data_9K1J
# 
_entry.id   9K1J 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9K1J         pdb_00009k1j 10.2210/pdb9k1j/pdb 
WWPDB D_1300052505 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        9K1J 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              screening_sz@163.com 
_pdbx_contact_author.name_first         Wei 
_pdbx_contact_author.name_last          Huang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8569-5184 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, W.' 1 0000-0002-8569-5184 
'Hu, C.X.'  2 ?                   
# 
_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                     'Crystal Structure of 6D1-Ab-ohrB complex' 
_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 'Huang, W.' 1 0000-0002-8569-5184 
primary 'Hu, C.X.'  2 ?                   
# 
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 'Organic hydroperoxide resistance protein' 15057.915 4   ? ? ? ? 
2 non-polymer syn 6-fluoranyl-1,2-benzothiazol-3-one         169.176   3   ? ? ? ? 
3 water       nat water                                      18.015    323 ? ? ? ? 
# 
_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       
;MSTLYSTQVKAVGGRSGTIRSEDGILELKLALPKELGGKGDATNPEQLFAAGYAACFGNAVIHVTRSNKEYKIRDNDVEV
LSTVGIVANGNGGFALTVHLDVTLSGISQADAEKIVEQTHQVCPYSNAIRGNIQVSTTVYTK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSTLYSTQVKAVGGRSGTIRSEDGILELKLALPKELGGKGDATNPEQLFAAGYAACFGNAVIHVTRSNKEYKIRDNDVEV
LSTVGIVANGNGGFALTVHLDVTLSGISQADAEKIVEQTHQVCPYSNAIRGNIQVSTTVYTK
;
_entity_poly.pdbx_strand_id                 B,A,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 6-fluoranyl-1,2-benzothiazol-3-one A1EEB 
3 water                              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   SER n 
1 3   THR n 
1 4   LEU n 
1 5   TYR n 
1 6   SER n 
1 7   THR n 
1 8   GLN n 
1 9   VAL n 
1 10  LYS n 
1 11  ALA n 
1 12  VAL n 
1 13  GLY n 
1 14  GLY n 
1 15  ARG n 
1 16  SER n 
1 17  GLY n 
1 18  THR n 
1 19  ILE n 
1 20  ARG n 
1 21  SER n 
1 22  GLU n 
1 23  ASP n 
1 24  GLY n 
1 25  ILE n 
1 26  LEU n 
1 27  GLU n 
1 28  LEU n 
1 29  LYS n 
1 30  LEU n 
1 31  ALA n 
1 32  LEU n 
1 33  PRO n 
1 34  LYS n 
1 35  GLU n 
1 36  LEU n 
1 37  GLY n 
1 38  GLY n 
1 39  LYS n 
1 40  GLY n 
1 41  ASP n 
1 42  ALA n 
1 43  THR n 
1 44  ASN n 
1 45  PRO n 
1 46  GLU n 
1 47  GLN n 
1 48  LEU n 
1 49  PHE n 
1 50  ALA n 
1 51  ALA n 
1 52  GLY n 
1 53  TYR n 
1 54  ALA n 
1 55  ALA n 
1 56  CYS n 
1 57  PHE n 
1 58  GLY n 
1 59  ASN n 
1 60  ALA n 
1 61  VAL n 
1 62  ILE n 
1 63  HIS n 
1 64  VAL n 
1 65  THR n 
1 66  ARG n 
1 67  SER n 
1 68  ASN n 
1 69  LYS n 
1 70  GLU n 
1 71  TYR n 
1 72  LYS n 
1 73  ILE n 
1 74  ARG n 
1 75  ASP n 
1 76  ASN n 
1 77  ASP n 
1 78  VAL n 
1 79  GLU n 
1 80  VAL n 
1 81  LEU n 
1 82  SER n 
1 83  THR n 
1 84  VAL n 
1 85  GLY n 
1 86  ILE n 
1 87  VAL n 
1 88  ALA n 
1 89  ASN n 
1 90  GLY n 
1 91  ASN n 
1 92  GLY n 
1 93  GLY n 
1 94  PHE n 
1 95  ALA n 
1 96  LEU n 
1 97  THR n 
1 98  VAL n 
1 99  HIS n 
1 100 LEU n 
1 101 ASP n 
1 102 VAL n 
1 103 THR n 
1 104 LEU n 
1 105 SER n 
1 106 GLY n 
1 107 ILE n 
1 108 SER n 
1 109 GLN n 
1 110 ALA n 
1 111 ASP n 
1 112 ALA n 
1 113 GLU n 
1 114 LYS n 
1 115 ILE n 
1 116 VAL n 
1 117 GLU n 
1 118 GLN n 
1 119 THR n 
1 120 HIS n 
1 121 GLN n 
1 122 VAL n 
1 123 CYS n 
1 124 PRO n 
1 125 TYR n 
1 126 SER n 
1 127 ASN n 
1 128 ALA n 
1 129 ILE n 
1 130 ARG n 
1 131 GLY n 
1 132 ASN n 
1 133 ILE n 
1 134 GLN n 
1 135 VAL n 
1 136 SER n 
1 137 THR n 
1 138 THR n 
1 139 VAL n 
1 140 TYR n 
1 141 THR n 
1 142 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   142 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ohr 
_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      'Acinetobacter baumannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     470 
_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 
A1EEB non-polymer         . 6-fluoranyl-1,2-benzothiazol-3-one ? 'C7 H4 F N O S'  169.176 
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 
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   1   1   MET MET B . n 
A 1 2   SER 2   2   2   SER SER B . n 
A 1 3   THR 3   3   3   THR THR B . n 
A 1 4   LEU 4   4   4   LEU LEU B . n 
A 1 5   TYR 5   5   5   TYR TYR B . n 
A 1 6   SER 6   6   6   SER SER B . n 
A 1 7   THR 7   7   7   THR THR B . n 
A 1 8   GLN 8   8   8   GLN GLN B . n 
A 1 9   VAL 9   9   9   VAL VAL B . n 
A 1 10  LYS 10  10  10  LYS LYS B . n 
A 1 11  ALA 11  11  11  ALA ALA B . n 
A 1 12  VAL 12  12  12  VAL VAL B . n 
A 1 13  GLY 13  13  13  GLY GLY B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  ARG 15  15  15  ARG ARG B . n 
A 1 16  SER 16  16  16  SER SER B . n 
A 1 17  GLY 17  17  17  GLY GLY B . n 
A 1 18  THR 18  18  18  THR THR B . n 
A 1 19  ILE 19  19  19  ILE ILE B . n 
A 1 20  ARG 20  20  20  ARG ARG B . n 
A 1 21  SER 21  21  21  SER SER B . n 
A 1 22  GLU 22  22  22  GLU GLU B . n 
A 1 23  ASP 23  23  23  ASP ASP B . n 
A 1 24  GLY 24  24  24  GLY GLY B . n 
A 1 25  ILE 25  25  25  ILE ILE B . n 
A 1 26  LEU 26  26  26  LEU LEU B . n 
A 1 27  GLU 27  27  27  GLU GLU B . n 
A 1 28  LEU 28  28  28  LEU LEU B . n 
A 1 29  LYS 29  29  29  LYS LYS B . n 
A 1 30  LEU 30  30  30  LEU LEU B . n 
A 1 31  ALA 31  31  31  ALA ALA B . n 
A 1 32  LEU 32  32  32  LEU LEU B . n 
A 1 33  PRO 33  33  33  PRO PRO B . n 
A 1 34  LYS 34  34  34  LYS LYS B . n 
A 1 35  GLU 35  35  35  GLU GLU B . n 
A 1 36  LEU 36  36  36  LEU LEU B . n 
A 1 37  GLY 37  37  37  GLY GLY B . n 
A 1 38  GLY 38  38  38  GLY GLY B . n 
A 1 39  LYS 39  39  39  LYS LYS B . n 
A 1 40  GLY 40  40  40  GLY GLY B . n 
A 1 41  ASP 41  41  41  ASP ASP B . n 
A 1 42  ALA 42  42  42  ALA ALA B . n 
A 1 43  THR 43  43  43  THR THR B . n 
A 1 44  ASN 44  44  44  ASN ASN B . n 
A 1 45  PRO 45  45  45  PRO PRO B . n 
A 1 46  GLU 46  46  46  GLU GLU B . n 
A 1 47  GLN 47  47  47  GLN GLN B . n 
A 1 48  LEU 48  48  48  LEU LEU B . n 
A 1 49  PHE 49  49  49  PHE PHE B . n 
A 1 50  ALA 50  50  50  ALA ALA B . n 
A 1 51  ALA 51  51  51  ALA ALA B . n 
A 1 52  GLY 52  52  52  GLY GLY B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  ALA 54  54  54  ALA ALA B . n 
A 1 55  ALA 55  55  55  ALA ALA B . n 
A 1 56  CYS 56  56  56  CYS CYS B . n 
A 1 57  PHE 57  57  57  PHE PHE B . n 
A 1 58  GLY 58  58  58  GLY GLY B . n 
A 1 59  ASN 59  59  59  ASN ASN B . n 
A 1 60  ALA 60  60  60  ALA ALA B . n 
A 1 61  VAL 61  61  61  VAL VAL B . n 
A 1 62  ILE 62  62  62  ILE ILE B . n 
A 1 63  HIS 63  63  63  HIS HIS B . n 
A 1 64  VAL 64  64  64  VAL VAL B . n 
A 1 65  THR 65  65  65  THR THR B . n 
A 1 66  ARG 66  66  66  ARG ARG B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  ASN 68  68  68  ASN ASN B . n 
A 1 69  LYS 69  69  69  LYS LYS B . n 
A 1 70  GLU 70  70  70  GLU GLU B . n 
A 1 71  TYR 71  71  71  TYR TYR B . n 
A 1 72  LYS 72  72  72  LYS LYS B . n 
A 1 73  ILE 73  73  73  ILE ILE B . n 
A 1 74  ARG 74  74  74  ARG ARG B . n 
A 1 75  ASP 75  75  75  ASP ASP B . n 
A 1 76  ASN 76  76  76  ASN ASN B . n 
A 1 77  ASP 77  77  77  ASP ASP B . n 
A 1 78  VAL 78  78  78  VAL VAL B . n 
A 1 79  GLU 79  79  79  GLU GLU B . n 
A 1 80  VAL 80  80  80  VAL VAL B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  SER 82  82  82  SER SER B . n 
A 1 83  THR 83  83  83  THR THR B . n 
A 1 84  VAL 84  84  84  VAL VAL B . n 
A 1 85  GLY 85  85  85  GLY GLY B . n 
A 1 86  ILE 86  86  86  ILE ILE B . n 
A 1 87  VAL 87  87  87  VAL VAL B . n 
A 1 88  ALA 88  88  88  ALA ALA B . n 
A 1 89  ASN 89  89  89  ASN ASN B . n 
A 1 90  GLY 90  90  90  GLY GLY B . n 
A 1 91  ASN 91  91  91  ASN ASN B . n 
A 1 92  GLY 92  92  92  GLY GLY B . n 
A 1 93  GLY 93  93  93  GLY GLY B . n 
A 1 94  PHE 94  94  94  PHE PHE B . n 
A 1 95  ALA 95  95  95  ALA ALA B . n 
A 1 96  LEU 96  96  96  LEU LEU B . n 
A 1 97  THR 97  97  97  THR THR B . n 
A 1 98  VAL 98  98  98  VAL VAL B . n 
A 1 99  HIS 99  99  99  HIS HIS B . n 
A 1 100 LEU 100 100 100 LEU LEU B . n 
A 1 101 ASP 101 101 101 ASP ASP B . n 
A 1 102 VAL 102 102 102 VAL VAL B . n 
A 1 103 THR 103 103 103 THR THR B . n 
A 1 104 LEU 104 104 104 LEU LEU B . n 
A 1 105 SER 105 105 105 SER SER B . n 
A 1 106 GLY 106 106 106 GLY GLY B . n 
A 1 107 ILE 107 107 107 ILE ILE B . n 
A 1 108 SER 108 108 108 SER SER B . n 
A 1 109 GLN 109 109 109 GLN GLN B . n 
A 1 110 ALA 110 110 110 ALA ALA B . n 
A 1 111 ASP 111 111 111 ASP ASP B . n 
A 1 112 ALA 112 112 112 ALA ALA B . n 
A 1 113 GLU 113 113 113 GLU GLU B . n 
A 1 114 LYS 114 114 114 LYS LYS B . n 
A 1 115 ILE 115 115 115 ILE ILE B . n 
A 1 116 VAL 116 116 116 VAL VAL B . n 
A 1 117 GLU 117 117 117 GLU GLU B . n 
A 1 118 GLN 118 118 118 GLN GLN B . n 
A 1 119 THR 119 119 119 THR THR B . n 
A 1 120 HIS 120 120 120 HIS HIS B . n 
A 1 121 GLN 121 121 121 GLN GLN B . n 
A 1 122 VAL 122 122 122 VAL VAL B . n 
A 1 123 CYS 123 123 123 CYS CYS B . n 
A 1 124 PRO 124 124 124 PRO PRO B . n 
A 1 125 TYR 125 125 125 TYR TYR B . n 
A 1 126 SER 126 126 126 SER SER B . n 
A 1 127 ASN 127 127 127 ASN ASN B . n 
A 1 128 ALA 128 128 128 ALA ALA B . n 
A 1 129 ILE 129 129 129 ILE ILE B . n 
A 1 130 ARG 130 130 130 ARG ARG B . n 
A 1 131 GLY 131 131 131 GLY GLY B . n 
A 1 132 ASN 132 132 132 ASN ASN B . n 
A 1 133 ILE 133 133 133 ILE ILE B . n 
A 1 134 GLN 134 134 134 GLN GLN B . n 
A 1 135 VAL 135 135 135 VAL VAL B . n 
A 1 136 SER 136 136 136 SER SER B . n 
A 1 137 THR 137 137 137 THR THR B . n 
A 1 138 THR 138 138 138 THR THR B . n 
A 1 139 VAL 139 139 139 VAL VAL B . n 
A 1 140 TYR 140 140 140 TYR TYR B . n 
A 1 141 THR 141 141 141 THR THR B . n 
A 1 142 LYS 142 142 142 LYS LYS B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   SER 2   2   2   SER SER A . n 
B 1 3   THR 3   3   3   THR THR A . n 
B 1 4   LEU 4   4   4   LEU LEU A . n 
B 1 5   TYR 5   5   5   TYR TYR A . n 
B 1 6   SER 6   6   6   SER SER A . n 
B 1 7   THR 7   7   7   THR THR A . n 
B 1 8   GLN 8   8   8   GLN GLN A . n 
B 1 9   VAL 9   9   9   VAL VAL A . n 
B 1 10  LYS 10  10  10  LYS LYS A . n 
B 1 11  ALA 11  11  11  ALA ALA A . n 
B 1 12  VAL 12  12  12  VAL VAL A . n 
B 1 13  GLY 13  13  13  GLY GLY A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  ARG 15  15  15  ARG ARG A . n 
B 1 16  SER 16  16  16  SER SER A . n 
B 1 17  GLY 17  17  17  GLY GLY A . n 
B 1 18  THR 18  18  18  THR THR A . n 
B 1 19  ILE 19  19  19  ILE ILE A . n 
B 1 20  ARG 20  20  20  ARG ARG A . n 
B 1 21  SER 21  21  21  SER SER A . n 
B 1 22  GLU 22  22  22  GLU GLU A . n 
B 1 23  ASP 23  23  23  ASP ASP A . n 
B 1 24  GLY 24  24  24  GLY GLY A . n 
B 1 25  ILE 25  25  25  ILE ILE A . n 
B 1 26  LEU 26  26  26  LEU LEU A . n 
B 1 27  GLU 27  27  27  GLU GLU A . n 
B 1 28  LEU 28  28  28  LEU LEU A . n 
B 1 29  LYS 29  29  29  LYS LYS A . n 
B 1 30  LEU 30  30  30  LEU LEU A . n 
B 1 31  ALA 31  31  31  ALA ALA A . n 
B 1 32  LEU 32  32  32  LEU LEU A . n 
B 1 33  PRO 33  33  33  PRO PRO A . n 
B 1 34  LYS 34  34  34  LYS LYS A . n 
B 1 35  GLU 35  35  35  GLU GLU A . n 
B 1 36  LEU 36  36  36  LEU LEU A . n 
B 1 37  GLY 37  37  37  GLY GLY A . n 
B 1 38  GLY 38  38  38  GLY GLY A . n 
B 1 39  LYS 39  39  39  LYS LYS A . n 
B 1 40  GLY 40  40  40  GLY GLY A . n 
B 1 41  ASP 41  41  41  ASP ASP A . n 
B 1 42  ALA 42  42  42  ALA ALA A . n 
B 1 43  THR 43  43  43  THR THR A . n 
B 1 44  ASN 44  44  44  ASN ASN A . n 
B 1 45  PRO 45  45  45  PRO PRO A . n 
B 1 46  GLU 46  46  46  GLU GLU A . n 
B 1 47  GLN 47  47  47  GLN GLN A . n 
B 1 48  LEU 48  48  48  LEU LEU A . n 
B 1 49  PHE 49  49  49  PHE PHE A . n 
B 1 50  ALA 50  50  50  ALA ALA A . n 
B 1 51  ALA 51  51  51  ALA ALA A . n 
B 1 52  GLY 52  52  52  GLY GLY A . n 
B 1 53  TYR 53  53  53  TYR TYR A . n 
B 1 54  ALA 54  54  54  ALA ALA A . n 
B 1 55  ALA 55  55  55  ALA ALA A . n 
B 1 56  CYS 56  56  56  CYS CYS A . n 
B 1 57  PHE 57  57  57  PHE PHE A . n 
B 1 58  GLY 58  58  58  GLY GLY A . n 
B 1 59  ASN 59  59  59  ASN ASN A . n 
B 1 60  ALA 60  60  60  ALA ALA A . n 
B 1 61  VAL 61  61  61  VAL VAL A . n 
B 1 62  ILE 62  62  62  ILE ILE A . n 
B 1 63  HIS 63  63  63  HIS HIS A . n 
B 1 64  VAL 64  64  64  VAL VAL A . n 
B 1 65  THR 65  65  65  THR THR A . n 
B 1 66  ARG 66  66  66  ARG ARG A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  ASN 68  68  68  ASN ASN A . n 
B 1 69  LYS 69  69  69  LYS LYS A . n 
B 1 70  GLU 70  70  70  GLU GLU A . n 
B 1 71  TYR 71  71  71  TYR TYR A . n 
B 1 72  LYS 72  72  72  LYS LYS A . n 
B 1 73  ILE 73  73  73  ILE ILE A . n 
B 1 74  ARG 74  74  74  ARG ARG A . n 
B 1 75  ASP 75  75  75  ASP ASP A . n 
B 1 76  ASN 76  76  76  ASN ASN A . n 
B 1 77  ASP 77  77  77  ASP ASP A . n 
B 1 78  VAL 78  78  78  VAL VAL A . n 
B 1 79  GLU 79  79  79  GLU GLU A . n 
B 1 80  VAL 80  80  80  VAL VAL A . n 
B 1 81  LEU 81  81  81  LEU LEU A . n 
B 1 82  SER 82  82  82  SER SER A . n 
B 1 83  THR 83  83  83  THR THR A . n 
B 1 84  VAL 84  84  84  VAL VAL A . n 
B 1 85  GLY 85  85  85  GLY GLY A . n 
B 1 86  ILE 86  86  86  ILE ILE A . n 
B 1 87  VAL 87  87  87  VAL VAL A . n 
B 1 88  ALA 88  88  88  ALA ALA A . n 
B 1 89  ASN 89  89  89  ASN ASN A . n 
B 1 90  GLY 90  90  90  GLY GLY A . n 
B 1 91  ASN 91  91  91  ASN ASN A . n 
B 1 92  GLY 92  92  92  GLY GLY A . n 
B 1 93  GLY 93  93  93  GLY GLY A . n 
B 1 94  PHE 94  94  94  PHE PHE A . n 
B 1 95  ALA 95  95  95  ALA ALA A . n 
B 1 96  LEU 96  96  96  LEU LEU A . n 
B 1 97  THR 97  97  97  THR THR A . n 
B 1 98  VAL 98  98  98  VAL VAL A . n 
B 1 99  HIS 99  99  99  HIS HIS A . n 
B 1 100 LEU 100 100 100 LEU LEU A . n 
B 1 101 ASP 101 101 101 ASP ASP A . n 
B 1 102 VAL 102 102 102 VAL VAL A . n 
B 1 103 THR 103 103 103 THR THR A . n 
B 1 104 LEU 104 104 104 LEU LEU A . n 
B 1 105 SER 105 105 105 SER SER A . n 
B 1 106 GLY 106 106 106 GLY GLY A . n 
B 1 107 ILE 107 107 107 ILE ILE A . n 
B 1 108 SER 108 108 108 SER SER A . n 
B 1 109 GLN 109 109 109 GLN GLN A . n 
B 1 110 ALA 110 110 110 ALA ALA A . n 
B 1 111 ASP 111 111 111 ASP ASP A . n 
B 1 112 ALA 112 112 112 ALA ALA A . n 
B 1 113 GLU 113 113 113 GLU GLU A . n 
B 1 114 LYS 114 114 114 LYS LYS A . n 
B 1 115 ILE 115 115 115 ILE ILE A . n 
B 1 116 VAL 116 116 116 VAL VAL A . n 
B 1 117 GLU 117 117 117 GLU GLU A . n 
B 1 118 GLN 118 118 118 GLN GLN A . n 
B 1 119 THR 119 119 119 THR THR A . n 
B 1 120 HIS 120 120 120 HIS HIS A . n 
B 1 121 GLN 121 121 121 GLN GLN A . n 
B 1 122 VAL 122 122 122 VAL VAL A . n 
B 1 123 CYS 123 123 123 CYS CYS A . n 
B 1 124 PRO 124 124 124 PRO PRO A . n 
B 1 125 TYR 125 125 125 TYR TYR A . n 
B 1 126 SER 126 126 126 SER SER A . n 
B 1 127 ASN 127 127 127 ASN ASN A . n 
B 1 128 ALA 128 128 128 ALA ALA A . n 
B 1 129 ILE 129 129 129 ILE ILE A . n 
B 1 130 ARG 130 130 130 ARG ARG A . n 
B 1 131 GLY 131 131 131 GLY GLY A . n 
B 1 132 ASN 132 132 132 ASN ASN A . n 
B 1 133 ILE 133 133 133 ILE ILE A . n 
B 1 134 GLN 134 134 134 GLN GLN A . n 
B 1 135 VAL 135 135 135 VAL VAL A . n 
B 1 136 SER 136 136 136 SER SER A . n 
B 1 137 THR 137 137 137 THR THR A . n 
B 1 138 THR 138 138 138 THR THR A . n 
B 1 139 VAL 139 139 139 VAL VAL A . n 
B 1 140 TYR 140 140 140 TYR TYR A . n 
B 1 141 THR 141 141 141 THR THR A . n 
B 1 142 LYS 142 142 142 LYS LYS A . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   SER 2   2   2   SER SER C . n 
C 1 3   THR 3   3   3   THR THR C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   TYR 5   5   5   TYR TYR C . n 
C 1 6   SER 6   6   6   SER SER C . n 
C 1 7   THR 7   7   7   THR THR C . n 
C 1 8   GLN 8   8   8   GLN GLN C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  LYS 10  10  10  LYS LYS C . n 
C 1 11  ALA 11  11  11  ALA ALA C . n 
C 1 12  VAL 12  12  12  VAL VAL C . n 
C 1 13  GLY 13  13  13  GLY GLY C . n 
C 1 14  GLY 14  14  14  GLY GLY C . n 
C 1 15  ARG 15  15  15  ARG ARG C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  THR 18  18  18  THR THR C . n 
C 1 19  ILE 19  19  19  ILE ILE C . n 
C 1 20  ARG 20  20  20  ARG ARG C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  GLU 22  22  22  GLU GLU C . n 
C 1 23  ASP 23  23  23  ASP ASP C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  ILE 25  25  25  ILE ILE C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  LEU 28  28  28  LEU LEU C . n 
C 1 29  LYS 29  29  29  LYS LYS C . n 
C 1 30  LEU 30  30  30  LEU LEU C . n 
C 1 31  ALA 31  31  31  ALA ALA C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  PRO 33  33  33  PRO PRO C . n 
C 1 34  LYS 34  34  34  LYS LYS C . n 
C 1 35  GLU 35  35  35  GLU GLU C . n 
C 1 36  LEU 36  36  36  LEU LEU C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  GLY 38  38  38  GLY GLY C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  GLY 40  40  40  GLY GLY C . n 
C 1 41  ASP 41  41  41  ASP ASP C . n 
C 1 42  ALA 42  42  42  ALA ALA C . n 
C 1 43  THR 43  43  43  THR THR C . n 
C 1 44  ASN 44  44  44  ASN ASN C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  GLU 46  46  46  GLU GLU C . n 
C 1 47  GLN 47  47  47  GLN GLN C . n 
C 1 48  LEU 48  48  48  LEU LEU C . n 
C 1 49  PHE 49  49  49  PHE PHE C . n 
C 1 50  ALA 50  50  50  ALA ALA C . n 
C 1 51  ALA 51  51  51  ALA ALA C . n 
C 1 52  GLY 52  52  52  GLY GLY C . n 
C 1 53  TYR 53  53  53  TYR TYR C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  CYS 56  56  56  CYS CYS C . n 
C 1 57  PHE 57  57  57  PHE PHE C . n 
C 1 58  GLY 58  58  58  GLY GLY C . n 
C 1 59  ASN 59  59  59  ASN ASN C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  VAL 61  61  61  VAL VAL C . n 
C 1 62  ILE 62  62  62  ILE ILE C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  VAL 64  64  64  VAL VAL C . n 
C 1 65  THR 65  65  65  THR THR C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  ASN 68  68  68  ASN ASN C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  GLU 70  70  70  GLU GLU C . n 
C 1 71  TYR 71  71  71  TYR TYR C . n 
C 1 72  LYS 72  72  72  LYS LYS C . n 
C 1 73  ILE 73  73  73  ILE ILE C . n 
C 1 74  ARG 74  74  74  ARG ARG C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  ASN 76  76  76  ASN ASN C . n 
C 1 77  ASP 77  77  77  ASP ASP C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  GLU 79  79  79  GLU GLU C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  THR 83  83  83  THR THR C . n 
C 1 84  VAL 84  84  84  VAL VAL C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ILE 86  86  86  ILE ILE C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  ALA 88  88  88  ALA ALA C . n 
C 1 89  ASN 89  89  89  ASN ASN C . n 
C 1 90  GLY 90  90  90  GLY GLY C . n 
C 1 91  ASN 91  91  91  ASN ASN C . n 
C 1 92  GLY 92  92  92  GLY GLY C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  PHE 94  94  94  PHE PHE C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  LEU 96  96  96  LEU LEU C . n 
C 1 97  THR 97  97  97  THR THR C . n 
C 1 98  VAL 98  98  98  VAL VAL C . n 
C 1 99  HIS 99  99  99  HIS HIS C . n 
C 1 100 LEU 100 100 100 LEU LEU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 VAL 102 102 102 VAL VAL C . n 
C 1 103 THR 103 103 103 THR THR C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 GLY 106 106 106 GLY GLY C . n 
C 1 107 ILE 107 107 107 ILE ILE C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLN 109 109 109 GLN GLN C . n 
C 1 110 ALA 110 110 110 ALA ALA C . n 
C 1 111 ASP 111 111 111 ASP ASP C . n 
C 1 112 ALA 112 112 112 ALA ALA C . n 
C 1 113 GLU 113 113 113 GLU GLU C . n 
C 1 114 LYS 114 114 114 LYS LYS C . n 
C 1 115 ILE 115 115 115 ILE ILE C . n 
C 1 116 VAL 116 116 116 VAL VAL C . n 
C 1 117 GLU 117 117 117 GLU GLU C . n 
C 1 118 GLN 118 118 118 GLN GLN C . n 
C 1 119 THR 119 119 119 THR THR C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLN 121 121 121 GLN GLN C . n 
C 1 122 VAL 122 122 122 VAL VAL C . n 
C 1 123 CYS 123 123 123 CYS CYS C . n 
C 1 124 PRO 124 124 124 PRO PRO C . n 
C 1 125 TYR 125 125 125 TYR TYR C . n 
C 1 126 SER 126 126 126 SER SER C . n 
C 1 127 ASN 127 127 127 ASN ASN C . n 
C 1 128 ALA 128 128 128 ALA ALA C . n 
C 1 129 ILE 129 129 129 ILE ILE C . n 
C 1 130 ARG 130 130 130 ARG ARG C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 ASN 132 132 132 ASN ASN C . n 
C 1 133 ILE 133 133 133 ILE ILE C . n 
C 1 134 GLN 134 134 134 GLN GLN C . n 
C 1 135 VAL 135 135 135 VAL VAL C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 THR 138 138 138 THR THR C . n 
C 1 139 VAL 139 139 139 VAL VAL C . n 
C 1 140 TYR 140 140 140 TYR TYR C . n 
C 1 141 THR 141 141 141 THR THR C . n 
C 1 142 LYS 142 142 142 LYS LYS C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   SER 2   2   2   SER SER D . n 
D 1 3   THR 3   3   3   THR THR D . n 
D 1 4   LEU 4   4   4   LEU LEU D . n 
D 1 5   TYR 5   5   5   TYR TYR D . n 
D 1 6   SER 6   6   6   SER SER D . n 
D 1 7   THR 7   7   7   THR THR D . n 
D 1 8   GLN 8   8   8   GLN GLN D . n 
D 1 9   VAL 9   9   9   VAL VAL D . n 
D 1 10  LYS 10  10  10  LYS LYS D . n 
D 1 11  ALA 11  11  11  ALA ALA D . n 
D 1 12  VAL 12  12  12  VAL VAL D . n 
D 1 13  GLY 13  13  13  GLY GLY D . n 
D 1 14  GLY 14  14  14  GLY GLY D . n 
D 1 15  ARG 15  15  15  ARG ARG D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  GLY 17  17  17  GLY GLY D . n 
D 1 18  THR 18  18  18  THR THR D . n 
D 1 19  ILE 19  19  19  ILE ILE D . n 
D 1 20  ARG 20  20  20  ARG ARG D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  GLU 22  22  22  GLU GLU D . n 
D 1 23  ASP 23  23  23  ASP ASP D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  ILE 25  25  25  ILE ILE D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLU 27  27  27  GLU GLU D . n 
D 1 28  LEU 28  28  28  LEU LEU D . n 
D 1 29  LYS 29  29  29  LYS LYS D . n 
D 1 30  LEU 30  30  30  LEU LEU D . n 
D 1 31  ALA 31  31  31  ALA ALA D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  PRO 33  33  33  PRO PRO D . n 
D 1 34  LYS 34  34  34  LYS LYS D . n 
D 1 35  GLU 35  35  35  GLU GLU D . n 
D 1 36  LEU 36  36  36  LEU LEU D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  GLY 38  38  38  GLY GLY D . n 
D 1 39  LYS 39  39  39  LYS LYS D . n 
D 1 40  GLY 40  40  40  GLY GLY D . n 
D 1 41  ASP 41  41  41  ASP ASP D . n 
D 1 42  ALA 42  42  42  ALA ALA D . n 
D 1 43  THR 43  43  43  THR THR D . n 
D 1 44  ASN 44  44  44  ASN ASN D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  GLU 46  46  46  GLU GLU D . n 
D 1 47  GLN 47  47  47  GLN GLN D . n 
D 1 48  LEU 48  48  48  LEU LEU D . n 
D 1 49  PHE 49  49  49  PHE PHE D . n 
D 1 50  ALA 50  50  50  ALA ALA D . n 
D 1 51  ALA 51  51  51  ALA ALA D . n 
D 1 52  GLY 52  52  52  GLY GLY D . n 
D 1 53  TYR 53  53  53  TYR TYR D . n 
D 1 54  ALA 54  54  54  ALA ALA D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  CYS 56  56  56  CYS CYS D . n 
D 1 57  PHE 57  57  57  PHE PHE D . n 
D 1 58  GLY 58  58  58  GLY GLY D . n 
D 1 59  ASN 59  59  59  ASN ASN D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  VAL 61  61  61  VAL VAL D . n 
D 1 62  ILE 62  62  62  ILE ILE D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  VAL 64  64  64  VAL VAL D . n 
D 1 65  THR 65  65  65  THR THR D . n 
D 1 66  ARG 66  66  66  ARG ARG D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  ASN 68  68  68  ASN ASN D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  GLU 70  70  70  GLU GLU D . n 
D 1 71  TYR 71  71  71  TYR TYR D . n 
D 1 72  LYS 72  72  72  LYS LYS D . n 
D 1 73  ILE 73  73  73  ILE ILE D . n 
D 1 74  ARG 74  74  74  ARG ARG D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  ASN 76  76  76  ASN ASN D . n 
D 1 77  ASP 77  77  77  ASP ASP D . n 
D 1 78  VAL 78  78  78  VAL VAL D . n 
D 1 79  GLU 79  79  79  GLU GLU D . n 
D 1 80  VAL 80  80  80  VAL VAL D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  SER 82  82  82  SER SER D . n 
D 1 83  THR 83  83  83  THR THR D . n 
D 1 84  VAL 84  84  84  VAL VAL D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ILE 86  86  86  ILE ILE D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  ALA 88  88  88  ALA ALA D . n 
D 1 89  ASN 89  89  89  ASN ASN D . n 
D 1 90  GLY 90  90  90  GLY GLY D . n 
D 1 91  ASN 91  91  91  ASN ASN D . n 
D 1 92  GLY 92  92  92  GLY GLY D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  PHE 94  94  94  PHE PHE D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  LEU 96  96  96  LEU LEU D . n 
D 1 97  THR 97  97  97  THR THR D . n 
D 1 98  VAL 98  98  98  VAL VAL D . n 
D 1 99  HIS 99  99  99  HIS HIS D . n 
D 1 100 LEU 100 100 100 LEU LEU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 VAL 102 102 102 VAL VAL D . n 
D 1 103 THR 103 103 103 THR THR D . n 
D 1 104 LEU 104 104 104 LEU LEU D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 GLY 106 106 106 GLY GLY D . n 
D 1 107 ILE 107 107 107 ILE ILE D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLN 109 109 109 GLN GLN D . n 
D 1 110 ALA 110 110 110 ALA ALA D . n 
D 1 111 ASP 111 111 111 ASP ASP D . n 
D 1 112 ALA 112 112 112 ALA ALA D . n 
D 1 113 GLU 113 113 113 GLU GLU D . n 
D 1 114 LYS 114 114 114 LYS LYS D . n 
D 1 115 ILE 115 115 115 ILE ILE D . n 
D 1 116 VAL 116 116 116 VAL VAL D . n 
D 1 117 GLU 117 117 117 GLU GLU D . n 
D 1 118 GLN 118 118 118 GLN GLN D . n 
D 1 119 THR 119 119 119 THR THR D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLN 121 121 121 GLN GLN D . n 
D 1 122 VAL 122 122 122 VAL VAL D . n 
D 1 123 CYS 123 123 123 CYS CYS D . n 
D 1 124 PRO 124 124 124 PRO PRO D . n 
D 1 125 TYR 125 125 125 TYR TYR D . n 
D 1 126 SER 126 126 126 SER SER D . n 
D 1 127 ASN 127 127 127 ASN ASN D . n 
D 1 128 ALA 128 128 128 ALA ALA D . n 
D 1 129 ILE 129 129 129 ILE ILE D . n 
D 1 130 ARG 130 130 130 ARG ARG D . n 
D 1 131 GLY 131 131 131 GLY GLY D . n 
D 1 132 ASN 132 132 132 ASN ASN D . n 
D 1 133 ILE 133 133 133 ILE ILE D . n 
D 1 134 GLN 134 134 134 GLN GLN D . n 
D 1 135 VAL 135 135 135 VAL VAL D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 THR 138 138 138 THR THR D . n 
D 1 139 VAL 139 139 139 VAL VAL D . n 
D 1 140 TYR 140 140 140 TYR TYR D . n 
D 1 141 THR 141 141 141 THR THR D . n 
D 1 142 LYS 142 142 142 LYS LYS D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EEB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EEB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 A1EEB 1   201 201 A1EEB 6D1 B . 
