ? 36  VAL D O   1 
ATOM   266  C CB  . VAL A 1 54  ? -4.47500  17.57300 2.59900   1.000 51.88000  ? 36  VAL D CB  1 
ATOM   267  C CG1 . VAL A 1 54  ? -5.56900  17.15000 3.56800   1.000 66.21000  ? 36  VAL D CG1 1 
ATOM   268  C CG2 . VAL A 1 54  ? -3.46800  18.48200 3.28300   1.000 60.40000  ? 36  VAL D CG2 1 
ATOM   269  N N   . THR A 1 55  ? -2.98200  17.24700 -0.08000  1.000 75.70000  ? 37  THR D N   1 
ATOM   270  C CA  . THR A 1 55  ? -1.95300  17.69800 -1.04500  1.000 72.64000  ? 37  THR D CA  1 
ATOM   271  C C   . THR A 1 55  ? -2.08400  19.20800 -1.22600  1.000 72.61000  ? 37  THR D C   1 
ATOM   272  O O   . THR A 1 55  ? -3.21600  19.68800 -1.36300  1.000 74.88000  ? 37  THR D O   1 
ATOM   273  C CB  . THR A 1 55  ? -2.06600  16.94500 -2.37300  1.000 87.73000  ? 37  THR D CB  1 
ATOM   274  O OG1 . THR A 1 55  ? -3.35600  17.20400 -2.92500  1.000 107.29000 ? 37  THR D OG1 1 
ATOM   275  C CG2 . THR A 1 55  ? -1.86100  15.45400 -2.22000  1.000 90.64000  ? 37  THR D CG2 1 
ATOM   276  N N   . ILE A 1 56  ? -0.95700  19.91100 -1.20000  1.000 76.17000  ? 38  ILE D N   1 
ATOM   277  C CA  . ILE A 1 56  ? -0.96200  21.38900 -1.37500  1.000 76.56000  ? 38  ILE D CA  1 
ATOM   278  C C   . ILE A 1 56  ? -0.02500  21.72900 -2.53200  1.000 80.89000  ? 38  ILE D C   1 
ATOM   279  O O   . ILE A 1 56  ? 0.99500   21.04200 -2.68700  1.000 75.41000  ? 38  ILE D O   1 
ATOM   280  C CB  . ILE A 1 56  ? -0.55100  22.09500 -0.06800  1.000 76.77000  ? 38  ILE D CB  1 
ATOM   281  C CG1 . ILE A 1 56  ? -1.53700  21.80300 1.06500   1.000 86.78000  ? 38  ILE D CG1 1 
ATOM   282  C CG2 . ILE A 1 56  ? -0.37400  23.58800 -0.28200  1.000 82.95000  ? 38  ILE D CG2 1 
ATOM   283  C CD1 . ILE A 1 56  ? -2.96300  22.17500 0.74600   1.000 82.74000  ? 38  ILE D CD1 1 
ATOM   284  N N   . LYS A 1 57  ? -0.37700  22.73800 -3.31900  1.000 76.46000  ? 39  LYS D N   1 
ATOM   285  C CA  . LYS A 1 57  ? 0.44500   23.18100 -4.43700  1.000 91.64000  ? 39  LYS D CA  1 
ATOM   286  C C   . LYS A 1 57  ? 1.31200   24.35800 -4.00800  1.000 89.54000  ? 39  LYS D C   1 
ATOM   287  O O   . LYS A 1 57  ? 0.81600   25.31100 -3.39900  1.000 93.20000  ? 39  LYS D O   1 
ATOM   288  C CB  . LYS A 1 57  ? -0.42900  23.57700 -5.62700  1.000 91.55000  ? 39  LYS D CB  1 
ATOM   289  N N   . ASP A 1 58  ? 2.60300   24.29100 -4.33200  1.000 87.86000  ? 40  ASP D N   1 
ATOM   290  C CA  . ASP A 1 58  ? 3.51500   25.38000 -4.01700  1.000 99.50000  ? 40  ASP D CA  1 
ATOM   291  C C   . ASP A 1 58  ? 3.36100   26.50400 -5.04100  1.000 102.86000 ? 40  ASP D C   1 
ATOM   292  O O   . ASP A 1 58  ? 2.53900   26.43900 -5.96000  1.000 95.87000  ? 40  ASP D O   1 
ATOM   293  C CB  . ASP A 1 58  ? 4.95500   24.87000 -3.95300  1.000 96.49000  ? 40  ASP D CB  1 
ATOM   294  C CG  . ASP A 1 58  ? 5.52100   24.52400 -5.32000  1.000 105.54000 ? 40  ASP D CG  1 
ATOM   295  O OD1 . ASP A 1 58  ? 4.73700   24.18000 -6.22800  1.000 117.17000 ? 40  ASP D OD1 1 
ATOM   296  O OD2 . ASP A 1 58  ? 6.75800   24.59300 -5.48300  1.000 101.67000 ? 40  ASP D OD2 1 
ATOM   297  N N   . GLU A 1 59  ? 4.16600   27.55900 -4.88100  1.000 122.08000 ? 41  GLU D N   1 
ATOM   298  C CA  . GLU A 1 59  ? 4.07400   28.69600 -5.79300  1.000 116.46000 ? 41  GLU D CA  1 
ATOM   299  C C   . GLU A 1 59  ? 4.48100   28.31100 -7.20900  1.000 120.22000 ? 41  GLU D C   1 
ATOM   300  O O   . GLU A 1 59  ? 3.98300   28.89600 -8.17800  1.000 117.40000 ? 41  GLU D O   1 
ATOM   301  C CB  . GLU A 1 59  ? 4.93200   29.85800 -5.28300  1.000 99.88000  ? 41  GLU D CB  1 
ATOM   302  N N   . ASN A 1 60  ? 5.37300   27.32900 -7.35200  1.000 117.61000 ? 42  ASN D N   1 
ATOM   303  C CA  . ASN A 1 60  ? 5.74600   26.84500 -8.67400  1.000 121.96000 ? 42  ASN D CA  1 
ATOM   304  C C   . ASN A 1 60  ? 4.64800   25.99600 -9.30200  1.000 126.02000 ? 42  ASN D C   1 
ATOM   305  O O   . ASN A 1 60  ? 4.60200   25.87000 -10.53000 1.000 129.76000 ? 42  ASN D O   1 
ATOM   306  C CB  . ASN A 1 60  ? 7.05500   26.05200 -8.58700  1.000 123.18000 ? 42  ASN D CB  1 
ATOM   307  N N   . GLY A 1 61  ? 3.75300   25.45000 -8.47000  1.000 118.21000 ? 43  GLY D N   1 
ATOM   308  C CA  . GLY A 1 61  ? 2.64300   24.61300 -8.97200  1.000 107.75000 ? 43  GLY D CA  1 
ATOM   309  C C   . GLY A 1 61  ? 2.84400   23.14200 -8.65100  1.000 96.37000  ? 43  GLY D C   1 
ATOM   310  O O   . GLY A 1 61  ? 1.95300   22.34400 -8.98200  1.000 95.38000  ? 43  GLY D O   1 
ATOM   311  N N   . GLU A 1 62  ? 3.97100   22.79600 -8.03100  1.000 85.98000  ? 44  GLU D N   1 
ATOM   312  C CA  . GLU A 1 62  ? 4.28100   21.37700 -7.71400  1.000 95.22000  ? 44  GLU D CA  1 
ATOM   313  C C   . GLU A 1 62  ? 3.41400   20.91100 -6.54300  1.000 97.17000  ? 44  GLU D C   1 
ATOM   314  O O   . GLU A 1 62  ? 3.10800   21.73900 -5.66900  1.000 97.34000  ? 44  GLU D O   1 
ATOM   315  C CB  . GLU A 1 62  ? 5.76900   21.22200 -7.39200  1.000 100.90000 ? 44  GLU D CB  1 
ATOM   316  N N   . GLU A 1 63  ? 3.04300   19.62900 -6.53200  1.000 84.92000  ? 45  GLU D N   1 
ATOM   317  C CA  . GLU A 1 63  ? 2.18800   19.08100 -5.44900  1.000 84.79000  ? 45  GLU D CA  1 
ATOM   318  C C   . GLU A 1 63  ? 3.05500   18.76500 -4.22900  1.000 79.19000  ? 45  GLU D C   1 
ATOM   319  O O   . GLU A 1 63  ? 4.14800   18.20500 -4.41400  1.000 79.75000  ? 45  GLU D O   1 
ATOM   320  C CB  . GLU A 1 63  ? 1.45400   17.83100 -5.93200  1.000 70.94000  ? 45  GLU D CB  1 
ATOM   321  C CG  . GLU A 1 63  ? -0.03200  17.85500 -5.62400  1.000 90.91000  ? 45  GLU D CG  1 
ATOM   322  C CD  . GLU A 1 63  ? -0.79300  16.61400 -6.05700  1.000 95.56000  ? 45  GLU D CD  1 
ATOM   323  O OE1 . GLU A 1 63  ? -0.15100  15.68200 -6.57700  1.000 97.57000  ? 45  GLU D OE1 1 
ATOM   324  O OE2 . GLU A 1 63  ? -2.02600  16.58700 -5.88100  1.000 83.67000  ? 45  GLU D OE2 1 
ATOM   325  N N   . ILE A 1 64  ? 2.57600   19.11800 -3.03500  1.000 74.28000  ? 46  ILE D N   1 
ATOM   326  C CA  . ILE A 1 64  ? 3.32800   18.84100 -1.77800  1.000 74.66000  ? 46  ILE D CA  1 
ATOM   327  C C   . ILE A 1 64  ? 2.42400   18.05100 -0.83300  1.000 64.76000  ? 46  ILE D C   1 
ATOM   328  O O   . ILE A 1 64  ? 1.31800   18.52600 -0.54000  1.000 68.60000  ? 46  ILE D O   1 
ATOM   329  C CB  . ILE A 1 64  ? 3.83200   20.14300 -1.12400  1.000 70.62000  ? 46  ILE D CB  1 
ATOM   330  C CG1 . ILE A 1 64  ? 4.68000   20.97900 -2.08500  1.000 79.00000  ? 46  ILE D CG1 1 
ATOM   331  C CG2 . ILE A 1 64  ? 4.57700   19.83800 0.16400   1.000 64.85000  ? 46  ILE D CG2 1 
ATOM   332  C CD1 . ILE A 1 64  ? 5.95600   20.30300 -2.52100  1.000 86.56000  ? 46  ILE D CD1 1 
ATOM   333  N N   . GLU A 1 65  ? 2.87800   16.88000 -0.39600  1.000 63.97000  ? 47  GLU D N   1 
ATOM   334  C CA  . GLU A 1 65  ? 2.12800   16.07500 0.55600   1.000 63.73000  ? 47  GLU D CA  1 
ATOM   335  C C   . GLU A 1 65  ? 2.19000   16.70700 1.94100   1.000 60.98000  ? 47  GLU D C   1 
ATOM   336  O O   . GLU A 1 65  ? 3.23900   17.19500 2.37000   1.000 57.79000  ? 47  GLU D O   1 
ATOM   337  C CB  . GLU A 1 65  ? 2.68300   14.65100 0.60000   1.000 61.32000  ? 47  GLU D CB  1 
ATOM   338  C CG  . GLU A 1 65  ? 2.03000   13.74900 1.63300   1.000 86.60000  ? 47  GLU D CG  1 
ATOM   339  C CD  . GLU A 1 65  ? 2.61600   12.35100 1.64200   1.000 100.79000 ? 47  GLU D CD  1 
ATOM   340  O OE1 . GLU A 1 65  ? 3.37400   12.01900 0.70600   1.000 104.83000 ? 47  GLU D OE1 1 
ATOM   341  O OE2 . GLU A 1 65  ? 2.32100   11.58700 2.58500   1.000 92.34000  ? 47  GLU D OE2 1 
ATOM   342  N N   . VAL A 1 66  ? 1.05500   16.70700 2.63700   1.000 51.43000  ? 48  VAL D N   1 
ATOM   343  C CA  . VAL A 1 66  ? 0.94200   17.31800 3.95800   1.000 58.68000  ? 48  VAL D CA  1 
ATOM   344  C C   . VAL A 1 66  ? 0.23500   16.34000 4.88600   1.000 64.31000  ? 48  VAL D C   1 
ATOM   345  O O   . VAL A 1 66  ? -0.92600  15.98400 4.65100   1.000 66.10000  ? 48  VAL D O   1 
ATOM   346  C CB  . VAL A 1 66  ? 0.18300   18.65600 3.91400   1.000 57.78000  ? 48  VAL D CB  1 
ATOM   347  C CG1 . VAL A 1 66  ? 0.05100   19.23400 5.31500   1.000 54.48000  ? 48  VAL D CG1 1 
ATOM   348  C CG2 . VAL A 1 66  ? 0.88200   19.64400 2.99000   1.000 51.76000  ? 48  VAL D CG2 1 
ATOM   349  N N   . GLU A 1 67  ? 0.94300   15.90000 5.92800   1.000 64.97000  ? 49  GLU D N   1 
ATOM   350  C CA  . GLU A 1 67  ? 0.30100   15.04100 6.95300   1.000 52.61000  ? 49  GLU D CA  1 
ATOM   351  C C   . GLU A 1 67  ? -0.37700  15.97400 7.95400   1.000 44.99000  ? 49  GLU D C   1 
ATOM   352  O O   . GLU A 1 67  ? 0.28600   16.91500 8.41300   1.000 57.04000  ? 49  GLU D O   1 
ATOM   353  C CB  . GLU A 1 67  ? 1.32800   14.16600 7.66800   1.000 53.84000  ? 49  GLU D CB  1 
ATOM   354  C CG  . GLU A 1 67  ? 1.86400   13.02500 6.83000   1.000 60.46000  ? 49  GLU D CG  1 
ATOM   355  C CD  . GLU A 1 67  ? 2.75100   12.07500 7.61600   1.000 88.21000  ? 49  GLU D CD  1 
ATOM   356  O OE1 . GLU A 1 67  ? 2.93200   12.30600 8.82700   1.000 74.60000  ? 49  GLU D OE1 1 
ATOM   357  O OE2 . GLU A 1 67  ? 3.26000   11.11000 7.01600   1.000 99.23000  ? 49  GLU D OE2 1 
ATOM   358  N N   . VAL A 1 68  ? -1.65100  15.73400 8.25200   1.000 46.67000  ? 50  VAL D N   1 
ATOM   359  C CA  . VAL A 1 68  ? -2.40700  16.64100 9.16200   1.000 47.66000  ? 50  VAL D CA  1 
ATOM   360  C C   . VAL A 1 68  ? -3.04100  15.80400 10.27600  1.000 62.54000  ? 50  VAL D C   1 
ATOM   361  O O   . VAL A 1 68  ? -3.50100  14.68600 9.98600   1.000 65.05000  ? 50  VAL D O   1 
ATOM   362  C CB  . VAL A 1 68  ? -3.45100  17.47000 8.39100   1.000 58.17000  ? 50  VAL D CB  1 
ATOM   363  C CG1 . VAL A 1 68  ? -2.79000  18.44100 7.42800   1.000 53.53000  ? 50  VAL D CG1 1 
ATOM   364  C CG2 . VAL A 1 68  ? -4.45300  16.59400 7.65700   1.000 69.13000  ? 50  VAL D CG2 1 
ATOM   365  N N   . ARG A 1 69  ? -3.04000  16.31900 11.50300  1.000 55.29000  ? 51  ARG D N   1 
ATOM   366  C CA  . ARG A 1 69  ? -3.58700  15.56600 12.65300  1.000 51.28000  ? 51  ARG D CA  1 
ATOM   367  C C   . ARG A 1 69  ? -4.30100  16.50500 13.62700  1.000 46.60000  ? 51  ARG D C   1 
ATOM   368  O O   . ARG A 1 69  ? -3.80300  17.60300 13.84500  1.000 49.50000  ? 51  ARG D O   1 
ATOM   369  C CB  . ARG A 1 69  ? -2.45400  14.78800 13.32300  1.000 52.43000  ? 51  ARG D CB  1 
ATOM   370  C CG  . ARG A 1 69  ? -1.95000  13.60400 12.51900  1.000 47.47000  ? 51  ARG D CG  1 
ATOM   371  C CD  . ARG A 1 69  ? -0.73900  12.96700 13.15900  1.000 64.46000  ? 51  ARG D CD  1 
ATOM   372  N NE  . ARG A 1 69  ? -0.02300  12.20000 12.15700  1.000 65.76000  ? 51  ARG D NE  1 
ATOM   373  C CZ  . ARG A 1 69  ? 0.15500   10.89100 12.20900  1.000 75.43000  ? 51  ARG D CZ  1 
ATOM   374  N NH1 . ARG A 1 69  ? -0.11700  10.23500 13.32100  1.000 89.73000  ? 51  ARG D NH1 1 
ATOM   375  N NH2 . ARG A 1 69  ? 0.60500   10.24400 11.15000  1.000 87.91000  ? 51  ARG D NH2 1 
ATOM   376  N N   . LEU A 1 70  ? -5.45300  16.08000 14.15300  1.000 57.42000  ? 52  LEU D N   1 
ATOM   377  C CA  . LEU A 1 70  ? -6.16900  16.87100 15.18900  1.000 57.57000  ? 52  LEU D CA  1 
ATOM   378  C C   . LEU A 1 70  ? -5.86600  16.20700 16.53000  1.000 48.81000  ? 52  LEU D C   1 
ATOM   379  O O   . LEU A 1 70  ? -6.35400  15.08800 16.74800  1.000 51.70000  ? 52  LEU D O   1 
ATOM   380  C CB  . LEU A 1 70  ? -7.67000  16.87300 14.89100  1.000 41.18000  ? 52  LEU D CB  1 
ATOM   381  C CG  . LEU A 1 70  ? -8.51600  17.71200 15.84400  1.000 55.64000  ? 52  LEU D CG  1 
ATOM   382  C CD1 . LEU A 1 70  ? -8.12700  19.17600 15.75100  1.000 52.72000  ? 52  LEU D CD1 1 
ATOM   383  C CD2 . LEU A 1 70  ? -9.99600  17.53500 15.54900  1.000 60.35000  ? 52  LEU D CD2 1 
ATOM   384  N N   . LEU A 1 71  ? -5.10000  16.87000 17.39300  1.000 48.02000  ? 53  LEU D N   1 
ATOM   385  C CA  . LEU A 1 71  ? -4.66000  16.18600 18.63500  1.000 44.28000  ? 53  LEU D CA  1 
ATOM   386  C C   . LEU A 1 71  ? -4.77300  17.08300 19.86400  1.000 40.93000  ? 53  LEU D C   1 
ATOM   387  O O   . LEU A 1 71  ? -4.67300  18.30700 19.70900  1.000 50.17000  ? 53  LEU D O   1 
ATOM   388  C CB  . LEU A 1 71  ? -3.19500  15.78300 18.44600  1.000 41.89000  ? 53  LEU D CB  1 
ATOM   389  C CG  . LEU A 1 71  ? -2.88400  14.84200 17.28400  1.000 50.12000  ? 53  LEU D CG  1 
ATOM   390  C CD1 . LEU A 1 71  ? -1.38400  14.62400 17.16400  1.000 43.81000  ? 53  LEU D CD1 1 
ATOM   391  C CD2 . LEU A 1 71  ? -3.59500  13.51000 17.45900  1.000 63.79000  ? 53  LEU D CD2 1 
ATOM   392  N N   . THR A 1 72  ? -4.97400  16.48200 21.03800  1.000 44.09000  ? 54  THR D N   1 
ATOM   393  C CA  . THR A 1 72  ? -4.93500  17.23200 22.28000  1.000 44.03000  ? 54  THR D CA  1 
ATOM   394  C C   . THR A 1 72  ? -3.49400  17.62900 22.59800  1.000 45.65000  ? 54  THR D C   1 
ATOM   395  O O   . THR A 1 72  ? -2.54600  17.22800 21.91700  1.000 41.38000  ? 54  THR D O   1 
ATOM   396  C CB  . THR A 1 72  ? -5.52600  16.41000 23.42600  1.000 53.13000  ? 54  THR D CB  1 
ATOM   397  O OG1 . THR A 1 72  ? -4.67900  15.28600 23.69700  1.000 42.49000  ? 54  THR D OG1 1 
ATOM   398  C CG2 . THR A 1 72  ? -6.91600  15.90900 23.06000  1.000 44.89000  ? 54  THR D CG2 1 
ATOM   399  N N   . LEU A 1 73  ? -3.33200  18.43300 23.65200  1.000 37.78000  ? 55  LEU D N   1 
ATOM   400  C CA  . LEU A 1 73  ? -1.99400  18.87800 24.03000  1.000 47.14000  ? 55  LEU D CA  1 
ATOM   401  C C   . LEU A 1 73  ? -1.10800  17.69800 24.41200  1.000 59.53000  ? 55  LEU D C   1 
ATOM   402  O O   . LEU A 1 73  ? 0.07000   17.65000 24.03900  1.000 39.91000  ? 55  LEU D O   1 
ATOM   403  C CB  . LEU A 1 73  ? -2.07700  19.88300 25.17800  1.000 47.89000  ? 55  LEU D CB  1 
ATOM   404  C CG  . LEU A 1 73  ? -0.73100  20.39600 25.69700  1.000 44.35000  ? 55  LEU D CG  1 
ATOM   405  C CD1 . LEU A 1 73  ? 0.03900   21.10300 24.59100  1.000 47.47000  ? 55  LEU D CD1 1 
ATOM   406  C CD2 . LEU A 1 73  ? -0.92900  21.31400 26.89200  1.000 39.66000  ? 55  LEU D CD2 1 
ATOM   407  N N   . GLU A 1 74  ? -1.65900  16.73100 25.14800  1.000 43.01000  ? 56  GLU D N   1 
ATOM   408  C CA  . GLU A 1 74  ? -0.87100  15.56800 25.54400  1.000 42.12000  ? 56  GLU D CA  1 
ATOM   409  C C   . GLU A 1 74  ? -0.56100  14.67800 24.34600  1.000 50.76000  ? 56  GLU D C   1 
ATOM   410  O O   . GLU A 1 74  ? 0.55900   14.16900 24.21800  1.000 52.06000  ? 56  GLU D O   1 
ATOM   411  C CB  . GLU A 1 74  ? -1.60800  14.78200 26.62600  1.000 51.94000  ? 56  GLU D CB  1 
ATOM   412  C CG  . GLU A 1 74  ? -0.77200  13.70600 27.29500  1.000 69.98000  ? 56  GLU D CG  1 
ATOM   413  C CD  . GLU A 1 74  ? -1.49600  13.04300 28.44900  1.000 82.21000  ? 56  GLU D CD  1 
ATOM   414  O OE1 . GLU A 1 74  ? -2.74500  13.07300 28.46700  1.000 83.55000  ? 56  GLU D OE1 1 
ATOM   415  O OE2 . GLU A 1 74  ? -0.81500  12.49700 29.34300  1.000 67.78000  ? 56  GLU D OE2 1 
ATOM   416  N N   . GLU A 1 75  ? -1.53900  14.48000 23.45900  1.000 38.66000  ? 57  GLU D N   1 
ATOM   417  C CA  . GLU A 1 75  ? -1.30300  13.67400 22.26600  1.000 42.66000  ? 57  GLU D CA  1 
ATOM   418  C C   . GLU A 1 75  ? -0.30500  14.34500 21.33300  1.000 39.37000  ? 57  GLU D C   1 
ATOM   419  O O   . GLU A 1 75  ? 0.50000   13.66600 20.68400  1.000 41.92000  ? 57  GLU D O   1 
ATOM   420  C CB  . GLU A 1 75  ? -2.62200  13.41700 21.53800  1.000 50.94000  ? 57  GLU D CB  1 
ATOM   421  C CG  . GLU A 1 75  ? -3.60800  12.56500 22.31400  1.000 50.95000  ? 57  GLU D CG  1 
ATOM   422  C CD  . GLU A 1 75  ? -4.96200  12.49300 21.63900  1.000 61.92000  ? 57  GLU D CD  1 
ATOM   423  O OE1 . GLU A 1 75  ? -5.22600  13.32800 20.74800  1.000 58.37000  ? 57  GLU D OE1 1 
ATOM   424  O OE2 . GLU A 1 75  ? -5.76200  11.60400 21.99800  1.000 91.57000  ? 57  GLU D OE2 1 
ATOM   425  N N   . ALA A 1 76  ? -0.34200  15.67700 21.25000  1.000 40.98000  ? 58  ALA D N   1 
ATOM   426  C CA  . ALA A 1 76  ? 0.58300   16.38500 20.37400  1.000 35.38000  ? 58  ALA D CA  1 
ATOM   427  C C   . ALA A 1 76  ? 2.01500   16.28600 20.88700  1.000 38.07000  ? 58  ALA D C   1 
ATOM   428  O O   . ALA A 1 76  ? 2.95600   16.17300 20.09400  1.000 36.16000  ? 58  ALA D O   1 
ATOM   429  C CB  . ALA A 1 76  ? 0.15800   17.84500 20.23100  1.000 34.05000  ? 58  ALA D CB  1 
ATOM   430  N N   . LEU A 1 77  ? 2.19900   16.32300 22.20900  1.000 40.62000  ? 59  LEU D N   1 
ATOM   431  C CA  . LEU A 1 77  ? 3.53700   16.16300 22.76900  1.000 41.31000  ? 59  LEU D CA  1 
ATOM   432  C C   . LEU A 1 77  ? 4.08300   14.76800 22.49400  1.000 48.04000  ? 59  LEU D C   1 
ATOM   433  O O   . LEU A 1 77  ? 5.28400   14.60000 22.25300  1.000 35.24000  ? 59  LEU D O   1 
ATOM   434  C CB  . LEU A 1 77  ? 3.51700   16.44900 24.27100  1.000 35.51000  ? 59  LEU D CB  1 
ATOM   435  C CG  . LEU A 1 77  ? 3.25700   17.90200 24.67500  1.000 48.06000  ? 59  LEU D CG  1 
ATOM   436  C CD1 . LEU A 1 77  ? 3.03200   18.01000 26.17400  1.000 45.87000  ? 59  LEU D CD1 1 
ATOM   437  C CD2 . LEU A 1 77  ? 4.41000   18.79400 24.23800  1.000 45.90000  ? 59  LEU D CD2 1 
ATOM   438  N N   . LYS A 1 78  ? 3.21500   13.75400 22.52600  1.000 36.20000  ? 60  LYS D N   1 
ATOM   439  C CA  . LYS A 1 78  ? 3.64900   12.40500 22.17700  1.000 45.17000  ? 60  LYS D CA  1 
ATOM   440  C C   . LYS A 1 78  ? 3.94900   12.29700 20.68700  1.000 35.70000  ? 60  LYS D C   1 
ATOM   441  O O   . LYS A 1 78  ? 4.88000   11.59000 20.28300  1.000 36.98000  ? 60  LYS D O   1 
ATOM   442  C CB  . LYS A 1 78  ? 2.58600   11.38700 22.58600  1.000 43.07000  ? 60  LYS D CB  1 
ATOM   443  C CG  . LYS A 1 78  ? 3.03800   9.94400  22.45200  1.000 61.28000  ? 60  LYS D CG  1 
ATOM   444  C CD  . LYS A 1 78  ? 1.90700   8.97500  22.74300  1.000 71.98000  ? 60  LYS D CD  1 
ATOM   445  C CE  . LYS A 1 78  ? 2.42000   7.54700  22.80200  1.000 78.07000  ? 60  LYS D CE  1 
ATOM   446  N NZ  . LYS A 1 78  ? 3.16200   7.17200  21.56700  1.000 81.78000  ? 60  LYS D NZ  1 
ATOM   447  N N   . TYR A 1 79  ? 3.17400   13.01300 19.87300  1.000 36.76000  ? 61  TYR D N   1 
ATOM   448  C CA  . TYR A 1 79  ? 3.44300   13.04500 18.41400  1.000 40.76000  ? 61  TYR D CA  1 
ATOM   449  C C   . TYR A 1 79  ? 4.83100   13.64100 18.17800  1.000 34.75000  ? 61  TYR D C   1 
ATOM   450  O O   . TYR A 1 79  ? 5.58000   13.10900 17.34400  1.000 33.61000  ? 61  TYR D O   1 
ATOM   451  C CB  . TYR A 1 79  ? 2.38800   13.88200 17.69000  1.000 44.01000  ? 61  TYR D CB  1 
ATOM   452  C CG  . TYR A 1 79  ? 2.68200   14.16600 16.24000  1.000 38.77000  ? 61  TYR D CG  1 
ATOM   453  C CD1 . TYR A 1 79  ? 2.66100   13.15700 15.29400  1.000 41.23000  ? 61  TYR D CD1 1 
ATOM   454  C CD2 . TYR A 1 79  ? 3.00400   15.44400 15.81600  1.000 34.70000  ? 61  TYR D CD2 1 
ATOM   455  C CE1 . TYR A 1 79  ? 2.93400   13.41200 13.96100  1.000 40.37000  ? 61  TYR D CE1 1 
ATOM   456  C CE2 . TYR A 1 79  ? 3.28400   15.71400 14.48800  1.000 39.49000  ? 61  TYR D CE2 1 
ATOM   457  C CZ  . TYR A 1 79  ? 3.24400   14.69600 13.55500  1.000 40.84000  ? 61  TYR D CZ  1 
ATOM   458  O OH  . TYR A 1 79  ? 3.51900   14.95800 12.23600  1.000 49.48000  ? 61  TYR D OH  1 
ATOM   459  N N   . ILE A 1 80  ? 5.14600   14.72300 18.89200  1.000 36.26000  ? 62  ILE D N   1 
ATOM   460  C CA  . ILE A 1 80  ? 6.44600   15.36400 18.72100  1.000 29.96000  ? 62  ILE D CA  1 
ATOM   461  C C   . ILE A 1 80  ? 7.56900   14.39600 19.06800  1.000 40.80000  ? 62  ILE D C   1 
ATOM   462  O O   . ILE A 1 80  ? 8.57800   14.31100 18.35700  1.000 27.87000  ? 62  ILE D O   1 
ATOM   463  C CB  . ILE A 1 80  ? 6.51800   16.64800 19.56800  1.000 29.90000  ? 62  ILE D CB  1 
ATOM   464  C CG1 . ILE A 1 80  ? 5.54700   17.69900 19.02700  1.000 35.02000  ? 62  ILE D CG1 1 
ATOM   465  C CG2 . ILE A 1 80  ? 7.93800   17.19300 19.60300  1.000 28.93000  ? 62  ILE D CG2 1 
ATOM   466  C CD1 . ILE A 1 80  ? 5.42900   18.92700 19.89800  1.000 35.04000  ? 62  ILE D CD1 1 
ATOM   467  N N   . ASN A 1 81  ? 7.40700   13.63800 20.15500  1.000 32.32000  ? 63  ASN D N   1 
ATOM   468  C CA  . ASN A 1 81  ? 8.44500   12.70200 20.56800  1.000 39.83000  ? 63  ASN D CA  1 
ATOM   469  C C   . ASN A 1 81  ? 8.62600   11.55300 19.58300  1.000 34.15000  ? 63  ASN D C   1 
ATOM   470  O O   . ASN A 1 81  ? 9.70300   10.94800 19.55200  1.000 32.47000  ? 63  ASN D O   1 
ATOM   471  C CB  . ASN A 1 81  ? 8.13200   12.15400 21.96300  1.000 38.84000  ? 63  ASN D CB  1 
ATOM   472  C CG  . ASN A 1 81  ? 8.21600   13.21800 23.04100  1.000 48.49000  ? 63  ASN D CG  1 
ATOM   473  O OD1 . ASN A 1 81  ? 8.86700   14.24800 22.86500  1.000 53.05000  ? 63  ASN D OD1 1 
ATOM   474  N ND2 . ASN A 1 81  ? 7.55900   12.97000 24.16900  1.000 41.25000  ? 63  ASN D ND2 1 
ATOM   475  N N   . ASP A 1 82  ? 7.61200   11.24500 18.77800  1.000 25.42000  ? 64  ASP D N   1 
ATOM   476  C CA  . ASP A 1 82  ? 7.69400   10.16300 17.80500  1.000 38.44000  ? 64  ASP D CA  1 
ATOM   477  C C   . ASP A 1 82  ? 8.16800   10.62200 16.43200  1.000 37.34000  ? 64  ASP D C   1 
ATOM   478  O O   . ASP A 1 82  ? 8.22200   9.80300  15.50900  1.000 48.32000  ? 64  ASP D O   1 
ATOM   479  C CB  . ASP A 1 82  ? 6.33400   9.47200  17.67000  1.000 34.39000  ? 64  ASP D CB  1 
ATOM   480  C CG  . ASP A 1 82  ? 6.02600   8.55700  18.83900  1.000 74.18000  ? 64  ASP D CG  1 
ATOM   481  O OD1 . ASP A 1 82  ? 6.92700   8.33900  19.67600  1.000 61.26000  ? 64  ASP D OD1 1 
ATOM   482  O OD2 . ASP A 1 82  ? 4.88500   8.05600  18.92000  1.000 82.49000  ? 64  ASP D OD2 1 
ATOM   483  N N   . LEU A 1 83  ? 8.51000   11.89800 16.27400  1.000 40.23000  ? 65  LEU D N   1 
ATOM   484  C CA  . LEU A 1 83  ? 8.94100   12.39500 14.97800  1.000 34.25000  ? 65  LEU D CA  1 
ATOM   485  C C   . LEU A 1 83  ? 10.37900  11.97400 14.68100  1.000 31.55000  ? 65  LEU D C   1 
ATOM   486  O O   . LEU A 1 83  ? 11.20700  11.87700 15.59000  1.000 34.88000  ? 65  LEU D O   1 
ATOM   487  C CB  . LEU A 1 83  ? 8.83300   13.91400 14.92600  1.000 40.67000  ? 65  LEU D CB  1 
ATOM   488  C CG  . LEU A 1 83  ? 7.42400   14.48700 14.78600  1.000 34.93000  ? 65  LEU D CG  1 
ATOM   489  C CD1 . LEU A 1 83  ? 7.46700   16.00200 14.87200  1.000 33.89000  ? 65  LEU D CD1 1 
ATOM   490  C CD2 . LEU A 1 83  ? 6.79900   14.03500 13.47400  1.000 37.48000  ? 65  LEU D CD2 1 
ATOM   491  N N   . PRO A 1 84  ? 10.69600  11.71700 13.41300  1.000 41.38000  ? 66  PRO D N   1 
ATOM   492  C CA  . PRO A 1 84  ? 12.07800  11.39100 13.02100  1.000 42.72000  ? 66  PRO D CA  1 
ATOM   493  C C   . PRO A 1 84  ? 12.93500  12.63900 12.83300  1.000 46.87000  ? 66  PRO D C   1 
ATOM   494  O O   . PRO A 1 84  ? 13.44900  12.92200 11.74700  1.000 42.93000  ? 66  PRO D O   1 
ATOM   495  C CB  . PRO A 1 84  ? 11.86800  10.61800 11.71300  1.000 33.34000  ? 66  PRO D CB  1 
ATOM   496  C CG  . PRO A 1 84  ? 10.65400  11.25100 11.11900  1.000 47.06000  ? 66  PRO D CG  1 
ATOM   497  C CD  . PRO A 1 84  ? 9.75800   11.60600 12.28100  1.000 40.77000  ? 66  PRO D CD  1 
ATOM   498  N N   . ILE A 1 85  ? 13.09300  13.40700 13.91100  1.000 41.35000  ? 67  ILE D N   1 
ATOM   499  C CA  . ILE A 1 85  ? 13.82400  14.66600 13.88500  1.000 38.00000  ? 67  ILE D CA  1 
ATOM   500  C C   . ILE A 1 85  ? 14.79400  14.69800 15.06100  1.000 42.13000  ? 67  ILE D C   1 
ATOM   501  O O   . ILE A 1 85  ? 14.79600  13.81600 15.92100  1.000 38.96000  ? 67  ILE D O   1 
ATOM   502  C CB  . ILE A 1 85  ? 12.88300  15.88800 13.92200  1.000 42.54000  ? 67  ILE D CB  1 
ATOM   503  C CG1 . ILE A 1 85  ? 12.02100  15.85800 15.18500  1.000 32.86000  ? 67  ILE D CG1 1 
ATOM   504  C CG2 . ILE A 1 85  ? 12.00500  15.92400 12.67800  1.000 30.99000  ? 67  ILE D CG2 1 
ATOM   505  C CD1 . ILE A 1 85  ? 11.04700  17.01200 15.28800  1.000 35.61000  ? 67  ILE D CD1 1 
ATOM   506  N N   . SER A 1 86  ? 15.62000  15.74200 15.09100  1.000 36.43000  ? 68  SER D N   1 
ATOM   507  C CA  . SER A 1 86  ? 16.64800  15.86500 16.11300  1.000 39.21000  ? 68  SER D CA  1 
ATOM   508  C C   . SER A 1 86  ? 16.03200  16.18700 17.47300  1.000 43.70000  ? 68  SER D C   1 
ATOM   509  O O   . SER A 1 86  ? 14.88300  16.62700 17.58100  1.000 37.33000  ? 68  SER D O   1 
ATOM   510  C CB  . SER A 1 86  ? 17.65600  16.94900 15.73200  1.000 50.61000  ? 68  SER D CB  1 
ATOM   511  O OG  . SER A 1 86  ? 17.09100  18.24200 15.86400  1.000 48.48000  ? 68  SER D OG  1 
ATOM   512  N N   . ASN A 1 87  ? 16.81000  15.97500 18.52600  1.000 27.76000  ? 69  ASN D N   1 
ATOM   513  C CA  . ASN A 1 87  ? 16.30900  16.20300 19.89500  1.000 30.90000  ? 69  ASN D CA  1 
ATOM   514  C C   . ASN A 1 87  ? 16.07900  17.69400 20.12700  1.000 36.80000  ? 69  ASN D C   1 
ATOM   515  O O   . ASN A 1 87  ? 15.17200  18.04600 20.86400  1.000 41.62000  ? 69  ASN D O   1 
ATOM   516  C CB  . ASN A 1 87  ? 17.28500  15.59800 20.89400  1.000 46.60000  ? 69  ASN D CB  1 
ATOM   517  C CG  . ASN A 1 87  ? 17.38900  14.09300 20.81300  1.000 52.35000  ? 69  ASN D CG  1 
ATOM   518  O OD1 . ASN A 1 87  ? 16.76700  13.46600 19.96200  1.000 55.82000  ? 69  ASN D OD1 1 
ATOM   519  N ND2 . ASN A 1 87  ? 18.17800  13.51100 21.69700  1.000 39.77000  ? 69  ASN D ND2 1 
ATOM   520  N N   . ASP A 1 88  ? 16.88100  18.52400 19.48600  1.000 45.41000  ? 70  ASP D N   1 
ATOM   521  C CA  . ASP A 1 88  ? 16.76400  19.99200 19.64700  1.000 42.51000  ? 70  ASP D CA  1 
ATOM   522  C C   . ASP A 1 88  ? 15.49500  20.45500 18.93100  1.000 37.26000  ? 70  ASP D C   1 
ATOM   523  O O   . ASP A 1 88  ? 14.84300  21.35800 19.44300  1.000 41.04000  ? 70  ASP D O   1 
ATOM   524  C CB  . ASP A 1 88  ? 18.07300  20.66800 19.23900  1.000 42.23000  ? 70  ASP D CB  1 
ATOM   525  C CG  . ASP A 1 88  ? 19.23400  20.37600 20.16700  1.000 46.98000  ? 70  ASP D CG  1 
ATOM   526  O OD1 . ASP A 1 88  ? 18.99400  20.21800 21.36500  1.000 47.85000  ? 70  ASP D OD1 1 
ATOM   527  O OD2 . ASP A 1 88  ? 20.36500  20.32000 19.67600  1.000 78.07000  ? 70  ASP D OD2 1 
ATOM   528  N N   . ALA A 1 89  ? 15.14400  19.81100 17.82600  1.000 39.99000  ? 71  ALA D N   1 
ATOM   529  C CA  . ALA A 1 89  ? 13.87800  20.14100 17.18200  1.000 39.82000  ? 71  ALA D CA  1 
ATOM   530  C C   . ALA A 1 89  ? 12.69700  19.75500 18.06300  1.000 45.28000  ? 71  ALA D C   1 
ATOM   531  O O   . ALA A 1 89  ? 11.70400  20.48700 18.13600  1.000 40.47000  ? 71  ALA D O   1 
ATOM   532  C CB  . ALA A 1 89  ? 13.78500  19.45000 15.82200  1.000 38.35000  ? 71  ALA D CB  1 
ATOM   533  N N   . LYS A 1 90  ? 12.78700  18.61000 18.74300  1.000 35.75000  ? 72  LYS D N   1 
ATOM   534  C CA  . LYS A 1 90  ? 11.70900  18.20100 19.63600  1.000 36.22000  ? 72  LYS D CA  1 
ATOM   535  C C   . LYS A 1 90  ? 11.60800  19.12700 20.84200  1.000 43.89000  ? 72  LYS D C   1 
ATOM   536  O O   . LYS A 1 90  ? 10.50300  19.48200 21.26800  1.000 39.15000  ? 72  LYS D O   1 
ATOM   537  C CB  . LYS A 1 90  ? 11.91400  16.75300 20.07600  1.000 28.16000  ? 72  LYS D CB  1 
ATOM   538  C CG  . LYS A 1 90  ? 11.75400  15.75200 18.94700  1.000 36.61000  ? 72  LYS D CG  1 
ATOM   539  C CD  . LYS A 1 90  ? 11.93700  14.33000 19.43900  1.000 33.33000  ? 72  LYS D CD  1 
ATOM   540  C CE  . LYS A 1 90  ? 11.72300  13.33500 18.31500  1.000 41.92000  ? 72  LYS D CE  1 
ATOM   541  N NZ  . LYS A 1 90  ? 11.96100  11.93400 18.75800  1.000 33.47000  ? 72  LYS D NZ  1 
ATOM   542  N N   . LYS A 1 91  ? 12.75000  19.53400 21.40300  1.000 44.36000  ? 73  LYS D N   1 
ATOM   543  C CA  . LYS A 1 91  ? 12.73100  20.48900 22.50700  1.000 44.53000  ? 73  LYS D CA  1 
ATOM   544  C C   . LYS A 1 91  ? 12.19200  21.84000 22.05700  1.000 45.27000  ? 73  LYS D C   1 
ATOM   545  O O   . LYS A 1 91  ? 11.46600  22.50900 22.80200  1.000 47.58000  ? 73  LYS D O   1 
ATOM   546  C CB  . LYS A 1 91  ? 14.13400  20.64300 23.09300  1.000 56.60000  ? 73  LYS D CB  1 
ATOM   547  C CG  . LYS A 1 91  ? 14.53000  19.54000 24.05600  1.000 66.20000  ? 73  LYS D CG  1 
ATOM   548  N N   . LEU A 1 92  ? 12.54200  22.25000 20.83800  1.000 43.54000  ? 74  LEU D N   1 
ATOM   549  C CA  . LEU A 1 92  ? 12.03600  23.53900 20.29900  1.000 33.95000  ? 74  LEU D CA  1 
ATOM   550  C C   . LEU A 1 92  ? 10.51400  23.45900 20.18500  1.000 44.65000  ? 74  LEU D C   1 
ATOM   551  O O   . LEU A 1 92  ? 9.84000   24.41200 20.59800  1.000 43.75000  ? 74  LEU D O   1 
ATOM   552  C CB  . LEU A 1 92  ? 12.67000  23.80500 18.93200  1.000 34.58000  ? 74  LEU D CB  1 
ATOM   553  C CG  . LEU A 1 92  ? 12.27700  25.11900 18.26000  1.000 45.03000  ? 74  LEU D CG  1 
ATOM   554  C CD1 . LEU A 1 92  ? 12.78300  26.30800 19.05900  1.000 49.02000  ? 74  LEU D CD1 1 
ATOM   555  C CD2 . LEU A 1 92  ? 12.80700  25.17400 16.83600  1.000 37.67000  ? 74  LEU D CD2 1 
ATOM   556  N N   . MET A 1 93  ? 10.00300  22.35600 19.64100  1.000 36.98000  ? 75  MET D N   1 
ATOM   557  C CA  . MET A 1 93  ? 8.55900   22.21800 19.47800  1.000 42.84000  ? 75  MET D CA  1 
ATOM   558  C C   . MET A 1 93  ? 7.85900   22.08900 20.82600  1.000 37.36000  ? 75  MET D C   1 
ATOM   559  O O   . MET A 1 93  ? 6.80100   22.69100 21.04000  1.000 36.13000  ? 75  MET D O   1 
ATOM   560  C CB  . MET A 1 93  ? 8.24000   21.01000 18.59600  1.000 43.72000  ? 75  MET D CB  1 
ATOM   561  C CG  . MET A 1 93  ? 8.71400   21.13300 17.15600  1.000 44.11000  ? 75  MET D CG  1 
ATOM   562  S SD  . MET A 1 93  ? 8.27400   19.68800 16.16900  1.000 43.54000  ? 75  MET D SD  1 
ATOM   563  C CE  . MET A 1 93  ? 9.03000   20.10300 14.59900  1.000 37.84000  ? 75  MET D CE  1 
ATOM   564  N N   . SER A 1 94  ? 8.43300   21.31000 21.74600  1.000 43.12000  ? 76  SER D N   1 
ATOM   565  C CA  . SER A 1 94  ? 7.77600   21.07600 23.02900  1.000 39.46000  ? 76  SER D CA  1 
ATOM   566  C C   . SER A 1 94  ? 7.73800   22.34100 23.87800  1.000 36.52000  ? 76  SER D C   1 
ATOM   567  O O   . SER A 1 94  ? 6.74100   22.60500 24.56100  1.000 52.08000  ? 76  SER D O   1 
ATOM   568  C CB  . SER A 1 94  ? 8.48000   19.94700 23.78000  1.000 40.83000  ? 76  SER D CB  1 
ATOM   569  O OG  . SER A 1 94  ? 8.51400   18.76000 23.00600  1.000 56.43000  ? 76  SER D OG  1 
ATOM   570  N N   . ASN A 1 95  ? 8.80800   23.13700 23.85000  1.000 36.75000  ? 77  ASN D N   1 
ATOM   571  C CA  . ASN A 1 95  ? 8.85200   24.34100 24.67200  1.000 46.64000  ? 77  ASN D CA  1 
ATOM   572  C C   . ASN A 1 95  ? 7.95000   25.45100 24.14400  1.000 46.35000  ? 77  ASN D C   1 
ATOM   573  O O   . ASN A 1 95  ? 7.63500   26.37900 24.89600  1.000 44.78000  ? 77  ASN D O   1 
ATOM   574  C CB  . ASN A 1 95  ? 10.28700  24.85800 24.78200  1.000 47.95000  ? 77  ASN D CB  1 
ATOM   575  C CG  . ASN A 1 95  ? 11.17800  23.94000 25.59400  1.000 51.02000  ? 77  ASN D CG  1 
ATOM   576  O OD1 . ASN A 1 95  ? 10.70300  23.18600 26.44300  1.000 68.25000  ? 77  ASN D OD1 1 
ATOM   577  N ND2 . ASN A 1 95  ? 12.48000  24.00400 25.34100  1.000 65.79000  ? 77  ASN D ND2 1 
ATOM   578  N N   . ASN A 1 96  ? 7.52800   25.38500 22.88100  1.000 43.23000  ? 78  ASN D N   1 
ATOM   579  C CA  . ASN A 1 96  ? 6.73700   26.45200 22.28200  1.000 43.44000  ? 78  ASN D CA  1 
ATOM   580  C C   . ASN A 1 96  ? 5.35900   26.01200 21.80500  1.000 43.01000  ? 78  ASN D C   1 
ATOM   581  O O   . ASN A 1 96  ? 4.62600   26.83900 21.24900  1.000 45.55000  ? 78  ASN D O   1 
ATOM   582  C CB  . ASN A 1 96  ? 7.49700   27.08100 21.10500  1.000 44.19000  ? 78  ASN D CB  1 
ATOM   583  C CG  . ASN A 1 96  ? 8.80700   27.71500 21.53000  1.000 46.68000  ? 78  ASN D CG  1 
ATOM   584  O OD1 . ASN A 1 96  ? 8.82200   28.78100 22.14500  1.000 63.04000  ? 78  ASN D OD1 1 
ATOM   585  N ND2 . ASN A 1 96  ? 9.91500   27.06400 21.19800  1.000 53.99000  ? 78  ASN D ND2 1 
ATOM   586  N N   . ILE A 1 97  ? 4.97700   24.74900 22.00900  1.000 52.36000  ? 79  ILE D N   1 
ATOM   587  C CA  . ILE A 1 97  ? 3.69300   24.27700 21.49700  1.000 41.34000  ? 79  ILE D CA  1 
ATOM   588  C C   . ILE A 1 97  ? 2.53100   24.96100 22.21100  1.000 42.78000  ? 79  ILE D C   1 
ATOM   589  O O   . ILE A 1 97  ? 1.43600   25.08500 21.64700  1.000 45.53000  ? 79  ILE D O   1 
ATOM   590  C CB  . ILE A 1 97  ? 3.60900   22.74200 21.61000  1.000 44.31000  ? 79  ILE D CB  1 
ATOM   591  C CG1 . ILE A 1 97  ? 2.37600   22.20900 20.87700  1.000 44.43000  ? 79  ILE D CG1 1 
ATOM   592  C CG2 . ILE A 1 97  ? 3.59500   22.30500 23.06900  1.000 44.96000  ? 79  ILE D CG2 1 
ATOM   593  C CD1 . ILE A 1 97  ? 2.23900   20.70600 20.93600  1.000 49.18000  ? 79  ILE D CD1 1 
ATOM   594  N N   . HIS A 1 98  ? 2.74400   25.43300 23.44200  1.000 43.69000  ? 80  HIS D N   1 
ATOM   595  C CA  . HIS A 1 98  ? 1.65600   26.04700 24.19700  1.000 40.22000  ? 80  HIS D CA  1 
ATOM   596  C C   . HIS A 1 98  ? 1.22700   27.37600 23.59000  1.000 58.14000  ? 80  HIS D C   1 
ATOM   597  O O   . HIS A 1 98  ? 0.08000   27.79900 23.77500  1.000 46.23000  ? 80  HIS D O   1 
ATOM   598  C CB  . HIS A 1 98  ? 2.07500   26.24500 25.65200  1.000 59.52000  ? 80  HIS D CB  1 
ATOM   599  C CG  . HIS A 1 98  ? 3.15700   27.26400 25.83100  1.000 43.96000  ? 80  HIS D CG  1 
ATOM   600  N ND1 . HIS A 1 98  ? 4.48900   26.98000 25.62400  1.000 68.29000  ? 80  HIS D ND1 1 
ATOM   601  C CD2 . HIS A 1 98  ? 3.10200   28.56700 26.19400  1.000 56.81000  ? 80  HIS D CD2 1 
ATOM   602  C CE1 . HIS A 1 98  ? 5.21000   28.06400 25.85300  1.000 47.12000  ? 80  HIS D CE1 1 
ATOM   603  N NE2 . HIS A 1 98  ? 4.39200   29.04100 26.20000  1.000 61.36000  ? 80  HIS D NE2 1 
ATOM   604  N N   . LYS A 1 99  ? 2.11900   28.01100 22.83000  1.000 47.60000  ? 81  LYS D N   1 
ATOM   605  C CA  . LYS A 1 99  ? 1.79800   29.32200 22.20700  1.000 49.80000  ? 81  LYS D CA  1 
ATOM   606  C C   . LYS A 1 99  ? 0.70700   29.13600 21.14800  1.000 53.36000  ? 81  LYS D C   1 
ATOM   607  O O   . LYS A 1 99  ? -0.03100  30.09800 20.89200  1.000 65.03000  ? 81  LYS D O   1 
ATOM   608  C CB  . LYS A 1 99  ? 3.05800   29.94900 21.61000  1.000 42.42000  ? 81  LYS D CB  1 
ATOM   609  C CG  . LYS A 1 99  ? 4.13800   30.29900 22.62100  1.000 46.63000  ? 81  LYS D CG  1 
ATOM   610  C CD  . LYS A 1 99  ? 5.43100   30.71100 21.96600  1.000 61.09000  ? 81  LYS D CD  1 
ATOM   611  C CE  . LYS A 1 99  ? 6.44600   31.26000 22.94300  1.000 65.88000  ? 81  LYS D CE  1 
ATOM   612  N NZ  . LYS A 1 99  ? 7.69600   31.65000 22.25200  1.000 61.84000  ? 81  LYS D NZ  1 
ATOM   613  N N   . ALA A 1 100 ? 0.59900   27.93700 20.57900  1.000 49.20000  ? 82  ALA D N   1 
ATOM   614  C CA  . ALA A 1 100 ? -0.40700  27.68000 19.52600  1.000 48.45000  ? 82  ALA D CA  1 
ATOM   615  C C   . ALA A 1 100 ? -1.78700  27.48800 20.15800  1.000 42.43000  ? 82  ALA D C   1 
ATOM   616  O O   . ALA A 1 100 ? -2.77100  27.43600 19.40800  1.000 54.63000  ? 82  ALA D O   1 
ATOM   617  C CB  . ALA A 1 100 ? -0.00300  26.48000 18.71500  1.000 47.94000  ? 82  ALA D CB  1 
ATOM   618  N N   . LEU A 1 101 ? -1.85100  27.38500 21.48500  1.000 54.61000  ? 83  LEU D N   1 
ATOM   619  C CA  . LEU A 1 101 ? -3.13300  27.16500 22.14000  1.000 64.26000  ? 83  LEU D CA  1 
ATOM   620  C C   . LEU A 1 101 ? -3.95100  28.44100 22.27200  1.000 71.52000  ? 83  LEU D C   1 
ATOM   621  O O   . LEU A 1 101 ? -5.16000  28.36200 22.51600  1.000 77.84000  ? 83  LEU D O   1 
ATOM   622  C CB  . LEU A 1 101 ? -2.91900  26.54600 23.52200  1.000 59.64000  ? 83  LEU D CB  1 
ATOM   623  C CG  . LEU A 1 101 ? -2.42900  25.09900 23.52400  1.000 73.09000  ? 83  LEU D CG  1 
ATOM   624  C CD1 . LEU A 1 101 ? -2.09700  24.64500 24.93300  1.000 59.47000  ? 83  LEU D CD1 1 
ATOM   625  C CD2 . LEU A 1 101 ? -3.47900  24.19500 22.90500  1.000 68.64000  ? 83  LEU D CD2 1 
ATOM   626  N N   . GLU A 1 102 ? -3.29300  29.58800 22.09300  1.000 62.63000  ? 84  GLU D N   1 
ATOM   627  C CA  . GLU A 1 102 ? -4.00300  30.88800 22.12400  1.000 72.87000  ? 84  GLU D CA  1 
ATOM   628  C C   . GLU A 1 102 ? -4.69100  31.09000 20.77300  1.000 72.86000  ? 84  GLU D C   1 
ATOM   629  O O   . GLU A 1 102 ? -3.99200  31.07000 19.74800  1.000 75.94000  ? 84  GLU D O   1 
ATOM   630  C CB  . GLU A 1 102 ? -3.00800  32.01500 22.38600  1.000 73.04000  ? 84  GLU D CB  1 
ATOM   631  C CG  . GLU A 1 102 ? -2.01600  31.69700 23.49000  1.000 88.64000  ? 84  GLU D CG  1 
ATOM   632  N N   . PRO A 1 103 ? -6.02700  31.27200 20.72800  1.000 85.99000  ? 85  PRO D N   1 
ATOM   633  C CA  . PRO A 1 103 ? -6.74400  31.41700 19.46200  1.000 73.21000  ? 85  PRO D CA  1 
ATOM   634  C C   . PRO A 1 103 ? -6.20600  32.59100 18.63300  1.000 69.97000  ? 85  PRO D C   1 
ATOM   635  O O   . PRO A 1 103 ? -5.98000  33.64600 19.19100  1.000 61.75000  ? 85  PRO D O   1 
ATOM   636  C CB  . PRO A 1 103 ? -8.18400  31.70300 19.90300  1.000 90.33000  ? 85  PRO D CB  1 
ATOM   637  C CG  . PRO A 1 103 ? -8.27800  31.08700 21.27900  1.000 94.96000  ? 85  PRO D CG  1 
ATOM   638  C CD  . PRO A 1 103 ? -6.91500  31.32600 21.89000  1.000 88.28000  ? 85  PRO D CD  1 
ATOM   639  N N   . GLY A 1 104 ? -6.01200  32.37300 17.33000  1.000 73.47000  ? 86  GLY D N   1 
ATOM   640  C CA  . GLY A 1 104 ? -5.47900  33.42900 16.44800  1.000 66.16000  ? 86  GLY D CA  1 
ATOM   641  C C   . GLY A 1 104 ? -3.96300  33.39600 16.37200  1.000 72.66000  ? 86  GLY D C   1 
ATOM   642  O O   . GLY A 1 104 ? -3.39000  34.30200 15.75000  1.000 75.65000  ? 86  GLY D O   1 
ATOM   643  N N   . ARG A 1 105 ? -3.33400  32.38600 16.96700  1.000 66.74000  ? 87  ARG D N   1 
ATOM   644  C CA  . ARG A 1 105 ? -1.85300  32.32100 17.00000  1.000 66.24000  ? 87  ARG D CA  1 
ATOM   645  C C   . ARG A 1 105 ? -1.38800  31.05900 16.27200  1.000 63.56000  ? 87  ARG D C   1 
ATOM   646  O O   . ARG A 1 105 ? -1.94000  29.98800 16.53600  1.000 78.68000  ? 87  ARG D O   1 
ATOM   647  C CB  . ARG A 1 105 ? -1.36500  32.39900 18.44400  1.000 63.45000  ? 87  ARG D CB  1 
ATOM   648  C CG  . ARG A 1 105 ? 0.01400   33.01200 18.62000  1.000 83.03000  ? 87  ARG D CG  1 
ATOM   649  C CD  . ARG A 1 105 ? 0.19100   33.25800 20.10200  1.000 92.18000  ? 87  ARG D CD  1 
ATOM   650  N NE  . ARG A 1 105 ? 1.56600   33.37800 20.55300  1.000 106.41000 ? 87  ARG D NE  1 
ATOM   651  C CZ  . ARG A 1 105 ? 1.91400   33.51500 21.82500  1.000 111.51000 ? 87  ARG D CZ  1 
ATOM   652  N NH1 . ARG A 1 105 ? 1.02800   33.28400 22.77900  1.000 113.66000 ? 87  ARG D NH1 1 
ATOM   653  N NH2 . ARG A 1 105 ? 3.14200   33.88300 22.14200  1.000 120.87000 ? 87  ARG D NH2 1 
ATOM   654  N N   . THR A 1 106 ? -0.43500  31.20800 15.36000  1.000 61.39000  ? 88  THR D N   1 
ATOM   655  C CA  . THR A 1 106 ? 0.09800   30.04600 14.60500  1.000 52.63000  ? 88  THR D CA  1 
ATOM   656  C C   . THR A 1 106 ? 1.61200   29.95400 14.80700  1.000 67.62000  ? 88  THR D C   1 
ATOM   657  O O   . THR A 1 106 ? 2.28900   30.98400 14.65300  1.000 65.46000  ? 88  THR D O   1 
ATOM   658  C CB  . THR A 1 106 ? -0.26700  30.13500 13.12000  1.000 71.70000  ? 88  THR D CB  1 
ATOM   659  O OG1 . THR A 1 106 ? -1.69000  30.17700 13.01600  1.000 69.72000  ? 88  THR D OG1 1 
ATOM   660  C CG2 . THR A 1 106 ? 0.27200   28.97700 12.31000  1.000 63.11000  ? 88  THR D CG2 1 
ATOM   661  N N   . VAL A 1 107 ? 2.10700   28.76700 15.15100  1.000 55.53000  ? 89  VAL D N   1 
ATOM   662  C CA  . VAL A 1 107 ? 3.56500   28.55300 15.36400  1.000 45.21000  ? 89  VAL D CA  1 
ATOM   663  C C   . VAL A 1 107 ? 4.12600   27.71700 14.21100  1.000 42.83000  ? 89  VAL D C   1 
ATOM   664  O O   . VAL A 1 107 ? 3.55400   26.68500 13.88700  1.000 44.81000  ? 89  VAL D O   1 
ATOM   665  C CB  . VAL A 1 107 ? 3.86500   27.95500 16.74900  1.000 43.07000  ? 89  VAL D CB  1 
ATOM   666  C CG1 . VAL A 1 107 ? 5.33900   28.05500 17.08900  1.000 43.54000  ? 89  VAL D CG1 1 
ATOM   667  C CG2 . VAL A 1 107 ? 3.03800   28.62800 17.82800  1.000 49.65000  ? 89  VAL D CG2 1 
ATOM   668  N N   . VAL A 1 108 ? 5.22500   28.18100 13.64000  1.000 46.09000  ? 90  VAL D N   1 
ATOM   669  C CA  . VAL A 1 108 ? 5.83600   27.49500 12.47500  1.000 48.94000  ? 90  VAL D CA  1 
ATOM   670  C C   . VAL A 1 108 ? 7.24900   27.02800 12.81100  1.000 40.69000  ? 90  VAL D C   1 
ATOM   671  O O   . VAL A 1 108 ? 8.00700   27.81300 13.36000  1.000 43.34000  ? 90  VAL D O   1 
ATOM   672  C CB  . VAL A 1 108 ? 5.82100   28.39900 11.23000  1.000 46.65000  ? 90  VAL D CB  1 
ATOM   673  C CG1 . VAL A 1 108 ? 6.14600   27.62200 9.96900   1.000 54.20000  ? 90  VAL D CG1 1 
ATOM   674  C CG2 . VAL A 1 108 ? 4.49600   29.12400 11.07900  1.000 48.66000  ? 90  VAL D CG2 1 
ATOM   675  N N   . PHE A 1 109 ? 7.54300   25.76700 12.52000  1.000 42.79000  ? 91  PHE D N   1 
ATOM   676  C CA  . PHE A 1 109 ? 8.88000   25.21000 12.69600  1.000 34.41000  ? 91  PHE D CA  1 
ATOM   677  C C   . PHE A 1 109 ? 9.37600   24.72000 11.34300  1.000 41.39000  ? 91  PHE D C   1 
ATOM   678  O O   . PHE A 1 109 ? 8.77100   23.82200 10.74800  1.000 35.29000  ? 91  PHE D O   1 
ATOM   679  C CB  . PHE A 1 109 ? 8.87900   24.06400 13.70900  1.000 36.86000  ? 91  PHE D CB  1 
ATOM   680  C CG  . PHE A 1 109 ? 8.31000   24.43300 15.04800  1.000 36.08000  ? 91  PHE D CG  1 
ATOM   681  C CD1 . PHE A 1 109 ? 9.10000   25.04700 16.00400  1.000 33.67000  ? 91  PHE D CD1 1 
ATOM   682  C CD2 . PHE A 1 109 ? 6.98700   24.15600 15.35300  1.000 42.41000  ? 91  PHE D CD2 1 
ATOM   683  C CE1 . PHE A 1 109 ? 8.58200   25.38600 17.23700  1.000 35.43000  ? 91  PHE D CE1 1 
ATOM   684  C CE2 . PHE A 1 109 ? 6.46200   24.49200 16.58500  1.000 37.51000  ? 91  PHE D CE2 1 
ATOM   685  C CZ  . PHE A 1 109 ? 7.26100   25.10600 17.52900  1.000 33.38000  ? 91  PHE D CZ  1 
ATOM   686  N N   . GLY A 1 110 ? 10.49300  25.27500 10.88300  1.000 37.51000  ? 92  GLY D N   1 
ATOM   687  C CA  . GLY A 1 110 ? 11.01900  24.88000 9.56900   1.000 40.74000  ? 92  GLY D CA  1 
ATOM   688  C C   . GLY A 1 110 ? 12.52800  24.95300 9.50000   1.000 42.68000  ? 92  GLY D C   1 
ATOM   689  O O   . GLY A 1 110 ? 13.16800  25.13800 10.54800  1.000 35.34000  ? 92  GLY D O   1 
ATOM   690  N N   . PRO A 1 111 ? 13.12000  24.82400 8.29700   1.000 47.33000  ? 93  PRO D N   1 
ATOM   691  C CA  . PRO A 1 111 ? 14.57400  24.83300 8.14700   1.000 52.56000  ? 93  PRO D CA  1 
ATOM   692  C C   . PRO A 1 111 ? 15.20800  26.11600 8.69500   1.000 58.63000  ? 93  PRO D C   1 
ATOM   693  O O   . PRO A 1 111 ? 16.32100  26.05200 9.16900   1.000 63.06000  ? 93  PRO D O   1 
ATOM   694  C CB  . PRO A 1 111 ? 14.74600  24.77400 6.62400   1.000 60.79000  ? 93  PRO D CB  1 
ATOM   695  C CG  . PRO A 1 111 ? 13.49900  24.08200 6.13300   1.000 56.16000  ? 93  PRO D CG  1 
ATOM   696  C CD  . PRO A 1 111 ? 12.41200  24.62400 7.03200   1.000 48.03000  ? 93  PRO D CD  1 
ATOM   697  N N   . GLU A 1 112 ? 14.47200  27.21700 8.67400   1.000 71.98000  ? 94  GLU D N   1 
ATOM   698  C CA  . GLU A 1 112 ? 15.04500  28.51500 9.10200   1.000 80.82000  ? 94  GLU D CA  1 
ATOM   699  C C   . GLU A 1 112 ? 15.06600  28.57900 10.62300  1.000 73.89000  ? 94  GLU D C   1 
ATOM   700  O O   . GLU A 1 112 ? 16.11600  28.92700 11.17500  1.000 78.13000  ? 94  GLU D O   1 