F 2 A1EEB 1   201 201 A1EEB 6D1 A . 
G 2 A1EEB 1   201 201 A1EEB 6D1 D . 
H 3 HOH   1   301 183 HOH   HOH B . 
H 3 HOH   2   302 109 HOH   HOH B . 
H 3 HOH   3   303 173 HOH   HOH B . 
H 3 HOH   4   304 123 HOH   HOH B . 
H 3 HOH   5   305 254 HOH   HOH B . 
H 3 HOH   6   306 168 HOH   HOH B . 
H 3 HOH   7   307 45  HOH   HOH B . 
H 3 HOH   8   308 297 HOH   HOH B . 
H 3 HOH   9   309 75  HOH   HOH B . 
H 3 HOH   10  310 93  HOH   HOH B . 
H 3 HOH   11  311 86  HOH   HOH B . 
H 3 HOH   12  312 150 HOH   HOH B . 
H 3 HOH   13  313 106 HOH   HOH B . 
H 3 HOH   14  314 143 HOH   HOH B . 
H 3 HOH   15  315 230 HOH   HOH B . 
H 3 HOH   16  316 26  HOH   HOH B . 
H 3 HOH   17  317 129 HOH   HOH B . 
H 3 HOH   18  318 282 HOH   HOH B . 
H 3 HOH   19  319 130 HOH   HOH B . 
H 3 HOH   20  320 312 HOH   HOH B . 
H 3 HOH   21  321 114 HOH   HOH B . 
H 3 HOH   22  322 152 HOH   HOH B . 
H 3 HOH   23  323 244 HOH   HOH B . 
H 3 HOH   24  324 199 HOH   HOH B . 
H 3 HOH   25  325 24  HOH   HOH B . 
H 3 HOH   26  326 299 HOH   HOH B . 
H 3 HOH   27  327 6   HOH   HOH B . 
H 3 HOH   28  328 111 HOH   HOH B . 
H 3 HOH   29  329 1   HOH   HOH B . 
H 3 HOH   30  330 306 HOH   HOH B . 
H 3 HOH   31  331 17  HOH   HOH B . 
H 3 HOH   32  332 37  HOH   HOH B . 
H 3 HOH   33  333 94  HOH   HOH B . 
H 3 HOH   34  334 164 HOH   HOH B . 
H 3 HOH   35  335 157 HOH   HOH B . 
H 3 HOH   36  336 247 HOH   HOH B . 
H 3 HOH   37  337 73  HOH   HOH B . 
H 3 HOH   38  338 290 HOH   HOH B . 
H 3 HOH   39  339 267 HOH   HOH B . 
H 3 HOH   40  340 201 HOH   HOH B . 
H 3 HOH   41  341 51  HOH   HOH B . 
H 3 HOH   42  342 39  HOH   HOH B . 
H 3 HOH   43  343 221 HOH   HOH B . 
H 3 HOH   44  344 223 HOH   HOH B . 
H 3 HOH   45  345 197 HOH   HOH B . 
H 3 HOH   46  346 80  HOH   HOH B . 
H 3 HOH   47  347 159 HOH   HOH B . 
H 3 HOH   48  348 57  HOH   HOH B . 
H 3 HOH   49  349 4   HOH   HOH B . 
H 3 HOH   50  350 317 HOH   HOH B . 
H 3 HOH   51  351 110 HOH   HOH B . 
H 3 HOH   52  352 22  HOH   HOH B . 
H 3 HOH   53  353 161 HOH   HOH B . 
H 3 HOH   54  354 102 HOH   HOH B . 
H 3 HOH   55  355 90  HOH   HOH B . 
H 3 HOH   56  356 318 HOH   HOH B . 
H 3 HOH   57  357 67  HOH   HOH B . 
H 3 HOH   58  358 36  HOH   HOH B . 
H 3 HOH   59  359 243 HOH   HOH B . 
H 3 HOH   60  360 118 HOH   HOH B . 
H 3 HOH   61  361 179 HOH   HOH B . 
H 3 HOH   62  362 280 HOH   HOH B . 
H 3 HOH   63  363 43  HOH   HOH B . 
H 3 HOH   64  364 272 HOH   HOH B . 
H 3 HOH   65  365 25  HOH   HOH B . 
H 3 HOH   66  366 322 HOH   HOH B . 
H 3 HOH   67  367 302 HOH   HOH B . 
H 3 HOH   68  368 127 HOH   HOH B . 
H 3 HOH   69  369 328 HOH   HOH B . 
H 3 HOH   70  370 58  HOH   HOH B . 
H 3 HOH   71  371 134 HOH   HOH B . 
H 3 HOH   72  372 160 HOH   HOH B . 
H 3 HOH   73  373 287 HOH   HOH B . 
H 3 HOH   74  374 291 HOH   HOH B . 
H 3 HOH   75  375 251 HOH   HOH B . 
H 3 HOH   76  376 138 HOH   HOH B . 
H 3 HOH   77  377 207 HOH   HOH B . 
H 3 HOH   78  378 222 HOH   HOH B . 
H 3 HOH   79  379 248 HOH   HOH B . 
H 3 HOH   80  380 139 HOH   HOH B . 
H 3 HOH   81  381 305 HOH   HOH B . 
H 3 HOH   82  382 228 HOH   HOH B . 
H 3 HOH   83  383 259 HOH   HOH B . 
H 3 HOH   84  384 56  HOH   HOH B . 
H 3 HOH   85  385 252 HOH   HOH B . 
H 3 HOH   86  386 30  HOH   HOH B . 
H 3 HOH   87  387 81  HOH   HOH B . 
H 3 HOH   88  388 258 HOH   HOH B . 
H 3 HOH   89  389 301 HOH   HOH B . 
H 3 HOH   90  390 212 HOH   HOH B . 
H 3 HOH   91  391 240 HOH   HOH B . 
H 3 HOH   92  392 311 HOH   HOH B . 
H 3 HOH   93  393 237 HOH   HOH B . 
H 3 HOH   94  394 140 HOH   HOH B . 
H 3 HOH   95  395 324 HOH   HOH B . 
H 3 HOH   96  396 196 HOH   HOH B . 
H 3 HOH   97  397 310 HOH   HOH B . 
H 3 HOH   98  398 275 HOH   HOH B . 
H 3 HOH   99  399 271 HOH   HOH B . 
H 3 HOH   100 400 255 HOH   HOH B . 
H 3 HOH   101 401 188 HOH   HOH B . 
H 3 HOH   102 402 89  HOH   HOH B . 
I 3 HOH   1   301 274 HOH   HOH A . 
I 3 HOH   2   302 288 HOH   HOH A . 
I 3 HOH   3   303 182 HOH   HOH A . 
I 3 HOH   4   304 125 HOH   HOH A . 
I 3 HOH   5   305 88  HOH   HOH A . 
I 3 HOH   6   306 262 HOH   HOH A . 
I 3 HOH   7   307 68  HOH   HOH A . 
I 3 HOH   8   308 31  HOH   HOH A . 
I 3 HOH   9   309 9   HOH   HOH A . 
I 3 HOH   10  310 300 HOH   HOH A . 
I 3 HOH   11  311 83  HOH   HOH A . 
I 3 HOH   12  312 69  HOH   HOH A . 
I 3 HOH   13  313 14  HOH   HOH A . 
I 3 HOH   14  314 289 HOH   HOH A . 
I 3 HOH   15  315 232 HOH   HOH A . 
I 3 HOH   16  316 66  HOH   HOH A . 
I 3 HOH   17  317 156 HOH   HOH A . 
I 3 HOH   18  318 128 HOH   HOH A . 
I 3 HOH   19  319 99  HOH   HOH A . 
I 3 HOH   20  320 116 HOH   HOH A . 
I 3 HOH   21  321 5   HOH   HOH A . 
I 3 HOH   22  322 34  HOH   HOH A . 
I 3 HOH   23  323 85  HOH   HOH A . 
I 3 HOH   24  324 21  HOH   HOH A . 
I 3 HOH   25  325 162 HOH   HOH A . 
I 3 HOH   26  326 313 HOH   HOH A . 
I 3 HOH   27  327 137 HOH   HOH A . 
I 3 HOH   28  328 216 HOH   HOH A . 
I 3 HOH   29  329 206 HOH   HOH A . 
I 3 HOH   30  330 18  HOH   HOH A . 
I 3 HOH   31  331 325 HOH   HOH A . 
I 3 HOH   32  332 136 HOH   HOH A . 
I 3 HOH   33  333 50  HOH   HOH A . 
I 3 HOH   34  334 53  HOH   HOH A . 
I 3 HOH   35  335 16  HOH   HOH A . 
I 3 HOH   36  336 15  HOH   HOH A . 
I 3 HOH   37  337 27  HOH   HOH A . 
I 3 HOH   38  338 38  HOH   HOH A . 
I 3 HOH   39  339 12  HOH   HOH A . 
I 3 HOH   40  340 55  HOH   HOH A . 
I 3 HOH   41  341 105 HOH   HOH A . 
I 3 HOH   42  342 295 HOH   HOH A . 
I 3 HOH   43  343 308 HOH   HOH A . 
I 3 HOH   44  344 329 HOH   HOH A . 
I 3 HOH   45  345 184 HOH   HOH A . 
I 3 HOH   46  346 204 HOH   HOH A . 
I 3 HOH   47  347 3   HOH   HOH A . 
I 3 HOH   48  348 115 HOH   HOH A . 
I 3 HOH   49  349 151 HOH   HOH A . 
I 3 HOH   50  350 119 HOH   HOH A . 
I 3 HOH   51  351 87  HOH   HOH A . 
I 3 HOH   52  352 190 HOH   HOH A . 
I 3 HOH   53  353 321 HOH   HOH A . 
I 3 HOH   54  354 124 HOH   HOH A . 
I 3 HOH   55  355 44  HOH   HOH A . 
I 3 HOH   56  356 19  HOH   HOH A . 
I 3 HOH   57  357 154 HOH   HOH A . 
I 3 HOH   58  358 92  HOH   HOH A . 
I 3 HOH   59  359 268 HOH   HOH A . 
I 3 HOH   60  360 42  HOH   HOH A . 
I 3 HOH   61  361 294 HOH   HOH A . 
I 3 HOH   62  362 60  HOH   HOH A . 
I 3 HOH   63  363 249 HOH   HOH A . 
I 3 HOH   64  364 48  HOH   HOH A . 
I 3 HOH   65  365 283 HOH   HOH A . 
I 3 HOH   66  366 144 HOH   HOH A . 
I 3 HOH   67  367 226 HOH   HOH A . 
I 3 HOH   68  368 141 HOH   HOH A . 
I 3 HOH   69  369 286 HOH   HOH A . 
I 3 HOH   70  370 319 HOH   HOH A . 
I 3 HOH   71  371 238 HOH   HOH A . 
I 3 HOH   72  372 218 HOH   HOH A . 
I 3 HOH   73  373 276 HOH   HOH A . 
I 3 HOH   74  374 10  HOH   HOH A . 
I 3 HOH   75  375 242 HOH   HOH A . 
I 3 HOH   76  376 323 HOH   HOH A . 
I 3 HOH   77  377 195 HOH   HOH A . 
I 3 HOH   78  378 269 HOH   HOH A . 
I 3 HOH   79  379 215 HOH   HOH A . 
I 3 HOH   80  380 239 HOH   HOH A . 
I 3 HOH   81  381 175 HOH   HOH A . 
I 3 HOH   82  382 279 HOH   HOH A . 
I 3 HOH   83  383 320 HOH   HOH A . 
I 3 HOH   84  384 217 HOH   HOH A . 
I 3 HOH   85  385 253 HOH   HOH A . 
I 3 HOH   86  386 121 HOH   HOH A . 
I 3 HOH   87  387 163 HOH   HOH A . 
I 3 HOH   88  388 149 HOH   HOH A . 
I 3 HOH   89  389 120 HOH   HOH A . 
I 3 HOH   90  390 298 HOH   HOH A . 
I 3 HOH   91  391 292 HOH   HOH A . 
I 3 HOH   92  392 214 HOH   HOH A . 
I 3 HOH   93  393 76  HOH   HOH A . 
I 3 HOH   94  394 233 HOH   HOH A . 
I 3 HOH   95  395 166 HOH   HOH A . 
I 3 HOH   96  396 62  HOH   HOH A . 
I 3 HOH   97  397 246 HOH   HOH A . 
J 3 HOH   1   201 145 HOH   HOH C . 
J 3 HOH   2   202 314 HOH   HOH C . 
J 3 HOH   3   203 296 HOH   HOH C . 
J 3 HOH   4   204 84  HOH   HOH C . 
J 3 HOH   5   205 211 HOH   HOH C . 
J 3 HOH   6   206 117 HOH   HOH C . 
J 3 HOH   7   207 315 HOH   HOH C . 
J 3 HOH   8   208 285 HOH   HOH C . 
J 3 HOH   9   209 23  HOH   HOH C . 
J 3 HOH   10  210 108 HOH   HOH C . 
J 3 HOH   11  211 104 HOH   HOH C . 
J 3 HOH   12  212 46  HOH   HOH C . 
J 3 HOH   13  213 187 HOH   HOH C . 
J 3 HOH   14  214 7   HOH   HOH C . 
J 3 HOH   15  215 72  HOH   HOH C . 
J 3 HOH   16  216 270 HOH   HOH C . 
J 3 HOH   17  217 8   HOH   HOH C . 
J 3 HOH   18  218 266 HOH   HOH C . 
J 3 HOH   19  219 77  HOH   HOH C . 
J 3 HOH   20  220 132 HOH   HOH C . 
J 3 HOH   21  221 170 HOH   HOH C . 
J 3 HOH   22  222 176 HOH   HOH C . 
J 3 HOH   23  223 200 HOH   HOH C . 
J 3 HOH   24  224 331 HOH   HOH C . 
J 3 HOH   25  225 225 HOH   HOH C . 
J 3 HOH   26  226 326 HOH   HOH C . 
J 3 HOH   27  227 78  HOH   HOH C . 
J 3 HOH   28  228 142 HOH   HOH C . 
J 3 HOH   29  229 11  HOH   HOH C . 
J 3 HOH   30  230 98  HOH   HOH C . 
J 3 HOH   31  231 278 HOH   HOH C . 
J 3 HOH   32  232 245 HOH   HOH C . 
J 3 HOH   33  233 181 HOH   HOH C . 
J 3 HOH   34  234 281 HOH   HOH C . 
J 3 HOH   35  235 189 HOH   HOH C . 
J 3 HOH   36  236 303 HOH   HOH C . 
J 3 HOH   37  237 264 HOH   HOH C . 
J 3 HOH   38  238 96  HOH   HOH C . 
J 3 HOH   39  239 224 HOH   HOH C . 
J 3 HOH   40  240 203 HOH   HOH C . 
J 3 HOH   41  241 250 HOH   HOH C . 
J 3 HOH   42  242 165 HOH   HOH C . 
J 3 HOH   43  243 74  HOH   HOH C . 
J 3 HOH   44  244 82  HOH   HOH C . 
J 3 HOH   45  245 13  HOH   HOH C . 
J 3 HOH   46  246 309 HOH   HOH C . 
J 3 HOH   47  247 40  HOH   HOH C . 
J 3 HOH   48  248 307 HOH   HOH C . 
J 3 HOH   49  249 220 HOH   HOH C . 
J 3 HOH   50  250 100 HOH   HOH C . 
J 3 HOH   51  251 107 HOH   HOH C . 
J 3 HOH   52  252 186 HOH   HOH C . 
J 3 HOH   53  253 219 HOH   HOH C . 
J 3 HOH   54  254 148 HOH   HOH C . 
J 3 HOH   55  255 135 HOH   HOH C . 
J 3 HOH   56  256 185 HOH   HOH C . 
J 3 HOH   57  257 191 HOH   HOH C . 
J 3 HOH   58  258 52  HOH   HOH C . 
J 3 HOH   59  259 198 HOH   HOH C . 
J 3 HOH   60  260 202 HOH   HOH C . 
J 3 HOH   61  261 229 HOH   HOH C . 
J 3 HOH   62  262 192 HOH   HOH C . 
J 3 HOH   63  263 112 HOH   HOH C . 
J 3 HOH   64  264 265 HOH   HOH C . 
J 3 HOH   65  265 227 HOH   HOH C . 
J 3 HOH   66  266 293 HOH   HOH C . 
J 3 HOH   67  267 327 HOH   HOH C . 
K 3 HOH   1   301 122 HOH   HOH D . 
K 3 HOH   2   302 261 HOH   HOH D . 
K 3 HOH   3   303 193 HOH   HOH D . 
K 3 HOH   4   304 20  HOH   HOH D . 
K 3 HOH   5   305 172 HOH   HOH D . 
K 3 HOH   6   306 97  HOH   HOH D . 
K 3 HOH   7   307 63  HOH   HOH D . 
K 3 HOH   8   308 41  HOH   HOH D . 
K 3 HOH   9   309 213 HOH   HOH D . 
K 3 HOH   10  310 47  HOH   HOH D . 
K 3 HOH   11  311 260 HOH   HOH D . 
K 3 HOH   12  312 174 HOH   HOH D . 
K 3 HOH   13  313 2   HOH   HOH D . 
K 3 HOH   14  314 177 HOH   HOH D . 
K 3 HOH   15  315 33  HOH   HOH D . 
K 3 HOH   16  316 101 HOH   HOH D . 
K 3 HOH   17  317 133 HOH   HOH D . 
K 3 HOH   18  318 113 HOH   HOH D . 
K 3 HOH   19  319 194 HOH   HOH D . 
K 3 HOH   20  320 263 HOH   HOH D . 
K 3 HOH   21  321 273 HOH   HOH D . 
K 3 HOH   22  322 59  HOH   HOH D . 
K 3 HOH   23  323 91  HOH   HOH D . 
K 3 HOH   24  324 316 HOH   HOH D . 
K 3 HOH   25  325 147 HOH   HOH D . 
K 3 HOH   26  326 79  HOH   HOH D . 
K 3 HOH   27  327 54  HOH   HOH D . 
K 3 HOH   28  328 28  HOH   HOH D . 
K 3 HOH   29  329 146 HOH   HOH D . 
K 3 HOH   30  330 155 HOH   HOH D . 
K 3 HOH   31  331 180 HOH   HOH D . 
K 3 HOH   32  332 71  HOH   HOH D . 
K 3 HOH   33  333 32  HOH   HOH D . 
K 3 HOH   34  334 70  HOH   HOH D . 
K 3 HOH   35  335 103 HOH   HOH D . 
K 3 HOH   36  336 61  HOH   HOH D . 
K 3 HOH   37  337 65  HOH   HOH D . 
K 3 HOH   38  338 169 HOH   HOH D . 
K 3 HOH   39  339 29  HOH   HOH D . 
K 3 HOH   40  340 284 HOH   HOH D . 
K 3 HOH   41  341 49  HOH   HOH D . 
K 3 HOH   42  342 178 HOH   HOH D . 
K 3 HOH   43  343 95  HOH   HOH D . 
K 3 HOH   44  344 158 HOH   HOH D . 
K 3 HOH   45  345 257 HOH   HOH D . 
K 3 HOH   46  346 35  HOH   HOH D . 
K 3 HOH   47  347 277 HOH   HOH D . 
K 3 HOH   48  348 256 HOH   HOH D . 
K 3 HOH   49  349 64  HOH   HOH D . 
K 3 HOH   50  350 235 HOH   HOH D . 
K 3 HOH   51  351 231 HOH   HOH D . 
K 3 HOH   52  352 330 HOH   HOH D . 
K 3 HOH   53  353 171 HOH   HOH D . 
K 3 HOH   54  354 153 HOH   HOH D . 
K 3 HOH   55  355 167 HOH   HOH D . 
K 3 HOH   56  356 126 HOH   HOH D . 
K 3 HOH   57  357 304 HOH   HOH D . 
# 
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  ? ? ? '(1.18.1_3865: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   107.82 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9K1J 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.884 
_cell.length_a_esd                 ? 
_cell.length_b                     54.235 
_cell.length_b_esd                 ? 
_cell.length_c                     87.853 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9K1J 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9K1J 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.18 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Sodium formate, 16 % w/v Polyethylene glycol 3350, 0.1 M  MES pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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         2021-06-25 
_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   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9K1J 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.09 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     38278 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.059 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.109 
_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                                    2.1 
_reflns_shell.d_res_low                                     2.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1907 
_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                               5.9 
_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                               0.399 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.809 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9K1J 
_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                            2.09 
_refine.ls_d_res_low                             41.82 
_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                     36010 
_refine.ls_number_reflns_R_free                  1850 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.50 
_refine.ls_percent_reflns_R_free                 5.14 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1977 
_refine.ls_R_factor_R_free                       0.2392 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1954 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.89 
_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                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4216 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.number_atoms_solvent             323 
_refine_hist.number_atoms_total               4572 
_refine_hist.d_res_high                       2.09 
_refine_hist.d_res_low                        41.82 
# 
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' ? 0.009 ? 4319 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.173 ? 5857 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.905 ? 631  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.071 ? 694  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 761  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.09 2.15  . . 112 1929 68.00  . . . . 0.2253 . . . . . . . . . . . 0.2943 
'X-RAY DIFFRACTION' 2.15 2.21  . . 93  2209 78.00  . . . . 0.2366 . . . . . . . . . . . 0.2592 
'X-RAY DIFFRACTION' 2.21 2.28  . . 138 2238 80.00  . . . . 0.2822 . . . . . . . . . . . 0.3863 
'X-RAY DIFFRACTION' 2.28 2.36  . . 132 2626 93.00  . . . . 0.2306 . . . . . . . . . . . 0.2958 
'X-RAY DIFFRACTION' 2.36 2.46  . . 141 2772 97.00  . . . . 0.2135 . . . . . . . . . . . 0.2598 
'X-RAY DIFFRACTION' 2.46 2.57  . . 156 2698 97.00  . . . . 0.2154 . . . . . . . . . . . 0.2757 
'X-RAY DIFFRACTION' 2.57 2.71  . . 166 2806 100.00 . . . . 0.2062 . . . . . . . . . . . 0.2722 
'X-RAY DIFFRACTION' 2.71 2.88  . . 149 2819 99.00  . . . . 0.2053 . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 2.88 3.10  . . 139 2813 99.00  . . . . 0.2098 . . . . . . . . . . . 0.2627 
'X-RAY DIFFRACTION' 3.10 3.41  . . 153 2756 97.00  . . . . 0.1899 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 3.41 3.90  . . 150 2849 99.00  . . . . 0.1907 . . . . . . . . . . . 0.2445 
'X-RAY DIFFRACTION' 3.90 4.92  . . 156 2788 97.00  . . . . 0.1617 . . . . . . . . . . . 0.1796 
'X-RAY DIFFRACTION' 4.92 41.82 . . 165 2857 97.00  . . . . 0.1610 . . . . . . . . . . . 0.1894 
# 
_struct.entry_id                     9K1J 
_struct.title                        'Crystal Structure of 6D1-Ab-ohrB complex' 
_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        9K1J 
_struct_keywords.text            'Organic hydroperoxide resistance enzyme, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q5DQT1_ACIBA 
_struct_ref.pdbx_db_accession          Q5DQT1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSTLYSTQVKAVGGRSGTIRSEDGILELKLALPKELGGKGDATNPEQLFAAGYAACFGNAVIHVTRSNKEYKIRDNDVEV
LSTVGIVANGNGGFALTVHLDVTLSGISQADAEKIVEQTHQVCPYSNAIRGNIQVSTTVYTK
;
_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 9K1J B 1 ? 142 ? Q5DQT1 1 ? 142 ? 1 142 
2 1 9K1J A 1 ? 142 ? Q5DQT1 1 ? 142 ? 1 142 
3 1 9K1J C 1 ? 142 ? Q5DQT1 1 ? 142 ? 1 142 
4 1 9K1J D 1 ? 142 ? Q5DQT1 1 ? 142 ? 1 142 
# 
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   ?    dimeric    2 
2 author_defined_assembly   ?    dimeric    2 
3 software_defined_assembly PISA tetrameric 4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
3 'ABSA (A^2)' 15890 ? 