ATOM   701  C CB  . GLU A 1 112 ? 14.19900  29.66600 8.55800   1.000 77.22000  ? 94  GLU D CB  1 
ATOM   702  C CG  . GLU A 1 112 ? 14.55700  30.07000 7.14500   1.000 92.38000  ? 94  GLU D CG  1 
ATOM   703  N N   . GLY A 1 113 ? 13.93800  28.27000 11.25000  1.000 60.46000  ? 95  GLY D N   1 
ATOM   704  C CA  . GLY A 1 113 ? 13.83200  28.33800 12.71800  1.000 44.88000  ? 95  GLY D CA  1 
ATOM   705  C C   . GLY A 1 113 ? 12.38200  28.32200 13.15600  1.000 52.81000  ? 95  GLY D C   1 
ATOM   706  O O   . GLY A 1 113 ? 11.57900  27.63900 12.50200  1.000 63.67000  ? 95  GLY D O   1 
ATOM   707  N N   . CYS A 1 114 ? 12.06100  29.05300 14.22200  1.000 59.02000  ? 96  CYS D N   1 
ATOM   708  C CA  . CYS A 1 114 ? 10.67000  29.10000 14.73300  1.000 55.48000  ? 96  CYS D CA  1 
ATOM   709  C C   . CYS A 1 114 ? 10.04900  30.43900 14.34600  1.000 52.36000  ? 96  CYS D C   1 
ATOM   710  O O   . CYS A 1 114 ? 10.79200  31.38200 14.10500  1.000 50.07000  ? 96  CYS D O   1 
ATOM   711  C CB  . CYS A 1 114 ? 10.61500  28.88900 16.24200  1.000 49.70000  ? 96  CYS D CB  1 
ATOM   712  S SG  . CYS A 1 114 ? 8.96900   29.11300 16.96000  1.000 65.72000  ? 96  CYS D SG  1 
ATOM   713  N N   . GLU A 1 115 ? 8.72700   30.48300 14.28000  1.000 60.70000  ? 97  GLU D N   1 
ATOM   714  C CA  . GLU A 1 115 ? 8.01500   31.70900 13.85300  1.000 57.09000  ? 97  GLU D CA  1 
ATOM   715  C C   . GLU A 1 115 ? 6.61900   31.72100 14.47100  1.000 56.17000  ? 97  GLU D C   1 
ATOM   716  O O   . GLU A 1 115 ? 5.90500   30.73000 14.31700  1.000 54.61000  ? 97  GLU D O   1 
ATOM   717  C CB  . GLU A 1 115 ? 7.97500   31.76300 12.32700  1.000 62.84000  ? 97  GLU D CB  1 
ATOM   718  C CG  . GLU A 1 115 ? 7.07900   32.82700 11.74400  1.000 72.40000  ? 97  GLU D CG  1 
ATOM   719  C CD  . GLU A 1 115 ? 6.93200   32.62200 10.24900  1.000 83.42000  ? 97  GLU D CD  1 
ATOM   720  O OE1 . GLU A 1 115 ? 7.49900   31.64200 9.73600   1.000 80.61000  ? 97  GLU D OE1 1 
ATOM   721  O OE2 . GLU A 1 115 ? 6.25700   33.43300 9.60800   1.000 87.79000  ? 97  GLU D OE2 1 
ATOM   722  N N   . GLU A 1 116 ? 6.27500   32.80800 15.15800  1.000 59.43000  ? 98  GLU D N   1 
ATOM   723  C CA  . GLU A 1 116 ? 4.92800   32.97700 15.74700  1.000 51.35000  ? 98  GLU D CA  1 
ATOM   724  C C   . GLU A 1 116 ? 4.12900   33.98200 14.91800  1.000 68.23000  ? 98  GLU D C   1 
ATOM   725  O O   . GLU A 1 116 ? 4.47400   35.15800 14.95400  1.000 69.88000  ? 98  GLU D O   1 
ATOM   726  C CB  . GLU A 1 116 ? 5.06400   33.55500 17.14500  1.000 64.56000  ? 98  GLU D CB  1 
ATOM   727  C CG  . GLU A 1 116 ? 5.56400   32.58400 18.18600  1.000 72.40000  ? 98  GLU D CG  1 
ATOM   728  C CD  . GLU A 1 116 ? 5.57200   33.21200 19.56600  1.000 80.30000  ? 98  GLU D CD  1 
ATOM   729  O OE1 . GLU A 1 116 ? 4.50500   33.67300 20.00500  1.000 81.14000  ? 98  GLU D OE1 1 
ATOM   730  O OE2 . GLU A 1 116 ? 6.64200   33.24800 20.19100  1.000 91.32000  ? 98  GLU D OE2 1 
ATOM   731  N N   . ARG A 1 117 ? 3.09400   33.50600 14.23600  1.000 62.21000  ? 99  ARG D N   1 
ATOM   732  C CA  . ARG A 1 117 ? 2.22800   34.42000 13.45400  1.000 70.05000  ? 99  ARG D CA  1 
ATOM   733  C C   . ARG A 1 117 ? 0.97300   34.73200 14.26900  1.000 82.97000  ? 99  ARG D C   1 
ATOM   734  O O   . ARG A 1 117 ? 0.01800   33.94200 14.20500  1.000 89.94000  ? 99  ARG D O   1 
ATOM   735  C CB  . ARG A 1 117 ? 1.88000   33.79100 12.10500  1.000 75.46000  ? 99  ARG D CB  1 
ATOM   736  C CG  . ARG A 1 117 ? 3.07700   33.66300 11.17700  1.000 81.80000  ? 99  ARG D CG  1 
ATOM   737  C CD  . ARG A 1 117 ? 3.01200   32.44200 10.28700  1.000 83.48000  ? 99  ARG D CD  1 
ATOM   738  N NE  . ARG A 1 117 ? 3.97400   32.57600 9.20600   1.000 113.22000 ? 99  ARG D NE  1 
ATOM   739  C CZ  . ARG A 1 117 ? 4.09600   31.73000 8.19200   1.000 103.28000 ? 99  ARG D CZ  1 
ATOM   740  N NH1 . ARG A 1 117 ? 3.46300   30.57200 8.21400   1.000 95.37000  ? 99  ARG D NH1 1 
ATOM   741  N NH2 . ARG A 1 117 ? 4.85600   32.04800 7.15900   1.000 82.33000  ? 99  ARG D NH2 1 
ATOM   742  N N   . ASP A 1 118 ? 0.98500   35.86400 14.98200  1.000 107.56000 ? 100 ASP D N   1 
ATOM   743  C CA  . ASP A 1 118 ? -0.18900  36.27500 15.79900  1.000 113.64000 ? 100 ASP D CA  1 
ATOM   744  C C   . ASP A 1 118 ? -1.24200  36.95600 14.91500  1.000 126.31000 ? 100 ASP D C   1 
ATOM   745  O O   . ASP A 1 118 ? -0.87300  37.45200 13.83900  1.000 135.31000 ? 100 ASP D O   1 
ATOM   746  C CB  . ASP A 1 118 ? 0.23900   37.16600 16.96800  1.000 108.79000 ? 100 ASP D CB  1 
ATOM   747  C CG  . ASP A 1 118 ? -0.57100  36.94000 18.23200  1.000 124.69000 ? 100 ASP D CG  1 
ATOM   748  O OD1 . ASP A 1 118 ? -1.77700  37.25400 18.21700  1.000 133.08000 ? 100 ASP D OD1 1 
ATOM   749  O OD2 . ASP A 1 118 ? 0.01100   36.45300 19.22000  1.000 126.08000 ? 100 ASP D OD2 1 
ATOM   750  N N   . LYS A 1 119 ? -2.50000  36.99000 15.36100  1.000 121.97000 ? 101 LYS D N   1 
ATOM   751  C CA  . LYS A 1 119 ? -3.60400  37.63300 14.60000  1.000 128.15000 ? 101 LYS D CA  1 
ATOM   752  C C   . LYS A 1 119 ? -3.36400  37.46200 13.09700  1.000 142.97000 ? 101 LYS D C   1 
ATOM   753  O O   . LYS A 1 119 ? -4.35600  37.50900 12.35000  1.000 147.64000 ? 101 LYS D O   1 
ATOM   754  C CB  . LYS A 1 119 ? -3.71800  39.10500 15.00800  1.000 122.24000 ? 101 LYS D CB  1 
ATOM   755  C CG  . LYS A 1 119 ? -4.55400  39.37500 16.25100  1.000 113.18000 ? 101 LYS D CG  1 
ATOM   756  C CD  . LYS A 1 119 ? -3.91400  40.36100 17.20400  1.000 113.38000 ? 101 LYS D CD  1 
ATOM   757  C CE  . LYS A 1 119 ? -4.17000  40.03400 18.65900  1.000 104.79000 ? 101 LYS D CE  1 
ATOM   758  N NZ  . LYS A 1 119 ? -3.99600  38.59000 18.93700  1.000 82.75000  ? 101 LYS D NZ  1 
ATOM   759  N N   . GLY A 1 122 ? -0.33600  38.65400 10.43400  1.000 138.88000 ? 104 GLY D N   1 
ATOM   760  C CA  . GLY A 1 122 ? 0.86900   38.13000 9.76600   1.000 132.13000 ? 104 GLY D CA  1 
ATOM   761  C C   . GLY A 1 122 ? 1.87800   37.67400 10.80300  1.000 111.70000 ? 104 GLY D C   1 
ATOM   762  O O   . GLY A 1 122 ? 1.44600   37.27400 11.89800  1.000 108.32000 ? 104 GLY D O   1 
ATOM   763  N N   . ILE A 1 123 ? 3.16600   37.87600 10.53200  1.000 115.71000 ? 105 ILE D N   1 
ATOM   764  C CA  . ILE A 1 123 ? 4.24100   37.46400 11.48000  1.000 102.22000 ? 105 ILE D CA  1 
ATOM   765  C C   . ILE A 1 123 ? 4.27200   38.41800 12.66900  1.000 94.94000  ? 105 ILE D C   1 
ATOM   766  O O   . ILE A 1 123 ? 3.76500   39.52900 12.54000  1.000 114.12000 ? 105 ILE D O   1 
ATOM   767  C CB  . ILE A 1 123 ? 5.61100   37.42400 10.77600  1.000 97.53000  ? 105 ILE D CB  1 
ATOM   768  N N   . ILE A 1 124 ? 4.78000   37.94700 13.80000  1.000 88.46000  ? 106 ILE D N   1 
ATOM   769  C CA  . ILE A 1 124 ? 4.93300   38.82100 14.98800  1.000 84.79000  ? 106 ILE D CA  1 
ATOM   770  C C   . ILE A 1 124 ? 6.33500   38.54800 15.53000  1.000 75.89000  ? 106 ILE D C   1 
ATOM   771  O O   . ILE A 1 124 ? 6.97600   39.50200 15.98200  1.000 78.73000  ? 106 ILE D O   1 
ATOM   772  C CB  . ILE A 1 124 ? 3.81300   38.55100 16.01200  1.000 89.43000  ? 106 ILE D CB  1 
ATOM   773  N N   . LYS A 1 125 ? 6.80200   37.30300 15.42000  1.000 60.18000  ? 107 LYS D N   1 
ATOM   774  C CA  . LYS A 1 125 ? 8.12200   36.95500 15.99600  1.000 65.33000  ? 107 LYS D CA  1 
ATOM   775  C C   . LYS A 1 125 ? 8.79800   35.80600 15.25000  1.000 63.39000  ? 107 LYS D C   1 
ATOM   776  O O   . LYS A 1 125 ? 8.14800   34.79200 15.01400  1.000 62.47000  ? 107 LYS D O   1 
ATOM   777  C CB  . LYS A 1 125 ? 7.98300   36.58000 17.47000  1.000 56.60000  ? 107 LYS D CB  1 
ATOM   778  C CG  . LYS A 1 125 ? 8.16500   37.70800 18.47100  1.000 81.57000  ? 107 LYS D CG  1 
ATOM   779  C CD  . LYS A 1 125 ? 7.92300   37.23800 19.88800  1.000 83.30000  ? 107 LYS D CD  1 
ATOM   780  C CE  . LYS A 1 125 ? 6.55800   36.60700 20.05700  1.000 85.21000  ? 107 LYS D CE  1 
ATOM   781  N NZ  . LYS A 1 125 ? 6.44800   35.87800 21.34200  1.000 91.19000  ? 107 LYS D NZ  1 
ATOM   782  N N   . THR A 1 126 ? 10.08000  35.97600 14.96200  1.000 49.65000  ? 108 THR D N   1 
ATOM   783  C CA  . THR A 1 126 ? 10.88200  34.93600 14.28400  1.000 62.08000  ? 108 THR D CA  1 
ATOM   784  C C   . THR A 1 126 ? 12.19200  34.75900 15.04800  1.000 50.19000  ? 108 THR D C   1 
ATOM   785  O O   . THR A 1 126 ? 12.77000  35.75800 15.44600  1.000 48.98000  ? 108 THR D O   1 
ATOM   786  C CB  . THR A 1 126 ? 11.13600  35.29400 12.81900  1.000 54.23000  ? 108 THR D CB  1 
ATOM   787  O OG1 . THR A 1 126 ? 9.86200   35.50800 12.21900  1.000 56.45000  ? 108 THR D OG1 1 
ATOM   788  C CG2 . THR A 1 126 ? 11.86300  34.20800 12.06600  1.000 55.67000  ? 108 THR D CG2 1 
ATOM   789  N N   . PHE A 1 127 ? 12.57800  33.51400 15.31400  1.000 57.76000  ? 109 PHE D N   1 
ATOM   790  C CA  . PHE A 1 127 ? 13.88000  33.23400 15.96500  1.000 63.95000  ? 109 PHE D CA  1 
ATOM   791  C C   . PHE A 1 127 ? 14.61000  32.24600 15.06100  1.000 57.31000  ? 109 PHE D C   1 
ATOM   792  O O   . PHE A 1 127 ? 13.99500  31.24600 14.65400  1.000 56.73000  ? 109 PHE D O   1 
ATOM   793  C CB  . PHE A 1 127 ? 13.68600  32.66900 17.37200  1.000 59.33000  ? 109 PHE D CB  1 
ATOM   794  N N   . SER A 1 128 ? 15.86900  32.50500 14.75000  1.000 65.33000  ? 110 SER D N   1 
ATOM   795  C CA  . SER A 1 128 ? 16.60000  31.63100 13.80900  1.000 68.34000  ? 110 SER D CA  1 
ATOM   796  C C   . SER A 1 128 ? 17.46500  30.64900 14.57800  1.000 79.72000  ? 110 SER D C   1 
ATOM   797  O O   . SER A 1 128 ? 18.31700  31.11300 15.33700  1.000 93.26000  ? 110 SER D O   1 
ATOM   798  C CB  . SER A 1 128 ? 17.45000  32.42600 12.88900  1.000 80.55000  ? 110 SER D CB  1 
ATOM   799  O OG  . SER A 1 128 ? 16.66200  33.02200 11.87200  1.000 86.34000  ? 110 SER D OG  1 
ATOM   800  N N   . THR A 1 129 ? 17.22200  29.34700 14.42400  1.000 70.94000  ? 111 THR D N   1 
ATOM   801  C CA  . THR A 1 129 ? 18.06000  28.29600 15.05500  1.000 68.98000  ? 111 THR D CA  1 
ATOM   802  C C   . THR A 1 129 ? 18.12600  27.12800 14.08600  1.000 69.98000  ? 111 THR D C   1 
ATOM   803  O O   . THR A 1 129 ? 17.10500  26.87100 13.44600  1.000 54.90000  ? 111 THR D O   1 
ATOM   804  C CB  . THR A 1 129 ? 17.47200  27.76200 16.35800  1.000 77.57000  ? 111 THR D CB  1 
ATOM   805  O OG1 . THR A 1 129 ? 18.23600  26.61200 16.72100  1.000 79.53000  ? 111 THR D OG1 1 
ATOM   806  C CG2 . THR A 1 129 ? 16.00700  27.40000 16.25300  1.000 58.49000  ? 111 THR D CG2 1 
ATOM   807  N N   . ASP A 1 130 ? 19.26100  26.43900 13.99400  1.000 68.85000  ? 112 ASP D N   1 
ATOM   808  C CA  . ASP A 1 130 ? 19.24900  25.28400 13.06600  1.000 78.17000  ? 112 ASP D CA  1 
ATOM   809  C C   . ASP A 1 130 ? 18.98600  24.04500 13.91500  1.000 74.53000  ? 112 ASP D C   1 
ATOM   810  O O   . ASP A 1 130 ? 19.78400  23.76200 14.82400  1.000 65.84000  ? 112 ASP D O   1 
ATOM   811  C CB  . ASP A 1 130 ? 20.53400  25.16100 12.24800  1.000 93.72000  ? 112 ASP D CB  1 
ATOM   812  C CG  . ASP A 1 130 ? 20.50500  23.97300 11.30100  1.000 93.61000  ? 112 ASP D CG  1 
ATOM   813  O OD1 . ASP A 1 130 ? 19.42700  23.69900 10.73900  1.000 105.56000 ? 112 ASP D OD1 1 
ATOM   814  O OD2 . ASP A 1 130 ? 21.55800  23.33000 11.14000  1.000 85.88000  ? 112 ASP D OD2 1 
ATOM   815  N N   . VAL A 1 131 ? 17.88600  23.36500 13.63900  1.000 54.21000  ? 113 VAL D N   1 
ATOM   816  C CA  . VAL A 1 131 ? 17.56200  22.11000 14.36400  1.000 71.40000  ? 113 VAL D CA  1 
ATOM   817  C C   . VAL A 1 131 ? 17.54100  20.99100 13.32000  1.000 62.90000  ? 113 VAL D C   1 
ATOM   818  O O   . VAL A 1 131 ? 16.91600  19.96400 13.57600  1.000 47.63000  ? 113 VAL D O   1 
ATOM   819  C CB  . VAL A 1 131 ? 16.23200  22.24700 15.12500  1.000 59.85000  ? 113 VAL D CB  1 
ATOM   820  C CG1 . VAL A 1 131 ? 16.42000  23.00400 16.42800  1.000 54.09000  ? 113 VAL D CG1 1 
ATOM   821  C CG2 . VAL A 1 131 ? 15.15900  22.89900 14.27200  1.000 38.93000  ? 113 VAL D CG2 1 
ATOM   822  N N   . LYS A 1 132 ? 18.19800  21.22600 12.18100  1.000 60.91000  ? 114 LYS D N   1 
ATOM   823  C CA  . LYS A 1 132 ? 18.29100  20.16800 11.13800  1.000 60.76000  ? 114 LYS D CA  1 
ATOM   824  C C   . LYS A 1 132 ? 16.93300  19.79900 10.53800  1.000 58.94000  ? 114 LYS D C   1 
ATOM   825  O O   . LYS A 1 132 ? 16.81500  18.70000 9.99300   1.000 67.31000  ? 114 LYS D O   1 
ATOM   826  C CB  . LYS A 1 132 ? 19.03900  18.95800 11.70300  1.000 52.93000  ? 114 LYS D CB  1 
ATOM   827  C CG  . LYS A 1 132 ? 20.39300  19.25700 12.33000  1.000 70.46000  ? 114 LYS D CG  1 
ATOM   828  C CD  . LYS A 1 132 ? 20.70500  18.38200 13.52400  1.000 66.60000  ? 114 LYS D CD  1 
ATOM   829  C CE  . LYS A 1 132 ? 20.43300  19.06200 14.84900  1.000 78.26000  ? 114 LYS D CE  1 
ATOM   830  N NZ  . LYS A 1 132 ? 20.79200  18.19300 15.99200  1.000 65.75000  ? 114 LYS D NZ  1 
ATOM   831  N N   . LEU A 1 133 ? 15.97500  20.70800 10.57900  1.000 59.24000  ? 115 LEU D N   1 
ATOM   832  C CA  . LEU A 1 133 ? 14.65300  20.41600 10.04200  1.000 59.38000  ? 115 LEU D CA  1 
ATOM   833  C C   . LEU A 1 133 ? 14.65500  20.56400 8.52600   1.000 55.01000  ? 115 LEU D C   1 
ATOM   834  O O   . LEU A 1 133 ? 15.08700  21.59100 7.99300   1.000 43.42000  ? 115 LEU D O   1 
ATOM   835  C CB  . LEU A 1 133 ? 13.60200  21.33900 10.65900  1.000 56.74000  ? 115 LEU D CB  1 
ATOM   836  C CG  . LEU A 1 133 ? 13.04100  20.92400 12.02100  1.000 54.19000  ? 115 LEU D CG  1 
ATOM   837  C CD1 . LEU A 1 133 ? 11.91800  21.85900 12.44200  1.000 42.30000  ? 115 LEU D CD1 1 
ATOM   838  C CD2 . LEU A 1 133 ? 12.55700  19.48400 11.98100  1.000 41.67000  ? 115 LEU D CD2 1 
ATOM   839  N N   . ASP A 1 134 ? 14.14700  19.55400 7.82700   1.000 52.28000  ? 116 ASP D N   1 
ATOM   840  C CA  . ASP A 1 134 ? 14.07200  19.56300 6.34200   1.000 56.99000  ? 116 ASP D CA  1 
ATOM   841  C C   . ASP A 1 134 ? 12.61700  19.73500 5.91000   1.000 55.13000  ? 116 ASP D C   1 
ATOM   842  O O   . ASP A 1 134 ? 12.35900  19.75100 4.70800   1.000 49.52000  ? 116 ASP D O   1 
ATOM   843  C CB  . ASP A 1 134 ? 14.61300  18.25700 5.76800   1.000 64.84000  ? 116 ASP D CB  1 
ATOM   844  C CG  . ASP A 1 134 ? 13.80300  17.04400 6.18800   1.000 82.84000  ? 116 ASP D CG  1 
ATOM   845  O OD1 . ASP A 1 134 ? 13.25300  17.06300 7.30600   1.000 91.80000  ? 116 ASP D OD1 1 
ATOM   846  O OD2 . ASP A 1 134 ? 13.72700  16.09500 5.39300   1.000 101.65000 ? 116 ASP D OD2 1 
ATOM   847  N N   . GLU A 1 135 ? 11.71400  19.83500 6.88300   1.000 64.84000  ? 117 GLU D N   1 
ATOM   848  C CA  . GLU A 1 135 ? 10.26800  19.98300 6.60000   1.000 47.93000  ? 117 GLU D CA  1 
ATOM   849  C C   . GLU A 1 135 ? 9.69900   21.10500 7.46200   1.000 39.08000  ? 117 GLU D C   1 
ATOM   850  O O   . GLU A 1 135 ? 10.42500  21.60100 8.31200   1.000 40.03000  ? 117 GLU D O   1 
ATOM   851  C CB  . GLU A 1 135 ? 9.56200   18.65500 6.84700   1.000 45.14000  ? 117 GLU D CB  1 
ATOM   852  C CG  . GLU A 1 135 ? 10.01500  17.53300 5.93800   1.000 65.21000  ? 117 GLU D CG  1 
ATOM   853  C CD  . GLU A 1 135 ? 9.27700   16.22700 6.17000   1.000 66.23000  ? 117 GLU D CD  1 
ATOM   854  O OE1 . GLU A 1 135 ? 8.71100   16.06300 7.25800   1.000 80.11000  ? 117 GLU D OE1 1 
ATOM   855  O OE2 . GLU A 1 135 ? 9.26800   15.38300 5.26000   1.000 75.83000  ? 117 GLU D OE2 1 
ATOM   856  N N   . THR A 1 136 ? 8.43800   21.45100 7.25500   1.000 39.97000  ? 118 THR D N   1 
ATOM   857  C CA  . THR A 1 136 ? 7.81200   22.57700 7.93400   1.000 44.27000  ? 118 THR D CA  1 
ATOM   858  C C   . THR A 1 136 ? 6.58700   22.09900 8.69900   1.000 43.17000  ? 118 THR D C   1 
ATOM   859  O O   . THR A 1 136 ? 5.74700   21.37800 8.14900   1.000 48.04000  ? 118 THR D O   1 
ATOM   860  C CB  . THR A 1 136 ? 7.42400   23.67100 6.93600   1.000 52.22000  ? 118 THR D CB  1 
ATOM   861  O OG1 . THR A 1 136 ? 8.55800   23.99900 6.12400   1.000 57.82000  ? 118 THR D OG1 1 
ATOM   862  C CG2 . THR A 1 136 ? 6.96200   24.91800 7.67100   1.000 42.84000  ? 118 THR D CG2 1 
ATOM   863  N N   . TYR A 1 137 ? 6.48700   22.50700 9.96200   1.000 36.80000  ? 119 TYR D N   1 
ATOM   864  C CA  . TYR A 1 137 ? 5.40200   22.10300 10.84700  1.000 40.77000  ? 119 TYR D CA  1 
ATOM   865  C C   . TYR A 1 137 ? 4.60900   23.33300 11.26600  1.000 42.72000  ? 119 TYR D C   1 
ATOM   866  O O   . TYR A 1 137 ? 5.19000   24.32900 11.71000  1.000 48.13000  ? 119 TYR D O   1 
ATOM   867  C CB  . TYR A 1 137 ? 5.94300   21.37400 12.08200  1.000 34.35000  ? 119 TYR D CB  1 
ATOM   868  C CG  . TYR A 1 137 ? 6.62000   20.05200 11.78500  1.000 34.33000  ? 119 TYR D CG  1 
ATOM   869  C CD1 . TYR A 1 137 ? 7.91400   20.00800 11.28100  1.000 34.24000  ? 119 TYR D CD1 1 
ATOM   870  C CD2 . TYR A 1 137 ? 5.97000   18.84800 12.02200  1.000 39.32000  ? 119 TYR D CD2 1 
ATOM   871  C CE1 . TYR A 1 137 ? 8.53800   18.80200 11.01400  1.000 40.73000  ? 119 TYR D CE1 1 
ATOM   872  C CE2 . TYR A 1 137 ? 6.58500   17.63700 11.75900  1.000 37.04000  ? 119 TYR D CE2 1 
ATOM   873  C CZ  . TYR A 1 137 ? 7.86900   17.62000 11.25400  1.000 43.36000  ? 119 TYR D CZ  1 
ATOM   874  O OH  . TYR A 1 137 ? 8.48100   16.41600 10.99200  1.000 50.37000  ? 119 TYR D OH  1 
ATOM   875  N N   . PHE A 1 138 ? 3.28700   23.23300 11.11100  1.000 43.56000  ? 120 PHE D N   1 
ATOM   876  C CA  . PHE A 1 138 ? 2.38800   24.35000 11.47800  1.000 44.80000  ? 120 PHE D CA  1 
ATOM   877  C C   . PHE A 1 138 ? 1.49900   23.92400 12.64600  1.000 47.81000  ? 120 PHE D C   1 
ATOM   878  O O   . PHE A 1 138 ? 0.78200   22.91800 12.51800  1.000 45.72000  ? 120 PHE D O   1 
ATOM   879  C CB  . PHE A 1 138 ? 1.55100   24.79300 10.27500  1.000 43.41000  ? 120 PHE D CB  1 
ATOM   880  C CG  . PHE A 1 138 ? 2.32800   25.34700 9.10800   1.000 54.89000  ? 120 PHE D CG  1 
ATOM   881  C CD1 . PHE A 1 138 ? 2.93700   24.50500 8.19200   1.000 52.56000  ? 120 PHE D CD1 1 
ATOM   882  C CD2 . PHE A 1 138 ? 2.41000   26.71300 8.89700   1.000 58.79000  ? 120 PHE D CD2 1 
ATOM   883  C CE1 . PHE A 1 138 ? 3.63300   25.01900 7.11000   1.000 57.65000  ? 120 PHE D CE1 1 
ATOM   884  C CE2 . PHE A 1 138 ? 3.11300   27.22600 7.81900   1.000 68.11000  ? 120 PHE D CE2 1 
ATOM   885  C CZ  . PHE A 1 138 ? 3.72100   26.37800 6.92600   1.000 49.69000  ? 120 PHE D CZ  1 
ATOM   886  N N   . PHE A 1 139 ? 1.56600   24.65600 13.75200  1.000 44.40000  ? 121 PHE D N   1 
ATOM   887  C CA  . PHE A 1 139 ? 0.75400   24.39900 14.93400  1.000 47.24000  ? 121 PHE D CA  1 
ATOM   888  C C   . PHE A 1 139 ? -0.27600  25.51300 15.06800  1.000 42.39000  ? 121 PHE D C   1 
ATOM   889  O O   . PHE A 1 139 ? 0.08400   26.69500 15.04400  1.000 42.68000  ? 121 PHE D O   1 
ATOM   890  C CB  . PHE A 1 139 ? 1.60400   24.34500 16.21100  1.000 52.38000  ? 121 PHE D CB  1 
ATOM   891  C CG  . PHE A 1 139 ? 2.62000   23.22500 16.25600  1.000 44.39000  ? 121 PHE D CG  1 
ATOM   892  C CD1 . PHE A 1 139 ? 2.85500   22.40100 15.16800  1.000 58.85000  ? 121 PHE D CD1 1 
ATOM   893  C CD2 . PHE A 1 139 ? 3.34100   23.00100 17.41800  1.000 67.34000  ? 121 PHE D CD2 1 
ATOM   894  C CE1 . PHE A 1 139 ? 3.79300   21.38500 15.23500  1.000 54.14000  ? 121 PHE D CE1 1 
ATOM   895  C CE2 . PHE A 1 139 ? 4.27400   21.98600 17.49200  1.000 66.83000  ? 121 PHE D CE2 1 
ATOM   896  C CZ  . PHE A 1 139 ? 4.50000   21.17700 16.40000  1.000 57.53000  ? 121 PHE D CZ  1 
ATOM   897  N N   . PHE A 1 140 ? -1.54300  25.13100 15.20300  1.000 43.72000  ? 122 PHE D N   1 
ATOM   898  C CA  . PHE A 1 140 ? -2.64900  26.12000 15.33800  1.000 58.45000  ? 122 PHE D CA  1 
ATOM   899  C C   . PHE A 1 140 ? -3.89300  25.52100 15.99800  1.000 50.69000  ? 122 PHE D C   1 
ATOM   900  O O   . PHE A 1 140 ? -4.36900  24.46800 15.57400  1.000 56.36000  ? 122 PHE D O   1 
ATOM   901  C CB  . PHE A 1 140 ? -3.04800  26.74400 13.99400  1.000 50.13000  ? 122 PHE D CB  1 
ATOM   902  C CG  . PHE A 1 140 ? -3.42000  25.82600 12.86200  1.000 47.52000  ? 122 PHE D CG  1 
ATOM   903  C CD1 . PHE A 1 140 ? -2.45100  25.31400 12.02000  1.000 51.47000  ? 122 PHE D CD1 1 
ATOM   904  C CD2 . PHE A 1 140 ? -4.74600  25.53800 12.59400  1.000 52.87000  ? 122 PHE D CD2 1 
ATOM   905  C CE1 . PHE A 1 140 ? -2.79700  24.49600 10.95900  1.000 58.37000  ? 122 PHE D CE1 1 
ATOM   906  C CE2 . PHE A 1 140 ? -5.09100  24.72000 11.53300  1.000 58.70000  ? 122 PHE D CE2 1 
ATOM   907  C CZ  . PHE A 1 140 ? -4.11600  24.20300 10.71600  1.000 60.37000  ? 122 PHE D CZ  1 
ATOM   908  N N   . ARG A 1 141 ? -4.44500  26.25100 16.95700  1.000 55.73000  ? 123 ARG D N   1 
ATOM   909  C CA  . ARG A 1 141 ? -5.67400  25.79900 17.64700  1.000 71.07000  ? 123 ARG D CA  1 
ATOM   910  C C   . ARG A 1 141 ? -6.81600  25.82800 16.64400  1.000 67.16000  ? 123 ARG D C   1 
ATOM   911  O O   . ARG A 1 141 ? -6.76800  26.63700 15.71200  1.000 75.50000  ? 123 ARG D O   1 
ATOM   912  C CB  . ARG A 1 141 ? -5.99600  26.69900 18.84100  1.000 68.54000  ? 123 ARG D CB  1 
ATOM   913  C CG  . ARG A 1 141 ? -7.16000  26.23400 19.69800  1.000 79.61000  ? 123 ARG D CG  1 
ATOM   914  C CD  . ARG A 1 141 ? -7.62100  27.34900 20.61400  1.000 83.79000  ? 123 ARG D CD  1 
ATOM   915  N NE  . ARG A 1 141 ? -8.67200  26.92600 21.52400  1.000 86.26000  ? 123 ARG D NE  1 
ATOM   916  C CZ  . ARG A 1 141 ? -8.58100  26.98700 22.84600  1.000 89.74000  ? 123 ARG D CZ  1 
ATOM   917  N NH1 . ARG A 1 141 ? -7.43500  27.31000 23.41500  1.000 85.46000  ? 123 ARG D NH1 1 
ATOM   918  N NH2 . ARG A 1 141 ? -9.63700  26.71900 23.59300  1.000 95.28000  ? 123 ARG D NH2 1 
ATOM   919  N N   . VAL A 1 142 ? -7.77600  24.94600 16.83200  1.000 64.32000  ? 124 VAL D N   1 
ATOM   920  C CA  . VAL A 1 142 ? -8.94400  24.92200 15.95900  1.000 78.41000  ? 124 VAL D CA  1 
ATOM   921  C C   . VAL A 1 142 ? -10.22300 25.07900 16.77300  1.000 87.34000  ? 124 VAL D C   1 
ATOM   922  O O   . VAL A 1 142 ? -10.52500 26.16200 17.27200  1.000 89.74000  ? 124 VAL D O   1 
ATOM   923  C CB  . VAL A 1 142 ? -8.99000  23.63200 15.12800  1.000 85.49000  ? 124 VAL D CB  1 
ATOM   924  C CG1 . VAL A 1 142 ? -9.35400  22.45200 16.01300  1.000 80.03000  ? 124 VAL D CG1 1 
ATOM   925  C CG2 . VAL A 1 142 ? -9.97900  23.77700 13.98200  1.000 86.25000  ? 124 VAL D CG2 1 
ATOM   926  N N   . MET B 1 19  ? 32.99400  53.24000 24.32100  1.000 79.13000  ? 1   MET A N   1 
ATOM   927  C CA  . MET B 1 19  ? 32.21700  52.40600 23.38400  1.000 80.61000  ? 1   MET A CA  1 
ATOM   928  C C   . MET B 1 19  ? 31.51400  53.36900 22.42900  1.000 71.51000  ? 1   MET A C   1 
ATOM   929  O O   . MET B 1 19  ? 30.83200  54.27900 22.91000  1.000 62.28000  ? 1   MET A O   1 
ATOM   930  C CB  . MET B 1 19  ? 31.19000  51.61100 24.18800  1.000 74.37000  ? 1   MET A CB  1 
ATOM   931  C CG  . MET B 1 19  ? 30.60800  50.44500 23.46200  1.000 77.91000  ? 1   MET A CG  1 
ATOM   932  S SD  . MET B 1 19  ? 29.97800  49.36900 24.74800  1.000 123.46000 ? 1   MET A SD  1 
ATOM   933  N N   . LYS B 1 20  ? 31.71200  53.19300 21.13200  1.000 50.27000  ? 2   LYS A N   1 
ATOM   934  C CA  . LYS B 1 20  ? 31.00300  54.05700 20.16300  1.000 61.42000  ? 2   LYS A CA  1 
ATOM   935  C C   . LYS B 1 20  ? 30.19900  53.17800 19.20000  1.000 69.55000  ? 2   LYS A C   1 
ATOM   936  O O   . LYS B 1 20  ? 30.67900  52.10300 18.82800  1.000 60.83000  ? 2   LYS A O   1 
ATOM   937  C CB  . LYS B 1 20  ? 31.98500  54.99800 19.46100  1.000 55.93000  ? 2   LYS A CB  1 
ATOM   938  C CG  . LYS B 1 20  ? 32.49700  56.15300 20.30700  1.000 68.23000  ? 2   LYS A CG  1 
ATOM   939  C CD  . LYS B 1 20  ? 32.87000  57.36200 19.49200  1.000 62.62000  ? 2   LYS A CD  1 
ATOM   940  C CE  . LYS B 1 20  ? 33.26600  58.54100 20.35200  1.000 56.53000  ? 2   LYS A CE  1 
ATOM   941  N NZ  . LYS B 1 20  ? 33.26400  59.80400 19.58000  1.000 85.96000  ? 2   LYS A NZ  1 
ATOM   942  N N   . LEU B 1 21  ? 29.00200  53.62700 18.84800  1.000 52.84000  ? 3   LEU A N   1 
ATOM   943  C CA  . LEU B 1 21  ? 28.15100  52.87700 17.90600  1.000 46.99000  ? 3   LEU A CA  1 
ATOM   944  C C   . LEU B 1 21  ? 28.06600  53.61500 16.57600  1.000 47.09000  ? 3   LEU A C   1 
ATOM   945  O O   . LEU B 1 21  ? 28.22600  54.83400 16.55700  1.000 45.17000  ? 3   LEU A O   1 
ATOM   946  C CB  . LEU B 1 21  ? 26.74400  52.73900 18.49500  1.000 46.04000  ? 3   LEU A CB  1 
ATOM   947  C CG  . LEU B 1 21  ? 26.48900  51.57600 19.44600  1.000 67.27000  ? 3   LEU A CG  1 
ATOM   948  C CD1 . LEU B 1 21  ? 25.17000  51.78200 20.17200  1.000 58.85000  ? 3   LEU A CD1 1 
ATOM   949  C CD2 . LEU B 1 21  ? 26.46500  50.26400 18.68900  1.000 56.99000  ? 3   LEU A CD2 1 
ATOM   950  N N   . VAL B 1 22  ? 27.84100  52.87000 15.51000  1.000 47.13000  ? 4   VAL A N   1 
ATOM   951  C CA  . VAL B 1 22  ? 27.58400  53.45200 14.19800  1.000 48.71000  ? 4   VAL A CA  1 
ATOM   952  C C   . VAL B 1 22  ? 26.08500  53.42100 13.95300  1.000 41.18000  ? 4   VAL A C   1 
ATOM   953  O O   . VAL B 1 22  ? 25.45400  52.36000 14.05000  1.000 43.30000  ? 4   VAL A O   1 
ATOM   954  C CB  . VAL B 1 22  ? 28.33100  52.69900 13.08400  1.000 54.57000  ? 4   VAL A CB  1 
ATOM   955  C CG1 . VAL B 1 22  ? 27.99800  53.31500 11.73100  1.000 49.60000  ? 4   VAL A CG1 1 
ATOM   956  C CG2 . VAL B 1 22  ? 29.82900  52.72400 13.33200  1.000 60.67000  ? 4   VAL A CG2 1 
ATOM   957  N N   . ILE B 1 23  ? 25.51200  54.57800 13.64700  1.000 41.82000  ? 5   ILE A N   1 
ATOM   958  C CA  . ILE B 1 23  ? 24.09600  54.69500 13.32400  1.000 41.92000  ? 5   ILE A CA  1 
ATOM   959  C C   . ILE B 1 23  ? 23.99700  55.01200 11.83900  1.000 48.10000  ? 5   ILE A C   1 
ATOM   960  O O   . ILE B 1 23  ? 24.36800  56.10900 11.40200  1.000 45.87000  ? 5   ILE A O   1 
ATOM   961  C CB  . ILE B 1 23  ? 23.39900  55.76700 14.17200  1.000 56.03000  ? 5   ILE A CB  1 
ATOM   962  C CG1 . ILE B 1 23  ? 23.70500  55.55900 15.65600  1.000 57.97000  ? 5   ILE A CG1 1 
ATOM   963  C CG2 . ILE B 1 23  ? 21.90000  55.73600 13.92800  1.000 49.88000  ? 5   ILE A CG2 1 
ATOM   964  C CD1 . ILE B 1 23  ? 23.20400  54.24600 16.21100  1.000 63.89000  ? 5   ILE A CD1 1 
ATOM   965  N N   . ALA B 1 24  ? 23.50700  54.05200 11.05900  1.000 40.97000  ? 6   ALA A N   1 
ATOM   966  C CA  . ALA B 1 24  ? 23.35000  54.20100 9.61700   1.000 48.09000  ? 6   ALA A CA  1 
ATOM   967  C C   . ALA B 1 24  ? 21.87300  54.41800 9.31400   1.000 47.95000  ? 6   ALA A C   1 
ATOM   968  O O   . ALA B 1 24  ? 21.05100  53.51900 9.52400   1.000 51.79000  ? 6   ALA A O   1 
ATOM   969  C CB  . ALA B 1 24  ? 23.89200  52.97900 8.87900   1.000 53.15000  ? 6   ALA A CB  1 
ATOM   970  N N   . ARG B 1 25  ? 21.53900  55.61200 8.83600   1.000 45.85000  ? 7   ARG A N   1 
ATOM   971  C CA  . ARG B 1 25  ? 20.13700  55.90600 8.45700   1.000 40.97000  ? 7   ARG A CA  1 
ATOM   972  C C   . ARG B 1 25  ? 20.02100  55.78500 6.94200   1.000 46.91000  ? 7   ARG A C   1 
ATOM   973  O O   . ARG B 1 25  ? 20.44200  56.69800 6.23800   1.000 47.94000  ? 7   ARG A O   1 
ATOM   974  C CB  . ARG B 1 25  ? 19.70000  57.28600 8.94500   1.000 46.12000  ? 7   ARG A CB  1 
ATOM   975  C CG  . ARG B 1 25  ? 18.30100  57.70700 8.52600   1.000 37.24000  ? 7   ARG A CG  1 
ATOM   976  C CD  . ARG B 1 25  ? 18.09600  59.15400 8.91900   1.000 49.84000  ? 7   ARG A CD  1 
ATOM   977  N NE  . ARG B 1 25  ? 16.74700  59.62600 8.66200   1.000 53.05000  ? 7   ARG A NE  1 
ATOM   978  C CZ  . ARG B 1 25  ? 16.31900  60.85200 8.92500   1.000 61.12000  ? 7   ARG A CZ  1 
ATOM   979  N NH1 . ARG B 1 25  ? 17.06900  61.67900 9.62900   1.000 42.17000  ? 7   ARG A NH1 1 
ATOM   980  N NH2 . ARG B 1 25  ? 15.14000  61.24800 8.48100   1.000 63.75000  ? 7   ARG A NH2 1 
ATOM   981  N N   . VAL B 1 26  ? 19.47100  54.67400 6.48900   1.000 47.94000  ? 8   VAL A N   1 
ATOM   982  C CA  . VAL B 1 26  ? 19.30900  54.44200 5.03200   1.000 65.01000  ? 8   VAL A CA  1 
ATOM   983  C C   . VAL B 1 26  ? 17.97300  55.05300 4.62200   1.000 58.93000  ? 8   VAL A C   1 
ATOM   984  O O   . VAL B 1 26  ? 16.93400  54.58600 5.09200   1.000 52.41000  ? 8   VAL A O   1 
ATOM   985  C CB  . VAL B 1 26  ? 19.41400  52.94700 4.69100   1.000 54.74000  ? 8   VAL A CB  1 
ATOM   986  C CG1 . VAL B 1 26  ? 19.18200  52.69200 3.21300   1.000 57.08000  ? 8   VAL A CG1 1 
ATOM   987  C CG2 . VAL B 1 26  ? 20.74900  52.37300 5.13100   1.000 49.02000  ? 8   VAL A CG2 1 
ATOM   988  N N   . LYS B 1 27  ? 18.02600  56.07700 3.77900   1.000 55.14000  ? 9   LYS A N   1 
ATOM   989  C CA  . LYS B 1 27  ? 16.79900  56.79400 3.36800   1.000 62.99000  ? 9   LYS A CA  1 
ATOM   990  C C   . LYS B 1 27  ? 16.07800  56.02600 2.26200   1.000 73.85000  ? 9   LYS A C   1 
ATOM   991  O O   . LYS B 1 27  ? 15.86600  56.59300 1.18500   1.000 79.16000  ? 9   LYS A O   1 
ATOM   992  C CB  . LYS B 1 27  ? 17.18200  58.18400 2.87800   1.000 75.37000  ? 9   LYS A CB  1 
ATOM   993  C CG  . LYS B 1 27  ? 18.14900  58.94600 3.76600   1.000 72.58000  ? 9   LYS A CG  1 
ATOM   994  C CD  . LYS B 1 27  ? 17.49500  59.42600 5.02400   1.000 82.74000  ? 9   LYS A CD  1 
ATOM   995  C CE  . LYS B 1 27  ? 18.31700  60.49700 5.69700   1.000 91.66000  ? 9   LYS A CE  1 
ATOM   996  N NZ  . LYS B 1 27  ? 18.71100  61.55800 4.74200   1.000 93.43000  ? 9   LYS A NZ  1 
ATOM   997  N N   . SER B 1 28  ? 15.71400  54.78400 2.53800   1.000 56.41000  ? 10  SER A N   1 
ATOM   998  C CA  . SER B 1 28  ? 14.99200  53.96300 1.54600   1.000 69.69000  ? 10  SER A CA  1 
ATOM   999  C C   . SER B 1 28  ? 14.14800  52.96700 2.32900   1.000 73.61000  ? 10  SER A C   1 
ATOM   1000 O O   . SER B 1 28  ? 14.65000  52.41100 3.31100   1.000 66.17000  ? 10  SER A O   1 
ATOM   1001 C CB  . SER B 1 28  ? 15.91400  53.24500 0.61200   1.000 72.84000  ? 10  SER A CB  1 
ATOM   1002 O OG  . SER B 1 28  ? 15.26100  52.13200 0.02600   1.000 73.66000  ? 10  SER A OG  1 
ATOM   1003 N N   . PRO B 1 29  ? 12.87900  52.75200 1.94800   1.000 83.35000  ? 11  PRO A N   1 
ATOM   1004 C CA  . PRO B 1 29  ? 12.03000  51.74800 2.61100   1.000 83.65000  ? 11  PRO A CA  1 
ATOM   1005 C C   . PRO B 1 29  ? 12.24300  50.32100 2.13200   1.000 80.61000  ? 11  PRO A C   1 
ATOM   1006 O O   . PRO B 1 29  ? 11.58200  49.41500 2.65200   1.000 79.57000  ? 11  PRO A O   1 
ATOM   1007 C CB  . PRO B 1 29  ? 10.62000  52.23000 2.24900   1.000 80.26000  ? 11  PRO A CB  1 
ATOM   1008 C CG  . PRO B 1 29  ? 10.78800  52.81900 0.88900   1.000 83.04000  ? 11  PRO A CG  1 
ATOM   1009 C CD  . PRO B 1 29  ? 12.15900  53.45300 0.87000   1.000 78.42000  ? 11  PRO A CD  1 
ATOM   1010 N N   . LYS B 1 30  ? 13.13600  50.09400 1.16700   1.000 71.42000  ? 12  LYS A N   1 
ATOM   1011 C CA  . LYS B 1 30  ? 13.33500  48.77300 0.57300   1.000 84.27000  ? 12  LYS A CA  1 
ATOM   1012 C C   . LYS B 1 30  ? 14.82200  48.41200 0.59800   1.000 81.45000  ? 12  LYS A C   1 
ATOM   1013 O O   . LYS B 1 30  ? 15.44100  48.13600 -0.42900  1.000 105.98000 ? 12  LYS A O   1 
ATOM   1014 C CB  . LYS B 1 30  ? 12.78400  48.72300 -0.85200  1.000 96.93000  ? 12  LYS A CB  1 
ATOM   1015 N N   . VAL B 1 31  ? 15.42000  48.43900 1.78400   1.000 75.78000  ? 13  VAL A N   1 
ATOM   1016 C CA  . VAL B 1 31  ? 16.82300  47.97000 1.94700   1.000 69.10000  ? 13  VAL A CA  1 
ATOM   1017 C C   . VAL B 1 31  ? 16.78900  47.09000 3.19100   1.000 71.87000  ? 13  VAL A C   1 
ATOM   1018 O O   . VAL B 1 31  ? 16.46200  47.61100 4.25800   1.000 82.39000  ? 13  VAL A O   1 
ATOM   1019 C CB  . VAL B 1 31  ? 17.84700  49.10900 2.08200   1.000 74.66000  ? 13  VAL A CB  1 
ATOM   1020 C CG1 . VAL B 1 31  ? 19.18600  48.60800 2.59600   1.000 63.74000  ? 13  VAL A CG1 1 
ATOM   1021 C CG2 . VAL B 1 31  ? 18.02400  49.86800 0.77900   1.000 70.03000  ? 13  VAL A CG2 1 
ATOM   1022 N N   . LYS B 1 32  ? 17.04800  45.79700 3.03600   1.000 77.16000  ? 14  LYS A N   1 
ATOM   1023 C CA  . LYS B 1 32  ? 16.93500  44.86300 4.17900   1.000 72.82000  ? 14  LYS A CA  1 
ATOM   1024 C C   . LYS B 1 32  ? 18.27400  44.77900 4.90600   1.000 76.12000  ? 14  LYS A C   1 
ATOM   1025 O O   . LYS B 1 32  ? 18.27500  44.56300 6.12100   1.000 83.54000  ? 14  LYS A O   1 
ATOM   1026 C CB  . LYS B 1 32  ? 16.49400  43.49200 3.66600   1.000 84.73000  ? 14  LYS A CB  1 
ATOM   1027 C CG  . LYS B 1 32  ? 16.06100  42.49000 4.73000   1.000 87.54000  ? 14  LYS A CG  1 
ATOM   1028 C CD  . LYS B 1 32  ? 17.15700  41.54700 5.17900   1.000 80.31000  ? 14  LYS A CD  1 
ATOM   1029 N N   . ARG B 1 33  ? 19.36700  44.94500 4.18300   1.000 57.53000  ? 15  ARG A N   1 
ATOM   1030 C CA  . ARG B 1 33  ? 20.66300  44.76100 4.85600   1.000 67.88000  ? 15  ARG A CA  1 
ATOM   1031 C C   . ARG B 1 33  ? 21.73400  45.54900 4.12700   1.000 63.58000  ? 15  ARG A C   1 
ATOM   1032 O O   . ARG B 1 33  ? 21.47300  46.00200 3.01600   1.000 78.60000  ? 15  ARG A O   1 
ATOM   1033 C CB  . ARG B 1 33  ? 21.03800  43.28100 4.87400   1.000 77.95000  ? 15  ARG A CB  1 
ATOM   1034 N N   . LEU B 1 34  ? 22.87900  45.70300 4.76700   1.000 70.19000  ? 16  LEU A N   1 
ATOM   1035 C CA  . LEU B 1 34  ? 24.01700  46.39300 4.13200   1.000 58.70000  ? 16  LEU A CA  1 
ATOM   1036 C C   . LEU B 1 34  ? 25.02700  45.32400 3.73700   1.000 83.14000  ? 16  LEU A C   1 
ATOM   1037 O O   . LEU B 1 34  ? 25.16200  44.34000 4.47200   1.000 80.19000  ? 16  LEU A O   1 
ATOM   1038 C CB  . LEU B 1 34  ? 24.65300  47.34900 5.13700   1.000 71.59000  ? 16  LEU A CB  1 
ATOM   1039 C CG  . LEU B 1 34  ? 23.75900  48.46300 5.67500   1.000 87.40000  ? 16  LEU A CG  1 
ATOM   1040 C CD1 . LEU B 1 34  ? 24.42700  49.15700 6.85000   1.000 59.34000  ? 16  LEU A CD1 1 
ATOM   1041 C CD2 . LEU B 1 34  ? 23.44100  49.46800 4.58100   1.000 73.14000  ? 16  LEU A CD2 1 
ATOM   1042 N N   . SER B 1 35  ? 25.71600  45.53300 2.62700   1.000 84.80000  ? 17  SER A N   1 
ATOM   1043 C CA  . SER B 1 35  ? 26.77200  44.59000 2.20700   1.000 87.09000  ? 17  SER A CA  1 
ATOM   1044 C C   . SER B 1 35  ? 28.06700  44.92800 2.93500   1.000 90.66000  ? 17  SER A C   1 
ATOM   1045 O O   . SER B 1 35  ? 28.18300  46.05500 3.44100   1.000 84.60000  ? 17  SER A O   1 
ATOM   1046 C CB  . SER B 1 35  ? 26.97900  44.69900 0.73300   1.000 92.67000  ? 17  SER A CB  1 
ATOM   1047 O OG  . SER B 1 35  ? 27.67600  45.89200 0.41200   1.000 79.62000  ? 17  SER A OG  1 
ATOM   1048 N N   . GLU B 1 36  ? 28.99700  43.98400 2.97900   1.000 87.93000  ? 18  GLU A N   1 
ATOM   1049 C CA  . GLU B 1 36  ? 30.31000  44.25600 3.55300   1.000 97.10000  ? 18  GLU A CA  1 
ATOM   1050 C C   . GLU B 1 36  ? 31.02300  45.36700 2.79700   1.000 88.34000  ? 18  GLU A C   1 
ATOM   1051 O O   . GLU B 1 36  ? 31.84300  46.08900 3.37700   1.000 80.59000  ? 18  GLU A O   1 
ATOM   1052 C CB  . GLU B 1 36  ? 31.14600  42.97800 3.55800   1.000 100.18000 ? 18  GLU A CB  1 
ATOM   1053 N N   . GLU B 1 37  ? 30.72300  45.52000 1.50500   1.000 85.01000  ? 19  GLU A N   1 
ATOM   1054 C CA  . GLU B 1 37  ? 31.23300  46.65800 0.75000   1.000 99.06000  ? 19  GLU A CA  1 
ATOM   1055 C C   . GLU B 1 37  ? 30.62500  47.96200 1.25200   1.000 94.52000  ? 19  GLU A C   1 
ATOM   1056 O O   . GLU B 1 37  ? 31.32900  48.96800 1.40000   1.000 88.02000  ? 19  GLU A O   1 
ATOM   1057 C CB  . GLU B 1 37  ? 30.94300  46.46300 -0.73800  1.000 99.62000  ? 19  GLU A CB  1 
ATOM   1058 C CG  . GLU B 1 37  ? 31.31500  47.64400 -1.61500  1.000 102.63000 ? 19  GLU A CG  1 
ATOM   1059 C CD  . GLU B 1 37  ? 30.88200  47.45300 -3.05600  1.000 117.06000 ? 19  GLU A CD  1 
ATOM   1060 O OE1 . GLU B 1 37  ? 30.21100  46.44000 -3.34600  1.000 116.27000 ? 19  GLU A OE1 1 
ATOM   1061 O OE2 . GLU B 1 37  ? 31.21200  48.31500 -3.89800  1.000 135.05000 ? 19  GLU A OE2 1 
ATOM   1062 N N   . ASP B 1 38  ? 29.31700  47.96100 1.52100   1.000 97.34000  ? 20  ASP A N   1 
ATOM   1063 C CA  . ASP B 1 38  ? 28.66700  49.15500 2.05100   1.000 96.59000  ? 20  ASP A CA  1 
ATOM   1064 C C   . ASP B 1 38  ? 29.11800  49.44100 3.47700   1.000 88.45000  ? 20  ASP A C   1 
ATOM   1065 O O   . ASP B 1 38  ? 29.31600  50.60300 3.85100   1.000 73.04000  ? 20  ASP A O   1 
ATOM   1066 C CB  . ASP B 1 38  ? 27.14900  48.99300 1.99500   1.000 89.48000  ? 20  ASP A CB  1 
ATOM   1067 C CG  . ASP B 1 38  ? 26.64400  48.72000 0.59300   1.000 103.18000 ? 20  ASP A CG  1 
ATOM   1068 O OD1 . ASP B 1 38  ? 27.25600  49.22700 -0.37100  1.000 103.64000 ? 20  ASP A OD1 1 
ATOM   1069 O OD2 . ASP B 1 38  ? 25.63600  47.99700 0.45600   1.000 98.48000  ? 20  ASP A OD2 1 
ATOM   1070 N N   . ILE B 1 39  ? 29.28000  48.39300 4.28900   1.000 78.19000  ? 21  ILE A N   1 
ATOM   1071 C CA  . ILE B 1 39  ? 29.71900  48.57800 5.66900   1.000 64.51000  ? 21  ILE A CA  1 
ATOM   1072 C C   . ILE B 1 39  ? 31.11400  49.18800 5.70700   1.000 73.81000  ? 21  ILE A C   1 
ATOM   1073 O O   . ILE B 1 39  ? 31.38500  50.10900 6.48700   1.000 76.03000  ? 21  ILE A O   1 
ATOM   1074 C CB  . ILE B 1 39  ? 29.66100  47.24100 6.43200   1.000 69.45000  ? 21  ILE A CB  1 
ATOM   1075 C CG1 . ILE B 1 39  ? 28.20800  46.81400 6.65000   1.000 73.96000  ? 21  ILE A CG1 1 
ATOM   1076 C CG2 . ILE B 1 39  ? 30.39500  47.34400 7.76000   1.000 68.11000  ? 21  ILE A CG2 1 
ATOM   1077 C CD1 . ILE B 1 39  ? 28.06100  45.49800 7.38400   1.000 77.77000  ? 21  ILE A CD1 1 
ATOM   1078 N N   . GLU B 1 40  ? 32.01900  48.69400 4.85800   1.000 86.17000  ? 22  GLU A N   1 
ATOM   1079 C CA  . GLU B 1 40  ? 33.36600  49.25100 4.81900   1.000 84.58000  ? 22  GLU A CA  1 
ATOM   1080 C C   . GLU B 1 40  ? 33.36700  50.67000 4.26300   1.000 75.19000  ? 22  GLU A C   1 
ATOM   1081 O O   . GLU B 1 40  ? 34.21200  51.48400 4.65200   1.000 70.84000  ? 22  GLU A O   1 
ATOM   1082 C CB  . GLU B 1 40  ? 34.28600  48.35100 3.99500   1.000 86.50000  ? 22  GLU A CB  1 
ATOM   1083 C CG  . GLU B 1 40  ? 35.67200  48.18400 4.59600   1.000 91.73000  ? 22  GLU A CG  1 
ATOM   1084 C CD  . GLU B 1 40  ? 35.63500  47.52600 5.96300   1.000 93.56000  ? 22  GLU A CD  1 
ATOM   1085 O OE1 . GLU B 1 40  ? 34.77100  46.65000 6.18000   1.000 87.81000  ? 22  GLU A OE1 1 
ATOM   1086 O OE2 . GLU B 1 40  ? 36.46600  47.88800 6.82300   1.000 88.19000  ? 22  GLU A OE2 1 
ATOM   1087 N N   . LYS B 1 41  ? 32.40900  50.99800 3.40300   1.000 78.40000  ? 23  LYS A N   1 
ATOM   1088 C CA  . LYS B 1 41  ? 32.30900  52.39700 2.90500   1.000 85.72000  ? 23  LYS A CA  1 
ATOM   1089 C C   . LYS B 1 41  ? 31.83500  53.29300 4.05200   1.000 84.59000  ? 23  LYS A C   1 
ATOM   1090 O O   . LYS B 1 41  ? 32.30600  54.43800 4.14000   1.000 71.04000  ? 23  LYS A O   1 
ATOM   1091 C CB  . LYS B 1 41  ? 31.36100  52.49300 1.70700   1.000 80.06000  ? 23  LYS A CB  1 
ATOM   1092 C CG  . LYS B 1 41  ? 31.01800  53.90000 1.24200   1.000 76.51000  ? 23  LYS A CG  1 
ATOM   1093 C CD  . LYS B 1 41  ? 31.38400  54.14600 -0.20200  1.000 87.33000  ? 23  LYS A CD  1 
ATOM   1094 C CE  . LYS B 1 41  ? 30.76900  53.14300 -1.15400  1.000 92.28000  ? 23  LYS A CE  1 
ATOM   1095 N NZ  . LYS B 1 41  ? 29.33900  53.42800 -1.41200  1.000 69.78000  ? 23  LYS A NZ  1 
ATOM   1096 N N   . ILE B 1 42  ? 30.96600  52.76500 4.91400   1.000 69.11000  ? 24  ILE A N   1 
ATOM   1097 C CA  . ILE B 1 42  ? 30.51500  53.54400 6.06300   1.000 74.70000  ? 24  ILE A CA  1 
ATOM   1098 C C   . ILE B 1 42  ? 31.66100  53.75300 7.04500   1.000 56.77000  ? 24  ILE A C   1 
ATOM   1099 O O   . ILE B 1 42  ? 31.89700  54.87000 7.52100   1.000 67.95000  ? 24  ILE A O   1 
ATOM   1100 C CB  . ILE B 1 42  ? 29.31500  52.85200 6.73400   1.000 72.32000  ? 24  ILE A CB  1 
ATOM   1101 C CG1 . ILE B 1 42  ? 28.09700  52.87900 5.80700   1.000 63.29000  ? 24  ILE A CG1 1 
ATOM   1102 C CG2 . ILE B 1 42  ? 29.00100  53.49800 8.07500   1.000 71.77000  ? 24  ILE A CG2 1 
ATOM   1103 C CD1 . ILE B 1 42  ? 26.92000  52.07700 6.31900   1.000 71.32000  ? 24  ILE A CD1 1 
ATOM   1104 N N   . LYS B 1 43  ? 32.39200  52.68000 7.36000   1.000 68.00000  ? 25  LYS A N   1 
ATOM   1105 C CA  . LYS B 1 43  ? 33.50100  52.78600 8.30100   1.000 73.50000  ? 25  LYS A CA  1 
ATOM   1106 C C   . LYS B 1 43  ? 34.61100  53.68000 7.76500   1.000 72.08000  ? 25  LYS A C   1 
ATOM   1107 O O   . LYS B 1 43  ? 35.29200  54.35700 8.54400   1.000 81.75000  ? 25  LYS A O   1 
ATOM   1108 C CB  . LYS B 1 43  ? 34.04700  51.39400 8.62100   1.000 78.84000  ? 25  LYS A CB  1 
ATOM   1109 C CG  . LYS B 1 43  ? 33.03100  50.46500 9.26300   1.000 67.47000  ? 25  LYS A CG  1 
ATOM   1110 C CD  . LYS B 1 43  ? 33.54400  49.03600 9.30900   1.000 82.25000  ? 25  LYS A CD  1 
ATOM   1111 N N   . SER B 1 44  ? 34.80800  53.69900 6.44500   1.000 72.36000  ? 26  SER A N   1 
ATOM   1112 C CA  . SER B 1 44  ? 35.83500  54.56000 5.86800   1.000 78.32000  ? 26  SER A CA  1 
ATOM   1113 C C   . SER B 1 44  ? 35.44900  56.03000 5.97500   1.000 76.64000  ? 26  SER A C   1 
ATOM   1114 O O   . SER B 1 44  ? 36.30000  56.88100 6.26200   1.000 84.58000  ? 26  SER A O   1 
ATOM   1115 C CB  . SER B 1 44  ? 36.08300  54.17500 4.41000   1.000 86.65000  ? 26  SER A CB  1 
ATOM   1116 O OG  . SER B 1 44  ? 37.03200  55.04000 3.81100   1.000 90.34000  ? 26  SER A OG  1 
ATOM   1117 N N   . ALA B 1 45  ? 34.17800  56.35200 5.75900   1.000 73.58000  ? 27  ALA A N   1 
ATOM   1118 C CA  . ALA B 1 45  ? 33.73800  57.76500 5.82600   1.000 78.40000  ? 27  ALA A CA  1 
ATOM   1119 C C   . ALA B 1 45  ? 33.79400  58.29200 7.26500   1.000 73.92000  ? 27  ALA A C   1 
ATOM   1120 O O   . ALA B 1 45  ? 33.92900  59.50600 7.43500   1.000 61.56000  ? 27  ALA A O   1 
ATOM   1121 C CB  . ALA B 1 45  ? 32.36000  57.89500 5.25200   1.000 61.28000  ? 27  ALA A CB  1 
ATOM   1122 N N   . LEU B 1 46  ? 33.68500  57.40600 8.24900   1.000 65.83000  ? 28  LEU A N   1 
ATOM   1123 C CA  . LEU B 1 46  ? 33.69300  57.81600 9.64600   1.000 70.56000  ? 28  LEU A CA  1 
ATOM   1124 C C   . LEU B 1 46  ? 35.09300  57.84600 10.24600  1.000 72.41000  ? 28  LEU A C   1 
ATOM   1125 O O   . LEU B 1 46  ? 35.22600  57.94200 11.47100  1.000 67.44000  ? 28  LEU A O   1 
ATOM   1126 C CB  . LEU B 1 46  ? 32.79600  56.89200 10.47200  1.000 61.83000  ? 28  LEU A CB  1 
ATOM   1127 C CG  . LEU B 1 46  ? 31.29200  57.02400 10.23100  1.000 56.00000  ? 28  LEU A CG  1 
ATOM   1128 C CD1 . LEU B 1 46  ? 30.52300  56.02600 11.08200  1.000 57.22000  ? 28  LEU A CD1 1 
ATOM   1129 C CD2 . LEU B 1 46  ? 30.83300  58.44500 10.51800  1.000 57.08000  ? 28  LEU A CD2 1 
ATOM   1130 N N   . LYS B 1 47  ? 36.13500  57.76700 9.41700   1.000 79.64000  ? 29  LYS A N   1 
ATOM   1131 C CA  . LYS B 1 47  ? 37.50000  57.79500 9.93200   1.000 62.15000  ? 29  LYS A CA  1 
ATOM   1132 C C   . LYS B 1 47  ? 37.92300  59.20900 10.31400  1.000 84.92000  ? 29  LYS A C   1 
ATOM   1133 O O   . LYS B 1 47  ? 38.43900  59.43300 11.41400  1.000 77.95000  ? 29  LYS A O   1 
ATOM   1134 C CB  . LYS B 1 47  ? 38.46400  57.20800 8.89900   1.000 78.89000  ? 29  LYS A CB  1 
ATOM   1135 C CG  . LYS B 1 47  ? 38.32200  55.70900 8.69700   1.000 84.89000  ? 29  LYS A CG  1 
ATOM   1136 N N   . SER B 1 48  ? 37.71100  60.17200 9.42100   1.000 79.42000  ? 30  SER A N   1 
ATOM   1137 C CA  . SER B 1 48  ? 38.12400  61.55000 9.65400   1.000 88.16000  ? 30  SER A CA  1 
ATOM   1138 C C   . SER B 1 48  ? 37.04000  62.40100 10.30200  1.000 82.79000  ? 30  SER A C   1 
ATOM   1139 O O   . SER B 1 48  ? 37.28400  63.58000 10.57500  1.000 87.03000  ? 30  SER A O   1 
ATOM   1140 C CB  . SER B 1 48  ? 38.56000  62.20100 8.33800   1.000 103.37000 ? 30  SER A CB  1 
ATOM   1141 O OG  . SER B 1 48  ? 37.46900  62.32600 7.44300   1.000 101.16000 ? 30  SER A OG  1 
ATOM   1142 N N   . THR B 1 49  ? 35.86000  61.84100 10.55400  1.000 68.82000  ? 31  THR A N   1 
ATOM   1143 C CA  . THR B 1 49  ? 34.77000  62.60100 11.15000  1.000 74.92000  ? 31  THR A CA  1 
ATOM   1144 C C   . THR B 1 49  ? 33.78700  61.63600 11.79400  1.000 73.08000  ? 31  THR A C   1 
ATOM   1145 O O   . THR B 1 49  ? 33.72400  60.45700 11.43800  1.000 71.92000  ? 31  THR A O   1 
ATOM   1146 C CB  . THR B 1 49  ? 34.05900  63.47800 10.11200  1.000 80.61000  ? 31  THR A CB  1 
ATOM   1147 O OG1 . THR B 1 49  ? 32.95600  64.15500 10.72700  1.000 81.99000  ? 31  THR A OG1 1 
ATOM   1148 C CG2 . THR B 1 49  ? 33.54900  62.62800 8.95500   1.000 64.09000  ? 31  THR A CG2 1 
ATOM   1149 N N   . ASN B 1 50  ? 33.02400  62.15400 12.75400  1.000 65.35000  ? 32  ASN A N   1 
ATOM   1150 C CA  . ASN B 1 50  ? 31.98100  61.38900 13.42400  1.000 68.17000  ? 32  ASN A CA  1 
ATOM   1151 C C   . ASN B 1 50  ? 30.60800  61.59700 12.79800  1.000 65.32000  ? 32  ASN A C   1 
ATOM   1152 O O   . ASN B 1 50  ? 29.60000  61.21700 13.40300  1.000 60.74000  ? 32  ASN A O   1 
ATOM   1153 C CB  . ASN B 1 50  ? 31.92800  61.75500 14.91100  1.000 66.45000  ? 32  ASN A CB  1 
ATOM   1154 C CG  . ASN B 1 50  ? 33.19100  61.36600 15.65400  1.000 75.25000  ? 32  ASN A CG  1 
ATOM   1155 O OD1 . ASN B 1 50  ? 33.78900  60.32500 15.38500  1.000 88.84000  ? 32  ASN A OD1 1 
ATOM   1156 N ND2 . ASN B 1 50  ? 33.60300  62.20500 16.59800  1.000 79.46000  ? 32  ASN A ND2 1 
ATOM   1157 N N   . LYS B 1 51  ? 30.54700  62.18600 11.60600  1.000 64.67000  ? 33  LYS A N   1 
ATOM   1158 C CA  . LYS B 1 51  ? 29.27300  62.49400 10.96000  1.000 58.97000  ? 33  LYS A CA  1 
ATOM   1159 C C   . LYS B 1 51  ? 29.53100  62.65200 9.47200   1.000 70.04000  ? 33  LYS A C   1 
ATOM   1160 O O   . LYS B 1 51  ? 30.25300  63.56800 9.06600   1.000 74.34000  ? 33  LYS A O   1 
ATOM   1161 C CB  . LYS B 1 51  ? 28.66500  63.76700 11.55100  1.000 57.97000  ? 33  LYS A CB  1 
ATOM   1162 C CG  . LYS B 1 51  ? 27.31900  64.16400 10.97000  1.000 67.88000  ? 33  LYS A CG  1 
ATOM   1163 C CD  . LYS B 1 51  ? 26.80100  65.43000 11.64000  1.000 70.71000  ? 33  LYS A CD  1 
ATOM   1164 C CE  . LYS B 1 51  ? 25.44200  65.83800 11.09500  1.000 79.54000  ? 33  LYS A CE  1 
ATOM   1165 N NZ  . LYS B 1 51  ? 25.49200  66.13200 9.63800   1.000 93.73000  ? 33  LYS A NZ  1 
ATOM   1166 N N   . ALA B 1 52  ? 28.90200  61.77300 8.70300   1.000 65.76000  ? 34  ALA A N   1 
ATOM   1167 C CA  . ALA B 1 52  ? 29.14600  61.79100 7.25300   1.000 66.47000  ? 34  ALA A CA  1 
ATOM   1168 C C   . ALA B 1 52  ? 27.92200  61.33200 6.47900   1.000 75.63000  ? 34  ALA A C   1 
ATOM   1169 O O   . ALA B 1 52  ? 26.93800  60.91500 7.09400   1.000 69.31000  ? 34  ALA A O   1 
ATOM   1170 C CB  . ALA B 1 52  ? 30.30800  60.90100 6.93900   1.000 69.43000  ? 34  ALA A CB  1 
ATOM   1171 N N   . VAL B 1 53  ? 28.02300  61.39500 5.16100   1.000 80.49000  ? 35  VAL A N   1 
ATOM   1172 C CA  . VAL B 1 53  ? 26.93700  60.98800 4.27600   1.000 75.58000  ? 35  VAL A CA  1 
ATOM   1173 C C   . VAL B 1 53  ? 27.52900  60.16100 3.14200   1.000 76.01000  ? 35  VAL A C   1 
ATOM   1174 O O   . VAL B 1 53  ? 28.45200  60.61300 2.45600   1.000 90.65000  ? 35  VAL A O   1 
ATOM   1175 C CB  . VAL B 1 53  ? 26.16700  62.19900 3.71400   1.000 79.47000  ? 35  VAL A CB  1 
ATOM   1176 C CG1 . VAL B 1 53  ? 25.18600  61.75200 2.64400   1.000 68.77000  ? 35  VAL A CG1 1 
ATOM   1177 C CG2 . VAL B 1 53  ? 25.44300  62.93900 4.83000   1.000 75.39000  ? 35  VAL A CG2 1 
ATOM   1178 N N   . VAL B 1 54  ? 26.99100  58.96000 2.97100   1.000 58.55000  ? 36  VAL A N   1 
ATOM   1179 C CA  . VAL B 1 54  ? 27.51500  58.03700 1.93500   1.000 68.10000  ? 36  VAL A CA  1 
ATOM   1180 C C   . VAL B 1 54  ? 26.38700  57.73100 0.95800   1.000 73.71000  ? 36  VAL A C   1 
ATOM   1181 O O   . VAL B 1 54  ? 25.23400  58.06700 1.25100   1.000 74.14000  ? 36  VAL A O   1 
ATOM   1182 C CB  . VAL B 1 54  ? 28.05700  56.73500 2.55200   1.000 61.54000  ? 36  VAL A CB  1 
ATOM   1183 C CG1 . VAL B 1 54  ? 29.20000  56.99800 3.51600   1.000 72.77000  ? 36  VAL A CG1 1 
ATOM   1184 C CG2 . VAL B 1 54  ? 26.96900  55.91200 3.21600   1.000 59.19000  ? 36  VAL A CG2 1 
ATOM   1185 N N   . THR B 1 55  ? 26.73300  57.12500 -0.16800  1.000 75.62000  ? 37  THR A N   1 
ATOM   1186 C CA  . THR B 1 55  ? 25.70000  56.72000 -1.14500  1.000 79.94000  ? 37  THR A CA  1 
ATOM   1187 C C   . THR B 1 55  ? 25.77900  55.20300 -1.30000  1.000 77.15000  ? 37  THR A C   1 
ATOM   1188 O O   . THR B 1 55  ? 26.88500  54.68100 -1.43500  1.000 84.73000  ? 37  THR A O   1 
ATOM   1189 C CB  . THR B 1 55  ? 25.85300  57.50600 -2.45100  1.000 92.00000  ? 37  THR A CB  1 
ATOM   1190 O OG1 . THR B 1 55  ? 27.18600  57.33100 -2.92900  1.000 108.34000 ? 37  THR A OG1 1 
ATOM   1191 C CG2 . THR B 1 55  ? 25.57100  58.98100 -2.27800  1.000 88.84000  ? 37  THR A CG2 1 
ATOM   1192 N N   . ILE B 1 56  ? 24.63900  54.53700 -1.23800  1.000 80.05000  ? 38  ILE A N   1 
ATOM   1193 C CA  . ILE B 1 56  ? 24.58600  53.06200 -1.38600  1.000 90.57000  ? 38  ILE A CA  1 
ATOM   1194 C C   . ILE B 1 56  ? 23.57900  52.78800 -2.49900  1.000 96.05000  ? 38  ILE A C   1 
ATOM   1195 O O   . ILE B 1 56  ? 22.52300  53.43000 -2.50600  1.000 96.45000  ? 38  ILE A O   1 
ATOM   1196 C CB  . ILE B 1 56  ? 24.16100  52.39600 -0.06300  1.000 72.43000  ? 38  ILE A CB  1 
ATOM   1197 C CG1 . ILE B 1 56  ? 25.14600  52.70200 1.06500   1.000 82.57000  ? 38  ILE A CG1 1 
ATOM   1198 C CG2 . ILE B 1 56  ? 23.96500  50.90200 -0.24600  1.000 94.22000  ? 38  ILE A CG2 1 
ATOM   1199 C CD1 . ILE B 1 56  ? 26.56900  52.32100 0.75200   1.000 88.51000  ? 38  ILE A CD1 1 
ATOM   1200 N N   . LYS B 1 57  ? 23.91800  51.88800 -3.42200  1.000 106.13000 ? 39  LYS A N   1 
ATOM   1201 C CA  . LYS B 1 57  ? 23.02000  51.61800 -4.57400  1.000 109.31000 ? 39  LYS A CA  1 
ATOM   1202 C C   . LYS B 1 57  ? 22.16500  50.38600 -4.27300  1.000 100.90000 ? 39  LYS A C   1 
ATOM   1203 O O   . LYS B 1 57  ? 22.65600  49.48600 -3.56800  1.000 105.20000 ? 39  LYS A O   1 
ATOM   1204 C CB  . LYS B 1 57  ? 23.84000  51.43500 -5.85600  1.000 110.94000 ? 39  LYS A CB  1 
ATOM   1205 N N   . ASP B 1 58  ? 20.93500  50.36200 -4.78500  1.000 95.31000  ? 40  ASP A N   1 
ATOM   1206 C CA  . ASP B 1 58  ? 20.04700  49.18900 -4.58800  1.000 109.04000 ? 40  ASP A CA  1 
ATOM   1207 C C   . ASP B 1 58  ? 19.95700  48.41500 -5.90400  1.000 111.06000 ? 40  ASP A C   1 
ATOM   1208 O O   . ASP B 1 58  ? 19.53700  49.02000 -6.90800  1.000 119.89000 ? 40  ASP A O   1 
ATOM   1209 C CB  . ASP B 1 58  ? 18.65900  49.61800 -4.10900  1.000 104.10000 ? 40  ASP A CB  1 
ATOM   1210 C CG  . ASP B 1 58  ? 17.75200  48.46500 -3.71600  1.000 105.59000 ? 40  ASP A CG  1 
ATOM   1211 O OD1 . ASP B 1 58  ? 18.21900  47.31100 -3.74800  1.000 112.48000 ? 40  ASP A OD1 1 
ATOM   1212 O OD2 . ASP B 1 58  ? 16.58100  48.73300 -3.38800  1.000 104.84000 ? 40  ASP A OD2 1 
ATOM   1213 N N   . GLU B 1 59  ? 20.33900  47.13600 -5.89600  1.000 96.83000  ? 41  GLU A N   1 
ATOM   1214 C CA  . GLU B 1 59  ? 20.20400  46.28600 -7.11000  1.000 107.85000 ? 41  GLU A CA  1 
ATOM   1215 C C   . GLU B 1 59  ? 20.18700  47.17100 -8.36000  1.000 114.32000 ? 41  GLU A C   1 
ATOM   1216 O O   . GLU B 1 59  ? 21.18800  47.12700 -9.09600  1.000 121.96000 ? 41  GLU A O   1 
ATOM   1217 C CB  . GLU B 1 59  ? 18.92900  45.45000 -7.00300  1.000 96.90000  ? 41  GLU A CB  1 
ATOM   1218 C CG  . GLU B 1 59  ? 18.88600  44.59500 -5.75100  1.000 92.76000  ? 41  GLU A CG  1 
ATOM   1219 C CD  . GLU B 1 59  ? 17.50800  44.07700 -5.37700  1.000 112.86000 ? 41  GLU A CD  1 
ATOM   1220 O OE1 . GLU B 1 59  ? 16.54200  44.40900 -6.09100  1.000 127.62000 ? 41  GLU A OE1 1 
ATOM   1221 O OE2 . GLU B 1 59  ? 17.40600  43.34300 -4.37400  1.000 100.81000 ? 41  GLU A OE2 1 
ATOM   1222 N N   . GLU B 1 62  ? 19.62700  51.60800 -7.75900  1.000 131.73000 ? 44  GLU A N   1 
ATOM   1223 C CA  . GLU B 1 62  ? 18.99800  52.91000 -7.42800  1.000 125.99000 ? 44  GLU A CA  1 
ATOM   1224 C C   . GLU B 1 62  ? 19.84700  53.54400 -6.32900  1.000 131.96000 ? 44  GLU A C   1 
ATOM   1225 O O   . GLU B 1 62  ? 20.08500  52.87300 -5.31100  1.000 132.24000 ? 44  GLU A O   1 
ATOM   1226 C CB  . GLU B 1 62  ? 17.55000  52.74800 -6.96800  1.000 116.39000 ? 44  GLU A CB  1 
ATOM   1227 N N   . GLU B 1 63  ? 20.29100  54.77900 -6.54700  1.000 119.62000 ? 45  GLU A N   1 
ATOM   1228 C CA  . GLU B 1 63  ? 21.15000  55.46500 -5.55400  1.000 107.11000 ? 45  GLU A CA  1 
ATOM   1229 C C   . GLU B 1 63  ? 20.32200  55.77700 -4.30600  1.000 98.54000  ? 45  GLU A C   1 
ATOM   1230 O O   . GLU B 1 63  ? 19.23900  56.35600 -4.45700  1.000 92.76000  ? 45  GLU A O   1 
ATOM   1231 C CB  . GLU B 1 63  ? 21.73500  56.72300 -6.18700  1.000 105.75000 ? 45  GLU A CB  1 
ATOM   1232 N N   . ILE B 1 64  ? 20.82300  55.39600 -3.13200  1.000 84.51000  ? 46  ILE A N   1 
ATOM   1233 C CA  . ILE B 1 64  ? 20.12500  55.70600 -1.85500  1.000 71.93000  ? 46  ILE A CA  1 
ATOM   1234 C C   . ILE B 1 64  ? 21.12300  56.37500 -0.91300  1.000 71.84000  ? 46  ILE A C   1 
ATOM   1235 O O   . ILE B 1 64  ? 22.18500  55.79500 -0.67100  1.000 73.38000  ? 46  ILE A O   1 
ATOM   1236 C CB  . ILE B 1 64  ? 19.52100  54.43500 -1.23700  1.000 87.62000  ? 46  ILE A CB  1 
ATOM   1237 C CG1 . ILE B 1 64  ? 18.47300  53.80300 -2.15600  1.000 88.78000  ? 46  ILE A CG1 1 
ATOM   1238 C CG2 . ILE B 1 64  ? 18.95500  54.73000 0.14100   1.000 75.37000  ? 46  ILE A CG2 1 
ATOM   1239 C CD1 . ILE B 1 64  ? 17.31500  54.71600 -2.47700  1.000 81.35000  ? 46  ILE A CD1 1 
ATOM   1240 N N   . GLU B 1 65  ? 20.78300  57.56100 -0.42300  1.000 63.95000  ? 47  GLU A N   1 
ATOM   1241 C CA  . GLU B 1 65  ? 21.67800  58.31100 0.48900   1.000 74.27000  ? 47  GLU A CA  1 
ATOM   1242 C C   . GLU B 1 65  ? 21.65200  57.65800 1.86800   1.000 68.72000  ? 47  GLU A C   1 
ATOM   1243 O O   . GLU B 1 65  ? 20.58400  57.20200 2.28500   1.000 67.13000  ? 47  GLU A O   1 
ATOM   1244 C CB  . GLU B 1 65  ? 21.22900  59.76800 0.57000   1.000 76.12000  ? 47  GLU A CB  1 
ATOM   1245 C CG  . GLU B 1 65  ? 22.07800  60.62900 1.48100   1.000 85.64000  ? 47  GLU A CG  1 
ATOM   1246 C CD  . GLU B 1 65  ? 21.72400  62.10400 1.43400   1.000 103.75000 ? 47  GLU A CD  1 
ATOM   1247 O OE1 . GLU B 1 65  ? 21.85600  62.70800 0.35300   1.000 102.57000 ? 47  GLU A OE1 1 
ATOM   1248 O OE2 . GLU B 1 65  ? 21.30800  62.64300 2.47600   1.000 101.85000 ? 47  GLU A OE2 1 
ATOM   1249 N N   . VAL B 1 66  ? 22.79900  57.61400 2.53000   1.000 50.04000  ? 48  VAL A N   1 
ATOM   1250 C CA  . VAL B 1 66  ? 22.83400  57.05700 3.90300   1.000 61.88000  ? 48  VAL A CA  1 
ATOM   1251 C C   . VAL B 1 66  ? 23.52200  58.04900 4.84000   1.000 64.35000  ? 48  VAL A C   1 
ATOM   1252 O O   . VAL B 1 66  ? 24.67700  58.39500 4.58800   1.000 50.45000  ? 48  VAL A O   1 
ATOM   1253 C CB  . VAL B 1 66  ? 23.49800  55.66900 3.95900   1.000 62.51000  ? 48  VAL A CB  1 
ATOM   1254 C CG1 . VAL B 1 66  ? 23.50900  55.11200 5.37400   1.000 50.84000  ? 48  VAL A CG1 1 
ATOM   1255 C CG2 . VAL B 1 66  ? 22.84200  54.68800 3.00500   1.000 59.38000  ? 48  VAL A CG2 1 
ATOM   1256 N N   . GLU B 1 67  ? 22.81200  58.47200 5.88300   1.000 61.01000  ? 49  GLU A N   1 
ATOM   1257 C CA  . GLU B 1 67  ? 23.42700  59.33200 6.91800   1.000 52.28000  ? 49  GLU A CA  1 
ATOM   1258 C C   . GLU B 1 67  ? 24.08900  58.40700 7.93400   1.000 52.69000  ? 49  GLU A C   1 
ATOM   1259 O O   . GLU B 1 67  ? 23.42700  57.48400 8.39500   1.000 58.62000  ? 49  GLU A O   1 
ATOM   1260 C CB  . GLU B 1 67  ? 22.37600  60.22900 7.56200   1.000 54.07000  ? 49  GLU A CB  1 
ATOM   1261 C CG  . GLU B 1 67  ? 21.85700  61.32600 6.65900   1.000 66.22000  ? 49  GLU A CG  1 
ATOM   1262 C CD  . GLU B 1 67  ? 20.94700  62.30900 7.37200   1.000 75.77000  ? 49  GLU A CD  1 
ATOM   1263 O OE1 . GLU B 1 67  ? 21.29200  62.72300 8.49300   1.000 74.41000  ? 49  GLU A OE1 1 
ATOM   1264 O OE2 . GLU B 1 67  ? 19.89400  62.65100 6.80800   1.000 75.74000  ? 49  GLU A OE2 1 
ATOM   1265 N N   . VAL B 1 68  ? 25.36200  58.62700 8.21600   1.000 48.50000  ? 50  VAL A N   1 
ATOM   1266 C CA  . VAL B 1 68  ? 26.11800  57.78400 9.13200   1.000 53.55000  ? 50  VAL A CA  1 
ATOM   1267 C C   . VAL B 1 68  ? 26.72300  58.65800 10.22100  1.000 53.87000  ? 50  VAL A C   1 
ATOM   1268 O O   . VAL B 1 68  ? 27.13200  59.79600 9.96500   1.000 64.62000  ? 50  VAL A O   1 
ATOM   1269 C CB  . VAL B 1 68  ? 27.21100  56.97800 8.39600   1.000 60.81000  ? 50  VAL A CB  1 
ATOM   1270 C CG1 . VAL B 1 68  ? 26.58000  56.07100 7.35000   1.000 60.48000  ? 50  VAL A CG1 1 
ATOM   1271 C CG2 . VAL B 1 68  ? 28.23100  57.90700 7.75200   1.000 59.04000  ? 50  VAL A CG2 1 
ATOM   1272 N N   . ARG B 1 69  ? 26.76300  58.13000 11.44300  1.000 46.30000  ? 51  ARG A N   1 
ATOM   1273 C CA  . ARG B 1 69  ? 27.29800  58.85700 12.58500  1.000 49.71000  ? 51  ARG A CA  1 
ATOM   1274 C C   . ARG B 1 69  ? 27.97900  57.87700 13.52800  1.000 48.44000  ? 51  ARG A C   1 
ATOM   1275 O O   . ARG B 1 69  ? 27.56400  56.72200 13.65400  1.000 50.98000  ? 51  ARG A O   1 
ATOM   1276 C CB  . ARG B 1 69  ? 26.20100  59.62700 13.33500  1.000 54.10000  ? 51  ARG A CB  1 
ATOM   1277 C CG  . ARG B 1 69  ? 25.60900  60.79400 12.56200  1.000 40.60000  ? 51  ARG A CG  1 
ATOM   1278 C CD  . ARG B 1 69  ? 24.23400  61.16300 13.08800  1.000 64.71000  ? 51  ARG A CD  1 
ATOM   1279 N NE  . ARG B 1 69  ? 23.49200  61.97800 12.13400  1.000 66.82000  ? 51  ARG A NE  1 
ATOM   1280 C CZ  . ARG B 1 69  ? 23.31300  63.28700 12.24500  1.000 65.69000  ? 51  ARG A CZ  1 
ATOM   1281 N NH1 . ARG B 1 69  ? 23.78800  63.96500 13.27700  1.000 90.92000  ? 51  ARG A NH1 1 
ATOM   1282 N NH2 . ARG B 1 69  ? 22.63500  63.93100 11.29900  1.000 85.35000  ? 51  ARG A NH2 1 
ATOM   1283 N N   . LEU B 1 70  ? 29.03000  58.35400 14.19000  1.000 50.39000  ? 52  LEU A N   1 
ATOM   1284 C CA  . LEU B 1 70  ? 29.73500  57.59900 15.22000  1.000 52.51000  ? 52  LEU A CA  1 
ATOM   1285 C C   . LEU B 1 70  ? 29.43500  58.26200 16.55900  1.000 51.57000  ? 52  LEU A C   1 
ATOM   1286 O O   . LEU B 1 70  ? 29.90700  59.37200 16.82800  1.000 56.65000  ? 52  LEU A O   1 
ATOM   1287 C CB  . LEU B 1 70  ? 31.23600  57.55600 14.94000  1.000 49.16000  ? 52  LEU A CB  1 
ATOM   1288 C CG  . LEU B 1 70  ? 32.05300  56.58300 15.79100  1.000 61.83000  ? 52  LEU A CG  1 
ATOM   1289 C CD1 . LEU B 1 70  ? 31.56700  55.15900 15.57700  1.000 54.68000  ? 52  LEU A CD1 1 
ATOM   1290 C CD2 . LEU B 1 70  ? 33.53500  56.70200 15.47500  1.000 58.22000  ? 52  LEU A CD2 1 
ATOM   1291 N N   . LEU B 1 71  ? 28.64800  57.58600 17.39300  1.000 50.85000  ? 53  LEU A N   1 
ATOM   1292 C CA  . LEU B 1 71  ? 28.13700  58.16900 18.62200  1.000 36.05000  ? 53  LEU A CA  1 
ATOM   1293 C C   . LEU B 1 71  ? 28.37600  57.23400 19.79600  1.000 40.76000  ? 53  LEU A C   1 
ATOM   1294 O O   . LEU B 1 71  ? 28.41100  56.01100 19.64300  1.000 44.80000  ? 53  LEU A O   1 
ATOM   1295 C CB  . LEU B 1 71  ? 26.63500  58.46300 18.51800  1.000 37.50000  ? 53  LEU A CB  1 
ATOM   1296 C CG  . LEU B 1 71  ? 26.16800  59.31300 17.33800  1.000 46.24000  ? 53  LEU A CG  1 
ATOM   1297 C CD1 . LEU B 1 71  ? 24.65000  59.31100 17.25100  1.000 40.94000  ? 53  LEU A CD1 1 
ATOM   1298 C CD2 . LEU B 1 71  ? 26.70300  60.73100 17.45800  1.000 53.68000  ? 53  LEU A CD2 1 
ATOM   1299 N N   . THR B 1 72  ? 28.53300  57.82900 20.97600  1.000 45.43000  ? 54  THR A N   1 
ATOM   1300 C CA  . THR B 1 72  ? 28.48600  57.06300 22.20800  1.000 38.52000  ? 54  THR A CA  1 
ATOM   1301 C C   . THR B 1 72  ? 27.04500  56.63900 22.49300  1.000 37.57000  ? 54  THR A C   1 
ATOM   1302 O O   . THR B 1 72  ? 26.10000  57.05300 21.81400  1.000 39.81000  ? 54  THR A O   1 
ATOM   1303 C CB  . THR B 1 72  ? 29.04000  57.88100 23.37400  1.000 43.17000  ? 54  THR A CB  1 
ATOM   1304 O OG1 . THR B 1 72  ? 28.18000  58.99900 23.62500  1.000 45.18000  ? 54  THR A OG1 1 
ATOM   1305 C CG2 . THR B 1 72  ? 30.43600  58.39300 23.04900  1.000 38.15000  ? 54  THR A CG2 1 
ATOM   1306 N N   . LEU B 1 73  ? 26.88100  55.79800 23.51700  1.000 37.27000  ? 55  LEU A N   1 
ATOM   1307 C CA  . LEU B 1 73  ? 25.54300  55.33600 23.87600  1.000 43.22000  ? 55  LEU A CA  1 
ATOM   1308 C C   . LEU B 1 73  ? 24.65100  56.50100 24.28700  1.000 51.14000  ? 55  LEU A C   1 
ATOM   1309 O O   . LEU B 1 73  ? 23.46800  56.54300 23.92900  1.000 40.43000  ? 55  LEU A O   1 
ATOM   1310 C CB  . LEU B 1 73  ? 25.62700  54.29700 24.99400  1.000 40.34000  ? 55  LEU A CB  1 
ATOM   1311 C CG  . LEU B 1 73  ? 24.29900  53.71600 25.47900  1.000 43.89000  ? 55  LEU A CG  1 
ATOM   1312 C CD1 . LEU B 1 73  ? 23.54600  53.06300 24.32900  1.000 46.20000  ? 55  LEU A CD1 1 
ATOM   1313 C CD2 . LEU B 1 73  ? 24.53100  52.72200 26.60600  1.000 44.94000  ? 55  LEU A CD2 1 
ATOM   1314 N N   . GLU B 1 74  ? 25.20500  57.46400 25.02600  1.000 39.86000  ? 56  GLU A N   1 
ATOM   1315 C CA  . GLU B 1 74  ? 24.41700  58.62100 25.43800  1.000 44.93000  ? 56  GLU A CA  1 
ATOM   1316 C C   . GLU B 1 74  ? 24.12100  59.53700 24.25800  1.000 42.03000  ? 56  GLU A C   1 
ATOM   1317 O O   . GLU B 1 74  ? 23.01800  60.08600 24.15200  1.000 39.23000  ? 56  GLU A O   1 
ATOM   1318 C CB  . GLU B 1 74  ? 25.14700  59.38100 26.54300  1.000 51.54000  ? 56  GLU A CB  1 
ATOM   1319 C CG  . GLU B 1 74  ? 24.31800  60.46700 27.20300  1.000 63.40000  ? 56  GLU A CG  1 
ATOM   1320 C CD  . GLU B 1 74  ? 25.03600  61.11400 28.36900  1.000 80.10000  ? 56  GLU A CD  1 
ATOM   1321 O OE1 . GLU B 1 74  ? 26.28300  61.05200 28.40600  1.000 77.50000  ? 56  GLU A OE1 1 
ATOM   1322 O OE2 . GLU B 1 74  ? 24.35500  61.67600 29.25200  1.000 69.38000  ? 56  GLU A OE2 1 
ATOM   1323 N N   . GLU B 1 75  ? 25.09300  59.71600 23.36000  1.000 36.88000  ? 57  GLU A N   1 
ATOM   1324 C CA  . GLU B 1 75  ? 24.85800  60.53300 22.17500  1.000 35.22000  ? 57  GLU A CA  1 
ATOM   1325 C C   . GLU B 1 75  ? 23.86600  59.87500 21.22600  1.000 36.16000  ? 57  GLU A C   1 
ATOM   1326 O O   . GLU B 1 75  ? 23.10600  60.57300 20.54600  1.000 36.69000  ? 57  GLU A O   1 
ATOM   1327 C CB  . GLU B 1 75  ? 26.17700  60.80300 21.45100  1.000 44.09000  ? 57  GLU A CB  1 
ATOM   1328 C CG  . GLU B 1 75  ? 27.14400  61.68600 22.21600  1.000 53.93000  ? 57  GLU A CG  1 
ATOM   1329 C CD  . GLU B 1 75  ? 28.52600  61.69900 21.59400  1.000 51.91000  ? 57  GLU A CD  1 
ATOM   1330 O OE1 . GLU B 1 75  ? 28.80800  60.81700 20.75600  1.000 59.86000  ? 57  GLU A OE1 1 
ATOM   1331 O OE2 . GLU B 1 75  ? 29.32900  62.59100 21.94000  1.000 78.46000  ? 57  GLU A OE2 1 
ATOM   1332 N N   . ALA B 1 76  ? 23.86100  58.54100 21.16400  1.000 37.66000  ? 58  ALA A N   1 
ATOM   1333 C CA  . ALA B 1 76  ? 22.94100  57.84700 20.27000  1.000 41.31000  ? 58  ALA A CA  1 
ATOM   1334 C C   . ALA B 1 76  ? 21.50500  57.94600 20.77000  1.000 37.88000  ? 58  ALA A C   1 
ATOM   1335 O O   . ALA B 1 76  ? 20.57400  58.08600 19.96900  1.000 33.25000  ? 58  ALA A O   1 
ATOM   1336 C CB  . ALA B 1 76  ? 23.36400  56.38700 20.11700  1.000 33.59000  ? 58  ALA A CB  1 
ATOM   1337 N N   . LEU B 1 77  ? 21.30600  57.87100 22.08800  1.000 39.18000  ? 59  LEU A N   1 
ATOM   1338 C CA  . LEU B 1 77  ? 19.96700  58.04200 22.64200  1.000 34.58000  ? 59  LEU A CA  1 
ATOM   1339 C C   . LEU B 1 77  ? 19.45300  59.45500 22.40100  1.000 40.84000  ? 59  LEU A C   1 
ATOM   1340 O O   . LEU B 1 77  ? 18.25900  59.65500 22.15000  1.000 33.70000  ? 59  LEU A O   1 
ATOM   1341 C CB  . LEU B 1 77  ? 19.97200  57.71700 24.13500  1.000 35.49000  ? 59  LEU A CB  1 
ATOM   1342 C CG  . LEU B 1 77  ? 20.28000  56.26300 24.49800  1.000 44.80000  ? 59  LEU A CG  1 
ATOM   1343 C CD1 . LEU B 1 77  ? 20.55500  56.12600 25.98500  1.000 40.04000  ? 59  LEU A CD1 1 
ATOM   1344 C CD2 . LEU B 1 77  ? 19.13700  55.35100 24.07700  1.000 37.56000  ? 59  LEU A CD2 1 
ATOM   1345 N N   . LYS B 1 78  ? 20.34200  60.44800 22.47500  1.000 35.99000  ? 60  LYS A N   1 
ATOM   1346 C CA  . LYS B 1 78  ? 19.95500  61.81500 22.14200  1.000 44.60000  ? 60  LYS A CA  1 
ATOM   1347 C C   . LYS B 1 78  ? 19.61800  61.93700 20.66200  1.000 35.25000  ? 60  LYS A C   1 
ATOM   1348 O O   . LYS B 1 78  ? 18.67200  62.64000 20.28700  1.000 40.33000  ? 60  LYS A O   1 
ATOM   1349 C CB  . LYS B 1 78  ? 21.07600  62.78100 22.52400  1.000 42.51000  ? 60  LYS A CB  1 
ATOM   1350 C CG  . LYS B 1 78  ? 20.73000  64.25000 22.35000  1.000 56.39000  ? 60  LYS A CG  1 
ATOM   1351 C CD  . LYS B 1 78  ? 21.91300  65.13600 22.71800  1.000 76.63000  ? 60  LYS A CD  1 
ATOM   1352 C CE  . LYS B 1 78  ? 21.52300  66.60600 22.74900  1.000 73.19000  ? 60  LYS A CE  1 
ATOM   1353 N NZ  . LYS B 1 78  ? 21.02000  67.08300 21.43300  1.000 80.75000  ? 60  LYS A NZ  1 
ATOM   1354 N N   . TYR B 1 79  ? 20.38300  61.25300 19.80800  1.000 41.80000  ? 61  TYR A N   1 
ATOM   1355 C CA  . TYR B 1 79  ? 20.09000  61.24200 18.37800  1.000 36.13000  ? 61  TYR A CA  1 
ATOM   1356 C C   . TYR B 1 79  ? 18.72500  60.62700 18.09700  1.000 30.92000  ? 61  TYR A C   1 
ATOM   1357 O O   . TYR B 1 79  ? 17.97400  61.12200 17.24900  1.000 29.74000  ? 61  TYR A O   1 
ATOM   1358 C CB  . TYR B 1 79  ? 21.18900  60.48000 17.63800  1.000 40.48000  ? 61  TYR A CB  1 
ATOM   1359 C CG  . TYR B 1 79  ? 20.88600  60.18900 16.18600  1.000 41.57000  ? 61  TYR A CG  1 
ATOM   1360 C CD1 . TYR B 1 79  ? 21.12200  61.14100 15.20600  1.000 46.19000  ? 61  TYR A CD1 1 
ATOM   1361 C CD2 . TYR B 1 79  ? 20.37600  58.95700 15.79500  1.000 36.61000  ? 61  TYR A CD2 1 
ATOM   1362 C CE1 . TYR B 1 79  ? 20.85000  60.88100 13.87800  1.000 40.03000  ? 61  TYR A CE1 1 
ATOM   1363 C CE2 . TYR B 1 79  ? 20.10000  58.68900 14.46800  1.000 42.80000  ? 61  TYR A CE2 1 
ATOM   1364 C CZ  . TYR B 1 79  ? 20.34200  59.65400 13.51400  1.000 51.32000  ? 61  TYR A CZ  1 
ATOM   1365 O OH  . TYR B 1 79  ? 20.07300  59.39500 12.19000  1.000 51.85000  ? 61  TYR A OH  1 
ATOM   1366 N N   . ILE B 1 80  ? 18.39200  59.53900 18.79600  1.000 34.41000  ? 62  ILE A N   1 
ATOM   1367 C CA  . ILE B 1 80  ? 17.10100  58.88600 18.59900  1.000 30.93000  ? 62  ILE A CA  1 
ATOM   1368 C C   . ILE B 1 80  ? 15.96200  59.83000 18.96000  1.000 47.82000  ? 62  ILE A C   1 
ATOM   1369 O O   . ILE B 1 80  ? 14.95500  59.91500 18.24600  1.000 29.88000  ? 62  ILE A O   1 
ATOM   1370 C CB  . ILE B 1 80  ? 17.04100  57.58000 19.41300  1.000 32.26000  ? 62  ILE A CB  1 
ATOM   1371 C CG1 . ILE B 1 80  ? 17.97200  56.52900 18.80400  1.000 34.34000  ? 62  ILE A CG1 1 
ATOM   1372 C CG2 . ILE B 1 80  ? 15.61500  57.05800 19.50100  1.000 29.23000  ? 62  ILE A CG2 1 
ATOM   1373 C CD1 . ILE B 1 80  ? 18.09200  55.26600 19.62900  1.000 42.99000  ? 62  ILE A CD1 1 
ATOM   1374 N N   . ASN B 1 81  ? 16.10800  60.56500 20.06600  1.000 33.33000  ? 63  ASN A N   1 
ATOM   1375 C CA  . ASN B 1 81  ? 15.05900  61.49100 20.47800  1.000 34.34000  ? 63  ASN A CA  1 
ATOM   1376 C C   . ASN B 1 81  ? 14.89600  62.64200 19.49100  1.000 33.26000  ? 63  ASN A C   1 
ATOM   1377 O O   . ASN B 1 81  ? 13.81200  63.22900 19.40300  1.000 33.72000  ? 63  ASN A O   1 
ATOM   1378 C CB  . ASN B 1 81  ? 15.35200  62.02800 21.88000  1.000 32.83000  ? 63  ASN A CB  1 
ATOM   1379 C CG  . ASN B 1 81  ? 15.26400  60.95200 22.94900  1.000 45.66000  ? 63  ASN A CG  1 
ATOM   1380 O OD1 . ASN B 1 81  ? 14.56500  59.95100 22.78200  1.000 51.73000  ? 63  ASN A OD1 1 
ATOM   1381 N ND2 . ASN B 1 81  ? 15.97100  61.15600 24.05500  1.000 56.01000  ? 63  ASN A ND2 1 
ATOM   1382 N N   . ASP B 1 82  ? 15.94800  62.97800 18.74300  1.000 30.85000  ? 64  ASP A N   1 
ATOM   1383 C CA  . ASP B 1 82  ? 15.86900  64.05200 17.76100  1.000 36.62000  ? 64  ASP A CA  1 
ATOM   1384 C C   . ASP B 1 82  ? 15.31000  63.60000 16.41900  1.000 36.59000  ? 64  ASP A C   1 
ATOM   1385 O O   . ASP B 1 82  ? 15.09500  64.44500 15.54400  1.000 46.13000  ? 64  ASP A O   1 
ATOM   1386 C CB  . ASP B 1 82  ? 17.25100  64.67700 17.54000  1.000 36.51000  ? 64  ASP A CB  1 
ATOM   1387 C CG  . ASP B 1 82  ? 17.66800  65.59600 18.67200  1.000 59.23000  ? 64  ASP A CG  1 
ATOM   1388 O OD1 . ASP B 1 82  ? 16.82400  65.89200 19.54500  1.000 68.06000  ? 64  ASP A OD1 1 
ATOM   1389 O OD2 . ASP B 1 82  ? 18.84200  66.02300 18.68800  1.000 86.32000  ? 64  ASP A OD2 1 
ATOM   1390 N N   . LEU B 1 83  ? 15.07200  62.30500 16.22800  1.000 40.14000  ? 65  LEU A N   1 
ATOM   1391 C CA  . LEU B 1 83  ? 14.63900  61.81800 14.92900  1.000 46.31000  ? 65  LEU A CA  1 
ATOM   1392 C C   . LEU B 1 83  ? 13.20400  62.25200 14.63500  1.000 39.05000  ? 65  LEU A C   1 
ATOM   1393 O O   . LEU B 1 83  ? 12.38500  62.38300 15.54900  1.000 33.45000  ? 65  LEU A O   1 
ATOM   1394 C CB  . LEU B 1 83  ? 14.74400  60.29700 14.86500  1.000 38.52000  ? 65  LEU A CB  1 
ATOM   1395 C CG  . LEU B 1 83  ? 16.16500  59.73700 14.78100  1.000 41.68000  ? 65  LEU A CG  1 
ATOM   1396 C CD1 . LEU B 1 83  ? 16.13900  58.21700 14.80900  1.000 36.05000  ? 65  LEU A CD1 1 
ATOM   1397 C CD2 . LEU B 1 83  ? 16.86600  60.24700 13.52900  1.000 38.52000  ? 65  LEU A CD2 1 
ATOM   1398 N N   . PRO B 1 84  ? 12.87700  62.49300 13.36500  1.000 40.64000  ? 66  PRO A N   1 
ATOM   1399 C CA  . PRO B 1 84  ? 11.49100  62.83100 12.98000  1.000 41.50000  ? 66  PRO A CA  1 
ATOM   1400 C C   . PRO B 1 84  ? 10.64300  61.58100 12.75300  1.000 39.44000  ? 66  PRO A C   1 
ATOM   1401 O O   . PRO B 1 84  ? 10.17000  61.28700 11.65000  1.000 44.00000  ? 66  PRO A O   1 
ATOM   1402 C CB  . PRO B 1 84  ? 11.69600  63.64300 11.70100  1.000 40.72000  ? 66  PRO A CB  1 
ATOM   1403 C CG  . PRO B 1 84  ? 12.91200  63.04000 11.08800  1.000 43.26000  ? 66  PRO A CG  1 
ATOM   1404 C CD  . PRO B 1 84  ? 13.81000  62.63400 12.23200  1.000 42.76000  ? 66  PRO A CD  1 
ATOM   1405 N N   . ILE B 1 85  ? 10.44400  60.81800 13.82600  1.000 41.40000  ? 67  ILE A N   1 
ATOM   1406 C CA  . ILE B 1 85  ? 9.72500   59.54900 13.79300  1.000 28.88000  ? 67  ILE A CA  1 
ATOM   1407 C C   . ILE B 1 85  ? 8.75000   59.51200 14.96600  1.000 47.21000  ? 67  ILE A C   1 
ATOM   1408 O O   . ILE B 1 85  ? 8.73600   60.40400 15.81800  1.000 39.45000  ? 67  ILE A O   1 
ATOM   1409 C CB  . ILE B 1 85  ? 10.68000  58.33600 13.83600  1.000 39.01000  ? 67  ILE A CB  1 
ATOM   1410 C CG1 . ILE B 1 85  ? 11.52800  58.37100 15.10600  1.000 40.71000  ? 67  ILE A CG1 1 
ATOM   1411 C CG2 . ILE B 1 85  ? 11.57700  58.32300 12.60800  1.000 32.97000  ? 67  ILE A CG2 1 
ATOM   1412 C CD1 . ILE B 1 85  ? 12.46500  57.19400 15.25000  1.000 40.56000  ? 67  ILE A CD1 1 
ATOM   1413 N N   . SER B 1 86  ? 7.93100   58.46300 15.00900  1.000 40.18000  ? 68  SER A N   1 
ATOM   1414 C CA  . SER B 1 86  ? 6.89900   58.34200 16.02900  1.000 47.52000  ? 68  SER A CA  1 
ATOM   1415 C C   . SER B 1 86  ? 7.51000   57.99400 17.38500  1.000 40.15000  ? 68  SER A C   1 
ATOM   1416 O O   . SER B 1 86  ? 8.66600   57.57600 17.49100  1.000 40.93000  ? 68  SER A O   1 
ATOM   1417 C CB  . SER B 1 86  ? 5.87800   57.27500 15.63300  1.000 38.88000  ? 68  SER A CB  1 
ATOM   1418 O OG  . SER B 1 86  ? 6.43800   55.97500 15.72700  1.000 48.42000  ? 68  SER A OG  1 
ATOM   1419 N N   . ASN B 1 87  ? 6.70600   58.17200 18.43700  1.000 35.68000  ? 69  ASN A N   1 
ATOM   1420 C CA  . ASN B 1 87  ? 7.16800   57.84200 19.78200  1.000 34.19000  ? 69  ASN A CA  1 
ATOM   1421 C C   . ASN B 1 87  ? 7.38000   56.34100 19.94000  1.000 42.59000  ? 69  ASN A C   1 
ATOM   1422 O O   . ASN B 1 87  ? 8.31400   55.90700 20.62600  1.000 48.70000  ? 69  ASN A O   1 
ATOM   1423 C CB  . ASN B 1 87  ? 6.17300   58.35200 20.82400  1.000 42.55000  ? 69  ASN A CB  1 
ATOM   1424 C CG  . ASN B 1 87  ? 6.04000   59.86300 20.81500  1.000 55.13000  ? 69  ASN A CG  1 
ATOM   1425 O OD1 . ASN B 1 87  ? 6.63200   60.54600 19.97900  1.000 52.48000  ? 69  ASN A OD1 1 
ATOM   1426 N ND2 . ASN B 1 87  ? 5.25300   60.39200 21.74500  1.000 46.57000  ? 69  ASN A ND2 1 
ATOM   1427 N N   . ASP B 1 88  ? 6.51900   55.53400 19.31600  1.000 44.61000  ? 70  ASP A N   1 
ATOM   1428 C CA  . ASP B 1 88  ? 6.67800   54.08500 19.38700  1.000 38.80000  ? 70  ASP A CA  1 
ATOM   1429 C C   . ASP B 1 88  ? 7.98000   53.64000 18.73400  1.000 41.19000  ? 70  ASP A C   1 
ATOM   1430 O O   . ASP B 1 88  ? 8.63500   52.70500 19.20900  1.000 37.53000  ? 70  ASP A O   1 
ATOM   1431 C CB  . ASP B 1 88  ? 5.48300   53.39400 18.72900  1.000 40.89000  ? 70  ASP A CB  1 
ATOM   1432 C CG  . ASP B 1 88  ? 4.21300   53.53400 19.54200  1.000 55.45000  ? 70  ASP A CG  1 
ATOM   1433 O OD1 . ASP B 1 88  ? 4.29400   54.03700 20.68200  1.000 57.79000  ? 70  ASP A OD1 1 
ATOM   1434 O OD2 . ASP B 1 88  ? 3.13600   53.14400 19.04300  1.000 90.94000  ? 70  ASP A OD2 1 
ATOM   1435 N N   . ALA B 1 89  ? 8.37200   54.29900 17.64100  1.000 37.38000  ? 71  ALA A N   1 
ATOM   1436 C CA  . ALA B 1 89  ? 9.63300   53.96700 16.99000  1.000 40.76000  ? 71  ALA A CA  1 
ATOM   1437 C C   . ALA B 1 89  ? 10.82200  54.36200 17.85700  1.000 41.45000  ? 71  ALA A C   1 
ATOM   1438 O O   . ALA B 1 89  ? 11.81700  53.63100 17.92600  1.000 43.62000  ? 71  ALA A O   1 
ATOM   1439 C CB  . ALA B 1 89  ? 9.71300   54.64700 15.62400  1.000 35.21000  ? 71  ALA A CB  1 
ATOM   1440 N N   . LYS B 1 90  ? 10.73700  55.51400 18.52600  1.000 45.16000  ? 72  LYS A N   1 
ATOM   1441 C CA  . LYS B 1 90  ? 11.82900  55.94400 19.39300  1.000 39.20000  ? 72  LYS A CA  1 
ATOM   1442 C C   . LYS B 1 90  ? 11.99400  55.00400 20.57900  1.000 46.63000  ? 72  LYS A C   1 
ATOM   1443 O O   . LYS B 1 90  ? 13.12000  54.65500 20.95100  1.000 40.04000  ? 72  LYS A O   1 
ATOM   1444 C CB  . LYS B 1 90  ? 11.59100  57.37600 19.86700  1.000 34.65000  ? 72  LYS A CB  1 
ATOM   1445 C CG  . LYS B 1 90  ? 11.71800  58.41300 18.76800  1.000 37.10000  ? 72  LYS A CG  1 
ATOM   1446 C CD  . LYS B 1 90  ? 11.47100  59.81200 19.30000  1.000 36.23000  ? 72  LYS A CD  1 
ATOM   1447 C CE  . LYS B 1 90  ? 11.65500  60.84900 18.20900  1.000 39.87000  ? 72  LYS A CE  1 
ATOM   1448 N NZ  . LYS B 1 90  ? 11.36600  62.22400 18.69800  1.000 37.20000  ? 72  LYS A NZ  1 
ATOM   1449 N N   . LYS B 1 91  ? 10.88200  54.57900 21.18500  1.000 42.72000  ? 73  LYS A N   1 
ATOM   1450 C CA  . LYS B 1 91  ? 10.97100  53.64800 22.30600  1.000 51.83000  ? 73  LYS A CA  1 
ATOM   1451 C C   . LYS B 1 91  ? 11.47900  52.28500 21.85600  1.000 45.81000  ? 73  LYS A C   1 
ATOM   1452 O O   . LYS B 1 91  ? 12.19700  51.60800 22.60100  1.000 52.38000  ? 73  LYS A O   1 
ATOM   1453 C CB  . LYS B 1 91  ? 9.61300   53.51600 22.99700  1.000 53.04000  ? 73  LYS A CB  1 
ATOM   1454 C CG  . LYS B 1 91  ? 9.42200   54.49700 24.13900  1.000 71.35000  ? 73  LYS A CG  1 
ATOM   1455 N N   . LEU B 1 92  ? 11.12100  51.86600 20.64100  1.000 41.68000  ? 74  LEU A N   1 
ATOM   1456 C CA  . LEU B 1 92  ? 11.63000  50.60300 20.11700  1.000 35.63000  ? 74  LEU A CA  1 
ATOM   1457 C C   . LEU B 1 92  ? 13.14100  50.66200 19.93400  1.000 42.97000  ? 74  LEU A C   1 
ATOM   1458 O O   . LEU B 1 92  ? 13.86400  49.73800 20.32600  1.000 45.66000  ? 74  LEU A O   1 
ATOM   1459 C CB  . LEU B 1 92  ? 10.93600  50.26600 18.79700  1.000 45.08000  ? 74  LEU A CB  1 
ATOM   1460 C CG  . LEU B 1 92  ? 11.24300  48.88900 18.20400  1.000 43.47000  ? 74  LEU A CG  1 
ATOM   1461 C CD1 . LEU B 1 92  ? 10.65800  47.78500 19.07300  1.000 41.64000  ? 74  LEU A CD1 1 
ATOM   1462 C CD2 . LEU B 1 92  ? 10.72600  48.79000 16.77800  1.000 47.76000  ? 74  LEU A CD2 1 
ATOM   1463 N N   . MET B 1 93  ? 13.63800  51.75300 19.34200  1.000 38.53000  ? 75  MET A N   1 
ATOM   1464 C CA  . MET B 1 93  ? 15.08000  51.92500 19.19900  1.000 36.37000  ? 75  MET A CA  1 
ATOM   1465 C C   . MET B 1 93  ? 15.75900  52.04500 20.55800  1.000 38.92000  ? 75  MET A C   1 
ATOM   1466 O O   . MET B 1 93  ? 16.81100  51.43900 20.79000  1.000 35.84000  ? 75  MET A O   1 
ATOM   1467 C CB  . MET B 1 93  ? 15.38600  53.15900 18.34800  1.000 31.31000  ? 75  MET A CB  1 
ATOM   1468 C CG  . MET B 1 93  ? 14.87200  53.10400 16.91900  1.000 42.30000  ? 75  MET A CG  1 
ATOM   1469 S SD  . MET B 1 93  ? 15.35000  54.57500 15.98700  1.000 39.19000  ? 75  MET A SD  1 
ATOM   1470 C CE  . MET B 1 93  ? 14.55300  54.27100 14.41200  1.000 44.50000  ? 75  MET A CE  1 
ATOM   1471 N N   . SER B 1 94  ? 15.17800  52.80900 21.46500  1.000 37.78000  ? 76  SER A N   1 
ATOM   1472 C CA  . SER B 1 94  ? 15.82400  53.07800 22.77100  1.000 46.73000  ? 76  SER A CA  1 
ATOM   1473 C C   . SER B 1 94  ? 15.90300  51.80300 23.60900  1.000 40.66000  ? 76  SER A C   1 
ATOM   1474 O O   . SER B 1 94  ? 16.93400  51.57900 24.23000  1.000 50.76000  ? 76  SER A O   1 
ATOM   1475 C CB  . SER B 1 94  ? 15.08700  54.17500 23.48100  1.000 39.81000  ? 76  SER A CB  1 
ATOM   1476 O OG  . SER B 1 94  ? 15.71400  54.49600 24.70700  1.000 83.44000  ? 76  SER A OG  1 
ATOM   1477 N N   . ASN B 1 95  ? 14.85300  50.99700 23.58300  1.000 43.03000  ? 77  ASN A N   1 
ATOM   1478 C CA  . ASN B 1 95  ? 14.82300  49.78600 24.39300  1.000 56.89000  ? 77  ASN A CA  1 
ATOM   1479 C C   . ASN B 1 95  ? 15.67700  48.66000 23.82400  1.000 43.82000  ? 77  ASN A C   1 
ATOM   1480 O O   . ASN B 1 95  ? 15.95800  47.69800 24.54500  1.000 51.50000  ? 77  ASN A O   1 
ATOM   1481 C CB  . ASN B 1 95  ? 13.38100  49.29300 24.55800  1.000 64.19000  ? 77  ASN A CB  1 
ATOM   1482 C CG  . ASN B 1 95  ? 12.55200  50.19600 25.45200  1.000 56.08000  ? 77  ASN A CG  1 
ATOM   1483 O OD1 . ASN B 1 95  ? 13.08900  50.93500 26.27800  1.000 74.62000  ? 77  ASN A OD1 1 
ATOM   1484 N ND2 . ASN B 1 95  ? 11.23500  50.13400 25.29600  1.000 57.31000  ? 77  ASN A ND2 1 
ATOM   1485 N N   . ASN B 1 96  ? 16.09500  48.74600 22.56000  1.000 42.31000  ? 78  ASN A N   1 
ATOM   1486 C CA  . ASN B 1 96  ? 16.89700  47.69700 21.94800  1.000 47.54000  ? 78  ASN A CA  1 
ATOM   1487 C C   . ASN B 1 96  ? 18.27400  48.16500 21.49600  1.000 49.10000  ? 78  ASN A C   1 
ATOM   1488 O O   . ASN B 1 96  ? 19.01000  47.37200 20.89700  1.000 46.21000  ? 78  ASN A O   1 
ATOM   1489 C CB  . ASN B 1 96  ? 16.15600  47.08500 20.75000  1.000 51.98000  ? 78  ASN A CB  1 
ATOM   1490 C CG  . ASN B 1 96  ? 14.88900  46.35800 21.15500  1.000 53.51000  ? 78  ASN A CG  1 
ATOM   1491 O OD1 . ASN B 1 96  ? 14.93500  45.23000 21.64400  1.000 63.01000  ? 78  ASN A OD1 1 
ATOM   1492 N ND2 . ASN B 1 96  ? 13.74600  46.99900 20.94000  1.000 53.70000  ? 78  ASN A ND2 1 
ATOM   1493 N N   . ILE B 1 97  ? 18.65000  49.41600 21.77000  1.000 49.76000  ? 79  ILE A N   1 
ATOM   1494 C CA  . ILE B 1 97  ? 19.92500  49.93100 21.27800  1.000 45.59000  ? 79  ILE A CA  1 
ATOM   1495 C C   . ILE B 1 97  ? 21.10100  49.24400 21.96500  1.000 38.64000  ? 79  ILE A C   1 
ATOM   1496 O O   . ILE B 1 97  ? 22.18700  49.12900 21.38200  1.000 41.92000  ? 79  ILE A O   1 
ATOM   1497 C CB  . ILE B 1 97  ? 19.98000  51.46300 21.45000  1.000 51.86000  ? 79  ILE A CB  1 
ATOM   1498 C CG1 . ILE B 1 97  ? 21.22800  52.04100 20.78000  1.000 42.43000  ? 79  ILE A CG1 1 
ATOM   1499 C CG2 . ILE B 1 97  ? 19.93400  51.84500 22.92500  1.000 46.46000  ? 79  ILE A CG2 1 
ATOM   1500 C CD1 . ILE B 1 97  ? 21.33000  53.54100 20.88800  1.000 44.85000  ? 79  ILE A CD1 1 
ATOM   1501 N N   . HIS B 1 98  ? 20.91200  48.76500 23.19800  1.000 46.36000  ? 80  HIS A N   1 
ATOM   1502 C CA  . HIS B 1 98  ? 22.00800  48.14200 23.93200  1.000 47.07000  ? 80  HIS A CA  1 
ATOM   1503 C C   . HIS B 1 98  ? 22.43900  46.81600 23.32100  1.000 54.63000  ? 80  HIS A C   1 
ATOM   1504 O O   . HIS B 1 98  ? 23.57600  46.38600 23.54200  1.000 44.82000  ? 80  HIS A O   1 
ATOM   1505 C CB  . HIS B 1 98  ? 21.61100  47.93300 25.39400  1.000 50.80000  ? 80  HIS A CB  1 
ATOM   1506 C CG  . HIS B 1 98  ? 20.55600  46.89100 25.59100  1.000 47.81000  ? 80  HIS A CG  1 
ATOM   1507 N ND1 . HIS B 1 98  ? 19.20800  47.16800 25.50000  1.000 53.10000  ? 80  HIS A ND1 1 
ATOM   1508 C CD2 . HIS B 1 98  ? 20.64800  45.57100 25.88100  1.000 50.50000  ? 80  HIS A CD2 1 
ATOM   1509 C CE1 . HIS B 1 98  ? 18.51700  46.06500 25.72200  1.000 53.99000  ? 80  HIS A CE1 1 
ATOM   1510 N NE2 . HIS B 1 98  ? 19.36800  45.08000 25.95600  1.000 53.07000  ? 80  HIS A NE2 1 
ATOM   1511 N N   . LYS B 1 99  ? 21.55800  46.15800 22.56300  1.000 44.61000  ? 81  LYS A N   1 
ATOM   1512 C CA  . LYS B 1 99  ? 21.92000  44.91000 21.90400  1.000 44.72000  ? 81  LYS A CA  1 
ATOM   1513 C C   . LYS B 1 99  ? 22.93200  45.11900 20.78700  1.000 50.88000  ? 81  LYS A C   1 
ATOM   1514 O O   . LYS B 1 99  ? 23.64800  44.17600 20.43100  1.000 51.03000  ? 81  LYS A O   1 
ATOM   1515 C CB  . LYS B 1 99  ? 20.66600  44.22600 21.35700  1.000 41.08000  ? 81  LYS A CB  1 
ATOM   1516 C CG  . LYS B 1 99  ? 19.64800  43.87000 22.42700  1.000 42.05000  ? 81  LYS A CG  1 
ATOM   1517 C CD  . LYS B 1 99  ? 18.38100  43.29000 21.82400  1.000 62.90000  ? 81  LYS A CD  1 
ATOM   1518 C CE  . LYS B 1 99  ? 17.37600  42.93000 22.90700  1.000 79.80000  ? 81  LYS A CE  1 
ATOM   1519 N NZ  . LYS B 1 99  ? 16.11700  42.37000 22.34300  1.000 67.21000  ? 81  LYS A NZ  1 
ATOM   1520 N N   . ALA B 1 100 ? 23.04300  46.32600 20.25700  1.000 46.52000  ? 82  ALA A N   1 
ATOM   1521 C CA  . ALA B 1 100 ? 24.04600  46.58100 19.20600  1.000 44.86000  ? 82  ALA A CA  1 
ATOM   1522 C C   . ALA B 1 100 ? 25.44500  46.75200 19.79800  1.000 50.74000  ? 82  ALA A C   1 
ATOM   1523 O O   . ALA B 1 100 ? 26.38500  46.89700 19.02300  1.000 51.03000  ? 82  ALA A O   1 
ATOM   1524 C CB  . ALA B 1 100 ? 23.64600  47.77600 18.39600  1.000 46.12000  ? 82  ALA A CB  1 
ATOM   1525 N N   . LEU B 1 101 ? 25.56400  46.73500 21.11900  1.000 55.89000  ? 83  LEU A N   1 
ATOM   1526 C CA  . LEU B 1 101 ? 26.88300  46.95200 21.76200  1.000 59.46000  ? 83  LEU A CA  1 
ATOM   1527 C C   . LEU B 1 101 ? 27.61200  45.61600 21.87300  1.000 59.29000  ? 83  LEU A C   1 
ATOM   1528 O O   . LEU B 1 101 ? 28.80000  45.63300 22.17800  1.000 64.43000  ? 83  LEU A O   1 
ATOM   1529 C CB  . LEU B 1 101 ? 26.68200  47.60800 23.12600  1.000 58.15000  ? 83  LEU A CB  1 
ATOM   1530 C CG  . LEU B 1 101 ? 26.30800  49.08600 23.08900  1.000 69.38000  ? 83  LEU A CG  1 
ATOM   1531 C CD1 . LEU B 1 101 ? 25.92300  49.57700 24.47300  1.000 62.95000  ? 83  LEU A CD1 1 
ATOM   1532 C CD2 . LEU B 1 101 ? 27.44900  49.91300 22.52800  1.000 53.83000  ? 83  LEU A CD2 1 
ATOM   1533 N N   . GLU B 1 102 ? 26.92200  44.51200 21.60200  1.000 60.23000  ? 84  GLU A N   1 
ATOM   1534 C CA  . GLU B 1 102 ? 27.60600  43.22900 21.61000  1.000 60.66000  ? 84  GLU A CA  1 
ATOM   1535 C C   . GLU B 1 102 ? 28.48300  43.10000 20.36700  1.000 67.34000  ? 84  GLU A C   1 
ATOM   1536 O O   . GLU B 1 102 ? 28.11200  43.58400 19.29200  1.000 72.75000  ? 84  GLU A O   1 
ATOM   1537 C CB  . GLU B 1 102 ? 26.59700  42.08100 21.66200  1.000 65.52000  ? 84  GLU A CB  1 
ATOM   1538 C CG  . GLU B 1 102 ? 25.64600  42.14000 22.84800  1.000 85.36000  ? 84  GLU A CG  1 
ATOM   1539 N N   . PRO B 1 103 ? 29.65100  42.47000 20.48100  1.000 76.20000  ? 85  PRO A N   1 
ATOM   1540 C CA  . PRO B 1 103 ? 30.53300  42.33000 19.31400  1.000 69.84000  ? 85  PRO A CA  1 
ATOM   1541 C C   . PRO B 1 103 ? 29.87000  41.52500 18.20400  1.000 53.70000  ? 85  PRO A C   1 
ATOM   1542 O O   . PRO B 1 103 ? 29.30100  40.45700 18.44000  1.000 58.47000  ? 85  PRO A O   1 
ATOM   1543 C CB  . PRO B 1 103 ? 31.76000  41.60700 19.88200  1.000 86.84000  ? 85  PRO A CB  1 
ATOM   1544 C CG  . PRO B 1 103 ? 31.73300  41.90500 21.34600  1.000 88.35000  ? 85  PRO A CG  1 
ATOM   1545 C CD  . PRO B 1 103 ? 30.28100  41.97000 21.71400  1.000 83.53000  ? 85  PRO A CD  1 
ATOM   1546 N N   . GLY B 1 104 ? 29.94800  42.05300 16.98500  1.000 63.59000  ? 86  GLY A N   1 
ATOM   1547 C CA  . GLY B 1 104 ? 29.39100  41.39700 15.82200  1.000 61.75000  ? 86  GLY A CA  1 
ATOM   1548 C C   . GLY B 1 104 ? 27.89300  41.52200 15.66100  1.000 78.79000  ? 86  GLY A C   1 
ATOM   1549 O O   . GLY B 1 104 ? 27.35300  41.02200 14.66500  1.000 69.30000  ? 86  GLY A O   1 
ATOM   1550 N N   . ARG B 1 105 ? 27.24400  42.21000 16.60300  1.000 57.55000  ? 87  ARG A N   1 
ATOM   1551 C CA  . ARG B 1 105 ? 25.76300  42.32100 16.58400  1.000 55.67000  ? 87  ARG A CA  1 
ATOM   1552 C C   . ARG B 1 105 ? 25.30900  43.60000 15.88000  1.000 62.47000  ? 87  ARG A C   1 
ATOM   1553 O O   . ARG B 1 105 ? 25.90900  44.66100 16.12500  1.000 66.30000  ? 87  ARG A O   1 
ATOM   1554 C CB  . ARG B 1 105 ? 25.20100  42.27500 18.00700  1.000 61.40000  ? 87  ARG A CB  1 
ATOM   1555 C CG  . ARG B 1 105 ? 25.23400  40.89300 18.64000  1.000 71.93000  ? 87  ARG A CG  1 
ATOM   1556 C CD  . ARG B 1 105 ? 24.50100  39.88100 17.78300  1.000 73.54000  ? 87  ARG A CD  1 
ATOM   1557 N NE  . ARG B 1 105 ? 24.31900  38.59800 18.44500  1.000 87.87000  ? 87  ARG A NE  1 
ATOM   1558 C CZ  . ARG B 1 105 ? 23.58600  38.40600 19.53600  1.000 94.02000  ? 87  ARG A CZ  1 
ATOM   1559 N NH1 . ARG B 1 105 ? 22.77800  39.35700 19.96800  1.000 100.29000 ? 87  ARG A NH1 1 
ATOM   1560 N NH2 . ARG B 1 105 ? 23.65300  37.25500 20.18200  1.000 82.52000  ? 87  ARG A NH2 1 
ATOM   1561 N N   . THR B 1 106 ? 24.28900  43.48600 15.03500  1.000 59.20000  ? 88  THR A N   1 
ATOM   1562 C CA  . THR B 1 106 ? 23.70900  44.62700 14.34100  1.000 51.08000  ? 88  THR A CA  1 
ATOM   1563 C C   . THR B 1 106 ? 22.19900  44.58800 14.51900  1.000 55.24000  ? 88  THR A C   1 
ATOM   1564 O O   . THR B 1 106 ? 21.57600  43.54100 14.31900  1.000 58.95000  ? 88  THR A O   1 
ATOM   1565 C CB  . THR B 1 106 ? 24.06700  44.62000 12.85000  1.000 62.35000  ? 88  THR A CB  1 
ATOM   1566 O OG1 . THR B 1 106 ? 25.49200  44.64300 12.69800  1.000 65.15000  ? 88  THR A OG1 1 
ATOM   1567 C CG2 . THR B 1 106 ? 23.46800  45.83200 12.14900  1.000 53.29000  ? 88  THR A CG2 1 
ATOM   1568 N N   . VAL B 1 107 ? 21.61700  45.72300 14.90100  1.000 45.50000  ? 89  VAL A N   1 
ATOM   1569 C CA  . VAL B 1 107 ? 20.17900  45.84800 15.10800  1.000 47.09000  ? 89  VAL A CA  1 
ATOM   1570 C C   . VAL B 1 107 ? 19.61100  46.72200 13.99900  1.000 47.31000  ? 89  VAL A C   1 
ATOM   1571 O O   . VAL B 1 107 ? 20.15800  47.79200 13.70100  1.000 47.06000  ? 89  VAL A O   1 