3 MORE         -85   ? 
3 'SSA (A^2)'  22290 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,H,I           
2 1 C,D,G,J,K             
3 1 A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 14  ? SER A 16  ? GLY B 14  SER B 16  5 ? 3  
HELX_P HELX_P2  AA2 PRO A 33  ? GLY A 37  ? PRO B 33  GLY B 37  5 ? 5  
HELX_P HELX_P3  AA3 ASN A 44  ? LYS A 69  ? ASN B 44  LYS B 69  1 ? 26 
HELX_P HELX_P4  AA4 ARG A 74  ? ASN A 76  ? ARG B 74  ASN B 76  5 ? 3  
HELX_P HELX_P5  AA5 SER A 108 ? CYS A 123 ? SER B 108 CYS B 123 1 ? 16 
HELX_P HELX_P6  AA6 CYS A 123 ? ARG A 130 ? CYS B 123 ARG B 130 1 ? 8  
HELX_P HELX_P7  AA7 GLY B 14  ? SER B 16  ? GLY A 14  SER A 16  5 ? 3  
HELX_P HELX_P8  AA8 PRO B 33  ? GLY B 37  ? PRO A 33  GLY A 37  5 ? 5  
HELX_P HELX_P9  AA9 ASN B 44  ? LYS B 69  ? ASN A 44  LYS A 69  1 ? 26 
HELX_P HELX_P10 AB1 ARG B 74  ? ASN B 76  ? ARG A 74  ASN A 76  5 ? 3  
HELX_P HELX_P11 AB2 SER B 108 ? CYS B 123 ? SER A 108 CYS A 123 1 ? 16 
HELX_P HELX_P12 AB3 CYS B 123 ? ARG B 130 ? CYS A 123 ARG A 130 1 ? 8  
HELX_P HELX_P13 AB4 GLY C 14  ? SER C 16  ? GLY C 14  SER C 16  5 ? 3  
HELX_P HELX_P14 AB5 PRO C 33  ? GLY C 37  ? PRO C 33  GLY C 37  5 ? 5  
HELX_P HELX_P15 AB6 ASN C 44  ? LYS C 69  ? ASN C 44  LYS C 69  1 ? 26 
HELX_P HELX_P16 AB7 ARG C 74  ? ASN C 76  ? ARG C 74  ASN C 76  5 ? 3  
HELX_P HELX_P17 AB8 SER C 108 ? CYS C 123 ? SER C 108 CYS C 123 1 ? 16 
HELX_P HELX_P18 AB9 CYS C 123 ? ARG C 130 ? CYS C 123 ARG C 130 1 ? 8  
HELX_P HELX_P19 AC1 GLY D 14  ? SER D 16  ? GLY D 14  SER D 16  5 ? 3  
HELX_P HELX_P20 AC2 PRO D 33  ? GLY D 37  ? PRO D 33  GLY D 37  5 ? 5  
HELX_P HELX_P21 AC3 ASN D 44  ? ARG D 66  ? ASN D 44  ARG D 66  1 ? 23 
HELX_P HELX_P22 AC4 ARG D 74  ? ASN D 76  ? ARG D 74  ASN D 76  5 ? 3  
HELX_P HELX_P23 AC5 SER D 108 ? HIS D 120 ? SER D 108 HIS D 120 1 ? 13 
HELX_P HELX_P24 AC6 CYS D 123 ? ARG D 130 ? CYS D 123 ARG D 130 1 ? 8  
# 
_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 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
# 
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 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? 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 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? 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 GLU A 27  ? LYS A 29  ? GLU B 27  LYS B 29  
AA1 2 THR A 18  ? SER A 21  ? THR B 18  SER B 21  
AA1 3 TYR A 5   ? VAL A 12  ? TYR B 5   VAL B 12  
AA1 4 VAL B 78  ? ALA B 88  ? VAL A 78  ALA A 88  
AA1 5 PHE B 94  ? LEU B 104 ? PHE A 94  LEU A 104 
AA1 6 SER B 136 ? TYR B 140 ? SER A 136 TYR A 140 
AA2 1 SER A 136 ? LYS A 142 ? SER B 136 LYS B 142 
AA2 2 GLY A 93  ? SER A 105 ? GLY B 93  SER B 105 
AA2 3 VAL A 78  ? ASN A 89  ? VAL B 78  ASN B 89  
AA2 4 THR B 3   ? VAL B 12  ? THR A 3   VAL A 12  
AA2 5 THR B 18  ? SER B 21  ? THR A 18  SER A 21  
AA2 6 GLU B 27  ? LYS B 29  ? GLU A 27  LYS A 29  
AA3 1 GLU C 27  ? LYS C 29  ? GLU C 27  LYS C 29  
AA3 2 THR C 18  ? SER C 21  ? THR C 18  SER C 21  
AA3 3 TYR C 5   ? VAL C 12  ? TYR C 5   VAL C 12  
AA3 4 VAL D 78  ? ALA D 88  ? VAL D 78  ALA D 88  
AA3 5 PHE D 94  ? SER D 105 ? PHE D 94  SER D 105 
AA3 6 SER D 136 ? LYS D 142 ? SER D 136 LYS D 142 
AA4 1 SER C 136 ? LYS C 142 ? SER C 136 LYS C 142 
AA4 2 PHE C 94  ? SER C 105 ? PHE C 94  SER C 105 
AA4 3 VAL C 78  ? ALA C 88  ? VAL C 78  ALA C 88  
AA4 4 THR D 3   ? VAL D 12  ? THR D 3   VAL D 12  
AA4 5 THR D 18  ? SER D 21  ? THR D 18  SER D 21  
AA4 6 GLU D 27  ? LYS D 29  ? GLU D 27  LYS D 29  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 28  ? O LEU B 28  N ILE A 19  ? N ILE B 19  
AA1 2 3 O ARG A 20  ? O ARG B 20  N LYS A 10  ? N LYS B 10  
AA1 3 4 N ALA A 11  ? N ALA B 11  O VAL B 80  ? O VAL A 80  
AA1 4 5 N VAL B 87  ? N VAL A 87  O ALA B 95  ? O ALA A 95  
AA1 5 6 N VAL B 102 ? N VAL A 102 O TYR B 140 ? O TYR A 140 
AA2 1 2 O TYR A 140 ? O TYR B 140 N VAL A 102 ? N VAL B 102 
AA2 2 3 O HIS A 99  ? O HIS B 99  N THR A 83  ? N THR B 83  
AA2 3 4 N VAL A 80  ? N VAL B 80  O ALA B 11  ? O ALA A 11  
AA2 4 5 N LYS B 10  ? N LYS A 10  O ARG B 20  ? O ARG A 20  
AA2 5 6 N ILE B 19  ? N ILE A 19  O LEU B 28  ? O LEU A 28  
AA3 1 2 O LEU C 28  ? O LEU C 28  N ILE C 19  ? N ILE C 19  
AA3 2 3 O ARG C 20  ? O ARG C 20  N LYS C 10  ? N LYS C 10  
AA3 3 4 N VAL C 9   ? N VAL C 9   O SER D 82  ? O SER D 82  
AA3 4 5 N VAL D 87  ? N VAL D 87  O ALA D 95  ? O ALA D 95  
AA3 5 6 N VAL D 102 ? N VAL D 102 O TYR D 140 ? O TYR D 140 
AA4 1 2 O TYR C 140 ? O TYR C 140 N VAL C 102 ? N VAL C 102 
AA4 2 3 O HIS C 99  ? O HIS C 99  N THR C 83  ? N THR C 83  
AA4 3 4 N VAL C 80  ? N VAL C 80  O ALA D 11  ? O ALA D 11  
AA4 4 5 N LYS D 10  ? N LYS D 10  O ARG D 20  ? O ARG D 20  
AA4 5 6 N ILE D 19  ? N ILE D 19  O LEU D 28  ? O LEU D 28  
# 
_pdbx_entry_details.entry_id                   9K1J 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 C GLU 22  ? ? O C HOH 201 ? ? 2.16 
2 1 NZ  A LYS 114 ? ? O A HOH 301 ? ? 2.17 
3 1 OD2 B ASP 41  ? ? O B HOH 301 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     383 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     387 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              2.06 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB B TYR 53 ? ? CG B TYR 53 ? ? CD2 B TYR 53 ? ? 116.95 121.00 -4.05 0.60 N 
2 1 CB C ASN 91 ? ? CA C ASN 91 ? ? C   C ASN 91 ? ? 122.79 110.40 12.39 2.00 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 SER A 67 ? ? 73.76   -43.80 
2 1 LYS C 69 ? ? 89.60   -6.54  
3 1 ASN C 91 ? ? -164.20 50.52  
4 1 SER D 67 ? ? 47.63   21.22  
5 1 LYS D 69 ? ? 80.60   -18.55 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ASP B 41 ? ? ALA B 42 ? ? -144.16 
2 1 GLY D 90 ? ? ASN D 91 ? ? -147.28 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR B 53 ? ? 0.079 'SIDE CHAIN' 
2 1 TYR A 53 ? ? 0.060 'SIDE CHAIN' 
3 1 TYR C 53 ? ? 0.058 'SIDE CHAIN' 
4 1 TYR D 53 ? ? 0.063 'SIDE CHAIN' 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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 
A1EEB N1   N N N 1   
A1EEB C1   C N N 2   
A1EEB C2   C Y N 3   
A1EEB C3   C Y N 4   
A1EEB C4   C Y N 5   
A1EEB C5   C Y N 6   
A1EEB C6   C Y N 7   
A1EEB C7   C Y N 8   
A1EEB O1   O N N 9   
A1EEB F1   F N N 10  
A1EEB S1   S N N 11  
A1EEB H1   H N N 12  
A1EEB H2   H N N 13  
A1EEB H3   H N N 14  
A1EEB H4   H N N 15  
ALA   N    N N N 16  
ALA   CA   C N S 17  
ALA   C    C N N 18  
ALA   O    O N N 19  
ALA   CB   C N N 20  
ALA   OXT  O N N 21  
ALA   H    H N N 22  
ALA   H2   H N N 23  
ALA   HA   H N N 24  
ALA   HB1  H N N 25  
ALA   HB2  H N N 26  
ALA   HB3  H N N 27  
ALA   HXT  H N N 28  
ARG   N    N N N 29  
ARG   CA   C N S 30  
ARG   C    C N N 31  
ARG   O    O N N 32  
ARG   CB   C N N 33  
ARG   CG   C N N 34  
ARG   CD   C N N 35  
ARG   NE   N N N 36  
ARG   CZ   C N N 37  
ARG   NH1  N N N 38  
ARG   NH2  N N N 39  
ARG   OXT  O N N 40  
ARG   H    H N N 41  
ARG   H2   H N N 42  
ARG   HA   H N N 43  
ARG   HB2  H N N 44  
ARG   HB3  H N N 45  
ARG   HG2  H N N 46  
ARG   HG3  H N N 47  
ARG   HD2  H N N 48  
ARG   HD3  H N N 49  
ARG   HE   H N N 50  
ARG   HH11 H N N 51  
ARG   HH12 H N N 52  
ARG   HH21 H N N 53  
ARG   HH22 H N N 54  
ARG   HXT  H N N 55  
ASN   N    N N N 56  
ASN   CA   C N S 57  
ASN   C    C N N 58  
ASN   O    O N N 59  
ASN   CB   C N N 60  
ASN   CG   C N N 61  
ASN   OD1  O N N 62  
ASN   ND2  N N N 63  
ASN   OXT  O N N 64  
ASN   H    H N N 65  
ASN   H2   H N N 66  
ASN   HA   H N N 67  
ASN   HB2  H N N 68  
ASN   HB3  H N N 69  
ASN   HD21 H N N 70  
ASN   HD22 H N N 71  
ASN   HXT  H N N 72  
ASP   N    N N N 73  
ASP   CA   C N S 74  
ASP   C    C N N 75  
ASP   O    O N N 76  
ASP   CB   C N N 77  
ASP   CG   C N N 78  
ASP   OD1  O N N 79  
ASP   OD2  O N N 80  
ASP   OXT  O N N 81  
ASP   H    H N N 82  
ASP   H2   H N N 83  
ASP   HA   H N N 84  
ASP   HB2  H N N 85  
ASP   HB3  H N N 86  
ASP   HD2  H N N 87  
ASP   HXT  H N N 88  
CYS   N    N N N 89  
CYS   CA   C N R 90  
CYS   C    C N N 91  
CYS   O    O N N 92  
CYS   CB   C N N 93  
CYS   SG   S N N 94  
CYS   OXT  O N N 95  
CYS   H    H N N 96  
CYS   H2   H N N 97  
CYS   HA   H N N 98  
CYS   HB2  H N N 99  
CYS   HB3  H N N 100 
CYS   HG   H N N 101 
CYS   HXT  H N N 102 
GLN   N    N N N 103 
GLN   CA   C N S 104 
GLN   C    C N N 105 
GLN   O    O N N 106 
GLN   CB   C N N 107 
GLN   CG   C N N 108 
GLN   CD   C N N 109 
GLN   OE1  O N N 110 
GLN   NE2  N N N 111 
GLN   OXT  O N N 112 
GLN   H    H N N 113 
GLN   H2   H N N 114 
GLN   HA   H N N 115 
GLN   HB2  H N N 116 
GLN   HB3  H N N 117 
GLN   HG2  H N N 118 
GLN   HG3  H N N 119 
GLN   HE21 H N N 120 
GLN   HE22 H N N 121 
GLN   HXT  H N N 122 
GLU   N    N N N 123 
GLU   CA   C N S 124 
GLU   C    C N N 125 
GLU   O    O N N 126 
GLU   CB   C N N 127 
GLU   CG   C N N 128 
GLU   CD   C N N 129 
GLU   OE1  O N N 130 
GLU   OE2  O N N 131 
GLU   OXT  O N N 132 
GLU   H    H N N 133 
GLU   H2   H N N 134 
GLU   HA   H N N 135 
GLU   HB2  H N N 136 
GLU   HB3  H N N 137 
GLU   HG2  H N N 138 
GLU   HG3  H N N 139 
GLU   HE2  H N N 140 
GLU   HXT  H N N 141 
GLY   N    N N N 142 
GLY   CA   C N N 143 
GLY   C    C N N 144 
GLY   O    O N N 145 
GLY   OXT  O N N 146 
GLY   H    H N N 147 
GLY   H2   H N N 148 
GLY   HA2  H N N 149 
GLY   HA3  H N N 150 
GLY   HXT  H N N 151 
HIS   N    N N N 152 
HIS   CA   C N S 153 
HIS   C    C N N 154 
HIS   O    O N N 155 
HIS   CB   C N N 156 
HIS   CG   C Y N 157 
HIS   ND1  N Y N 158 
HIS   CD2  C Y N 159 
HIS   CE1  C Y N 160 
HIS   NE2  N Y N 161 
HIS   OXT  O N N 162 
HIS   H    H N N 163 
HIS   H2   H N N 164 
HIS   HA   H N N 165 
HIS   HB2  H N N 166 
HIS   HB3  H N N 167 
HIS   HD1  H N N 168 
HIS   HD2  H N N 169 
HIS   HE1  H N N 170 
HIS   HE2  H N N 171 
HIS   HXT  H N N 172 
HOH   O    O N N 173 
HOH   H1   H N N 174 
HOH   H2   H N N 175 
ILE   N    N N N 176 
ILE   CA   C N S 177 
ILE   C    C N N 178 
ILE   O    O N N 179 
ILE   CB   C N S 180 
ILE   CG1  C N N 181 
ILE   CG2  C N N 182 
ILE   CD1  C N N 183 
ILE   OXT  O N N 184 
ILE   H    H N N 185 
ILE   H2   H N N 186 
ILE   HA   H N N 187 
ILE   HB   H N N 188 
ILE   HG12 H N N 189 
ILE   HG13 H N N 190 
ILE   HG21 H N N 191 
ILE   HG22 H N N 192 
ILE   HG23 H N N 193 
ILE   HD11 H N N 194 
ILE   HD12 H N N 195 
ILE   HD13 H N N 196 
ILE   HXT  H N N 197 
LEU   N    N N N 198 
LEU   CA   C N S 199 
LEU   C    C N N 200 
LEU   O    O N N 201 
LEU   CB   C N N 202 
LEU   CG   C N N 203 
LEU   CD1  C N N 204 
LEU   CD2  C N N 205 
LEU   OXT  O N N 206 
LEU   H    H N N 207 
LEU   H2   H N N 208 
LEU   HA   H N N 209 
LEU   HB2  H N N 210 
LEU   HB3  H N N 211 
LEU   HG   H N N 212 
LEU   HD11 H N N 213 
LEU   HD12 H N N 214 
LEU   HD13 H N N 215 
LEU   HD21 H N N 216 
LEU   HD22 H N N 217 
LEU   HD23 H N N 218 
LEU   HXT  H N N 219 
LYS   N    N N N 220 
LYS   CA   C N S 221 
LYS   C    C N N 222 
LYS   O    O N N 223 
LYS   CB   C N N 224 
LYS   CG   C N N 225 
LYS   CD   C N N 226 
LYS   CE   C N N 227 
LYS   NZ   N N N 228 
LYS   OXT  O N N 229 
LYS   H    H N N 230 
LYS   H2   H N N 231 
LYS   HA   H N N 232 
LYS   HB2  H N N 233 
LYS   HB3  H N N 234 
LYS   HG2  H N N 235 
LYS   HG3  H N N 236 
LYS   HD2  H N N 237 
LYS   HD3  H N N 238 
LYS   HE2  H N N 239 
LYS   HE3  H N N 240 
LYS   HZ1  H N N 241 
LYS   HZ2  H N N 242 
LYS   HZ3  H N N 243 
LYS   HXT  H N N 244 
MET   N    N N N 245 
MET   CA   C N S 246 
MET   C    C N N 247 
MET   O    O N N 248 
MET   CB   C N N 249 
MET   CG   C N N 250 
MET   SD   S N N 251 
MET   CE   C N N 252 
MET   OXT  O N N 253 
MET   H    H N N 254 
MET   H2   H N N 255 
MET   HA   H N N 256 
MET   HB2  H N N 257 
MET   HB3  H N N 258 
MET   HG2  H N N 259 
MET   HG3  H N N 260 
MET   HE1  H N N 261 
MET   HE2  H N N 262 
MET   HE3  H N N 263 
MET   HXT  H N N 264 
PHE   N    N N N 265 
PHE   CA   C N S 266 
PHE   C    C N N 267 
PHE   O    O N N 268 
PHE   CB   C N N 269 
PHE   CG   C Y N 270 
PHE   CD1  C Y N 271 
PHE   CD2  C Y N 272 
PHE   CE1  C Y N 273 
PHE   CE2  C Y N 274 
PHE   CZ   C Y N 275 
PHE   OXT  O N N 276 
PHE   H    H N N 277 
PHE   H2   H N N 278 
PHE   HA   H N N 279 
PHE   HB2  H N N 280 
PHE   HB3  H N N 281 
PHE   HD1  H N N 282 
PHE   HD2  H N N 283 
PHE   HE1  H N N 284 
PHE   HE2  H N N 285 
PHE   HZ   H N N 286 
PHE   HXT  H N N 287 
PRO   N    N N N 288 
PRO   CA   C N S 289 
PRO   C    C N N 290 
PRO   O    O N N 291 
PRO   CB   C N N 292 
PRO   CG   C N N 293 
PRO   CD   C N N 294 
PRO   OXT  O N N 295 
PRO   H    H N N 296 
PRO   HA   H N N 297 
PRO   HB2  H N N 298 
PRO   HB3  H N N 299 
PRO   HG2  H N N 300 
PRO   HG3  H N N 301 
PRO   HD2  H N N 302 
PRO   HD3  H N N 303 
PRO   HXT  H N N 304 
SER   N    N N N 305 
SER   CA   C N S 306 
SER   C    C N N 307 
SER   O    O N N 308 
SER   CB   C N N 309 
SER   OG   O N N 310 
SER   OXT  O N N 311 
SER   H    H N N 312 
SER   H2   H N N 313 
SER   HA   H N N 314 
SER   HB2  H N N 315 
SER   HB3  H N N 316 
SER   HG   H N N 317 
SER   HXT  H N N 318 
THR   N    N N N 319 
THR   CA   C N S 320 
THR   C    C N N 321 
THR   O    O N N 322 
THR   CB   C N R 323 
THR   OG1  O N N 324 
THR   CG2  C N N 325 
THR   OXT  O N N 326 
THR   H    H N N 327 
THR   H2   H N N 328 
THR   HA   H N N 329 
THR   HB   H N N 330 
THR   HG1  H N N 331 
THR   HG21 H N N 332 
THR   HG22 H N N 333 
THR   HG23 H N N 334 
THR   HXT  H N N 335 
TYR   N    N N N 336 
TYR   CA   C N S 337 
TYR   C    C N N 338 
TYR   O    O N N 339 
TYR   CB   C N N 340 
TYR   CG   C Y N 341 
TYR   CD1  C Y N 342 
TYR   CD2  C Y N 343 
TYR   CE1  C Y N 344 
TYR   CE2  C Y N 345 
TYR   CZ   C Y N 346 
TYR   OH   O N N 347 
TYR   OXT  O N N 348 
TYR   H    H N N 349 
TYR   H2   H N N 350 
TYR   HA   H N N 351 
TYR   HB2  H N N 352 
TYR   HB3  H N N 353 
TYR   HD1  H N N 354 
TYR   HD2  H N N 355 
TYR   HE1  H N N 356 
TYR   HE2  H N N 357 
TYR   HH   H N N 358 
TYR   HXT  H N N 359 
VAL   N    N N N 360 
VAL   CA   C N S 361 
VAL   C    C N N 362 
VAL   O    O N N 363 
VAL   CB   C N N 364 
VAL   CG1  C N N 365 
VAL   CG2  C N N 366 
VAL   OXT  O N N 367 
VAL   H    H N N 368 
VAL   H2   H N N 369 
VAL   HA   H N N 370 
VAL   HB   H N N 371 
VAL   HG11 H N N 372 
VAL   HG12 H N N 373 
VAL   HG13 H N N 374 
VAL   HG21 H N N 375 
VAL   HG22 H N N 376 
VAL   HG23 H N N 377 
VAL   HXT  H N N 378 
# 
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 
A1EEB F1  C4   sing N N 1   
A1EEB C3  C4   doub Y N 2   
A1EEB C3  C2   sing Y N 3   
A1EEB C4  C5   sing Y N 4   
A1EEB C2  S1   sing N N 5   
A1EEB C2  C7   doub Y N 6   
A1EEB S1  N1   sing N N 7   
A1EEB C5  C6   doub Y N 8   
A1EEB C7  C6   sing Y N 9   
A1EEB C7  C1   sing N N 10  
A1EEB N1  C1   sing N N 11  
A1EEB C1  O1   doub N N 12  
A1EEB N1  H1   sing N N 13  
A1EEB C3  H2   sing N N 14  
A1EEB C5  H3   sing N N 15  
A1EEB C6  H4   sing N N 16  
ALA   N   CA   sing N N 17  
ALA   N   H    sing N N 18  
ALA   N   H2   sing N N 19  
ALA   CA  C    sing N N 20  
ALA   CA  CB   sing N N 21  
ALA   CA  HA   sing N N 22  
ALA   C   O    doub N N 23  
ALA   C   OXT  sing N N 24  
ALA   CB  HB1  sing N N 25  
ALA   CB  HB2  sing N N 26  
ALA   CB  HB3  sing N N 27  
ALA   OXT HXT  sing N N 28  
ARG   N   CA   sing N N 29  
ARG   N   H    sing N N 30  
ARG   N   H2   sing N N 31  
ARG   CA  C    sing N N 32  
ARG   CA  CB   sing N N 33  
ARG   CA  HA   sing N N 34  
ARG   C   O    doub N N 35  
ARG   C   OXT  sing N N 36  
ARG   CB  CG   sing N N 37  
ARG   CB  HB2  sing N N 38  
ARG   CB  HB3  sing N N 39  
ARG   CG  CD   sing N N 40  
ARG   CG  HG2  sing N N 41  
ARG   CG  HG3  sing N N 42  
ARG   CD  NE   sing N N 43  
ARG   CD  HD2  sing N N 44  
ARG   CD  HD3  sing N N 45  
ARG   NE  CZ   sing N N 46  
ARG   NE  HE   sing N N 47  
ARG   CZ  NH1  sing N N 48  
ARG   CZ  NH2  doub N N 49  
ARG   NH1 HH11 sing N N 50  
ARG   NH1 HH12 sing N N 51  
ARG   NH2 HH21 sing N N 52  
ARG   NH2 HH22 sing N N 53  
ARG   OXT HXT  sing N N 54  
ASN   N   CA   sing N N 55  
ASN   N   H    sing N N 56  
ASN   N   H2   sing N N 57  
ASN   CA  C    sing N N 58  
ASN   CA  CB   sing N N 59  
ASN   CA  HA   sing N N 60  
ASN   C   O    doub N N 61  
ASN   C   OXT  sing N N 62  
ASN   CB  CG   sing N N 63  
ASN   CB  HB2  sing N N 64  
ASN   CB  HB3  sing N N 65  
ASN   CG  OD1  doub N N 66  
ASN   CG  ND2  sing N N 67  
ASN   ND2 HD21 sing N N 68  
ASN   ND2 HD22 sing N N 69  
ASN   OXT HXT  sing N N 70  
ASP   N   CA   sing N N 71  
ASP   N   H    sing N N 72  
ASP   N   H2   sing N N 73  
ASP   CA  C    sing N N 74  
ASP   CA  CB   sing N N 75  
ASP   CA  HA   sing N N 76  
ASP   C   O    doub N N 77  
ASP   C   OXT  sing N N 78  
ASP   CB  CG   sing N N 79  
ASP   CB  HB2  sing N N 80  
ASP   CB  HB3  sing N N 81  
ASP   CG  OD1  doub N N 82  
ASP   CG  OD2  sing N N 83  
ASP   OD2 HD2  sing N N 84  
ASP   OXT HXT  sing N N 85  
CYS   N   CA   sing N N 86  
CYS   N   H    sing N N 87  
CYS   N   H2   sing N N 88  
CYS   CA  C    sing N N 89  
CYS   CA  CB   sing N N 90  
CYS   CA  HA   sing N N 91  
CYS   C   O    doub N N 92  
CYS   C   OXT  sing N N 93  
CYS   CB  SG   sing N N 94  
CYS   CB  HB2  sing N N 95  
CYS   CB  HB3  sing N N 96  
CYS   SG  HG   sing N N 97  
CYS   OXT HXT  sing N N 98  
GLN   N   CA   sing N N 99  
GLN   N   H    sing N N 100 
GLN   N   H2   sing N N 101 
GLN   CA  C    sing N N 102 
GLN   CA  CB   sing N N 103 
GLN   CA  HA   sing N N 104 
GLN   C   O    doub N N 105 
GLN   C   OXT  sing N N 106 
GLN   CB  CG   sing N N 107 
GLN   CB  HB2  sing N N 108 
GLN   CB  HB3  sing N N 109 
GLN   CG  CD   sing N N 110 
GLN   CG  HG2  sing N N 111 
GLN   CG  HG3  sing N N 112 
GLN   CD  OE1  doub N N 113 
GLN   CD  NE2  sing N N 114 
GLN   NE2 HE21 sing N N 115 
GLN   NE2 HE22 sing N N 116 
GLN   OXT HXT  sing N N 117 
GLU   N   CA   sing N N 118 
GLU   N   H    sing N N 119 
GLU   N   H2   sing N N 120 
GLU   CA  C    sing N N 121 
GLU   CA  CB   sing N N 122 
GLU   CA  HA   sing N N 123 
GLU   C   O    doub N N 124 
GLU   C   OXT  sing N N 125 
GLU   CB  CG   sing N N 126 
GLU   CB  HB2  sing N N 127 
GLU   CB  HB3  sing N N 128 
GLU   CG  CD   sing N N 129 
GLU   CG  HG2  sing N N 130 
GLU   CG  HG3  sing N N 131 
GLU   CD  OE1  doub N N 132 
GLU   CD  OE2  sing N N 133 
GLU   OE2 HE2  sing N N 134 
GLU   OXT HXT  sing N N 135 
GLY   N   CA   sing N N 136 
GLY   N   H    sing N N 137 
GLY   N   H2   sing N N 138 
GLY   CA  C    sing N N 139 
GLY   CA  HA2  sing N N 140 
GLY   CA  HA3  sing N N 141 
GLY   C   O    doub N N 142 
GLY   C   OXT  sing N N 143 
GLY   OXT HXT  sing N N 144 
HIS   N   CA   sing N N 145 
HIS   N   H    sing N N 146 
HIS   N   H2   sing N N 147 
HIS   CA  C    sing N N 148 
HIS   CA  CB   sing N N 149 
HIS   CA  HA   sing N N 150 
HIS   C   O    doub N N 151 