ATOM   1572 C CB  . VAL B 1 107 ? 19.85600  46.43400 16.49300  1.000 44.80000  ? 89  VAL A CB  1 
ATOM   1573 C CG1 . VAL B 1 107 ? 18.36700  46.33500 16.76900  1.000 49.13000  ? 89  VAL A CG1 1 
ATOM   1574 C CG2 . VAL B 1 107 ? 20.65100  45.71600 17.57300  1.000 52.51000  ? 89  VAL A CG2 1 
ATOM   1575 N N   . VAL B 1 108 ? 18.51600  46.27000 13.39300  1.000 44.03000  ? 90  VAL A N   1 
ATOM   1576 C CA  . VAL B 1 108 ? 17.91200  46.93400 12.24600  1.000 35.74000  ? 90  VAL A CA  1 
ATOM   1577 C C   . VAL B 1 108 ? 16.50300  47.38100 12.61300  1.000 36.34000  ? 90  VAL A C   1 
ATOM   1578 O O   . VAL B 1 108 ? 15.74600  46.63100 13.23900  1.000 45.67000  ? 90  VAL A O   1 
ATOM   1579 C CB  . VAL B 1 108 ? 17.88600  46.01100 11.00900  1.000 56.18000  ? 90  VAL A CB  1 
ATOM   1580 C CG1 . VAL B 1 108 ? 17.47200  46.78800 9.77200   1.000 50.16000  ? 90  VAL A CG1 1 
ATOM   1581 C CG2 . VAL B 1 108 ? 19.24400  45.35300 10.80700  1.000 52.36000  ? 90  VAL A CG2 1 
ATOM   1582 N N   . PHE B 1 109 ? 16.15600  48.60600 12.22300  1.000 44.38000  ? 91  PHE A N   1 
ATOM   1583 C CA  . PHE B 1 109 ? 14.81600  49.15100 12.41100  1.000 39.70000  ? 91  PHE A CA  1 
ATOM   1584 C C   . PHE B 1 109 ? 14.31700  49.65600 11.06600  1.000 36.36000  ? 91  PHE A C   1 
ATOM   1585 O O   . PHE B 1 109 ? 14.95600  50.51700 10.45300  1.000 41.41000  ? 91  PHE A O   1 
ATOM   1586 C CB  . PHE B 1 109 ? 14.80900  50.28700 13.44000  1.000 32.11000  ? 91  PHE A CB  1 
ATOM   1587 C CG  . PHE B 1 109 ? 15.42700  49.92000 14.76100  1.000 35.81000  ? 91  PHE A CG  1 
ATOM   1588 C CD1 . PHE B 1 109 ? 14.66100  49.35600 15.76800  1.000 31.85000  ? 91  PHE A CD1 1 
ATOM   1589 C CD2 . PHE B 1 109 ? 16.77100  50.15300 14.99900  1.000 39.64000  ? 91  PHE A CD2 1 
ATOM   1590 C CE1 . PHE B 1 109 ? 15.22700  49.02300 16.98500  1.000 35.20000  ? 91  PHE A CE1 1 
ATOM   1591 C CE2 . PHE B 1 109 ? 17.34200  49.82300 16.21400  1.000 39.40000  ? 91  PHE A CE2 1 
ATOM   1592 C CZ  . PHE B 1 109 ? 16.56700  49.25900 17.20800  1.000 41.76000  ? 91  PHE A CZ  1 
ATOM   1593 N N   . GLY B 1 110 ? 13.18200  49.12900 10.61000  1.000 43.72000  ? 92  GLY A N   1 
ATOM   1594 C CA  . GLY B 1 110 ? 12.63100  49.51200 9.33200   1.000 38.77000  ? 92  GLY A CA  1 
ATOM   1595 C C   . GLY B 1 110 ? 11.11900  49.41100 9.28300   1.000 43.20000  ? 92  GLY A C   1 
ATOM   1596 O O   . GLY B 1 110 ? 10.44800  49.28200 10.31100  1.000 41.12000  ? 92  GLY A O   1 
ATOM   1597 N N   . PRO B 1 111 ? 10.55300  49.48100 8.07400   1.000 51.44000  ? 93  PRO A N   1 
ATOM   1598 C CA  . PRO B 1 111 ? 9.09100   49.35500 7.94400   1.000 48.60000  ? 93  PRO A CA  1 
ATOM   1599 C C   . PRO B 1 111 ? 8.54800   48.02600 8.43900   1.000 49.94000  ? 93  PRO A C   1 
ATOM   1600 O O   . PRO B 1 111 ? 7.38500   47.96100 8.85500   1.000 66.34000  ? 93  PRO A O   1 
ATOM   1601 C CB  . PRO B 1 111 ? 8.85900   49.53400 6.43600   1.000 48.76000  ? 93  PRO A CB  1 
ATOM   1602 C CG  . PRO B 1 111 ? 10.04900  50.29900 5.95700   1.000 57.21000  ? 93  PRO A CG  1 
ATOM   1603 C CD  . PRO B 1 111 ? 11.19700  49.81400 6.79300   1.000 47.48000  ? 93  PRO A CD  1 
ATOM   1604 N N   . GLU B 1 112 ? 9.35400   46.96100 8.40300   1.000 63.30000  ? 94  GLU A N   1 
ATOM   1605 C CA  . GLU B 1 112 ? 8.91900   45.68100 8.95400   1.000 75.14000  ? 94  GLU A CA  1 
ATOM   1606 C C   . GLU B 1 112 ? 8.86600   45.72500 10.47600  1.000 74.73000  ? 94  GLU A C   1 
ATOM   1607 O O   . GLU B 1 112 ? 7.84700   45.37400 11.08200  1.000 88.45000  ? 94  GLU A O   1 
ATOM   1608 C CB  . GLU B 1 112 ? 9.85000   44.55900 8.49100   1.000 71.03000  ? 94  GLU A CB  1 
ATOM   1609 C CG  . GLU B 1 112 ? 9.47700   43.92500 7.16300   1.000 84.08000  ? 94  GLU A CG  1 
ATOM   1610 N N   . GLY B 1 113 ? 9.95800   46.14600 11.10900  1.000 65.21000  ? 95  GLY A N   1 
ATOM   1611 C CA  . GLY B 1 113 ? 10.04600  46.16000 12.55600  1.000 51.94000  ? 95  GLY A CA  1 
ATOM   1612 C C   . GLY B 1 113 ? 11.47800  46.13900 13.04500  1.000 56.07000  ? 95  GLY A C   1 
ATOM   1613 O O   . GLY B 1 113 ? 12.33500  46.83700 12.49200  1.000 55.68000  ? 95  GLY A O   1 
ATOM   1614 N N   . CYS B 1 114 ? 11.72300  45.34300 14.09000  1.000 64.08000  ? 96  CYS A N   1 
ATOM   1615 C CA  . CYS B 1 114 ? 13.09200  45.22400 14.65100  1.000 53.54000  ? 96  CYS A CA  1 
ATOM   1616 C C   . CYS B 1 114 ? 13.73700  43.94200 14.12600  1.000 59.23000  ? 96  CYS A C   1 
ATOM   1617 O O   . CYS B 1 114 ? 12.99700  43.01900 13.75000  1.000 49.24000  ? 96  CYS A O   1 
ATOM   1618 C CB  . CYS B 1 114 ? 13.06900  45.20500 16.17400  1.000 40.84000  ? 96  CYS A CB  1 
ATOM   1619 S SG  . CYS B 1 114 ? 14.72000  45.22500 16.92000  1.000 59.06000  ? 96  CYS A SG  1 
ATOM   1620 N N   . GLU B 1 115 ? 15.06500  43.89300 14.13200  1.000 53.99000  ? 97  GLU A N   1 
ATOM   1621 C CA  . GLU B 1 115 ? 15.79400  42.74900 13.60000  1.000 53.08000  ? 97  GLU A CA  1 
ATOM   1622 C C   . GLU B 1 115 ? 17.20800  42.75100 14.16100  1.000 62.65000  ? 97  GLU A C   1 
ATOM   1623 O O   . GLU B 1 115 ? 17.92900  43.74400 14.02400  1.000 62.65000  ? 97  GLU A O   1 
ATOM   1624 C CB  . GLU B 1 115 ? 15.82300  42.79100 12.06800  1.000 56.64000  ? 97  GLU A CB  1 
ATOM   1625 C CG  . GLU B 1 115 ? 16.69600  41.72600 11.42100  1.000 69.00000  ? 97  GLU A CG  1 
ATOM   1626 C CD  . GLU B 1 115 ? 16.77400  41.87600 9.91300   1.000 81.76000  ? 97  GLU A CD  1 
ATOM   1627 O OE1 . GLU B 1 115 ? 16.00300  42.68300 9.35100   1.000 81.87000  ? 97  GLU A OE1 1 
ATOM   1628 O OE2 . GLU B 1 115 ? 17.60900  41.18900 9.28800   1.000 86.13000  ? 97  GLU A OE2 1 
ATOM   1629 N N   . GLU B 1 116 ? 17.58400  41.66000 14.83200  1.000 55.44000  ? 98  GLU A N   1 
ATOM   1630 C CA  . GLU B 1 116 ? 18.97100  41.49300 15.32900  1.000 46.88000  ? 98  GLU A CA  1 
ATOM   1631 C C   . GLU B 1 116 ? 19.73200  40.56700 14.37600  1.000 60.36000  ? 98  GLU A C   1 
ATOM   1632 O O   . GLU B 1 116 ? 19.14800  39.58800 13.92000  1.000 69.56000  ? 98  GLU A O   1 
ATOM   1633 C CB  . GLU B 1 116 ? 18.97300  40.87800 16.72100  1.000 62.43000  ? 98  GLU A CB  1 
ATOM   1634 C CG  . GLU B 1 116 ? 18.48500  41.78900 17.82500  1.000 68.99000  ? 98  GLU A CG  1 
ATOM   1635 C CD  . GLU B 1 116 ? 18.48000  41.10600 19.18100  1.000 86.32000  ? 98  GLU A CD  1 
ATOM   1636 O OE1 . GLU B 1 116 ? 19.55500  40.65100 19.61700  1.000 85.93000  ? 98  GLU A OE1 1 
ATOM   1637 O OE2 . GLU B 1 116 ? 17.40300  41.02400 19.79400  1.000 86.41000  ? 98  GLU A OE2 1 
ATOM   1638 N N   . ARG B 1 117 ? 20.99900  40.87900 14.09700  1.000 62.21000  ? 99  ARG A N   1 
ATOM   1639 C CA  . ARG B 1 117 ? 21.78700  40.07200 13.13200  1.000 70.05000  ? 99  ARG A CA  1 
ATOM   1640 C C   . ARG B 1 117 ? 23.20700  39.82400 13.65100  1.000 82.97000  ? 99  ARG A C   1 
ATOM   1641 O O   . ARG B 1 117 ? 23.72000  40.67700 14.39300  1.000 89.94000  ? 99  ARG A O   1 
ATOM   1642 C CB  . ARG B 1 117 ? 21.87700  40.78800 11.78300  1.000 75.46000  ? 99  ARG A CB  1 
ATOM   1643 C CG  . ARG B 1 117 ? 20.59900  41.49400 11.35500  1.000 81.80000  ? 99  ARG A CG  1 
ATOM   1644 C CD  . ARG B 1 117 ? 20.69100  42.01900 9.93700   1.000 83.48000  ? 99  ARG A CD  1 
ATOM   1645 N NE  . ARG B 1 117 ? 20.32200  41.00500 8.96100   1.000 113.22000 ? 99  ARG A NE  1 
ATOM   1646 C CZ  . ARG B 1 117 ? 21.13100  40.53500 8.02000   1.000 103.28000 ? 99  ARG A CZ  1 
ATOM   1647 N NH1 . ARG B 1 117 ? 22.43000  40.77100 8.08400   1.000 82.33000  ? 99  ARG A NH1 1 
ATOM   1648 N NH2 . ARG B 1 117 ? 20.63800  39.83500 7.01500   1.000 95.37000  ? 99  ARG A NH2 1 
ATOM   1649 N N   . ASP B 1 118 ? 23.81000  38.69600 13.26600  1.000 78.18000  ? 100 ASP A N   1 
ATOM   1650 C CA  . ASP B 1 118 ? 25.21400  38.38200 13.63500  1.000 79.68000  ? 100 ASP A CA  1 
ATOM   1651 C C   . ASP B 1 118 ? 26.06600  38.57500 12.38000  1.000 82.87000  ? 100 ASP A C   1 
ATOM   1652 O O   . ASP B 1 118 ? 25.69900  38.02500 11.33600  1.000 85.18000  ? 100 ASP A O   1 
ATOM   1653 C CB  . ASP B 1 118 ? 25.35800  36.99000 14.24600  1.000 83.70000  ? 100 ASP A CB  1 
ATOM   1654 C CG  . ASP B 1 118 ? 26.78900  36.59400 14.55600  1.000 94.01000  ? 100 ASP A CG  1 
ATOM   1655 O OD1 . ASP B 1 118 ? 27.59100  36.49500 13.60900  1.000 88.72000  ? 100 ASP A OD1 1 
ATOM   1656 O OD2 . ASP B 1 118 ? 27.08500  36.38200 15.74400  1.000 102.64000 ? 100 ASP A OD2 1 
ATOM   1657 N N   . LYS B 1 119 ? 27.15200  39.33600 12.49300  1.000 84.35000  ? 101 LYS A N   1 
ATOM   1658 C CA  . LYS B 1 119 ? 27.98700  39.66900 11.30500  1.000 97.87000  ? 101 LYS A CA  1 
ATOM   1659 C C   . LYS B 1 119 ? 28.27500  38.42300 10.46000  1.000 106.89000 ? 101 LYS A C   1 
ATOM   1660 O O   . LYS B 1 119 ? 28.47800  38.57300 9.24700   1.000 107.40000 ? 101 LYS A O   1 
ATOM   1661 C CB  . LYS B 1 119 ? 29.29500  40.33400 11.74400  1.000 102.83000 ? 101 LYS A CB  1 
ATOM   1662 N N   . ASN B 1 120 ? 28.31400  37.25000 11.08000  1.000 97.57000  ? 102 ASN A N   1 
ATOM   1663 C CA  . ASN B 1 120 ? 28.66900  36.02500 10.32900  1.000 97.84000  ? 102 ASN A CA  1 
ATOM   1664 C C   . ASN B 1 120 ? 27.44000  35.13100 10.18700  1.000 95.14000  ? 102 ASN A C   1 
ATOM   1665 O O   . ASN B 1 120 ? 27.17900  34.69400 9.06000   1.000 93.38000  ? 102 ASN A O   1 
ATOM   1666 C CB  . ASN B 1 120 ? 29.81300  35.27200 11.01000  1.000 60.00000  ? 102 ASN A CB  1 
ATOM   1667 C CG  . ASN B 1 120 ? 31.14600  35.98000 10.86400  1.000 60.00000  ? 102 ASN A CG  1 
ATOM   1668 O OD1 . ASN B 1 120 ? 31.34200  36.77500 9.94500   1.000 60.00000  ? 102 ASN A OD1 1 
ATOM   1669 N ND2 . ASN B 1 120 ? 32.07200  35.69200 11.77100  1.000 60.00000  ? 102 ASN A ND2 1 
ATOM   1670 N N   . ARG B 1 121 ? 26.69600  34.91200 11.27200  1.000 101.95000 ? 103 ARG A N   1 
ATOM   1671 C CA  . ARG B 1 121 ? 25.54500  33.96800 11.27100  1.000 90.62000  ? 103 ARG A CA  1 
ATOM   1672 C C   . ARG B 1 121 ? 24.31900  34.53000 10.53800  1.000 82.67000  ? 103 ARG A C   1 
ATOM   1673 O O   . ARG B 1 121 ? 23.46000  33.73400 10.15500  1.000 74.69000  ? 103 ARG A O   1 
ATOM   1674 C CB  . ARG B 1 121 ? 25.21800  33.60200 12.72100  1.000 85.62000  ? 103 ARG A CB  1 
ATOM   1675 N N   . GLY B 1 122 ? 24.18500  35.78900 10.25100  1.000 87.22000  ? 104 GLY A N   1 
ATOM   1676 C CA  . GLY B 1 122 ? 23.01200  36.45900 9.66700   1.000 74.99000  ? 104 GLY A CA  1 
ATOM   1677 C C   . GLY B 1 122 ? 21.94600  36.79400 10.69100  1.000 74.65000  ? 104 GLY A C   1 
ATOM   1678 O O   . GLY B 1 122 ? 22.30700  37.25700 11.76900  1.000 72.02000  ? 104 GLY A O   1 
ATOM   1679 N N   . ILE B 1 123 ? 20.67900  36.55600 10.36100  1.000 71.94000  ? 105 ILE A N   1 
ATOM   1680 C CA  . ILE B 1 123 ? 19.55500  36.94300 11.25700  1.000 72.11000  ? 105 ILE A CA  1 
ATOM   1681 C C   . ILE B 1 123 ? 19.49200  36.01700 12.46700  1.000 68.23000  ? 105 ILE A C   1 
ATOM   1682 O O   . ILE B 1 123 ? 19.81600  34.83900 12.32500  1.000 70.92000  ? 105 ILE A O   1 
ATOM   1683 C CB  . ILE B 1 123 ? 18.21200  36.97300 10.50200  1.000 70.30000  ? 105 ILE A CB  1 
ATOM   1684 C CG1 . ILE B 1 123 ? 18.18800  38.04900 9.41700   1.000 77.15000  ? 105 ILE A CG1 1 
ATOM   1685 C CG2 . ILE B 1 123 ? 17.04400  37.13600 11.46100  1.000 64.08000  ? 105 ILE A CG2 1 
ATOM   1686 C CD1 . ILE B 1 123 ? 16.82600  38.23800 8.79200   1.000 85.76000  ? 105 ILE A CD1 1 
ATOM   1687 N N   . ILE B 1 124 ? 19.09600  36.57000 13.60600  1.000 72.59000  ? 106 ILE A N   1 
ATOM   1688 C CA  . ILE B 1 124 ? 18.96700  35.79600 14.86100  1.000 57.09000  ? 106 ILE A CA  1 
ATOM   1689 C C   . ILE B 1 124 ? 17.53800  35.99800 15.36600  1.000 71.87000  ? 106 ILE A C   1 
ATOM   1690 O O   . ILE B 1 124 ? 16.87600  34.98700 15.60400  1.000 64.49000  ? 106 ILE A O   1 
ATOM   1691 C CB  . ILE B 1 124 ? 20.00200  36.29700 15.88000  1.000 70.53000  ? 106 ILE A CB  1 
ATOM   1692 C CG1 . ILE B 1 124 ? 21.37600  36.51400 15.24400  1.000 73.31000  ? 106 ILE A CG1 1 
ATOM   1693 C CG2 . ILE B 1 124 ? 20.07100  35.37200 17.08400  1.000 69.74000  ? 106 ILE A CG2 1 
ATOM   1694 C CD1 . ILE B 1 124 ? 22.30200  37.34600 16.09000  1.000 83.36000  ? 106 ILE A CD1 1 
ATOM   1695 N N   . LYS B 1 125 ? 17.07700  37.24600 15.52300  1.000 61.03000  ? 107 LYS A N   1 
ATOM   1696 C CA  . LYS B 1 125 ? 15.67100  37.40200 15.93900  1.000 54.99000  ? 107 LYS A CA  1 
ATOM   1697 C C   . LYS B 1 125 ? 14.94600  38.40800 15.04500  1.000 52.96000  ? 107 LYS A C   1 
ATOM   1698 O O   . LYS B 1 125 ? 15.60600  39.24200 14.43700  1.000 58.44000  ? 107 LYS A O   1 
ATOM   1699 C CB  . LYS B 1 125 ? 15.61900  37.82800 17.40500  1.000 65.60000  ? 107 LYS A CB  1 
ATOM   1700 C CG  . LYS B 1 125 ? 16.64000  37.17300 18.32200  1.000 75.39000  ? 107 LYS A CG  1 
ATOM   1701 C CD  . LYS B 1 125 ? 16.49200  37.59600 19.76500  1.000 76.58000  ? 107 LYS A CD  1 
ATOM   1702 C CE  . LYS B 1 125 ? 17.62200  37.10700 20.64500  1.000 95.29000  ? 107 LYS A CE  1 
ATOM   1703 N N   . THR B 1 126 ? 13.63000  38.30400 14.97600  1.000 50.16000  ? 108 THR A N   1 
ATOM   1704 C CA  . THR B 1 126 ? 12.81000  39.26700 14.20800  1.000 43.97000  ? 108 THR A CA  1 
ATOM   1705 C C   . THR B 1 126 ? 11.53700  39.55500 14.99400  1.000 43.57000  ? 108 THR A C   1 
ATOM   1706 O O   . THR B 1 126 ? 10.95300  38.62300 15.52400  1.000 44.72000  ? 108 THR A O   1 
ATOM   1707 C CB  . THR B 1 126 ? 12.49400  38.76700 12.79600  1.000 66.47000  ? 108 THR A CB  1 
ATOM   1708 O OG1 . THR B 1 126 ? 13.59000  39.13000 11.95800  1.000 60.70000  ? 108 THR A OG1 1 
ATOM   1709 C CG2 . THR B 1 126 ? 11.20900  39.32900 12.23100  1.000 49.95000  ? 108 THR A CG2 1 
ATOM   1710 N N   . PHE B 1 127 ? 11.19400  40.83400 15.11400  1.000 68.00000  ? 109 PHE A N   1 
ATOM   1711 C CA  . PHE B 1 127 ? 9.91800   41.22600 15.76400  1.000 63.76000  ? 109 PHE A CA  1 
ATOM   1712 C C   . PHE B 1 127 ? 9.20500   42.14600 14.77500  1.000 65.70000  ? 109 PHE A C   1 
ATOM   1713 O O   . PHE B 1 127 ? 9.69800   43.26100 14.54100  1.000 69.97000  ? 109 PHE A O   1 
ATOM   1714 C CB  . PHE B 1 127 ? 10.19400  41.87900 17.11900  1.000 62.51000  ? 109 PHE A CB  1 
ATOM   1715 C CG  . PHE B 1 127 ? 9.00300   42.53200 17.77100  1.000 77.20000  ? 109 PHE A CG  1 
ATOM   1716 C CD1 . PHE B 1 127 ? 7.84100   41.81700 18.00800  1.000 81.47000  ? 109 PHE A CD1 1 
ATOM   1717 C CD2 . PHE B 1 127 ? 9.05300   43.85700 18.17100  1.000 82.31000  ? 109 PHE A CD2 1 
ATOM   1718 C CE1 . PHE B 1 127 ? 6.74900   42.41700 18.61300  1.000 85.67000  ? 109 PHE A CE1 1 
ATOM   1719 C CE2 . PHE B 1 127 ? 7.96300   44.45600 18.78000  1.000 88.72000  ? 109 PHE A CE2 1 
ATOM   1720 C CZ  . PHE B 1 127 ? 6.81200   43.73500 18.99900  1.000 97.69000  ? 109 PHE A CZ  1 
ATOM   1721 N N   . SER B 1 128 ? 8.09300   41.69000 14.20100  1.000 63.73000  ? 110 SER A N   1 
ATOM   1722 C CA  . SER B 1 128 ? 7.44000   42.48600 13.13200  1.000 73.26000  ? 110 SER A CA  1 
ATOM   1723 C C   . SER B 1 128 ? 6.34000   43.38400 13.69300  1.000 83.23000  ? 110 SER A C   1 
ATOM   1724 O O   . SER B 1 128 ? 5.16300   43.00100 13.59000  1.000 94.05000  ? 110 SER A O   1 
ATOM   1725 C CB  . SER B 1 128 ? 6.92200   41.59800 12.03400  1.000 79.97000  ? 110 SER A CB  1 
ATOM   1726 O OG  . SER B 1 128 ? 7.99400   40.96300 11.35400  1.000 79.12000  ? 110 SER A OG  1 
ATOM   1727 N N   . THR B 1 129 ? 6.71500   44.51800 14.28100  1.000 74.18000  ? 111 THR A N   1 
ATOM   1728 C CA  . THR B 1 129 ? 5.71800   45.51600 14.71600  1.000 68.05000  ? 111 THR A CA  1 
ATOM   1729 C C   . THR B 1 129 ? 5.76600   46.69100 13.75000  1.000 76.04000  ? 111 THR A C   1 
ATOM   1730 O O   . THR B 1 129 ? 6.81300   46.90900 13.14300  1.000 82.84000  ? 111 THR A O   1 
ATOM   1731 C CB  . THR B 1 129 ? 6.00400   46.04900 16.11400  1.000 79.67000  ? 111 THR A CB  1 
ATOM   1732 O OG1 . THR B 1 129 ? 4.87200   46.82900 16.49600  1.000 88.93000  ? 111 THR A OG1 1 
ATOM   1733 C CG2 . THR B 1 129 ? 7.26200   46.88500 16.18500  1.000 68.98000  ? 111 THR A CG2 1 
ATOM   1734 N N   . ASP B 1 130 ? 4.67200   47.41900 13.63000  1.000 77.73000  ? 112 ASP A N   1 
ATOM   1735 C CA  . ASP B 1 130 ? 4.56300   48.55800 12.72600  1.000 80.67000  ? 112 ASP A CA  1 
ATOM   1736 C C   . ASP B 1 130 ? 4.67700   49.83700 13.54700  1.000 80.38000  ? 112 ASP A C   1 
ATOM   1737 O O   . ASP B 1 130 ? 3.81100   50.12800 14.37800  1.000 79.61000  ? 112 ASP A O   1 
ATOM   1738 C CB  . ASP B 1 130 ? 3.25200   48.51300 11.94400  1.000 79.71000  ? 112 ASP A CB  1 
ATOM   1739 C CG  . ASP B 1 130 ? 3.26700   49.42200 10.72900  1.000 85.68000  ? 112 ASP A CG  1 
ATOM   1740 O OD1 . ASP B 1 130 ? 3.67300   50.59800 10.86000  1.000 78.72000  ? 112 ASP A OD1 1 
ATOM   1741 O OD2 . ASP B 1 130 ? 2.87800   48.96000 9.63600   1.000 83.39000  ? 112 ASP A OD2 1 
ATOM   1742 N N   . VAL B 1 131 ? 5.75300   50.58700 13.32400  1.000 62.94000  ? 113 VAL A N   1 
ATOM   1743 C CA  . VAL B 1 131 ? 6.00600   51.83900 14.01900  1.000 79.65000  ? 113 VAL A CA  1 
ATOM   1744 C C   . VAL B 1 131 ? 6.07400   53.00400 13.03500  1.000 64.67000  ? 113 VAL A C   1 
ATOM   1745 O O   . VAL B 1 131 ? 6.70100   54.02300 13.31500  1.000 54.69000  ? 113 VAL A O   1 
ATOM   1746 C CB  . VAL B 1 131 ? 7.28300   51.75000 14.87600  1.000 64.80000  ? 113 VAL A CB  1 
ATOM   1747 C CG1 . VAL B 1 131 ? 7.09500   50.75300 16.00600  1.000 65.33000  ? 113 VAL A CG1 1 
ATOM   1748 C CG2 . VAL B 1 131 ? 8.47500   51.36500 14.01100  1.000 43.82000  ? 113 VAL A CG2 1 
ATOM   1749 N N   . LYS B 1 132 ? 5.43400   52.84600 11.87400  1.000 65.76000  ? 114 LYS A N   1 
ATOM   1750 C CA  . LYS B 1 132 ? 5.29100   53.91200 10.87900  1.000 68.23000  ? 114 LYS A CA  1 
ATOM   1751 C C   . LYS B 1 132 ? 6.63800   54.37400 10.32800  1.000 60.79000  ? 114 LYS A C   1 
ATOM   1752 O O   . LYS B 1 132 ? 6.78000   55.52000 9.89600   1.000 70.56000  ? 114 LYS A O   1 
ATOM   1753 C CB  . LYS B 1 132 ? 4.51000   55.10600 11.44300  1.000 59.75000  ? 114 LYS A CB  1 
ATOM   1754 N N   . LEU B 1 133 ? 7.63300   53.49300 10.33400  1.000 53.63000  ? 115 LEU A N   1 
ATOM   1755 C CA  . LEU B 1 133 ? 8.94000   53.83200 9.79000   1.000 61.26000  ? 115 LEU A CA  1 
ATOM   1756 C C   . LEU B 1 133 ? 8.93100   53.69000 8.27300   1.000 65.72000  ? 115 LEU A C   1 
ATOM   1757 O O   . LEU B 1 133 ? 8.53600   52.64900 7.73900   1.000 55.40000  ? 115 LEU A O   1 
ATOM   1758 C CB  . LEU B 1 133 ? 10.02700  52.94500 10.39500  1.000 57.93000  ? 115 LEU A CB  1 
ATOM   1759 C CG  . LEU B 1 133 ? 10.59500  53.38000 11.74700  1.000 53.00000  ? 115 LEU A CG  1 
ATOM   1760 C CD1 . LEU B 1 133 ? 11.68200  52.41900 12.20100  1.000 45.12000  ? 115 LEU A CD1 1 
ATOM   1761 C CD2 . LEU B 1 133 ? 11.13300  54.79800 11.66600  1.000 50.55000  ? 115 LEU A CD2 1 
ATOM   1762 N N   . ASP B 1 134 ? 9.36300   54.74300 7.58200   1.000 56.03000  ? 116 ASP A N   1 
ATOM   1763 C CA  . ASP B 1 134 ? 9.50100   54.72400 6.13300   1.000 68.17000  ? 116 ASP A CA  1 
ATOM   1764 C C   . ASP B 1 134 ? 10.95100  54.60500 5.68800   1.000 61.68000  ? 116 ASP A C   1 
ATOM   1765 O O   . ASP B 1 134 ? 11.21900  54.59300 4.48300   1.000 56.38000  ? 116 ASP A O   1 
ATOM   1766 C CB  . ASP B 1 134 ? 8.87000   55.98100 5.52300   1.000 73.50000  ? 116 ASP A CB  1 
ATOM   1767 C CG  . ASP B 1 134 ? 9.57500   57.25500 5.94800   1.000 93.06000  ? 116 ASP A CG  1 
ATOM   1768 O OD1 . ASP B 1 134 ? 10.16600  57.27500 7.04800   1.000 104.14000 ? 116 ASP A OD1 1 
ATOM   1769 O OD2 . ASP B 1 134 ? 9.53500   58.24000 5.17900   1.000 107.60000 ? 116 ASP A OD2 1 
ATOM   1770 N N   . GLU B 1 135 ? 11.86200  54.54700 6.65800   1.000 75.44000  ? 117 GLU A N   1 
ATOM   1771 C CA  . GLU B 1 135 ? 13.31100  54.40600 6.37200   1.000 51.53000  ? 117 GLU A CA  1 
ATOM   1772 C C   . GLU B 1 135 ? 13.88400  53.27600 7.22700   1.000 40.33000  ? 117 GLU A C   1 
ATOM   1773 O O   . GLU B 1 135 ? 13.15200  52.75300 8.06700   1.000 42.10000  ? 117 GLU A O   1 
ATOM   1774 C CB  . GLU B 1 135 ? 14.03500  55.72800 6.62100   1.000 43.82000  ? 117 GLU A CB  1 
ATOM   1775 C CG  . GLU B 1 135 ? 13.78600  56.77800 5.55800   1.000 68.70000  ? 117 GLU A CG  1 
ATOM   1776 C CD  . GLU B 1 135 ? 14.31600  58.15800 5.90400   1.000 76.09000  ? 117 GLU A CD  1 
ATOM   1777 O OE1 . GLU B 1 135 ? 14.78800  58.33700 7.03700   1.000 77.34000  ? 117 GLU A OE1 1 
ATOM   1778 O OE2 . GLU B 1 135 ? 14.27300  59.04200 5.03200   1.000 79.57000  ? 117 GLU A OE2 1 
ATOM   1779 N N   . THR B 1 136 ? 15.15200  52.95000 7.02500   1.000 43.02000  ? 118 THR A N   1 
ATOM   1780 C CA  . THR B 1 136 ? 15.79800  51.83300 7.70300   1.000 49.76000  ? 118 THR A CA  1 
ATOM   1781 C C   . THR B 1 136 ? 17.01400  52.32500 8.47600   1.000 45.36000  ? 118 THR A C   1 
ATOM   1782 O O   . THR B 1 136 ? 17.81700  53.10400 7.95100   1.000 47.75000  ? 118 THR A O   1 
ATOM   1783 C CB  . THR B 1 136 ? 16.20600  50.74900 6.70200   1.000 53.60000  ? 118 THR A CB  1 
ATOM   1784 O OG1 . THR B 1 136 ? 15.09700  50.45200 5.84500   1.000 68.75000  ? 118 THR A OG1 1 
ATOM   1785 C CG2 . THR B 1 136 ? 16.61800  49.48200 7.43300   1.000 51.77000  ? 118 THR A CG2 1 
ATOM   1786 N N   . TYR B 1 137 ? 17.14800  51.86000 9.71700   1.000 38.69000  ? 119 TYR A N   1 
ATOM   1787 C CA  . TYR B 1 137 ? 18.22000  52.27200 10.61300  1.000 39.91000  ? 119 TYR A CA  1 
ATOM   1788 C C   . TYR B 1 137 ? 19.04900  51.05800 11.00700  1.000 37.23000  ? 119 TYR A C   1 
ATOM   1789 O O   . TYR B 1 137 ? 18.49600  50.02200 11.39300  1.000 44.59000  ? 119 TYR A O   1 
ATOM   1790 C CB  . TYR B 1 137 ? 17.65800  52.95500 11.86300  1.000 36.47000  ? 119 TYR A CB  1 
ATOM   1791 C CG  . TYR B 1 137 ? 16.95400  54.26500 11.58400  1.000 41.28000  ? 119 TYR A CG  1 
ATOM   1792 C CD1 . TYR B 1 137 ? 15.65400  54.28700 11.09500  1.000 39.76000  ? 119 TYR A CD1 1 
ATOM   1793 C CD2 . TYR B 1 137 ? 17.58700  55.47800 11.81600  1.000 39.39000  ? 119 TYR A CD2 1 
ATOM   1794 C CE1 . TYR B 1 137 ? 15.00600  55.48100 10.84100  1.000 50.63000  ? 119 TYR A CE1 1 
ATOM   1795 C CE2 . TYR B 1 137 ? 16.94800  56.67800 11.56600  1.000 39.78000  ? 119 TYR A CE2 1 
ATOM   1796 C CZ  . TYR B 1 137 ? 15.65800  56.67300 11.07800  1.000 43.15000  ? 119 TYR A CZ  1 
ATOM   1797 O OH  . TYR B 1 137 ? 15.02000  57.86600 10.82800  1.000 50.58000  ? 119 TYR A OH  1 
ATOM   1798 N N   . PHE B 1 138 ? 20.35700  51.22100 10.90500  1.000 38.94000  ? 120 PHE A N   1 
ATOM   1799 C CA  . PHE B 1 138 ? 21.29000  50.13200 11.25800  1.000 47.74000  ? 120 PHE A CA  1 
ATOM   1800 C C   . PHE B 1 138 ? 22.17300  50.56300 12.43200  1.000 53.42000  ? 120 PHE A C   1 
ATOM   1801 O O   . PHE B 1 138 ? 22.90100  51.54700 12.31700  1.000 43.99000  ? 120 PHE A O   1 
ATOM   1802 C CB  . PHE B 1 138 ? 22.12200  49.73000 10.03700  1.000 43.23000  ? 120 PHE A CB  1 
ATOM   1803 C CG  . PHE B 1 138 ? 21.34400  49.15200 8.88500   1.000 58.86000  ? 120 PHE A CG  1 
ATOM   1804 C CD1 . PHE B 1 138 ? 20.69800  49.97200 7.97700   1.000 47.63000  ? 120 PHE A CD1 1 
ATOM   1805 C CD2 . PHE B 1 138 ? 21.24700  47.78200 8.71500   1.000 45.30000  ? 120 PHE A CD2 1 
ATOM   1806 C CE1 . PHE B 1 138 ? 19.98400  49.43500 6.92000   1.000 56.86000  ? 120 PHE A CE1 1 
ATOM   1807 C CE2 . PHE B 1 138 ? 20.53000  47.24800 7.65800   1.000 66.63000  ? 120 PHE A CE2 1 
ATOM   1808 C CZ  . PHE B 1 138 ? 19.90000  48.07400 6.76200   1.000 46.84000  ? 120 PHE A CZ  1 
ATOM   1809 N N   . PHE B 1 139 ? 22.08100  49.84000 13.53500  1.000 49.31000  ? 121 PHE A N   1 
ATOM   1810 C CA  . PHE B 1 139 ? 22.90100  50.08800 14.71300  1.000 47.39000  ? 121 PHE A CA  1 
ATOM   1811 C C   . PHE B 1 139 ? 23.93000  48.97200 14.82800  1.000 42.67000  ? 121 PHE A C   1 
ATOM   1812 O O   . PHE B 1 139 ? 23.56200  47.79400 14.86800  1.000 44.98000  ? 121 PHE A O   1 
ATOM   1813 C CB  . PHE B 1 139 ? 22.06200  50.13200 15.99700  1.000 50.04000  ? 121 PHE A CB  1 
ATOM   1814 C CG  . PHE B 1 139 ? 21.04600  51.25000 16.05800  1.000 41.23000  ? 121 PHE A CG  1 
ATOM   1815 C CD1 . PHE B 1 139 ? 20.79200  52.07400 14.97300  1.000 53.02000  ? 121 PHE A CD1 1 
ATOM   1816 C CD2 . PHE B 1 139 ? 20.34200  51.47100 17.23200  1.000 76.47000  ? 121 PHE A CD2 1 
ATOM   1817 C CE1 . PHE B 1 139 ? 19.85400  53.08700 15.05600  1.000 62.18000  ? 121 PHE A CE1 1 
ATOM   1818 C CE2 . PHE B 1 139 ? 19.40700  52.48300 17.32100  1.000 62.98000  ? 121 PHE A CE2 1 
ATOM   1819 C CZ  . PHE B 1 139 ? 19.16300  53.29200 16.23300  1.000 51.00000  ? 121 PHE A CZ  1 
ATOM   1820 N N   . PHE B 1 140 ? 25.20200  49.35900 14.88900  1.000 41.56000  ? 122 PHE A N   1 
ATOM   1821 C CA  . PHE B 1 140 ? 26.30000  48.36800 15.01300  1.000 48.08000  ? 122 PHE A CA  1 
ATOM   1822 C C   . PHE B 1 140 ? 27.54800  48.99400 15.64000  1.000 49.54000  ? 122 PHE A C   1 
ATOM   1823 O O   . PHE B 1 140 ? 27.88200  50.13600 15.32800  1.000 49.82000  ? 122 PHE A O   1 
ATOM   1824 C CB  . PHE B 1 140 ? 26.62100  47.71400 13.66700  1.000 52.34000  ? 122 PHE A CB  1 
ATOM   1825 C CG  . PHE B 1 140 ? 27.03100  48.60800 12.52800  1.000 39.97000  ? 122 PHE A CG  1 
ATOM   1826 C CD1 . PHE B 1 140 ? 26.08300  49.18300 11.70200  1.000 50.51000  ? 122 PHE A CD1 1 
ATOM   1827 C CD2 . PHE B 1 140 ? 28.36800  48.81100 12.23900  1.000 47.60000  ? 122 PHE A CD2 1 
ATOM   1828 C CE1 . PHE B 1 140 ? 26.46500  49.97900 10.63500  1.000 61.73000  ? 122 PHE A CE1 1 
ATOM   1829 C CE2 . PHE B 1 140 ? 28.74900  49.60700 11.17200  1.000 51.87000  ? 122 PHE A CE2 1 
ATOM   1830 C CZ  . PHE B 1 140 ? 27.79700  50.18600 10.37100  1.000 53.29000  ? 122 PHE A CZ  1 
ATOM   1831 N N   . ARG B 1 141 ? 28.24000  48.22000 16.47900  1.000 55.73000  ? 123 ARG A N   1 
ATOM   1832 C CA  . ARG B 1 141 ? 29.45800  48.71400 17.17500  1.000 71.07000  ? 123 ARG A CA  1 
ATOM   1833 C C   . ARG B 1 141 ? 30.62100  48.80000 16.18500  1.000 67.16000  ? 123 ARG A C   1 
ATOM   1834 O O   . ARG B 1 141 ? 30.61400  48.04100 15.20300  1.000 75.50000  ? 123 ARG A O   1 
ATOM   1835 C CB  . ARG B 1 141 ? 29.80300  47.77600 18.33500  1.000 68.54000  ? 123 ARG A CB  1 
ATOM   1836 C CG  . ARG B 1 141 ? 30.80100  48.33400 19.33800  1.000 79.61000  ? 123 ARG A CG  1 
ATOM   1837 C CD  . ARG B 1 141 ? 31.36100  47.20100 20.17400  1.000 83.79000  ? 123 ARG A CD  1 
ATOM   1838 N NE  . ARG B 1 141 ? 32.30100  47.64100 21.19300  1.000 86.26000  ? 123 ARG A NE  1 
ATOM   1839 C CZ  . ARG B 1 141 ? 32.16200  47.39500 22.49000  1.000 89.74000  ? 123 ARG A CZ  1 
ATOM   1840 N NH1 . ARG B 1 141 ? 31.11700  46.71700 22.92500  1.000 85.46000  ? 123 ARG A NH1 1 
ATOM   1841 N NH2 . ARG B 1 141 ? 33.07100  47.82700 23.34700  1.000 95.28000  ? 123 ARG A NH2 1 
ATOM   1842 N N   . VAL B 1 142 ? 31.57500  49.69500 16.44300  1.000 64.32000  ? 124 VAL A N   1 
ATOM   1843 C CA  . VAL B 1 142 ? 32.73700  49.88000 15.52900  1.000 78.41000  ? 124 VAL A CA  1 
ATOM   1844 C C   . VAL B 1 142 ? 33.95100  49.16000 16.12300  1.000 87.34000  ? 124 VAL A C   1 
ATOM   1845 O O   . VAL B 1 142 ? 33.83800  48.71500 17.28000  1.000 89.74000  ? 124 VAL A O   1 
ATOM   1846 C CB  . VAL B 1 142 ? 33.03200  51.37300 15.30800  1.000 85.49000  ? 124 VAL A CB  1 
ATOM   1847 C CG1 . VAL B 1 142 ? 33.31000  52.08700 16.62100  1.000 80.03000  ? 124 VAL A CG1 1 
ATOM   1848 C CG2 . VAL B 1 142 ? 34.17900  51.58000 14.33200  1.000 86.25000  ? 124 VAL A CG2 1 
ATOM   1849 N N   . MET C 1 19  ? 12.01100  23.62900 30.17000  1.000 68.98000  ? 1   MET B N   1 
ATOM   1850 C CA  . MET C 1 19  ? 10.89000  24.49400 30.62700  1.000 87.79000  ? 1   MET B CA  1 
ATOM   1851 C C   . MET C 1 19  ? 10.04200  23.67600 31.59500  1.000 86.48000  ? 1   MET B C   1 
ATOM   1852 O O   . MET C 1 19  ? 9.31800   22.78100 31.12700  1.000 78.52000  ? 1   MET B O   1 
ATOM   1853 C CB  . MET C 1 19  ? 10.01900  24.97800 29.46600  1.000 70.37000  ? 1   MET B CB  1 
ATOM   1854 C CG  . MET C 1 19  ? 9.09500   26.11000 29.86600  1.000 90.50000  ? 1   MET B CG  1 
ATOM   1855 S SD  . MET C 1 19  ? 8.18000   26.81500 28.48100  1.000 94.41000  ? 1   MET B SD  1 
ATOM   1856 N N   . LYS C 1 20  ? 10.12800  23.97100 32.88800  1.000 69.23000  ? 2   LYS B N   1 
ATOM   1857 C CA  . LYS C 1 20  ? 9.43800   23.07800 33.85500  1.000 62.67000  ? 2   LYS B CA  1 
ATOM   1858 C C   . LYS C 1 20  ? 8.42900   23.86700 34.68900  1.000 69.38000  ? 2   LYS B C   1 
ATOM   1859 O O   . LYS C 1 20  ? 8.58600   25.09300 34.81000  1.000 64.86000  ? 2   LYS B O   1 
ATOM   1860 C CB  . LYS C 1 20  ? 10.46000  22.37700 34.75300  1.000 60.11000  ? 2   LYS B CB  1 
ATOM   1861 C CG  . LYS C 1 20  ? 11.21500  21.22100 34.11100  1.000 63.87000  ? 2   LYS B CG  1 
ATOM   1862 C CD  . LYS C 1 20  ? 12.26200  20.62600 35.02800  1.000 70.28000  ? 2   LYS B CD  1 
ATOM   1863 C CE  . LYS C 1 20  ? 12.94800  19.40800 34.44800  1.000 57.74000  ? 2   LYS B CE  1 
ATOM   1864 N NZ  . LYS C 1 20  ? 12.02500  18.25400 34.35100  1.000 88.56000  ? 2   LYS B NZ  1 
ATOM   1865 N N   . LEU C 1 21  ? 7.43600   23.16900 35.23900  1.000 61.07000  ? 3   LEU B N   1 
ATOM   1866 C CA  . LEU C 1 21  ? 6.38700   23.82800 36.05500  1.000 53.68000  ? 3   LEU B CA  1 
ATOM   1867 C C   . LEU C 1 21  ? 6.43700   23.28600 37.48100  1.000 53.71000  ? 3   LEU B C   1 
ATOM   1868 O O   . LEU C 1 21  ? 6.88000   22.14000 37.66000  1.000 54.07000  ? 3   LEU B O   1 
ATOM   1869 C CB  . LEU C 1 21  ? 5.02000   23.52900 35.43500  1.000 56.69000  ? 3   LEU B CB  1 
ATOM   1870 C CG  . LEU C 1 21  ? 4.62500   24.37800 34.23000  1.000 66.68000  ? 3   LEU B CG  1 
ATOM   1871 C CD1 . LEU C 1 21  ? 3.21800   24.02800 33.77200  1.000 77.87000  ? 3   LEU B CD1 1 
ATOM   1872 C CD2 . LEU C 1 21  ? 4.71400   25.85600 34.56600  1.000 67.21000  ? 3   LEU B CD2 1 
ATOM   1873 N N   . VAL C 1 22  ? 6.00200   24.08600 38.44800  1.000 46.16000  ? 4   VAL B N   1 
ATOM   1874 C CA  . VAL C 1 22  ? 5.91400   23.63600 39.83200  1.000 67.45000  ? 4   VAL B CA  1 
ATOM   1875 C C   . VAL C 1 22  ? 4.46700   23.27200 40.12500  1.000 55.99000  ? 4   VAL B C   1 
ATOM   1876 O O   . VAL C 1 22  ? 3.55700   24.08400 39.91200  1.000 52.14000  ? 4   VAL B O   1 
ATOM   1877 C CB  . VAL C 1 22  ? 6.41800   24.71000 40.81200  1.000 74.77000  ? 4   VAL B CB  1 
ATOM   1878 C CG1 . VAL C 1 22  ? 6.25900   24.21900 42.24500  1.000 62.41000  ? 4   VAL B CG1 1 
ATOM   1879 C CG2 . VAL C 1 22  ? 7.86600   25.05700 40.52300  1.000 70.10000  ? 4   VAL B CG2 1 
ATOM   1880 N N   . ILE C 1 23  ? 4.25200   22.05200 40.60700  1.000 54.93000  ? 5   ILE B N   1 
ATOM   1881 C CA  . ILE C 1 23  ? 2.93200   21.57000 40.99300  1.000 61.86000  ? 5   ILE B CA  1 
ATOM   1882 C C   . ILE C 1 23  ? 2.93300   21.37200 42.50100  1.000 60.12000  ? 5   ILE B C   1 
ATOM   1883 O O   . ILE C 1 23  ? 3.68100   20.53700 43.02500  1.000 57.65000  ? 5   ILE B O   1 
ATOM   1884 C CB  . ILE C 1 23  ? 2.56700   20.26800 40.26500  1.000 61.24000  ? 5   ILE B CB  1 
ATOM   1885 C CG1 . ILE C 1 23  ? 2.56200   20.48800 38.75100  1.000 54.17000  ? 5   ILE B CG1 1 
ATOM   1886 C CG2 . ILE C 1 23  ? 1.21800   19.75400 40.74100  1.000 58.07000  ? 5   ILE B CG2 1 
ATOM   1887 C CD1 . ILE C 1 23  ? 2.23500   19.24400 37.96100  1.000 61.43000  ? 5   ILE B CD1 1 
ATOM   1888 N N   . ALA C 1 24  ? 2.09900   22.13800 43.19700  1.000 64.97000  ? 6   ALA B N   1 
ATOM   1889 C CA  . ALA C 1 24  ? 2.00200   22.08800 44.65200  1.000 64.80000  ? 6   ALA B CA  1 
ATOM   1890 C C   . ALA C 1 24  ? 0.65600   21.47800 45.02600  1.000 60.65000  ? 6   ALA B C   1 
ATOM   1891 O O   . ALA C 1 24  ? -0.39300  22.09100 44.80400  1.000 50.85000  ? 6   ALA B O   1 
ATOM   1892 C CB  . ALA C 1 24  ? 2.16500   23.48000 45.25900  1.000 64.02000  ? 6   ALA B CB  1 
ATOM   1893 N N   . ARG C 1 25  ? 0.69200   20.24800 45.55200  1.000 65.55000  ? 7   ARG B N   1 
ATOM   1894 C CA  . ARG C 1 25  ? -0.53500  19.54600 46.02200  1.000 74.58000  ? 7   ARG B CA  1 
ATOM   1895 C C   . ARG C 1 25  ? -0.70600  19.77500 47.52600  1.000 68.79000  ? 7   ARG B C   1 
ATOM   1896 O O   . ARG C 1 25  ? -0.11000  19.03800 48.31100  1.000 62.97000  ? 7   ARG B O   1 
ATOM   1897 C CB  . ARG C 1 25  ? -0.48800  18.05100 45.69000  1.000 63.99000  ? 7   ARG B CB  1 
ATOM   1898 C CG  . ARG C 1 25  ? -1.66500  17.24500 46.21700  1.000 60.25000  ? 7   ARG B CG  1 
ATOM   1899 C CD  . ARG C 1 25  ? -1.47600  15.76900 45.93600  1.000 65.77000  ? 7   ARG B CD  1 
ATOM   1900 N NE  . ARG C 1 25  ? -2.66400  14.98600 46.23200  1.000 76.64000  ? 7   ARG B NE  1 
ATOM   1901 C CZ  . ARG C 1 25  ? -2.77800  13.67900 46.03600  1.000 74.40000  ? 7   ARG B CZ  1 
ATOM   1902 N NH1 . ARG C 1 25  ? -1.79200  13.00400 45.47600  1.000 73.65000  ? 7   ARG B NH1 1 
ATOM   1903 N NH2 . ARG C 1 25  ? -3.88100  13.04800 46.39900  1.000 71.12000  ? 7   ARG B NH2 1 
ATOM   1904 N N   . VAL C 1 26  ? -1.50400  20.76600 47.88700  1.000 64.71000  ? 8   VAL B N   1 
ATOM   1905 C CA  . VAL C 1 26  ? -1.76000  21.08500 49.28800  1.000 78.58000  ? 8   VAL B CA  1 
ATOM   1906 C C   . VAL C 1 26  ? -2.84200  20.13700 49.79400  1.000 80.60000  ? 8   VAL B C   1 
ATOM   1907 O O   . VAL C 1 26  ? -3.99800  20.21700 49.37200  1.000 74.41000  ? 8   VAL B O   1 
ATOM   1908 C CB  . VAL C 1 26  ? -2.17300  22.55000 49.46500  1.000 74.95000  ? 8   VAL B CB  1 
ATOM   1909 C CG1 . VAL C 1 26  ? -2.43400  22.85300 50.93100  1.000 84.38000  ? 8   VAL B CG1 1 
ATOM   1910 C CG2 . VAL C 1 26  ? -1.09700  23.47300 48.91000  1.000 79.38000  ? 8   VAL B CG2 1 
ATOM   1911 N N   . LYS C 1 27  ? -2.46700  19.23600 50.70400  1.000 78.70000  ? 9   LYS B N   1 
ATOM   1912 C CA  . LYS C 1 27  ? -3.38000  18.22300 51.23200  1.000 81.14000  ? 9   LYS B CA  1 
ATOM   1913 C C   . LYS C 1 27  ? -4.34900  18.84300 52.24300  1.000 87.36000  ? 9   LYS B C   1 
ATOM   1914 O O   . LYS C 1 27  ? -4.40700  18.46500 53.41300  1.000 93.60000  ? 9   LYS B O   1 
ATOM   1915 C CB  . LYS C 1 27  ? -2.58800  17.08200 51.85900  1.000 76.71000  ? 9   LYS B CB  1 
ATOM   1916 C CG  . LYS C 1 27  ? -1.45900  16.54000 50.99300  1.000 85.89000  ? 9   LYS B CG  1 
ATOM   1917 C CD  . LYS C 1 27  ? -1.80000  15.17700 50.41500  1.000 78.44000  ? 9   LYS B CD  1 
ATOM   1918 C CE  . LYS C 1 27  ? -0.62200  14.58500 49.65600  1.000 78.38000  ? 9   LYS B CE  1 
ATOM   1919 N NZ  . LYS C 1 27  ? -0.91600  13.21400 49.15600  1.000 87.28000  ? 9   LYS B NZ  1 
ATOM   1920 N N   . SER C 1 28  ? -5.11000  19.84500 51.79400  1.000 82.82000  ? 10  SER B N   1 
ATOM   1921 C CA  . SER C 1 28  ? -6.04500  20.54300 52.71700  1.000 87.15000  ? 10  SER B CA  1 
ATOM   1922 C C   . SER C 1 28  ? -7.18200  21.20500 51.93600  1.000 91.93000  ? 10  SER B C   1 
ATOM   1923 O O   . SER C 1 28  ? -6.90800  21.80700 50.88300  1.000 94.84000  ? 10  SER B O   1 
ATOM   1924 C CB  . SER C 1 28  ? -5.32600  21.56000 53.55800  1.000 94.34000  ? 10  SER B CB  1 
ATOM   1925 O OG  . SER C 1 28  ? -6.25000  22.41300 54.21700  1.000 98.16000  ? 10  SER B OG  1 
ATOM   1926 N N   . PRO C 1 29  ? -8.43800  21.13600 52.42300  1.000 96.15000  ? 11  PRO B N   1 
ATOM   1927 C CA  . PRO C 1 29  ? -9.56500  21.76800 51.74400  1.000 99.36000  ? 11  PRO B CA  1 
ATOM   1928 C C   . PRO C 1 29  ? -9.67400  23.25700 52.08600  1.000 100.75000 ? 11  PRO B C   1 
ATOM   1929 O O   . PRO C 1 29  ? -10.51400 23.91900 51.50700  1.000 94.96000  ? 11  PRO B O   1 
ATOM   1930 C CB  . PRO C 1 29  ? -10.76600 21.02500 52.33700  1.000 90.06000  ? 11  PRO B CB  1 
ATOM   1931 C CG  . PRO C 1 29  ? -10.32700 20.70000 53.74500  1.000 92.41000  ? 11  PRO B CG  1 
ATOM   1932 C CD  . PRO C 1 29  ? -8.84300  20.41600 53.63300  1.000 91.14000  ? 11  PRO B CD  1 
ATOM   1933 N N   . LYS C 1 30  ? -8.83000  23.74400 52.99800  1.000 105.16000 ? 12  LYS B N   1 
ATOM   1934 C CA  . LYS C 1 30  ? -8.94700  25.15700 53.44600  1.000 108.14000 ? 12  LYS B CA  1 
ATOM   1935 C C   . LYS C 1 30  ? -7.85200  26.01000 52.80100  1.000 113.94000 ? 12  LYS B C   1 
ATOM   1936 O O   . LYS C 1 30  ? -8.20000  27.01700 52.15800  1.000 116.85000 ? 12  LYS B O   1 
ATOM   1937 C CB  . LYS C 1 30  ? -8.85900  25.22900 54.97400  1.000 105.66000 ? 12  LYS B CB  1 
ATOM   1938 N N   . VAL C 1 31  ? -6.58600  25.61600 52.95900  1.000 112.85000 ? 13  VAL B N   1 
ATOM   1939 C CA  . VAL C 1 31  ? -5.46000  26.44400 52.43300  1.000 110.61000 ? 13  VAL B CA  1 
ATOM   1940 C C   . VAL C 1 31  ? -5.82400  26.90900 51.02100  1.000 108.68000 ? 13  VAL B C   1 
ATOM   1941 O O   . VAL C 1 31  ? -6.06300  26.04100 50.16300  1.000 108.01000 ? 13  VAL B O   1 
ATOM   1942 C CB  . VAL C 1 31  ? -4.13300  25.66600 52.45000  1.000 105.78000 ? 13  VAL B CB  1 
ATOM   1943 N N   . LYS C 1 32  ? -5.84400  28.22200 50.77900  1.000 106.65000 ? 14  LYS B N   1 
ATOM   1944 C CA  . LYS C 1 32  ? -6.30300  28.73200 49.45900  1.000 106.07000 ? 14  LYS B CA  1 
ATOM   1945 C C   . LYS C 1 32  ? -5.25600  29.66100 48.83600  1.000 107.20000 ? 14  LYS B C   1 
ATOM   1946 O O   . LYS C 1 32  ? -5.55200  30.25300 47.78400  1.000 103.15000 ? 14  LYS B O   1 
ATOM   1947 C CB  . LYS C 1 32  ? -7.64300  29.45400 49.62000  1.000 106.91000 ? 14  LYS B CB  1 
ATOM   1948 N N   . ARG C 1 33  ? -4.08300  29.78300 49.45400  1.000 98.34000  ? 15  ARG B N   1 
ATOM   1949 C CA  . ARG C 1 33  ? -3.00800  30.59700 48.83700  1.000 95.89000  ? 15  ARG B CA  1 
ATOM   1950 C C   . ARG C 1 33  ? -1.67200  30.17000 49.43500  1.000 98.49000  ? 15  ARG B C   1 
ATOM   1951 O O   . ARG C 1 33  ? -1.67200  29.61200 50.54500  1.000 96.12000  ? 15  ARG B O   1 
ATOM   1952 C CB  . ARG C 1 33  ? -3.24900  32.08900 49.07000  1.000 101.51000 ? 15  ARG B CB  1 
ATOM   1953 N N   . LEU C 1 34  ? -0.58300  30.43100 48.71700  1.000 102.88000 ? 16  LEU B N   1 
ATOM   1954 C CA  . LEU C 1 34  ? 0.76100   30.03000 49.20100  1.000 109.19000 ? 16  LEU B CA  1 
ATOM   1955 C C   . LEU C 1 34  ? 1.58600   31.29400 49.47600  1.000 112.06000 ? 16  LEU B C   1 
ATOM   1956 O O   . LEU C 1 34  ? 1.42600   32.27800 48.73000  1.000 104.15000 ? 16  LEU B O   1 
ATOM   1957 C CB  . LEU C 1 34  ? 1.40000   29.14500 48.12900  1.000 102.28000 ? 16  LEU B CB  1 
ATOM   1958 C CG  . LEU C 1 34  ? 0.70900   27.80800 47.87000  1.000 83.40000  ? 16  LEU B CG  1 
ATOM   1959 C CD1 . LEU C 1 34  ? 1.34000   27.08600 46.69300  1.000 90.09000  ? 16  LEU B CD1 1 
ATOM   1960 C CD2 . LEU C 1 34  ? 0.75400   26.93600 49.11300  1.000 93.52000  ? 16  LEU B CD2 1 
ATOM   1961 N N   . SER C 1 35  ? 2.41300   31.26800 50.52200  1.000 110.06000 ? 17  SER B N   1 
ATOM   1962 C CA  . SER C 1 35  ? 3.08400   32.49300 51.02600  1.000 111.35000 ? 17  SER B CA  1 
ATOM   1963 C C   . SER C 1 35  ? 4.48900   32.61500 50.43400  1.000 114.06000 ? 17  SER B C   1 
ATOM   1964 O O   . SER C 1 35  ? 5.09000   31.58300 50.13100  1.000 109.97000 ? 17  SER B O   1 
ATOM   1965 C CB  . SER C 1 35  ? 3.15000   32.47700 52.51600  1.000 112.82000 ? 17  SER B CB  1 
ATOM   1966 O OG  . SER C 1 35  ? 4.33400   31.82900 52.95400  1.000 122.28000 ? 17  SER B OG  1 
ATOM   1967 N N   . GLU C 1 36  ? 4.98000   33.84500 50.28100  1.000 118.01000 ? 18  GLU B N   1 
ATOM   1968 C CA  . GLU C 1 36  ? 6.32300   34.05900 49.69200  1.000 116.35000 ? 18  GLU B CA  1 
ATOM   1969 C C   . GLU C 1 36  ? 7.30400   33.11900 50.38300  1.000 105.28000 ? 18  GLU B C   1 
ATOM   1970 O O   . GLU C 1 36  ? 8.15400   32.53300 49.70500  1.000 90.49000  ? 18  GLU B O   1 
ATOM   1971 C CB  . GLU C 1 36  ? 6.74800   35.51200 49.90400  1.000 122.51000 ? 18  GLU B CB  1 
ATOM   1972 N N   . GLU C 1 37  ? 7.16900   32.99700 51.69500  1.000 109.11000 ? 19  GLU B N   1 
ATOM   1973 C CA  . GLU C 1 37  ? 8.07000   32.10400 52.45500  1.000 114.92000 ? 19  GLU B CA  1 
ATOM   1974 C C   . GLU C 1 37  ? 7.81100   30.68900 51.95000  1.000 112.81000 ? 19  GLU B C   1 
ATOM   1975 O O   . GLU C 1 37  ? 8.78300   29.94500 51.74400  1.000 103.80000 ? 19  GLU B O   1 
ATOM   1976 C CB  . GLU C 1 37  ? 7.78900   32.24800 53.95300  1.000 108.79000 ? 19  GLU B CB  1 
ATOM   1977 C CG  . GLU C 1 37  ? 8.60200   31.31200 54.82400  1.000 110.01000 ? 19  GLU B CG  1 
ATOM   1978 C CD  . GLU C 1 37  ? 8.31600   31.45900 56.30700  1.000 115.50000 ? 19  GLU B CD  1 
ATOM   1979 O OE1 . GLU C 1 37  ? 7.46100   32.29200 56.66100  1.000 114.52000 ? 19  GLU B OE1 1 
ATOM   1980 O OE2 . GLU C 1 37  ? 8.95100   30.74400 57.10300  1.000 119.56000 ? 19  GLU B OE2 1 
ATOM   1981 N N   . ASP C 1 38  ? 6.53900   30.36500 51.73300  1.000 115.99000 ? 20  ASP B N   1 
ATOM   1982 C CA  . ASP C 1 38  ? 6.15900   28.99700 51.29900  1.000 116.93000 ? 20  ASP B CA  1 
ATOM   1983 C C   . ASP C 1 38  ? 6.66400   28.75100 49.87600  1.000 106.77000 ? 20  ASP B C   1 
ATOM   1984 O O   . ASP C 1 38  ? 7.29200   27.71000 49.64500  1.000 100.72000 ? 20  ASP B O   1 
ATOM   1985 C CB  . ASP C 1 38  ? 4.64700   28.80700 51.44900  1.000 116.22000 ? 20  ASP B CB  1 
ATOM   1986 N N   . ILE C 1 39  ? 6.42500   29.69600 48.97500  1.000 105.32000 ? 21  ILE B N   1 
ATOM   1987 C CA  . ILE C 1 39  ? 6.91900   29.55400 47.57900  1.000 104.14000 ? 21  ILE B CA  1 
ATOM   1988 C C   . ILE C 1 39  ? 8.43800   29.39300 47.64500  1.000 109.84000 ? 21  ILE B C   1 
ATOM   1989 O O   . ILE C 1 39  ? 8.98100   28.56600 46.88700  1.000 101.54000 ? 21  ILE B O   1 
ATOM   1990 C CB  . ILE C 1 39  ? 6.47800   30.75900 46.73200  1.000 91.32000  ? 21  ILE B CB  1 
ATOM   1991 C CG1 . ILE C 1 39  ? 4.95300   30.89000 46.71200  1.000 94.00000  ? 21  ILE B CG1 1 
ATOM   1992 C CG2 . ILE C 1 39  ? 7.05700   30.67700 45.33100  1.000 93.09000  ? 21  ILE B CG2 1 
ATOM   1993 C CD1 . ILE C 1 39  ? 4.43100   31.90700 45.72800  1.000 72.22000  ? 21  ILE B CD1 1 
ATOM   1994 N N   . GLU C 1 40  ? 9.08500   30.13300 48.55200  1.000 106.64000 ? 22  GLU B N   1 
ATOM   1995 C CA  . GLU C 1 40  ? 10.56200  30.06900 48.66900  1.000 101.88000 ? 22  GLU B CA  1 
ATOM   1996 C C   . GLU C 1 40  ? 10.94300  28.67500 49.16500  1.000 101.90000 ? 22  GLU B C   1 
ATOM   1997 O O   . GLU C 1 40  ? 11.83200  28.04400 48.57800  1.000 99.41000  ? 22  GLU B O   1 
ATOM   1998 C CB  . GLU C 1 40  ? 11.06200  31.16100 49.61300  1.000 95.50000  ? 22  GLU B CB  1 
ATOM   1999 C CG  . GLU C 1 40  ? 12.22200  31.96300 49.05500  1.000 96.80000  ? 22  GLU B CG  1 
ATOM   2000 C CD  . GLU C 1 40  ? 11.88800  32.81500 47.84300  1.000 111.18000 ? 22  GLU B CD  1 
ATOM   2001 O OE1 . GLU C 1 40  ? 10.98500  33.66300 47.95100  1.000 110.14000 ? 22  GLU B OE1 1 
ATOM   2002 O OE2 . GLU C 1 40  ? 12.54300  32.63900 46.79800  1.000 108.46000 ? 22  GLU B OE2 1 
ATOM   2003 N N   . LYS C 1 41  ? 10.26700  28.21300 50.20400  1.000 103.83000 ? 23  LYS B N   1 
ATOM   2004 C CA  . LYS C 1 41  ? 10.55400  26.86200 50.73100  1.000 102.79000 ? 23  LYS B CA  1 
ATOM   2005 C C   . LYS C 1 41  ? 10.43300  25.88100 49.57400  1.000 95.16000  ? 23  LYS B C   1 
ATOM   2006 O O   . LYS C 1 41  ? 11.32500  25.04300 49.42500  1.000 82.71000  ? 23  LYS B O   1 