HIS   C   OXT  sing N N 152 
HIS   CB  CG   sing N N 153 
HIS   CB  HB2  sing N N 154 
HIS   CB  HB3  sing N N 155 
HIS   CG  ND1  sing Y N 156 
HIS   CG  CD2  doub Y N 157 
HIS   ND1 CE1  doub Y N 158 
HIS   ND1 HD1  sing N N 159 
HIS   CD2 NE2  sing Y N 160 
HIS   CD2 HD2  sing N N 161 
HIS   CE1 NE2  sing Y N 162 
HIS   CE1 HE1  sing N N 163 
HIS   NE2 HE2  sing N N 164 
HIS   OXT HXT  sing N N 165 
HOH   O   H1   sing N N 166 
HOH   O   H2   sing N N 167 
ILE   N   CA   sing N N 168 
ILE   N   H    sing N N 169 
ILE   N   H2   sing N N 170 
ILE   CA  C    sing N N 171 
ILE   CA  CB   sing N N 172 
ILE   CA  HA   sing N N 173 
ILE   C   O    doub N N 174 
ILE   C   OXT  sing N N 175 
ILE   CB  CG1  sing N N 176 
ILE   CB  CG2  sing N N 177 
ILE   CB  HB   sing N N 178 
ILE   CG1 CD1  sing N N 179 
ILE   CG1 HG12 sing N N 180 
ILE   CG1 HG13 sing N N 181 
ILE   CG2 HG21 sing N N 182 
ILE   CG2 HG22 sing N N 183 
ILE   CG2 HG23 sing N N 184 
ILE   CD1 HD11 sing N N 185 
ILE   CD1 HD12 sing N N 186 
ILE   CD1 HD13 sing N N 187 
ILE   OXT HXT  sing N N 188 
LEU   N   CA   sing N N 189 
LEU   N   H    sing N N 190 
LEU   N   H2   sing N N 191 
LEU   CA  C    sing N N 192 
LEU   CA  CB   sing N N 193 
LEU   CA  HA   sing N N 194 
LEU   C   O    doub N N 195 
LEU   C   OXT  sing N N 196 
LEU   CB  CG   sing N N 197 
LEU   CB  HB2  sing N N 198 
LEU   CB  HB3  sing N N 199 
LEU   CG  CD1  sing N N 200 
LEU   CG  CD2  sing N N 201 
LEU   CG  HG   sing N N 202 
LEU   CD1 HD11 sing N N 203 
LEU   CD1 HD12 sing N N 204 
LEU   CD1 HD13 sing N N 205 
LEU   CD2 HD21 sing N N 206 
LEU   CD2 HD22 sing N N 207 
LEU   CD2 HD23 sing N N 208 
LEU   OXT HXT  sing N N 209 
LYS   N   CA   sing N N 210 
LYS   N   H    sing N N 211 
LYS   N   H2   sing N N 212 
LYS   CA  C    sing N N 213 
LYS   CA  CB   sing N N 214 
LYS   CA  HA   sing N N 215 
LYS   C   O    doub N N 216 
LYS   C   OXT  sing N N 217 
LYS   CB  CG   sing N N 218 
LYS   CB  HB2  sing N N 219 
LYS   CB  HB3  sing N N 220 
LYS   CG  CD   sing N N 221 
LYS   CG  HG2  sing N N 222 
LYS   CG  HG3  sing N N 223 
LYS   CD  CE   sing N N 224 
LYS   CD  HD2  sing N N 225 
LYS   CD  HD3  sing N N 226 
LYS   CE  NZ   sing N N 227 
LYS   CE  HE2  sing N N 228 
LYS   CE  HE3  sing N N 229 
LYS   NZ  HZ1  sing N N 230 
LYS   NZ  HZ2  sing N N 231 
LYS   NZ  HZ3  sing N N 232 
LYS   OXT HXT  sing N N 233 
MET   N   CA   sing N N 234 
MET   N   H    sing N N 235 
MET   N   H2   sing N N 236 
MET   CA  C    sing N N 237 
MET   CA  CB   sing N N 238 
MET   CA  HA   sing N N 239 
MET   C   O    doub N N 240 
MET   C   OXT  sing N N 241 
MET   CB  CG   sing N N 242 
MET   CB  HB2  sing N N 243 
MET   CB  HB3  sing N N 244 
MET   CG  SD   sing N N 245 
MET   CG  HG2  sing N N 246 
MET   CG  HG3  sing N N 247 
MET   SD  CE   sing N N 248 
MET   CE  HE1  sing N N 249 
MET   CE  HE2  sing N N 250 
MET   CE  HE3  sing N N 251 
MET   OXT HXT  sing N N 252 
PHE   N   CA   sing N N 253 
PHE   N   H    sing N N 254 
PHE   N   H2   sing N N 255 
PHE   CA  C    sing N N 256 
PHE   CA  CB   sing N N 257 
PHE   CA  HA   sing N N 258 
PHE   C   O    doub N N 259 
PHE   C   OXT  sing N N 260 
PHE   CB  CG   sing N N 261 
PHE   CB  HB2  sing N N 262 
PHE   CB  HB3  sing N N 263 
PHE   CG  CD1  doub Y N 264 
PHE   CG  CD2  sing Y N 265 
PHE   CD1 CE1  sing Y N 266 
PHE   CD1 HD1  sing N N 267 
PHE   CD2 CE2  doub Y N 268 
PHE   CD2 HD2  sing N N 269 
PHE   CE1 CZ   doub Y N 270 
PHE   CE1 HE1  sing N N 271 
PHE   CE2 CZ   sing Y N 272 
PHE   CE2 HE2  sing N N 273 
PHE   CZ  HZ   sing N N 274 
PHE   OXT HXT  sing N N 275 
PRO   N   CA   sing N N 276 
PRO   N   CD   sing N N 277 
PRO   N   H    sing N N 278 
PRO   CA  C    sing N N 279 
PRO   CA  CB   sing N N 280 
PRO   CA  HA   sing N N 281 
PRO   C   O    doub N N 282 
PRO   C   OXT  sing N N 283 
PRO   CB  CG   sing N N 284 
PRO   CB  HB2  sing N N 285 
PRO   CB  HB3  sing N N 286 
PRO   CG  CD   sing N N 287 
PRO   CG  HG2  sing N N 288 
PRO   CG  HG3  sing N N 289 
PRO   CD  HD2  sing N N 290 
PRO   CD  HD3  sing N N 291 
PRO   OXT HXT  sing N N 292 
SER   N   CA   sing N N 293 
SER   N   H    sing N N 294 
SER   N   H2   sing N N 295 
SER   CA  C    sing N N 296 
SER   CA  CB   sing N N 297 
SER   CA  HA   sing N N 298 
SER   C   O    doub N N 299 
SER   C   OXT  sing N N 300 
SER   CB  OG   sing N N 301 
SER   CB  HB2  sing N N 302 
SER   CB  HB3  sing N N 303 
SER   OG  HG   sing N N 304 
SER   OXT HXT  sing N N 305 
THR   N   CA   sing N N 306 
THR   N   H    sing N N 307 
THR   N   H2   sing N N 308 
THR   CA  C    sing N N 309 
THR   CA  CB   sing N N 310 
THR   CA  HA   sing N N 311 
THR   C   O    doub N N 312 
THR   C   OXT  sing N N 313 
THR   CB  OG1  sing N N 314 
THR   CB  CG2  sing N N 315 
THR   CB  HB   sing N N 316 
THR   OG1 HG1  sing N N 317 
THR   CG2 HG21 sing N N 318 
THR   CG2 HG22 sing N N 319 
THR   CG2 HG23 sing N N 320 
THR   OXT HXT  sing N N 321 
TYR   N   CA   sing N N 322 
TYR   N   H    sing N N 323 
TYR   N   H2   sing N N 324 
TYR   CA  C    sing N N 325 
TYR   CA  CB   sing N N 326 
TYR   CA  HA   sing N N 327 
TYR   C   O    doub N N 328 
TYR   C   OXT  sing N N 329 
TYR   CB  CG   sing N N 330 
TYR   CB  HB2  sing N N 331 
TYR   CB  HB3  sing N N 332 
TYR   CG  CD1  doub Y N 333 
TYR   CG  CD2  sing Y N 334 
TYR   CD1 CE1  sing Y N 335 
TYR   CD1 HD1  sing N N 336 
TYR   CD2 CE2  doub Y N 337 
TYR   CD2 HD2  sing N N 338 
TYR   CE1 CZ   doub Y N 339 
TYR   CE1 HE1  sing N N 340 
TYR   CE2 CZ   sing Y N 341 
TYR   CE2 HE2  sing N N 342 
TYR   CZ  OH   sing N N 343 
TYR   OH  HH   sing N N 344 
TYR   OXT HXT  sing N N 345 
VAL   N   CA   sing N N 346 
VAL   N   H    sing N N 347 
VAL   N   H2   sing N N 348 
VAL   CA  C    sing N N 349 
VAL   CA  CB   sing N N 350 
VAL   CA  HA   sing N N 351 
VAL   C   O    doub N N 352 
VAL   C   OXT  sing N N 353 
VAL   CB  CG1  sing N N 354 
VAL   CB  CG2  sing N N 355 
VAL   CB  HB   sing N N 356 
VAL   CG1 HG11 sing N N 357 
VAL   CG1 HG12 sing N N 358 
VAL   CG1 HG13 sing N N 359 
VAL   CG2 HG21 sing N N 360 
VAL   CG2 HG22 sing N N 361 
VAL   CG2 HG23 sing N N 362 
VAL   OXT HXT  sing N N 363 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6D9N 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9K1J 
_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]   0.013720 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004410 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018438 
_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]   0.011956 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 1   ? 4.181   -26.423 49.538 1.00 40.67  ? 1   MET   B N   1 
ATOM   2    C CA  . MET   A 1 1   ? 3.682   -25.112 49.957 1.00 41.96  ? 1   MET   B CA  1 
ATOM   3    C C   . MET   A 1 1   ? 2.404   -24.755 49.209 1.00 44.50  ? 1   MET   B C   1 
ATOM   4    O O   . MET   A 1 1   ? 2.248   -25.101 48.032 1.00 41.56  ? 1   MET   B O   1 
ATOM   5    C CB  . MET   A 1 1   ? 4.721   -24.017 49.699 1.00 39.66  ? 1   MET   B CB  1 
ATOM   6    C CG  . MET   A 1 1   ? 6.113   -24.377 50.104 1.00 44.56  ? 1   MET   B CG  1 
ATOM   7    S SD  . MET   A 1 1   ? 6.357   -24.420 51.886 1.00 67.77  ? 1   MET   B SD  1 
ATOM   8    C CE  . MET   A 1 1   ? 8.096   -24.834 51.989 1.00 50.72  ? 1   MET   B CE  1 
ATOM   9    N N   . SER   A 1 2   ? 1.504   -24.028 49.863 1.00 42.56  ? 2   SER   B N   1 
ATOM   10   C CA  . SER   A 1 2   ? 0.307   -23.556 49.179 1.00 41.64  ? 2   SER   B CA  1 
ATOM   11   C C   . SER   A 1 2   ? 0.594   -22.305 48.355 1.00 31.58  ? 2   SER   B C   1 
ATOM   12   O O   . SER   A 1 2   ? 1.413   -21.455 48.730 1.00 28.89  ? 2   SER   B O   1 
ATOM   13   C CB  . SER   A 1 2   ? -0.818  -23.273 50.174 1.00 41.50  ? 2   SER   B CB  1 
ATOM   14   O OG  . SER   A 1 2   ? -1.227  -24.463 50.819 1.00 49.62  ? 2   SER   B OG  1 
ATOM   15   N N   . THR   A 1 3   ? -0.101  -22.198 47.228 1.00 27.29  ? 3   THR   B N   1 
ATOM   16   C CA  . THR   A 1 3   ? 0.008   -21.016 46.383 1.00 31.37  ? 3   THR   B CA  1 
ATOM   17   C C   . THR   A 1 3   ? -0.465  -19.751 47.102 1.00 28.13  ? 3   THR   B C   1 
ATOM   18   O O   . THR   A 1 3   ? -1.577  -19.697 47.632 1.00 22.36  ? 3   THR   B O   1 
ATOM   19   C CB  . THR   A 1 3   ? -0.787  -21.262 45.101 1.00 28.33  ? 3   THR   B CB  1 
ATOM   20   O OG1 . THR   A 1 3   ? -0.079  -22.231 44.304 1.00 26.28  ? 3   THR   B OG1 1 
ATOM   21   C CG2 . THR   A 1 3   ? -0.990  -19.999 44.323 1.00 19.47  ? 3   THR   B CG2 1 
ATOM   22   N N   . LEU   A 1 4   ? 0.380   -18.716 47.082 1.00 18.47  ? 4   LEU   B N   1 
ATOM   23   C CA  . LEU   A 1 4   ? 0.066   -17.447 47.726 1.00 19.17  ? 4   LEU   B CA  1 
ATOM   24   C C   . LEU   A 1 4   ? -0.867  -16.573 46.888 1.00 25.93  ? 4   LEU   B C   1 
ATOM   25   O O   . LEU   A 1 4   ? -1.677  -15.822 47.447 1.00 22.42  ? 4   LEU   B O   1 
ATOM   26   C CB  . LEU   A 1 4   ? 1.362   -16.689 48.014 1.00 20.08  ? 4   LEU   B CB  1 
ATOM   27   C CG  . LEU   A 1 4   ? 2.279   -17.452 48.975 1.00 26.80  ? 4   LEU   B CG  1 
ATOM   28   C CD1 . LEU   A 1 4   ? 3.569   -16.699 49.153 1.00 30.73  ? 4   LEU   B CD1 1 
ATOM   29   C CD2 . LEU   A 1 4   ? 1.595   -17.660 50.315 1.00 27.99  ? 4   LEU   B CD2 1 
ATOM   30   N N   . TYR   A 1 5   ? -0.762  -16.644 45.559 1.00 18.41  ? 5   TYR   B N   1 
ATOM   31   C CA  . TYR   A 1 5   ? -1.604  -15.844 44.683 1.00 12.52  ? 5   TYR   B CA  1 
ATOM   32   C C   . TYR   A 1 5   ? -1.587  -16.450 43.284 1.00 21.74  ? 5   TYR   B C   1 
ATOM   33   O O   . TYR   A 1 5   ? -0.540  -16.908 42.802 1.00 14.67  ? 5   TYR   B O   1 
ATOM   34   C CB  . TYR   A 1 5   ? -1.132  -14.397 44.632 1.00 16.64  ? 5   TYR   B CB  1 
ATOM   35   C CG  . TYR   A 1 5   ? -1.766  -13.578 43.533 1.00 17.72  ? 5   TYR   B CG  1 
ATOM   36   C CD1 . TYR   A 1 5   ? -3.100  -13.183 43.602 1.00 18.04  ? 5   TYR   B CD1 1 
ATOM   37   C CD2 . TYR   A 1 5   ? -1.032  -13.220 42.406 1.00 14.19  ? 5   TYR   B CD2 1 
ATOM   38   C CE1 . TYR   A 1 5   ? -3.684  -12.428 42.566 1.00 18.04  ? 5   TYR   B CE1 1 
ATOM   39   C CE2 . TYR   A 1 5   ? -1.605  -12.478 41.380 1.00 15.16  ? 5   TYR   B CE2 1 
ATOM   40   C CZ  . TYR   A 1 5   ? -2.927  -12.073 41.474 1.00 14.12  ? 5   TYR   B CZ  1 
ATOM   41   O OH  . TYR   A 1 5   ? -3.463  -11.316 40.468 1.00 16.74  ? 5   TYR   B OH  1 
ATOM   42   N N   . SER   A 1 6   ? -2.751  -16.448 42.644 1.00 14.79  ? 6   SER   B N   1 
ATOM   43   C CA  . SER   A 1 6   ? -2.935  -17.061 41.341 1.00 14.24  ? 6   SER   B CA  1 
ATOM   44   C C   . SER   A 1 6   ? -3.752  -16.105 40.492 1.00 16.21  ? 6   SER   B C   1 
ATOM   45   O O   . SER   A 1 6   ? -4.630  -15.422 41.010 1.00 19.89  ? 6   SER   B O   1 
ATOM   46   C CB  . SER   A 1 6   ? -3.646  -18.401 41.468 1.00 19.80  ? 6   SER   B CB  1 
ATOM   47   O OG  . SER   A 1 6   ? -3.756  -19.019 40.207 1.00 33.60  ? 6   SER   B OG  1 
ATOM   48   N N   . THR   A 1 7   ? -3.457  -16.037 39.197 1.00 17.29  ? 7   THR   B N   1 
ATOM   49   C CA  . THR   A 1 7   ? -4.211  -15.170 38.307 1.00 15.11  ? 7   THR   B CA  1 
ATOM   50   C C   . THR   A 1 7   ? -4.351  -15.841 36.947 1.00 18.51  ? 7   THR   B C   1 
ATOM   51   O O   . THR   A 1 7   ? -3.568  -16.718 36.569 1.00 14.70  ? 7   THR   B O   1 
ATOM   52   C CB  . THR   A 1 7   ? -3.544  -13.794 38.174 1.00 23.59  ? 7   THR   B CB  1 
ATOM   53   O OG1 . THR   A 1 7   ? -4.429  -12.898 37.475 1.00 21.21  ? 7   THR   B OG1 1 
ATOM   54   C CG2 . THR   A 1 7   ? -2.202  -13.925 37.431 1.00 13.44  ? 7   THR   B CG2 1 
ATOM   55   N N   . GLN   A 1 8   ? -5.377  -15.437 36.213 1.00 16.65  ? 8   GLN   B N   1 
ATOM   56   C CA  . GLN   A 1 8   ? -5.653  -16.010 34.906 1.00 17.85  ? 8   GLN   B CA  1 
ATOM   57   C C   . GLN   A 1 8   ? -5.673  -14.918 33.853 1.00 20.31  ? 8   GLN   B C   1 
ATOM   58   O O   . GLN   A 1 8   ? -6.207  -13.833 34.092 1.00 25.16  ? 8   GLN   B O   1 
ATOM   59   C CB  . GLN   A 1 8   ? -6.995  -16.753 34.903 1.00 20.50  ? 8   GLN   B CB  1 
ATOM   60   C CG  . GLN   A 1 8   ? -6.996  -18.013 35.725 1.00 23.90  ? 8   GLN   B CG  1 
ATOM   61   C CD  . GLN   A 1 8   ? -8.132  -18.943 35.327 1.00 31.13  ? 8   GLN   B CD  1 
ATOM   62   O OE1 . GLN   A 1 8   ? -9.215  -18.487 34.959 1.00 35.32  ? 8   GLN   B OE1 1 
ATOM   63   N NE2 . GLN   A 1 8   ? -7.887  -20.245 35.388 1.00 28.39  ? 8   GLN   B NE2 1 
ATOM   64   N N   . VAL   A 1 9   ? -5.116  -15.208 32.676 1.00 17.01  ? 9   VAL   B N   1 
ATOM   65   C CA  . VAL   A 1 9   ? -5.113  -14.260 31.570 1.00 13.07  ? 9   VAL   B CA  1 
ATOM   66   C C   . VAL   A 1 9   ? -5.446  -15.018 30.295 1.00 22.75  ? 9   VAL   B C   1 
ATOM   67   O O   . VAL   A 1 9   ? -4.825  -16.049 29.994 1.00 16.13  ? 9   VAL   B O   1 
ATOM   68   C CB  . VAL   A 1 9   ? -3.769  -13.523 31.404 1.00 13.24  ? 9   VAL   B CB  1 
ATOM   69   C CG1 . VAL   A 1 9   ? -3.851  -12.574 30.201 1.00 18.01  ? 9   VAL   B CG1 1 
ATOM   70   C CG2 . VAL   A 1 9   ? -3.384  -12.753 32.678 1.00 13.54  ? 9   VAL   B CG2 1 
ATOM   71   N N   . LYS   A 1 10  ? -6.415  -14.496 29.539 1.00 18.48  ? 10  LYS   B N   1 
ATOM   72   C CA  . LYS   A 1 10  ? -6.873  -15.104 28.296 1.00 21.40  ? 10  LYS   B CA  1 
ATOM   73   C C   . LYS   A 1 10  ? -6.256  -14.332 27.139 1.00 17.08  ? 10  LYS   B C   1 
ATOM   74   O O   . LYS   A 1 10  ? -6.403  -13.108 27.066 1.00 23.83  ? 10  LYS   B O   1 
ATOM   75   C CB  . LYS   A 1 10  ? -8.403  -15.072 28.222 1.00 24.48  ? 10  LYS   B CB  1 
ATOM   76   C CG  . LYS   A 1 10  ? -8.981  -15.739 26.977 1.00 20.01  ? 10  LYS   B CG  1 
ATOM   77   C CD  . LYS   A 1 10  ? -10.502 -15.649 26.883 1.00 30.93  ? 10  LYS   B CD  1 
ATOM   78   C CE  . LYS   A 1 10  ? -11.218 -16.166 28.120 1.00 34.55  ? 10  LYS   B CE  1 
ATOM   79   N NZ  . LYS   A 1 10  ? -12.715 -16.125 27.940 1.00 43.10  ? 10  LYS   B NZ  1 
ATOM   80   N N   . ALA   A 1 11  ? -5.548  -15.035 26.255 1.00 21.42  ? 11  ALA   B N   1 
ATOM   81   C CA  . ALA   A 1 11  ? -4.966  -14.442 25.057 1.00 17.12  ? 11  ALA   B CA  1 
ATOM   82   C C   . ALA   A 1 11  ? -5.594  -15.078 23.820 1.00 27.24  ? 11  ALA   B C   1 
ATOM   83   O O   . ALA   A 1 11  ? -5.604  -16.310 23.686 1.00 27.94  ? 11  ALA   B O   1 
ATOM   84   C CB  . ALA   A 1 11  ? -3.450  -14.619 25.031 1.00 18.03  ? 11  ALA   B CB  1 
ATOM   85   N N   . VAL   A 1 12  ? -6.090  -14.236 22.911 1.00 27.29  ? 12  VAL   B N   1 
ATOM   86   C CA  . VAL   A 1 12  ? -6.754  -14.683 21.689 1.00 32.98  ? 12  VAL   B CA  1 
ATOM   87   C C   . VAL   A 1 12  ? -6.010  -14.138 20.472 1.00 33.47  ? 12  VAL   B C   1 
ATOM   88   O O   . VAL   A 1 12  ? -5.784  -12.923 20.370 1.00 31.79  ? 12  VAL   B O   1 
ATOM   89   C CB  . VAL   A 1 12  ? -8.227  -14.234 21.656 1.00 27.87  ? 12  VAL   B CB  1 
ATOM   90   C CG1 . VAL   A 1 12  ? -8.873  -14.667 20.348 1.00 25.57  ? 12  VAL   B CG1 1 
ATOM   91   C CG2 . VAL   A 1 12  ? -8.967  -14.804 22.851 1.00 27.63  ? 12  VAL   B CG2 1 
ATOM   92   N N   . GLY   A 1 13  ? -5.660  -15.028 19.539 1.00 26.22  ? 13  GLY   B N   1 
ATOM   93   C CA  . GLY   A 1 13  ? -5.153  -14.598 18.246 1.00 26.00  ? 13  GLY   B CA  1 
ATOM   94   C C   . GLY   A 1 13  ? -3.666  -14.325 18.182 1.00 34.20  ? 13  GLY   B C   1 
ATOM   95   O O   . GLY   A 1 13  ? -3.218  -13.606 17.273 1.00 26.55  ? 13  GLY   B O   1 
ATOM   96   N N   . GLY   A 1 14  ? -2.887  -14.856 19.128 1.00 20.96  ? 14  GLY   B N   1 
ATOM   97   C CA  . GLY   A 1 14  ? -1.434  -14.764 19.051 1.00 27.49  ? 14  GLY   B CA  1 
ATOM   98   C C   . GLY   A 1 14  ? -0.896  -13.343 19.113 1.00 26.68  ? 14  GLY   B C   1 
ATOM   99   O O   . GLY   A 1 14  ? -1.442  -12.457 19.793 1.00 26.43  ? 14  GLY   B O   1 
ATOM   100  N N   . ARG   A 1 15  ? 0.210   -13.120 18.400 1.00 24.43  ? 15  ARG   B N   1 
ATOM   101  C CA  . ARG   A 1 15  ? 0.934   -11.859 18.514 1.00 21.31  ? 15  ARG   B CA  1 
ATOM   102  C C   . ARG   A 1 15  ? 0.226   -10.690 17.837 1.00 32.06  ? 15  ARG   B C   1 
ATOM   103  O O   . ARG   A 1 15  ? 0.648   -9.543  18.038 1.00 24.96  ? 15  ARG   B O   1 
ATOM   104  C CB  . ARG   A 1 15  ? 2.343   -12.025 17.941 1.00 30.75  ? 15  ARG   B CB  1 
ATOM   105  C CG  . ARG   A 1 15  ? 3.282   -12.706 18.929 1.00 26.03  ? 15  ARG   B CG  1 
ATOM   106  C CD  . ARG   A 1 15  ? 4.578   -13.085 18.283 1.00 26.73  ? 15  ARG   B CD  1 
ATOM   107  N NE  . ARG   A 1 15  ? 5.398   -13.870 19.202 1.00 27.20  ? 15  ARG   B NE  1 
ATOM   108  C CZ  . ARG   A 1 15  ? 6.384   -13.380 19.932 1.00 24.18  ? 15  ARG   B CZ  1 
ATOM   109  N NH1 . ARG   A 1 15  ? 6.705   -12.098 19.833 1.00 24.96  ? 15  ARG   B NH1 1 
ATOM   110  N NH2 . ARG   A 1 15  ? 7.071   -14.186 20.724 1.00 21.04  ? 15  ARG   B NH2 1 
ATOM   111  N N   . SER   A 1 16  ? -0.837  -10.937 17.064 1.00 23.85  ? 16  SER   B N   1 
ATOM   112  C CA  . SER   A 1 16  ? -1.657  -9.862  16.518 1.00 29.27  ? 16  SER   B CA  1 
ATOM   113  C C   . SER   A 1 16  ? -3.011  -9.737  17.208 1.00 30.20  ? 16  SER   B C   1 
ATOM   114  O O   . SER   A 1 16  ? -3.870  -9.000  16.719 1.00 30.60  ? 16  SER   B O   1 
ATOM   115  C CB  . SER   A 1 16  ? -1.871  -10.050 15.011 1.00 29.79  ? 16  SER   B CB  1 
ATOM   116  O OG  . SER   A 1 16  ? -0.745  -9.604  14.271 1.00 45.78  ? 16  SER   B OG  1 
ATOM   117  N N   . GLY   A 1 17  ? -3.217  -10.414 18.337 1.00 31.91  ? 17  GLY   B N   1 
ATOM   118  C CA  . GLY   A 1 17  ? -4.520  -10.458 18.978 1.00 26.30  ? 17  GLY   B CA  1 
ATOM   119  C C   . GLY   A 1 17  ? -4.672  -9.619  20.229 1.00 28.16  ? 17  GLY   B C   1 
ATOM   120  O O   . GLY   A 1 17  ? -4.360  -8.428  20.217 1.00 31.13  ? 17  GLY   B O   1 
ATOM   121  N N   . THR   A 1 18  ? -5.183  -10.213 21.311 1.00 26.20  ? 18  THR   B N   1 
ATOM   122  C CA  . THR   A 1 18  ? -5.520  -9.472  22.523 1.00 29.11  ? 18  THR   B CA  1 
ATOM   123  C C   . THR   A 1 18  ? -5.190  -10.320 23.751 1.00 25.34  ? 18  THR   B C   1 
ATOM   124  O O   . THR   A 1 18  ? -5.092  -11.551 23.671 1.00 26.38  ? 18  THR   B O   1 
ATOM   125  C CB  . THR   A 1 18  ? -7.005  -9.096  22.573 1.00 29.69  ? 18  THR   B CB  1 
ATOM   126  O OG1 . THR   A 1 18  ? -7.791  -10.297 22.568 1.00 33.56  ? 18  THR   B OG1 1 
ATOM   127  C CG2 . THR   A 1 18  ? -7.403  -8.248  21.370 1.00 32.20  ? 18  THR   B CG2 1 
ATOM   128  N N   . ILE   A 1 19  ? -5.013  -9.645  24.891 1.00 20.11  ? 19  ILE   B N   1 
ATOM   129  C CA  . ILE   A 1 19  ? -4.908  -10.297 26.194 1.00 24.52  ? 19  ILE   B CA  1 
ATOM   130  C C   . ILE   A 1 19  ? -5.871  -9.604  27.138 1.00 25.07  ? 19  ILE   B C   1 
ATOM   131  O O   . ILE   A 1 19  ? -6.085  -8.388  27.052 1.00 22.58  ? 19  ILE   B O   1 
ATOM   132  C CB  . ILE   A 1 19  ? -3.493  -10.243 26.823 1.00 20.73  ? 19  ILE   B CB  1 
ATOM   133  C CG1 . ILE   A 1 19  ? -3.111  -8.770  27.039 1.00 24.23  ? 19  ILE   B CG1 1 