ATOM   2007 C CB  . LYS C 1 41  ? 9.55300   26.52600 51.83800  1.000 87.80000  ? 23  LYS B CB  1 
ATOM   2008 C CG  . LYS C 1 41  ? 9.47000   25.05700 52.23200  1.000 91.07000  ? 23  LYS B CG  1 
ATOM   2009 C CD  . LYS C 1 41  ? 10.76200  24.48900 52.77600  1.000 101.11000 ? 23  LYS B CD  1 
ATOM   2010 N N   . ILE C 1 42  ? 9.37100   26.01500 48.78300  1.000 94.51000  ? 24  ILE B N   1 
ATOM   2011 C CA  . ILE C 1 42  ? 9.12700   25.03700 47.68500  1.000 101.62000 ? 24  ILE B CA  1 
ATOM   2012 C C   . ILE C 1 42  ? 10.27000  25.14600 46.67300  1.000 104.71000 ? 24  ILE B C   1 
ATOM   2013 O O   . ILE C 1 42  ? 10.90700  24.11800 46.37800  1.000 90.01000  ? 24  ILE B O   1 
ATOM   2014 C CB  . ILE C 1 42  ? 7.74500   25.28200 47.04800  1.000 102.56000 ? 24  ILE B CB  1 
ATOM   2015 C CG1 . ILE C 1 42  ? 6.61200   25.05500 48.05100  1.000 97.51000  ? 24  ILE B CG1 1 
ATOM   2016 C CG2 . ILE C 1 42  ? 7.56600   24.43500 45.80000  1.000 92.34000  ? 24  ILE B CG2 1 
ATOM   2017 C CD1 . ILE C 1 42  ? 5.25600   25.47500 47.54700  1.000 82.43000  ? 24  ILE B CD1 1 
ATOM   2018 N N   . LYS C 1 43  ? 10.53500  26.36200 46.20000  1.000 101.62000 ? 25  LYS B N   1 
ATOM   2019 C CA  . LYS C 1 43  ? 11.64300  26.56800 45.24300  1.000 92.57000  ? 25  LYS B CA  1 
ATOM   2020 C C   . LYS C 1 43  ? 12.88400  25.89100 45.81500  1.000 97.80000  ? 25  LYS B C   1 
ATOM   2021 O O   . LYS C 1 43  ? 13.49300  25.06700 45.12100  1.000 98.45000  ? 25  LYS B O   1 
ATOM   2022 C CB  . LYS C 1 43  ? 11.87200  28.06400 45.05300  1.000 101.75000 ? 25  LYS B CB  1 
ATOM   2023 N N   . SER C 1 44  ? 13.21000  26.21400 47.06000  1.000 102.88000 ? 26  SER B N   1 
ATOM   2024 C CA  . SER C 1 44  ? 14.42700  25.64700 47.68000  1.000 112.46000 ? 26  SER B CA  1 
ATOM   2025 C C   . SER C 1 44  ? 14.34300  24.12500 47.72400  1.000 97.73000  ? 26  SER B C   1 
ATOM   2026 O O   . SER C 1 44  ? 15.34500  23.46600 47.42000  1.000 93.35000  ? 26  SER B O   1 
ATOM   2027 C CB  . SER C 1 44  ? 14.59700  26.20800 49.06400  1.000 115.70000 ? 26  SER B CB  1 
ATOM   2028 O OG  . SER C 1 44  ? 14.41700  27.61500 49.05800  1.000 120.62000 ? 26  SER B OG  1 
ATOM   2029 N N   . ALA C 1 45  ? 13.18200  23.59900 48.08000  1.000 91.68000  ? 27  ALA B N   1 
ATOM   2030 C CA  . ALA C 1 45  ? 13.05800  22.14100 48.26200  1.000 87.00000  ? 27  ALA B CA  1 
ATOM   2031 C C   . ALA C 1 45  ? 13.27600  21.41000 46.94200  1.000 91.41000  ? 27  ALA B C   1 
ATOM   2032 O O   . ALA C 1 45  ? 13.51200  20.19900 46.99400  1.000 96.65000  ? 27  ALA B O   1 
ATOM   2033 C CB  . ALA C 1 45  ? 11.70100  21.85400 48.81900  1.000 83.50000  ? 27  ALA B CB  1 
ATOM   2034 N N   . LEU C 1 46  ? 13.18500  22.11000 45.81200  1.000 94.71000  ? 28  LEU B N   1 
ATOM   2035 C CA  . LEU C 1 46  ? 13.27100  21.40400 44.50700  1.000 102.50000 ? 28  LEU B CA  1 
ATOM   2036 C C   . LEU C 1 46  ? 14.51900  21.83600 43.73700  1.000 106.60000 ? 28  LEU B C   1 
ATOM   2037 O O   . LEU C 1 46  ? 14.63800  21.45500 42.56800  1.000 105.77000 ? 28  LEU B O   1 
ATOM   2038 C CB  . LEU C 1 46  ? 12.01900  21.72600 43.68700  1.000 104.39000 ? 28  LEU B CB  1 
ATOM   2039 C CG  . LEU C 1 46  ? 10.69600  21.19800 44.23700  1.000 96.03000  ? 28  LEU B CG  1 
ATOM   2040 C CD1 . LEU C 1 46  ? 9.52700   21.83500 43.50500  1.000 77.75000  ? 28  LEU B CD1 1 
ATOM   2041 C CD2 . LEU C 1 46  ? 10.63100  19.68500 44.11500  1.000 73.69000  ? 28  LEU B CD2 1 
ATOM   2042 N N   . LYS C 1 47  ? 15.39900  22.62000 44.36300  1.000 110.78000 ? 29  LYS B N   1 
ATOM   2043 C CA  . LYS C 1 47  ? 16.65100  23.06700 43.69300  1.000 97.77000  ? 29  LYS B CA  1 
ATOM   2044 C C   . LYS C 1 47  ? 17.56800  21.85500 43.50200  1.000 99.76000  ? 29  LYS B C   1 
ATOM   2045 O O   . LYS C 1 47  ? 18.42000  21.89300 42.60400  1.000 94.96000  ? 29  LYS B O   1 
ATOM   2046 C CB  . LYS C 1 47  ? 17.32000  24.19100 44.48600  1.000 99.13000  ? 29  LYS B CB  1 
ATOM   2047 N N   . SER C 1 48  ? 17.35600  20.80300 44.28600  1.000 90.06000  ? 30  SER B N   1 
ATOM   2048 C CA  . SER C 1 48  ? 18.20900  19.59700 44.18000  1.000 92.94000  ? 30  SER B CA  1 
ATOM   2049 C C   . SER C 1 48  ? 17.39000  18.40800 43.67700  1.000 102.34000 ? 30  SER B C   1 
ATOM   2050 O O   . SER C 1 48  ? 17.98900  17.51200 43.05600  1.000 97.01000  ? 30  SER B O   1 
ATOM   2051 C CB  . SER C 1 48  ? 18.84300  19.30000 45.50300  1.000 94.88000  ? 30  SER B CB  1 
ATOM   2052 O OG  . SER C 1 48  ? 19.66500  20.37700 45.92400  1.000 92.92000  ? 30  SER B OG  1 
ATOM   2053 N N   . THR C 1 49  ? 16.07500  18.41200 43.92400  1.000 107.24000 ? 31  THR B N   1 
ATOM   2054 C CA  . THR C 1 49  ? 15.21200  17.26400 43.53000  1.000 100.57000 ? 31  THR B CA  1 
ATOM   2055 C C   . THR C 1 49  ? 14.04500  17.74500 42.67100  1.000 97.14000  ? 31  THR B C   1 
ATOM   2056 O O   . THR C 1 49  ? 13.78300  18.94900 42.65900  1.000 90.51000  ? 31  THR B O   1 
ATOM   2057 C CB  . THR C 1 49  ? 14.64000  16.53200 44.74500  1.000 93.02000  ? 31  THR B CB  1 
ATOM   2058 O OG1 . THR C 1 49  ? 13.78700  15.49300 44.26800  1.000 95.92000  ? 31  THR B OG1 1 
ATOM   2059 C CG2 . THR C 1 49  ? 13.86500  17.44500 45.66700  1.000 90.74000  ? 31  THR B CG2 1 
ATOM   2060 N N   . ASN C 1 50  ? 13.38500  16.81700 41.97900  1.000 93.56000  ? 32  ASN B N   1 
ATOM   2061 C CA  . ASN C 1 50  ? 12.20400  17.18100 41.15500  1.000 97.27000  ? 32  ASN B CA  1 
ATOM   2062 C C   . ASN C 1 50  ? 10.96400  16.66300 41.87600  1.000 88.03000  ? 32  ASN B C   1 
ATOM   2063 O O   . ASN C 1 50  ? 9.90800   16.59000 41.23700  1.000 79.34000  ? 32  ASN B O   1 
ATOM   2064 C CB  . ASN C 1 50  ? 12.32800  16.64300 39.73200  1.000 92.04000  ? 32  ASN B CB  1 
ATOM   2065 C CG  . ASN C 1 50  ? 13.40600  17.32600 38.92200  1.000 81.90000  ? 32  ASN B CG  1 
ATOM   2066 O OD1 . ASN C 1 50  ? 13.46500  18.55000 38.86500  1.000 71.10000  ? 32  ASN B OD1 1 
ATOM   2067 N ND2 . ASN C 1 50  ? 14.26800  16.54000 38.30000  1.000 79.08000  ? 32  ASN B ND2 1 
ATOM   2068 N N   . LYS C 1 51  ? 11.09900  16.37100 43.16600  1.000 83.17000  ? 33  LYS B N   1 
ATOM   2069 C CA  . LYS C 1 51  ? 10.01000  15.78900 43.94700  1.000 78.47000  ? 33  LYS B CA  1 
ATOM   2070 C C   . LYS C 1 51  ? 10.34800  15.93900 45.42000  1.000 87.21000  ? 33  LYS B C   1 
ATOM   2071 O O   . LYS C 1 51  ? 11.35100  15.38400 45.88100  1.000 90.70000  ? 33  LYS B O   1 
ATOM   2072 C CB  . LYS C 1 51  ? 9.81200   14.31900 43.57700  1.000 71.86000  ? 33  LYS B CB  1 
ATOM   2073 C CG  . LYS C 1 51  ? 8.60000   13.65800 44.20400  1.000 75.21000  ? 33  LYS B CG  1 
ATOM   2074 C CD  . LYS C 1 51  ? 8.46200   12.22700 43.70700  1.000 77.98000  ? 33  LYS B CD  1 
ATOM   2075 C CE  . LYS C 1 51  ? 7.23600   11.54600 44.28900  1.000 85.68000  ? 33  LYS B CE  1 
ATOM   2076 N NZ  . LYS C 1 51  ? 7.29700   11.46400 45.77300  1.000 91.76000  ? 33  LYS B NZ  1 
ATOM   2077 N N   . ALA C 1 52  ? 9.51900   16.69800 46.14000  1.000 92.01000  ? 34  ALA B N   1 
ATOM   2078 C CA  . ALA C 1 52  ? 9.77600   16.97300 47.56500  1.000 78.71000  ? 34  ALA B CA  1 
ATOM   2079 C C   . ALA C 1 52  ? 8.46400   17.08000 48.33500  1.000 85.19000  ? 34  ALA B C   1 
ATOM   2080 O O   . ALA C 1 52  ? 7.41200   17.15000 47.69300  1.000 89.10000  ? 34  ALA B O   1 
ATOM   2081 C CB  . ALA C 1 52  ? 10.53300  18.26400 47.66900  1.000 75.72000  ? 34  ALA B CB  1 
ATOM   2082 N N   . VAL C 1 53  ? 8.53500   17.07000 49.66300  1.000 83.42000  ? 35  VAL B N   1 
ATOM   2083 C CA  . VAL C 1 53  ? 7.32500   17.28700 50.50500  1.000 85.99000  ? 35  VAL B CA  1 
ATOM   2084 C C   . VAL C 1 53  ? 7.66100   18.40500 51.49100  1.000 74.81000  ? 35  VAL B C   1 
ATOM   2085 O O   . VAL C 1 53  ? 8.68300   18.30900 52.17000  1.000 83.89000  ? 35  VAL B O   1 
ATOM   2086 C CB  . VAL C 1 53  ? 6.88400   16.01200 51.23500  1.000 76.68000  ? 35  VAL B CB  1 
ATOM   2087 C CG1 . VAL C 1 53  ? 5.60500   16.23800 52.02300  1.000 74.47000  ? 35  VAL B CG1 1 
ATOM   2088 C CG2 . VAL C 1 53  ? 6.73200   14.83100 50.29100  1.000 86.15000  ? 35  VAL B CG2 1 
ATOM   2089 N N   . VAL C 1 54  ? 6.84300   19.44200 51.53200  1.000 82.05000  ? 36  VAL B N   1 
ATOM   2090 C CA  . VAL C 1 54  ? 7.09100   20.58900 52.44400  1.000 98.87000  ? 36  VAL B CA  1 
ATOM   2091 C C   . VAL C 1 54  ? 5.90400   20.71100 53.39500  1.000 110.36000 ? 36  VAL B C   1 
ATOM   2092 O O   . VAL C 1 54  ? 4.96200   19.91900 53.24900  1.000 112.33000 ? 36  VAL B O   1 
ATOM   2093 C CB  . VAL C 1 54  ? 7.30200   21.89600 51.66700  1.000 95.63000  ? 36  VAL B CB  1 
ATOM   2094 C CG1 . VAL C 1 54  ? 8.41300   21.76900 50.63900  1.000 95.92000  ? 36  VAL B CG1 1 
ATOM   2095 C CG2 . VAL C 1 54  ? 6.01800   22.37800 51.01300  1.000 104.84000 ? 36  VAL B CG2 1 
ATOM   2096 N N   . THR C 1 55  ? 5.97100   21.65200 54.33800  1.000 106.64000 ? 37  THR B N   1 
ATOM   2097 C CA  . THR C 1 55  ? 4.88700   21.86100 55.29600  1.000 102.74000 ? 37  THR B CA  1 
ATOM   2098 C C   . THR C 1 55  ? 4.72800   23.35900 55.52400  1.000 106.34000 ? 37  THR B C   1 
ATOM   2099 O O   . THR C 1 55  ? 5.63900   24.00800 56.04600  1.000 106.02000 ? 37  THR B O   1 
ATOM   2100 C CB  . THR C 1 55  ? 5.15900   21.13900 56.61800  1.000 101.51000 ? 37  THR B CB  1 
ATOM   2101 O OG1 . THR C 1 55  ? 6.48600   21.44000 57.06800  1.000 102.26000 ? 37  THR B OG1 1 
ATOM   2102 C CG2 . THR C 1 55  ? 5.00800   19.63100 56.45300  1.000 103.72000 ? 37  THR B CG2 1 
ATOM   2103 N N   . ILE C 1 56  ? 3.60700   23.90600 55.05800  1.000 113.36000 ? 38  ILE B N   1 
ATOM   2104 C CA  . ILE C 1 56  ? 3.33500   25.35900 55.24100  1.000 118.19000 ? 38  ILE B CA  1 
ATOM   2105 C C   . ILE C 1 56  ? 2.26300   25.48500 56.32900  1.000 125.24000 ? 38  ILE B C   1 
ATOM   2106 O O   . ILE C 1 56  ? 1.76000   24.43900 56.78300  1.000 116.17000 ? 38  ILE B O   1 
ATOM   2107 C CB  . ILE C 1 56  ? 2.91300   26.00100 53.90500  1.000 105.49000 ? 38  ILE B CB  1 
ATOM   2108 C CG1 . ILE C 1 56  ? 2.88500   27.52900 53.98200  1.000 117.96000 ? 38  ILE B CG1 1 
ATOM   2109 C CG2 . ILE C 1 56  ? 1.58200   25.43800 53.43200  1.000 104.21000 ? 38  ILE B CG2 1 
ATOM   2110 C CD1 . ILE C 1 56  ? 4.24400   28.15700 54.18900  1.000 106.27000 ? 38  ILE B CD1 1 
ATOM   2111 N N   . LYS C 1 57  ? 1.94500   26.70500 56.76300  1.000 119.45000 ? 39  LYS B N   1 
ATOM   2112 C CA  . LYS C 1 57  ? 0.95900   26.88300 57.86100  1.000 121.67000 ? 39  LYS B CA  1 
ATOM   2113 C C   . LYS C 1 57  ? -0.01500  28.00500 57.48600  1.000 119.86000 ? 39  LYS B C   1 
ATOM   2114 O O   . LYS C 1 57  ? 0.45700   29.05700 57.01400  1.000 114.44000 ? 39  LYS B O   1 
ATOM   2115 C CB  . LYS C 1 57  ? 1.68100   27.17800 59.17900  1.000 117.71000 ? 39  LYS B CB  1 
ATOM   2116 N N   . ASP C 1 58  ? -1.31800  27.78500 57.69000  1.000 116.28000 ? 40  ASP B N   1 
ATOM   2117 C CA  . ASP C 1 58  ? -2.32500  28.80200 57.28800  1.000 118.43000 ? 40  ASP B CA  1 
ATOM   2118 C C   . ASP C 1 58  ? -3.48000  28.84600 58.29300  1.000 119.41000 ? 40  ASP B C   1 
ATOM   2119 O O   . ASP C 1 58  ? -3.93400  27.75800 58.69800  1.000 110.40000 ? 40  ASP B O   1 
ATOM   2120 C CB  . ASP C 1 58  ? -2.83800  28.53300 55.87200  1.000 112.64000 ? 40  ASP B CB  1 
ATOM   2121 N N   . GLU C 1 59  ? -3.91100  30.04800 58.69500  1.000 124.09000 ? 41  GLU B N   1 
ATOM   2122 C CA  . GLU C 1 59  ? -5.08500  30.22000 59.60100  1.000 126.25000 ? 41  GLU B CA  1 
ATOM   2123 C C   . GLU C 1 59  ? -4.80600  29.67100 61.00500  1.000 130.80000 ? 41  GLU B C   1 
ATOM   2124 O O   . GLU C 1 59  ? -5.41100  30.19000 61.96000  1.000 137.51000 ? 41  GLU B O   1 
ATOM   2125 C CB  . GLU C 1 59  ? -6.33300  29.56400 59.00300  1.000 120.35000 ? 41  GLU B CB  1 
ATOM   2126 N N   . ASN C 1 60  ? -3.94000  28.66400 61.12700  1.000 123.66000 ? 42  ASN B N   1 
ATOM   2127 C CA  . ASN C 1 60  ? -3.69800  28.03000 62.44700  1.000 123.02000 ? 42  ASN B CA  1 
ATOM   2128 C C   . ASN C 1 60  ? -2.37200  27.26900 62.40300  1.000 126.85000 ? 42  ASN B C   1 
ATOM   2129 O O   . ASN C 1 60  ? -1.80200  27.14500 61.30200  1.000 132.79000 ? 42  ASN B O   1 
ATOM   2130 C CB  . ASN C 1 60  ? -4.84600  27.09800 62.83500  1.000 114.93000 ? 42  ASN B CB  1 
ATOM   2131 N N   . GLY C 1 61  ? -1.92000  26.75500 63.55000  1.000 121.45000 ? 43  GLY B N   1 
ATOM   2132 C CA  . GLY C 1 61  ? -0.67300  25.96900 63.59500  1.000 115.98000 ? 43  GLY B CA  1 
ATOM   2133 C C   . GLY C 1 61  ? -0.88400  24.60000 62.98000  1.000 110.44000 ? 43  GLY B C   1 
ATOM   2134 O O   . GLY C 1 61  ? -0.13400  23.66800 63.33100  1.000 101.38000 ? 43  GLY B O   1 
ATOM   2135 N N   . ILE C 1 64  ? 0.31300   21.62600 57.25700  1.000 121.19000 ? 46  ILE B N   1 
ATOM   2136 C CA  . ILE C 1 64  ? -0.35000  20.83600 56.17400  1.000 111.76000 ? 46  ILE B CA  1 
ATOM   2137 C C   . ILE C 1 64  ? 0.72900   20.28900 55.23700  1.000 96.21000  ? 46  ILE B C   1 
ATOM   2138 O O   . ILE C 1 64  ? 1.53600   21.09100 54.73700  1.000 104.01000 ? 46  ILE B O   1 
ATOM   2139 C CB  . ILE C 1 64  ? -1.38400  21.69100 55.41700  1.000 104.54000 ? 46  ILE B CB  1 
ATOM   2140 C CG1 . ILE C 1 64  ? -2.57100  22.06800 56.30700  1.000 94.61000  ? 46  ILE B CG1 1 
ATOM   2141 C CG2 . ILE C 1 64  ? -1.83500  20.98800 54.14700  1.000 99.00000  ? 46  ILE B CG2 1 
ATOM   2142 N N   . GLU C 1 65  ? 0.74000   18.97200 55.02300  1.000 88.70000  ? 47  GLU B N   1 
ATOM   2143 C CA  . GLU C 1 65  ? 1.73900   18.36200 54.11300  1.000 89.68000  ? 47  GLU B CA  1 
ATOM   2144 C C   . GLU C 1 65  ? 1.47200   18.82600 52.67800  1.000 101.10000 ? 47  GLU B C   1 
ATOM   2145 O O   . GLU C 1 65  ? 0.32300   18.72300 52.24400  1.000 102.38000 ? 47  GLU B O   1 
ATOM   2146 C CB  . GLU C 1 65  ? 1.64700   16.84400 54.21500  1.000 74.30000  ? 47  GLU B CB  1 
ATOM   2147 N N   . VAL C 1 66  ? 2.49900   19.30800 51.97300  1.000 97.28000  ? 48  VAL B N   1 
ATOM   2148 C CA  . VAL C 1 66  ? 2.33000   19.82900 50.58500  1.000 86.38000  ? 48  VAL B CA  1 
ATOM   2149 C C   . VAL C 1 66  ? 3.30000   19.10900 49.64900  1.000 84.97000  ? 48  VAL B C   1 
ATOM   2150 O O   . VAL C 1 66  ? 4.50300   19.34500 49.75400  1.000 101.42000 ? 48  VAL B O   1 
ATOM   2151 C CB  . VAL C 1 66  ? 2.52800   21.35000 50.51500  1.000 81.73000  ? 48  VAL B CB  1 
ATOM   2152 N N   . GLU C 1 67  ? 2.77400   18.27500 48.76300  1.000 79.28000  ? 49  GLU B N   1 
ATOM   2153 C CA  . GLU C 1 67  ? 3.61300   17.52400 47.80200  1.000 81.94000  ? 49  GLU B CA  1 
ATOM   2154 C C   . GLU C 1 67  ? 4.01200   18.49500 46.69100  1.000 88.74000  ? 49  GLU B C   1 
ATOM   2155 O O   . GLU C 1 67  ? 3.12300   19.17700 46.15900  1.000 84.61000  ? 49  GLU B O   1 
ATOM   2156 C CB  . GLU C 1 67  ? 2.83600   16.30200 47.31600  1.000 79.64000  ? 49  GLU B CB  1 
ATOM   2157 C CG  . GLU C 1 67  ? 3.69600   15.16700 46.80800  1.000 88.89000  ? 49  GLU B CG  1 
ATOM   2158 C CD  . GLU C 1 67  ? 2.92200   13.86400 46.74300  1.000 90.06000  ? 49  GLU B CD  1 
ATOM   2159 O OE1 . GLU C 1 67  ? 1.74200   13.87300 47.13400  1.000 84.92000  ? 49  GLU B OE1 1 
ATOM   2160 O OE2 . GLU C 1 67  ? 3.49500   12.85000 46.30600  1.000 87.66000  ? 49  GLU B OE2 1 
ATOM   2161 N N   . VAL C 1 68  ? 5.30500   18.57100 46.38100  1.000 84.57000  ? 50  VAL B N   1 
ATOM   2162 C CA  . VAL C 1 68  ? 5.78800   19.55700 45.38100  1.000 75.05000  ? 50  VAL B CA  1 
ATOM   2163 C C   . VAL C 1 68  ? 6.58000   18.80200 44.32200  1.000 67.68000  ? 50  VAL B C   1 
ATOM   2164 O O   . VAL C 1 68  ? 7.21300   17.81000 44.66900  1.000 77.88000  ? 50  VAL B O   1 
ATOM   2165 C CB  . VAL C 1 68  ? 6.59900   20.68900 46.03900  1.000 86.97000  ? 50  VAL B CB  1 
ATOM   2166 C CG1 . VAL C 1 68  ? 5.77400   21.45500 47.05800  1.000 75.83000  ? 50  VAL B CG1 1 
ATOM   2167 C CG2 . VAL C 1 68  ? 7.88700   20.19200 46.66500  1.000 80.12000  ? 50  VAL B CG2 1 
ATOM   2168 N N   . ARG C 1 69  ? 6.48500   19.25200 43.07400  1.000 75.88000  ? 51  ARG B N   1 
ATOM   2169 C CA  . ARG C 1 69  ? 7.19800   18.59500 41.98700  1.000 71.75000  ? 51  ARG B CA  1 
ATOM   2170 C C   . ARG C 1 69  ? 7.58000   19.63200 40.94100  1.000 65.00000  ? 51  ARG B C   1 
ATOM   2171 O O   . ARG C 1 69  ? 6.86400   20.61400 40.73000  1.000 69.83000  ? 51  ARG B O   1 
ATOM   2172 C CB  . ARG C 1 69  ? 6.35500   17.49000 41.33200  1.000 67.59000  ? 51  ARG B CB  1 
ATOM   2173 C CG  . ARG C 1 69  ? 6.06400   16.28700 42.21700  1.000 61.61000  ? 51  ARG B CG  1 
ATOM   2174 C CD  . ARG C 1 69  ? 4.91000   15.46900 41.66400  1.000 64.42000  ? 51  ARG B CD  1 
ATOM   2175 N NE  . ARG C 1 69  ? 4.40400   14.51100 42.63900  1.000 62.01000  ? 51  ARG B NE  1 
ATOM   2176 C CZ  . ARG C 1 69  ? 4.65700   13.21000 42.61600  1.000 80.74000  ? 51  ARG B CZ  1 
ATOM   2177 N NH1 . ARG C 1 69  ? 5.40300   12.66800 41.66800  1.000 76.05000  ? 51  ARG B NH1 1 
ATOM   2178 N NH2 . ARG C 1 69  ? 4.14300   12.43300 43.56500  1.000 72.32000  ? 51  ARG B NH2 1 
ATOM   2179 N N   . LEU C 1 70  ? 8.72900   19.41600 40.29600  1.000 69.11000  ? 52  LEU B N   1 
ATOM   2180 C CA  . LEU C 1 70  ? 9.14000   20.29500 39.17200  1.000 59.04000  ? 52  LEU B CA  1 
ATOM   2181 C C   . LEU C 1 70  ? 9.04900   19.42900 37.92000  1.000 71.96000  ? 52  LEU B C   1 
ATOM   2182 O O   . LEU C 1 70  ? 9.89900   18.53400 37.77300  1.000 66.62000  ? 52  LEU B O   1 
ATOM   2183 C CB  . LEU C 1 70  ? 10.56900  20.79000 39.39600  1.000 66.78000  ? 52  LEU B CB  1 
ATOM   2184 C CG  . LEU C 1 70  ? 11.06700  21.82300 38.38900  1.000 66.11000  ? 52  LEU B CG  1 
ATOM   2185 C CD1 . LEU C 1 70  ? 10.28800  23.12000 38.52100  1.000 70.47000  ? 52  LEU B CD1 1 
ATOM   2186 C CD2 . LEU C 1 70  ? 12.55500  22.07700 38.56800  1.000 70.43000  ? 52  LEU B CD2 1 
ATOM   2187 N N   . LEU C 1 71  ? 8.05600   19.66900 37.06500  1.000 65.56000  ? 53  LEU B N   1 
ATOM   2188 C CA  . LEU C 1 71  ? 7.85100   18.74700 35.91800  1.000 66.49000  ? 53  LEU B CA  1 
ATOM   2189 C C   . LEU C 1 71  ? 7.75900   19.50100 34.59300  1.000 57.71000  ? 53  LEU B C   1 
ATOM   2190 O O   . LEU C 1 71  ? 7.41200   20.69000 34.61300  1.000 50.87000  ? 53  LEU B O   1 
ATOM   2191 C CB  . LEU C 1 71  ? 6.55300   17.97000 36.16000  1.000 51.30000  ? 53  LEU B CB  1 
ATOM   2192 C CG  . LEU C 1 71  ? 6.50900   17.10900 37.42000  1.000 61.55000  ? 53  LEU B CG  1 
ATOM   2193 C CD1 . LEU C 1 71  ? 5.17700   16.38600 37.52800  1.000 57.26000  ? 53  LEU B CD1 1 
ATOM   2194 C CD2 . LEU C 1 71  ? 7.65400   16.10800 37.43200  1.000 60.20000  ? 53  LEU B CD2 1 
ATOM   2195 N N   . THR C 1 72  ? 8.05800   18.81400 33.49000  1.000 47.75000  ? 54  THR B N   1 
ATOM   2196 C CA  . THR C 1 72  ? 7.87500   19.42500 32.15200  1.000 60.14000  ? 54  THR B CA  1 
ATOM   2197 C C   . THR C 1 72  ? 6.37700   19.41500 31.84400  1.000 55.54000  ? 54  THR B C   1 
ATOM   2198 O O   . THR C 1 72  ? 5.61800   18.82100 32.62700  1.000 54.17000  ? 54  THR B O   1 
ATOM   2199 C CB  . THR C 1 72  ? 8.64000   18.64900 31.07700  1.000 54.25000  ? 54  THR B CB  1 
ATOM   2200 O OG1 . THR C 1 72  ? 7.98100   17.39900 30.87300  1.000 48.27000  ? 54  THR B OG1 1 
ATOM   2201 C CG2 . THR C 1 72  ? 10.08900  18.41500 31.44200  1.000 60.50000  ? 54  THR B CG2 1 
ATOM   2202 N N   . LEU C 1 73  ? 5.97500   20.02700 30.73500  1.000 45.16000  ? 55  LEU B N   1 
ATOM   2203 C CA  . LEU C 1 73  ? 4.56300   20.03600 30.36400  1.000 53.31000  ? 55  LEU B CA  1 
ATOM   2204 C C   . LEU C 1 73  ? 4.04800   18.62200 30.12100  1.000 41.41000  ? 55  LEU B C   1 
ATOM   2205 O O   . LEU C 1 73  ? 2.93200   18.28200 30.52900  1.000 47.43000  ? 55  LEU B O   1 
ATOM   2206 C CB  . LEU C 1 73  ? 4.34300   20.91100 29.12900  1.000 46.62000  ? 55  LEU B CB  1 
ATOM   2207 C CG  . LEU C 1 73  ? 2.88700   21.06700 28.68000  1.000 55.00000  ? 55  LEU B CG  1 
ATOM   2208 C CD1 . LEU C 1 73  ? 2.03700   21.65400 29.80000  1.000 39.06000  ? 55  LEU B CD1 1 
ATOM   2209 C CD2 . LEU C 1 73  ? 2.79800   21.92500 27.42700  1.000 49.80000  ? 55  LEU B CD2 1 
ATOM   2210 N N   . GLU C 1 74  ? 4.85000   17.78100 29.46400  1.000 39.12000  ? 56  GLU B N   1 
ATOM   2211 C CA  . GLU C 1 74  ? 4.43500   16.40300 29.22900  1.000 45.47000  ? 56  GLU B CA  1 
ATOM   2212 C C   . GLU C 1 74  ? 4.38900   15.61100 30.52900  1.000 41.54000  ? 56  GLU B C   1 
ATOM   2213 O O   . GLU C 1 74  ? 3.46900   14.81200 30.74200  1.000 56.00000  ? 56  GLU B O   1 
ATOM   2214 C CB  . GLU C 1 74  ? 5.37500   15.73300 28.22700  1.000 41.28000  ? 56  GLU B CB  1 
ATOM   2215 C CG  . GLU C 1 74  ? 4.92500   14.34900 27.78800  1.000 54.56000  ? 56  GLU B CG  1 
ATOM   2216 C CD  . GLU C 1 74  ? 5.94400   13.65800 26.90300  1.000 74.46000  ? 56  GLU B CD  1 
ATOM   2217 O OE1 . GLU C 1 74  ? 7.15600   13.90100 27.08600  1.000 55.02000  ? 56  GLU B OE1 1 
ATOM   2218 O OE2 . GLU C 1 74  ? 5.53400   12.87600 26.01900  1.000 67.08000  ? 56  GLU B OE2 1 
ATOM   2219 N N   . GLU C 1 75  ? 5.36600   15.84400 31.40200  1.000 40.98000  ? 57  GLU B N   1 
ATOM   2220 C CA  . GLU C 1 75  ? 5.39800   15.14300 32.71100  1.000 48.28000  ? 57  GLU B CA  1 
ATOM   2221 C C   . GLU C 1 75  ? 4.20200   15.58800 33.55500  1.000 47.25000  ? 57  GLU B C   1 
ATOM   2222 O O   . GLU C 1 75  ? 3.57200   14.72600 34.18300  1.000 43.46000  ? 57  GLU B O   1 
ATOM   2223 C CB  . GLU C 1 75  ? 6.70500   15.45300 33.43900  1.000 52.88000  ? 57  GLU B CB  1 
ATOM   2224 C CG  . GLU C 1 75  ? 7.91700   14.76700 32.84100  1.000 74.76000  ? 57  GLU B CG  1 
ATOM   2225 C CD  . GLU C 1 75  ? 9.24500   15.26000 33.38900  1.000 65.07000  ? 57  GLU B CD  1 
ATOM   2226 O OE1 . GLU C 1 75  ? 9.23300   16.19700 34.20600  1.000 57.16000  ? 57  GLU B OE1 1 
ATOM   2227 O OE2 . GLU C 1 75  ? 10.28600  14.69800 33.00200  1.000 70.84000  ? 57  GLU B OE2 1 
ATOM   2228 N N   . ALA C 1 76  ? 3.91200   16.88800 33.55900  1.000 40.34000  ? 58  ALA B N   1 
ATOM   2229 C CA  . ALA C 1 76  ? 2.82700   17.40600 34.38400  1.000 39.50000  ? 58  ALA B CA  1 
ATOM   2230 C C   . ALA C 1 76  ? 1.47400   16.89900 33.90400  1.000 36.67000  ? 58  ALA B C   1 
ATOM   2231 O O   . ALA C 1 76  ? 0.57600   16.65900 34.71800  1.000 38.06000  ? 58  ALA B O   1 
ATOM   2232 C CB  . ALA C 1 76  ? 2.86500   18.93200 34.39400  1.000 34.98000  ? 58  ALA B CB  1 
ATOM   2233 N N   . LEU C 1 77  ? 1.30700   16.72900 32.59100  1.000 39.43000  ? 59  LEU B N   1 
ATOM   2234 C CA  . LEU C 1 77  ? 0.05400   16.18600 32.07600  1.000 45.19000  ? 59  LEU B CA  1 
ATOM   2235 C C   . LEU C 1 77  ? -0.10500  14.71800 32.45000  1.000 47.72000  ? 59  LEU B C   1 
ATOM   2236 O O   . LEU C 1 77  ? -1.22000  14.26300 32.73200  1.000 40.24000  ? 59  LEU B O   1 
ATOM   2237 C CB  . LEU C 1 77  ? -0.01200  16.36700 30.56100  1.000 38.20000  ? 59  LEU B CB  1 
ATOM   2238 C CG  . LEU C 1 77  ? -0.25400  17.79300 30.06500  1.000 46.46000  ? 59  LEU B CG  1 
ATOM   2239 C CD1 . LEU C 1 77  ? 0.05700   17.89500 28.58300  1.000 43.76000  ? 59  LEU B CD1 1 
ATOM   2240 C CD2 . LEU C 1 77  ? -1.68800  18.21300 30.34400  1.000 36.17000  ? 59  LEU B CD2 1 
ATOM   2241 N N   . LYS C 1 78  ? 0.99600   13.96300 32.45800  1.000 43.26000  ? 60  LYS B N   1 
ATOM   2242 C CA  . LYS C 1 78  ? 0.92900   12.57000 32.88300  1.000 57.05000  ? 60  LYS B CA  1 
ATOM   2243 C C   . LYS C 1 78  ? 0.67900   12.46700 34.38200  1.000 45.79000  ? 60  LYS B C   1 
ATOM   2244 O O   . LYS C 1 78  ? -0.02300  11.55800 34.83900  1.000 41.27000  ? 60  LYS B O   1 
ATOM   2245 C CB  . LYS C 1 78  ? 2.21800   11.84200 32.50100  1.000 48.07000  ? 60  LYS B CB  1 
ATOM   2246 C CG  . LYS C 1 78  ? 2.16500   10.34100 32.73200  1.000 66.75000  ? 60  LYS B CG  1 
ATOM   2247 C CD  . LYS C 1 78  ? 3.50500   9.68200  32.45900  1.000 58.88000  ? 60  LYS B CD  1 
ATOM   2248 C CE  . LYS C 1 78  ? 3.39500   8.16800  32.55500  1.000 74.84000  ? 60  LYS B CE  1 
ATOM   2249 N NZ  . LYS C 1 78  ? 2.85200   7.72800  33.86900  1.000 63.14000  ? 60  LYS B NZ  1 
ATOM   2250 N N   . TYR C 1 79  ? 1.24800   13.38900 35.16200  1.000 40.66000  ? 61  TYR B N   1 
ATOM   2251 C CA  . TYR C 1 79  ? 1.00000   13.40300 36.60000  1.000 43.81000  ? 61  TYR B CA  1 
ATOM   2252 C C   . TYR C 1 79  ? -0.46400  13.69300 36.90300  1.000 44.89000  ? 61  TYR B C   1 
ATOM   2253 O O   . TYR C 1 79  ? -1.04900  13.09300 37.81200  1.000 49.68000  ? 61  TYR B O   1 
ATOM   2254 C CB  . TYR C 1 79  ? 1.90800   14.43300 37.27200  1.000 51.23000  ? 61  TYR B CB  1 
ATOM   2255 C CG  . TYR C 1 79  ? 1.55400   14.73300 38.71000  1.000 40.92000  ? 61  TYR B CG  1 
ATOM   2256 C CD1 . TYR C 1 79  ? 1.94500   13.88200 39.73500  1.000 48.80000  ? 61  TYR B CD1 1 
ATOM   2257 C CD2 . TYR C 1 79  ? 0.83700   15.87500 39.04500  1.000 48.24000  ? 61  TYR B CD2 1 
ATOM   2258 C CE1 . TYR C 1 79  ? 1.62500   14.15600 41.05000  1.000 41.38000  ? 61  TYR B CE1 1 
ATOM   2259 C CE2 . TYR C 1 79  ? 0.51400   16.15700 40.35700  1.000 52.90000  ? 61  TYR B CE2 1 
ATOM   2260 C CZ  . TYR C 1 79  ? 0.91000   15.29500 41.35500  1.000 50.22000  ? 61  TYR B CZ  1 
ATOM   2261 O OH  . TYR C 1 79  ? 0.58900   15.57300 42.66400  1.000 60.40000  ? 61  TYR B OH  1 
ATOM   2262 N N   . ILE C 1 80  ? -1.07200  14.61500 36.15100  1.000 46.82000  ? 62  ILE B N   1 
ATOM   2263 C CA  . ILE C 1 80  ? -2.48600  14.92500 36.34300  1.000 33.42000  ? 62  ILE B CA  1 
ATOM   2264 C C   . ILE C 1 80  ? -3.34600  13.71100 36.01800  1.000 37.05000  ? 62  ILE B C   1 
ATOM   2265 O O   . ILE C 1 80  ? -4.31300  13.40500 36.72800  1.000 41.12000  ? 62  ILE B O   1 
ATOM   2266 C CB  . ILE C 1 80  ? -2.88200  16.14500 35.48800  1.000 40.06000  ? 62  ILE B CB  1 
ATOM   2267 C CG1 . ILE C 1 80  ? -2.23400  17.41800 36.03600  1.000 37.39000  ? 62  ILE B CG1 1 
ATOM   2268 C CG2 . ILE C 1 80  ? -4.39600  16.29200 35.41900  1.000 44.12000  ? 62  ILE B CG2 1 
ATOM   2269 C CD1 . ILE C 1 80  ? -2.42400  18.62600 35.14600  1.000 45.05000  ? 62  ILE B CD1 1 
ATOM   2270 N N   . ASN C 1 81  ? -3.00000  12.99200 34.94800  1.000 35.29000  ? 63  ASN B N   1 
ATOM   2271 C CA  . ASN C 1 81  ? -3.79500  11.84200 34.53600  1.000 40.49000  ? 63  ASN B CA  1 
ATOM   2272 C C   . ASN C 1 81  ? -3.70300  10.69800 35.53900  1.000 39.67000  ? 63  ASN B C   1 
ATOM   2273 O O   . ASN C 1 81  ? -4.62900  9.88500  35.63500  1.000 40.61000  ? 63  ASN B O   1 
ATOM   2274 C CB  . ASN C 1 81  ? -3.34800  11.37000 33.15200  1.000 49.67000  ? 63  ASN B CB  1 
ATOM   2275 C CG  . ASN C 1 81  ? -4.27800  10.33000 32.56100  1.000 56.60000  ? 63  ASN B CG  1 
ATOM   2276 O OD1 . ASN C 1 81  ? -5.49700  10.42500 32.69300  1.000 67.79000  ? 63  ASN B OD1 1 
ATOM   2277 N ND2 . ASN C 1 81  ? -3.70400  9.32400  31.91000  1.000 64.13000  ? 63  ASN B ND2 1 
ATOM   2278 N N   . ASP C 1 82  ? -2.60600  10.62000 36.29300  1.000 42.48000  ? 64  ASP B N   1 
ATOM   2279 C CA  . ASP C 1 82  ? -2.39800  9.54400  37.25400  1.000 49.41000  ? 64  ASP B CA  1 
ATOM   2280 C C   . ASP C 1 82  ? -2.98800  9.83400  38.62800  1.000 45.19000  ? 64  ASP B C   1 
ATOM   2281 O O   . ASP C 1 82  ? -3.00700  8.93500  39.47600  1.000 51.90000  ? 64  ASP B O   1 
ATOM   2282 C CB  . ASP C 1 82  ? -0.90100  9.24800  37.40500  1.000 51.35000  ? 64  ASP B CB  1 
ATOM   2283 C CG  . ASP C 1 82  ? -0.28300  8.70400  36.13300  1.000 63.40000  ? 64  ASP B CG  1 
ATOM   2284 O OD1 . ASP C 1 82  ? -1.00300  8.03600  35.35900  1.000 61.14000  ? 64  ASP B OD1 1 
ATOM   2285 O OD2 . ASP C 1 82  ? 0.92200   8.94500  35.90800  1.000 55.20000  ? 64  ASP B OD2 1 
ATOM   2286 N N   . LEU C 1 83  ? -3.46400  11.05100 38.87000  1.000 42.62000  ? 65  LEU B N   1 
ATOM   2287 C CA  . LEU C 1 83  ? -3.99500  11.39400 40.18200  1.000 39.67000  ? 65  LEU B CA  1 
ATOM   2288 C C   . LEU C 1 83  ? -5.27500  10.60800 40.45500  1.000 54.56000  ? 65  LEU B C   1 
ATOM   2289 O O   . LEU C 1 83  ? -6.05000  10.34400 39.53200  1.000 51.45000  ? 65  LEU B O   1 
ATOM   2290 C CB  . LEU C 1 83  ? -4.27600  12.89300 40.27100  1.000 41.76000  ? 65  LEU B CB  1 
ATOM   2291 C CG  . LEU C 1 83  ? -3.06200  13.81300 40.42100  1.000 45.70000  ? 65  LEU B CG  1 
ATOM   2292 C CD1 . LEU C 1 83  ? -3.46100  15.27200 40.26700  1.000 37.05000  ? 65  LEU B CD1 1 
ATOM   2293 C CD2 . LEU C 1 83  ? -2.38500  13.58300 41.76400  1.000 39.81000  ? 65  LEU B CD2 1 
ATOM   2294 N N   . PRO C 1 84  ? -5.51800  10.19900 41.70200  1.000 43.80000  ? 66  PRO B N   1 
ATOM   2295 C CA  . PRO C 1 84  ? -6.78200  9.51900  42.03900  1.000 37.22000  ? 66  PRO B CA  1 
ATOM   2296 C C   . PRO C 1 84  ? -7.90700  10.51200 42.33600  1.000 35.63000  ? 66  PRO B C   1 
ATOM   2297 O O   . PRO C 1 84  ? -8.43000  10.58700 43.45400  1.000 44.68000  ? 66  PRO B O   1 
ATOM   2298 C CB  . PRO C 1 84  ? -6.38900  8.68900  43.26500  1.000 49.13000  ? 66  PRO B CB  1 
ATOM   2299 C CG  . PRO C 1 84  ? -5.34800  9.51500  43.93200  1.000 43.17000  ? 66  PRO B CG  1 
ATOM   2300 C CD  . PRO C 1 84  ? -4.57300  10.19500 42.83300  1.000 46.39000  ? 66  PRO B CD  1 
ATOM   2301 N N   . ILE C 1 85  ? -8.27900  11.29200 41.32400  1.000 43.18000  ? 67  ILE B N   1 
ATOM   2302 C CA  . ILE C 1 85  ? -9.33100  12.29000 41.43500  1.000 40.30000  ? 67  ILE B CA  1 
ATOM   2303 C C   . ILE C 1 85  ? -10.35400 12.04500 40.33100  1.000 33.84000  ? 67  ILE B C   1 
ATOM   2304 O O   . ILE C 1 85  ? -10.23000 11.11500 39.53600  1.000 41.55000  ? 67  ILE B O   1 
ATOM   2305 C CB  . ILE C 1 85  ? -8.78200  13.73000 41.36400  1.000 42.37000  ? 67  ILE B CB  1 
ATOM   2306 C CG1 . ILE C 1 85  ? -8.05000  13.95700 40.04000  1.000 33.78000  ? 67  ILE B CG1 1 
ATOM   2307 C CG2 . ILE C 1 85  ? -7.86800  14.01200 42.54700  1.000 38.38000  ? 67  ILE B CG2 1 
ATOM   2308 C CD1 . ILE C 1 85  ? -7.53100  15.36500 39.86100  1.000 42.67000  ? 67  ILE B CD1 1 
ATOM   2309 N N   . SER C 1 86  ? -11.35000 12.91700 40.29000  1.000 36.20000  ? 68  SER B N   1 
ATOM   2310 C CA  . SER C 1 86  ? -12.40600 12.87600 39.25400  1.000 39.23000  ? 68  SER B CA  1 
ATOM   2311 C C   . SER C 1 86  ? -11.82200 13.15900 37.87400  1.000 37.03000  ? 68  SER B C   1 
ATOM   2312 O O   . SER C 1 86  ? -10.94200 13.99600 37.76800  1.000 44.28000  ? 68  SER B O   1 
ATOM   2313 C CB  . SER C 1 86  ? -13.47000 13.87600 39.56600  1.000 33.63000  ? 68  SER B CB  1 
ATOM   2314 O OG  . SER C 1 86  ? -13.25700 15.08900 38.87600  1.000 54.00000  ? 68  SER B OG  1 
ATOM   2315 N N   . ASN C 1 87  ? -12.33600 12.47600 36.86500  1.000 32.91000  ? 69  ASN B N   1 
ATOM   2316 C CA  . ASN C 1 87  ? -11.87300 12.75400 35.51000  1.000 37.37000  ? 69  ASN B CA  1 
ATOM   2317 C C   . ASN C 1 87  ? -12.21700 14.17300 35.08100  1.000 39.85000  ? 69  ASN B C   1 
ATOM   2318 O O   . ASN C 1 87  ? -11.48100 14.77700 34.29100  1.000 37.14000  ? 69  ASN B O   1 
ATOM   2319 C CB  . ASN C 1 87  ? -12.46900 11.74300 34.53200  1.000 39.59000  ? 69  ASN B CB  1 
ATOM   2320 C CG  . ASN C 1 87  ? -11.88500 10.35700 34.70100  1.000 48.96000  ? 69  ASN B CG  1 
ATOM   2321 O OD1 . ASN C 1 87  ? -11.15900 10.08900 35.65900  1.000 43.35000  ? 69  ASN B OD1 1 
ATOM   2322 N ND2 . ASN C 1 87  ? -12.19700 9.46500  33.76900  1.000 46.84000  ? 69  ASN B ND2 1 
ATOM   2323 N N   . ASP C 1 88  ? -13.30000 14.71800 35.61200  1.000 41.95000  ? 70  ASP B N   1 
ATOM   2324 C CA  . ASP C 1 88  ? -13.66900 16.11600 35.30000  1.000 42.12000  ? 70  ASP B CA  1 
ATOM   2325 C C   . ASP C 1 88  ? -12.56800 17.05500 35.79900  1.000 43.79000  ? 70  ASP B C   1 
ATOM   2326 O O   . ASP C 1 88  ? -12.12300 17.88000 35.01000  1.000 53.54000  ? 70  ASP B O   1 
ATOM   2327 C CB  . ASP C 1 88  ? -15.06500 16.42900 35.82600  1.000 38.94000  ? 70  ASP B CB  1 
ATOM   2328 C CG  . ASP C 1 88  ? -16.16800 15.79500 34.99900  1.000 64.74000  ? 70  ASP B CG  1 
ATOM   2329 O OD1 . ASP C 1 88  ? -15.84400 15.16700 33.97500  1.000 45.01000  ? 70  ASP B OD1 1 
ATOM   2330 O OD2 . ASP C 1 88  ? -17.33900 15.92500 35.39300  1.000 60.77000  ? 70  ASP B OD2 1 
ATOM   2331 N N   . ALA C 1 89  ? -12.14300 16.92800 37.04700  1.000 43.78000  ? 71  ALA B N   1 
ATOM   2332 C CA  . ALA C 1 89  ? -11.01200 17.72700 37.55800  1.000 42.54000  ? 71  ALA B CA  1 
ATOM   2333 C C   . ALA C 1 89  ? -9.80100  17.54100 36.64300  1.000 41.93000  ? 71  ALA B C   1 
ATOM   2334 O O   . ALA C 1 89  ? -9.16400  18.53300 36.33600  1.000 47.69000  ? 71  ALA B O   1 
ATOM   2335 C CB  . ALA C 1 89  ? -10.70000 17.32400 38.96500  1.000 32.49000  ? 71  ALA B CB  1 
ATOM   2336 N N   . LYS C 1 90  ? -9.50200  16.30700 36.25000  1.000 36.63000  ? 72  LYS B N   1 
ATOM   2337 C CA  . LYS C 1 90  ? -8.33300  16.09500 35.40100  1.000 34.89000  ? 72  LYS B CA  1 
ATOM   2338 C C   . LYS C 1 90  ? -8.44100  16.89800 34.11200  1.000 34.56000  ? 72  LYS B C   1 
ATOM   2339 O O   . LYS C 1 90  ? -7.48100  17.55400 33.69200  1.000 38.54000  ? 72  LYS B O   1 
ATOM   2340 C CB  . LYS C 1 90  ? -8.17100  14.60900 35.08300  1.000 36.63000  ? 72  LYS B CB  1 
ATOM   2341 C CG  . LYS C 1 90  ? -7.92800  13.72300 36.28600  1.000 41.31000  ? 72  LYS B CG  1 
ATOM   2342 C CD  . LYS C 1 90  ? -7.66200  12.29900 35.83500  1.000 29.29000  ? 72  LYS B CD  1 
ATOM   2343 C CE  . LYS C 1 90  ? -7.51000  11.36200 37.01100  1.000 31.60000  ? 72  LYS B CE  1 
ATOM   2344 N NZ  . LYS C 1 90  ? -7.11400  9.99700  36.56800  1.000 40.32000  ? 72  LYS B NZ  1 
ATOM   2345 N N   . LYS C 1 91  ? -9.60800  16.85100 33.46400  1.000 36.51000  ? 73  LYS B N   1 
ATOM   2346 C CA  . LYS C 1 91  ? -9.79700  17.59800 32.22500  1.000 47.00000  ? 73  LYS B CA  1 
ATOM   2347 C C   . LYS C 1 91  ? -9.71500  19.09900 32.47100  1.000 38.07000  ? 73  LYS B C   1 
ATOM   2348 O O   . LYS C 1 91  ? -9.20400  19.84800 31.62900  1.000 40.85000  ? 73  LYS B O   1 
ATOM   2349 C CB  . LYS C 1 91  ? -11.13800 17.22600 31.59100  1.000 49.56000  ? 73  LYS B CB  1 
ATOM   2350 C CG  . LYS C 1 91  ? -11.42500 17.93200 30.28000  1.000 71.27000  ? 73  LYS B CG  1 
ATOM   2351 C CD  . LYS C 1 91  ? -12.79300 17.55300 29.74000  1.000 76.31000  ? 73  LYS B CD  1 
ATOM   2352 C CE  . LYS C 1 91  ? -13.09900 18.29700 28.45200  1.000 88.47000  ? 73  LYS B CE  1 
ATOM   2353 N NZ  . LYS C 1 91  ? -14.45000 17.95800 27.92700  1.000 93.11000  ? 73  LYS B NZ  1 
ATOM   2354 N N   . LEU C 1 92  ? -10.18600 19.55700 33.62000  1.000 35.95000  ? 74  LEU B N   1 
ATOM   2355 C CA  . LEU C 1 92  ? -10.11900 21.00000 33.94400  1.000 50.41000  ? 74  LEU B CA  1 
ATOM   2356 C C   . LEU C 1 92  ? -8.65700  21.41000 34.17000  1.000 52.52000  ? 74  LEU B C   1 
ATOM   2357 O O   . LEU C 1 92  ? -8.28900  22.50200 33.74900  1.000 45.41000  ? 74  LEU B O   1 
ATOM   2358 C CB  . LEU C 1 92  ? -11.00100 21.29200 35.16000  1.000 46.27000  ? 74  LEU B CB  1 
ATOM   2359 C CG  . LEU C 1 92  ? -11.07700 22.75100 35.59300  1.000 65.36000  ? 74  LEU B CG  1 
ATOM   2360 C CD1 . LEU C 1 92  ? -11.97300 23.53700 34.65500  1.000 70.07000  ? 74  LEU B CD1 1 
ATOM   2361 C CD2 . LEU C 1 92  ? -11.57800 22.85700 37.02300  1.000 78.21000  ? 74  LEU B CD2 1 
ATOM   2362 N N   . MET C 1 93  ? -7.85500  20.54600 34.78600  1.000 42.96000  ? 75  MET B N   1 
ATOM   2363 C CA  . MET C 1 93  ? -6.44400  20.87000 34.97100  1.000 40.28000  ? 75  MET B CA  1 
ATOM   2364 C C   . MET C 1 93  ? -5.67700  20.77000 33.65800  1.000 42.20000  ? 75  MET B C   1 
ATOM   2365 O O   . MET C 1 93  ? -4.76900  21.56800 33.40100  1.000 46.20000  ? 75  MET B O   1 
ATOM   2366 C CB  . MET C 1 93  ? -5.82300  19.94800 36.02100  1.000 44.71000  ? 75  MET B CB  1 
ATOM   2367 C CG  . MET C 1 93  ? -6.41200  20.09500 37.41400  1.000 56.25000  ? 75  MET B CG  1 
ATOM   2368 S SD  . MET C 1 93  ? -5.62800  18.99000 38.60500  1.000 54.54000  ? 75  MET B SD  1 
ATOM   2369 C CE  . MET C 1 93  ? -6.60200  19.33100 40.06600  1.000 66.91000  ? 75  MET B CE  1 
ATOM   2370 N N   . SER C 1 94  ? -6.03000  19.79700 32.81400  1.000 48.15000  ? 76  SER B N   1 
ATOM   2371 C CA  . SER C 1 94  ? -5.29600  19.59300 31.56900  1.000 39.03000  ? 76  SER B CA  1 
ATOM   2372 C C   . SER C 1 94  ? -5.56800  20.70100 30.56000  1.000 38.07000  ? 76  SER B C   1 
ATOM   2373 O O   . SER C 1 94  ? -4.67900  21.05500 29.77700  1.000 47.17000  ? 76  SER B O   1 
ATOM   2374 C CB  . SER C 1 94  ? -5.65100  18.23200 30.96800  1.000 36.75000  ? 76  SER B CB  1 
ATOM   2375 O OG  . SER C 1 94  ? -5.34900  17.18000 31.87000  1.000 54.09000  ? 76  SER B OG  1 
ATOM   2376 N N   . ASN C 1 95  ? -6.77900  21.25900 30.55900  1.000 46.45000  ? 77  ASN B N   1 
ATOM   2377 C CA  . ASN C 1 95  ? -7.12400  22.30400 29.60500  1.000 43.79000  ? 77  ASN B CA  1 
ATOM   2378 C C   . ASN C 1 95  ? -6.60900  23.68100 30.00600  1.000 43.89000  ? 77  ASN B C   1 
ATOM   2379 O O   . ASN C 1 95  ? -6.66200  24.60300 29.18500  1.000 46.61000  ? 77  ASN B O   1 
ATOM   2380 C CB  . ASN C 1 95  ? -8.64200  22.36400 29.41400  1.000 44.35000  ? 77  ASN B CB  1 
ATOM   2381 C CG  . ASN C 1 95  ? -9.18100  21.18000 28.63700  1.000 54.32000  ? 77  ASN B CG  1 
ATOM   2382 O OD1 . ASN C 1 95  ? -8.46600  20.56000 27.85100  1.000 74.70000  ? 77  ASN B OD1 1 
ATOM   2383 N ND2 . ASN C 1 95  ? -10.45300 20.86300 28.85000  1.000 52.84000  ? 77  ASN B ND2 1 
ATOM   2384 N N   . ASN C 1 96  ? -6.11200  23.84900 31.23300  1.000 40.86000  ? 78  ASN B N   1 
ATOM   2385 C CA  . ASN C 1 96  ? -5.65900  25.15200 31.69600  1.000 39.66000  ? 78  ASN B CA  1 
ATOM   2386 C C   . ASN C 1 96  ? -4.23600  25.15600 32.23700  1.000 57.31000  ? 78  ASN B C   1 
ATOM   2387 O O   . ASN C 1 96  ? -3.75500  26.21900 32.64600  1.000 55.76000  ? 78  ASN B O   1 
ATOM   2388 C CB  . ASN C 1 96  ? -6.60500  25.69700 32.77900  1.000 43.78000  ? 78  ASN B CB  1 
ATOM   2389 C CG  . ASN C 1 96  ? -8.03900  25.80000 32.30100  1.000 50.37000  ? 78  ASN B CG  1 
ATOM   2390 O OD1 . ASN C 1 96  ? -8.39000  26.70300 31.54300  1.000 57.62000  ? 78  ASN B OD1 1 
ATOM   2391 N ND2 . ASN C 1 96  ? -8.88000  24.87500 32.75100  1.000 54.67000  ? 78  ASN B ND2 1 
ATOM   2392 N N   . ILE C 1 97  ? -3.54700  24.01200 32.24900  1.000 47.91000  ? 79  ILE B N   1 
ATOM   2393 C CA  . ILE C 1 97  ? -2.20800  23.96300 32.83000  1.000 50.82000  ? 79  ILE B CA  1 
ATOM   2394 C C   . ILE C 1 97  ? -1.22100  24.78100 32.00500  1.000 48.46000  ? 79  ILE B C   1 
ATOM   2395 O O   . ILE C 1 97  ? -0.23500  25.30100 32.54200  1.000 38.65000  ? 79  ILE B O   1 
ATOM   2396 C CB  . ILE C 1 97  ? -1.74900  22.50000 32.98400  1.000 61.05000  ? 79  ILE B CB  1 
ATOM   2397 C CG1 . ILE C 1 97  ? -0.41300  22.42900 33.72200  1.000 65.66000  ? 79  ILE B CG1 1 
ATOM   2398 C CG2 . ILE C 1 97  ? -1.65300  21.81300 31.62600  1.000 59.27000  ? 79  ILE B CG2 1 
ATOM   2399 C CD1 . ILE C 1 97  ? 0.09500   21.02800 33.89800  1.000 65.01000  ? 79  ILE B CD1 1 
ATOM   2400 N N   . HIS C 1 98  ? -1.46800  24.92500 30.70000  1.000 47.75000  ? 80  HIS B N   1 
ATOM   2401 C CA  . HIS C 1 98  ? -0.56800  25.69800 29.85200  1.000 52.49000  ? 80  HIS B CA  1 
ATOM   2402 C C   . HIS C 1 98  ? -0.53400  27.17000 30.23900  1.000 58.92000  ? 80  HIS B C   1 
ATOM   2403 O O   . HIS C 1 98  ? 0.44100   27.86100 29.92300  1.000 57.52000  ? 80  HIS B O   1 
ATOM   2404 C CB  . HIS C 1 98  ? -0.97600  25.55900 28.38500  1.000 41.98000  ? 80  HIS B CB  1 
ATOM   2405 C CG  . HIS C 1 98  ? -2.27500  26.22700 28.05400  1.000 51.94000  ? 80  HIS B CG  1 
ATOM   2406 N ND1 . HIS C 1 98  ? -3.49700  25.63300 28.28100  1.000 55.80000  ? 80  HIS B ND1 1 
ATOM   2407 C CD2 . HIS C 1 98  ? -2.54100  27.43900 27.51200  1.000 48.61000  ? 80  HIS B CD2 1 
ATOM   2408 C CE1 . HIS C 1 98  ? -4.46000  26.45000 27.89400  1.000 56.76000  ? 80  HIS B CE1 1 
ATOM   2409 N NE2 . HIS C 1 98  ? -3.90700  27.55300 27.42300  1.000 55.54000  ? 80  HIS B NE2 1 
ATOM   2410 N N   . LYS C 1 99  ? -1.57400  27.66500 30.91500  1.000 54.43000  ? 81  LYS B N   1 
ATOM   2411 C CA  . LYS C 1 99  ? -1.59000  29.06400 31.32700  1.000 41.67000  ? 81  LYS B CA  1 
ATOM   2412 C C   . LYS C 1 99  ? -0.51800  29.35300 32.36800  1.000 51.56000  ? 81  LYS B C   1 
ATOM   2413 O O   . LYS C 1 99  ? -0.04900  30.49200 32.47700  1.000 58.54000  ? 81  LYS B O   1 
ATOM   2414 C CB  . LYS C 1 99  ? -2.96900  29.43700 31.86900  1.000 55.00000  ? 81  LYS B CB  1 
ATOM   2415 C CG  . LYS C 1 99  ? -4.11300  29.17400 30.90300  1.000 62.33000  ? 81  LYS B CG  1 
ATOM   2416 C CD  . LYS C 1 99  ? -5.43800  29.62200 31.49500  1.000 55.54000  ? 81  LYS B CD  1 
ATOM   2417 C CE  . LYS C 1 99  ? -6.60300  29.24700 30.59500  1.000 57.59000  ? 81  LYS B CE  1 
ATOM   2418 N NZ  . LYS C 1 99  ? -6.48100  29.85100 29.24100  1.000 64.61000  ? 81  LYS B NZ  1 
ATOM   2419 N N   . ALA C 1 100 ? -0.11500  28.34000 33.13700  1.000 39.61000  ? 82  ALA B N   1 
ATOM   2420 C CA  . ALA C 1 100 ? 0.91100   28.51400 34.15800  1.000 59.66000  ? 82  ALA B CA  1 
ATOM   2421 C C   . ALA C 1 100 ? 2.30700   28.67200 33.57200  1.000 56.19000  ? 82  ALA B C   1 
ATOM   2422 O O   . ALA C 1 100 ? 3.24400   28.96600 34.32300  1.000 48.36000  ? 82  ALA B O   1 
ATOM   2423 C CB  . ALA C 1 100 ? 0.89200   27.33200 35.12800  1.000 46.08000  ? 82  ALA B CB  1 
ATOM   2424 N N   . LEU C 1 101 ? 2.47100   28.48100 32.26300  1.000 51.43000  ? 83  LEU B N   1 
ATOM   2425 C CA  . LEU C 1 101 ? 3.77400   28.65000 31.63300  1.000 66.79000  ? 83  LEU B CA  1 
ATOM   2426 C C   . LEU C 1 101 ? 4.14800   30.11300 31.43600  1.000 71.34000  ? 83  LEU B C   1 
ATOM   2427 O O   . LEU C 1 101 ? 5.33600   30.41900 31.28800  1.000 52.55000  ? 83  LEU B O   1 
ATOM   2428 C CB  . LEU C 1 101 ? 3.80200   27.92900 30.28500  1.000 52.70000  ? 83  LEU B CB  1 
ATOM   2429 C CG  . LEU C 1 101 ? 3.71500   26.40300 30.35600  1.000 62.40000  ? 83  LEU B CG  1 
ATOM   2430 C CD1 . LEU C 1 101 ? 3.44400   25.81600 28.98500  1.000 55.74000  ? 83  LEU B CD1 1 
ATOM   2431 C CD2 . LEU C 1 101 ? 4.99600   25.83200 30.93600  1.000 56.36000  ? 83  LEU B CD2 1 
ATOM   2432 N N   . GLU C 1 102 ? 3.17100   31.01600 31.42900  1.000 69.64000  ? 84  GLU B N   1 
ATOM   2433 C CA  . GLU C 1 102 ? 3.47100   32.42700 31.26900  1.000 67.66000  ? 84  GLU B CA  1 
ATOM   2434 C C   . GLU C 1 102 ? 4.05700   32.99100 32.56400  1.000 60.28000  ? 84  GLU B C   1 
ATOM   2435 O O   . GLU C 1 102 ? 3.69200   32.55600 33.65900  1.000 68.99000  ? 84  GLU B O   1 
ATOM   2436 C CB  . GLU C 1 102 ? 2.21500   33.19900 30.87600  1.000 64.83000  ? 84  GLU B CB  1 
ATOM   2437 C CG  . GLU C 1 102 ? 1.57000   32.71200 29.58500  1.000 59.16000  ? 84  GLU B CG  1 
ATOM   2438 C CD  . GLU C 1 102 ? 2.47800   32.87100 28.37700  1.000 90.99000  ? 84  GLU B CD  1 
ATOM   2439 O OE1 . GLU C 1 102 ? 3.31200   33.80000 28.37200  1.000 91.60000  ? 84  GLU B OE1 1 
ATOM   2440 O OE2 . GLU C 1 102 ? 2.35800   32.06300 27.43200  1.000 95.59000  ? 84  GLU B OE2 1 
ATOM   2441 N N   . PRO C 1 103 ? 4.97900   33.94700 32.46200  1.000 79.32000  ? 85  PRO B N   1 