ATOM   134  C CG2 . ILE   A 1 19  ? -2.500  -10.957 25.971 1.00 21.77  ? 19  ILE   B CG2 1 
ATOM   135  C CD1 . ILE   A 1 19  ? -1.929  -8.544  27.894 1.00 29.96  ? 19  ILE   B CD1 1 
ATOM   136  N N   . ARG   A 1 20  ? -6.391  -10.371 28.094 1.00 27.55  ? 20  ARG   B N   1 
ATOM   137  C CA  . ARG   A 1 20  ? -7.253  -9.790  29.112 1.00 21.32  ? 20  ARG   B CA  1 
ATOM   138  C C   . ARG   A 1 20  ? -7.269  -10.700 30.327 1.00 18.10  ? 20  ARG   B C   1 
ATOM   139  O O   . ARG   A 1 20  ? -7.521  -11.899 30.197 1.00 22.64  ? 20  ARG   B O   1 
ATOM   140  C CB  . ARG   A 1 20  ? -8.675  -9.569  28.561 1.00 28.88  ? 20  ARG   B CB  1 
ATOM   141  C CG  . ARG   A 1 20  ? -9.634  -9.032  29.581 1.00 28.84  ? 20  ARG   B CG  1 
ATOM   142  C CD  . ARG   A 1 20  ? -11.078 -9.173  29.117 1.00 34.42  ? 20  ARG   B CD  1 
ATOM   143  N NE  . ARG   A 1 20  ? -11.949 -8.490  30.062 1.00 32.52  ? 20  ARG   B NE  1 
ATOM   144  C CZ  . ARG   A 1 20  ? -12.437 -9.038  31.165 1.00 37.37  ? 20  ARG   B CZ  1 
ATOM   145  N NH1 . ARG   A 1 20  ? -12.188 -10.316 31.459 1.00 32.22  ? 20  ARG   B NH1 1 
ATOM   146  N NH2 . ARG   A 1 20  ? -13.193 -8.306  31.971 1.00 32.97  ? 20  ARG   B NH2 1 
ATOM   147  N N   . SER   A 1 21  ? -6.980  -10.142 31.496 1.00 17.16  ? 21  SER   B N   1 
ATOM   148  C CA  . SER   A 1 21  ? -7.072  -10.932 32.709 1.00 24.40  ? 21  SER   B CA  1 
ATOM   149  C C   . SER   A 1 21  ? -8.538  -11.176 33.057 1.00 32.02  ? 21  SER   B C   1 
ATOM   150  O O   . SER   A 1 21  ? -9.433  -10.405 32.686 1.00 30.37  ? 21  SER   B O   1 
ATOM   151  C CB  . SER   A 1 21  ? -6.349  -10.235 33.863 1.00 22.84  ? 21  SER   B CB  1 
ATOM   152  O OG  . SER   A 1 21  ? -6.719  -8.872  33.950 1.00 26.03  ? 21  SER   B OG  1 
ATOM   153  N N   . GLU   A 1 22  ? -8.781  -12.276 33.764 1.00 30.14  ? 22  GLU   B N   1 
ATOM   154  C CA  . GLU   A 1 22  ? -10.150 -12.650 34.090 1.00 35.14  ? 22  GLU   B CA  1 
ATOM   155  C C   . GLU   A 1 22  ? -10.772 -11.695 35.102 1.00 35.40  ? 22  GLU   B C   1 
ATOM   156  O O   . GLU   A 1 22  ? -12.000 -11.665 35.227 1.00 41.02  ? 22  GLU   B O   1 
ATOM   157  C CB  . GLU   A 1 22  ? -10.186 -14.090 34.607 1.00 34.47  ? 22  GLU   B CB  1 
ATOM   158  C CG  . GLU   A 1 22  ? -10.102 -15.168 33.516 1.00 34.95  ? 22  GLU   B CG  1 
ATOM   159  C CD  . GLU   A 1 22  ? -11.265 -15.134 32.511 1.00 42.67  ? 22  GLU   B CD  1 
ATOM   160  O OE1 . GLU   A 1 22  ? -12.444 -15.148 32.925 1.00 51.29  ? 22  GLU   B OE1 1 
ATOM   161  O OE2 . GLU   A 1 22  ? -10.995 -15.098 31.296 1.00 37.69  ? 22  GLU   B OE2 1 
ATOM   162  N N   . ASP   A 1 23  ? -9.955  -10.902 35.808 1.00 37.39  ? 23  ASP   B N   1 
ATOM   163  C CA  . ASP   A 1 23  ? -10.435 -9.868  36.717 1.00 31.32  ? 23  ASP   B CA  1 
ATOM   164  C C   . ASP   A 1 23  ? -10.598 -8.509  36.042 1.00 33.82  ? 23  ASP   B C   1 
ATOM   165  O O   . ASP   A 1 23  ? -10.959 -7.541  36.715 1.00 37.57  ? 23  ASP   B O   1 
ATOM   166  C CB  . ASP   A 1 23  ? -9.497  -9.758  37.938 1.00 38.79  ? 23  ASP   B CB  1 
ATOM   167  C CG  . ASP   A 1 23  ? -8.079  -9.235  37.597 1.00 36.40  ? 23  ASP   B CG  1 
ATOM   168  O OD1 . ASP   A 1 23  ? -7.791  -8.837  36.442 1.00 32.68  ? 23  ASP   B OD1 1 
ATOM   169  O OD2 . ASP   A 1 23  ? -7.222  -9.259  38.517 1.00 34.97  ? 23  ASP   B OD2 1 
ATOM   170  N N   . GLY   A 1 24  ? -10.340 -8.417  34.737 1.00 26.51  ? 24  GLY   B N   1 
ATOM   171  C CA  . GLY   A 1 24  ? -10.468 -7.183  33.991 1.00 28.54  ? 24  GLY   B CA  1 
ATOM   172  C C   . GLY   A 1 24  ? -9.348  -6.176  34.161 1.00 34.25  ? 24  GLY   B C   1 
ATOM   173  O O   . GLY   A 1 24  ? -9.262  -5.237  33.354 1.00 25.68  ? 24  GLY   B O   1 
ATOM   174  N N   . ILE   A 1 25  ? -8.464  -6.356  35.153 1.00 24.81  ? 25  ILE   B N   1 
ATOM   175  C CA  . ILE   A 1 25  ? -7.493  -5.316  35.482 1.00 29.19  ? 25  ILE   B CA  1 
ATOM   176  C C   . ILE   A 1 25  ? -6.512  -5.095  34.334 1.00 27.50  ? 25  ILE   B C   1 
ATOM   177  O O   . ILE   A 1 25  ? -6.240  -3.952  33.959 1.00 30.89  ? 25  ILE   B O   1 
ATOM   178  C CB  . ILE   A 1 25  ? -6.782  -5.629  36.817 1.00 31.08  ? 25  ILE   B CB  1 
ATOM   179  C CG1 . ILE   A 1 25  ? -7.757  -5.478  37.986 1.00 38.34  ? 25  ILE   B CG1 1 
ATOM   180  C CG2 . ILE   A 1 25  ? -5.595  -4.723  37.035 1.00 29.99  ? 25  ILE   B CG2 1 
ATOM   181  C CD1 . ILE   A 1 25  ? -7.436  -6.331  39.198 1.00 39.17  ? 25  ILE   B CD1 1 
ATOM   182  N N   . LEU   A 1 26  ? -5.977  -6.162  33.736 1.00 31.63  ? 26  LEU   B N   1 
ATOM   183  C CA  . LEU   A 1 26  ? -5.063  -6.022  32.600 1.00 28.53  ? 26  LEU   B CA  1 
ATOM   184  C C   . LEU   A 1 26  ? -5.789  -6.418  31.322 1.00 27.22  ? 26  LEU   B C   1 
ATOM   185  O O   . LEU   A 1 26  ? -6.264  -7.549  31.202 1.00 29.63  ? 26  LEU   B O   1 
ATOM   186  C CB  . LEU   A 1 26  ? -3.795  -6.865  32.790 1.00 22.53  ? 26  LEU   B CB  1 
ATOM   187  C CG  . LEU   A 1 26  ? -2.809  -6.867  31.614 1.00 21.22  ? 26  LEU   B CG  1 
ATOM   188  C CD1 . LEU   A 1 26  ? -2.081  -5.527  31.540 1.00 16.47  ? 26  LEU   B CD1 1 
ATOM   189  C CD2 . LEU   A 1 26  ? -1.795  -8.026  31.782 1.00 16.60  ? 26  LEU   B CD2 1 
ATOM   190  N N   . GLU   A 1 27  ? -5.863  -5.498  30.365 1.00 28.56  ? 27  GLU   B N   1 
ATOM   191  C CA  . GLU   A 1 27  ? -6.613  -5.714  29.130 1.00 31.28  ? 27  GLU   B CA  1 
ATOM   192  C C   . GLU   A 1 27  ? -5.933  -4.908  28.035 1.00 30.38  ? 27  GLU   B C   1 
ATOM   193  O O   . GLU   A 1 27  ? -5.925  -3.675  28.093 1.00 34.06  ? 27  GLU   B O   1 
ATOM   194  C CB  . GLU   A 1 27  ? -8.080  -5.287  29.311 1.00 35.03  ? 27  GLU   B CB  1 
ATOM   195  C CG  . GLU   A 1 27  ? -8.872  -5.084  28.012 1.00 45.62  ? 27  GLU   B CG  1 
ATOM   196  C CD  . GLU   A 1 27  ? -10.395 -4.987  28.233 1.00 45.80  ? 27  GLU   B CD  1 
ATOM   197  O OE1 . GLU   A 1 27  ? -11.103 -4.459  27.344 1.00 55.56  ? 27  GLU   B OE1 1 
ATOM   198  O OE2 . GLU   A 1 27  ? -10.885 -5.455  29.284 1.00 51.04  ? 27  GLU   B OE2 1 
ATOM   199  N N   . LEU   A 1 28  ? -5.339  -5.592  27.062 1.00 27.44  ? 28  LEU   B N   1 
ATOM   200  C CA  . LEU   A 1 28  ? -4.460  -4.901  26.134 1.00 29.40  ? 28  LEU   B CA  1 
ATOM   201  C C   . LEU   A 1 28  ? -4.549  -5.562  24.778 1.00 33.00  ? 28  LEU   B C   1 
ATOM   202  O O   . LEU   A 1 28  ? -4.799  -6.759  24.673 1.00 29.69  ? 28  LEU   B O   1 
ATOM   203  C CB  . LEU   A 1 28  ? -3.002  -4.920  26.611 1.00 39.39  ? 28  LEU   B CB  1 
ATOM   204  C CG  . LEU   A 1 28  ? -2.538  -4.207  27.894 1.00 40.57  ? 28  LEU   B CG  1 
ATOM   205  C CD1 . LEU   A 1 28  ? -1.060  -4.545  28.109 1.00 43.13  ? 28  LEU   B CD1 1 
ATOM   206  C CD2 . LEU   A 1 28  ? -2.755  -2.701  27.859 1.00 48.35  ? 28  LEU   B CD2 1 
ATOM   207  N N   . LYS   A 1 29  ? -4.262  -4.796  23.748 1.00 24.76  ? 29  LYS   B N   1 
ATOM   208  C CA  . LYS   A 1 29  ? -4.076  -5.384  22.436 1.00 26.43  ? 29  LYS   B CA  1 
ATOM   209  C C   . LYS   A 1 29  ? -2.586  -5.464  22.113 1.00 31.83  ? 29  LYS   B C   1 
ATOM   210  O O   . LYS   A 1 29  ? -1.761  -4.751  22.702 1.00 29.86  ? 29  LYS   B O   1 
ATOM   211  C CB  . LYS   A 1 29  ? -4.852  -4.565  21.410 1.00 35.48  ? 29  LYS   B CB  1 
ATOM   212  C CG  . LYS   A 1 29  ? -4.802  -4.996  19.956 1.00 46.05  ? 29  LYS   B CG  1 
ATOM   213  C CD  . LYS   A 1 29  ? -3.707  -4.215  19.298 1.00 51.90  ? 29  LYS   B CD  1 
ATOM   214  C CE  . LYS   A 1 29  ? -4.149  -2.759  19.259 1.00 60.37  ? 29  LYS   B CE  1 
ATOM   215  N NZ  . LYS   A 1 29  ? -3.145  -1.857  18.630 1.00 58.44  ? 29  LYS   B NZ  1 
ATOM   216  N N   . LEU   A 1 30  ? -2.243  -6.397  21.221 1.00 22.47  ? 30  LEU   B N   1 
ATOM   217  C CA  . LEU   A 1 30  ? -0.863  -6.709  20.877 1.00 29.46  ? 30  LEU   B CA  1 
ATOM   218  C C   . LEU   A 1 30  ? -0.625  -6.487  19.393 1.00 27.71  ? 30  LEU   B C   1 
ATOM   219  O O   . LEU   A 1 30  ? -1.536  -6.619  18.576 1.00 28.92  ? 30  LEU   B O   1 
ATOM   220  C CB  . LEU   A 1 30  ? -0.521  -8.168  21.208 1.00 23.47  ? 30  LEU   B CB  1 
ATOM   221  C CG  . LEU   A 1 30  ? -0.785  -8.635  22.645 1.00 26.68  ? 30  LEU   B CG  1 
ATOM   222  C CD1 . LEU   A 1 30  ? -0.359  -10.081 22.812 1.00 26.84  ? 30  LEU   B CD1 1 
ATOM   223  C CD2 . LEU   A 1 30  ? -0.104  -7.758  23.642 1.00 17.27  ? 30  LEU   B CD2 1 
ATOM   224  N N   . ALA   A 1 31  ? 0.616   -6.180  19.049 1.00 25.52  ? 31  ALA   B N   1 
ATOM   225  C CA  . ALA   A 1 31  ? 1.003   -6.019  17.662 1.00 27.86  ? 31  ALA   B CA  1 
ATOM   226  C C   . ALA   A 1 31  ? 2.428   -6.521  17.503 1.00 30.64  ? 31  ALA   B C   1 
ATOM   227  O O   . ALA   A 1 31  ? 3.260   -6.332  18.398 1.00 34.58  ? 31  ALA   B O   1 
ATOM   228  C CB  . ALA   A 1 31  ? 0.894   -4.556  17.206 1.00 29.33  ? 31  ALA   B CB  1 
ATOM   229  N N   . LEU   A 1 32  ? 2.690   -7.190  16.386 1.00 27.45  ? 32  LEU   B N   1 
ATOM   230  C CA  . LEU   A 1 32  ? 4.058   -7.436  15.979 1.00 32.86  ? 32  LEU   B CA  1 
ATOM   231  C C   . LEU   A 1 32  ? 4.780   -6.092  15.858 1.00 37.26  ? 32  LEU   B C   1 
ATOM   232  O O   . LEU   A 1 32  ? 4.234   -5.159  15.252 1.00 35.85  ? 32  LEU   B O   1 
ATOM   233  C CB  . LEU   A 1 32  ? 4.091   -8.167  14.633 1.00 32.27  ? 32  LEU   B CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? 3.775   -9.657  14.490 1.00 40.61  ? 32  LEU   B CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? 3.907   -10.058 13.017 1.00 39.67  ? 32  LEU   B CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? 4.690   -10.522 15.357 1.00 31.66  ? 32  LEU   B CD2 1 
ATOM   237  N N   . PRO   A 1 33  ? 5.977   -5.952  16.421 1.00 32.09  ? 33  PRO   B N   1 
ATOM   238  C CA  . PRO   A 1 33  ? 6.758   -4.732  16.180 1.00 35.80  ? 33  PRO   B CA  1 
ATOM   239  C C   . PRO   A 1 33  ? 7.208   -4.686  14.721 1.00 38.24  ? 33  PRO   B C   1 
ATOM   240  O O   . PRO   A 1 33  ? 7.194   -5.700  14.023 1.00 35.16  ? 33  PRO   B O   1 
ATOM   241  C CB  . PRO   A 1 33  ? 7.946   -4.880  17.136 1.00 35.14  ? 33  PRO   B CB  1 
ATOM   242  C CG  . PRO   A 1 33  ? 8.089   -6.390  17.292 1.00 37.97  ? 33  PRO   B CG  1 
ATOM   243  C CD  . PRO   A 1 33  ? 6.705   -6.944  17.235 1.00 30.19  ? 33  PRO   B CD  1 
ATOM   244  N N   . LYS   A 1 34  ? 7.604   -3.490  14.246 1.00 40.85  ? 34  LYS   B N   1 
ATOM   245  C CA  . LYS   A 1 34  ? 7.998   -3.371  12.831 1.00 45.05  ? 34  LYS   B CA  1 
ATOM   246  C C   . LYS   A 1 34  ? 9.158   -4.302  12.484 1.00 40.68  ? 34  LYS   B C   1 
ATOM   247  O O   . LYS   A 1 34  ? 9.195   -4.869  11.384 1.00 41.03  ? 34  LYS   B O   1 
ATOM   248  C CB  . LYS   A 1 34  ? 8.347   -1.927  12.413 1.00 41.01  ? 34  LYS   B CB  1 
ATOM   249  C CG  . LYS   A 1 34  ? 7.149   -0.974  12.346 1.00 51.61  ? 34  LYS   B CG  1 
ATOM   250  C CD  . LYS   A 1 34  ? 7.533   0.448   11.875 1.00 58.63  ? 34  LYS   B CD  1 
ATOM   251  C CE  . LYS   A 1 34  ? 7.793   0.486   10.341 1.00 53.57  ? 34  LYS   B CE  1 
ATOM   252  N NZ  . LYS   A 1 34  ? 6.527   0.209   9.561  1.00 54.14  ? 34  LYS   B NZ  1 
ATOM   253  N N   . GLU   A 1 35  ? 10.088  -4.514  13.421 1.00 40.91  ? 35  GLU   B N   1 
ATOM   254  C CA  . GLU   A 1 35  ? 11.229  -5.380  13.126 1.00 43.15  ? 35  GLU   B CA  1 
ATOM   255  C C   . GLU   A 1 35  ? 10.804  -6.796  12.759 1.00 40.51  ? 35  GLU   B C   1 
ATOM   256  O O   . GLU   A 1 35  ? 11.557  -7.509  12.088 1.00 48.17  ? 35  GLU   B O   1 
ATOM   257  C CB  . GLU   A 1 35  ? 12.210  -5.442  14.307 1.00 45.32  ? 35  GLU   B CB  1 
ATOM   258  C CG  . GLU   A 1 35  ? 12.889  -4.130  14.669 1.00 45.83  ? 35  GLU   B CG  1 
ATOM   259  C CD  . GLU   A 1 35  ? 12.179  -3.380  15.770 1.00 45.74  ? 35  GLU   B CD  1 
ATOM   260  O OE1 . GLU   A 1 35  ? 10.929  -3.331  15.770 1.00 45.00  ? 35  GLU   B OE1 1 
ATOM   261  O OE2 . GLU   A 1 35  ? 12.884  -2.857  16.658 1.00 52.81  ? 35  GLU   B OE2 1 
ATOM   262  N N   . LEU   A 1 36  ? 9.610   -7.216  13.171 1.00 44.60  ? 36  LEU   B N   1 
ATOM   263  C CA  . LEU   A 1 36  ? 9.065   -8.514  12.797 1.00 47.33  ? 36  LEU   B CA  1 
ATOM   264  C C   . LEU   A 1 36  ? 7.898   -8.383  11.819 1.00 47.29  ? 36  LEU   B C   1 
ATOM   265  O O   . LEU   A 1 36  ? 7.036   -9.260  11.758 1.00 48.56  ? 36  LEU   B O   1 
ATOM   266  C CB  . LEU   A 1 36  ? 8.636   -9.296  14.042 1.00 46.39  ? 36  LEU   B CB  1 
ATOM   267  C CG  . LEU   A 1 36  ? 9.597   -9.346  15.240 1.00 45.76  ? 36  LEU   B CG  1 
ATOM   268  C CD1 . LEU   A 1 36  ? 9.023   -10.213 16.351 1.00 40.51  ? 36  LEU   B CD1 1 
ATOM   269  C CD2 . LEU   A 1 36  ? 10.992  -9.828  14.839 1.00 41.23  ? 36  LEU   B CD2 1 
ATOM   270  N N   . GLY   A 1 37  ? 7.850   -7.287  11.063 1.00 50.99  ? 37  GLY   B N   1 
ATOM   271  C CA  . GLY   A 1 37  ? 6.875   -7.143  9.999  1.00 50.11  ? 37  GLY   B CA  1 
ATOM   272  C C   . GLY   A 1 37  ? 5.517   -6.634  10.423 1.00 48.43  ? 37  GLY   B C   1 
ATOM   273  O O   . GLY   A 1 37  ? 4.525   -6.928  9.751  1.00 52.41  ? 37  GLY   B O   1 
ATOM   274  N N   . GLY   A 1 38  ? 5.438   -5.876  11.514 1.00 37.58  ? 38  GLY   B N   1 
ATOM   275  C CA  . GLY   A 1 38  ? 4.178   -5.302  11.955 1.00 40.50  ? 38  GLY   B CA  1 
ATOM   276  C C   . GLY   A 1 38  ? 4.213   -3.789  12.034 1.00 43.13  ? 38  GLY   B C   1 
ATOM   277  O O   . GLY   A 1 38  ? 5.113   -3.166  11.466 1.00 48.64  ? 38  GLY   B O   1 
ATOM   278  N N   . LYS   A 1 39  ? 3.242   -3.186  12.726 1.00 45.62  ? 39  LYS   B N   1 
ATOM   279  C CA  . LYS   A 1 39  ? 3.189   -1.735  12.894 1.00 50.75  ? 39  LYS   B CA  1 
ATOM   280  C C   . LYS   A 1 39  ? 3.825   -1.236  14.188 1.00 49.58  ? 39  LYS   B C   1 
ATOM   281  O O   . LYS   A 1 39  ? 4.308   -0.098  14.218 1.00 49.17  ? 39  LYS   B O   1 
ATOM   282  C CB  . LYS   A 1 39  ? 1.740   -1.230  12.857 1.00 61.37  ? 39  LYS   B CB  1 
ATOM   283  C CG  . LYS   A 1 39  ? 0.917   -1.573  11.602 1.00 71.33  ? 39  LYS   B CG  1 
ATOM   284  C CD  . LYS   A 1 39  ? 1.291   -0.744  10.370 1.00 75.13  ? 39  LYS   B CD  1 
ATOM   285  C CE  . LYS   A 1 39  ? 0.139   -0.723  9.354  1.00 73.89  ? 39  LYS   B CE  1 
ATOM   286  N NZ  . LYS   A 1 39  ? -0.931  0.263   9.698  1.00 71.61  ? 39  LYS   B NZ  1 
ATOM   287  N N   . GLY   A 1 40  ? 3.840   -2.034  15.259 1.00 39.72  ? 40  GLY   B N   1 
ATOM   288  C CA  . GLY   A 1 40  ? 4.334   -1.528  16.530 1.00 39.98  ? 40  GLY   B CA  1 
ATOM   289  C C   . GLY   A 1 40  ? 3.323   -0.699  17.277 1.00 37.95  ? 40  GLY   B C   1 
ATOM   290  O O   . GLY   A 1 40  ? 3.687   0.074   18.171 1.00 43.31  ? 40  GLY   B O   1 
ATOM   291  N N   . ASP   A 1 41  ? 2.052   -0.856  16.923 1.00 42.58  ? 41  ASP   B N   1 
ATOM   292  C CA  . ASP   A 1 41  ? 0.884   -0.200  17.515 1.00 53.63  ? 41  ASP   B CA  1 
ATOM   293  C C   . ASP   A 1 41  ? 0.834   -0.302  19.020 1.00 48.21  ? 41  ASP   B C   1 
ATOM   294  O O   . ASP   A 1 41  ? 0.193   0.534   19.675 1.00 42.04  ? 41  ASP   B O   1 
ATOM   295  C CB  . ASP   A 1 41  ? -0.411  -0.877  17.037 1.00 52.39  ? 41  ASP   B CB  1 
ATOM   296  C CG  . ASP   A 1 41  ? -0.637  -0.708  15.581 1.00 68.59  ? 41  ASP   B CG  1 
ATOM   297  O OD1 . ASP   A 1 41  ? -0.161  0.300   15.038 1.00 79.37  ? 41  ASP   B OD1 1 
ATOM   298  O OD2 . ASP   A 1 41  ? -1.340  -1.537  14.968 1.00 77.97  ? 41  ASP   B OD2 1 
ATOM   299  N N   . ALA   A 1 42  ? 1.460   -1.333  19.566 1.00 33.34  ? 42  ALA   B N   1 
ATOM   300  C CA  . ALA   A 1 42  ? 0.930   -1.993  20.741 1.00 34.02  ? 42  ALA   B CA  1 
ATOM   301  C C   . ALA   A 1 42  ? 2.004   -2.932  21.262 1.00 31.21  ? 42  ALA   B C   1 
ATOM   302  O O   . ALA   A 1 42  ? 3.002   -3.220  20.585 1.00 27.81  ? 42  ALA   B O   1 
ATOM   303  C CB  . ALA   A 1 42  ? -0.364  -2.760  20.404 1.00 33.35  ? 42  ALA   B CB  1 
ATOM   304  N N   . THR   A 1 43  ? 1.781   -3.412  22.476 1.00 23.44  ? 43  THR   B N   1 
ATOM   305  C CA  . THR   A 1 43  ? 2.811   -4.176  23.141 1.00 20.50  ? 43  THR   B CA  1 
ATOM   306  C C   . THR   A 1 43  ? 2.864   -5.590  22.554 1.00 23.55  ? 43  THR   B C   1 
ATOM   307  O O   . THR   A 1 43  ? 2.214   -5.905  21.552 1.00 25.00  ? 43  THR   B O   1 
ATOM   308  C CB  . THR   A 1 43  ? 2.570   -4.153  24.650 1.00 28.62  ? 43  THR   B CB  1 
ATOM   309  O OG1 . THR   A 1 43  ? 3.710   -4.704  25.310 1.00 19.45  ? 43  THR   B OG1 1 
ATOM   310  C CG2 . THR   A 1 43  ? 1.314   -4.957  25.020 1.00 25.29  ? 43  THR   B CG2 1 
ATOM   311  N N   . ASN   A 1 44  ? 3.657   -6.452  23.184 1.00 17.74  ? 44  ASN   B N   1 
ATOM   312  C CA  . ASN   A 1 44  ? 4.028   -7.734  22.611 1.00 18.61  ? 44  ASN   B CA  1 
ATOM   313  C C   . ASN   A 1 44  ? 4.593   -8.609  23.726 1.00 17.65  ? 44  ASN   B C   1 
ATOM   314  O O   . ASN   A 1 44  ? 4.909   -8.097  24.817 1.00 18.90  ? 44  ASN   B O   1 
ATOM   315  C CB  . ASN   A 1 44  ? 5.051   -7.555  21.468 1.00 16.07  ? 44  ASN   B CB  1 
ATOM   316  C CG  . ASN   A 1 44  ? 6.333   -6.850  21.929 1.00 25.04  ? 44  ASN   B CG  1 
ATOM   317  O OD1 . ASN   A 1 44  ? 7.007   -7.300  22.866 1.00 20.19  ? 44  ASN   B OD1 1 
ATOM   318  N ND2 . ASN   A 1 44  ? 6.673   -5.750  21.271 1.00 16.68  ? 44  ASN   B ND2 1 
ATOM   319  N N   . PRO   A 1 45  ? 4.714   -9.920  23.508 1.00 16.56  ? 45  PRO   B N   1 
ATOM   320  C CA  . PRO   A 1 45  ? 5.120   -10.830 24.590 1.00 18.90  ? 45  PRO   B CA  1 
ATOM   321  C C   . PRO   A 1 45  ? 6.467   -10.520 25.231 1.00 21.74  ? 45  PRO   B C   1 
ATOM   322  O O   . PRO   A 1 45  ? 6.655   -10.796 26.432 1.00 20.10  ? 45  PRO   B O   1 
ATOM   323  C CB  . PRO   A 1 45  ? 5.148   -12.187 23.872 1.00 17.90  ? 45  PRO   B CB  1 
ATOM   324  C CG  . PRO   A 1 45  ? 3.994   -12.059 22.914 1.00 18.84  ? 45  PRO   B CG  1 
ATOM   325  C CD  . PRO   A 1 45  ? 4.272   -10.686 22.325 1.00 17.02  ? 45  PRO   B CD  1 
ATOM   326  N N   . GLU   A 1 46  ? 7.433   -10.012 24.460 1.00 18.45  ? 46  GLU   B N   1 
ATOM   327  C CA  . GLU   A 1 46  ? 8.755   -9.720  25.024 1.00 15.96  ? 46  GLU   B CA  1 
ATOM   328  C C   . GLU   A 1 46  ? 8.696   -8.502  25.928 1.00 19.00  ? 46  GLU   B C   1 
ATOM   329  O O   . GLU   A 1 46  ? 9.278   -8.499  27.012 1.00 16.88  ? 46  GLU   B O   1 
ATOM   330  C CB  . GLU   A 1 46  ? 9.784   -9.518  23.909 1.00 17.70  ? 46  GLU   B CB  1 
ATOM   331  C CG  . GLU   A 1 46  ? 10.168  -10.829 23.217 1.00 18.29  ? 46  GLU   B CG  1 
ATOM   332  C CD  . GLU   A 1 46  ? 9.019   -11.392 22.396 1.00 28.62  ? 46  GLU   B CD  1 
ATOM   333  O OE1 . GLU   A 1 46  ? 8.426   -10.620 21.591 1.00 22.52  ? 46  GLU   B OE1 1 
ATOM   334  O OE2 . GLU   A 1 46  ? 8.668   -12.584 22.605 1.00 21.78  ? 46  GLU   B OE2 1 
ATOM   335  N N   . GLN   A 1 47  ? 7.948   -7.481  25.516 1.00 16.52  ? 47  GLN   B N   1 
ATOM   336  C CA  . GLN   A 1 47  ? 7.735   -6.295  26.340 1.00 13.98  ? 47  GLN   B CA  1 
ATOM   337  C C   . GLN   A 1 47  ? 6.979   -6.628  27.636 1.00 11.35  ? 47  GLN   B C   1 
ATOM   338  O O   . GLN   A 1 47  ? 7.308   -6.123  28.720 1.00 14.48  ? 47  GLN   B O   1 
ATOM   339  C CB  . GLN   A 1 47  ? 6.977   -5.287  25.469 1.00 13.85  ? 47  GLN   B CB  1 
ATOM   340  C CG  . GLN   A 1 47  ? 7.132   -3.852  25.791 1.00 22.93  ? 47  GLN   B CG  1 
ATOM   341  C CD  . GLN   A 1 47  ? 6.527   -2.998  24.693 1.00 22.93  ? 47  GLN   B CD  1 
ATOM   342  O OE1 . GLN   A 1 47  ? 5.312   -2.814  24.637 1.00 20.95  ? 47  GLN   B OE1 1 
ATOM   343  N NE2 . GLN   A 1 47  ? 7.377   -2.497  23.792 1.00 23.99  ? 47  GLN   B NE2 1 
ATOM   344  N N   . LEU   A 1 48  ? 5.994   -7.520  27.554 1.00 16.31  ? 48  LEU   B N   1 
ATOM   345  C CA  . LEU   A 1 48  ? 5.258   -7.923  28.752 1.00 16.52  ? 48  LEU   B CA  1 
ATOM   346  C C   . LEU   A 1 48  ? 6.129   -8.759  29.691 1.00 11.46  ? 48  LEU   B C   1 
ATOM   347  O O   . LEU   A 1 48  ? 6.116   -8.541  30.913 1.00 13.79  ? 48  LEU   B O   1 
ATOM   348  C CB  . LEU   A 1 48  ? 4.001   -8.702  28.358 1.00 14.93  ? 48  LEU   B CB  1 
ATOM   349  C CG  . LEU   A 1 48  ? 2.809   -7.924  27.794 1.00 23.37  ? 48  LEU   B CG  1 
ATOM   350  C CD1 . LEU   A 1 48  ? 1.859   -8.913  27.120 1.00 13.81  ? 48  LEU   B CD1 1 
ATOM   351  C CD2 . LEU   A 1 48  ? 2.090   -7.078  28.870 1.00 17.18  ? 48  LEU   B CD2 1 
ATOM   352  N N   . PHE   A 1 49  ? 6.887   -9.723  29.146 1.00 11.02  ? 49  PHE   B N   1 
ATOM   353  C CA  . PHE   A 1 49  ? 7.876   -10.449 29.957 1.00 10.31  ? 49  PHE   B CA  1 
ATOM   354  C C   . PHE   A 1 49  ? 8.900   -9.499  30.592 1.00 13.38  ? 49  PHE   B C   1 
ATOM   355  O O   . PHE   A 1 49  ? 9.215   -9.609  31.788 1.00 11.50  ? 49  PHE   B O   1 
ATOM   356  C CB  . PHE   A 1 49  ? 8.586   -11.490 29.093 1.00 11.99  ? 49  PHE   B CB  1 
ATOM   357  C CG  . PHE   A 1 49  ? 9.633   -12.328 29.851 1.00 22.59  ? 49  PHE   B CG  1 
ATOM   358  C CD1 . PHE   A 1 49  ? 9.280   -13.103 30.938 1.00 22.88  ? 49  PHE   B CD1 1 
ATOM   359  C CD2 . PHE   A 1 49  ? 10.956  -12.355 29.445 1.00 19.35  ? 49  PHE   B CD2 1 
ATOM   360  C CE1 . PHE   A 1 49  ? 10.228  -13.866 31.621 1.00 22.21  ? 49  PHE   B CE1 1 
ATOM   361  C CE2 . PHE   A 1 49  ? 11.917  -13.119 30.145 1.00 24.40  ? 49  PHE   B CE2 1 
ATOM   362  C CZ  . PHE   A 1 49  ? 11.541  -13.868 31.227 1.00 15.20  ? 49  PHE   B CZ  1 
ATOM   363  N N   . ALA   A 1 50  ? 9.453   -8.571  29.796 1.00 11.44  ? 50  ALA   B N   1 
ATOM   364  C CA  . ALA   A 1 50  ? 10.451  -7.639  30.320 1.00 13.73  ? 50  ALA   B CA  1 
ATOM   365  C C   . ALA   A 1 50  ? 9.887   -6.848  31.490 1.00 11.62  ? 50  ALA   B C   1 
ATOM   366  O O   . ALA   A 1 50  ? 10.560  -6.668  32.514 1.00 12.46  ? 50  ALA   B O   1 
ATOM   367  C CB  . ALA   A 1 50  ? 10.912  -6.678  29.216 1.00 12.21  ? 50  ALA   B CB  1 
ATOM   368  N N   . ALA   A 1 51  ? 8.640   -6.382  31.357 1.00 10.66  ? 51  ALA   B N   1 
ATOM   369  C CA  . ALA   A 1 51  ? 8.025   -5.577  32.403 1.00 12.94  ? 51  ALA   B CA  1 
ATOM   370  C C   . ALA   A 1 51  ? 7.821   -6.394  33.670 1.00 12.81  ? 51  ALA   B C   1 
ATOM   371  O O   . ALA   A 1 51  ? 8.151   -5.943  34.779 1.00 13.09  ? 51  ALA   B O   1 
ATOM   372  C CB  . ALA   A 1 51  ? 6.689   -5.021  31.896 1.00 9.21   ? 51  ALA   B CB  1 
ATOM   373  N N   . GLY   A 1 52  ? 7.278   -7.611  33.525 1.00 13.66  ? 52  GLY   B N   1 
ATOM   374  C CA  . GLY   A 1 52  ? 7.034   -8.421  34.707 1.00 12.44  ? 52  GLY   B CA  1 
ATOM   375  C C   . GLY   A 1 52  ? 8.330   -8.766  35.415 1.00 11.62  ? 52  GLY   B C   1 
ATOM   376  O O   . GLY   A 1 52  ? 8.421   -8.734  36.650 1.00 11.37  ? 52  GLY   B O   1 
ATOM   377  N N   . TYR   A 1 53  ? 9.374   -9.044  34.650 1.00 13.83  ? 53  TYR   B N   1 
ATOM   378  C CA  . TYR   A 1 53  ? 10.615  -9.437  35.306 1.00 18.87  ? 53  TYR   B CA  1 
ATOM   379  C C   . TYR   A 1 53  ? 11.359  -8.268  35.910 1.00 15.75  ? 53  TYR   B C   1 
ATOM   380  O O   . TYR   A 1 53  ? 11.854  -8.380  37.036 1.00 16.33  ? 53  TYR   B O   1 
ATOM   381  C CB  . TYR   A 1 53  ? 11.421  -10.339 34.374 1.00 13.30  ? 53  TYR   B CB  1 
ATOM   382  C CG  . TYR   A 1 53  ? 12.803  -10.796 34.803 1.00 11.49  ? 53  TYR   B CG  1 
ATOM   383  C CD1 . TYR   A 1 53  ? 13.002  -11.328 36.036 1.00 12.47  ? 53  TYR   B CD1 1 
ATOM   384  C CD2 . TYR   A 1 53  ? 13.620  -11.323 33.823 1.00 12.01  ? 53  TYR   B CD2 1 
ATOM   385  C CE1 . TYR   A 1 53  ? 14.224  -11.921 36.390 1.00 16.55  ? 53  TYR   B CE1 1 
ATOM   386  C CE2 . TYR   A 1 53  ? 14.815  -12.013 34.123 1.00 12.69  ? 53  TYR   B CE2 1 
ATOM   387  C CZ  . TYR   A 1 53  ? 15.108  -12.319 35.427 1.00 10.04  ? 53  TYR   B CZ  1 
ATOM   388  O OH  . TYR   A 1 53  ? 16.285  -12.989 35.799 1.00 13.52  ? 53  TYR   B OH  1 
ATOM   389  N N   . ALA   A 1 54  ? 11.381  -7.133  35.238 1.00 10.35  ? 54  ALA   B N   1 
ATOM   390  C CA  . ALA   A 1 54  ? 11.990  -5.959  35.853 1.00 9.46   ? 54  ALA   B CA  1 
ATOM   391  C C   . ALA   A 1 54  ? 11.282  -5.586  37.158 1.00 10.92  ? 54  ALA   B C   1 
ATOM   392  O O   . ALA   A 1 54  ? 11.934  -5.241  38.152 1.00 8.82   ? 54  ALA   B O   1 
ATOM   393  C CB  . ALA   A 1 54  ? 11.972  -4.790  34.857 1.00 9.26   ? 54  ALA   B CB  1 
ATOM   394  N N   . ALA   A 1 55  ? 9.941   -5.697  37.198 1.00 13.24  ? 55  ALA   B N   1 
ATOM   395  C CA  . ALA   A 1 55  ? 9.206   -5.269  38.392 1.00 9.42   ? 55  ALA   B CA  1 
ATOM   396  C C   . ALA   A 1 55  ? 9.354   -6.280  39.531 1.00 13.41  ? 55  ALA   B C   1 
ATOM   397  O O   . ALA   A 1 55  ? 9.550   -5.899  40.700 1.00 12.49  ? 55  ALA   B O   1 
ATOM   398  C CB  . ALA   A 1 55  ? 7.713   -5.052  38.060 1.00 9.73   ? 55  ALA   B CB  1 
ATOM   399  N N   . CYS   A 1 56  ? 9.270   -7.575  39.211 1.00 13.87  ? 56  CYS   B N   1 
ATOM   400  C CA  . CYS   A 1 56  ? 9.458   -8.602  40.236 1.00 12.08  ? 56  CYS   B CA  1 
ATOM   401  C C   . CYS   A 1 56  ? 10.873  -8.561  40.805 1.00 11.78  ? 56  CYS   B C   1 
ATOM   402  O O   . CYS   A 1 56  ? 11.079  -8.674  42.018 1.00 14.31  ? 56  CYS   B O   1 
ATOM   403  C CB  . CYS   A 1 56  ? 9.155   -9.991  39.659 1.00 14.13  ? 56  CYS   B CB  1 
ATOM   404  S SG  . CYS   A 1 56  ? 9.493   -11.305 40.859 1.00 22.59  ? 56  CYS   B SG  1 
ATOM   405  N N   . PHE   A 1 57  ? 11.864  -8.404  39.940 1.00 15.30  ? 57  PHE   B N   1 
ATOM   406  C CA  . PHE   A 1 57  ? 13.249  -8.367  40.401 1.00 16.30  ? 57  PHE   B CA  1 
ATOM   407  C C   . PHE   A 1 57  ? 13.523  -7.132  41.257 1.00 13.07  ? 57  PHE   B C   1 
ATOM   408  O O   . PHE   A 1 57  ? 14.161  -7.233  42.314 1.00 9.46   ? 57  PHE   B O   1 
ATOM   409  C CB  . PHE   A 1 57  ? 14.191  -8.424  39.205 1.00 11.44  ? 57  PHE   B CB  1 
ATOM   410  C CG  . PHE   A 1 57  ? 15.597  -8.794  39.561 1.00 16.79  ? 57  PHE   B CG  1 
ATOM   411  C CD1 . PHE   A 1 57  ? 15.987  -10.131 39.596 1.00 11.65  ? 57  PHE   B CD1 1 
ATOM   412  C CD2 . PHE   A 1 57  ? 16.530  -7.796  39.890 1.00 11.53  ? 57  PHE   B CD2 1 
ATOM   413  C CE1 . PHE   A 1 57  ? 17.310  -10.485 39.931 1.00 13.35  ? 57  PHE   B CE1 1 
ATOM   414  C CE2 . PHE   A 1 57  ? 17.853  -8.134  40.227 1.00 13.42  ? 57  PHE   B CE2 1 
ATOM   415  C CZ  . PHE   A 1 57  ? 18.251  -9.495  40.227 1.00 12.44  ? 57  PHE   B CZ  1 
ATOM   416  N N   . GLY   A 1 58  ? 13.045  -5.953  40.834 1.00 12.10  ? 58  GLY   B N   1 
ATOM   417  C CA  . GLY   A 1 58  ? 13.168  -4.789  41.703 1.00 9.05   ? 58  GLY   B CA  1 
ATOM   418  C C   . GLY   A 1 58  ? 12.545  -5.005  43.066 1.00 11.01  ? 58  GLY   B C   1 
ATOM   419  O O   . GLY   A 1 58  ? 13.084  -4.578  44.094 1.00 13.13  ? 58  GLY   B O   1 
ATOM   420  N N   . ASN   A 1 59  ? 11.376  -5.653  43.092 1.00 13.37  ? 59  ASN   B N   1 
ATOM   421  C CA  . ASN   A 1 59  ? 10.715  -5.890  44.367 1.00 12.12  ? 59  ASN   B CA  1 
ATOM   422  C C   . ASN   A 1 59  ? 11.550  -6.803  45.249 1.00 11.98  ? 59  ASN   B C   1 
ATOM   423  O O   . ASN   A 1 59  ? 11.703  -6.567  46.461 1.00 13.18  ? 59  ASN   B O   1 
ATOM   424  C CB  . ASN   A 1 59  ? 9.340   -6.504  44.124 1.00 14.80  ? 59  ASN   B CB  1 
ATOM   425  C CG  . ASN   A 1 59  ? 8.481   -6.432  45.346 1.00 16.61  ? 59  ASN   B CG  1 
ATOM   426  O OD1 . ASN   A 1 59  ? 7.839   -5.411  45.593 1.00 12.55  ? 59  ASN   B OD1 1 
ATOM   427  N ND2 . ASN   A 1 59  ? 8.535   -7.474  46.171 1.00 14.58  ? 59  ASN   B ND2 1 
ATOM   428  N N   . ALA   A 1 60  ? 12.098  -7.872  44.661 1.00 11.63  ? 60  ALA   B N   1 
ATOM   429  C CA  . ALA   A 1 60  ? 12.978  -8.728  45.441 1.00 13.32  ? 60  ALA   B CA  1 
ATOM   430  C C   . ALA   A 1 60  ? 14.239  -7.975  45.900 1.00 13.02  ? 60  ALA   B C   1 
ATOM   431  O O   . ALA   A 1 60  ? 14.740  -8.219  47.006 1.00 12.29  ? 60  ALA   B O   1 
ATOM   432  C CB  . ALA   A 1 60  ? 13.317  -9.999  44.650 1.00 12.69  ? 60  ALA   B CB  1 
ATOM   433  N N   . VAL   A 1 61  ? 14.771  -7.053  45.087 1.00 9.50   ? 61  VAL   B N   1 
ATOM   434  C CA  . VAL   A 1 61  ? 15.937  -6.274  45.548 1.00 10.41  ? 61  VAL   B CA  1 
ATOM   435  C C   . VAL   A 1 61  ? 15.573  -5.513  46.816 1.00 13.82  ? 61  VAL   B C   1 
ATOM   436  O O   . VAL   A 1 61  ? 16.333  -5.497  47.796 1.00 14.00  ? 61  VAL   B O   1 
ATOM   437  C CB  . VAL   A 1 61  ? 16.450  -5.312  44.453 1.00 11.22  ? 61  VAL   B CB  1 
ATOM   438  C CG1 . VAL   A 1 61  ? 17.518  -4.320  45.025 1.00 14.83  ? 61  VAL   B CG1 1 
ATOM   439  C CG2 . VAL   A 1 61  ? 17.020  -6.079  43.236 1.00 9.15   ? 61  VAL   B CG2 1 
ATOM   440  N N   . ILE   A 1 62  ? 14.381  -4.903  46.822 1.00 13.89  ? 62  ILE   B N   1 
ATOM   441  C CA  . ILE   A 1 62  ? 13.902  -4.182  48.000 1.00 19.39  ? 62  ILE   B CA  1 
ATOM   442  C C   . ILE   A 1 62  ? 13.816  -5.118  49.201 1.00 16.78  ? 62  ILE   B C   1 
ATOM   443  O O   . ILE   A 1 62  ? 14.295  -4.811  50.302 1.00 19.70  ? 62  ILE   B O   1 
ATOM   444  C CB  . ILE   A 1 62  ? 12.537  -3.535  47.699 1.00 21.94  ? 62  ILE   B CB  1 
ATOM   445  C CG1 . ILE   A 1 62  ? 12.683  -2.474  46.608 1.00 12.01  ? 62  ILE   B CG1 1 
ATOM   446  C CG2 . ILE   A 1 62  ? 11.953  -2.961  48.980 1.00 21.44  ? 62  ILE   B CG2 1 
ATOM   447  C CD1 . ILE   A 1 62  ? 11.387  -2.141  45.827 1.00 15.96  ? 62  ILE   B CD1 1 
ATOM   448  N N   . HIS   A 1 63  ? 13.204  -6.281  49.001 1.00 17.21  ? 63  HIS   B N   1 
ATOM   449  C CA  . HIS   A 1 63  ? 13.036  -7.226  50.094 1.00 16.86  ? 63  HIS   B CA  1 
ATOM   450  C C   . HIS   A 1 63  ? 14.396  -7.646  50.658 1.00 24.31  ? 63  HIS   B C   1 
ATOM   451  O O   . HIS   A 1 63  ? 14.611  -7.608  51.874 1.00 25.46  ? 63  HIS   B O   1 
ATOM   452  C CB  . HIS   A 1 63  ? 12.215  -8.425  49.597 1.00 24.51  ? 63  HIS   B CB  1 
ATOM   453  C CG  . HIS   A 1 63  ? 12.110  -9.561  50.571 1.00 38.51  ? 63  HIS   B CG  1 
ATOM   454  N ND1 . HIS   A 1 63  ? 12.731  -10.780 50.372 1.00 45.33  ? 63  HIS   B ND1 1 
ATOM   455  C CD2 . HIS   A 1 63  ? 11.413  -9.684  51.728 1.00 46.48  ? 63  HIS   B CD2 1 
ATOM   456  C CE1 . HIS   A 1 63  ? 12.446  -11.590 51.375 1.00 49.93  ? 63  HIS   B CE1 1 
ATOM   457  N NE2 . HIS   A 1 63  ? 11.648  -10.949 52.215 1.00 57.98  ? 63  HIS   B NE2 1 
ATOM   458  N N   . VAL   A 1 64  ? 15.345  -8.005  49.787 1.00 17.82  ? 64  VAL   B N   1 
ATOM   459  C CA  . VAL   A 1 64  ? 16.678  -8.411  50.240 1.00 18.22  ? 64  VAL   B CA  1 
ATOM   460  C C   . VAL   A 1 64  ? 17.397  -7.275  50.966 1.00 21.16  ? 64  VAL   B C   1 
ATOM   461  O O   . VAL   A 1 64  ? 18.086  -7.496  51.978 1.00 18.07  ? 64  VAL   B O   1 
ATOM   462  C CB  . VAL   A 1 64  ? 17.523  -8.906  49.058 1.00 20.48  ? 64  VAL   B CB  1 
ATOM   463  C CG1 . VAL   A 1 64  ? 19.003  -9.027  49.495 1.00 11.73  ? 64  VAL   B CG1 1 
ATOM   464  C CG2 . VAL   A 1 64  ? 16.990  -10.252 48.537 1.00 15.20  ? 64  VAL   B CG2 1 
ATOM   465  N N   . THR   A 1 65  ? 17.317  -6.056  50.426 1.00 20.73  ? 65  THR   B N   1 
ATOM   466  C CA  . THR   A 1 65  ? 17.965  -4.939  51.095 1.00 19.39  ? 65  THR   B CA  1 
ATOM   467  C C   . THR   A 1 65  ? 17.420  -4.806  52.503 1.00 27.96  ? 65  THR   B C   1 
ATOM   468  O O   . THR   A 1 65  ? 18.175  -4.666  53.474 1.00 20.21  ? 65  THR   B O   1 
ATOM   469  C CB  . THR   A 1 65  ? 17.730  -3.645  50.328 1.00 15.41  ? 65  THR   B CB  1 
ATOM   470  O OG1 . THR   A 1 65  ? 18.138  -3.807  48.972 1.00 14.33  ? 65  THR   B OG1 1 
ATOM   471  C CG2 . THR   A 1 65  ? 18.572  -2.503  50.947 1.00 19.69  ? 65  THR   B CG2 1 
ATOM   472  N N   . ARG   A 1 66  ? 16.093  -4.900  52.624 1.00 24.00  ? 66  ARG   B N   1 
ATOM   473  C CA  . ARG   A 1 66  ? 15.443  -4.722  53.915 1.00 32.08  ? 66  ARG   B CA  1 
ATOM   474  C C   . ARG   A 1 66  ? 15.741  -5.874  54.869 1.00 33.06  ? 66  ARG   B C   1 
ATOM   475  O O   . ARG   A 1 66  ? 15.877  -5.656  56.078 1.00 32.74  ? 66  ARG   B O   1 
ATOM   476  C CB  . ARG   A 1 66  ? 13.938  -4.512  53.706 1.00 37.12  ? 66  ARG   B CB  1 
ATOM   477  C CG  . ARG   A 1 66  ? 13.641  -3.032  53.426 1.00 38.62  ? 66  ARG   B CG  1 
ATOM   478  C CD  . ARG   A 1 66  ? 12.296  -2.713  52.769 1.00 47.88  ? 66  ARG   B CD  1 
ATOM   479  N NE  . ARG   A 1 66  ? 12.232  -1.293  52.382 1.00 44.81  ? 66  ARG   B NE  1 
ATOM   480  C CZ  . ARG   A 1 66  ? 11.262  -0.737  51.652 1.00 41.78  ? 66  ARG   B CZ  1 
ATOM   481  N NH1 . ARG   A 1 66  ? 10.223  -1.465  51.250 1.00 47.24  ? 66  ARG   B NH1 1 
ATOM   482  N NH2 . ARG   A 1 66  ? 11.303  0.560   51.359 1.00 45.33  ? 66  ARG   B NH2 1 
ATOM   483  N N   . SER   A 1 67  ? 15.898  -7.094  54.353 1.00 28.88  ? 67  SER   B N   1 
ATOM   484  C CA  . SER   A 1 67  ? 16.170  -8.218  55.247 1.00 35.77  ? 67  SER   B CA  1 
ATOM   485  C C   . SER   A 1 67  ? 17.636  -8.273  55.652 1.00 32.07  ? 67  SER   B C   1 
ATOM   486  O O   . SER   A 1 67  ? 17.975  -8.936  56.639 1.00 34.13  ? 67  SER   B O   1 
ATOM   487  C CB  . SER   A 1 67  ? 15.779  -9.547  54.603 1.00 35.04  ? 67  SER   B CB  1 
ATOM   488  O OG  . SER   A 1 67  ? 16.284  -9.606  53.286 1.00 48.99  ? 67  SER   B OG  1 
ATOM   489  N N   . ASN   A 1 68  ? 18.523  -7.598  54.906 1.00 35.51  ? 68  ASN   B N   1 
ATOM   490  C CA  . ASN   A 1 68  ? 19.914  -7.518  55.343 1.00 35.43  ? 68  ASN   B CA  1 
ATOM   491  C C   . ASN   A 1 68  ? 20.100  -6.517  56.474 1.00 35.55  ? 68  ASN   B C   1 
ATOM   492  O O   . ASN   A 1 68  ? 21.162  -6.518  57.104 1.00 43.58  ? 68  ASN   B O   1 
ATOM   493  C CB  . ASN   A 1 68  ? 20.828  -7.156  54.174 1.00 39.57  ? 68  ASN   B CB  1 
ATOM   494  C CG  . ASN   A 1 68  ? 20.987  -8.300  53.192 1.00 37.99  ? 68  ASN   B CG  1 
ATOM   495  O OD1 . ASN   A 1 68  ? 20.449  -9.387  53.417 1.00 34.49  ? 68  ASN   B OD1 1 
ATOM   496  N ND2 . ASN   A 1 68  ? 21.672  -8.042  52.064 1.00 28.32  ? 68  ASN   B ND2 1 
ATOM   497  N N   . LYS   A 1 69  ? 19.099  -5.669  56.733 1.00 34.25  ? 69  LYS   B N   1 
ATOM   498  C CA  . LYS   A 1 69  ? 18.937  -4.785  57.902 1.00 39.70  ? 69  LYS   B CA  1 
ATOM   499  C C   . LYS   A 1 69  ? 19.881  -3.593  57.966 1.00 35.55  ? 69  LYS   B C   1 
ATOM   500  O O   . LYS   A 1 69  ? 19.872  -2.889  58.992 1.00 34.17  ? 69  LYS   B O   1 
ATOM   501  C CB  . LYS   A 1 69  ? 19.095  -5.501  59.257 1.00 37.03  ? 69  LYS   B CB  1 
ATOM   502  C CG  . LYS   A 1 69  ? 18.119  -6.632  59.571 1.00 40.70  ? 69  LYS   B CG  1 
ATOM   503  C CD  . LYS   A 1 69  ? 16.631  -6.254  59.750 1.00 40.30  ? 69  LYS   B CD  1 
ATOM   504  C CE  . LYS   A 1 69  ? 15.836  -7.499  60.210 1.00 45.58  ? 69  LYS   B CE  1 
ATOM   505  N NZ  . LYS   A 1 69  ? 15.732  -8.608  59.250 1.00 49.20  ? 69  LYS   B NZ  1 
ATOM   506  N N   . GLU   A 1 70  ? 20.694  -3.330  56.953 1.00 33.46  ? 70  GLU   B N   1 
ATOM   507  C CA  . GLU   A 1 70  ? 21.658  -2.253  57.126 1.00 33.14  ? 70  GLU   B CA  1 
ATOM   508  C C   . GLU   A 1 70  ? 21.064  -0.927  56.666 1.00 31.34  ? 70  GLU   B C   1 
ATOM   509  O O   . GLU   A 1 70  ? 20.996  0.028   57.441 1.00 28.24  ? 70  GLU   B O   1 
ATOM   510  C CB  . GLU   A 1 70  ? 22.965  -2.587  56.387 1.00 37.90  ? 70  GLU   B CB  1 
ATOM   511  C CG  . GLU   A 1 70  ? 23.553  -3.957  56.762 1.00 44.36  ? 70  GLU   B CG  1 
ATOM   512  C CD  . GLU   A 1 70  ? 24.653  -4.450  55.813 1.00 56.16  ? 70  GLU   B CD  1 
ATOM   513  O OE1 . GLU   A 1 70  ? 24.499  -4.313  54.570 1.00 53.50  ? 70  GLU   B OE1 1 
ATOM   514  O OE2 . GLU   A 1 70  ? 25.659  -5.011  56.314 1.00 53.76  ? 70  GLU   B OE2 1 
ATOM   515  N N   . TYR   A 1 71  ? 20.565  -0.883  55.436 1.00 26.02  ? 71  TYR   B N   1 
ATOM   516  C CA  . TYR   A 1 71  ? 20.236  0.362   54.760 1.00 25.06  ? 71  TYR   B CA  1 
ATOM   517  C C   . TYR   A 1 71  ? 18.800  0.820   55.011 1.00 24.36  ? 71  TYR   B C   1 
ATOM   518  O O   . TYR   A 1 71  ? 17.887  0.010   55.159 1.00 24.19  ? 71  TYR   B O   1 
ATOM   519  C CB  . TYR   A 1 71  ? 20.452  0.183   53.256 1.00 20.43  ? 71  TYR   B CB  1 
ATOM   520  C CG  . TYR   A 1 71  ? 21.905  0.120   52.857 1.00 28.89  ? 71  TYR   B CG  1 
ATOM   521  C CD1 . TYR   A 1 71  ? 22.636  1.297   52.722 1.00 29.67  ? 71  TYR   B CD1 1 
ATOM   522  C CD2 . TYR   A 1 71  ? 22.549  -1.102  52.619 1.00 24.76  ? 71  TYR   B CD2 1 
ATOM   523  C CE1 . TYR   A 1 71  ? 23.954  1.284   52.350 1.00 23.25  ? 71  TYR   B CE1 1 
ATOM   524  C CE2 . TYR   A 1 71  ? 23.895  -1.135  52.254 1.00 22.86  ? 71  TYR   B CE2 1 
ATOM   525  C CZ  . TYR   A 1 71  ? 24.581  0.079   52.101 1.00 27.68  ? 71  TYR   B CZ  1 
ATOM   526  O OH  . TYR   A 1 71  ? 25.900  0.140   51.737 1.00 18.52  ? 71  TYR   B OH  1 
ATOM   527  N N   . LYS   A 1 72  ? 18.607  2.138   55.011 1.00 22.74  ? 72  LYS   B N   1 
ATOM   528  C CA  . LYS   A 1 72  ? 17.276  2.740   54.974 1.00 35.03  ? 72  LYS   B CA  1 
ATOM   529  C C   . LYS   A 1 72  ? 16.955  3.051   53.524 1.00 30.65  ? 72  LYS   B C   1 
ATOM   530  O O   . LYS   A 1 72  ? 17.577  3.935   52.934 1.00 34.94  ? 72  LYS   B O   1 
ATOM   531  C CB  . LYS   A 1 72  ? 17.209  4.039   55.770 1.00 25.90  ? 72  LYS   B CB  1 
ATOM   532  C CG  . LYS   A 1 72  ? 17.465  3.936   57.240 1.00 37.33  ? 72  LYS   B CG  1 
ATOM   533  C CD  . LYS   A 1 72  ? 17.287  5.320   57.851 1.00 42.10  ? 72  LYS   B CD  1 
ATOM   534  C CE  . LYS   A 1 72  ? 18.306  5.596   58.946 1.00 42.69  ? 72  LYS   B CE  1 
ATOM   535  N NZ  . LYS   A 1 72  ? 18.080  4.759   60.150 1.00 49.25  ? 72  LYS   B NZ  1 
ATOM   536  N N   . ILE   A 1 73  ? 15.982  2.362   52.946 1.00 18.87  ? 73  ILE   B N   1 
ATOM   537  C CA  . ILE   A 1 73  ? 15.586  2.697   51.591 1.00 25.91  ? 73  ILE   B CA  1 
ATOM   538  C C   . ILE   A 1 73  ? 14.078  2.855   51.521 1.00 28.97  ? 73  ILE   B C   1 
ATOM   539  O O   . ILE   A 1 73  ? 13.327  2.292   52.324 1.00 35.88  ? 73  ILE   B O   1 
ATOM   540  C CB  . ILE   A 1 73  ? 16.060  1.660   50.547 1.00 23.83  ? 73  ILE   B CB  1 