ATOM   2442 C CA  . PRO C 1 103 ? 5.59900   34.50600 33.67200  1.000 69.37000  ? 85  PRO B CA  1 
ATOM   2443 C C   . PRO C 1 103 ? 4.57400   35.21400 34.54500  1.000 54.41000  ? 85  PRO B C   1 
ATOM   2444 O O   . PRO C 1 103 ? 3.76400   36.01000 34.06400  1.000 52.08000  ? 85  PRO B O   1 
ATOM   2445 C CB  . PRO C 1 103 ? 6.64200   35.48300 33.11600  1.000 76.79000  ? 85  PRO B CB  1 
ATOM   2446 C CG  . PRO C 1 103 ? 6.89800   35.02000 31.71900  1.000 76.85000  ? 85  PRO B CG  1 
ATOM   2447 C CD  . PRO C 1 103 ? 5.59400   34.47200 31.23100  1.000 83.82000  ? 85  PRO B CD  1 
ATOM   2448 N N   . GLY C 1 104 ? 4.61500   34.91300 35.84300  1.000 55.69000  ? 86  GLY B N   1 
ATOM   2449 C CA  . GLY C 1 104 ? 3.72900   35.52800 36.80600  1.000 67.89000  ? 86  GLY B CA  1 
ATOM   2450 C C   . GLY C 1 104 ? 2.35000   34.91500 36.90600  1.000 78.32000  ? 86  GLY B C   1 
ATOM   2451 O O   . GLY C 1 104 ? 1.59100   35.28800 37.81000  1.000 68.09000  ? 86  GLY B O   1 
ATOM   2452 N N   . ARG C 1 105 ? 1.99500   33.99000 36.01800  1.000 67.77000  ? 87  ARG B N   1 
ATOM   2453 C CA  . ARG C 1 105 ? 0.67400   33.37800 36.02700  1.000 54.72000  ? 87  ARG B CA  1 
ATOM   2454 C C   . ARG C 1 105 ? 0.66000   32.16300 36.94500  1.000 58.59000  ? 87  ARG B C   1 
ATOM   2455 O O   . ARG C 1 105 ? 1.56100   31.31900 36.88600  1.000 67.52000  ? 87  ARG B O   1 
ATOM   2456 C CB  . ARG C 1 105 ? 0.25200   32.98100 34.61200  1.000 54.95000  ? 87  ARG B CB  1 
ATOM   2457 C CG  . ARG C 1 105 ? -0.32800  34.12900 33.80400  1.000 68.28000  ? 87  ARG B CG  1 
ATOM   2458 C CD  . ARG C 1 105 ? -1.71600  33.78500 33.28800  1.000 65.35000  ? 87  ARG B CD  1 
ATOM   2459 N NE  . ARG C 1 105 ? -1.67000  32.92700 32.11000  1.000 77.00000  ? 87  ARG B NE  1 
ATOM   2460 C CZ  . ARG C 1 105 ? -1.85300  33.35500 30.86800  1.000 89.33000  ? 87  ARG B CZ  1 
ATOM   2461 N NH1 . ARG C 1 105 ? -2.10600  34.62600 30.60500  1.000 83.32000  ? 87  ARG B NH1 1 
ATOM   2462 N NH2 . ARG C 1 105 ? -1.78500  32.48400 29.86500  1.000 78.98000  ? 87  ARG B NH2 1 
ATOM   2463 N N   . THR C 1 106 ? -0.36600  32.11300 37.79400  1.000 62.05000  ? 88  THR B N   1 
ATOM   2464 C CA  . THR C 1 106 ? -0.55500  30.97500 38.72300  1.000 67.90000  ? 88  THR B CA  1 
ATOM   2465 C C   . THR C 1 106 ? -1.95800  30.41500 38.51300  1.000 66.80000  ? 88  THR B C   1 
ATOM   2466 O O   . THR C 1 106 ? -2.89100  31.20700 38.38500  1.000 62.62000  ? 88  THR B O   1 
ATOM   2467 C CB  . THR C 1 106 ? -0.34500  31.36200 40.19000  1.000 62.55000  ? 88  THR B CB  1 
ATOM   2468 O OG1 . THR C 1 106 ? 1.00700   31.78800 40.33800  1.000 65.32000  ? 88  THR B OG1 1 
ATOM   2469 C CG2 . THR C 1 106 ? -0.62800  30.22900 41.15100  1.000 46.33000  ? 88  THR B CG2 1 
ATOM   2470 N N   . VAL C 1 107 ? -2.07600  29.09900 38.43500  1.000 62.60000  ? 89  VAL B N   1 
ATOM   2471 C CA  . VAL C 1 107 ? -3.35600  28.42000 38.27200  1.000 61.79000  ? 89  VAL B CA  1 
ATOM   2472 C C   . VAL C 1 107 ? -3.63200  27.61400 39.53200  1.000 55.07000  ? 89  VAL B C   1 
ATOM   2473 O O   . VAL C 1 107 ? -2.76600  26.86200 39.99800  1.000 49.69000  ? 89  VAL B O   1 
ATOM   2474 C CB  . VAL C 1 107 ? -3.36400  27.51700 37.02600  1.000 55.90000  ? 89  VAL B CB  1 
ATOM   2475 C CG1 . VAL C 1 107 ? -4.79000  27.22500 36.60000  1.000 60.04000  ? 89  VAL B CG1 1 
ATOM   2476 C CG2 . VAL C 1 107 ? -2.58800  28.16700 35.89200  1.000 61.22000  ? 89  VAL B CG2 1 
ATOM   2477 N N   . VAL C 1 108 ? -4.83200  27.77200 40.08400  1.000 58.52000  ? 90  VAL B N   1 
ATOM   2478 C CA  . VAL C 1 108 ? -5.22500  27.13600 41.33600  1.000 53.77000  ? 90  VAL B CA  1 
ATOM   2479 C C   . VAL C 1 108 ? -6.47900  26.31100 41.08600  1.000 46.24000  ? 90  VAL B C   1 
ATOM   2480 O O   . VAL C 1 108 ? -7.42100  26.78900 40.44600  1.000 56.56000  ? 90  VAL B O   1 
ATOM   2481 C CB  . VAL C 1 108 ? -5.47300  28.17700 42.44400  1.000 60.21000  ? 90  VAL B CB  1 
ATOM   2482 C CG1 . VAL C 1 108 ? -5.67100  27.49000 43.78500  1.000 54.46000  ? 90  VAL B CG1 1 
ATOM   2483 C CG2 . VAL C 1 108 ? -4.32500  29.17500 42.50800  1.000 60.11000  ? 90  VAL B CG2 1 
ATOM   2484 N N   . PHE C 1 109 ? -6.48800  25.07700 41.58900  1.000 49.94000  ? 91  PHE B N   1 
ATOM   2485 C CA  . PHE C 1 109 ? -7.65400  24.20200 41.52300  1.000 44.44000  ? 91  PHE B CA  1 
ATOM   2486 C C   . PHE C 1 109 ? -7.97100  23.72000 42.93000  1.000 47.03000  ? 91  PHE B C   1 
ATOM   2487 O O   . PHE C 1 109 ? -7.10300  23.15400 43.60100  1.000 47.27000  ? 91  PHE B O   1 
ATOM   2488 C CB  . PHE C 1 109 ? -7.41000  23.00900 40.59400  1.000 50.15000  ? 91  PHE B CB  1 
ATOM   2489 C CG  . PHE C 1 109 ? -7.04400  23.39400 39.19000  1.000 54.37000  ? 91  PHE B CG  1 
ATOM   2490 C CD1 . PHE C 1 109 ? -8.02400  23.60200 38.23300  1.000 44.12000  ? 91  PHE B CD1 1 
ATOM   2491 C CD2 . PHE C 1 109 ? -5.71600  23.54400 38.82400  1.000 38.72000  ? 91  PHE B CD2 1 
ATOM   2492 C CE1 . PHE C 1 109 ? -7.68700  23.95500 36.93900  1.000 34.91000  ? 91  PHE B CE1 1 
ATOM   2493 C CE2 . PHE C 1 109 ? -5.37400  23.89700 37.53200  1.000 58.93000  ? 91  PHE B CE2 1 
ATOM   2494 C CZ  . PHE C 1 109 ? -6.36000  24.10200 36.58900  1.000 58.90000  ? 91  PHE B CZ  1 
ATOM   2495 N N   . GLY C 1 110 ? -9.20900  23.93400 43.37100  1.000 42.75000  ? 92  GLY B N   1 
ATOM   2496 C CA  . GLY C 1 110 ? -9.60600  23.56500 44.70800  1.000 40.96000  ? 92  GLY B CA  1 
ATOM   2497 C C   . GLY C 1 110 ? -11.05100 23.12000 44.80600  1.000 63.29000  ? 92  GLY B C   1 
ATOM   2498 O O   . GLY C 1 110 ? -11.74700 22.95900 43.79800  1.000 52.97000  ? 92  GLY B O   1 
ATOM   2499 N N   . PRO C 1 111 ? -11.54900 22.87600 46.03300  1.000 62.52000  ? 93  PRO B N   1 
ATOM   2500 C CA  . PRO C 1 111 ? -12.92800 22.45700 46.20200  1.000 72.00000  ? 93  PRO B CA  1 
ATOM   2501 C C   . PRO C 1 111 ? -13.95100 23.47700 45.67900  1.000 67.64000  ? 93  PRO B C   1 
ATOM   2502 O O   . PRO C 1 111 ? -15.03000 23.06500 45.35100  1.000 61.31000  ? 93  PRO B O   1 
ATOM   2503 C CB  . PRO C 1 111 ? -13.03800 22.29600 47.72300  1.000 66.06000  ? 93  PRO B CB  1 
ATOM   2504 C CG  . PRO C 1 111 ? -11.63800 22.02200 48.18500  1.000 63.52000  ? 93  PRO B CG  1 
ATOM   2505 C CD  . PRO C 1 111 ? -10.82900 22.94900 47.31500  1.000 62.62000  ? 93  PRO B CD  1 
ATOM   2506 N N   . GLU C 1 112 ? -13.57100 24.74600 45.60200  1.000 79.30000  ? 94  GLU B N   1 
ATOM   2507 C CA  . GLU C 1 112 ? -14.50800 25.81900 45.18800  1.000 77.66000  ? 94  GLU B CA  1 
ATOM   2508 C C   . GLU C 1 112 ? -14.40500 26.01800 43.67800  1.000 71.88000  ? 94  GLU B C   1 
ATOM   2509 O O   . GLU C 1 112 ? -15.31300 26.61100 43.09600  1.000 80.22000  ? 94  GLU B O   1 
ATOM   2510 C CB  . GLU C 1 112 ? -14.14000 27.10700 45.91700  1.000 78.32000  ? 94  GLU B CB  1 
ATOM   2511 N N   . GLY C 1 113 ? -13.33300 25.52700 43.08100  1.000 57.15000  ? 95  GLY B N   1 
ATOM   2512 C CA  . GLY C 1 113 ? -13.21700 25.62000 41.62800  1.000 71.11000  ? 95  GLY B CA  1 
ATOM   2513 C C   . GLY C 1 113 ? -11.84200 26.09000 41.23400  1.000 64.40000  ? 95  GLY B C   1 
ATOM   2514 O O   . GLY C 1 113 ? -10.93400 25.95900 42.04800  1.000 73.58000  ? 95  GLY B O   1 
ATOM   2515 N N   . CYS C 1 114 ? -11.71600 26.64200 40.03300  1.000 70.08000  ? 96  CYS B N   1 
ATOM   2516 C CA  . CYS C 1 114 ? -10.38000 27.03600 39.53700  1.000 63.58000  ? 96  CYS B CA  1 
ATOM   2517 C C   . CYS C 1 114 ? -10.17700 28.54500 39.65200  1.000 68.84000  ? 96  CYS B C   1 
ATOM   2518 O O   . CYS C 1 114 ? -11.16100 29.27800 39.74200  1.000 63.49000  ? 96  CYS B O   1 
ATOM   2519 C CB  . CYS C 1 114 ? -10.22600 26.60200 38.09300  1.000 68.17000  ? 96  CYS B CB  1 
ATOM   2520 S SG  . CYS C 1 114 ? -11.43200 27.35000 36.97500  1.000 100.11000 ? 96  CYS B SG  1 
ATOM   2521 N N   . GLU C 1 115 ? -8.92500  28.97300 39.63900  1.000 61.43000  ? 97  GLU B N   1 
ATOM   2522 C CA  . GLU C 1 115 ? -8.60300  30.38900 39.75900  1.000 49.67000  ? 97  GLU B CA  1 
ATOM   2523 C C   . GLU C 1 115 ? -7.32700  30.67800 38.98400  1.000 67.37000  ? 97  GLU B C   1 
ATOM   2524 O O   . GLU C 1 115 ? -6.32200  29.98400 39.16100  1.000 63.74000  ? 97  GLU B O   1 
ATOM   2525 C CB  . GLU C 1 115 ? -8.44300  30.79100 41.23000  1.000 43.88000  ? 97  GLU B CB  1 
ATOM   2526 C CG  . GLU C 1 115 ? -8.16800  32.27000 41.45600  1.000 73.51000  ? 97  GLU B CG  1 
ATOM   2527 C CD  . GLU C 1 115 ? -8.09400  32.62500 42.92900  1.000 82.34000  ? 97  GLU B CD  1 
ATOM   2528 O OE1 . GLU C 1 115 ? -8.39500  31.74900 43.76700  1.000 98.37000  ? 97  GLU B OE1 1 
ATOM   2529 O OE2 . GLU C 1 115 ? -7.73200  33.77700 43.25000  1.000 78.27000  ? 97  GLU B OE2 1 
ATOM   2530 N N   . GLU C 1 116 ? -7.38200  31.69800 38.12400  1.000 48.97000  ? 98  GLU B N   1 
ATOM   2531 C CA  . GLU C 1 116 ? -6.20500  32.08900 37.30800  1.000 65.49000  ? 98  GLU B CA  1 
ATOM   2532 C C   . GLU C 1 116 ? -5.67600  33.43000 37.82200  1.000 67.69000  ? 98  GLU B C   1 
ATOM   2533 O O   . GLU C 1 116 ? -6.45500  34.39600 37.83400  1.000 69.44000  ? 98  GLU B O   1 
ATOM   2534 C CB  . GLU C 1 116 ? -6.60200  32.19200 35.83700  1.000 63.19000  ? 98  GLU B CB  1 
ATOM   2535 C CG  . GLU C 1 116 ? -5.48500  32.67800 34.93300  1.000 76.77000  ? 98  GLU B CG  1 
ATOM   2536 C CD  . GLU C 1 116 ? -5.86300  32.72500 33.46300  1.000 76.66000  ? 98  GLU B CD  1 
ATOM   2537 O OE1 . GLU C 1 116 ? -7.00000  32.33800 33.13600  1.000 73.62000  ? 98  GLU B OE1 1 
ATOM   2538 O OE2 . GLU C 1 116 ? -5.02200  33.15300 32.65200  1.000 84.83000  ? 98  GLU B OE2 1 
ATOM   2539 N N   . ARG C 1 117 ? -4.41000  33.47500 38.23800  1.000 62.21000  ? 99  ARG B N   1 
ATOM   2540 C CA  . ARG C 1 117 ? -3.83000  34.71800 38.80700  1.000 70.05000  ? 99  ARG B CA  1 
ATOM   2541 C C   . ARG C 1 117 ? -2.67900  35.20000 37.91900  1.000 82.97000  ? 99  ARG B C   1 
ATOM   2542 O O   . ARG C 1 117 ? -1.60200  34.59100 37.98600  1.000 89.94000  ? 99  ARG B O   1 
ATOM   2543 C CB  . ARG C 1 117 ? -3.37300  34.44700 40.24300  1.000 75.46000  ? 99  ARG B CB  1 
ATOM   2544 C CG  . ARG C 1 117 ? -4.42800  33.76000 41.09800  1.000 81.80000  ? 99  ARG B CG  1 
ATOM   2545 C CD  . ARG C 1 117 ? -3.94200  33.34900 42.47400  1.000 83.48000  ? 99  ARG B CD  1 
ATOM   2546 N NE  . ARG C 1 117 ? -5.00100  32.70400 43.23800  1.000 113.22000 ? 99  ARG B NE  1 
ATOM   2547 C CZ  . ARG C 1 117 ? -4.86800  32.23500 44.47300  1.000 103.28000 ? 99  ARG B CZ  1 
ATOM   2548 N NH1 . ARG C 1 117 ? -3.73000  32.39700 45.12300  1.000 95.37000  ? 99  ARG B NH1 1 
ATOM   2549 N NH2 . ARG C 1 117 ? -5.87600  31.60900 45.05500  1.000 82.33000  ? 99  ARG B NH2 1 
ATOM   2550 N N   . ASP C 1 118 ? -2.90200  36.24900 37.12300  1.000 83.57000  ? 100 ASP B N   1 
ATOM   2551 C CA  . ASP C 1 118 ? -1.82600  36.83400 36.27400  1.000 83.44000  ? 100 ASP B CA  1 
ATOM   2552 C C   . ASP C 1 118 ? -1.25700  38.06700 36.98200  1.000 89.23000  ? 100 ASP B C   1 
ATOM   2553 O O   . ASP C 1 118 ? -1.81600  39.16000 36.78800  1.000 87.85000  ? 100 ASP B O   1 
ATOM   2554 C CB  . ASP C 1 118 ? -2.34600  37.17600 34.87600  1.000 88.36000  ? 100 ASP B CB  1 
ATOM   2555 C CG  . ASP C 1 118 ? -1.28600  37.70400 33.92400  1.000 90.58000  ? 100 ASP B CG  1 
ATOM   2556 O OD1 . ASP C 1 118 ? -0.11000  37.77600 34.32900  1.000 84.47000  ? 100 ASP B OD1 1 
ATOM   2557 O OD2 . ASP C 1 118 ? -1.64900  38.04000 32.78200  1.000 83.22000  ? 100 ASP B OD2 1 
ATOM   2558 N N   . LYS C 1 119 ? -0.18200  37.89800 37.75400  1.000 77.24000  ? 101 LYS B N   1 
ATOM   2559 C CA  . LYS C 1 119 ? 0.37500   39.02500 38.54800  1.000 80.61000  ? 101 LYS B CA  1 
ATOM   2560 C C   . LYS C 1 119 ? 1.13200   39.98900 37.63100  1.000 88.25000  ? 101 LYS B C   1 
ATOM   2561 O O   . LYS C 1 119 ? 1.25100   41.17100 37.99100  1.000 89.95000  ? 101 LYS B O   1 
ATOM   2562 C CB  . LYS C 1 119 ? 1.28500   38.49300 39.65800  1.000 78.43000  ? 101 LYS B CB  1 
ATOM   2563 C CG  . LYS C 1 119 ? 1.78700   39.53300 40.65100  1.000 79.16000  ? 101 LYS B CG  1 
ATOM   2564 N N   . ASN C 1 120 ? 1.63000   39.50500 36.49600  1.000 86.96000  ? 102 ASN B N   1 
ATOM   2565 C CA  . ASN C 1 120 ? 2.29800   40.42800 35.54400  1.000 90.49000  ? 102 ASN B CA  1 
ATOM   2566 C C   . ASN C 1 120 ? 1.28500   41.51100 35.17500  1.000 98.93000  ? 102 ASN B C   1 
ATOM   2567 O O   . ASN C 1 120 ? 1.71300   42.63700 34.87100  1.000 106.78000 ? 102 ASN B O   1 
ATOM   2568 C CB  . ASN C 1 120 ? 2.88300   39.68800 34.34100  1.000 77.44000  ? 102 ASN B CB  1 
ATOM   2569 C CG  . ASN C 1 120 ? 4.31200   39.24900 34.56900  1.000 78.08000  ? 102 ASN B CG  1 
ATOM   2570 O OD1 . ASN C 1 120 ? 4.84800   39.41100 35.66200  1.000 87.51000  ? 102 ASN B OD1 1 
ATOM   2571 N ND2 . ASN C 1 120 ? 4.93600   38.69200 33.54500  1.000 75.36000  ? 102 ASN B ND2 1 
ATOM   2572 N N   . ARG C 1 121 ? -0.00200  41.17600 35.18900  1.000 94.50000  ? 103 ARG B N   1 
ATOM   2573 C CA  . ARG C 1 121 ? -1.05300  42.19300 34.94400  1.000 90.83000  ? 103 ARG B CA  1 
ATOM   2574 C C   . ARG C 1 121 ? -1.78100  42.39000 36.27200  1.000 94.42000  ? 103 ARG B C   1 
ATOM   2575 O O   . ARG C 1 121 ? -1.16700  42.13900 37.31500  1.000 98.24000  ? 103 ARG B O   1 
ATOM   2576 C CB  . ARG C 1 121 ? -2.00200  41.73200 33.83700  1.000 90.47000  ? 103 ARG B CB  1 
ATOM   2577 C CG  . ARG C 1 121 ? -1.35200  41.63400 32.46500  1.000 79.05000  ? 103 ARG B CG  1 
ATOM   2578 C CD  . ARG C 1 121 ? -2.37500  41.40800 31.36900  1.000 83.00000  ? 103 ARG B CD  1 
ATOM   2579 N NE  . ARG C 1 121 ? -2.81100  40.02300 31.29900  1.000 87.95000  ? 103 ARG B NE  1 
ATOM   2580 C CZ  . ARG C 1 121 ? -3.99100  39.62800 30.83700  1.000 86.16000  ? 103 ARG B CZ  1 
ATOM   2581 N NH1 . ARG C 1 121 ? -4.80400  40.50000 30.26900  1.000 91.69000  ? 103 ARG B NH1 1 
ATOM   2582 N NH2 . ARG C 1 121 ? -4.35400  38.36200 30.94400  1.000 83.43000  ? 103 ARG B NH2 1 
ATOM   2583 N N   . GLY C 1 122 ? -3.03600  42.81700 36.24400  1.000 92.98000  ? 104 GLY B N   1 
ATOM   2584 C CA  . GLY C 1 122 ? -3.78000  42.91100 37.51300  1.000 98.61000  ? 104 GLY B CA  1 
ATOM   2585 C C   . GLY C 1 122 ? -5.07000  42.12400 37.43200  1.000 98.25000  ? 104 GLY B C   1 
ATOM   2586 O O   . GLY C 1 122 ? -6.06800  42.59500 37.99900  1.000 101.36000 ? 104 GLY B O   1 
ATOM   2587 N N   . ILE C 1 123 ? -5.05000  40.96700 36.76300  1.000 99.32000  ? 105 ILE B N   1 
ATOM   2588 C CA  . ILE C 1 123 ? -6.32100  40.22500 36.53100  1.000 84.48000  ? 105 ILE B CA  1 
ATOM   2589 C C   . ILE C 1 123 ? -6.34900  38.90100 37.29300  1.000 78.55000  ? 105 ILE B C   1 
ATOM   2590 O O   . ILE C 1 123 ? -5.41900  38.10000 37.11400  1.000 85.07000  ? 105 ILE B O   1 
ATOM   2591 C CB  . ILE C 1 123 ? -6.53700  40.00200 35.02500  1.000 90.28000  ? 105 ILE B CB  1 
ATOM   2592 C CG1 . ILE C 1 123 ? -6.21200  41.25800 34.21200  1.000 96.97000  ? 105 ILE B CG1 1 
ATOM   2593 C CG2 . ILE C 1 123 ? -7.94900  39.50800 34.75700  1.000 86.71000  ? 105 ILE B CG2 1 
ATOM   2594 N N   . ILE C 1 124 ? -7.38000  38.69700 38.11200  1.000 72.63000  ? 106 ILE B N   1 
ATOM   2595 C CA  . ILE C 1 124 ? -7.57500  37.38400 38.78900  1.000 79.80000  ? 106 ILE B CA  1 
ATOM   2596 C C   . ILE C 1 124 ? -8.92900  36.85500 38.31300  1.000 70.41000  ? 106 ILE B C   1 
ATOM   2597 O O   . ILE C 1 124 ? -9.93600  37.54300 38.53200  1.000 72.17000  ? 106 ILE B O   1 
ATOM   2598 C CB  . ILE C 1 124 ? -7.50000  37.50000 40.32100  1.000 61.31000  ? 106 ILE B CB  1 
ATOM   2599 C CG1 . ILE C 1 124 ? -6.08800  37.85500 40.79000  1.000 67.12000  ? 106 ILE B CG1 1 
ATOM   2600 C CG2 . ILE C 1 124 ? -8.00700  36.22700 40.97700  1.000 60.50000  ? 106 ILE B CG2 1 
ATOM   2601 C CD1 . ILE C 1 124 ? -5.68600  37.18400 42.08100  1.000 78.33000  ? 106 ILE B CD1 1 
ATOM   2602 N N   . LYS C 1 125 ? -8.93500  35.70300 37.64700  1.000 63.70000  ? 107 LYS B N   1 
ATOM   2603 C CA  . LYS C 1 125 ? -10.18300 35.09900 37.12700  1.000 59.28000  ? 107 LYS B CA  1 
ATOM   2604 C C   . LYS C 1 125 ? -10.54100 33.89500 37.99700  1.000 60.50000  ? 107 LYS B C   1 
ATOM   2605 O O   . LYS C 1 125 ? -9.69700  33.01500 38.14700  1.000 54.10000  ? 107 LYS B O   1 
ATOM   2606 C CB  . LYS C 1 125 ? -9.99900  34.71200 35.66200  1.000 62.42000  ? 107 LYS B CB  1 
ATOM   2607 C CG  . LYS C 1 125 ? -9.40400  35.78700 34.76600  1.000 76.98000  ? 107 LYS B CG  1 
ATOM   2608 C CD  . LYS C 1 125 ? -8.80100  35.22700 33.49700  1.000 83.09000  ? 107 LYS B CD  1 
ATOM   2609 C CE  . LYS C 1 125 ? -8.28800  36.29000 32.55000  1.000 84.87000  ? 107 LYS B CE  1 
ATOM   2610 N NZ  . LYS C 1 125 ? -9.39200  36.94300 31.80700  1.000 79.87000  ? 107 LYS B NZ  1 
ATOM   2611 N N   . THR C 1 126 ? -11.74400 33.89500 38.56200  1.000 58.21000  ? 108 THR B N   1 
ATOM   2612 C CA  . THR C 1 126 ? -12.20300 32.77800 39.42100  1.000 56.51000  ? 108 THR B CA  1 
ATOM   2613 C C   . THR C 1 126 ? -13.37400 32.04900 38.76700  1.000 69.13000  ? 108 THR B C   1 
ATOM   2614 O O   . THR C 1 126 ? -14.38400 32.69700 38.47000  1.000 53.25000  ? 108 THR B O   1 
ATOM   2615 C CB  . THR C 1 126 ? -12.61800 33.26700 40.80700  1.000 53.99000  ? 108 THR B CB  1 
ATOM   2616 O OG1 . THR C 1 126 ? -11.44900 33.76500 41.45200  1.000 71.50000  ? 108 THR B OG1 1 
ATOM   2617 C CG2 . THR C 1 126 ? -13.24200 32.17800 41.64700  1.000 55.31000  ? 108 THR B CG2 1 
ATOM   2618 N N   . PHE C 1 127 ? -13.24400 30.74000 38.56600  1.000 56.41000  ? 109 PHE B N   1 
ATOM   2619 C CA  . PHE C 1 127 ? -14.38700 29.97000 38.01700  1.000 72.27000  ? 109 PHE B CA  1 
ATOM   2620 C C   . PHE C 1 127 ? -14.88700 29.01100 39.09700  1.000 70.04000  ? 109 PHE B C   1 
ATOM   2621 O O   . PHE C 1 127 ? -14.13400 28.10200 39.47900  1.000 62.62000  ? 109 PHE B O   1 
ATOM   2622 C CB  . PHE C 1 127 ? -14.00100 29.28100 36.70700  1.000 70.65000  ? 109 PHE B CB  1 
ATOM   2623 C CG  . PHE C 1 127 ? -13.40200 30.19600 35.66900  1.000 93.30000  ? 109 PHE B CG  1 
ATOM   2624 N N   . SER C 1 128 ? -16.11800 29.22200 39.57100  1.000 77.39000  ? 110 SER B N   1 
ATOM   2625 C CA  . SER C 1 128 ? -16.66900 28.39000 40.67300  1.000 78.91000  ? 110 SER B CA  1 
ATOM   2626 C C   . SER C 1 128 ? -17.32400 27.12900 40.10700  1.000 89.07000  ? 110 SER B C   1 
ATOM   2627 O O   . SER C 1 128 ? -18.52500 27.17500 39.79300  1.000 81.96000  ? 110 SER B O   1 
ATOM   2628 C CB  . SER C 1 128 ? -17.63000 29.18200 41.51300  1.000 77.99000  ? 110 SER B CB  1 
ATOM   2629 O OG  . SER C 1 128 ? -16.98400 30.30900 42.08500  1.000 86.25000  ? 110 SER B OG  1 
ATOM   2630 N N   . THR C 1 129 ? -16.55100 26.04800 39.99400  1.000 84.66000  ? 111 THR B N   1 
ATOM   2631 C CA  . THR C 1 129 ? -17.08700 24.76500 39.47800  1.000 83.83000  ? 111 THR B CA  1 
ATOM   2632 C C   . THR C 1 129 ? -16.78500 23.66100 40.48900  1.000 94.51000  ? 111 THR B C   1 
ATOM   2633 O O   . THR C 1 129 ? -15.60700 23.28300 40.60800  1.000 98.77000  ? 111 THR B O   1 
ATOM   2634 C CB  . THR C 1 129 ? -16.47500 24.41600 38.11700  1.000 90.34000  ? 111 THR B CB  1 
ATOM   2635 O OG1 . THR C 1 129 ? -17.18300 23.29400 37.59000  1.000 96.46000  ? 111 THR B OG1 1 
ATOM   2636 C CG2 . THR C 1 129 ? -14.99900 24.09200 38.19700  1.000 77.11000  ? 111 THR B CG2 1 
ATOM   2637 N N   . ASP C 1 130 ? -17.80300 23.16900 41.19300  1.000 92.65000  ? 112 ASP B N   1 
ATOM   2638 C CA  . ASP C 1 130 ? -17.56200 22.02400 42.10500  1.000 80.81000  ? 112 ASP B CA  1 
ATOM   2639 C C   . ASP C 1 130 ? -17.00800 20.87900 41.25900  1.000 89.66000  ? 112 ASP B C   1 
ATOM   2640 O O   . ASP C 1 130 ? -17.77400 20.32200 40.45000  1.000 77.60000  ? 112 ASP B O   1 
ATOM   2641 C CB  . ASP C 1 130 ? -18.83200 21.62200 42.85600  1.000 98.29000  ? 112 ASP B CB  1 
ATOM   2642 N N   . VAL C 1 131 ? -15.72700 20.55400 41.43800  1.000 83.42000  ? 113 VAL B N   1 
ATOM   2643 C CA  . VAL C 1 131 ? -15.08700 19.50400 40.59200  1.000 75.86000  ? 113 VAL B CA  1 
ATOM   2644 C C   . VAL C 1 131 ? -14.77700 18.29700 41.48100  1.000 69.12000  ? 113 VAL B C   1 
ATOM   2645 O O   . VAL C 1 131 ? -14.10200 17.37100 41.00000  1.000 75.44000  ? 113 VAL B O   1 
ATOM   2646 C CB  . VAL C 1 131 ? -13.85100 20.07700 39.87400  1.000 74.49000  ? 113 VAL B CB  1 
ATOM   2647 C CG1 . VAL C 1 131 ? -12.94000 20.87700 40.78700  1.000 51.19000  ? 113 VAL B CG1 1 
ATOM   2648 C CG2 . VAL C 1 131 ? -13.09600 19.01500 39.09500  1.000 67.88000  ? 113 VAL B CG2 1 
ATOM   2649 N N   . LYS C 1 132 ? -15.27200 18.31300 42.72100  1.000 80.08000  ? 114 LYS B N   1 
ATOM   2650 C CA  . LYS C 1 132 ? -15.09500 17.17200 43.66300  1.000 77.79000  ? 114 LYS B CA  1 
ATOM   2651 C C   . LYS C 1 132 ? -13.64600 17.08900 44.15500  1.000 77.20000  ? 114 LYS B C   1 
ATOM   2652 O O   . LYS C 1 132 ? -13.18700 15.96900 44.43300  1.000 89.62000  ? 114 LYS B O   1 
ATOM   2653 C CB  . LYS C 1 132 ? -15.56800 15.85700 43.03100  1.000 73.36000  ? 114 LYS B CB  1 
ATOM   2654 C CG  . LYS C 1 132 ? -17.06800 15.75700 42.79200  1.000 72.20000  ? 114 LYS B CG  1 
ATOM   2655 C CD  . LYS C 1 132 ? -17.50000 14.41500 42.24800  1.000 73.23000  ? 114 LYS B CD  1 
ATOM   2656 C CE  . LYS C 1 132 ? -19.00100 14.30400 42.08500  1.000 89.84000  ? 114 LYS B CE  1 
ATOM   2657 N NZ  . LYS C 1 132 ? -19.70800 14.52100 43.36900  1.000 84.41000  ? 114 LYS B NZ  1 
ATOM   2658 N N   . LEU C 1 133 ? -12.96700 18.22600 44.29100  1.000 61.21000  ? 115 LEU B N   1 
ATOM   2659 C CA  . LEU C 1 133 ? -11.59500 18.19800 44.85600  1.000 69.71000  ? 115 LEU B CA  1 
ATOM   2660 C C   . LEU C 1 133 ? -11.67300 18.39000 46.37100  1.000 63.53000  ? 115 LEU B C   1 
ATOM   2661 O O   . LEU C 1 133 ? -12.51700 19.17900 46.81700  1.000 74.87000  ? 115 LEU B O   1 
ATOM   2662 C CB  . LEU C 1 133 ? -10.75800 19.30000 44.20400  1.000 61.47000  ? 115 LEU B CB  1 
ATOM   2663 C CG  . LEU C 1 133 ? -10.09000 18.93200 42.88200  1.000 59.22000  ? 115 LEU B CG  1 
ATOM   2664 C CD1 . LEU C 1 133 ? -9.15300  20.04000 42.43300  1.000 35.38000  ? 115 LEU B CD1 1 
ATOM   2665 C CD2 . LEU C 1 133 ? -9.33800  17.61700 43.00300  1.000 46.43000  ? 115 LEU B CD2 1 
ATOM   2666 N N   . ASP C 1 134 ? -10.83900 17.67500 47.12500  1.000 72.13000  ? 116 ASP B N   1 
ATOM   2667 C CA  . ASP C 1 134 ? -10.78800 17.84000 48.60000  1.000 79.01000  ? 116 ASP B CA  1 
ATOM   2668 C C   . ASP C 1 134 ? -9.44300  18.47900 48.94400  1.000 85.85000  ? 116 ASP B C   1 
ATOM   2669 O O   . ASP C 1 134 ? -9.19000  18.71400 50.13800  1.000 83.74000  ? 116 ASP B O   1 
ATOM   2670 C CB  . ASP C 1 134 ? -10.96800 16.49700 49.30500  1.000 94.46000  ? 116 ASP B CB  1 
ATOM   2671 C CG  . ASP C 1 134 ? -9.82600  15.53300 49.04200  1.000 96.48000  ? 116 ASP B CG  1 
ATOM   2672 O OD1 . ASP C 1 134 ? -9.56800  15.24200 47.85800  1.000 103.21000 ? 116 ASP B OD1 1 
ATOM   2673 O OD2 . ASP C 1 134 ? -9.20600  15.08000 50.02200  1.000 101.64000 ? 116 ASP B OD2 1 
ATOM   2674 N N   . GLU C 1 135 ? -8.61000  18.72200 47.93100  1.000 77.34000  ? 117 GLU B N   1 
ATOM   2675 C CA  . GLU C 1 135 ? -7.31200  19.34400 48.12900  1.000 65.79000  ? 117 GLU B CA  1 
ATOM   2676 C C   . GLU C 1 135 ? -7.14900  20.46800 47.11500  1.000 62.59000  ? 117 GLU B C   1 
ATOM   2677 O O   . GLU C 1 135 ? -7.96900  20.64000 46.20800  1.000 52.95000  ? 117 GLU B O   1 
ATOM   2678 C CB  . GLU C 1 135 ? -6.17900  18.31700 48.00000  1.000 62.60000  ? 117 GLU B CB  1 
ATOM   2679 C CG  . GLU C 1 135 ? -6.22700  17.21800 49.05200  1.000 71.22000  ? 117 GLU B CG  1 
ATOM   2680 C CD  . GLU C 1 135 ? -5.28700  16.06900 48.74600  1.000 80.04000  ? 117 GLU B CD  1 
ATOM   2681 O OE1 . GLU C 1 135 ? -4.85600  15.94600 47.58000  1.000 81.21000  ? 117 GLU B OE1 1 
ATOM   2682 O OE2 . GLU C 1 135 ? -4.98000  15.28900 49.67200  1.000 91.70000  ? 117 GLU B OE2 1 
ATOM   2683 N N   . THR C 1 136 ? -6.09300  21.25700 47.32500  1.000 61.83000  ? 118 THR B N   1 
ATOM   2684 C CA  . THR C 1 136 ? -5.85200  22.43000 46.44800  1.000 59.81000  ? 118 THR B CA  1 
ATOM   2685 C C   . THR C 1 136 ? -4.53300  22.24900 45.69400  1.000 50.15000  ? 118 THR B C   1 
ATOM   2686 O O   . THR C 1 136 ? -3.53300  21.89400 46.33600  1.000 58.37000  ? 118 THR B O   1 
ATOM   2687 C CB  . THR C 1 136 ? -5.92700  23.73700 47.25000  1.000 56.91000  ? 118 THR B CB  1 
ATOM   2688 O OG1 . THR C 1 136 ? -7.14000  23.72800 48.00300  1.000 73.75000  ? 118 THR B OG1 1 
ATOM   2689 C CG2 . THR C 1 136 ? -5.88600  24.96900 46.37600  1.000 60.61000  ? 118 THR B CG2 1 
ATOM   2690 N N   . TYR C 1 137 ? -4.54600  22.48300 44.38700  1.000 44.36000  ? 119 TYR B N   1 
ATOM   2691 C CA  . TYR C 1 137 ? -3.37900  22.35400 43.52700  1.000 56.86000  ? 119 TYR B CA  1 
ATOM   2692 C C   . TYR C 1 137 ? -2.96600  23.72400 43.00500  1.000 54.74000  ? 119 TYR B C   1 
ATOM   2693 O O   . TYR C 1 137 ? -3.81500  24.52600 42.60500  1.000 43.27000  ? 119 TYR B O   1 
ATOM   2694 C CB  . TYR C 1 137 ? -3.66400  21.41000 42.35300  1.000 45.33000  ? 119 TYR B CB  1 
ATOM   2695 C CG  . TYR C 1 137 ? -3.90400  19.96900 42.75400  1.000 46.04000  ? 119 TYR B CG  1 
ATOM   2696 C CD1 . TYR C 1 137 ? -5.13800  19.55900 43.24300  1.000 42.15000  ? 119 TYR B CD1 1 
ATOM   2697 C CD2 . TYR C 1 137 ? -2.90000  19.01800 42.63200  1.000 38.57000  ? 119 TYR B CD2 1 
ATOM   2698 C CE1 . TYR C 1 137 ? -5.36200  18.24300 43.60500  1.000 52.15000  ? 119 TYR B CE1 1 
ATOM   2699 C CE2 . TYR C 1 137 ? -3.11500  17.70100 42.99100  1.000 40.81000  ? 119 TYR B CE2 1 
ATOM   2700 C CZ  . TYR C 1 137 ? -4.34700  17.31900 43.47800  1.000 41.78000  ? 119 TYR B CZ  1 
ATOM   2701 O OH  . TYR C 1 137 ? -4.56300  16.01000 43.83700  1.000 50.66000  ? 119 TYR B OH  1 
ATOM   2702 N N   . PHE C 1 138 ? -1.65600  23.95600 43.01300  1.000 58.26000  ? 120 PHE B N   1 
ATOM   2703 C CA  . PHE C 1 138 ? -1.11300  25.25000 42.54800  1.000 64.38000  ? 120 PHE B CA  1 
ATOM   2704 C C   . PHE C 1 138 ? -0.10000  25.01000 41.42900  1.000 52.31000  ? 120 PHE B C   1 
ATOM   2705 O O   . PHE C 1 138 ? 0.88700   24.30500 41.66900  1.000 56.55000  ? 120 PHE B O   1 
ATOM   2706 C CB  . PHE C 1 138 ? -0.47600  25.99900 43.71900  1.000 72.14000  ? 120 PHE B CB  1 
ATOM   2707 C CG  . PHE C 1 138 ? -1.42900  26.46400 44.78900  1.000 69.80000  ? 120 PHE B CG  1 
ATOM   2708 C CD1 . PHE C 1 138 ? -1.82800  25.61200 45.80400  1.000 63.77000  ? 120 PHE B CD1 1 
ATOM   2709 C CD2 . PHE C 1 138 ? -1.90900  27.76300 44.79300  1.000 67.72000  ? 120 PHE B CD2 1 
ATOM   2710 C CE1 . PHE C 1 138 ? -2.69500  26.04600 46.79300  1.000 74.29000  ? 120 PHE B CE1 1 
ATOM   2711 C CE2 . PHE C 1 138 ? -2.77700  28.19500 45.78200  1.000 66.81000  ? 120 PHE B CE2 1 
ATOM   2712 C CZ  . PHE C 1 138 ? -3.16900  27.33600 46.78000  1.000 70.11000  ? 120 PHE B CZ  1 
ATOM   2713 N N   . PHE C 1 139 ? -0.36300  25.55300 40.24500  1.000 50.98000  ? 121 PHE B N   1 
ATOM   2714 C CA  . PHE C 1 139 ? 0.53700   25.46000 39.10200  1.000 51.13000  ? 121 PHE B CA  1 
ATOM   2715 C C   . PHE C 1 139 ? 1.17600   26.82200 38.86900  1.000 45.07000  ? 121 PHE B C   1 
ATOM   2716 O O   . PHE C 1 139 ? 0.46700   27.82600 38.74700  1.000 46.25000  ? 121 PHE B O   1 
ATOM   2717 C CB  . PHE C 1 139 ? -0.19900  25.01800 37.83100  1.000 58.62000  ? 121 PHE B CB  1 
ATOM   2718 C CG  . PHE C 1 139 ? -0.89200  23.68400 37.94000  1.000 58.05000  ? 121 PHE B CG  1 
ATOM   2719 C CD1 . PHE C 1 139 ? -0.60400  22.80200 38.96900  1.000 62.50000  ? 121 PHE B CD1 1 
ATOM   2720 C CD2 . PHE C 1 139 ? -1.83100  23.31000 36.99100  1.000 79.04000  ? 121 PHE B CD2 1 
ATOM   2721 C CE1 . PHE C 1 139 ? -1.24800  21.58200 39.05600  1.000 70.11000  ? 121 PHE B CE1 1 
ATOM   2722 C CE2 . PHE C 1 139 ? -2.47400  22.08900 37.07000  1.000 87.03000  ? 121 PHE B CE2 1 
ATOM   2723 C CZ  . PHE C 1 139 ? -2.18200  21.22500 38.10400  1.000 50.34000  ? 121 PHE B CZ  1 
ATOM   2724 N N   . PHE C 1 140 ? 2.50500   26.85700 38.80500  1.000 43.94000  ? 122 PHE B N   1 
ATOM   2725 C CA  . PHE C 1 140 ? 3.20000   28.09700 38.49000  1.000 59.47000  ? 122 PHE B CA  1 
ATOM   2726 C C   . PHE C 1 140 ? 4.60500   27.77700 38.00500  1.000 53.38000  ? 122 PHE B C   1 
ATOM   2727 O O   . PHE C 1 140 ? 5.25100   26.85700 38.51400  1.000 54.22000  ? 122 PHE B O   1 
ATOM   2728 C CB  . PHE C 1 140 ? 3.25200   29.04500 39.69800  1.000 58.78000  ? 122 PHE B CB  1 
ATOM   2729 C CG  . PHE C 1 140 ? 3.93300   28.46500 40.90700  1.000 68.12000  ? 122 PHE B CG  1 
ATOM   2730 C CD1 . PHE C 1 140 ? 3.20900   27.75600 41.85200  1.000 62.06000  ? 122 PHE B CD1 1 
ATOM   2731 C CD2 . PHE C 1 140 ? 5.29200   28.64900 41.11200  1.000 67.35000  ? 122 PHE B CD2 1 
ATOM   2732 C CE1 . PHE C 1 140 ? 3.82900   27.22900 42.97000  1.000 52.64000  ? 122 PHE B CE1 1 
ATOM   2733 C CE2 . PHE C 1 140 ? 5.91800   28.12300 42.22800  1.000 67.66000  ? 122 PHE B CE2 1 
ATOM   2734 C CZ  . PHE C 1 140 ? 5.18400   27.41400 43.15800  1.000 65.69000  ? 122 PHE B CZ  1 
ATOM   2735 N N   . ARG C 1 141 ? 5.10100   28.57600 37.06300  1.000 55.73000  ? 123 ARG B N   1 
ATOM   2736 C CA  . ARG C 1 141 ? 6.49000   28.39900 36.57000  1.000 71.07000  ? 123 ARG B CA  1 
ATOM   2737 C C   . ARG C 1 141 ? 7.45100   29.05000 37.56900  1.000 67.16000  ? 123 ARG B C   1 
ATOM   2738 O O   . ARG C 1 141 ? 7.06800   30.07300 38.16700  1.000 75.50000  ? 123 ARG B O   1 
ATOM   2739 C CB  . ARG C 1 141 ? 6.62900   29.03200 35.18500  1.000 68.54000  ? 123 ARG B CB  1 
ATOM   2740 C CG  . ARG C 1 141 ? 8.01500   28.90300 34.57200  1.000 79.61000  ? 123 ARG B CG  1 
ATOM   2741 C CD  . ARG C 1 141 ? 8.19200   29.86000 33.41200  1.000 83.79000  ? 123 ARG B CD  1 
ATOM   2742 N NE  . ARG C 1 141 ? 9.47100   29.66100 32.75100  1.000 86.26000  ? 123 ARG B NE  1 
ATOM   2743 C CZ  . ARG C 1 141 ? 9.60400   29.31800 31.47600  1.000 89.74000  ? 123 ARG B CZ  1 
ATOM   2744 N NH1 . ARG C 1 141 ? 8.55100   29.32700 30.67900  1.000 85.46000  ? 123 ARG B NH1 1 
ATOM   2745 N NH2 . ARG C 1 141 ? 10.78900  28.96900 31.00500  1.000 95.28000  ? 123 ARG B NH2 1 
ATOM   2746 N N   . VAL C 1 142 ? 8.64500   28.47700 37.74800  1.000 64.32000  ? 124 VAL B N   1 
ATOM   2747 C CA  . VAL C 1 142 ? 9.62300   29.01500 38.74200  1.000 78.41000  ? 124 VAL B CA  1 
ATOM   2748 C C   . VAL C 1 142 ? 10.79900  29.66000 37.99900  1.000 87.34000  ? 124 VAL B C   1 
ATOM   2749 O O   . VAL C 1 142 ? 10.86600  29.47700 36.76900  1.000 89.74000  ? 124 VAL B O   1 
ATOM   2750 C CB  . VAL C 1 142 ? 10.10400  27.91800 39.70900  1.000 85.49000  ? 124 VAL B CB  1 
ATOM   2751 C CG1 . VAL C 1 142 ? 10.87600  26.82800 38.98200  1.000 80.03000  ? 124 VAL B CG1 1 
ATOM   2752 C CG2 . VAL C 1 142 ? 10.93400  28.49600 40.84400  1.000 86.25000  ? 124 VAL B CG2 1 
ATOM   2753 N N   . SER D 1 18  ? 9.28400   50.28800 28.33800  1.000 68.41000  ? 0   SER C N   1 
ATOM   2754 C CA  . SER D 1 18  ? 10.54600  50.96500 28.61300  1.000 92.59000  ? 0   SER C CA  1 
ATOM   2755 C C   . SER D 1 18  ? 11.33500  50.23400 29.69300  1.000 78.59000  ? 0   SER C C   1 
ATOM   2756 O O   . SER D 1 18  ? 10.92300  50.19500 30.85300  1.000 81.30000  ? 0   SER C O   1 
ATOM   2757 C CB  . SER D 1 18  ? 10.29800  52.41500 29.03400  1.000 78.97000  ? 0   SER C CB  1 
ATOM   2758 O OG  . SER D 1 18  ? 9.60600   53.13000 28.02500  1.000 84.47000  ? 0   SER C OG  1 
ATOM   2759 N N   . MET D 1 19  ? 12.48300  49.67800 29.28800  1.000 80.78000  ? 1   MET C N   1 
ATOM   2760 C CA  . MET D 1 19  ? 13.37800  48.94000 30.21700  1.000 87.60000  ? 1   MET C CA  1 
ATOM   2761 C C   . MET D 1 19  ? 14.01400  49.92500 31.19900  1.000 80.18000  ? 1   MET C C   1 
ATOM   2762 O O   . MET D 1 19  ? 14.72700  50.83900 30.74500  1.000 74.53000  ? 1   MET C O   1 
ATOM   2763 C CB  . MET D 1 19  ? 14.48000  48.23000 29.42700  1.000 77.52000  ? 1   MET C CB  1 
ATOM   2764 C CG  . MET D 1 19  ? 13.98600  47.07300 28.60100  1.000 87.07000  ? 1   MET C CG  1 
ATOM   2765 S SD  . MET D 1 19  ? 15.32300  45.90600 28.30000  1.000 106.26000 ? 1   MET C SD  1 
ATOM   2766 N N   . LYS D 1 20  ? 13.76400  49.73900 32.48700  1.000 52.31000  ? 2   LYS C N   1 
ATOM   2767 C CA  . LYS D 1 20  ? 14.26100  50.70300 33.49100  1.000 69.46000  ? 2   LYS C CA  1 
ATOM   2768 C C   . LYS D 1 20  ? 15.20500  49.96800 34.44200  1.000 58.52000  ? 2   LYS C C   1 
ATOM   2769 O O   . LYS D 1 20  ? 14.98700  48.78300 34.69800  1.000 55.46000  ? 2   LYS C O   1 
ATOM   2770 C CB  . LYS D 1 20  ? 13.08500  51.42800 34.15300  1.000 48.64000  ? 2   LYS C CB  1 
ATOM   2771 C CG  . LYS D 1 20  ? 12.36400  52.42500 33.26300  1.000 49.61000  ? 2   LYS C CG  1 
ATOM   2772 C CD  . LYS D 1 20  ? 11.66900  53.51500 34.03600  1.000 64.70000  ? 2   LYS C CD  1 
ATOM   2773 C CE  . LYS D 1 20  ? 10.59000  52.99200 34.95700  1.000 77.58000  ? 2   LYS C CE  1 
ATOM   2774 N NZ  . LYS D 1 20  ? 9.91700   54.09300 35.68400  1.000 80.98000  ? 2   LYS C NZ  1 
ATOM   2775 N N   . LEU D 1 21  ? 16.23000  50.66700 34.91000  1.000 53.39000  ? 3   LEU C N   1 
ATOM   2776 C CA  . LEU D 1 21  ? 17.25400  50.02400 35.75500  1.000 50.14000  ? 3   LEU C CA  1 
ATOM   2777 C C   . LEU D 1 21  ? 17.19000  50.59600 37.15900  1.000 45.38000  ? 3   LEU C C   1 
ATOM   2778 O O   . LEU D 1 21  ? 16.75400  51.73200 37.32100  1.000 47.51000  ? 3   LEU C O   1 
ATOM   2779 C CB  . LEU D 1 21  ? 18.62700  50.31500 35.15400  1.000 62.54000  ? 3   LEU C CB  1 
ATOM   2780 C CG  . LEU D 1 21  ? 19.12900  49.32900 34.10700  1.000 73.57000  ? 3   LEU C CG  1 
ATOM   2781 C CD1 . LEU D 1 21  ? 20.55400  49.67000 33.70700  1.000 75.75000  ? 3   LEU C CD1 1 
ATOM   2782 C CD2 . LEU D 1 21  ? 19.05800  47.91300 34.64200  1.000 60.00000  ? 3   LEU C CD2 1 
ATOM   2783 N N   . VAL D 1 22  ? 17.65700  49.81300 38.11100  1.000 45.91000  ? 4   VAL C N   1 
ATOM   2784 C CA  . VAL D 1 22  ? 17.71100  50.29200 39.51100  1.000 53.51000  ? 4   VAL C CA  1 
ATOM   2785 C C   . VAL D 1 22  ? 19.14400  50.70500 39.82100  1.000 45.98000  ? 4   VAL C C   1 
ATOM   2786 O O   . VAL D 1 22  ? 20.03600  49.90100 39.60800  1.000 43.92000  ? 4   VAL C O   1 
ATOM   2787 C CB  . VAL D 1 22  ? 17.21500  49.22200 40.49500  1.000 65.02000  ? 4   VAL C CB  1 
ATOM   2788 C CG1 . VAL D 1 22  ? 17.34200  49.69900 41.93200  1.000 60.09000  ? 4   VAL C CG1 1 
ATOM   2789 C CG2 . VAL D 1 22  ? 15.78900  48.79600 40.19400  1.000 51.47000  ? 4   VAL C CG2 1 
ATOM   2790 N N   . ILE D 1 23  ? 19.31700  51.93900 40.26700  1.000 47.66000  ? 5   ILE C N   1 
ATOM   2791 C CA  . ILE D 1 23  ? 20.65600  52.41000 40.69800  1.000 48.94000  ? 5   ILE C CA  1 
ATOM   2792 C C   . ILE D 1 23  ? 20.62000  52.56400 42.22200  1.000 48.54000  ? 5   ILE C C   1 
ATOM   2793 O O   . ILE D 1 23  ? 19.81800  53.35700 42.70600  1.000 52.05000  ? 5   ILE C O   1 
ATOM   2794 C CB  . ILE D 1 23  ? 21.07700  53.69700 39.96400  1.000 51.17000  ? 5   ILE C CB  1 
ATOM   2795 C CG1 . ILE D 1 23  ? 20.81600  53.61000 38.46000  1.000 60.27000  ? 5   ILE C CG1 1 
ATOM   2796 C CG2 . ILE D 1 23  ? 22.52300  54.04000 40.27100  1.000 45.85000  ? 5   ILE C CG2 1 
ATOM   2797 C CD1 . ILE D 1 23  ? 21.67100  52.59300 37.74700  1.000 70.23000  ? 5   ILE C CD1 1 
ATOM   2798 N N   . ALA D 1 24  ? 21.45200  51.81900 42.93400  1.000 47.08000  ? 6   ALA C N   1 
ATOM   2799 C CA  . ALA D 1 24  ? 21.55400  51.83800 44.39000  1.000 48.42000  ? 6   ALA C CA  1 
ATOM   2800 C C   . ALA D 1 24  ? 22.88700  52.46300 44.78000  1.000 58.64000  ? 6   ALA C C   1 
ATOM   2801 O O   . ALA D 1 24  ? 23.94800  51.87000 44.55600  1.000 47.89000  ? 6   ALA C O   1 
ATOM   2802 C CB  . ALA D 1 24  ? 21.41600  50.43000 44.96500  1.000 47.10000  ? 6   ALA C CB  1 
ATOM   2803 N N   . ARG D 1 25  ? 22.83100  53.65700 45.36600  1.000 41.48000  ? 7   ARG C N   1 
ATOM   2804 C CA  . ARG D 1 25  ? 24.01900  54.37700 45.82100  1.000 49.60000  ? 7   ARG C CA  1 
ATOM   2805 C C   . ARG D 1 25  ? 24.17000  54.13100 47.31900  1.000 49.21000  ? 7   ARG C C   1 
ATOM   2806 O O   . ARG D 1 25  ? 23.50900  54.77700 48.13600  1.000 50.72000  ? 7   ARG C O   1 
ATOM   2807 C CB  . ARG D 1 25  ? 23.90600  55.86400 45.50400  1.000 44.79000  ? 7   ARG C CB  1 
ATOM   2808 C CG  . ARG D 1 25  ? 25.06300  56.70500 46.02100  1.000 46.23000  ? 7   ARG C CG  1 
ATOM   2809 C CD  . ARG D 1 25  ? 24.86500  58.17300 45.68200  1.000 53.09000  ? 7   ARG C CD  1 
ATOM   2810 N NE  . ARG D 1 25  ? 25.96400  59.00300 46.16200  1.000 73.39000  ? 7   ARG C NE  1 
ATOM   2811 C CZ  . ARG D 1 25  ? 26.06800  60.30700 45.94400  1.000 65.23000  ? 7   ARG C CZ  1 
ATOM   2812 N NH1 . ARG D 1 25  ? 25.15300  60.96700 45.25200  1.000 63.09000  ? 7   ARG C NH1 1 
ATOM   2813 N NH2 . ARG D 1 25  ? 27.11700  60.96500 46.43100  1.000 64.39000  ? 7   ARG C NH2 1 
ATOM   2814 N N   . VAL D 1 26  ? 25.04300  53.19400 47.67600  1.000 50.29000  ? 8   VAL C N   1 
ATOM   2815 C CA  . VAL D 1 26  ? 25.26700  52.82600 49.06900  1.000 61.21000  ? 8   VAL C CA  1 
ATOM   2816 C C   . VAL D 1 26  ? 26.32700  53.76200 49.63900  1.000 65.43000  ? 8   VAL C C   1 
ATOM   2817 O O   . VAL D 1 26  ? 27.48700  53.73200 49.22000  1.000 55.10000  ? 8   VAL C O   1 
ATOM   2818 C CB  . VAL D 1 26  ? 25.68700  51.35700 49.19900  1.000 61.85000  ? 8   VAL C CB  1 
ATOM   2819 C CG1 . VAL D 1 26  ? 25.97800  51.01400 50.65000  1.000 59.77000  ? 8   VAL C CG1 1 
ATOM   2820 C CG2 . VAL D 1 26  ? 24.60300  50.45000 48.63900  1.000 49.47000  ? 8   VAL C CG2 1 
ATOM   2821 N N   . LYS D 1 27  ? 25.92900  54.59300 50.60500  1.000 65.34000  ? 9   LYS C N   1 
ATOM   2822 C CA  . LYS D 1 27  ? 26.82000  55.59100 51.19900  1.000 64.71000  ? 9   LYS C CA  1 
ATOM   2823 C C   . LYS D 1 27  ? 27.75000  54.94300 52.22900  1.000 63.92000  ? 9   LYS C C   1 
ATOM   2824 O O   . LYS D 1 27  ? 27.75700  55.28200 53.41300  1.000 71.09000  ? 9   LYS C O   1 
ATOM   2825 C CB  . LYS D 1 27  ? 26.00200  56.71300 51.82500  1.000 53.85000  ? 9   LYS C CB  1 
ATOM   2826 C CG  . LYS D 1 27  ? 24.86100  57.22400 50.95700  1.000 69.42000  ? 9   LYS C CG  1 
ATOM   2827 C CD  . LYS D 1 27  ? 25.13800  58.61100 50.40500  1.000 64.70000  ? 9   LYS C CD  1 
ATOM   2828 C CE  . LYS D 1 27  ? 23.93900  59.13700 49.63200  1.000 71.04000  ? 9   LYS C CE  1 
ATOM   2829 N NZ  . LYS D 1 27  ? 24.15500  60.52300 49.13000  1.000 93.49000  ? 9   LYS C NZ  1 
ATOM   2830 N N   . SER D 1 28  ? 28.55500  53.98900 51.74900  1.000 71.07000  ? 10  SER C N   1 
ATOM   2831 C CA  . SER D 1 28  ? 29.49400  53.27700 52.60300  1.000 71.08000  ? 10  SER C CA  1 
ATOM   2832 C C   . SER D 1 28  ? 30.55600  52.62400 51.73700  1.000 78.67000  ? 10  SER C C   1 
ATOM   2833 O O   . SER D 1 28  ? 30.22000  52.12800 50.64900  1.000 68.41000  ? 10  SER C O   1 
ATOM   2834 C CB  . SER D 1 28  ? 28.78700  52.21700 53.45500  1.000 70.26000  ? 10  SER C CB  1 
ATOM   2835 O OG  . SER D 1 28  ? 29.72100  51.45300 54.19900  1.000 74.60000  ? 10  SER C OG  1 
ATOM   2836 N N   . PRO D 1 29  ? 31.81700  52.59900 52.16100  1.000 76.14000  ? 11  PRO C N   1 
ATOM   2837 C CA  . PRO D 1 29  ? 32.86100  51.93700 51.37000  1.000 69.09000  ? 11  PRO C CA  1 
ATOM   2838 C C   . PRO D 1 29  ? 33.02600  50.44900 51.63600  1.000 79.39000  ? 11  PRO C C   1 
ATOM   2839 O O   . PRO D 1 29  ? 33.72500  49.78100 50.86100  1.000 83.67000  ? 11  PRO C O   1 
ATOM   2840 C CB  . PRO D 1 29  ? 34.12600  52.70000 51.78600  1.000 78.69000  ? 11  PRO C CB  1 
ATOM   2841 C CG  . PRO D 1 29  ? 33.86800  53.06000 53.20700  1.000 71.68000  ? 11  PRO C CG  1 
ATOM   2842 C CD  . PRO D 1 29  ? 32.38100  53.32000 53.31900  1.000 73.27000  ? 11  PRO C CD  1 
ATOM   2843 N N   . LYS D 1 30  ? 32.41300  49.90900 52.69100  1.000 91.31000  ? 12  LYS C N   1 
ATOM   2844 C CA  . LYS D 1 30  ? 32.60900  48.50800 53.05000  1.000 89.89000  ? 12  LYS C CA  1 
ATOM   2845 C C   . LYS D 1 30  ? 31.56400  47.58600 52.43400  1.000 92.28000  ? 12  LYS C C   1 
ATOM   2846 O O   . LYS D 1 30  ? 31.89100  46.45800 52.04700  1.000 95.72000  ? 12  LYS C O   1 
ATOM   2847 C CB  . LYS D 1 30  ? 32.60300  48.34100 54.57300  1.000 89.28000  ? 12  LYS C CB  1 
ATOM   2848 N N   . VAL D 1 31  ? 30.31100  48.03600 52.34400  1.000 89.93000  ? 13  VAL C N   1 
ATOM   2849 C CA  . VAL D 1 31  ? 29.24100  47.18500 51.83200  1.000 90.88000  ? 13  VAL C CA  1 
ATOM   2850 C C   . VAL D 1 31  ? 29.52200  46.84400 50.37600  1.000 89.55000  ? 13  VAL C C   1 
ATOM   2851 O O   . VAL D 1 31  ? 29.56300  47.72800 49.51100  1.000 102.95000 ? 13  VAL C O   1 
ATOM   2852 C CB  . VAL D 1 31  ? 27.88200  47.87100 51.99200  1.000 92.92000  ? 13  VAL C CB  1 
ATOM   2853 C CG1 . VAL D 1 31  ? 26.79200  47.04900 51.32000  1.000 84.57000  ? 13  VAL C CG1 1 
ATOM   2854 C CG2 . VAL D 1 31  ? 27.56700  48.07900 53.46100  1.000 83.76000  ? 13  VAL C CG2 1 
ATOM   2855 N N   . LYS D 1 32  ? 29.71400  45.55500 50.09800  1.000 90.89000  ? 14  LYS C N   1 
ATOM   2856 C CA  . LYS D 1 32  ? 29.98400  45.08100 48.74700  1.000 92.72000  ? 14  LYS C CA  1 
ATOM   2857 C C   . LYS D 1 32  ? 28.89700  44.14300 48.23500  1.000 89.97000  ? 14  LYS C C   1 
ATOM   2858 O O   . LYS D 1 32  ? 29.02900  43.59800 47.13200  1.000 97.32000  ? 14  LYS C O   1 
ATOM   2859 C CB  . LYS D 1 32  ? 31.35100  44.39000 48.69100  1.000 102.80000 ? 14  LYS C CB  1 
ATOM   2860 N N   . ARG D 1 33  ? 27.82700  43.94200 49.00000  1.000 80.36000  ? 15  ARG C N   1 
ATOM   2861 C CA  . ARG D 1 33  ? 26.75300  43.05700 48.57400  1.000 85.14000  ? 15  ARG C CA  1 
ATOM   2862 C C   . ARG D 1 33  ? 25.46600  43.46500 49.27400  1.000 76.07000  ? 15  ARG C C   1 
ATOM   2863 O O   . ARG D 1 33  ? 25.48600  43.94200 50.41200  1.000 92.27000  ? 15  ARG C O   1 
ATOM   2864 C CB  . ARG D 1 33  ? 27.08400  41.59100 48.87100  1.000 81.93000  ? 15  ARG C CB  1 
ATOM   2865 N N   . LEU D 1 34  ? 24.35000  43.27500 48.57600  1.000 80.93000  ? 16  LEU C N   1 
ATOM   2866 C CA  . LEU D 1 34  ? 23.02200  43.55900 49.10200  1.000 81.04000  ? 16  LEU C CA  1 
ATOM   2867 C C   . LEU D 1 34  ? 22.29000  42.24800 49.34800  1.000 89.10000  ? 16  LEU C C   1 
ATOM   2868 O O   . LEU D 1 34  ? 22.21700  41.39700 48.45400  1.000 84.19000  ? 16  LEU C O   1 
ATOM   2869 C CB  . LEU D 1 34  ? 22.22100  44.43200 48.13200  1.000 82.00000  ? 16  LEU C CB  1 
ATOM   2870 C CG  . LEU D 1 34  ? 22.78800  45.81000 47.79200  1.000 80.36000  ? 16  LEU C CG  1 
ATOM   2871 C CD1 . LEU D 1 34  ? 21.96400  46.46500 46.69400  1.000 68.25000  ? 16  LEU C CD1 1 
ATOM   2872 C CD2 . LEU D 1 34  ? 22.82700  46.68900 49.03000  1.000 71.61000  ? 16  LEU C CD2 1 
ATOM   2873 N N   . SER D 1 35  ? 21.75200  42.08500 50.55300  1.000 84.17000  ? 17  SER C N   1 
ATOM   2874 C CA  . SER D 1 35  ? 20.98200  40.89100 50.85800  1.000 91.14000  ? 17  SER C CA  1 
ATOM   2875 C C   . SER D 1 35  ? 19.64500  40.92200 50.12200  1.000 98.07000  ? 17  SER C C   1 
ATOM   2876 O O   . SER D 1 35  ? 19.19100  41.96600 49.64500  1.000 97.18000  ? 17  SER C O   1 