ATOM   541  C CG1 . ILE   A 1 73  ? 15.475  0.283   50.841 1.00 27.09  ? 73  ILE   B CG1 1 
ATOM   542  C CG2 . ILE   A 1 73  ? 17.588  1.626   50.454 1.00 26.22  ? 73  ILE   B CG2 1 
ATOM   543  C CD1 . ILE   A 1 73  ? 15.728  -0.670  49.694 1.00 27.92  ? 73  ILE   B CD1 1 
ATOM   544  N N   . ARG   A 1 74  ? 13.645  3.660   50.566 1.00 28.87  ? 74  ARG   B N   1 
ATOM   545  C CA  . ARG   A 1 74  ? 12.277  3.618   50.104 1.00 33.36  ? 74  ARG   B CA  1 
ATOM   546  C C   . ARG   A 1 74  ? 12.208  2.846   48.787 1.00 30.28  ? 74  ARG   B C   1 
ATOM   547  O O   . ARG   A 1 74  ? 13.216  2.636   48.104 1.00 24.35  ? 74  ARG   B O   1 
ATOM   548  C CB  . ARG   A 1 74  ? 11.708  5.036   49.982 1.00 33.55  ? 74  ARG   B CB  1 
ATOM   549  C CG  . ARG   A 1 74  ? 12.577  6.022   49.257 1.00 36.12  ? 74  ARG   B CG  1 
ATOM   550  C CD  . ARG   A 1 74  ? 11.983  7.429   49.326 1.00 40.06  ? 74  ARG   B CD  1 
ATOM   551  N NE  . ARG   A 1 74  ? 12.682  8.356   48.435 1.00 55.46  ? 74  ARG   B NE  1 
ATOM   552  C CZ  . ARG   A 1 74  ? 13.477  9.348   48.842 1.00 57.32  ? 74  ARG   B CZ  1 
ATOM   553  N NH1 . ARG   A 1 74  ? 13.683  9.557   50.143 1.00 48.27  ? 74  ARG   B NH1 1 
ATOM   554  N NH2 . ARG   A 1 74  ? 14.074  10.132  47.943 1.00 56.25  ? 74  ARG   B NH2 1 
ATOM   555  N N   . ASP   A 1 75  ? 10.993  2.395   48.468 1.00 29.59  ? 75  ASP   B N   1 
ATOM   556  C CA  . ASP   A 1 75  ? 10.742  1.593   47.271 1.00 24.98  ? 75  ASP   B CA  1 
ATOM   557  C C   . ASP   A 1 75  ? 11.373  2.189   46.021 1.00 22.24  ? 75  ASP   B C   1 
ATOM   558  O O   . ASP   A 1 75  ? 11.992  1.478   45.219 1.00 17.70  ? 75  ASP   B O   1 
ATOM   559  C CB  . ASP   A 1 75  ? 9.234   1.440   47.068 1.00 27.98  ? 75  ASP   B CB  1 
ATOM   560  C CG  . ASP   A 1 75  ? 8.587   0.519   48.100 1.00 35.57  ? 75  ASP   B CG  1 
ATOM   561  O OD1 . ASP   A 1 75  ? 9.306   -0.058  48.957 1.00 33.36  ? 75  ASP   B OD1 1 
ATOM   562  O OD2 . ASP   A 1 75  ? 7.346   0.371   48.043 1.00 41.98  ? 75  ASP   B OD2 1 
ATOM   563  N N   . ASN   A 1 76  ? 11.191  3.483   45.808 1.00 20.59  ? 76  ASN   B N   1 
ATOM   564  C CA  . ASN   A 1 76  ? 11.663  4.076   44.561 1.00 18.77  ? 76  ASN   B CA  1 
ATOM   565  C C   . ASN   A 1 76  ? 13.184  4.243   44.502 1.00 21.75  ? 76  ASN   B C   1 
ATOM   566  O O   . ASN   A 1 76  ? 13.683  4.806   43.519 1.00 19.70  ? 76  ASN   B O   1 
ATOM   567  C CB  . ASN   A 1 76  ? 11.008  5.442   44.331 1.00 30.68  ? 76  ASN   B CB  1 
ATOM   568  C CG  . ASN   A 1 76  ? 9.530   5.338   44.020 1.00 34.79  ? 76  ASN   B CG  1 
ATOM   569  O OD1 . ASN   A 1 76  ? 8.814   6.334   44.058 1.00 48.16  ? 76  ASN   B OD1 1 
ATOM   570  N ND2 . ASN   A 1 76  ? 9.058   4.125   43.746 1.00 33.78  ? 76  ASN   B ND2 1 
ATOM   571  N N   . ASP   A 1 77  ? 13.936  3.796   45.514 1.00 20.37  ? 77  ASP   B N   1 
ATOM   572  C CA  . ASP   A 1 77  ? 15.395  3.775   45.388 1.00 20.32  ? 77  ASP   B CA  1 
ATOM   573  C C   . ASP   A 1 77  ? 15.906  2.587   44.567 1.00 19.87  ? 77  ASP   B C   1 
ATOM   574  O O   . ASP   A 1 77  ? 17.121  2.447   44.386 1.00 14.21  ? 77  ASP   B O   1 
ATOM   575  C CB  . ASP   A 1 77  ? 16.072  3.774   46.770 1.00 20.33  ? 77  ASP   B CB  1 
ATOM   576  C CG  . ASP   A 1 77  ? 15.864  5.088   47.537 1.00 28.56  ? 77  ASP   B CG  1 
ATOM   577  O OD1 . ASP   A 1 77  ? 15.679  6.134   46.869 1.00 31.35  ? 77  ASP   B OD1 1 
ATOM   578  O OD2 . ASP   A 1 77  ? 15.865  5.076   48.789 1.00 24.56  ? 77  ASP   B OD2 1 
ATOM   579  N N   . VAL   A 1 78  ? 15.029  1.732   44.064 1.00 14.28  ? 78  VAL   B N   1 
ATOM   580  C CA  . VAL   A 1 78  ? 15.442  0.588   43.267 1.00 14.53  ? 78  VAL   B CA  1 
ATOM   581  C C   . VAL   A 1 78  ? 14.848  0.748   41.883 1.00 14.10  ? 78  VAL   B C   1 
ATOM   582  O O   . VAL   A 1 78  ? 13.647  1.008   41.739 1.00 18.91  ? 78  VAL   B O   1 
ATOM   583  C CB  . VAL   A 1 78  ? 15.015  -0.742  43.907 1.00 15.80  ? 78  VAL   B CB  1 
ATOM   584  C CG1 . VAL   A 1 78  ? 15.351  -1.895  42.970 1.00 15.97  ? 78  VAL   B CG1 1 
ATOM   585  C CG2 . VAL   A 1 78  ? 15.717  -0.911  45.239 1.00 12.28  ? 78  VAL   B CG2 1 
ATOM   586  N N   . GLU   A 1 79  ? 15.689  0.609   40.868 1.00 15.00  ? 79  GLU   B N   1 
ATOM   587  C CA  . GLU   A 1 79  ? 15.256  0.658   39.487 1.00 12.14  ? 79  GLU   B CA  1 
ATOM   588  C C   . GLU   A 1 79  ? 15.839  -0.532  38.742 1.00 20.47  ? 79  GLU   B C   1 
ATOM   589  O O   . GLU   A 1 79  ? 17.015  -0.860  38.924 1.00 15.09  ? 79  GLU   B O   1 
ATOM   590  C CB  . GLU   A 1 79  ? 15.722  1.956   38.841 1.00 15.56  ? 79  GLU   B CB  1 
ATOM   591  C CG  . GLU   A 1 79  ? 15.383  2.082   37.389 1.00 26.18  ? 79  GLU   B CG  1 
ATOM   592  C CD  . GLU   A 1 79  ? 16.129  3.255   36.758 1.00 39.08  ? 79  GLU   B CD  1 
ATOM   593  O OE1 . GLU   A 1 79  ? 15.951  4.403   37.242 1.00 37.42  ? 79  GLU   B OE1 1 
ATOM   594  O OE2 . GLU   A 1 79  ? 16.923  3.003   35.817 1.00 32.67  ? 79  GLU   B OE2 1 
ATOM   595  N N   . VAL   A 1 80  ? 15.019  -1.167  37.895 1.00 15.95  ? 80  VAL   B N   1 
ATOM   596  C CA  . VAL   A 1 80  ? 15.464  -2.255  37.038 1.00 15.18  ? 80  VAL   B CA  1 
ATOM   597  C C   . VAL   A 1 80  ? 15.073  -1.945  35.597 1.00 14.26  ? 80  VAL   B C   1 
ATOM   598  O O   . VAL   A 1 80  ? 13.901  -1.704  35.300 1.00 15.36  ? 80  VAL   B O   1 
ATOM   599  C CB  . VAL   A 1 80  ? 14.878  -3.613  37.473 1.00 14.82  ? 80  VAL   B CB  1 
ATOM   600  C CG1 . VAL   A 1 80  ? 15.368  -4.702  36.528 1.00 11.55  ? 80  VAL   B CG1 1 
ATOM   601  C CG2 . VAL   A 1 80  ? 15.232  -3.901  38.952 1.00 10.56  ? 80  VAL   B CG2 1 
ATOM   602  N N   . LEU   A 1 81  ? 16.056  -1.948  34.714 1.00 12.16  ? 81  LEU   B N   1 
ATOM   603  C CA  . LEU   A 1 81  ? 15.870  -1.786  33.286 1.00 11.47  ? 81  LEU   B CA  1 
ATOM   604  C C   . LEU   A 1 81  ? 16.190  -3.133  32.662 1.00 14.08  ? 81  LEU   B C   1 
ATOM   605  O O   . LEU   A 1 81  ? 17.359  -3.538  32.626 1.00 15.41  ? 81  LEU   B O   1 
ATOM   606  C CB  . LEU   A 1 81  ? 16.809  -0.720  32.732 1.00 14.01  ? 81  LEU   B CB  1 
ATOM   607  C CG  . LEU   A 1 81  ? 16.686  -0.393  31.238 1.00 18.98  ? 81  LEU   B CG  1 
ATOM   608  C CD1 . LEU   A 1 81  ? 15.254  -0.089  30.853 1.00 25.88  ? 81  LEU   B CD1 1 
ATOM   609  C CD2 . LEU   A 1 81  ? 17.604  0.753   30.852 1.00 34.20  ? 81  LEU   B CD2 1 
ATOM   610  N N   . SER   A 1 82  ? 15.171  -3.832  32.177 1.00 14.29  ? 82  SER   B N   1 
ATOM   611  C CA  . SER   A 1 82  ? 15.394  -5.115  31.532 1.00 16.94  ? 82  SER   B CA  1 
ATOM   612  C C   . SER   A 1 82  ? 15.425  -4.955  30.017 1.00 21.45  ? 82  SER   B C   1 
ATOM   613  O O   . SER   A 1 82  ? 14.655  -4.175  29.438 1.00 17.19  ? 82  SER   B O   1 
ATOM   614  C CB  . SER   A 1 82  ? 14.312  -6.118  31.923 1.00 11.18  ? 82  SER   B CB  1 
ATOM   615  O OG  . SER   A 1 82  ? 13.055  -5.583  31.608 1.00 19.71  ? 82  SER   B OG  1 
ATOM   616  N N   . THR   A 1 83  ? 16.319  -5.705  29.378 1.00 17.55  ? 83  THR   B N   1 
ATOM   617  C CA  . THR   A 1 83  ? 16.388  -5.803  27.929 1.00 14.43  ? 83  THR   B CA  1 
ATOM   618  C C   . THR   A 1 83  ? 16.053  -7.234  27.566 1.00 18.15  ? 83  THR   B C   1 
ATOM   619  O O   . THR   A 1 83  ? 16.739  -8.159  28.003 1.00 17.38  ? 83  THR   B O   1 
ATOM   620  C CB  . THR   A 1 83  ? 17.772  -5.438  27.394 1.00 18.68  ? 83  THR   B CB  1 
ATOM   621  O OG1 . THR   A 1 83  ? 18.114  -4.110  27.802 1.00 23.40  ? 83  THR   B OG1 1 
ATOM   622  C CG2 . THR   A 1 83  ? 17.792  -5.506  25.847 1.00 22.47  ? 83  THR   B CG2 1 
ATOM   623  N N   . VAL   A 1 84  ? 14.987  -7.425  26.809 1.00 14.79  ? 84  VAL   B N   1 
ATOM   624  C CA  . VAL   A 1 84  ? 14.589  -8.759  26.384 1.00 18.72  ? 84  VAL   B CA  1 
ATOM   625  C C   . VAL   A 1 84  ? 14.653  -8.796  24.871 1.00 20.92  ? 84  VAL   B C   1 
ATOM   626  O O   . VAL   A 1 84  ? 14.168  -7.877  24.203 1.00 19.06  ? 84  VAL   B O   1 
ATOM   627  C CB  . VAL   A 1 84  ? 13.198  -9.123  26.904 1.00 11.34  ? 84  VAL   B CB  1 
ATOM   628  C CG1 . VAL   A 1 84  ? 12.724  -10.424 26.271 1.00 18.28  ? 84  VAL   B CG1 1 
ATOM   629  C CG2 . VAL   A 1 84  ? 13.244  -9.223  28.431 1.00 13.54  ? 84  VAL   B CG2 1 
ATOM   630  N N   . GLY   A 1 85  ? 15.288  -9.827  24.344 1.00 16.80  ? 85  GLY   B N   1 
ATOM   631  C CA  . GLY   A 1 85  ? 15.349  -10.004 22.909 1.00 18.90  ? 85  GLY   B CA  1 
ATOM   632  C C   . GLY   A 1 85  ? 14.915  -11.396 22.503 1.00 27.36  ? 85  GLY   B C   1 
ATOM   633  O O   . GLY   A 1 85  ? 14.843  -12.305 23.343 1.00 24.69  ? 85  GLY   B O   1 
ATOM   634  N N   . ILE   A 1 86  ? 14.626  -11.580 21.220 1.00 23.58  ? 86  ILE   B N   1 
ATOM   635  C CA  . ILE   A 1 86  ? 14.277  -12.880 20.663 1.00 23.47  ? 86  ILE   B CA  1 
ATOM   636  C C   . ILE   A 1 86  ? 15.271  -13.166 19.537 1.00 21.77  ? 86  ILE   B C   1 
ATOM   637  O O   . ILE   A 1 86  ? 15.503  -12.312 18.677 1.00 28.49  ? 86  ILE   B O   1 
ATOM   638  C CB  . ILE   A 1 86  ? 12.800  -12.912 20.209 1.00 23.41  ? 86  ILE   B CB  1 
ATOM   639  C CG1 . ILE   A 1 86  ? 12.414  -14.275 19.613 1.00 33.30  ? 86  ILE   B CG1 1 
ATOM   640  C CG2 . ILE   A 1 86  ? 12.457  -11.726 19.310 1.00 23.53  ? 86  ILE   B CG2 1 
ATOM   641  C CD1 . ILE   A 1 86  ? 10.911  -14.618 19.780 1.00 30.69  ? 86  ILE   B CD1 1 
ATOM   642  N N   . VAL   A 1 87  ? 15.931  -14.320 19.607 1.00 25.99  ? 87  VAL   B N   1 
ATOM   643  C CA  . VAL   A 1 87  ? 17.010  -14.689 18.698 1.00 35.62  ? 87  VAL   B CA  1 
ATOM   644  C C   . VAL   A 1 87  ? 16.641  -15.998 18.012 1.00 35.20  ? 87  VAL   B C   1 
ATOM   645  O O   . VAL   A 1 87  ? 15.804  -16.764 18.499 1.00 39.73  ? 87  VAL   B O   1 
ATOM   646  C CB  . VAL   A 1 87  ? 18.381  -14.837 19.407 1.00 35.84  ? 87  VAL   B CB  1 
ATOM   647  C CG1 . VAL   A 1 87  ? 18.814  -13.541 20.048 1.00 32.22  ? 87  VAL   B CG1 1 
ATOM   648  C CG2 . VAL   A 1 87  ? 18.345  -15.963 20.433 1.00 28.92  ? 87  VAL   B CG2 1 
ATOM   649  N N   . ALA   A 1 88  ? 17.264  -16.246 16.864 1.00 46.66  ? 88  ALA   B N   1 
ATOM   650  C CA  . ALA   A 1 88  ? 17.115  -17.538 16.201 1.00 52.84  ? 88  ALA   B CA  1 
ATOM   651  C C   . ALA   A 1 88  ? 17.956  -18.597 16.909 1.00 49.10  ? 88  ALA   B C   1 
ATOM   652  O O   . ALA   A 1 88  ? 19.162  -18.403 17.090 1.00 53.66  ? 88  ALA   B O   1 
ATOM   653  C CB  . ALA   A 1 88  ? 17.538  -17.414 14.742 1.00 46.88  ? 88  ALA   B CB  1 
ATOM   654  N N   . ASN   A 1 89  ? 17.341  -19.717 17.309 1.00 57.50  ? 89  ASN   B N   1 
ATOM   655  C CA  . ASN   A 1 89  ? 18.133  -20.877 17.704 1.00 66.91  ? 89  ASN   B CA  1 
ATOM   656  C C   . ASN   A 1 89  ? 17.892  -22.044 16.749 1.00 70.92  ? 89  ASN   B C   1 
ATOM   657  O O   . ASN   A 1 89  ? 16.952  -22.047 15.938 1.00 61.44  ? 89  ASN   B O   1 
ATOM   658  C CB  . ASN   A 1 89  ? 17.849  -21.405 19.136 1.00 64.41  ? 89  ASN   B CB  1 
ATOM   659  C CG  . ASN   A 1 89  ? 16.477  -22.085 19.297 1.00 61.67  ? 89  ASN   B CG  1 
ATOM   660  O OD1 . ASN   A 1 89  ? 15.726  -22.287 18.348 1.00 60.30  ? 89  ASN   B OD1 1 
ATOM   661  N ND2 . ASN   A 1 89  ? 16.202  -22.524 20.524 1.00 58.75  ? 89  ASN   B ND2 1 
ATOM   662  N N   . GLY   A 1 90  ? 18.757  -23.048 16.902 1.00 79.11  ? 90  GLY   B N   1 
ATOM   663  C CA  . GLY   A 1 90  ? 18.598  -24.369 16.341 1.00 81.91  ? 90  GLY   B CA  1 
ATOM   664  C C   . GLY   A 1 90  ? 18.303  -24.376 14.863 1.00 85.15  ? 90  GLY   B C   1 
ATOM   665  O O   . GLY   A 1 90  ? 19.155  -24.061 14.026 1.00 85.39  ? 90  GLY   B O   1 
ATOM   666  N N   . ASN   A 1 91  ? 17.061  -24.703 14.545 1.00 88.44  ? 91  ASN   B N   1 
ATOM   667  C CA  . ASN   A 1 91  ? 16.632  -24.976 13.182 1.00 91.74  ? 91  ASN   B CA  1 
ATOM   668  C C   . ASN   A 1 91  ? 15.398  -24.144 12.833 1.00 88.30  ? 91  ASN   B C   1 
ATOM   669  O O   . ASN   A 1 91  ? 14.298  -24.657 12.634 1.00 97.57  ? 91  ASN   B O   1 
ATOM   670  C CB  . ASN   A 1 91  ? 16.429  -26.483 13.048 1.00 97.21  ? 91  ASN   B CB  1 
ATOM   671  C CG  . ASN   A 1 91  ? 15.424  -27.034 14.055 1.00 101.59 ? 91  ASN   B CG  1 
ATOM   672  O OD1 . ASN   A 1 91  ? 14.806  -26.284 14.819 1.00 103.11 ? 91  ASN   B OD1 1 
ATOM   673  N ND2 . ASN   A 1 91  ? 15.252  -28.357 14.052 1.00 102.30 ? 91  ASN   B ND2 1 
ATOM   674  N N   . GLY   A 1 92  ? 15.606  -22.833 12.720 1.00 80.50  ? 92  GLY   B N   1 
ATOM   675  C CA  . GLY   A 1 92  ? 14.511  -21.913 12.514 1.00 73.64  ? 92  GLY   B CA  1 
ATOM   676  C C   . GLY   A 1 92  ? 13.699  -21.629 13.753 1.00 65.00  ? 92  GLY   B C   1 
ATOM   677  O O   . GLY   A 1 92  ? 12.632  -21.012 13.648 1.00 62.04  ? 92  GLY   B O   1 
ATOM   678  N N   . GLY   A 1 93  ? 14.168  -22.073 14.922 1.00 60.19  ? 93  GLY   B N   1 
ATOM   679  C CA  . GLY   A 1 93  ? 13.477  -21.825 16.164 1.00 53.15  ? 93  GLY   B CA  1 
ATOM   680  C C   . GLY   A 1 93  ? 13.885  -20.501 16.773 1.00 45.56  ? 93  GLY   B C   1 
ATOM   681  O O   . GLY   A 1 93  ? 14.694  -19.750 16.229 1.00 46.10  ? 93  GLY   B O   1 
ATOM   682  N N   . PHE   A 1 94  ? 13.330  -20.221 17.951 1.00 36.32  ? 94  PHE   B N   1 
ATOM   683  C CA  . PHE   A 1 94  ? 13.548  -18.927 18.584 1.00 35.90  ? 94  PHE   B CA  1 
ATOM   684  C C   . PHE   A 1 94  ? 13.756  -19.095 20.084 1.00 33.78  ? 94  PHE   B C   1 
ATOM   685  O O   . PHE   A 1 94  ? 13.133  -19.955 20.717 1.00 32.41  ? 94  PHE   B O   1 
ATOM   686  C CB  . PHE   A 1 94  ? 12.376  -17.987 18.302 1.00 31.49  ? 94  PHE   B CB  1 
ATOM   687  C CG  . PHE   A 1 94  ? 12.157  -17.739 16.842 1.00 33.45  ? 94  PHE   B CG  1 
ATOM   688  C CD1 . PHE   A 1 94  ? 12.933  -16.819 16.155 1.00 42.29  ? 94  PHE   B CD1 1 
ATOM   689  C CD2 . PHE   A 1 94  ? 11.210  -18.469 16.144 1.00 43.28  ? 94  PHE   B CD2 1 
ATOM   690  C CE1 . PHE   A 1 94  ? 12.744  -16.607 14.799 1.00 43.40  ? 94  PHE   B CE1 1 
ATOM   691  C CE2 . PHE   A 1 94  ? 11.013  -18.264 14.793 1.00 47.15  ? 94  PHE   B CE2 1 
ATOM   692  C CZ  . PHE   A 1 94  ? 11.779  -17.330 14.118 1.00 43.68  ? 94  PHE   B CZ  1 
ATOM   693  N N   . ALA   A 1 95  ? 14.647  -18.273 20.636 1.00 24.76  ? 95  ALA   B N   1 
ATOM   694  C CA  . ALA   A 1 95  ? 14.934  -18.246 22.066 1.00 27.43  ? 95  ALA   B CA  1 
ATOM   695  C C   . ALA   A 1 95  ? 14.867  -16.806 22.569 1.00 21.49  ? 95  ALA   B C   1 
ATOM   696  O O   . ALA   A 1 95  ? 14.935  -15.853 21.788 1.00 22.48  ? 95  ALA   B O   1 
ATOM   697  C CB  . ALA   A 1 95  ? 16.313  -18.862 22.371 1.00 19.27  ? 95  ALA   B CB  1 
ATOM   698  N N   . LEU   A 1 96  ? 14.745  -16.653 23.886 1.00 17.75  ? 96  LEU   B N   1 
ATOM   699  C CA  . LEU   A 1 96  ? 14.748  -15.352 24.536 1.00 17.86  ? 96  LEU   B CA  1 
ATOM   700  C C   . LEU   A 1 96  ? 16.129  -15.074 25.118 1.00 19.81  ? 96  LEU   B C   1 
ATOM   701  O O   . LEU   A 1 96  ? 16.837  -15.990 25.531 1.00 13.38  ? 96  LEU   B O   1 
ATOM   702  C CB  . LEU   A 1 96  ? 13.708  -15.301 25.659 1.00 17.04  ? 96  LEU   B CB  1 
ATOM   703  C CG  . LEU   A 1 96  ? 12.236  -15.402 25.232 1.00 25.33  ? 96  LEU   B CG  1 
ATOM   704  C CD1 . LEU   A 1 96  ? 11.361  -15.535 26.462 1.00 24.10  ? 96  LEU   B CD1 1 
ATOM   705  C CD2 . LEU   A 1 96  ? 11.844  -14.160 24.424 1.00 24.91  ? 96  LEU   B CD2 1 
ATOM   706  N N   . THR   A 1 97  ? 16.493  -13.794 25.163 1.00 14.79  ? 97  THR   B N   1 
ATOM   707  C CA  . THR   A 1 97  ? 17.658  -13.320 25.896 1.00 15.42  ? 97  THR   B CA  1 
ATOM   708  C C   . THR   A 1 97  ? 17.220  -12.226 26.862 1.00 14.89  ? 97  THR   B C   1 
ATOM   709  O O   . THR   A 1 97  ? 16.270  -11.483 26.590 1.00 16.46  ? 97  THR   B O   1 
ATOM   710  C CB  . THR   A 1 97  ? 18.741  -12.759 24.956 1.00 16.46  ? 97  THR   B CB  1 
ATOM   711  O OG1 . THR   A 1 97  ? 18.192  -11.654 24.227 1.00 20.01  ? 97  THR   B OG1 1 
ATOM   712  C CG2 . THR   A 1 97  ? 19.231  -13.821 23.982 1.00 14.07  ? 97  THR   B CG2 1 
ATOM   713  N N   . VAL   A 1 98  ? 17.920  -12.116 27.990 1.00 16.56  ? 98  VAL   B N   1 
ATOM   714  C CA  . VAL   A 1 98  ? 17.583  -11.141 29.017 1.00 15.00  ? 98  VAL   B CA  1 
ATOM   715  C C   . VAL   A 1 98  ? 18.868  -10.533 29.569 1.00 21.83  ? 98  VAL   B C   1 
ATOM   716  O O   . VAL   A 1 98  ? 19.783  -11.253 29.977 1.00 13.23  ? 98  VAL   B O   1 
ATOM   717  C CB  . VAL   A 1 98  ? 16.770  -11.764 30.174 1.00 12.86  ? 98  VAL   B CB  1 
ATOM   718  C CG1 . VAL   A 1 98  ? 16.449  -10.679 31.194 1.00 11.61  ? 98  VAL   B CG1 1 
ATOM   719  C CG2 . VAL   A 1 98  ? 15.499  -12.443 29.658 1.00 10.11  ? 98  VAL   B CG2 1 
ATOM   720  N N   . HIS   A 1 99  ? 18.926  -9.212  29.607 1.00 14.31  ? 99  HIS   B N   1 
ATOM   721  C CA  . HIS   A 1 99  ? 19.935  -8.497  30.363 1.00 13.41  ? 99  HIS   B CA  1 
ATOM   722  C C   . HIS   A 1 99  ? 19.243  -7.586  31.364 1.00 14.88  ? 99  HIS   B C   1 
ATOM   723  O O   . HIS   A 1 99  ? 18.268  -6.925  31.007 1.00 11.59  ? 99  HIS   B O   1 
ATOM   724  C CB  . HIS   A 1 99  ? 20.829  -7.653  29.447 1.00 13.90  ? 99  HIS   B CB  1 
ATOM   725  C CG  . HIS   A 1 99  ? 21.798  -6.809  30.210 1.00 12.88  ? 99  HIS   B CG  1 
ATOM   726  N ND1 . HIS   A 1 99  ? 22.989  -7.300  30.699 1.00 12.03  ? 99  HIS   B ND1 1 
ATOM   727  C CD2 . HIS   A 1 99  ? 21.713  -5.523  30.635 1.00 14.66  ? 99  HIS   B CD2 1 
ATOM   728  C CE1 . HIS   A 1 99  ? 23.616  -6.344  31.367 1.00 14.32  ? 99  HIS   B CE1 1 
ATOM   729  N NE2 . HIS   A 1 99  ? 22.863  -5.255  31.340 1.00 16.87  ? 99  HIS   B NE2 1 
ATOM   730  N N   . LEU   A 1 100 ? 19.768  -7.503  32.599 1.00 13.04  ? 100 LEU   B N   1 
ATOM   731  C CA  . LEU   A 1 100 ? 19.214  -6.629  33.642 1.00 11.14  ? 100 LEU   B CA  1 
ATOM   732  C C   . LEU   A 1 100 ? 20.234  -5.556  34.042 1.00 13.78  ? 100 LEU   B C   1 
ATOM   733  O O   . LEU   A 1 100 ? 21.354  -5.883  34.445 1.00 11.59  ? 100 LEU   B O   1 
ATOM   734  C CB  . LEU   A 1 100 ? 18.829  -7.450  34.870 1.00 11.48  ? 100 LEU   B CB  1 
ATOM   735  C CG  . LEU   A 1 100 ? 17.744  -8.522  34.734 1.00 15.56  ? 100 LEU   B CG  1 
ATOM   736  C CD1 . LEU   A 1 100 ? 17.559  -9.127  36.133 1.00 10.98  ? 100 LEU   B CD1 1 
ATOM   737  C CD2 . LEU   A 1 100 ? 16.415  -7.954  34.215 1.00 11.32  ? 100 LEU   B CD2 1 
ATOM   738  N N   . ASP   A 1 101 ? 19.844  -4.276  33.949 1.00 12.36  ? 101 ASP   B N   1 
ATOM   739  C CA  . ASP   A 1 101 ? 20.595  -3.170  34.550 1.00 12.45  ? 101 ASP   B CA  1 
ATOM   740  C C   . ASP   A 1 101 ? 19.885  -2.796  35.847 1.00 13.55  ? 101 ASP   B C   1 
ATOM   741  O O   . ASP   A 1 101 ? 18.728  -2.350  35.824 1.00 15.52  ? 101 ASP   B O   1 
ATOM   742  C CB  . ASP   A 1 101 ? 20.675  -1.964  33.607 1.00 12.62  ? 101 ASP   B CB  1 
ATOM   743  C CG  . ASP   A 1 101 ? 21.500  -2.260  32.351 1.00 23.16  ? 101 ASP   B CG  1 
ATOM   744  O OD1 . ASP   A 1 101 ? 22.648  -2.750  32.486 1.00 17.30  ? 101 ASP   B OD1 1 
ATOM   745  O OD2 . ASP   A 1 101 ? 20.988  -2.052  31.225 1.00 25.12  ? 101 ASP   B OD2 1 