ATOM   2877 C CB  . SER D 1 35  ? 20.74900  40.76600 52.36400  1.000 89.44000  ? 17  SER C CB  1 
ATOM   2878 O OG  . SER D 1 35  ? 19.81600  41.73000 52.81800  1.000 92.65000  ? 17  SER C OG  1 
ATOM   2879 N N   . GLU D 1 36  ? 19.01000  39.75500 50.05600  1.000 100.89000 ? 18  GLU C N   1 
ATOM   2880 C CA  . GLU D 1 36  ? 17.68200  39.63900 49.41300  1.000 90.40000  ? 18  GLU C CA  1 
ATOM   2881 C C   . GLU D 1 36  ? 16.70600  40.55100 50.14300  1.000 88.79000  ? 18  GLU C C   1 
ATOM   2882 O O   . GLU D 1 36  ? 15.84000  41.13700 49.48700  1.000 76.31000  ? 18  GLU C O   1 
ATOM   2883 C CB  . GLU D 1 36  ? 17.22700  38.18700 49.53900  1.000 105.87000 ? 18  GLU C CB  1 
ATOM   2884 N N   . GLU D 1 37  ? 16.84100  40.62500 51.46500  1.000 95.45000  ? 19  GLU C N   1 
ATOM   2885 C CA  . GLU D 1 37  ? 15.96200  41.49700 52.23600  1.000 91.02000  ? 19  GLU C CA  1 
ATOM   2886 C C   . GLU D 1 37  ? 16.18000  42.95800 51.86200  1.000 90.38000  ? 19  GLU C C   1 
ATOM   2887 O O   . GLU D 1 37  ? 15.21900  43.73100 51.76300  1.000 83.93000  ? 19  GLU C O   1 
ATOM   2888 C CB  . GLU D 1 37  ? 16.19300  41.28200 53.73100  1.000 90.12000  ? 19  GLU C CB  1 
ATOM   2889 N N   . ASP D 1 38  ? 17.43200  43.31300 51.60000  1.000 95.84000  ? 20  ASP C N   1 
ATOM   2890 C CA  . ASP D 1 38  ? 17.73800  44.70700 51.19500  1.000 90.30000  ? 20  ASP C CA  1 
ATOM   2891 C C   . ASP D 1 38  ? 17.14000  44.93900 49.81200  1.000 80.47000  ? 20  ASP C C   1 
ATOM   2892 O O   . ASP D 1 38  ? 16.46300  45.94800 49.61500  1.000 78.66000  ? 20  ASP C O   1 
ATOM   2893 C CB  . ASP D 1 38  ? 19.24200  44.96900 51.21700  1.000 88.38000  ? 20  ASP C CB  1 
ATOM   2894 C CG  . ASP D 1 38  ? 19.89300  44.69300 52.55900  1.000 97.29000  ? 20  ASP C CG  1 
ATOM   2895 O OD1 . ASP D 1 38  ? 19.33100  45.12500 53.58200  1.000 93.46000  ? 20  ASP C OD1 1 
ATOM   2896 O OD2 . ASP D 1 38  ? 20.97300  44.07200 52.56600  1.000 102.59000 ? 20  ASP C OD2 1 
ATOM   2897 N N   . ILE D 1 39  ? 17.36600  43.99800 48.91300  1.000 70.69000  ? 21  ILE C N   1 
ATOM   2898 C CA  . ILE D 1 39  ? 16.85700  44.14400 47.55300  1.000 75.20000  ? 21  ILE C CA  1 
ATOM   2899 C C   . ILE D 1 39  ? 15.33800  44.25700 47.56400  1.000 81.93000  ? 21  ILE C C   1 
ATOM   2900 O O   . ILE D 1 39  ? 14.75200  45.04300 46.81000  1.000 80.08000  ? 21  ILE C O   1 
ATOM   2901 C CB  . ILE D 1 39  ? 17.33600  42.97200 46.67500  1.000 73.92000  ? 21  ILE C CB  1 
ATOM   2902 C CG1 . ILE D 1 39  ? 18.85400  43.02700 46.49400  1.000 69.34000  ? 21  ILE C CG1 1 
ATOM   2903 C CG2 . ILE D 1 39  ? 16.63500  42.98600 45.32400  1.000 79.64000  ? 21  ILE C CG2 1 
ATOM   2904 C CD1 . ILE D 1 39  ? 19.40600  41.92200 45.62000  1.000 70.80000  ? 21  ILE C CD1 1 
ATOM   2905 N N   . GLU D 1 40  ? 14.67600  43.48200 48.42800  1.000 82.80000  ? 22  GLU C N   1 
ATOM   2906 C CA  . GLU D 1 40  ? 13.22400  43.57100 48.52600  1.000 76.38000  ? 22  GLU C CA  1 
ATOM   2907 C C   . GLU D 1 40  ? 12.78700  44.90100 49.12300  1.000 78.19000  ? 22  GLU C C   1 
ATOM   2908 O O   . GLU D 1 40  ? 11.72000  45.41800 48.76900  1.000 83.49000  ? 22  GLU C O   1 
ATOM   2909 C CB  . GLU D 1 40  ? 12.68000  42.40700 49.35400  1.000 83.89000  ? 22  GLU C CB  1 
ATOM   2910 C CG  . GLU D 1 40  ? 11.32800  41.90200 48.88300  1.000 88.40000  ? 22  GLU C CG  1 
ATOM   2911 C CD  . GLU D 1 40  ? 11.38400  41.32300 47.48200  1.000 95.73000  ? 22  GLU C CD  1 
ATOM   2912 O OE1 . GLU D 1 40  ? 12.41600  40.71300 47.13000  1.000 97.80000  ? 22  GLU C OE1 1 
ATOM   2913 O OE2 . GLU D 1 40  ? 10.40000  41.48400 46.73000  1.000 94.83000  ? 22  GLU C OE2 1 
ATOM   2914 N N   . LYS D 1 41  ? 13.59100  45.46700 50.02600  1.000 75.40000  ? 23  LYS C N   1 
ATOM   2915 C CA  . LYS D 1 41  ? 13.30500  46.80400 50.53600  1.000 81.88000  ? 23  LYS C CA  1 
ATOM   2916 C C   . LYS D 1 41  ? 13.42900  47.84700 49.43200  1.000 80.39000  ? 23  LYS C C   1 
ATOM   2917 O O   . LYS D 1 41  ? 12.65600  48.81100 49.38900  1.000 76.62000  ? 23  LYS C O   1 
ATOM   2918 C CB  . LYS D 1 41  ? 14.24500  47.13200 51.69700  1.000 75.48000  ? 23  LYS C CB  1 
ATOM   2919 C CG  . LYS D 1 41  ? 14.05500  48.52300 52.28300  1.000 85.74000  ? 23  LYS C CG  1 
ATOM   2920 N N   . ILE D 1 42  ? 14.39400  47.66700 48.52800  1.000 75.84000  ? 24  ILE C N   1 
ATOM   2921 C CA  . ILE D 1 42  ? 14.58000  48.61200 47.43100  1.000 82.53000  ? 24  ILE C CA  1 
ATOM   2922 C C   . ILE D 1 42  ? 13.43500  48.49900 46.43200  1.000 73.68000  ? 24  ILE C C   1 
ATOM   2923 O O   . ILE D 1 42  ? 12.88000  49.50900 45.98300  1.000 73.21000  ? 24  ILE C O   1 
ATOM   2924 C CB  . ILE D 1 42  ? 15.94500  48.38600 46.75600  1.000 85.23000  ? 24  ILE C CB  1 
ATOM   2925 C CG1 . ILE D 1 42  ? 17.08300  48.73300 47.72000  1.000 62.69000  ? 24  ILE C CG1 1 
ATOM   2926 C CG2 . ILE D 1 42  ? 16.05000  49.20100 45.47500  1.000 68.56000  ? 24  ILE C CG2 1 
ATOM   2927 C CD1 . ILE D 1 42  ? 18.46200  48.47300 47.15400  1.000 56.11000  ? 24  ILE C CD1 1 
ATOM   2928 N N   . LYS D 1 43  ? 13.06400  47.26700 46.07000  1.000 73.14000  ? 25  LYS C N   1 
ATOM   2929 C CA  . LYS D 1 43  ? 11.96800  47.07100 45.12600  1.000 80.34000  ? 25  LYS C CA  1 
ATOM   2930 C C   . LYS D 1 43  ? 10.65700  47.61500 45.67900  1.000 77.57000  ? 25  LYS C C   1 
ATOM   2931 O O   . LYS D 1 43  ? 9.85400   48.19300 44.93800  1.000 79.58000  ? 25  LYS C O   1 
ATOM   2932 C CB  . LYS D 1 43  ? 11.82800  45.58800 44.78400  1.000 71.09000  ? 25  LYS C CB  1 
ATOM   2933 C CG  . LYS D 1 43  ? 13.01900  44.99600 44.04800  1.000 75.81000  ? 25  LYS C CG  1 
ATOM   2934 N N   . SER D 1 44  ? 10.42200  47.43700 46.98100  1.000 68.47000  ? 26  SER C N   1 
ATOM   2935 C CA  . SER D 1 44  ? 9.20900   47.97000 47.59200  1.000 82.71000  ? 26  SER C CA  1 
ATOM   2936 C C   . SER D 1 44  ? 9.20900   49.49300 47.57700  1.000 72.53000  ? 26  SER C C   1 
ATOM   2937 O O   . SER D 1 44  ? 8.17700   50.11900 47.30700  1.000 75.24000  ? 26  SER C O   1 
ATOM   2938 C CB  . SER D 1 44  ? 9.06900   47.44800 49.02200  1.000 89.08000  ? 26  SER C CB  1 
ATOM   2939 O OG  . SER D 1 44  ? 7.99000   48.07600 49.69100  1.000 92.76000  ? 26  SER C OG  1 
ATOM   2940 N N   . ALA D 1 45  ? 10.36100  50.10600 47.85900  1.000 73.25000  ? 27  ALA C N   1 
ATOM   2941 C CA  . ALA D 1 45  ? 10.44600  51.56000 47.89200  1.000 71.53000  ? 27  ALA C CA  1 
ATOM   2942 C C   . ALA D 1 45  ? 10.30100  52.18500 46.51100  1.000 70.41000  ? 27  ALA C C   1 
ATOM   2943 O O   . ALA D 1 45  ? 9.94400   53.36300 46.41500  1.000 66.93000  ? 27  ALA C O   1 
ATOM   2944 C CB  . ALA D 1 45  ? 11.77100  51.99500 48.52100  1.000 81.55000  ? 27  ALA C CB  1 
ATOM   2945 N N   . LEU D 1 46  ? 10.56400  51.42900 45.44700  1.000 66.66000  ? 28  LEU C N   1 
ATOM   2946 C CA  . LEU D 1 46  ? 10.49800  51.94100 44.08500  1.000 82.44000  ? 28  LEU C CA  1 
ATOM   2947 C C   . LEU D 1 46  ? 9.22700   51.52800 43.35500  1.000 84.81000  ? 28  LEU C C   1 
ATOM   2948 O O   . LEU D 1 46  ? 9.12800   51.74100 42.14200  1.000 82.20000  ? 28  LEU C O   1 
ATOM   2949 C CB  . LEU D 1 46  ? 11.72300  51.48200 43.29100  1.000 63.98000  ? 28  LEU C CB  1 
ATOM   2950 C CG  . LEU D 1 46  ? 13.07000  52.05500 43.72900  1.000 66.68000  ? 28  LEU C CG  1 
ATOM   2951 C CD1 . LEU D 1 46  ? 14.19200  51.44400 42.90700  1.000 60.37000  ? 28  LEU C CD1 1 
ATOM   2952 C CD2 . LEU D 1 46  ? 13.06700  53.57100 43.60100  1.000 61.85000  ? 28  LEU C CD2 1 
ATOM   2953 N N   . LYS D 1 47  ? 8.25700   50.94000 44.05900  1.000 79.85000  ? 29  LYS C N   1 
ATOM   2954 C CA  . LYS D 1 47  ? 7.01900   50.52000 43.40800  1.000 73.22000  ? 29  LYS C CA  1 
ATOM   2955 C C   . LYS D 1 47  ? 6.22200   51.71800 42.91200  1.000 77.91000  ? 29  LYS C C   1 
ATOM   2956 O O   . LYS D 1 47  ? 5.74000   51.72800 41.77300  1.000 77.18000  ? 29  LYS C O   1 
ATOM   2957 C CB  . LYS D 1 47  ? 6.17100   49.68500 44.36500  1.000 88.32000  ? 29  LYS C CB  1 
ATOM   2958 N N   . SER D 1 48  ? 6.06900   52.73500 43.75500  1.000 66.45000  ? 30  SER C N   1 
ATOM   2959 C CA  . SER D 1 48  ? 5.22600   53.88300 43.45400  1.000 73.08000  ? 30  SER C CA  1 
ATOM   2960 C C   . SER D 1 48  ? 6.02700   55.14800 43.17200  1.000 78.11000  ? 30  SER C C   1 
ATOM   2961 O O   . SER D 1 48  ? 5.43400   56.21900 43.00900  1.000 76.68000  ? 30  SER C O   1 
ATOM   2962 C CB  . SER D 1 48  ? 4.24700   54.12400 44.60200  1.000 97.88000  ? 30  SER C CB  1 
ATOM   2963 O OG  . SER D 1 48  ? 3.33900   53.04800 44.70800  1.000 100.98000 ? 30  SER C OG  1 
ATOM   2964 N N   . THR D 1 49  ? 7.35400   55.05900 43.11900  1.000 79.37000  ? 31  THR C N   1 
ATOM   2965 C CA  . THR D 1 49  ? 8.18300   56.21700 42.81100  1.000 78.68000  ? 31  THR C CA  1 
ATOM   2966 C C   . THR D 1 49  ? 9.46400   55.75400 42.13400  1.000 65.23000  ? 31  THR C C   1 
ATOM   2967 O O   . THR D 1 49  ? 9.86200   54.58900 42.23600  1.000 62.71000  ? 31  THR C O   1 
ATOM   2968 C CB  . THR D 1 49  ? 8.52400   57.02600 44.07000  1.000 73.73000  ? 31  THR C CB  1 
ATOM   2969 O OG1 . THR D 1 49  ? 9.34500   58.15000 43.72400  1.000 72.47000  ? 31  THR C OG1 1 
ATOM   2970 C CG2 . THR D 1 49  ? 9.28100   56.15500 45.05300  1.000 68.77000  ? 31  THR C CG2 1 
ATOM   2971 N N   . ASN D 1 50  ? 10.10900  56.69300 41.44500  1.000 63.47000  ? 32  ASN C N   1 
ATOM   2972 C CA  . ASN D 1 50  ? 11.37400  56.45400 40.76500  1.000 61.39000  ? 32  ASN C CA  1 
ATOM   2973 C C   . ASN D 1 50  ? 12.56300  57.01600 41.53400  1.000 65.47000  ? 32  ASN C C   1 
ATOM   2974 O O   . ASN D 1 50  ? 13.66500  57.09600 40.98200  1.000 62.23000  ? 32  ASN C O   1 
ATOM   2975 C CB  . ASN D 1 50  ? 11.33300  57.05100 39.35600  1.000 50.28000  ? 32  ASN C CB  1 
ATOM   2976 C CG  . ASN D 1 50  ? 10.20000  56.48700 38.51700  1.000 57.46000  ? 32  ASN C CG  1 
ATOM   2977 O OD1 . ASN D 1 50  ? 9.86900   55.30600 38.61900  1.000 61.88000  ? 32  ASN C OD1 1 
ATOM   2978 N ND2 . ASN D 1 50  ? 9.59200   57.33200 37.68800  1.000 59.56000  ? 32  ASN C ND2 1 
ATOM   2979 N N   . LYS D 1 51  ? 12.36400  57.40300 42.79200  1.000 52.57000  ? 33  LYS C N   1 
ATOM   2980 C CA  . LYS D 1 51  ? 13.44000  57.95900 43.60800  1.000 56.04000  ? 33  LYS C CA  1 
ATOM   2981 C C   . LYS D 1 51  ? 13.05700  57.79800 45.06900  1.000 74.28000  ? 33  LYS C C   1 
ATOM   2982 O O   . LYS D 1 51  ? 12.03200  58.33300 45.50100  1.000 68.84000  ? 33  LYS C O   1 
ATOM   2983 C CB  . LYS D 1 51  ? 13.67800  59.42900 43.26700  1.000 47.98000  ? 33  LYS C CB  1 
ATOM   2984 C CG  . LYS D 1 51  ? 14.78600  60.08600 44.07100  1.000 59.50000  ? 33  LYS C CG  1 
ATOM   2985 C CD  . LYS D 1 51  ? 15.00800  61.52500 43.63000  1.000 66.18000  ? 33  LYS C CD  1 
ATOM   2986 C CE  . LYS D 1 51  ? 16.10700  62.19800 44.43800  1.000 67.13000  ? 33  LYS C CE  1 
ATOM   2987 N NZ  . LYS D 1 51  ? 16.37400  63.58400 43.96200  1.000 84.38000  ? 33  LYS C NZ  1 
ATOM   2988 N N   . ALA D 1 52  ? 13.87200  57.06600 45.82500  1.000 61.86000  ? 34  ALA C N   1 
ATOM   2989 C CA  . ALA D 1 52  ? 13.59000  56.82400 47.23100  1.000 61.87000  ? 34  ALA C CA  1 
ATOM   2990 C C   . ALA D 1 52  ? 14.90200  56.68700 47.99000  1.000 72.18000  ? 34  ALA C C   1 
ATOM   2991 O O   . ALA D 1 52  ? 15.98800  56.67400 47.40400  1.000 61.78000  ? 34  ALA C O   1 
ATOM   2992 C CB  . ALA D 1 52  ? 12.71900  55.57800 47.42100  1.000 51.68000  ? 34  ALA C CB  1 
ATOM   2993 N N   . VAL D 1 53  ? 14.78700  56.58800 49.31200  1.000 61.75000  ? 35  VAL C N   1 
ATOM   2994 C CA  . VAL D 1 53  ? 15.93200  56.42300 50.20000  1.000 65.04000  ? 35  VAL C CA  1 
ATOM   2995 C C   . VAL D 1 53  ? 15.61100  55.30300 51.17800  1.000 58.12000  ? 35  VAL C C   1 
ATOM   2996 O O   . VAL D 1 53  ? 14.59800  55.36400 51.88600  1.000 69.49000  ? 35  VAL C O   1 
ATOM   2997 C CB  . VAL D 1 53  ? 16.27300  57.71800 50.95800  1.000 65.38000  ? 35  VAL C CB  1 
ATOM   2998 C CG1 . VAL D 1 53  ? 17.39800  57.46900 51.95000  1.000 75.18000  ? 35  VAL C CG1 1 
ATOM   2999 C CG2 . VAL D 1 53  ? 16.65400  58.82300 49.98500  1.000 62.25000  ? 35  VAL C CG2 1 
ATOM   3000 N N   . VAL D 1 54  ? 16.46600  54.28400 51.21700  1.000 59.72000  ? 36  VAL C N   1 
ATOM   3001 C CA  . VAL D 1 54  ? 16.31000  53.15800 52.12500  1.000 60.49000  ? 36  VAL C CA  1 
ATOM   3002 C C   . VAL D 1 54  ? 17.50200  53.13200 53.07600  1.000 74.08000  ? 36  VAL C C   1 
ATOM   3003 O O   . VAL D 1 54  ? 18.52500  53.78000 52.84900  1.000 72.73000  ? 36  VAL C O   1 
ATOM   3004 C CB  . VAL D 1 54  ? 16.17300  51.81800 51.37700  1.000 68.34000  ? 36  VAL C CB  1 
ATOM   3005 C CG1 . VAL D 1 54  ? 14.87100  51.78100 50.59200  1.000 76.46000  ? 36  VAL C CG1 1 
ATOM   3006 C CG2 . VAL D 1 54  ? 17.35600  51.60800 50.45200  1.000 66.40000  ? 36  VAL C CG2 1 
ATOM   3007 N N   . THR D 1 55  ? 17.32000  52.39700 54.16600  1.000 79.55000  ? 37  THR C N   1 
ATOM   3008 C CA  . THR D 1 55  ? 18.39200  52.29100 55.17400  1.000 71.62000  ? 37  THR C CA  1 
ATOM   3009 C C   . THR D 1 55  ? 18.67300  50.81200 55.36200  1.000 71.58000  ? 37  THR C C   1 
ATOM   3010 O O   . THR D 1 55  ? 17.79100  50.09200 55.80900  1.000 74.73000  ? 37  THR C O   1 
ATOM   3011 C CB  . THR D 1 55  ? 18.01300  53.01500 56.46200  1.000 77.98000  ? 37  THR C CB  1 
ATOM   3012 O OG1 . THR D 1 55  ? 16.70400  52.58300 56.83100  1.000 103.13000 ? 37  THR C OG1 1 
ATOM   3013 C CG2 . THR D 1 55  ? 18.02800  54.51900 56.31000  1.000 78.63000  ? 37  THR C CG2 1 
ATOM   3014 N N   . ILE D 1 56  ? 19.84100  50.39400 54.91800  1.000 82.76000  ? 38  ILE C N   1 
ATOM   3015 C CA  . ILE D 1 56  ? 20.24500  48.98300 55.09700  1.000 82.33000  ? 38  ILE C CA  1 
ATOM   3016 C C   . ILE D 1 56  ? 21.16200  48.97200 56.31000  1.000 81.76000  ? 38  ILE C C   1 
ATOM   3017 O O   . ILE D 1 56  ? 21.71000  50.02000 56.66000  1.000 84.20000  ? 38  ILE C O   1 
ATOM   3018 C CB  . ILE D 1 56  ? 20.93700  48.46300 53.82600  1.000 79.95000  ? 38  ILE C CB  1 
ATOM   3019 C CG1 . ILE D 1 56  ? 22.34800  49.03200 53.66900  1.000 82.98000  ? 38  ILE C CG1 1 
ATOM   3020 C CG2 . ILE D 1 56  ? 20.07800  48.74300 52.60600  1.000 84.95000  ? 38  ILE C CG2 1 
ATOM   3021 C CD1 . ILE D 1 56  ? 23.07600  48.52700 52.45000  1.000 97.17000  ? 38  ILE C CD1 1 
ATOM   3022 N N   . LYS D 1 57  ? 21.28900  47.82300 56.94000  1.000 87.55000  ? 39  LYS C N   1 
ATOM   3023 C CA  . LYS D 1 57  ? 22.23500  47.72700 58.07000  1.000 90.10000  ? 39  LYS C CA  1 
ATOM   3024 C C   . LYS D 1 57  ? 23.31500  46.72800 57.66700  1.000 102.03000 ? 39  LYS C C   1 
ATOM   3025 O O   . LYS D 1 57  ? 22.97500  45.61600 57.23100  1.000 104.11000 ? 39  LYS C O   1 
ATOM   3026 C CB  . LYS D 1 57  ? 21.50000  47.31700 59.34700  1.000 85.93000  ? 39  LYS C CB  1 
ATOM   3027 N N   . ASP D 1 58  ? 24.56900  47.13200 57.80500  1.000 100.15000 ? 40  ASP C N   1 
ATOM   3028 C CA  . ASP D 1 58  ? 25.67500  46.23000 57.43600  1.000 106.08000 ? 40  ASP C CA  1 
ATOM   3029 C C   . ASP D 1 58  ? 26.20200  45.54000 58.67400  1.000 111.02000 ? 40  ASP C C   1 
ATOM   3030 O O   . ASP D 1 58  ? 25.56900  45.64800 59.73600  1.000 103.95000 ? 40  ASP C O   1 
ATOM   3031 C CB  . ASP D 1 58  ? 26.88300  47.00300 56.93200  1.000 104.30000 ? 40  ASP C CB  1 
ATOM   3032 N N   . GLU D 1 59  ? 27.33100  44.86400 58.52200  1.000 110.85000 ? 41  GLU C N   1 
ATOM   3033 C CA  . GLU D 1 59  ? 27.98400  44.29600 59.72400  1.000 114.44000 ? 41  GLU C CA  1 
ATOM   3034 C C   . GLU D 1 59  ? 28.15000  45.45400 60.70800  1.000 119.23000 ? 41  GLU C C   1 
ATOM   3035 O O   . GLU D 1 59  ? 28.14300  46.60700 60.23400  1.000 117.85000 ? 41  GLU C O   1 
ATOM   3036 C CB  . GLU D 1 59  ? 29.32200  43.66400 59.35700  1.000 107.07000 ? 41  GLU C CB  1 
ATOM   3037 N N   . ASN D 1 60  ? 28.25300  45.16700 62.00200  1.000 118.42000 ? 42  ASN C N   1 
ATOM   3038 C CA  . ASN D 1 60  ? 28.38800  46.23000 63.03100  1.000 117.84000 ? 42  ASN C CA  1 
ATOM   3039 C C   . ASN D 1 60  ? 27.03100  46.88700 63.27900  1.000 113.62000 ? 42  ASN C C   1 
ATOM   3040 O O   . ASN D 1 60  ? 27.01900  47.99700 63.82700  1.000 118.26000 ? 42  ASN C O   1 
ATOM   3041 C CB  . ASN D 1 60  ? 29.42400  47.29900 62.66400  1.000 116.24000 ? 42  ASN C CB  1 
ATOM   3042 N N   . GLY D 1 61  ? 25.94000  46.22600 62.89600  1.000 112.04000 ? 43  GLY C N   1 
ATOM   3043 C CA  . GLY D 1 61  ? 24.59000  46.76500 63.14500  1.000 95.84000  ? 43  GLY C CA  1 
ATOM   3044 C C   . GLY D 1 61  ? 24.50300  48.23300 62.78100  1.000 102.70000 ? 43  GLY C C   1 
ATOM   3045 O O   . GLY D 1 61  ? 23.62900  48.92000 63.33100  1.000 95.17000  ? 43  GLY C O   1 
ATOM   3046 N N   . GLU D 1 62  ? 25.37700  48.69800 61.89000  1.000 100.34000 ? 44  GLU C N   1 
ATOM   3047 C CA  . GLU D 1 62  ? 25.42000  50.14500 61.56100  1.000 105.93000 ? 44  GLU C CA  1 
ATOM   3048 C C   . GLU D 1 62  ? 24.41600  50.46200 60.44900  1.000 105.48000 ? 44  GLU C C   1 
ATOM   3049 O O   . GLU D 1 62  ? 24.18400  49.59000 59.60200  1.000 96.92000  ? 44  GLU C O   1 
ATOM   3050 C CB  . GLU D 1 62  ? 26.84700  50.53700 61.17300  1.000 103.97000 ? 44  GLU C CB  1 
ATOM   3051 C CG  . GLU D 1 62  ? 27.12000  52.02500 61.23000  1.000 97.95000  ? 44  GLU C CG  1 
ATOM   3052 C CD  . GLU D 1 62  ? 28.57800  52.36400 60.97900  1.000 107.05000 ? 44  GLU C CD  1 
ATOM   3053 O OE1 . GLU D 1 62  ? 29.35800  51.43100 60.72300  1.000 102.68000 ? 44  GLU C OE1 1 
ATOM   3054 O OE2 . GLU D 1 62  ? 28.93100  53.55500 61.05300  1.000 112.70000 ? 44  GLU C OE2 1 
ATOM   3055 N N   . GLU D 1 63  ? 23.86100  51.67500 60.46000  1.000 101.29000 ? 45  GLU C N   1 
ATOM   3056 C CA  . GLU D 1 63  ? 22.85900  52.07700 59.44300  1.000 94.24000  ? 45  GLU C CA  1 
ATOM   3057 C C   . GLU D 1 63  ? 23.56200  52.79900 58.28800  1.000 95.53000  ? 45  GLU C C   1 
ATOM   3058 O O   . GLU D 1 63  ? 24.44100  53.63000 58.56000  1.000 82.17000  ? 45  GLU C O   1 
ATOM   3059 C CB  . GLU D 1 63  ? 21.77600  52.95400 60.06900  1.000 89.55000  ? 45  GLU C CB  1 
ATOM   3060 C CG  . GLU D 1 63  ? 21.01700  52.29000 61.19900  1.000 109.22000 ? 45  GLU C CG  1 
ATOM   3061 C CD  . GLU D 1 63  ? 19.75900  53.01800 61.64400  1.000 105.57000 ? 45  GLU C CD  1 
ATOM   3062 O OE1 . GLU D 1 63  ? 19.40900  54.03400 61.01500  1.000 103.70000 ? 45  GLU C OE1 1 
ATOM   3063 O OE2 . GLU D 1 63  ? 19.13700  52.57200 62.62700  1.000 95.72000  ? 45  GLU C OE2 1 
ATOM   3064 N N   . ILE D 1 64  ? 23.18500  52.47300 57.05000  1.000 84.55000  ? 46  ILE C N   1 
ATOM   3065 C CA  . ILE D 1 64  ? 23.80000  53.10000 55.84600  1.000 77.46000  ? 46  ILE C CA  1 
ATOM   3066 C C   . ILE D 1 64  ? 22.68100  53.62500 54.95600  1.000 64.76000  ? 46  ILE C C   1 
ATOM   3067 O O   . ILE D 1 64  ? 21.81300  52.83200 54.59800  1.000 65.85000  ? 46  ILE C O   1 
ATOM   3068 C CB  . ILE D 1 64  ? 24.68400  52.09500 55.08400  1.000 71.57000  ? 46  ILE C CB  1 
ATOM   3069 C CG1 . ILE D 1 64  ? 25.96300  51.76100 55.85300  1.000 73.54000  ? 46  ILE C CG1 1 
ATOM   3070 C CG2 . ILE D 1 64  ? 24.99100  52.59900 53.68600  1.000 67.69000  ? 46  ILE C CG2 1 
ATOM   3071 C CD1 . ILE D 1 64  ? 25.84700  50.54500 56.73200  1.000 81.31000  ? 46  ILE C CD1 1 
ATOM   3072 N N   . GLU D 1 65  ? 22.68100  54.92100 54.66800  1.000 64.80000  ? 47  GLU C N   1 
ATOM   3073 C CA  . GLU D 1 65  ? 21.72500  55.45300 53.70900  1.000 59.78000  ? 47  GLU C CA  1 
ATOM   3074 C C   . GLU D 1 65  ? 22.02800  54.91400 52.31600  1.000 70.08000  ? 47  GLU C C   1 
ATOM   3075 O O   . GLU D 1 65  ? 23.19000  54.77100 51.92700  1.000 73.64000  ? 47  GLU C O   1 
ATOM   3076 C CB  . GLU D 1 65  ? 21.76700  56.98300 53.70900  1.000 57.66000  ? 47  GLU C CB  1 
ATOM   3077 C CG  . GLU D 1 65  ? 21.08100  57.63400 52.51700  1.000 83.47000  ? 47  GLU C CG  1 
ATOM   3078 C CD  . GLU D 1 65  ? 21.01600  59.14400 52.62900  1.000 98.10000  ? 47  GLU C CD  1 
ATOM   3079 O OE1 . GLU D 1 65  ? 20.75400  59.64700 53.74200  1.000 120.48000 ? 47  GLU C OE1 1 
ATOM   3080 O OE2 . GLU D 1 65  ? 21.23200  59.82800 51.60600  1.000 103.96000 ? 47  GLU C OE2 1 
ATOM   3081 N N   . VAL D 1 66  ? 20.96900  54.54700 51.60000  1.000 59.45000  ? 48  VAL C N   1 
ATOM   3082 C CA  . VAL D 1 66  ? 21.12500  54.06700 50.20200  1.000 58.53000  ? 48  VAL C CA  1 
ATOM   3083 C C   . VAL D 1 66  ? 20.14300  54.81300 49.30000  1.000 61.13000  ? 48  VAL C C   1 
ATOM   3084 O O   . VAL D 1 66  ? 18.94200  54.66600 49.50200  1.000 72.17000  ? 48  VAL C O   1 
ATOM   3085 C CB  . VAL D 1 66  ? 20.94600  52.54600 50.08600  1.000 51.80000  ? 48  VAL C CB  1 
ATOM   3086 C CG1 . VAL D 1 66  ? 21.07400  52.07500 48.64800  1.000 54.85000  ? 48  VAL C CG1 1 
ATOM   3087 C CG2 . VAL D 1 66  ? 21.90300  51.78900 50.98600  1.000 55.26000  ? 48  VAL C CG2 1 
ATOM   3088 N N   . GLU D 1 67  ? 20.64900  55.62400 48.38100  1.000 60.95000  ? 49  GLU C N   1 
ATOM   3089 C CA  . GLU D 1 67  ? 19.81300  56.28000 47.38500  1.000 57.58000  ? 49  GLU C CA  1 
ATOM   3090 C C   . GLU D 1 67  ? 19.45800  55.28800 46.28600  1.000 59.55000  ? 49  GLU C C   1 
ATOM   3091 O O   . GLU D 1 67  ? 20.34500  54.68000 45.67900  1.000 51.23000  ? 49  GLU C O   1 
ATOM   3092 C CB  . GLU D 1 67  ? 20.52800  57.49300 46.78800  1.000 56.14000  ? 49  GLU C CB  1 
ATOM   3093 C CG  . GLU D 1 67  ? 20.76700  58.63700 47.76000  1.000 74.92000  ? 49  GLU C CG  1 
ATOM   3094 C CD  . GLU D 1 67  ? 21.22600  59.90400 47.05800  1.000 83.99000  ? 49  GLU C CD  1 
ATOM   3095 O OE1 . GLU D 1 67  ? 20.92000  60.06300 45.85700  1.000 84.60000  ? 49  GLU C OE1 1 
ATOM   3096 O OE2 . GLU D 1 67  ? 21.89400  60.73700 47.70500  1.000 106.17000 ? 49  GLU C OE2 1 
ATOM   3097 N N   . VAL D 1 68  ? 18.16300  55.11900 46.03400  1.000 52.68000  ? 50  VAL C N   1 
ATOM   3098 C CA  . VAL D 1 68  ? 17.67600  54.19900 45.01400  1.000 54.75000  ? 50  VAL C CA  1 
ATOM   3099 C C   . VAL D 1 68  ? 16.83900  54.97600 44.00900  1.000 63.44000  ? 50  VAL C C   1 
ATOM   3100 O O   . VAL D 1 68  ? 16.10300  55.89900 44.37600  1.000 54.28000  ? 50  VAL C O   1 
ATOM   3101 C CB  . VAL D 1 68  ? 16.86800  53.03400 45.62700  1.000 60.99000  ? 50  VAL C CB  1 
ATOM   3102 C CG1 . VAL D 1 68  ? 17.74800  52.21900 46.56000  1.000 62.34000  ? 50  VAL C CG1 1 
ATOM   3103 C CG2 . VAL D 1 68  ? 15.63900  53.54800 46.36300  1.000 64.99000  ? 50  VAL C CG2 1 
ATOM   3104 N N   . ARG D 1 69  ? 17.00000  54.60500 42.74300  1.000 56.40000  ? 51  ARG C N   1 
ATOM   3105 C CA  . ARG D 1 69  ? 16.23900  55.26900 41.66800  1.000 49.85000  ? 51  ARG C CA  1 
ATOM   3106 C C   . ARG D 1 69  ? 15.86100  54.23300 40.61300  1.000 57.95000  ? 51  ARG C C   1 
ATOM   3107 O O   . ARG D 1 69  ? 16.63200  53.29200 40.42400  1.000 51.15000  ? 51  ARG C O   1 
ATOM   3108 C CB  . ARG D 1 69  ? 17.08000  56.39700 41.06800  1.000 50.47000  ? 51  ARG C CB  1 
ATOM   3109 C CG  . ARG D 1 69  ? 17.10600  57.67300 41.89000  1.000 47.61000  ? 51  ARG C CG  1 
ATOM   3110 C CD  . ARG D 1 69  ? 18.18200  58.60800 41.39100  1.000 58.86000  ? 51  ARG C CD  1 
ATOM   3111 N NE  . ARG D 1 69  ? 18.83600  59.23700 42.52100  1.000 50.56000  ? 51  ARG C NE  1 
ATOM   3112 C CZ  . ARG D 1 69  ? 18.83500  60.54000 42.74200  1.000 67.39000  ? 51  ARG C CZ  1 
ATOM   3113 N NH1 . ARG D 1 69  ? 18.37100  61.36200 41.81900  1.000 75.66000  ? 51  ARG C NH1 1 
ATOM   3114 N NH2 . ARG D 1 69  ? 19.30100  61.01600 43.88200  1.000 63.97000  ? 51  ARG C NH2 1 
ATOM   3115 N N   . LEU D 1 70  ? 14.69000  54.38700 39.99800  1.000 54.56000  ? 52  LEU C N   1 
ATOM   3116 C CA  . LEU D 1 70  ? 14.29900  53.50700 38.86900  1.000 48.54000  ? 52  LEU C CA  1 
ATOM   3117 C C   . LEU D 1 70  ? 14.41600  54.37400 37.62500  1.000 61.56000  ? 52  LEU C C   1 
ATOM   3118 O O   . LEU D 1 70  ? 13.62900  55.31500 37.48900  1.000 58.24000  ? 52  LEU C O   1 
ATOM   3119 C CB  . LEU D 1 70  ? 12.87900  52.97700 39.06400  1.000 49.50000  ? 52  LEU C CB  1 
ATOM   3120 C CG  . LEU D 1 70  ? 12.42700  51.90500 38.07700  1.000 56.00000  ? 52  LEU C CG  1 
ATOM   3121 C CD1 . LEU D 1 70  ? 13.27800  50.65500 38.21200  1.000 49.48000  ? 52  LEU C CD1 1 
ATOM   3122 C CD2 . LEU D 1 70  ? 10.96300  51.56800 38.29200  1.000 47.11000  ? 52  LEU C CD2 1 
ATOM   3123 N N   . LEU D 1 71  ? 15.36300  54.06000 36.75700  1.000 49.71000  ? 53  LEU C N   1 
ATOM   3124 C CA  . LEU D 1 71  ? 15.61900  54.98200 35.62900  1.000 56.72000  ? 53  LEU C CA  1 
ATOM   3125 C C   . LEU D 1 71  ? 15.77800  54.26400 34.29300  1.000 60.51000  ? 53  LEU C C   1 
ATOM   3126 O O   . LEU D 1 71  ? 16.22300  53.11700 34.27700  1.000 44.78000  ? 53  LEU C O   1 
ATOM   3127 C CB  . LEU D 1 71  ? 16.91700  55.73300 35.95000  1.000 55.46000  ? 53  LEU C CB  1 
ATOM   3128 C CG  . LEU D 1 71  ? 16.88400  56.70600 37.12500  1.000 59.14000  ? 53  LEU C CG  1 
ATOM   3129 C CD1 . LEU D 1 71  ? 18.25000  57.33900 37.32400  1.000 57.15000  ? 53  LEU C CD1 1 
ATOM   3130 C CD2 . LEU D 1 71  ? 15.83700  57.78300 36.90800  1.000 47.75000  ? 53  LEU C CD2 1 
ATOM   3131 N N   . THR D 1 72  ? 15.40900  54.94000 33.21400  1.000 46.75000  ? 54  THR C N   1 
ATOM   3132 C CA  . THR D 1 72  ? 15.71900  54.39500 31.90400  1.000 57.42000  ? 54  THR C CA  1 
ATOM   3133 C C   . THR D 1 72  ? 17.21900  54.50300 31.63900  1.000 44.33000  ? 54  THR C C   1 
ATOM   3134 O O   . THR D 1 72  ? 17.97400  55.10200 32.41100  1.000 44.00000  ? 54  THR C O   1 
ATOM   3135 C CB  . THR D 1 72  ? 14.93700  55.12700 30.81200  1.000 46.26000  ? 54  THR C CB  1 
ATOM   3136 O OG1 . THR D 1 72  ? 15.35800  56.49500 30.75700  1.000 48.31000  ? 54  THR C OG1 1 
ATOM   3137 C CG2 . THR D 1 72  ? 13.44400  55.07600 31.09900  1.000 53.23000  ? 54  THR C CG2 1 
ATOM   3138 N N   . LEU D 1 73  ? 17.65300  53.91100 30.52400  1.000 46.37000  ? 55  LEU C N   1 
ATOM   3139 C CA  . LEU D 1 73  ? 19.07100  53.95200 30.17900  1.000 41.53000  ? 55  LEU C CA  1 
ATOM   3140 C C   . LEU D 1 73  ? 19.54500  55.38500 29.97000  1.000 41.42000  ? 55  LEU C C   1 
ATOM   3141 O O   . LEU D 1 73  ? 20.62700  55.76300 30.43400  1.000 43.92000  ? 55  LEU C O   1 
ATOM   3142 C CB  . LEU D 1 73  ? 19.33400  53.11000 28.93100  1.000 36.41000  ? 55  LEU C CB  1 
ATOM   3143 C CG  . LEU D 1 73  ? 20.79100  53.02700 28.47300  1.000 39.23000  ? 55  LEU C CG  1 
ATOM   3144 C CD1 . LEU D 1 73  ? 21.67300  52.46400 29.57900  1.000 45.91000  ? 55  LEU C CD1 1 
ATOM   3145 C CD2 . LEU D 1 73  ? 20.90400  52.18600 27.21200  1.000 42.97000  ? 55  LEU C CD2 1 
ATOM   3146 N N   . GLU D 1 74  ? 18.74400  56.20200 29.30400  1.000 41.28000  ? 56  GLU C N   1 
ATOM   3147 C CA  . GLU D 1 74  ? 19.12300  57.61300 29.06800  1.000 42.01000  ? 56  GLU C CA  1 
ATOM   3148 C C   . GLU D 1 74  ? 19.14400  58.36000 30.39800  1.000 38.88000  ? 56  GLU C C   1 
ATOM   3149 O O   . GLU D 1 74  ? 20.08900  59.10300 30.62000  1.000 50.44000  ? 56  GLU C O   1 
ATOM   3150 C CB  . GLU D 1 74  ? 18.16400  58.28400 28.09000  1.000 47.89000  ? 56  GLU C CB  1 
ATOM   3151 C CG  . GLU D 1 74  ? 18.53700  59.70300 27.71800  1.000 43.50000  ? 56  GLU C CG  1 
ATOM   3152 C CD  . GLU D 1 74  ? 17.42800  60.46200 27.01100  1.000 61.25000  ? 56  GLU C CD  1 
ATOM   3153 O OE1 . GLU D 1 74  ? 16.25500  60.18000 27.29400  1.000 57.89000  ? 56  GLU C OE1 1 
ATOM   3154 O OE2 . GLU D 1 74  ? 17.74100  61.32900 26.17800  1.000 66.38000  ? 56  GLU C OE2 1 
ATOM   3155 N N   . GLU D 1 75  ? 18.12600  58.15600 31.22800  1.000 38.05000  ? 57  GLU C N   1 
ATOM   3156 C CA  . GLU D 1 75  ? 18.08300  58.84200 32.51600  1.000 39.20000  ? 57  GLU C CA  1 
ATOM   3157 C C   . GLU D 1 75  ? 19.24000  58.41600 33.41000  1.000 40.43000  ? 57  GLU C C   1 
ATOM   3158 O O   . GLU D 1 75  ? 19.84400  59.24800 34.09600  1.000 38.84000  ? 57  GLU C O   1 
ATOM   3159 C CB  . GLU D 1 75  ? 16.74900  58.57300 33.21100  1.000 45.38000  ? 57  GLU C CB  1 
ATOM   3160 C CG  . GLU D 1 75  ? 15.54700  59.18600 32.51800  1.000 58.29000  ? 57  GLU C CG  1 
ATOM   3161 C CD  . GLU D 1 75  ? 14.23800  58.69500 33.10100  1.000 59.15000  ? 57  GLU C CD  1 
ATOM   3162 O OE1 . GLU D 1 75  ? 14.25100  57.65800 33.79700  1.000 46.97000  ? 57  GLU C OE1 1 
ATOM   3163 O OE2 . GLU D 1 75  ? 13.19800  59.34500 32.86500  1.000 63.08000  ? 57  GLU C OE2 1 
ATOM   3164 N N   . ALA D 1 76  ? 19.56300  57.12100 33.41600  1.000 41.71000  ? 58  ALA C N   1 
ATOM   3165 C CA  . ALA D 1 76  ? 20.64700  56.63900 34.26400  1.000 35.60000  ? 58  ALA C CA  1 
ATOM   3166 C C   . ALA D 1 76  ? 21.99400  57.18200 33.80300  1.000 41.18000  ? 58  ALA C C   1 
ATOM   3167 O O   . ALA D 1 76  ? 22.86700  57.47100 34.62900  1.000 42.50000  ? 58  ALA C O   1 
ATOM   3168 C CB  . ALA D 1 76  ? 20.65600  55.11200 34.28700  1.000 35.14000  ? 58  ALA C CB  1 
ATOM   3169 N N   . LEU D 1 77  ? 22.18100  57.33300 32.49000  1.000 39.35000  ? 59  LEU C N   1 
ATOM   3170 C CA  . LEU D 1 77  ? 23.43300  57.88700 31.98400  1.000 39.64000  ? 59  LEU C CA  1 
ATOM   3171 C C   . LEU D 1 77  ? 23.57900  59.35600 32.36000  1.000 47.39000  ? 59  LEU C C   1 
ATOM   3172 O O   . LEU D 1 77  ? 24.68600  59.81600 32.66500  1.000 36.80000  ? 59  LEU C O   1 
ATOM   3173 C CB  . LEU D 1 77  ? 23.51500  57.70800 30.46900  1.000 33.51000  ? 59  LEU C CB  1 
ATOM   3174 C CG  . LEU D 1 77  ? 23.79000  56.28600 29.97900  1.000 48.23000  ? 59  LEU C CG  1 
ATOM   3175 C CD1 . LEU D 1 77  ? 23.47100  56.16500 28.49900  1.000 37.40000  ? 59  LEU C CD1 1 
ATOM   3176 C CD2 . LEU D 1 77  ? 25.23700  55.89900 30.25200  1.000 37.89000  ? 59  LEU C CD2 1 
ATOM   3177 N N   . LYS D 1 78  ? 22.47700  60.10900 32.34300  1.000 40.61000  ? 60  LYS C N   1 
ATOM   3178 C CA  . LYS D 1 78  ? 22.53900  61.49900 32.78300  1.000 51.47000  ? 60  LYS C CA  1 
ATOM   3179 C C   . LYS D 1 78  ? 22.77100  61.58500 34.28600  1.000 41.29000  ? 60  LYS C C   1 
ATOM   3180 O O   . LYS D 1 78  ? 23.46900  62.48800 34.76100  1.000 41.56000  ? 60  LYS C O   1 
ATOM   3181 C CB  . LYS D 1 78  ? 21.25900  62.23500 32.39200  1.000 49.93000  ? 60  LYS C CB  1 
ATOM   3182 C CG  . LYS D 1 78  ? 21.31600  63.73600 32.63300  1.000 65.96000  ? 60  LYS C CG  1 
ATOM   3183 C CD  . LYS D 1 78  ? 19.98100  64.39800 32.33900  1.000 59.15000  ? 60  LYS C CD  1 
ATOM   3184 C CE  . LYS D 1 78  ? 20.10500  65.91300 32.35800  1.000 56.95000  ? 60  LYS C CE  1 
ATOM   3185 N NZ  . LYS D 1 78  ? 20.64900  66.41300 33.65000  1.000 55.74000  ? 60  LYS C NZ  1 
ATOM   3186 N N   . TYR D 1 79  ? 22.19500  60.65200 35.04800  1.000 32.70000  ? 61  TYR C N   1 
ATOM   3187 C CA  . TYR D 1 79  ? 22.43000  60.61600 36.48900  1.000 36.50000  ? 61  TYR C CA  1 
ATOM   3188 C C   . TYR D 1 79  ? 23.89900  60.35900 36.80100  1.000 38.10000  ? 61  TYR C C   1 
ATOM   3189 O O   . TYR D 1 79  ? 24.46900  60.98700 37.70000  1.000 43.72000  ? 61  TYR C O   1 
ATOM   3190 C CB  . TYR D 1 79  ? 21.54800  59.54800 37.13600  1.000 46.74000  ? 61  TYR C CB  1 
ATOM   3191 C CG  . TYR D 1 79  ? 21.91500  59.22100 38.56700  1.000 40.44000  ? 61  TYR C CG  1 
ATOM   3192 C CD1 . TYR D 1 79  ? 21.53400  60.05300 39.61100  1.000 42.86000  ? 61  TYR C CD1 1 
ATOM   3193 C CD2 . TYR D 1 79  ? 22.63200  58.07000 38.87600  1.000 38.31000  ? 61  TYR C CD2 1 
ATOM   3194 C CE1 . TYR D 1 79  ? 21.86400  59.75400 40.92000  1.000 35.60000  ? 61  TYR C CE1 1 
ATOM   3195 C CE2 . TYR D 1 79  ? 22.96600  57.76400 40.18200  1.000 53.67000  ? 61  TYR C CE2 1 
ATOM   3196 C CZ  . TYR D 1 79  ? 22.58000  58.60900 41.20000  1.000 48.44000  ? 61  TYR C CZ  1 
ATOM   3197 O OH  . TYR D 1 79  ? 22.91000  58.30900 42.50200  1.000 52.58000  ? 61  TYR C OH  1 
ATOM   3198 N N   . ILE D 1 80  ? 24.53700  59.47400 36.05500  1.000 38.28000  ? 62  ILE C N   1 
ATOM   3199 C CA  . ILE D 1 80  ? 25.96600  59.15800 36.29100  1.000 26.23000  ? 62  ILE C CA  1 
ATOM   3200 C C   . ILE D 1 80  ? 26.80400  60.38700 35.93700  1.000 40.24000  ? 62  ILE C C   1 
ATOM   3201 O O   . ILE D 1 80  ? 27.72700  60.70000 36.67200  1.000 37.36000  ? 62  ILE C O   1 
ATOM   3202 C CB  . ILE D 1 80  ? 26.37700  57.91000 35.49300  1.000 34.27000  ? 62  ILE C CB  1 
ATOM   3203 C CG1 . ILE D 1 80  ? 25.69700  56.64800 36.02800  1.000 35.21000  ? 62  ILE C CG1 1 
ATOM   3204 C CG2 . ILE D 1 80  ? 27.88800  57.76200 35.45100  1.000 32.69000  ? 62  ILE C CG2 1 
ATOM   3205 C CD1 . ILE D 1 80  ? 25.77300  55.47500 35.09000  1.000 37.01000  ? 62  ILE C CD1 1 
ATOM   3206 N N   . ASN D 1 81  ? 26.43900  61.07500 34.86600  1.000 33.22000  ? 63  ASN C N   1 
ATOM   3207 C CA  . ASN D 1 81  ? 27.22100  62.23400 34.44700  1.000 35.50000  ? 63  ASN C CA  1 
ATOM   3208 C C   . ASN D 1 81  ? 27.11300  63.38200 35.44400  1.000 38.98000  ? 63  ASN C C   1 
ATOM   3209 O O   . ASN D 1 81  ? 28.02800  64.20900 35.53200  1.000 38.85000  ? 63  ASN C O   1 
ATOM   3210 C CB  . ASN D 1 81  ? 26.77000  62.69100 33.05900  1.000 42.66000  ? 63  ASN C CB  1 
ATOM   3211 C CG  . ASN D 1 81  ? 27.73600  63.67500 32.42600  1.000 54.39000  ? 63  ASN C CG  1 
ATOM   3212 O OD1 . ASN D 1 81  ? 28.95200  63.55200 32.57400  1.000 63.20000  ? 63  ASN C OD1 1 
ATOM   3213 N ND2 . ASN D 1 81  ? 27.19700  64.66200 31.71900  1.000 54.10000  ? 63  ASN C ND2 1 
ATOM   3214 N N   . ASP D 1 82  ? 26.01800  63.45100 36.20000  1.000 32.54000  ? 64  ASP C N   1 
ATOM   3215 C CA  . ASP D 1 82  ? 25.80600  64.53000 37.15500  1.000 40.27000  ? 64  ASP C CA  1 
ATOM   3216 C C   . ASP D 1 82  ? 26.38300  64.23900 38.53500  1.000 41.21000  ? 64  ASP C C   1 
ATOM   3217 O O   . ASP D 1 82  ? 26.37300  65.13100 39.39100  1.000 46.56000  ? 64  ASP C O   1 
ATOM   3218 C CB  . ASP D 1 82  ? 24.30800  64.83300 37.28800  1.000 41.51000  ? 64  ASP C CB  1 
ATOM   3219 C CG  . ASP D 1 82  ? 23.69800  65.34000 35.99500  1.000 60.24000  ? 64  ASP C CG  1 
ATOM   3220 O OD1 . ASP D 1 82  ? 24.44300  65.90500 35.16700  1.000 60.60000  ? 64  ASP C OD1 1 
ATOM   3221 O OD2 . ASP D 1 82  ? 22.47400  65.17600 35.80800  1.000 60.80000  ? 64  ASP C OD2 1 
ATOM   3222 N N   . LEU D 1 83  ? 26.88200  63.03000 38.77200  1.000 35.93000  ? 65  LEU C N   1 
ATOM   3223 C CA  . LEU D 1 83  ? 27.40300  62.68600 40.08700  1.000 35.98000  ? 65  LEU C CA  1 
ATOM   3224 C C   . LEU D 1 83  ? 28.67500  63.47700 40.37900  1.000 51.93000  ? 65  LEU C C   1 
ATOM   3225 O O   . LEU D 1 83  ? 29.47700  63.72300 39.47200  1.000 46.57000  ? 65  LEU C O   1 
ATOM   3226 C CB  . LEU D 1 83  ? 27.69000  61.18700 40.17600  1.000 42.03000  ? 65  LEU C CB  1 
ATOM   3227 C CG  . LEU D 1 83  ? 26.47700  60.25600 40.22600  1.000 45.09000  ? 65  LEU C CG  1 
ATOM   3228 C CD1 . LEU D 1 83  ? 26.90100  58.79700 40.11900  1.000 30.51000  ? 65  LEU C CD1 1 
ATOM   3229 C CD2 . LEU D 1 83  ? 25.68100  60.49500 41.50000  1.000 39.89000  ? 65  LEU C CD2 1 
ATOM   3230 N N   . PRO D 1 84  ? 28.88700  63.90300 41.62500  1.000 46.23000  ? 66  PRO C N   1 
ATOM   3231 C CA  . PRO D 1 84  ? 30.14200  64.58300 41.99000  1.000 39.23000  ? 66  PRO C CA  1 
ATOM   3232 C C   . PRO D 1 84  ? 31.26800  63.59500 42.29200  1.000 39.56000  ? 66  PRO C C   1 
ATOM   3233 O O   . PRO D 1 84  ? 31.77500  63.50700 43.41300  1.000 48.97000  ? 66  PRO C O   1 
ATOM   3234 C CB  . PRO D 1 84  ? 29.72700  65.40000 43.21800  1.000 53.37000  ? 66  PRO C CB  1 
ATOM   3235 C CG  . PRO D 1 84  ? 28.67200  64.56800 43.86000  1.000 46.12000  ? 66  PRO C CG  1 
ATOM   3236 C CD  . PRO D 1 84  ? 27.91600  63.90200 42.73600  1.000 43.77000  ? 66  PRO C CD  1 
ATOM   3237 N N   . ILE D 1 85  ? 31.66200  62.83100 41.27600  1.000 47.84000  ? 67  ILE C N   1 
ATOM   3238 C CA  . ILE D 1 85  ? 32.70900  61.82900 41.39300  1.000 37.02000  ? 67  ILE C CA  1 
ATOM   3239 C C   . ILE D 1 85  ? 33.72100  62.05200 40.27400  1.000 38.34000  ? 67  ILE C C   1 
ATOM   3240 O O   . ILE D 1 85  ? 33.56900  62.94400 39.43900  1.000 40.19000  ? 67  ILE C O   1 
ATOM   3241 C CB  . ILE D 1 85  ? 32.15200  60.39100 41.35500  1.000 42.97000  ? 67  ILE C CB  1 
ATOM   3242 C CG1 . ILE D 1 85  ? 31.40800  60.13900 40.04200  1.000 34.92000  ? 67  ILE C CG1 1 
ATOM   3243 C CG2 . ILE D 1 85  ? 31.23900  60.13900 42.54800  1.000 44.71000  ? 67  ILE C CG2 1 
ATOM   3244 C CD1 . ILE D 1 85  ? 30.89500  58.72300 39.89300  1.000 39.70000  ? 67  ILE C CD1 1 
ATOM   3245 N N   . SER D 1 86  ? 34.75100  61.20800 40.26200  1.000 35.82000  ? 68  SER C N   1 
ATOM   3246 C CA  . SER D 1 86  ? 35.81000  61.24700 39.23100  1.000 33.18000  ? 68  SER C CA  1 
ATOM   3247 C C   . SER D 1 86  ? 35.22500  60.97600 37.85000  1.000 39.31000  ? 68  SER C C   1 
ATOM   3248 O O   . SER D 1 86  ? 34.34200  60.13500 37.74200  1.000 41.74000  ? 68  SER C O   1 
ATOM   3249 C CB  . SER D 1 86  ? 36.84800  60.23700 39.54800  1.000 33.77000  ? 68  SER C CB  1 
ATOM   3250 O OG  . SER D 1 86  ? 36.62800  59.03700 38.83600  1.000 61.65000  ? 68  SER C OG  1 
ATOM   3251 N N   . ASN D 1 87  ? 35.73100  61.67200 36.84300  1.000 28.70000  ? 69  ASN C N   1 
ATOM   3252 C CA  . ASN D 1 87  ? 35.25900  61.40200 35.49000  1.000 37.85000  ? 69  ASN C CA  1 
ATOM   3253 C C   . ASN D 1 87  ? 35.64100  60.00200 35.03500  1.000 41.17000  ? 69  ASN C C   1 
ATOM   3254 O O   . ASN D 1 87  ? 34.95300  59.41400 34.19300  1.000 40.31000  ? 69  ASN C O   1 
ATOM   3255 C CB  . ASN D 1 87  ? 35.80800  62.45200 34.52500  1.000 30.74000  ? 69  ASN C CB  1 
ATOM   3256 C CG  . ASN D 1 87  ? 35.16600  63.81100 34.71900  1.000 47.44000  ? 69  ASN C CG  1 
ATOM   3257 O OD1 . ASN D 1 87  ? 34.41600  64.02800 35.67100  1.000 60.92000  ? 69  ASN C OD1 1 
ATOM   3258 N ND2 . ASN D 1 87  ? 35.45900  64.73800 33.81400  1.000 56.77000  ? 69  ASN C ND2 1 
ATOM   3259 N N   . ASP D 1 88  ? 36.70200  59.44600 35.58600  1.000 39.84000  ? 70  ASP C N   1 
ATOM   3260 C CA  . ASP D 1 88  ? 37.09000  58.06200 35.23500  1.000 49.36000  ? 70  ASP C CA  1 
ATOM   3261 C C   . ASP D 1 88  ? 36.04400  57.08400 35.78200  1.000 45.46000  ? 70  ASP C C   1 
ATOM   3262 O O   . ASP D 1 88  ? 35.75400  56.11000 35.09800  1.000 49.81000  ? 70  ASP C O   1 
ATOM   3263 C CB  . ASP D 1 88  ? 38.52200  57.74900 35.68000  1.000 46.09000  ? 70  ASP C CB  1 
ATOM   3264 C CG  . ASP D 1 88  ? 39.59100  58.42300 34.84000  1.000 64.88000  ? 70  ASP C CG  1 
ATOM   3265 O OD1 . ASP D 1 88  ? 39.23100  59.07000 33.84300  1.000 49.84000  ? 70  ASP C OD1 1 
ATOM   3266 O OD2 . ASP D 1 88  ? 40.77200  58.30900 35.20600  1.000 56.50000  ? 70  ASP C OD2 1 
ATOM   3267 N N   . ALA D 1 89  ? 35.49700  57.35400 36.95900  1.000 45.03000  ? 71  ALA C N   1 
ATOM   3268 C CA  . ALA D 1 89  ? 34.43900  56.49400 37.48000  1.000 39.43000  ? 71  ALA C CA  1 
ATOM   3269 C C   . ALA D 1 89  ? 33.17900  56.61000 36.63500  1.000 43.91000  ? 71  ALA C C   1 
ATOM   3270 O O   . ALA D 1 89  ? 32.47400  55.61800 36.41500  1.000 44.68000  ? 71  ALA C O   1 
ATOM   3271 C CB  . ALA D 1 89  ? 34.14500  56.84400 38.93900  1.000 30.85000  ? 71  ALA C CB  1 
ATOM   3272 N N   . LYS D 1 90  ? 32.88300  57.81700 36.14900  1.000 37.35000  ? 72  LYS C N   1 
ATOM   3273 C CA  . LYS D 1 90  ? 31.73400  57.99600 35.26900  1.000 37.86000  ? 72  LYS C CA  1 
ATOM   3274 C C   . LYS D 1 90  ? 31.90100  57.20400 33.98100  1.000 37.24000  ? 72  LYS C C   1 
ATOM   3275 O O   . LYS D 1 90  ? 30.96200  56.54100 33.52300  1.000 45.25000  ? 72  LYS C O   1 
ATOM   3276 C CB  . LYS D 1 90  ? 31.53600  59.47800 34.95700  1.000 34.79000  ? 72  LYS C CB  1 
ATOM   3277 C CG  . LYS D 1 90  ? 31.30300  60.34900 36.17500  1.000 39.86000  ? 72  LYS C CG  1 
ATOM   3278 C CD  . LYS D 1 90  ? 31.02700  61.77700 35.74700  1.000 36.02000  ? 72  LYS C CD  1 
ATOM   3279 C CE  . LYS D 1 90  ? 30.88800  62.69400 36.93500  1.000 30.74000  ? 72  LYS C CE  1 
ATOM   3280 N NZ  . LYS D 1 90  ? 30.51000  64.06500 36.50200  1.000 48.42000  ? 72  LYS C NZ  1 
ATOM   3281 N N   . LYS D 1 91  ? 33.10800  57.24000 33.42200  1.000 41.24000  ? 73  LYS C N   1 
ATOM   3282 C CA  . LYS D 1 91  ? 33.38200  56.51700 32.15300  1.000 44.97000  ? 73  LYS C CA  1 
ATOM   3283 C C   . LYS D 1 91  ? 33.27100  55.01300 32.40400  1.000 33.48000  ? 73  LYS C C   1 
ATOM   3284 O O   . LYS D 1 91  ? 32.71100  54.31600 31.54900  1.000 40.59000  ? 73  LYS C O   1 
ATOM   3285 C CB  . LYS D 1 91  ? 34.76500  56.90900 31.62700  1.000 46.87000  ? 73  LYS C CB  1 
ATOM   3286 C CG  . LYS D 1 91  ? 35.22700  56.16500 30.38300  1.000 72.10000  ? 73  LYS C CG  1 
ATOM   3287 C CD  . LYS D 1 91  ? 36.59600  56.60000 29.91400  1.000 72.81000  ? 73  LYS C CD  1 
ATOM   3288 C CE  . LYS D 1 91  ? 37.11600  55.75300 28.77400  1.000 76.08000  ? 73  LYS C CE  1 
ATOM   3289 N NZ  . LYS D 1 91  ? 36.12000  55.65300 27.68300  1.000 81.11000  ? 73  LYS C NZ  1 
ATOM   3290 N N   . LEU D 1 92  ? 33.77300  54.55000 33.54700  1.000 36.40000  ? 74  LEU C N   1 
ATOM   3291 C CA  . LEU D 1 92  ? 33.68900  53.13100 33.87400  1.000 46.34000  ? 74  LEU C CA  1 
ATOM   3292 C C   . LEU D 1 92  ? 32.23900  52.69300 34.03500  1.000 48.13000  ? 74  LEU C C   1 
ATOM   3293 O O   . LEU D 1 92  ? 31.86100  51.59600 33.60600  1.000 46.53000  ? 74  LEU C O   1 
ATOM   3294 C CB  . LEU D 1 92  ? 34.48500  52.83700 35.14500  1.000 38.76000  ? 74  LEU C CB  1 
ATOM   3295 C CG  . LEU D 1 92  ? 34.64600  51.36400 35.52400  1.000 53.03000  ? 74  LEU C CG  1 
ATOM   3296 C CD1 . LEU D 1 92  ? 35.48400  50.63500 34.48400  1.000 60.92000  ? 74  LEU C CD1 1 
ATOM   3297 C CD2 . LEU D 1 92  ? 35.26000  51.22500 36.90800  1.000 68.63000  ? 74  LEU C CD2 1 
ATOM   3298 N N   . MET D 1 93  ? 31.40800  53.54200 34.64400  1.000 41.58000  ? 75  MET C N   1 
ATOM   3299 C CA  . MET D 1 93  ? 29.99300  53.21700 34.78800  1.000 42.82000  ? 75  MET C CA  1 
ATOM   3300 C C   . MET D 1 93  ? 29.26200  53.31800 33.45500  1.000 42.31000  ? 75  MET C C   1 
ATOM   3301 O O   . MET D 1 93  ? 28.42100  52.47100 33.13700  1.000 50.80000  ? 75  MET C O   1 
ATOM   3302 C CB  . MET D 1 93  ? 29.34200  54.13500 35.82200  1.000 42.32000  ? 75  MET C CB  1 
ATOM   3303 C CG  . MET D 1 93  ? 29.87700  53.96700 37.23300  1.000 57.56000  ? 75  MET C CG  1 
ATOM   3304 S SD  . MET D 1 93  ? 29.03300  55.03200 38.41700  1.000 55.55000  ? 75  MET C SD  1 
ATOM   3305 C CE  . MET D 1 93  ? 29.98600  54.70800 39.89500  1.000 55.05000  ? 75  MET C CE  1 
ATOM   3306 N N   . SER D 1 94  ? 29.57000  54.34700 32.66100  1.000 37.08000  ? 76  SER C N   1 
ATOM   3307 C CA  . SER D 1 94  ? 28.86300  54.54600 31.40000  1.000 36.05000  ? 76  SER C CA  1 
ATOM   3308 C C   . SER D 1 94  ? 29.20100  53.46300 30.38200  1.000 39.49000  ? 76  SER C C   1 
ATOM   3309 O O   . SER D 1 94  ? 28.37300  53.14600 29.52100  1.000 45.45000  ? 76  SER C O   1 
ATOM   3310 C CB  . SER D 1 94  ? 29.18200  55.93000 30.83100  1.000 38.19000  ? 76  SER C CB  1 
ATOM   3311 O OG  . SER D 1 94  ? 28.75900  56.95500 31.71400  1.000 50.44000  ? 76  SER C OG  1 
ATOM   3312 N N   . ASN D 1 95  ? 30.37800  52.85100 30.50900  1.000 38.46000  ? 77  ASN C N   1 
ATOM   3313 C CA  . ASN D 1 95  ? 30.82100  51.83600 29.51600  1.000 48.76000  ? 77  ASN C CA  1 
ATOM   3314 C C   . ASN D 1 95  ? 30.28100  50.44500 29.87300  1.000 49.94000  ? 77  ASN C C   1 
ATOM   3315 O O   . ASN D 1 95  ? 30.35900  49.55800 29.01200  1.000 49.47000  ? 77  ASN C O   1 
ATOM   3316 C CB  . ASN D 1 95  ? 32.34300  51.83900 29.35900  1.000 42.69000  ? 77  ASN C CB  1 
ATOM   3317 C CG  . ASN D 1 95  ? 32.84900  52.99700 28.52600  1.000 57.83000  ? 77  ASN C CG  1 
ATOM   3318 O OD1 . ASN D 1 95  ? 32.06200  53.77700 27.99500  1.000 58.81000  ? 77  ASN C OD1 1 
ATOM   3319 N ND2 . ASN D 1 95  ? 34.15900  53.11100 28.39800  1.000 56.32000  ? 77  ASN C ND2 1 
ATOM   3320 N N   . ASN D 1 96  ? 29.75500  50.26400 31.08600  1.000 46.26000  ? 78  ASN C N   1 
ATOM   3321 C CA  . ASN D 1 96  ? 29.28100  48.95000 31.49400  1.000 37.57000  ? 78  ASN C CA  1 
ATOM   3322 C C   . ASN D 1 96  ? 27.84700  48.93300 32.00500  1.000 39.33000  ? 78  ASN C C   1 
ATOM   3323 O O   . ASN D 1 96  ? 27.36600  47.86500 32.39900  1.000 50.82000  ? 78  ASN C O   1 
ATOM   3324 C CB  . ASN D 1 96  ? 30.20100  48.36200 32.57700  1.000 38.58000  ? 78  ASN C CB  1 
ATOM   3325 C CG  . ASN D 1 96  ? 31.63500  48.22000 32.10900  1.000 53.08000  ? 78  ASN C CG  1 
ATOM   3326 O OD1 . ASN D 1 96  ? 31.98700  47.25400 31.43000  1.000 41.97000  ? 78  ASN C OD1 1 
ATOM   3327 N ND2 . ASN D 1 96  ? 32.47500  49.18200 32.47400  1.000 48.29000  ? 78  ASN C ND2 1 
ATOM   3328 N N   . ILE D 1 97  ? 27.14600  50.05800 32.01700  1.000 44.09000  ? 79  ILE C N   1 
ATOM   3329 C CA  . ILE D 1 97  ? 25.76700  50.08600 32.58700  1.000 46.30000  ? 79  ILE C CA  1 
ATOM   3330 C C   . ILE D 1 97  ? 24.84400  49.22200 31.72100  1.000 62.88000  ? 79  ILE C C   1 
ATOM   3331 O O   . ILE D 1 97  ? 23.91600  48.62900 32.27100  1.000 49.19000  ? 79  ILE C O   1 
ATOM   3332 C CB  . ILE D 1 97  ? 25.23200  51.52600 32.71200  1.000 59.27000  ? 79  ILE C CB  1 
ATOM   3333 C CG1 . ILE D 1 97  ? 23.89500  51.58700 33.45100  1.000 59.97000  ? 79  ILE C CG1 1 
ATOM   3334 C CG2 . ILE D 1 97  ? 25.14600  52.20600 31.35600  1.000 58.69000  ? 79  ILE C CG2 1 
ATOM   3335 C CD1 . ILE D 1 97  ? 23.32300  52.97400 33.53300  1.000 54.79000  ? 79  ILE C CD1 1 
ATOM   3336 N N   . HIS D 1 98  ? 25.10300  49.15500 30.41400  1.000 52.14000  ? 80  HIS C N   1 
ATOM   3337 C CA  . HIS D 1 98  ? 24.20400  48.40900 29.53900  1.000 44.05000  ? 80  HIS C CA  1 
ATOM   3338 C C   . HIS D 1 98  ? 24.14400  46.93700 29.91900  1.000 58.00000  ? 80  HIS C C   1 
ATOM   3339 O O   . HIS D 1 98  ? 23.15000  46.26100 29.62800  1.000 50.08000  ? 80  HIS C O   1 
ATOM   3340 C CB  . HIS D 1 98  ? 24.64800  48.55800 28.08500  1.000 46.95000  ? 80  HIS C CB  1 
ATOM   3341 C CG  . HIS D 1 98  ? 25.93700  47.86200 27.77800  1.000 52.48000  ? 80  HIS C CG  1 
ATOM   3342 N ND1 . HIS D 1 98  ? 27.16700  48.42900 28.03200  1.000 52.85000  ? 80  HIS C ND1 1 
ATOM   3343 C CD2 . HIS D 1 98  ? 26.18700  46.64300 27.24400  1.000 53.12000  ? 80  HIS C CD2 1 
ATOM   3344 C CE1 . HIS D 1 98  ? 28.12000  47.59000 27.66500  1.000 54.42000  ? 80  HIS C CE1 1 
ATOM   3345 N NE2 . HIS D 1 98  ? 27.55200  46.49900 27.18400  1.000 55.61000  ? 80  HIS C NE2 1 
ATOM   3346 N N   . LYS D 1 99  ? 25.19400  46.42200 30.56400  1.000 44.92000  ? 81  LYS C N   1 
ATOM   3347 C CA  . LYS D 1 99  ? 25.20600  45.02000 30.96400  1.000 42.40000  ? 81  LYS C CA  1 
ATOM   3348 C C   . LYS D 1 99  ? 24.14500  44.72700 32.01700  1.000 65.72000  ? 81  LYS C C   1 
ATOM   3349 O O   . LYS D 1 99  ? 23.63800  43.60300 32.08800  1.000 64.18000  ? 81  LYS C O   1 
ATOM   3350 C CB  . LYS D 1 99  ? 26.59300  44.63800 31.47800  1.000 50.55000  ? 81  LYS C CB  1 
ATOM   3351 C CG  . LYS D 1 99  ? 27.70600  44.90500 30.47600  1.000 48.92000  ? 81  LYS C CG  1 
ATOM   3352 C CD  . LYS D 1 99  ? 29.07200  44.54800 31.03600  1.000 49.42000  ? 81  LYS C CD  1 
ATOM   3353 C CE  . LYS D 1 99  ? 30.16200  44.80700 30.00800  1.000 52.53000  ? 81  LYS C CE  1 
ATOM   3354 N NZ  . LYS D 1 99  ? 31.51200  44.43700 30.51400  1.000 59.04000  ? 81  LYS C NZ  1 
ATOM   3355 N N   . ALA D 1 100 ? 23.73000  45.73500 32.76800  1.000 43.98000  ? 82  ALA C N   1 
ATOM   3356 C CA  . ALA D 1 100 ? 22.72400  45.51500 33.82000  1.000 50.73000  ? 82  ALA C CA  1 
ATOM   3357 C C   . ALA D 1 100 ? 21.32700  45.33700 33.22000  1.000 67.43000  ? 82  ALA C C   1 
ATOM   3358 O O   . ALA D 1 100 ? 20.39600  45.04400 33.97500  1.000 56.23000  ? 82  ALA C O   1 
ATOM   3359 C CB  . ALA D 1 100 ? 22.75400  46.65600 34.78400  1.000 60.74000  ? 82  ALA C CB  1 
ATOM   3360 N N   . LEU D 1 101 ? 21.20100  45.49900 31.91000  1.000 54.85000  ? 83  LEU C N   1 
ATOM   3361 C CA  . LEU D 1 101 ? 19.86700  45.41100 31.27400  1.000 67.20000  ? 83  LEU C CA  1 
ATOM   3362 C C   . LEU D 1 101 ? 19.50400  43.94100 31.02800  1.000 71.66000  ? 83  LEU C C   1 
ATOM   3363 O O   . LEU D 1 101 ? 18.33600  43.66900 30.73700  1.000 60.02000  ? 83  LEU C O   1 
ATOM   3364 C CB  . LEU D 1 101 ? 19.89300  46.23200 29.98700  1.000 46.76000  ? 83  LEU C CB  1 
ATOM   3365 C CG  . LEU D 1 101 ? 19.97800  47.74200 30.18600  1.000 63.10000  ? 83  LEU C CG  1 
ATOM   3366 C CD1 . LEU D 1 101 ? 20.29100  48.44000 28.87500  1.000 52.71000  ? 83  LEU C CD1 1 
ATOM   3367 C CD2 . LEU D 1 101 ? 18.68300  48.27500 30.77200  1.000 50.68000  ? 83  LEU C CD2 1 
ATOM   3368 N N   . GLU D 1 102 ? 20.45900  43.02900 31.19600  1.000 72.15000  ? 84  GLU C N   1 
ATOM   3369 C CA  . GLU D 1 102 ? 20.13200  41.62000 31.03000  1.000 68.78000  ? 84  GLU C CA  1 
ATOM   3370 C C   . GLU D 1 102 ? 19.58800  41.05200 32.33900  1.000 67.83000  ? 84  GLU C C   1 
ATOM   3371 O O   . GLU D 1 102 ? 20.06300  41.41700 33.41800  1.000 64.70000  ? 84  GLU C O   1 
ATOM   3372 C CB  . GLU D 1 102 ? 21.36300  40.83000 30.58800  1.000 67.61000  ? 84  GLU C CB  1 
ATOM   3373 C CG  . GLU D 1 102 ? 21.98400  41.32300 29.28900  1.000 74.46000  ? 84  GLU C CG  1 
ATOM   3374 C CD  . GLU D 1 102 ? 21.04500  41.19700 28.10300  1.000 97.78000  ? 84  GLU C CD  1 
ATOM   3375 O OE1 . GLU D 1 102 ? 20.19400  40.28300 28.10500  1.000 104.97000 ? 84  GLU C OE1 1 
ATOM   3376 O OE2 . GLU D 1 102 ? 21.15800  42.01700 27.16600  1.000 99.34000  ? 84  GLU C OE2 1 
ATOM   3377 N N   . PRO D 1 103 ? 18.59300  40.16700 32.27300  1.000 79.29000  ? 85  PRO C N   1 
ATOM   3378 C CA  . PRO D 1 103 ? 17.99900  39.63100 33.50400  1.000 76.37000  ? 85  PRO C CA  1 
ATOM   3379 C C   . PRO D 1 103 ? 19.01500  38.85500 34.33000  1.000 60.55000  ? 85  PRO C C   1 
ATOM   3380 O O   . PRO D 1 103 ? 19.80000  38.06400 33.80400  1.000 47.26000  ? 85  PRO C O   1 
ATOM   3381 C CB  . PRO D 1 103 ? 16.88000  38.71700 32.99000  1.000 79.81000  ? 85  PRO C CB  1 
ATOM   3382 C CG  . PRO D 1 103 ? 16.58100  39.21300 31.61400  1.000 80.63000  ? 85  PRO C CG  1 
ATOM   3383 C CD  . PRO D 1 103 ? 17.88900  39.69800 31.06800  1.000 83.92000  ? 85  PRO C CD  1 
ATOM   3384 N N   . GLY D 1 104 ? 18.98900  39.09200 35.64000  1.000 54.88000  ? 86  GLY C N   1 
ATOM   3385 C CA  . GLY D 1 104 ? 19.85500  38.39600 36.56700  1.000 73.03000  ? 86  GLY C CA  1 
ATOM   3386 C C   . GLY D 1 104 ? 21.26800  38.92500 36.66400  1.000 83.44000  ? 86  GLY C C   1 
ATOM   3387 O O   . GLY D 1 104 ? 22.03500  38.43600 37.50400  1.000 79.29000  ? 86  GLY C O   1 
ATOM   3388 N N   . ARG D 1 105 ? 21.63900  39.90300 35.84400  1.000 61.41000  ? 87  ARG C N   1 
ATOM   3389 C CA  . ARG D 1 105 ? 22.98900  40.44700 35.83900  1.000 59.13000  ? 87  ARG C CA  1 
ATOM   3390 C C   . ARG D 1 105 ? 23.03200  41.72000 36.67400  1.000 53.36000  ? 87  ARG C C   1 
ATOM   3391 O O   . ARG D 1 105 ? 22.19500  42.61200 36.50000  1.000 60.09000  ? 87  ARG C O   1 
ATOM   3392 C CB  . ARG D 1 105 ? 23.45800  40.73000 34.41200  1.000 60.50000  ? 87  ARG C CB  1 
ATOM   3393 C CG  . ARG D 1 105 ? 24.96800  40.74200 34.25500  1.000 81.81000  ? 87  ARG C CG  1 
ATOM   3394 C CD  . ARG D 1 105 ? 25.37900  41.14100 32.84900  1.000 87.78000  ? 87  ARG C CD  1 
ATOM   3395 N NE  . ARG D 1 105 ? 24.82500  40.26200 31.82600  1.000 103.94000 ? 87  ARG C NE  1 
ATOM   3396 C CZ  . ARG D 1 105 ? 25.49900  39.28900 31.23000  1.000 105.66000 ? 87  ARG C CZ  1 
ATOM   3397 N NH1 . ARG D 1 105 ? 26.75500  39.02300 31.54800  1.000 103.13000 ? 87  ARG C NH1 1 
ATOM   3398 N NH2 . ARG D 1 105 ? 24.90100  38.56800 30.28600  1.000 112.67000 ? 87  ARG C NH2 1 
ATOM   3399 N N   . THR D 1 106 ? 23.97900  41.76500 37.60200  1.000 54.12000  ? 88  THR C N   1 
ATOM   3400 C CA  . THR D 1 106 ? 24.14800  42.94800 38.47400  1.000 60.00000  ? 88  THR C CA  1 
ATOM   3401 C C   . THR D 1 106 ? 25.56200  43.49700 38.27500  1.000 69.50000  ? 88  THR C C   1 
ATOM   3402 O O   . THR D 1 106 ? 26.49500  42.70500 38.12300  1.000 55.73000  ? 88  THR C O   1 
ATOM   3403 C CB  . THR D 1 106 ? 23.87300  42.61000 39.94100  1.000 63.46000  ? 88  THR C CB  1 
ATOM   3404 O OG1 . THR D 1 106 ? 22.49300  42.27600 40.06200  1.000 65.91000  ? 88  THR C OG1 1 
ATOM   3405 C CG2 . THR D 1 106 ? 24.19500  43.74700 40.88400  1.000 55.20000  ? 88  THR C CG2 1 
ATOM   3406 N N   . VAL D 1 107 ? 25.68500  44.81700 38.22700  1.000 58.48000  ? 89  VAL C N   1 
ATOM   3407 C CA  . VAL D 1 107 ? 27.01400  45.45900 38.07400  1.000 54.74000  ? 89  VAL C CA  1 
ATOM   3408 C C   . VAL D 1 107 ? 27.25100  46.29600 39.32600  1.000 46.54000  ? 89  VAL C C   1 
ATOM   3409 O O   . VAL D 1 107 ? 26.33500  47.00100 39.74900  1.000 48.32000  ? 89  VAL C O   1 
ATOM   3410 C CB  . VAL D 1 107 ? 27.13400  46.26800 36.77000  1.000 51.19000  ? 89  VAL C CB  1 
ATOM   3411 C CG1 . VAL D 1 107 ? 28.57300  46.66400 36.49600  1.000 40.97000  ? 89  VAL C CG1 1 
ATOM   3412 C CG2 . VAL D 1 107 ? 26.56900  45.50000 35.58900  1.000 61.69000  ? 89  VAL C CG2 1 
ATOM   3413 N N   . VAL D 1 108 ? 28.43900  46.17600 39.89400  1.000 51.89000  ? 90  VAL C N   1 
ATOM   3414 C CA  . VAL D 1 108 ? 28.78000  46.86600 41.13000  1.000 49.05000  ? 90  VAL C CA  1 
ATOM   3415 C C   . VAL D 1 108 ? 30.00600  47.73200 40.88100  1.000 44.72000  ? 90  VAL C C   1 
ATOM   3416 O O   . VAL D 1 108 ? 30.93800  47.31400 40.18800  1.000 50.05000  ? 90  VAL C O   1 
ATOM   3417 C CB  . VAL D 1 108 ? 29.03700  45.86700 42.27800  1.000 58.28000  ? 90  VAL C CB  1 
ATOM   3418 C CG1 . VAL D 1 108 ? 29.14700  46.59300 43.60600  1.000 46.92000  ? 90  VAL C CG1 1 
ATOM   3419 C CG2 . VAL D 1 108 ? 27.93700  44.81600 42.32400  1.000 43.23000  ? 90  VAL C CG2 1 
ATOM   3420 N N   . PHE D 1 109 ? 30.01200  48.91300 41.47800  1.000 47.50000  ? 91  PHE C N   1 
ATOM   3421 C CA  . PHE D 1 109 ? 31.14500  49.85600 41.35400  1.000 47.43000  ? 91  PHE C CA  1 
ATOM   3422 C C   . PHE D 1 109 ? 31.46500  50.37100 42.75700  1.000 40.40000  ? 91  PHE C C   1 
ATOM   3423 O O   . PHE D 1 109 ? 30.59600  50.95200 43.39400  1.000 44.76000  ? 91  PHE C O   1 
ATOM   3424 C CB  . PHE D 1 109 ? 30.78500  50.98200 40.39000  1.000 41.75000  ? 91  PHE C CB  1 
ATOM   3425 C CG  . PHE D 1 109 ? 30.45000  50.58800 38.97600  1.000 47.63000  ? 91  PHE C CG  1 
ATOM   3426 C CD1 . PHE D 1 109 ? 31.44900  50.31400 38.05900  1.000 40.33000  ? 91  PHE C CD1 1 
ATOM   3427 C CD2 . PHE D 1 109 ? 29.13300  50.50900 38.55800  1.000 39.29000  ? 91  PHE C CD2 1 
ATOM   3428 C CE1 . PHE D 1 109 ? 31.14000  49.97100 36.75500  1.000 36.47000  ? 91  PHE C CE1 1 
ATOM   3429 C CE2 . PHE D 1 109 ? 28.82600  50.15700 37.25500  1.000 57.60000  ? 91  PHE C CE2 1 
ATOM   3430 C CZ  . PHE D 1 109 ? 29.82900  49.89200 36.35700  1.000 52.94000  ? 91  PHE C CZ  1 
ATOM   3431 N N   . GLY D 1 110 ? 32.67400  50.12400 43.22400  1.000 40.49000  ? 92  GLY C N   1 
ATOM   3432 C CA  . GLY D 1 110 ? 33.06300  50.50200 44.56300  1.000 48.32000  ? 92  GLY C CA  1 
ATOM   3433 C C   . GLY D 1 110 ? 34.50900  50.94300 44.67400  1.000 52.02000  ? 92  GLY C C   1 
ATOM   3434 O O   . GLY D 1 110 ? 35.20900  51.12600 43.67300  1.000 44.90000  ? 92  GLY C O   1 
ATOM   3435 N N   . PRO D 1 111 ? 35.01500  51.15600 45.90900  1.000 52.41000  ? 93  PRO C N   1 
ATOM   3436 C CA  . PRO D 1 111 ? 36.39000  51.60200 46.09500  1.000 61.18000  ? 93  PRO C CA  1 
ATOM   3437 C C   . PRO D 1 111 ? 37.44500  50.63800 45.53400  1.000 59.90000  ? 93  PRO C C   1 
ATOM   3438 O O   . PRO D 1 111 ? 38.50000  51.09700 45.19000  1.000 55.73000  ? 93  PRO C O   1 
ATOM   3439 C CB  . PRO D 1 111 ? 36.49200  51.67300 47.62100  1.000 53.62000  ? 93  PRO C CB  1 
ATOM   3440 C CG  . PRO D 1 111 ? 35.09800  51.95800 48.07700  1.000 55.29000  ? 93  PRO C CG  1 
ATOM   3441 C CD  . PRO D 1 111 ? 34.29500  51.04600 47.18800  1.000 52.61000  ? 93  PRO C CD  1 
ATOM   3442 N N   . GLU D 1 112 ? 37.13100  49.34000 45.50200  1.000 67.91000  ? 94  GLU C N   1 
ATOM   3443 C CA  . GLU D 1 112 ? 38.09400  48.30800 45.03100  1.000 67.91000  ? 94  GLU C CA  1 
ATOM   3444 C C   . GLU D 1 112 ? 37.92900  48.10100 43.52600  1.000 72.42000  ? 94  GLU C C   1 
ATOM   3445 O O   . GLU D 1 112 ? 38.82800  47.50000 42.91200  1.000 69.85000  ? 94  GLU C O   1 
ATOM   3446 C CB  . GLU D 1 112 ? 37.85500  46.99200 45.76900  1.000 72.68000  ? 94  GLU C CB  1 
ATOM   3447 C CG  . GLU D 1 112 ? 38.01900  47.10900 47.27300  1.000 93.32000  ? 94  GLU C CG  1 
ATOM   3448 N N   . GLY D 1 113 ? 36.81800  48.57000 42.96200  1.000 59.98000  ? 95  GLY C N   1 
ATOM   3449 C CA  . GLY D 1 113 ? 36.64500  48.48300 41.50400  1.000 55.62000  ? 95  GLY C CA  1 
ATOM   3450 C C   . GLY D 1 113 ? 35.26200  48.01200 41.11900  1.000 63.65000  ? 95  GLY C C   1 
ATOM   3451 O O   . GLY D 1 113 ? 34.32700  48.22000 41.90700  1.000 66.08000  ? 95  GLY C O   1 
ATOM   3452 N N   . CYS D 1 114 ? 35.14600  47.39500 39.94500  1.000 65.62000  ? 96  CYS C N   1 
ATOM   3453 C CA  . CYS D 1 114 ? 33.85000  46.95000 39.46200  1.000 68.79000  ? 96  CYS C CA  1 
ATOM   3454 C C   . CYS D 1 114 ? 33.74700  45.43100 39.51800  1.000 73.70000  ? 96  CYS C C   1 
ATOM   3455 O O   . CYS D 1 114 ? 34.75100  44.71300 39.54300  1.000 52.57000  ? 96  CYS C O   1 
ATOM   3456 C CB  . CYS D 1 114 ? 33.59500  47.44800 38.03600  1.000 63.07000  ? 96  CYS C CB  1 
ATOM   3457 S SG  . CYS D 1 114 ? 34.97600  47.22000 36.90300  1.000 91.67000  ? 96  CYS C SG  1 
ATOM   3458 N N   . GLU D 1 115 ? 32.50600  44.94900 39.53900  1.000 64.80000  ? 97  GLU C N   1 
ATOM   3459 C CA  . GLU D 1 115 ? 32.23100  43.52100 39.65900  1.000 56.14000  ? 97  GLU C CA  1 
ATOM   3460 C C   . GLU D 1 115 ? 30.94900  43.20900 38.90300  1.000 59.04000  ? 97  GLU C C   1 
ATOM   3461 O O   . GLU D 1 115 ? 29.90600  43.80900 39.17900  1.000 62.47000  ? 97  GLU C O   1 
ATOM   3462 C CB  . GLU D 1 115 ? 32.10800  43.11100 41.12800  1.000 61.09000  ? 97  GLU C CB  1 
ATOM   3463 C CG  . GLU D 1 115 ? 31.81700  41.63500 41.35000  1.000 77.07000  ? 97  GLU C CG  1 
ATOM   3464 C CD  . GLU D 1 115 ? 31.70400  41.28000 42.82100  1.000 78.40000  ? 97  GLU C CD  1 
ATOM   3465 O OE1 . GLU D 1 115 ? 32.00600  42.14600 43.66900  1.000 98.10000  ? 97  GLU C OE1 1 
ATOM   3466 O OE2 . GLU D 1 115 ? 31.30900  40.13500 43.13000  1.000 85.59000  ? 97  GLU C OE2 1 
ATOM   3467 N N   . GLU D 1 116 ? 31.04900  42.30700 37.92500  1.000 50.58000  ? 98  GLU C N   1 
ATOM   3468 C CA  . GLU D 1 116 ? 29.86400  41.89800 37.13000  1.000 46.16000  ? 98  GLU C CA  1 
ATOM   3469 C C   . GLU D 1 116 ? 29.38900  40.53300 37.63200  1.000 60.18000  ? 98  GLU C C   1 
ATOM   3470 O O   . GLU D 1 116 ? 30.18600  39.58300 37.58700  1.000 59.21000  ? 98  GLU C O   1 
ATOM   3471 C CB  . GLU D 1 116 ? 30.22700  41.84900 35.64900  1.000 51.71000  ? 98  GLU C CB  1 
ATOM   3472 C CG  . GLU D 1 116 ? 29.08500  41.40900 34.75300  1.000 66.94000  ? 98  GLU C CG  1 
ATOM   3473 C CD  . GLU D 1 116 ? 29.45300  41.33300 33.28200  1.000 75.17000  ? 98  GLU C CD  1 
ATOM   3474 O OE1 . GLU D 1 116 ? 30.61100  41.64800 32.94900  1.000 74.88000  ? 98  GLU C OE1 1 
ATOM   3475 O OE2 . GLU D 1 116 ? 28.58500  40.95500 32.47500  1.000 88.91000  ? 98  GLU C OE2 1 
ATOM   3476 N N   . ARG D 1 117 ? 28.14300  40.44900 38.09800  1.000 62.21000  ? 99  ARG C N   1 
ATOM   3477 C CA  . ARG D 1 117 ? 27.62400  39.18200 38.67300  1.000 70.05000  ? 99  ARG C CA  1 
ATOM   3478 C C   . ARG D 1 117 ? 26.49600  38.64100 37.79100  1.000 82.97000  ? 99  ARG C C   1 
ATOM   3479 O O   . ARG D 1 117 ? 25.44300  39.29000 37.72600  1.000 89.94000  ? 99  ARG C O   1 
ATOM   3480 C CB  . ARG D 1 117 ? 27.14600  39.42200 40.10600  1.000 75.46000  ? 99  ARG C CB  1 
ATOM   3481 C CG  . ARG D 1 117 ? 28.19000  40.07300 41.00100  1.000 81.80000  ? 99  ARG C CG  1 
ATOM   3482 C CD  . ARG D 1 117 ? 27.62000  40.56200 42.31800  1.000 83.48000  ? 99  ARG C CD  1 
ATOM   3483 N NE  . ARG D 1 117 ? 28.62600  41.27000 43.09300  1.000 113.22000 ? 99  ARG C NE  1 
ATOM   3484 C CZ  . ARG D 1 117 ? 28.41300  41.83900 44.27300  1.000 103.28000 ? 99  ARG C CZ  1 
ATOM   3485 N NH1 . ARG D 1 117 ? 27.22300  41.76300 44.84100  1.000 95.37000  ? 99  ARG C NH1 1 
ATOM   3486 N NH2 . ARG D 1 117 ? 29.39200  42.48800 44.87900  1.000 82.33000  ? 99  ARG C NH2 1 
ATOM   3487 N N   . ASP D 1 118 ? 26.72200  37.49600 37.14400  1.000 74.98000  ? 100 ASP C N   1 
ATOM   3488 C CA  . ASP D 1 118 ? 25.68200  36.85400 36.29500  1.000 87.58000  ? 100 ASP C CA  1 
ATOM   3489 C C   . ASP D 1 118 ? 25.12600  35.64500 37.04900  1.000 84.33000  ? 100 ASP C C   1 
ATOM   3490 O O   . ASP D 1 118 ? 25.76700  34.58300 37.00200  1.000 88.37000  ? 100 ASP C O   1 
ATOM   3491 C CB  . ASP D 1 118 ? 26.24600  36.45500 34.92900  1.000 89.86000  ? 100 ASP C CB  1 
ATOM   3492 C CG  . ASP D 1 118 ? 25.18600  36.05100 33.92000  1.000 96.20000  ? 100 ASP C CG  1 
ATOM   3493 O OD1 . ASP D 1 118 ? 24.42300  35.11200 34.21300  1.000 91.96000  ? 100 ASP C OD1 1 
ATOM   3494 O OD2 . ASP D 1 118 ? 25.14100  36.67100 32.84300  1.000 88.36000  ? 100 ASP C OD2 1 
ATOM   3495 N N   . LYS D 1 119 ? 23.97800  35.80500 37.70800  1.000 89.30000  ? 101 LYS C N   1 
ATOM   3496 C CA  . LYS D 1 119 ? 23.41500  34.70900 38.54000  1.000 100.46000 ? 101 LYS C CA  1 
ATOM   3497 C C   . LYS D 1 119 ? 22.94700  33.56000 37.64200  1.000 97.95000  ? 101 LYS C C   1 
ATOM   3498 O O   . LYS D 1 119 ? 23.22300  32.39700 37.98400  1.000 91.56000  ? 101 LYS C O   1 
ATOM   3499 C CB  . LYS D 1 119 ? 22.26700  35.24100 39.40300  1.000 95.86000  ? 101 LYS C CB  1 
ATOM   3500 N N   . ASN D 1 120 ? 22.27400  33.87600 36.53700  1.000 90.25000  ? 102 ASN C N   1 
ATOM   3501 C CA  . ASN D 1 120 ? 21.73900  32.82500 35.68000  1.000 95.18000  ? 102 ASN C CA  1 
ATOM   3502 C C   . ASN D 1 120 ? 22.82400  31.93100 35.09100  1.000 92.13000  ? 102 ASN C C   1 
ATOM   3503 O O   . ASN D 1 120 ? 22.50400  30.84900 34.58800  1.000 102.51000 ? 102 ASN C O   1 
ATOM   3504 C CB  . ASN D 1 120 ? 20.90900  33.44000 34.55100  1.000 94.90000  ? 102 ASN C CB  1 
ATOM   3505 C CG  . ASN D 1 120 ? 19.73400  34.24600 35.06400  1.000 92.09000  ? 102 ASN C CG  1 
ATOM   3506 O OD1 . ASN D 1 120 ? 19.31900  34.09700 36.21400  1.000 92.13000  ? 102 ASN C OD1 1 
ATOM   3507 N ND2 . ASN D 1 120 ? 19.18800  35.10400 34.21000  1.000 80.35000  ? 102 ASN C ND2 1 
ATOM   3508 N N   . ARG D 1 121 ? 24.08900  32.35000 35.13400  1.000 82.87000  ? 103 ARG C N   1 
ATOM   3509 C CA  . ARG D 1 121 ? 25.18300  31.54300 34.61800  1.000 83.53000  ? 103 ARG C CA  1 
ATOM   3510 C C   . ARG D 1 121 ? 26.25700  31.25400 35.65800  1.000 76.66000  ? 103 ARG C C   1 
ATOM   3511 O O   . ARG D 1 121 ? 27.27700  30.64100 35.31800  1.000 81.57000  ? 103 ARG C O   1 
ATOM   3512 C CB  . ARG D 1 121 ? 25.81200  32.22800 33.39700  1.000 82.02000  ? 103 ARG C CB  1 
ATOM   3513 C CG  . ARG D 1 121 ? 24.89000  32.29500 32.19000  1.000 80.20000  ? 103 ARG C CG  1 
ATOM   3514 C CD  . ARG D 1 121 ? 25.30500  33.40400 31.24000  1.000 93.45000  ? 103 ARG C CD  1 
ATOM   3515 N NE  . ARG D 1 121 ? 26.71100  33.30900 30.86600  1.000 86.86000  ? 103 ARG C NE  1 
ATOM   3516 C CZ  . ARG D 1 121 ? 27.30900  34.11700 30.00200  1.000 101.53000 ? 103 ARG C CZ  1 
ATOM   3517 N NH1 . ARG D 1 121 ? 26.64800  35.08600 29.39000  1.000 93.79000  ? 103 ARG C NH1 1 
ATOM   3518 N NH2 . ARG D 1 121 ? 28.60300  33.94800 29.74400  1.000 113.10000 ? 103 ARG C NH2 1 
ATOM   3519 N N   . GLY D 1 122 ? 26.06100  31.66900 36.90800  1.000 76.94000  ? 104 GLY C N   1 
ATOM   3520 C CA  . GLY D 1 122 ? 27.01900  31.37600 37.96400  1.000 80.83000  ? 104 GLY C CA  1 
ATOM   3521 C C   . GLY D 1 122 ? 28.40100  31.93700 37.72600  1.000 76.09000  ? 104 GLY C C   1 
ATOM   3522 O O   . GLY D 1 122 ? 29.39000  31.34300 38.17200  1.000 72.95000  ? 104 GLY C O   1 
ATOM   3523 N N   . ILE D 1 123 ? 28.50000  33.06900 37.03500  1.000 89.56000  ? 105 ILE C N   1 
ATOM   3524 C CA  . ILE D 1 123 ? 29.77700  33.67000 36.67000  1.000 84.55000  ? 105 ILE C CA  1 
ATOM   3525 C C   . ILE D 1 123 ? 29.87800  35.03900 37.32600  1.000 74.17000  ? 105 ILE C C   1 
ATOM   3526 O O   . ILE D 1 123 ? 28.97600  35.87200 37.18200  1.000 72.68000  ? 105 ILE C O   1 
ATOM   3527 C CB  . ILE D 1 123 ? 29.93500  33.78000 35.14300  1.000 84.18000  ? 105 ILE C CB  1 
ATOM   3528 N N   . ILE D 1 124 ? 30.97800  35.26800 38.04100  1.000 63.49000  ? 106 ILE C N   1 
ATOM   3529 C CA  . ILE D 1 124 ? 31.25200  36.54200 38.69600  1.000 67.25000  ? 106 ILE C CA  1 
ATOM   3530 C C   . ILE D 1 124 ? 32.63300  37.00800 38.25700  1.000 68.52000  ? 106 ILE C C   1 
ATOM   3531 O O   . ILE D 1 124 ? 33.63300  36.33000 38.52400  1.000 55.82000  ? 106 ILE C O   1 
ATOM   3532 C CB  . ILE D 1 124 ? 31.18000  36.43500 40.22900  1.000 58.02000  ? 106 ILE C CB  1 
ATOM   3533 C CG1 . ILE D 1 124 ? 29.76500  36.05900 40.67200  1.000 60.99000  ? 106 ILE C CG1 1 
ATOM   3534 C CG2 . ILE D 1 124 ? 31.61500  37.74000 40.87600  1.000 57.14000  ? 106 ILE C CG2 1 
ATOM   3535 C CD1 . ILE D 1 124 ? 29.59900  35.96400 42.17200  1.000 73.34000  ? 106 ILE C CD1 1 
ATOM   3536 N N   . LYS D 1 125 ? 32.68800  38.15500 37.58700  1.000 59.49000  ? 107 LYS C N   1 
ATOM   3537 C CA  . LYS D 1 125 ? 33.93700  38.76400 37.15000  1.000 63.41000  ? 107 LYS C CA  1 
ATOM   3538 C C   . LYS D 1 125 ? 34.24300  39.95900 38.04100  1.000 69.81000  ? 107 LYS C C   1 
ATOM   3539 O O   . LYS D 1 125 ? 33.36000  40.78100 38.30700  1.000 67.37000  ? 107 LYS C O   1 
ATOM   3540 C CB  . LYS D 1 125 ? 33.85300  39.20200 35.68600  1.000 69.67000  ? 107 LYS C CB  1 
ATOM   3541 N N   . THR D 1 126 ? 35.49000  40.05600 38.49900  1.000 68.13000  ? 108 THR C N   1 
ATOM   3542 C CA  . THR D 1 126 ? 35.90800  41.11400 39.41500  1.000 64.24000  ? 108 THR C CA  1 
ATOM   3543 C C   . THR D 1 126 ? 37.12300  41.82300 38.83400  1.000 73.16000  ? 108 THR C C   1 
ATOM   3544 O O   . THR D 1 126 ? 38.20500  41.23300 38.74400  1.000 65.65000  ? 108 THR C O   1 
ATOM   3545 C CB  . THR D 1 126 ? 36.22400  40.55000 40.80000  1.000 57.51000  ? 108 THR C CB  1 
ATOM   3546 O OG1 . THR D 1 126 ? 35.05100  39.92900 41.34300  1.000 71.88000  ? 108 THR C OG1 1 
ATOM   3547 C CG2 . THR D 1 126 ? 36.68100  41.66100 41.73100  1.000 63.80000  ? 108 THR C CG2 1 
ATOM   3548 N N   . PHE D 1 127 ? 36.93700  43.08700 38.46000  1.000 66.34000  ? 109 PHE C N   1 
ATOM   3549 C CA  . PHE D 1 127 ? 38.06500  43.88500 37.92400  1.000 72.76000  ? 109 PHE C CA  1 
ATOM   3550 C C   . PHE D 1 127 ? 38.62000  44.75100 39.05800  1.000 74.38000  ? 109 PHE C C   1 
ATOM   3551 O O   . PHE D 1 127 ? 37.87800  45.61100 39.56200  1.000 81.20000  ? 109 PHE C O   1 
ATOM   3552 C CB  . PHE D 1 127 ? 37.59400  44.73600 36.74600  1.000 75.15000  ? 109 PHE C CB  1 
ATOM   3553 C CG  . PHE D 1 127 ? 37.02400  43.97600 35.57400  1.000 95.62000  ? 109 PHE C CG  1 
ATOM   3554 C CD1 . PHE D 1 127 ? 37.02900  42.59100 35.54400  1.000 100.35000 ? 109 PHE C CD1 1 
ATOM   3555 C CD2 . PHE D 1 127 ? 36.46900  44.65300 34.50000  1.000 103.48000 ? 109 PHE C CD2 1 
ATOM   3556 C CE1 . PHE D 1 127 ? 36.49800  41.90200 34.46600  1.000 101.37000 ? 109 PHE C CE1 1 
ATOM   3557 C CE2 . PHE D 1 127 ? 35.93900  43.96300 33.42200  1.000 99.84000  ? 109 PHE C CE2 1 
ATOM   3558 C CZ  . PHE D 1 127 ? 35.95500  42.58900 33.40700  1.000 117.48000 ? 109 PHE C CZ  1 
ATOM   3559 N N   . SER D 1 128 ? 39.87600  44.52200 39.45000  1.000 79.42000  ? 110 SER C N   1 
ATOM   3560 C CA  . SER D 1 128 ? 40.47800  45.27900 40.57800  1.000 79.15000  ? 110 SER C CA  1 
ATOM   3561 C C   . SER D 1 128 ? 41.07700  46.59200 40.06500  1.000 79.01000  ? 110 SER C C   1 
ATOM   3562 O O   . SER D 1 128 ? 42.16200  46.55500 39.46200  1.000 81.49000  ? 110 SER C O   1 
ATOM   3563 C CB  . SER D 1 128 ? 41.49800  44.45100 41.31400  1.000 86.60000  ? 110 SER C CB  1 
ATOM   3564 O OG  . SER D 1 128 ? 40.88100  43.33300 41.93400  1.000 97.67000  ? 110 SER C OG  1 
ATOM   3565 N N   . THR D 1 129 ? 40.37900  47.70400 40.29900  1.000 83.73000  ? 111 THR C N   1 
ATOM   3566 C CA  . THR D 1 129 ? 40.85400  49.02400 39.82000  1.000 69.14000  ? 111 THR C CA  1 
ATOM   3567 C C   . THR D 1 129 ? 40.36200  50.11000 40.77500  1.000 82.71000  ? 111 THR C C   1 
ATOM   3568 O O   . THR D 1 129 ? 39.14300  50.20900 40.96800  1.000 85.61000  ? 111 THR C O   1 
ATOM   3569 C CB  . THR D 1 129 ? 40.35900  49.29900 38.39700  1.000 88.87000  ? 111 THR C CB  1 
ATOM   3570 O OG1 . THR D 1 129 ? 41.01800  50.47300 37.92300  1.000 84.39000  ? 111 THR C OG1 1 
ATOM   3571 C CG2 . THR D 1 129 ? 38.86000  49.49000 38.31400  1.000 81.54000  ? 111 THR C CG2 1 
ATOM   3572 N N   . ASP D 1 130 ? 41.27400  50.89400 41.34700  1.000 96.61000  ? 112 ASP C N   1 
ATOM   3573 C CA  . ASP D 1 130 ? 40.83800  52.03200 42.19600  1.000 85.78000  ? 112 ASP C CA  1 
ATOM   3574 C C   . ASP D 1 130 ? 40.43500  53.18300 41.27300  1.000 90.80000  ? 112 ASP C C   1 
ATOM   3575 O O   . ASP D 1 130 ? 41.31700  53.71000 40.56700  1.000 84.19000  ? 112 ASP C O   1 
ATOM   3576 C CB  . ASP D 1 130 ? 41.92800  52.45100 43.18400  1.000 60.00000  ? 112 ASP C CB  1 
ATOM   3577 N N   . VAL D 1 131 ? 39.15100  53.54400 41.27600  1.000 86.55000  ? 113 VAL C N   1 
ATOM   3578 C CA  . VAL D 1 131 ? 38.65900  54.65100 40.40400  1.000 80.52000  ? 113 VAL C CA  1 
ATOM   3579 C C   . VAL D 1 131 ? 38.25000  55.82100 41.30700  1.000 59.48000  ? 113 VAL C C   1 
ATOM   3580 O O   . VAL D 1 131 ? 37.47300  56.68300 40.86100  1.000 58.82000  ? 113 VAL C O   1 
ATOM   3581 C CB  . VAL D 1 131 ? 37.54000  54.15100 39.47100  1.000 70.86000  ? 113 VAL C CB  1 
ATOM   3582 C CG1 . VAL D 1 131 ? 36.20300  53.99600 40.17700  1.000 63.43000  ? 113 VAL C CG1 1 
ATOM   3583 C CG2 . VAL D 1 131 ? 37.42100  54.99300 38.21300  1.000 64.86000  ? 113 VAL C CG2 1 
ATOM   3584 N N   . LYS D 1 132 ? 38.77500  55.84900 42.53000  1.000 74.25000  ? 114 LYS C N   1 
ATOM   3585 C CA  . LYS D 1 132 ? 38.52000  56.96900 43.46900  1.000 77.38000  ? 114 LYS C CA  1 
ATOM   3586 C C   . LYS D 1 132 ? 37.04800  56.99700 43.86500  1.000 77.61000  ? 114 LYS C C   1 
ATOM   3587 O O   . LYS D 1 132 ? 36.47000  58.07600 43.93200  1.000 93.68000  ? 114 LYS C O   1 
ATOM   3588 C CB  . LYS D 1 132 ? 39.07000  58.27700 42.88900  1.000 66.28000  ? 114 LYS C CB  1 
ATOM   3589 C CG  . LYS D 1 132 ? 40.58700  58.35900 42.80500  1.000 71.25000  ? 114 LYS C CG  1 
ATOM   3590 C CD  . LYS D 1 132 ? 41.11300  59.77200 42.92300  1.000 89.25000  ? 114 LYS C CD  1 
ATOM   3591 C CE  . LYS D 1 132 ? 42.55600  59.83200 43.37900  1.000 84.36000  ? 114 LYS C CE  1 
ATOM   3592 N NZ  . LYS D 1 132 ? 42.98400  61.22000 43.66700  1.000 85.89000  ? 114 LYS C NZ  1 
ATOM   3593 N N   . LEU D 1 133 ? 36.49100  55.84300 44.16700  1.000 65.38000  ? 115 LEU C N   1 
ATOM   3594 C CA  . LEU D 1 133 ? 35.10900  55.84700 44.67400  1.000 60.41000  ? 115 LEU C CA  1 
ATOM   3595 C C   . LEU D 1 133 ? 35.15800  55.55300 46.16600  1.000 58.95000  ? 115 LEU C C   1 
ATOM   3596 O O   . LEU D 1 133 ? 35.86700  54.63200 46.54500  1.000 70.72000  ? 115 LEU C O   1 
ATOM   3597 C CB  . LEU D 1 133 ? 34.29700  54.78900 43.92900  1.000 59.81000  ? 115 LEU C CB  1 
ATOM   3598 C CG  . LEU D 1 133 ? 33.73000  55.18500 42.57000  1.000 57.86000  ? 115 LEU C CG  1 
ATOM   3599 C CD1 . LEU D 1 133 ? 32.94800  54.02600 41.98000  1.000 39.55000  ? 115 LEU C CD1 1 
ATOM   3600 C CD2 . LEU D 1 133 ? 32.83800  56.40700 42.69300  1.000 50.22000  ? 115 LEU C CD2 1 
ATOM   3601 N N   . ASP D 1 134 ? 34.50400  56.36600 46.97300  1.000 53.96000  ? 116 ASP C N   1 
ATOM   3602 C CA  . ASP D 1 134 ? 34.35900  56.12200 48.40000  1.000 56.83000  ? 116 ASP C CA  1 
ATOM   3603 C C   . ASP D 1 134 ? 33.00800  55.51400 48.75100  1.000 67.58000  ? 116 ASP C C   1 
ATOM   3604 O O   . ASP D 1 134 ? 32.76300  55.21500 49.92400  1.000 71.96000  ? 116 ASP C O   1 
ATOM   3605 C CB  . ASP D 1 134 ? 34.57200  57.41900 49.19200  1.000 84.11000  ? 116 ASP C CB  1 
ATOM   3606 C CG  . ASP D 1 134 ? 33.50100  58.45700 48.91900  1.000 92.02000  ? 116 ASP C CG  1 
ATOM   3607 O OD1 . ASP D 1 134 ? 32.95300  58.47100 47.79700  1.000 101.55000 ? 116 ASP C OD1 1 
ATOM   3608 O OD2 . ASP D 1 134 ? 33.20800  59.26100 49.82800  1.000 95.65000  ? 116 ASP C OD2 1 
ATOM   3609 N N   . GLU D 1 135 ? 32.13400  55.32300 47.76600  1.000 57.38000  ? 117 GLU C N   1 
ATOM   3610 C CA  . GLU D 1 135 ? 30.83000  54.70500 47.94900  1.000 48.11000  ? 117 GLU C CA  1 
ATOM   3611 C C   . GLU D 1 135 ? 30.66200  53.59700 46.91700  1.000 55.29000  ? 117 GLU C C   1 
ATOM   3612 O O   . GLU D 1 135 ? 31.47600  53.43800 46.00400  1.000 45.76000  ? 117 GLU C O   1 
ATOM   3613 C CB  . GLU D 1 135 ? 29.70100  55.73700 47.82900  1.000 51.35000  ? 117 GLU C CB  1 
ATOM   3614 C CG  . GLU D 1 135 ? 29.73200  56.81000 48.90600  1.000 62.15000  ? 117 GLU C CG  1 
ATOM   3615 C CD  . GLU D 1 135 ? 28.70200  57.89700 48.67700  1.000 60.67000  ? 117 GLU C CD  1 
ATOM   3616 O OE1 . GLU D 1 135 ? 28.29400  58.09600 47.51300  1.000 71.98000  ? 117 GLU C OE1 1 
ATOM   3617 O OE2 . GLU D 1 135 ? 28.29900  58.55000 49.66100  1.000 76.85000  ? 117 GLU C OE2 1 
ATOM   3618 N N   . THR D 1 136 ? 29.59200  52.82100 47.06600  1.000 51.65000  ? 118 THR C N   1 
ATOM   3619 C CA  . THR D 1 136 ? 29.34200  51.66500 46.21700  1.000 44.82000  ? 118 THR C CA  1 
ATOM   3620 C C   . THR D 1 136 ? 28.02800  51.83700 45.46800  1.000 42.28000  ? 118 THR C C   1 
ATOM   3621 O O   . THR D 1 136 ? 27.01800  52.24800 46.04900  1.000 44.93000  ? 118 THR C O   1 
ATOM   3622 C CB  . THR D 1 136 ? 29.31200  50.37300 47.03800  1.000 56.58000  ? 118 THR C CB  1 
ATOM   3623 O OG1 . THR D 1 136 ? 30.45300  50.32900 47.90300  1.000 66.62000  ? 118 THR C OG1 1 
ATOM   3624 C CG2 . THR D 1 136 ? 29.34700  49.16600 46.12000  1.000 59.31000  ? 118 THR C CG2 1 
ATOM   3625 N N   . TYR D 1 137 ? 28.10200  51.51700 44.18600  1.000 37.27000  ? 119 TYR C N   1 
ATOM   3626 C CA  . TYR D 1 137 ? 26.92700  51.67200 43.30900  1.000 55.96000  ? 119 TYR C CA  1 
ATOM   3627 C C   . TYR D 1 137 ? 26.53300  50.30400 42.75900  1.000 43.44000  ? 119 TYR C C   1 
ATOM   3628 O O   . TYR D 1 137 ? 27.39800  49.56300 42.30400  1.000 40.77000  ? 119 TYR C O   1 
ATOM   3629 C CB  . TYR D 1 137 ? 27.22800  52.67600 42.19300  1.000 41.08000  ? 119 TYR C CB  1 
ATOM   3630 C CG  . TYR D 1 137 ? 27.40000  54.11600 42.59800  1.000 42.97000  ? 119 TYR C CG  1 
ATOM   3631 C CD1 . TYR D 1 137 ? 28.57000  54.56700 43.18200  1.000 44.86000  ? 119 TYR C CD1 1 
ATOM   3632 C CD2 . TYR D 1 137 ? 26.39200  55.03500 42.37700  1.000 32.21000  ? 119 TYR C CD2 1 
ATOM   3633 C CE1 . TYR D 1 137 ? 28.73400  55.89500 43.54000  1.000 45.10000  ? 119 TYR C CE1 1 
ATOM   3634 C CE2 . TYR D 1 137 ? 26.53700  56.36400 42.73100  1.000 47.18000  ? 119 TYR C CE2 1 
ATOM   3635 C CZ  . TYR D 1 137 ? 27.71200  56.79600 43.31500  1.000 43.84000  ? 119 TYR C CZ  1 
ATOM   3636 O OH  . TYR D 1 137 ? 27.84800  58.10900 43.66000  1.000 45.15000  ? 119 TYR C OH  1 
ATOM   3637 N N   . PHE D 1 138 ? 25.23900  50.01400 42.81300  1.000 52.42000  ? 120 PHE C N   1 
ATOM   3638 C CA  . PHE D 1 138 ? 24.71500  48.72500 42.30500  1.000 59.28000  ? 120 PHE C CA  1 
ATOM   3639 C C   . PHE D 1 138 ? 23.69300  48.97800 41.19500  1.000 42.73000  ? 120 PHE C C   1 
ATOM   3640 O O   . PHE D 1 138 ? 22.73700  49.70300 41.43700  1.000 50.95000  ? 120 PHE C O   1 
ATOM   3641 C CB  . PHE D 1 138 ? 24.06900  47.91600 43.43300  1.000 58.02000  ? 120 PHE C CB  1 
ATOM   3642 C CG  . PHE D 1 138 ? 24.97200  47.46800 44.55100  1.000 56.09000  ? 120 PHE C CG  1 
ATOM   3643 C CD1 . PHE D 1 138 ? 25.41400  48.36000 45.51100  1.000 43.43000  ? 120 PHE C CD1 1 
ATOM   3644 C CD2 . PHE D 1 138 ? 25.37500  46.14800 44.64300  1.000 50.11000  ? 120 PHE C CD2 1 
ATOM   3645 C CE1 . PHE D 1 138 ? 26.23600  47.93900 46.54200  1.000 47.86000  ? 120 PHE C CE1 1 
ATOM   3646 C CE2 . PHE D 1 138 ? 26.20200  45.73100 45.67200  1.000 70.71000  ? 120 PHE C CE2 1 
ATOM   3647 C CZ  . PHE D 1 138 ? 26.63000  46.62700 46.61900  1.000 62.01000  ? 120 PHE C CZ  1 
ATOM   3648 N N   . PHE D 1 139 ? 23.94500  48.40500 40.02800  1.000 50.35000  ? 121 PHE C N   1 
ATOM   3649 C CA  . PHE D 1 139 ? 23.01500  48.53500 38.88500  1.000 46.27000  ? 121 PHE C CA  1 
ATOM   3650 C C   . PHE D 1 139 ? 22.38900  47.17100 38.61100  1.000 39.63000  ? 121 PHE C C   1 
ATOM   3651 O O   . PHE D 1 139 ? 23.11200  46.19300 38.47300  1.000 45.08000  ? 121 PHE C O   1 
ATOM   3652 C CB  . PHE D 1 139 ? 23.71300  49.07700 37.63500  1.000 48.32000  ? 121 PHE C CB  1 
ATOM   3653 C CG  . PHE D 1 139 ? 24.48600  50.36700 37.76000  1.000 51.47000  ? 121 PHE C CG  1 
ATOM   3654 C CD1 . PHE D 1 139 ? 24.54400  51.07300 38.94800  1.000 62.70000  ? 121 PHE C CD1 1 
ATOM   3655 C CD2 . PHE D 1 139 ? 25.17600  50.87000 36.67200  1.000 70.23000  ? 121 PHE C CD2 1 
ATOM   3656 C CE1 . PHE D 1 139 ? 25.26800  52.24900 39.04500  1.000 63.84000  ? 121 PHE C CE1 1 
ATOM   3657 C CE2 . PHE D 1 139 ? 25.89800  52.04800 36.76700  1.000 80.47000  ? 121 PHE C CE2 1 
ATOM   3658 C CZ  . PHE D 1 139 ? 25.94000  52.73700 37.95400  1.000 61.73000  ? 121 PHE C CZ  1 
ATOM   3659 N N   . PHE D 1 140 ? 21.06900  47.13600 38.56200  1.000 43.92000  ? 122 PHE C N   1 
ATOM   3660 C CA  . PHE D 1 140 ? 20.32800  45.88300 38.30100  1.000 57.02000  ? 122 PHE C CA  1 
ATOM   3661 C C   . PHE D 1 140 ? 18.91800  46.23200 37.84500  1.000 51.78000  ? 122 PHE C C   1 
ATOM   3662 O O   . PHE D 1 140 ? 18.42000  47.30800 38.14800  1.000 55.46000  ? 122 PHE C O   1 
ATOM   3663 C CB  . PHE D 1 140 ? 20.23300  44.99400 39.54000  1.000 46.71000  ? 122 PHE C CB  1 
ATOM   3664 C CG  . PHE D 1 140 ? 19.71700  45.64700 40.79400  1.000 46.66000  ? 122 PHE C CG  1 
ATOM   3665 C CD1 . PHE D 1 140 ? 20.55000  46.41300 41.59100  1.000 44.44000  ? 122 PHE C CD1 1 
ATOM   3666 C CD2 . PHE D 1 140 ? 18.40000  45.48400 41.18300  1.000 54.95000  ? 122 PHE C CD2 1 
ATOM   3667 C CE1 . PHE D 1 140 ? 20.07500  47.00400 42.74800  1.000 46.28000  ? 122 PHE C CE1 1 
ATOM   3668 C CE2 . PHE D 1 140 ? 17.92600  46.07700 42.34100  1.000 57.75000  ? 122 PHE C CE2 1 
ATOM   3669 C CZ  . PHE D 1 140 ? 18.76500  46.83300 43.12100  1.000 57.86000  ? 122 PHE C CZ  1 
ATOM   3670 N N   . ARG D 1 141 ? 18.30200  45.31800 37.12500  1.000 55.73000  ? 123 ARG C N   1 
ATOM   3671 C CA  . ARG D 1 141 ? 16.91800  45.52100 36.65200  1.000 71.07000  ? 123 ARG C CA  1 
ATOM   3672 C C   . ARG D 1 141 ? 15.98700  44.95000 37.72000  1.000 67.16000  ? 123 ARG C C   1 
ATOM   3673 O O   . ARG D 1 141 ? 16.44500  44.08800 38.47600  1.000 75.50000  ? 123 ARG C O   1 
ATOM   3674 C CB  . ARG D 1 141 ? 16.80400  44.82300 35.30000  1.000 68.54000  ? 123 ARG C CB  1 
ATOM   3675 C CG  . ARG D 1 141 ? 15.64200  45.23900 34.41500  1.000 79.61000  ? 123 ARG C CG  1 
ATOM   3676 C CD  . ARG D 1 141 ? 15.86500  44.45100 33.14000  1.000 83.79000  ? 123 ARG C CD  1 
ATOM   3677 N NE  . ARG D 1 141 ? 14.78900  44.53100 32.16700  1.000 86.26000  ? 123 ARG C NE  1 
ATOM   3678 C CZ  . ARG D 1 141 ? 14.77900  43.86000 31.02400  1.000 89.74000  ? 123 ARG C CZ  1 
ATOM   3679 N NH1 . ARG D 1 141 ? 15.80700  43.09700 30.69800  1.000 85.46000  ? 123 ARG C NH1 1 
ATOM   3680 N NH2 . ARG D 1 141 ? 13.74100  43.95100 30.21200  1.000 95.28000  ? 123 ARG C NH2 1 
ATOM   3681 N N   . VAL D 1 142 ? 14.73900  45.41900 37.78600  1.000 64.32000  ? 124 VAL C N   1 
ATOM   3682 C CA  . VAL D 1 142 ? 13.79000  44.98200 38.85800  1.000 78.41000  ? 124 VAL C CA  1 
ATOM   3683 C C   . VAL D 1 142 ? 12.81900  43.92400 38.31900  1.000 87.34000  ? 124 VAL C C   1 
ATOM   3684 O O   . VAL D 1 142 ? 11.81400  44.31400 37.71200  1.000 89.74000  ? 124 VAL C O   1 
ATOM   3685 C CB  . VAL D 1 142 ? 13.04900  46.19300 39.44800  1.000 85.49000  ? 124 VAL C CB  1 
HETATM 3686 O O   . HOH E 2 .   ? 2.13700   13.31300 25.79000  1.000 54.28000  ? 201 HOH D O   1 
HETATM 3687 O O   . HOH E 2 .   ? 9.47100   33.08000 23.16400  1.000 60.00000  ? 202 HOH D O   1 
HETATM 3688 O O   . HOH E 2 .   ? -5.47100  19.69300 24.91700  1.000 61.26000  ? 203 HOH D O   1 
HETATM 3689 O O   . HOH E 2 .   ? 10.37300  16.03800 9.40500   1.000 48.83000  ? 204 HOH D O   1 
HETATM 3690 O O   . HOH E 2 .   ? 12.77300  13.88000 6.19400   1.000 60.00000  ? 205 HOH D O   1 
HETATM 3691 O O   . HOH E 2 .   ? 15.00100  12.72400 18.28400  1.000 40.89000  ? 206 HOH D O   1 
HETATM 3692 O O   . HOH E 2 .   ? 22.97000  21.42000 12.19100  1.000 60.00000  ? 207 HOH D O   1 
HETATM 3693 O O   . HOH E 2 .   ? 7.42700   16.32000 23.48700  1.000 44.11000  ? 208 HOH D O   1 
HETATM 3694 O O   . HOH E 2 .   ? 14.56400  16.52600 22.88600  1.000 55.15000  ? 209 HOH D O   1 
HETATM 3695 O O   . HOH E 2 .   ? 18.74400  18.05000 22.78300  1.000 60.00000  ? 210 HOH D O   1 
HETATM 3696 O O   . HOH E 2 .   ? 15.90000  17.63600 12.93000  1.000 47.19000  ? 211 HOH D O   1 
HETATM 3697 O O   . HOH E 2 .   ? 14.64300  34.43400 10.95800  1.000 60.00000  ? 212 HOH D O   1 
HETATM 3698 O O   . HOH E 2 .   ? -2.75000  32.91900 13.58900  1.000 60.00000  ? 213 HOH D O   1 
HETATM 3699 O O   . HOH E 2 .   ? 5.01500   9.46900  8.36100   1.000 63.47000  ? 214 HOH D O   1 
HETATM 3700 O O   . HOH E 2 .   ? 2.92300   9.59500  17.64200  1.000 51.33000  ? 215 HOH D O   1 
HETATM 3701 O O   . HOH E 2 .   ? 4.24400   11.98900 11.37800  1.000 60.00000  ? 216 HOH D O   1 
HETATM 3702 O O   . HOH E 2 .   ? 8.83500   29.74500 7.85800   1.000 60.00000  ? 217 HOH D O   1 
HETATM 3703 O O   . HOH E 2 .   ? 11.21300  28.16900 8.86100   1.000 60.22000  ? 218 HOH D O   1 
HETATM 3704 O O   . HOH E 2 .   ? -15.20700 15.02500 15.13400  1.000 60.00000  ? 219 HOH D O   1 
HETATM 3705 O O   . HOH F 2 .   ? 21.45100  60.90500 25.72700  1.000 48.91000  ? 201 HOH A O   1 
HETATM 3706 O O   . HOH F 2 .   ? 14.15100  47.56500 5.01600   1.000 56.20000  ? 202 HOH A O   1 
HETATM 3707 O O   . HOH F 2 .   ? 13.95700  65.58500 13.68000  1.000 46.94000  ? 203 HOH A O   1 
HETATM 3708 O O   . HOH F 2 .   ? 8.38500   61.37600 18.34300  1.000 37.69000  ? 204 HOH A O   1 
HETATM 3709 O O   . HOH F 2 .   ? 16.27400  57.80400 23.42600  1.000 52.94000  ? 205 HOH A O   1 
HETATM 3710 O O   . HOH F 2 .   ? 27.66900  57.26200 26.42400  1.000 48.94000  ? 206 HOH A O   1 
HETATM 3711 O O   . HOH F 2 .   ? 28.89000  54.65500 25.18600  1.000 53.62000  ? 207 HOH A O   1 
HETATM 3712 O O   . HOH F 2 .   ? 19.35100  62.33600 11.24300  1.000 55.48000  ? 208 HOH A O   1 
HETATM 3713 O O   . HOH F 2 .   ? 23.49200  63.05100 19.06700  1.000 53.52000  ? 209 HOH A O   1 
HETATM 3714 O O   . HOH F 2 .   ? 16.48500  55.27000 27.51800  1.000 37.46000  ? 210 HOH A O   1 
HETATM 3715 O O   . HOH F 2 .   ? 34.08500  49.78800 0.44400   1.000 70.90000  ? 211 HOH A O   1 
HETATM 3716 O O   . HOH F 2 .   ? 33.51900  61.75100 5.02800   1.000 60.00000  ? 212 HOH A O   1 
HETATM 3717 O O   . HOH F 2 .   ? 2.43200   46.64000 18.96200  1.000 60.00000  ? 213 HOH A O   1 
HETATM 3718 O O   . HOH G 2 .   ? -12.08800 14.38600 42.88200  1.000 55.74000  ? 201 HOH B O   1 
HETATM 3719 O O   . HOH G 2 .   ? -6.37600  15.22200 45.76300  1.000 59.51000  ? 202 HOH B O   1 
HETATM 3720 O O   . HOH G 2 .   ? -3.21700  22.94300 28.92600  1.000 45.77000  ? 203 HOH B O   1 
HETATM 3721 O O   . HOH G 2 .   ? 3.98500   30.78600 36.33700  1.000 55.69000  ? 204 HOH B O   1 
HETATM 3722 O O   . HOH G 2 .   ? 2.03600   13.40200 29.08000  1.000 57.80000  ? 205 HOH B O   1 
HETATM 3723 O O   . HOH G 2 .   ? -10.56700 14.24900 45.52200  1.000 59.60000  ? 206 HOH B O   1 
HETATM 3724 O O   . HOH G 2 .   ? -3.77900  14.92200 31.70200  1.000 42.64000  ? 207 HOH B O   1 
HETATM 3725 O O   . HOH G 2 .   ? -2.59400  10.54100 46.42700  1.000 65.39000  ? 208 HOH B O   1 
HETATM 3726 O O   . HOH G 2 .   ? 2.42600   31.47500 42.82600  1.000 60.00000  ? 209 HOH B O   1 
HETATM 3727 O O   . HOH G 2 .   ? 9.77700   15.49000 29.41100  1.000 60.00000  ? 210 HOH B O   1 
HETATM 3728 O O   . HOH G 2 .   ? -4.68300  35.24200 45.25900  1.000 68.77000  ? 211 HOH B O   1 
HETATM 3729 O O   . HOH G 2 .   ? 7.04000   18.91900 27.68300  1.000 43.06000  ? 212 HOH B O   1 
HETATM 3730 O O   . HOH G 2 .   ? 8.02200   16.76600 25.82100  1.000 50.07000  ? 213 HOH B O   1 
HETATM 3731 O O   . HOH G 2 .   ? 1.23700   10.47100 46.99100  1.000 65.10000  ? 214 HOH B O   1 
HETATM 3732 O O   . HOH G 2 .   ? -7.88900  14.90500 31.33400  1.000 45.82000  ? 215 HOH B O   1 
HETATM 3733 O O   . HOH G 2 .   ? -8.20700  15.41200 28.67600  1.000 61.08000  ? 216 HOH B O   1 
HETATM 3734 O O   . HOH H 2 .   ? 35.30900  59.84400 42.91000  1.000 51.98000  ? 201 HOH C O   1 
HETATM 3735 O O   . HOH H 2 .   ? 26.85600  51.24100 28.73500  1.000 47.42000  ? 202 HOH C O   1 
HETATM 3736 O O   . HOH H 2 .   ? 29.78200  58.69300 45.48600  1.000 51.32000  ? 203 HOH C O   1 
HETATM 3737 O O   . HOH H 2 .   ? 31.46200  62.84500 32.46100  1.000 56.66000  ? 204 HOH C O   1 
HETATM 3738 O O   . HOH H 2 .   ? 27.21900  59.13000 31.43100  1.000 49.30000  ? 205 HOH C O   1 
HETATM 3739 O O   . HOH H 2 .   ? 21.47100  60.57200 28.85400  1.000 55.34000  ? 206 HOH C O   1 
HETATM 3740 O O   . HOH H 2 .   ? 19.60000  43.12600 36.01800  1.000 58.52000  ? 207 HOH C O   1 
HETATM 3741 O O   . HOH H 2 .   ? 33.58700  60.27800 45.72000  1.000 50.86000  ? 208 HOH C O   1 
HETATM 3742 O O   . HOH H 2 .   ? 14.06600  58.45900 29.14100  1.000 54.09000  ? 209 HOH C O   1 
HETATM 3743 O O   . HOH H 2 .   ? 33.76400  60.85300 31.90800  1.000 57.49000  ? 210 HOH C O   1 
HETATM 3744 O O   . HOH H 2 .   ? 31.76000  61.77500 45.97800  1.000 51.03000  ? 211 HOH C O   1 
HETATM 3745 O O   . HOH H 2 .   ? 15.25500  57.56300 25.84000  1.000 60.00000  ? 212 HOH C O   1 
HETATM 3746 O O   . HOH H 2 .   ? 31.29600  59.23000 31.34400  1.000 43.82000  ? 213 HOH C O   1 
HETATM 3747 O O   . HOH H 2 .   ? 19.57300  62.82500 29.45600  1.000 54.36000  ? 214 HOH C O   1 
# 