ATOM   746  N N   . VAL   A 1 102 ? 20.542  -3.014  36.975 1.00 11.48  ? 102 VAL   B N   1 
ATOM   747  C CA  . VAL   A 1 102 ? 19.950  -2.731  38.276 1.00 15.75  ? 102 VAL   B CA  1 
ATOM   748  C C   . VAL   A 1 102 ? 20.667  -1.543  38.899 1.00 19.38  ? 102 VAL   B C   1 
ATOM   749  O O   . VAL   A 1 102 ? 21.895  -1.573  39.077 1.00 15.56  ? 102 VAL   B O   1 
ATOM   750  C CB  . VAL   A 1 102 ? 20.022  -3.948  39.207 1.00 13.19  ? 102 VAL   B CB  1 
ATOM   751  C CG1 . VAL   A 1 102 ? 19.312  -3.628  40.515 1.00 12.12  ? 102 VAL   B CG1 1 
ATOM   752  C CG2 . VAL   A 1 102 ? 19.411  -5.141  38.526 1.00 9.79   ? 102 VAL   B CG2 1 
ATOM   753  N N   . THR   A 1 103 ? 19.895  -0.518  39.263 1.00 17.59  ? 103 THR   B N   1 
ATOM   754  C CA  . THR   A 1 103 ? 20.408  0.726   39.830 1.00 15.22  ? 103 THR   B CA  1 
ATOM   755  C C   . THR   A 1 103 ? 19.821  0.905   41.228 1.00 16.30  ? 103 THR   B C   1 
ATOM   756  O O   . THR   A 1 103 ? 18.596  1.005   41.379 1.00 15.47  ? 103 THR   B O   1 
ATOM   757  C CB  . THR   A 1 103 ? 20.049  1.922   38.939 1.00 18.61  ? 103 THR   B CB  1 
ATOM   758  O OG1 . THR   A 1 103 ? 20.560  1.731   37.608 1.00 17.57  ? 103 THR   B OG1 1 
ATOM   759  C CG2 . THR   A 1 103 ? 20.649  3.195   39.508 1.00 19.39  ? 103 THR   B CG2 1 
ATOM   760  N N   . LEU   A 1 104 ? 20.685  0.938   42.248 1.00 12.77  ? 104 LEU   B N   1 
ATOM   761  C CA  . LEU   A 1 104 ? 20.287  1.177   43.633 1.00 11.14  ? 104 LEU   B CA  1 
ATOM   762  C C   . LEU   A 1 104 ? 20.793  2.557   44.053 1.00 21.08  ? 104 LEU   B C   1 
ATOM   763  O O   . LEU   A 1 104 ? 21.957  2.906   43.806 1.00 16.87  ? 104 LEU   B O   1 
ATOM   764  C CB  . LEU   A 1 104 ? 20.846  0.097   44.576 1.00 10.33  ? 104 LEU   B CB  1 
ATOM   765  C CG  . LEU   A 1 104 ? 20.573  -1.386  44.246 1.00 11.41  ? 104 LEU   B CG  1 
ATOM   766  C CD1 . LEU   A 1 104 ? 20.692  -2.288  45.467 1.00 14.31  ? 104 LEU   B CD1 1 
ATOM   767  C CD2 . LEU   A 1 104 ? 19.196  -1.570  43.624 1.00 18.16  ? 104 LEU   B CD2 1 
ATOM   768  N N   . SER   A 1 105 ? 19.914  3.353   44.645 1.00 17.15  ? 105 SER   B N   1 
ATOM   769  C CA  . SER   A 1 105 ? 20.272  4.675   45.130 1.00 12.30  ? 105 SER   B CA  1 
ATOM   770  C C   . SER   A 1 105 ? 20.681  4.584   46.590 1.00 10.73  ? 105 SER   B C   1 
ATOM   771  O O   . SER   A 1 105 ? 19.968  4.009   47.406 1.00 14.49  ? 105 SER   B O   1 
ATOM   772  C CB  . SER   A 1 105 ? 19.092  5.643   44.967 1.00 16.06  ? 105 SER   B CB  1 
ATOM   773  O OG  . SER   A 1 105 ? 18.634  5.608   43.627 1.00 24.00  ? 105 SER   B OG  1 
ATOM   774  N N   . GLY   A 1 106 ? 21.815  5.171   46.921 1.00 13.54  ? 106 GLY   B N   1 
ATOM   775  C CA  . GLY   A 1 106 ? 22.159  5.354   48.308 1.00 13.34  ? 106 GLY   B CA  1 
ATOM   776  C C   . GLY   A 1 106 ? 22.823  4.162   48.970 1.00 14.44  ? 106 GLY   B C   1 
ATOM   777  O O   . GLY   A 1 106 ? 22.866  4.104   50.210 1.00 14.42  ? 106 GLY   B O   1 
ATOM   778  N N   . ILE   A 1 107 ? 23.368  3.205   48.211 1.00 13.47  ? 107 ILE   B N   1 
ATOM   779  C CA  . ILE   A 1 107 ? 24.113  2.159   48.889 1.00 13.02  ? 107 ILE   B CA  1 
ATOM   780  C C   . ILE   A 1 107 ? 25.442  2.017   48.151 1.00 12.49  ? 107 ILE   B C   1 
ATOM   781  O O   . ILE   A 1 107 ? 25.596  2.446   46.999 1.00 13.33  ? 107 ILE   B O   1 
ATOM   782  C CB  . ILE   A 1 107 ? 23.416  0.781   48.949 1.00 28.42  ? 107 ILE   B CB  1 
ATOM   783  C CG1 . ILE   A 1 107 ? 23.418  0.059   47.679 1.00 18.24  ? 107 ILE   B CG1 1 
ATOM   784  C CG2 . ILE   A 1 107 ? 21.860  0.932   49.189 1.00 15.86  ? 107 ILE   B CG2 1 
ATOM   785  C CD1 . ILE   A 1 107 ? 23.040  -1.343  48.046 1.00 32.10  ? 107 ILE   B CD1 1 
ATOM   786  N N   . SER   A 1 108 ? 26.398  1.391   48.825 1.00 13.18  ? 108 SER   B N   1 
ATOM   787  C CA  . SER   A 1 108 ? 27.742  1.273   48.291 1.00 12.96  ? 108 SER   B CA  1 
ATOM   788  C C   . SER   A 1 108 ? 27.797  0.216   47.186 1.00 14.86  ? 108 SER   B C   1 
ATOM   789  O O   . SER   A 1 108 ? 26.926  -0.660  47.074 1.00 10.55  ? 108 SER   B O   1 
ATOM   790  C CB  . SER   A 1 108 ? 28.716  0.945   49.424 1.00 13.75  ? 108 SER   B CB  1 
ATOM   791  O OG  . SER   A 1 108 ? 28.670  -0.441  49.740 1.00 15.84  ? 108 SER   B OG  1 
ATOM   792  N N   . GLN   A 1 109 ? 28.827  0.313   46.350 1.00 12.60  ? 109 GLN   B N   1 
ATOM   793  C CA  . GLN   A 1 109 ? 28.854  -0.517  45.150 1.00 14.57  ? 109 GLN   B CA  1 
ATOM   794  C C   . GLN   A 1 109 ? 28.979  -1.996  45.523 1.00 11.71  ? 109 GLN   B C   1 
ATOM   795  O O   . GLN   A 1 109 ? 28.240  -2.848  44.997 1.00 11.79  ? 109 GLN   B O   1 
ATOM   796  C CB  . GLN   A 1 109 ? 29.989  -0.057  44.232 1.00 12.66  ? 109 GLN   B CB  1 
ATOM   797  C CG  . GLN   A 1 109 ? 30.063  -0.757  42.863 1.00 15.61  ? 109 GLN   B CG  1 
ATOM   798  C CD  . GLN   A 1 109 ? 28.861  -0.511  41.946 1.00 19.26  ? 109 GLN   B CD  1 
ATOM   799  O OE1 . GLN   A 1 109 ? 28.329  0.597   41.864 1.00 16.41  ? 109 GLN   B OE1 1 
ATOM   800  N NE2 . GLN   A 1 109 ? 28.420  -1.571  41.257 1.00 16.58  ? 109 GLN   B NE2 1 
ATOM   801  N N   . ALA   A 1 110 ? 29.856  -2.318  46.481 1.00 12.36  ? 110 ALA   B N   1 
ATOM   802  C CA  . ALA   A 1 110 ? 30.020  -3.732  46.842 1.00 18.50  ? 110 ALA   B CA  1 
ATOM   803  C C   . ALA   A 1 110 ? 28.752  -4.284  47.503 1.00 18.44  ? 110 ALA   B C   1 
ATOM   804  O O   . ALA   A 1 110 ? 28.341  -5.430  47.241 1.00 15.36  ? 110 ALA   B O   1 
ATOM   805  C CB  . ALA   A 1 110 ? 31.229  -3.916  47.759 1.00 11.41  ? 110 ALA   B CB  1 
ATOM   806  N N   . ASP   A 1 111 ? 28.113  -3.482  48.364 1.00 14.23  ? 111 ASP   B N   1 
ATOM   807  C CA  . ASP   A 1 111 ? 26.868  -3.931  48.987 1.00 15.02  ? 111 ASP   B CA  1 
ATOM   808  C C   . ASP   A 1 111 ? 25.778  -4.159  47.945 1.00 14.10  ? 111 ASP   B C   1 
ATOM   809  O O   . ASP   A 1 111 ? 25.056  -5.160  48.002 1.00 14.41  ? 111 ASP   B O   1 
ATOM   810  C CB  . ASP   A 1 111 ? 26.411  -2.933  50.047 1.00 19.38  ? 111 ASP   B CB  1 
ATOM   811  C CG  . ASP   A 1 111 ? 27.284  -2.975  51.284 1.00 23.16  ? 111 ASP   B CG  1 
ATOM   812  O OD1 . ASP   A 1 111 ? 28.186  -3.839  51.360 1.00 27.00  ? 111 ASP   B OD1 1 
ATOM   813  O OD2 . ASP   A 1 111 ? 27.087  -2.158  52.194 1.00 25.03  ? 111 ASP   B OD2 1 
ATOM   814  N N   . ALA   A 1 112 ? 25.653  -3.243  46.980 1.00 13.36  ? 112 ALA   B N   1 
ATOM   815  C CA  . ALA   A 1 112 ? 24.677  -3.391  45.909 1.00 11.82  ? 112 ALA   B CA  1 
ATOM   816  C C   . ALA   A 1 112 ? 24.919  -4.662  45.100 1.00 11.22  ? 112 ALA   B C   1 
ATOM   817  O O   . ALA   A 1 112 ? 23.978  -5.386  44.758 1.00 14.72  ? 112 ALA   B O   1 
ATOM   818  C CB  . ALA   A 1 112 ? 24.717  -2.155  45.010 1.00 9.65   ? 112 ALA   B CB  1 
ATOM   819  N N   . GLU   A 1 113 ? 26.179  -4.971  44.811 1.00 11.64  ? 113 GLU   B N   1 
ATOM   820  C CA  . GLU   A 1 113 ? 26.480  -6.202  44.081 1.00 17.26  ? 113 GLU   B CA  1 
ATOM   821  C C   . GLU   A 1 113 ? 26.094  -7.447  44.880 1.00 13.62  ? 113 GLU   B C   1 
ATOM   822  O O   . GLU   A 1 113 ? 25.532  -8.395  44.321 1.00 13.43  ? 113 GLU   B O   1 
ATOM   823  C CB  . GLU   A 1 113 ? 27.963  -6.228  43.704 1.00 15.68  ? 113 GLU   B CB  1 
ATOM   824  C CG  . GLU   A 1 113 ? 28.253  -5.363  42.484 1.00 13.69  ? 113 GLU   B CG  1 
ATOM   825  C CD  . GLU   A 1 113 ? 29.706  -4.992  42.352 1.00 27.65  ? 113 GLU   B CD  1 
ATOM   826  O OE1 . GLU   A 1 113 ? 30.537  -5.592  43.092 1.00 34.54  ? 113 GLU   B OE1 1 
ATOM   827  O OE2 . GLU   A 1 113 ? 30.031  -4.113  41.505 1.00 28.82  ? 113 GLU   B OE2 1 
ATOM   828  N N   . LYS   A 1 114 ? 26.391  -7.464  46.185 1.00 13.47  ? 114 LYS   B N   1 
ATOM   829  C CA  . LYS   A 1 114 ? 25.948  -8.577  47.029 1.00 11.09  ? 114 LYS   B CA  1 
ATOM   830  C C   . LYS   A 1 114 ? 24.414  -8.692  47.091 1.00 14.27  ? 114 LYS   B C   1 
ATOM   831  O O   . LYS   A 1 114 ? 23.857  -9.794  46.989 1.00 12.41  ? 114 LYS   B O   1 
ATOM   832  C CB  . LYS   A 1 114 ? 26.529  -8.442  48.442 1.00 13.35  ? 114 LYS   B CB  1 
ATOM   833  C CG  . LYS   A 1 114 ? 26.048  -9.528  49.415 1.00 17.11  ? 114 LYS   B CG  1 
ATOM   834  C CD  . LYS   A 1 114 ? 26.662  -9.345  50.782 1.00 32.27  ? 114 LYS   B CD  1 
ATOM   835  C CE  . LYS   A 1 114 ? 26.190  -10.468 51.809 1.00 40.35  ? 114 LYS   B CE  1 
ATOM   836  N NZ  . LYS   A 1 114 ? 24.706  -10.226 52.240 1.00 37.10  ? 114 LYS   B NZ  1 
ATOM   837  N N   . ILE   A 1 115 ? 23.714  -7.576  47.253 1.00 11.65  ? 115 ILE   B N   1 
ATOM   838  C CA  . ILE   A 1 115 ? 22.253  -7.607  47.252 1.00 11.40  ? 115 ILE   B CA  1 
ATOM   839  C C   . ILE   A 1 115 ? 21.715  -8.192  45.946 1.00 10.21  ? 115 ILE   B C   1 
ATOM   840  O O   . ILE   A 1 115 ? 20.824  -9.033  45.966 1.00 11.28  ? 115 ILE   B O   1 
ATOM   841  C CB  . ILE   A 1 115 ? 21.691  -6.204  47.522 1.00 10.75  ? 115 ILE   B CB  1 
ATOM   842  C CG1 . ILE   A 1 115 ? 21.944  -5.879  49.002 1.00 12.38  ? 115 ILE   B CG1 1 
ATOM   843  C CG2 . ILE   A 1 115 ? 20.213  -6.137  47.186 1.00 13.73  ? 115 ILE   B CG2 1 
ATOM   844  C CD1 . ILE   A 1 115 ? 21.665  -4.450  49.378 1.00 14.70  ? 115 ILE   B CD1 1 
ATOM   845  N N   . VAL   A 1 116 ? 22.250  -7.766  44.799 1.00 9.26   ? 116 VAL   B N   1 
ATOM   846  C CA  . VAL   A 1 116 ? 21.700  -8.224  43.518 1.00 12.58  ? 116 VAL   B CA  1 
ATOM   847  C C   . VAL   A 1 116 ? 21.977  -9.726  43.319 1.00 11.12  ? 116 VAL   B C   1 
ATOM   848  O O   . VAL   A 1 116 ? 21.134  -10.481 42.808 1.00 10.59  ? 116 VAL   B O   1 
ATOM   849  C CB  . VAL   A 1 116 ? 22.262  -7.354  42.376 1.00 7.73   ? 116 VAL   B CB  1 
ATOM   850  C CG1 . VAL   A 1 116 ? 21.965  -7.956  41.011 1.00 11.20  ? 116 VAL   B CG1 1 
ATOM   851  C CG2 . VAL   A 1 116 ? 21.677  -5.917  42.467 1.00 10.54  ? 116 VAL   B CG2 1 
ATOM   852  N N   . GLU   A 1 117 ? 23.152  -10.184 43.753 1.00 13.07  ? 117 GLU   B N   1 
ATOM   853  C CA  . GLU   A 1 117 ? 23.462  -11.611 43.656 1.00 16.70  ? 117 GLU   B CA  1 
ATOM   854  C C   . GLU   A 1 117 ? 22.507  -12.429 44.525 1.00 15.32  ? 117 GLU   B C   1 
ATOM   855  O O   . GLU   A 1 117 ? 21.970  -13.448 44.086 1.00 13.26  ? 117 GLU   B O   1 
ATOM   856  C CB  . GLU   A 1 117 ? 24.930  -11.838 44.041 1.00 14.33  ? 117 GLU   B CB  1 
ATOM   857  C CG  . GLU   A 1 117 ? 25.361  -13.300 44.121 1.00 26.80  ? 117 GLU   B CG  1 
ATOM   858  C CD  . GLU   A 1 117 ? 26.812  -13.452 44.581 1.00 33.67  ? 117 GLU   B CD  1 
ATOM   859  O OE1 . GLU   A 1 117 ? 27.625  -14.035 43.830 1.00 47.69  ? 117 GLU   B OE1 1 
ATOM   860  O OE2 . GLU   A 1 117 ? 27.140  -12.985 45.699 1.00 45.68  ? 117 GLU   B OE2 1 
ATOM   861  N N   . GLN   A 1 118 ? 22.229  -11.959 45.740 1.00 12.79  ? 118 GLN   B N   1 
ATOM   862  C CA  . GLN   A 1 118 ? 21.233  -12.638 46.574 1.00 18.10  ? 118 GLN   B CA  1 
ATOM   863  C C   . GLN   A 1 118 ? 19.830  -12.601 45.961 1.00 15.33  ? 118 GLN   B C   1 
ATOM   864  O O   . GLN   A 1 118 ? 19.068  -13.569 46.103 1.00 14.39  ? 118 GLN   B O   1 
ATOM   865  C CB  . GLN   A 1 118 ? 21.158  -12.014 47.973 1.00 15.11  ? 118 GLN   B CB  1 
ATOM   866  C CG  . GLN   A 1 118 ? 22.315  -12.261 48.914 1.00 22.14  ? 118 GLN   B CG  1 
ATOM   867  C CD  . GLN   A 1 118 ? 22.266  -11.277 50.111 1.00 26.60  ? 118 GLN   B CD  1 
ATOM   868  O OE1 . GLN   A 1 118 ? 22.753  -10.148 50.027 1.00 27.42  ? 118 GLN   B OE1 1 
ATOM   869  N NE2 . GLN   A 1 118 ? 21.634  -11.694 51.197 1.00 31.63  ? 118 GLN   B NE2 1 
ATOM   870  N N   A THR   A 1 119 ? 19.452  -11.501 45.305 0.50 13.36  ? 119 THR   B N   1 
ATOM   871  N N   B THR   A 1 119 ? 19.459  -11.500 45.308 0.50 13.32  ? 119 THR   B N   1 
ATOM   872  C CA  A THR   A 1 119 ? 18.071  -11.470 44.824 0.50 13.41  ? 119 THR   B CA  1 
ATOM   873  C CA  B THR   A 1 119 ? 18.090  -11.420 44.811 0.50 13.70  ? 119 THR   B CA  1 
ATOM   874  C C   A THR   A 1 119 ? 17.861  -12.414 43.652 0.50 14.61  ? 119 THR   B C   1 
ATOM   875  C C   B THR   A 1 119 ? 17.858  -12.357 43.630 0.50 13.96  ? 119 THR   B C   1 
ATOM   876  O O   A THR   A 1 119 ? 16.732  -12.865 43.423 0.50 11.76  ? 119 THR   B O   1 
ATOM   877  O O   B THR   A 1 119 ? 16.720  -12.794 43.410 0.50 11.14  ? 119 THR   B O   1 
ATOM   878  C CB  A THR   A 1 119 ? 17.590  -10.066 44.428 0.50 14.47  ? 119 THR   B CB  1 
ATOM   879  C CB  B THR   A 1 119 ? 17.714  -9.960  44.501 0.50 14.39  ? 119 THR   B CB  1 
ATOM   880  O OG1 A THR   A 1 119 ? 17.880  -9.809  43.058 0.50 20.58  ? 119 THR   B OG1 1 
ATOM   881  O OG1 B THR   A 1 119 ? 16.362  -9.892  44.030 0.50 20.58  ? 119 THR   B OG1 1 
ATOM   882  C CG2 A THR   A 1 119 ? 18.132  -8.980  45.301 0.50 8.92   ? 119 THR   B CG2 1 
ATOM   883  C CG2 B THR   A 1 119 ? 18.568  -9.352  43.510 0.50 15.50  ? 119 THR   B CG2 1 
ATOM   884  N N   . HIS   A 1 120 ? 18.912  -12.739 42.898 1.00 15.75  ? 120 HIS   B N   1 
ATOM   885  C CA  . HIS   A 1 120 ? 18.692  -13.770 41.862 1.00 14.31  ? 120 HIS   B CA  1 
ATOM   886  C C   . HIS   A 1 120 ? 18.235  -15.120 42.446 1.00 12.20  ? 120 HIS   B C   1 
ATOM   887  O O   . HIS   A 1 120 ? 17.636  -15.916 41.721 1.00 12.24  ? 120 HIS   B O   1 
ATOM   888  C CB  . HIS   A 1 120 ? 19.916  -14.018 40.964 1.00 16.06  ? 120 HIS   B CB  1 
ATOM   889  C CG  . HIS   A 1 120 ? 20.054  -13.035 39.840 1.00 14.76  ? 120 HIS   B CG  1 
ATOM   890  N ND1 . HIS   A 1 120 ? 19.233  -13.051 38.727 1.00 14.19  ? 120 HIS   B ND1 1 
ATOM   891  C CD2 . HIS   A 1 120 ? 20.947  -12.034 39.635 1.00 14.76  ? 120 HIS   B CD2 1 
ATOM   892  C CE1 . HIS   A 1 120 ? 19.603  -12.093 37.897 1.00 13.73  ? 120 HIS   B CE1 1 
ATOM   893  N NE2 . HIS   A 1 120 ? 20.643  -11.464 38.421 1.00 14.88  ? 120 HIS   B NE2 1 
ATOM   894  N N   . GLN   A 1 121 ? 18.472  -15.384 43.742 1.00 15.17  ? 121 GLN   B N   1 
ATOM   895  C CA  . GLN   A 1 121 ? 17.984  -16.598 44.397 1.00 13.42  ? 121 GLN   B CA  1 
ATOM   896  C C   . GLN   A 1 121 ? 16.532  -16.468 44.855 1.00 17.91  ? 121 GLN   B C   1 
ATOM   897  O O   . GLN   A 1 121 ? 15.857  -17.478 45.070 1.00 13.38  ? 121 GLN   B O   1 
ATOM   898  C CB  . GLN   A 1 121 ? 18.866  -16.922 45.611 1.00 14.11  ? 121 GLN   B CB  1 
ATOM   899  C CG  . GLN   A 1 121 ? 20.199  -17.563 45.259 1.00 16.15  ? 121 GLN   B CG  1 
ATOM   900  C CD  . GLN   A 1 121 ? 19.998  -18.942 44.657 1.00 27.09  ? 121 GLN   B CD  1 
ATOM   901  O OE1 . GLN   A 1 121 ? 20.191  -19.148 43.452 1.00 17.29  ? 121 GLN   B OE1 1 
ATOM   902  N NE2 . GLN   A 1 121 ? 19.543  -19.885 45.490 1.00 25.52  ? 121 GLN   B NE2 1 
ATOM   903  N N   . VAL   A 1 122 ? 16.048  -15.243 45.030 1.00 19.06  ? 122 VAL   B N   1 
ATOM   904  C CA  . VAL   A 1 122 ? 14.702  -14.978 45.559 1.00 19.72  ? 122 VAL   B CA  1 
ATOM   905  C C   . VAL   A 1 122 ? 13.669  -14.862 44.443 1.00 17.92  ? 122 VAL   B C   1 
ATOM   906  O O   . VAL   A 1 122 ? 12.579  -15.443 44.542 1.00 13.91  ? 122 VAL   B O   1 
ATOM   907  C CB  . VAL   A 1 122 ? 14.732  -13.693 46.428 1.00 15.55  ? 122 VAL   B CB  1 
ATOM   908  C CG1 . VAL   A 1 122 ? 13.329  -13.320 46.939 1.00 18.32  ? 122 VAL   B CG1 1 
ATOM   909  C CG2 . VAL   A 1 122 ? 15.694  -13.849 47.588 1.00 16.03  ? 122 VAL   B CG2 1 
ATOM   910  N N   . CYS   A 1 123 ? 13.999  -14.077 43.408 1.00 8.96   ? 123 CYS   B N   1 
ATOM   911  C CA  . CYS   A 1 123 ? 13.038  -13.682 42.386 1.00 11.43  ? 123 CYS   B CA  1 
ATOM   912  C C   . CYS   A 1 123 ? 12.545  -14.905 41.620 1.00 11.62  ? 123 CYS   B C   1 
ATOM   913  O O   . CYS   A 1 123 ? 13.367  -15.704 41.150 1.00 10.80  ? 123 CYS   B O   1 
ATOM   914  C CB  . CYS   A 1 123 ? 13.685  -12.680 41.431 1.00 11.43  ? 123 CYS   B CB  1 
ATOM   915  S SG  . CYS   A 1 123 ? 12.737  -12.253 39.961 1.00 15.37  ? 123 CYS   B SG  1 
ATOM   916  N N   . PRO   A 1 124 ? 11.229  -15.108 41.504 1.00 8.88   ? 124 PRO   B N   1 
ATOM   917  C CA  . PRO   A 1 124 ? 10.747  -16.346 40.866 1.00 9.62   ? 124 PRO   B CA  1 
ATOM   918  C C   . PRO   A 1 124 ? 10.961  -16.378 39.352 1.00 9.05   ? 124 PRO   B C   1 
ATOM   919  O O   . PRO   A 1 124 ? 11.001  -17.467 38.776 1.00 12.98  ? 124 PRO   B O   1 
ATOM   920  C CB  . PRO   A 1 124 ? 9.247   -16.391 41.224 1.00 11.69  ? 124 PRO   B CB  1 
ATOM   921  C CG  . PRO   A 1 124 ? 8.848   -14.974 41.585 1.00 10.54  ? 124 PRO   B CG  1 
ATOM   922  C CD  . PRO   A 1 124 ? 10.136  -14.278 42.058 1.00 11.74  ? 124 PRO   B CD  1 
ATOM   923  N N   . TYR   A 1 125 ? 11.094  -15.235 38.674 1.00 11.83  ? 125 TYR   B N   1 
ATOM   924  C CA  . TYR   A 1 125 ? 11.457  -15.266 37.254 1.00 11.51  ? 125 TYR   B CA  1 
ATOM   925  C C   . TYR   A 1 125 ? 12.887  -15.760 37.044 1.00 9.77   ? 125 TYR   B C   1 
ATOM   926  O O   . TYR   A 1 125 ? 13.154  -16.526 36.109 1.00 11.15  ? 125 TYR   B O   1 
ATOM   927  C CB  . TYR   A 1 125 ? 11.351  -13.887 36.652 1.00 13.88  ? 125 TYR   B CB  1 
ATOM   928  C CG  . TYR   A 1 125 ? 9.989   -13.360 36.398 1.00 16.85  ? 125 TYR   B CG  1 
ATOM   929  C CD1 . TYR   A 1 125 ? 9.082   -13.147 37.426 1.00 18.67  ? 125 TYR   B CD1 1 
ATOM   930  C CD2 . TYR   A 1 125 ? 9.654   -12.962 35.111 1.00 29.10  ? 125 TYR   B CD2 1 
ATOM   931  C CE1 . TYR   A 1 125 ? 7.835   -12.605 37.147 1.00 28.48  ? 125 TYR   B CE1 1 
ATOM   932  C CE2 . TYR   A 1 125 ? 8.450   -12.405 34.817 1.00 28.83  ? 125 TYR   B CE2 1 
ATOM   933  C CZ  . TYR   A 1 125 ? 7.529   -12.230 35.821 1.00 35.81  ? 125 TYR   B CZ  1 
ATOM   934  O OH  . TYR   A 1 125 ? 6.319   -11.663 35.448 1.00 33.31  ? 125 TYR   B OH  1 
ATOM   935  N N   . SER   A 1 126 ? 13.827  -15.283 37.866 1.00 11.13  ? 126 SER   B N   1 
ATOM   936  C CA  . SER   A 1 126 ? 15.194  -15.806 37.802 1.00 12.12  ? 126 SER   B CA  1 
ATOM   937  C C   . SER   A 1 126 ? 15.201  -17.309 38.050 1.00 12.99  ? 126 SER   B C   1 
ATOM   938  O O   . SER   A 1 126 ? 15.827  -18.065 37.305 1.00 13.45  ? 126 SER   B O   1 
ATOM   939  C CB  . SER   A 1 126 ? 16.100  -15.105 38.814 1.00 10.96  ? 126 SER   B CB  1 
ATOM   940  O OG  . SER   A 1 126 ? 16.210  -13.725 38.523 1.00 13.69  ? 126 SER   B OG  1 
ATOM   941  N N   . ASN   A 1 127 ? 14.507  -17.757 39.101 1.00 12.69  ? 127 ASN   B N   1 
ATOM   942  C CA  . ASN   A 1 127 ? 14.411  -19.198 39.352 1.00 13.82  ? 127 ASN   B CA  1 
ATOM   943  C C   . ASN   A 1 127 ? 13.736  -19.915 38.205 1.00 10.94  ? 127 ASN   B C   1 
ATOM   944  O O   . ASN   A 1 127 ? 14.058  -21.076 37.932 1.00 14.53  ? 127 ASN   B O   1 
ATOM   945  C CB  . ASN   A 1 127 ? 13.659  -19.474 40.658 1.00 11.61  ? 127 ASN   B CB  1 
ATOM   946  C CG  . ASN   A 1 127 ? 14.438  -19.036 41.869 1.00 20.44  ? 127 ASN   B CG  1 
ATOM   947  O OD1 . ASN   A 1 127 ? 15.689  -19.137 41.888 1.00 15.18  ? 127 ASN   B OD1 1 
ATOM   948  N ND2 . ASN   A 1 127 ? 13.733  -18.475 42.870 1.00 14.89  ? 127 ASN   B ND2 1 
ATOM   949  N N   . ALA   A 1 128 ? 12.817  -19.236 37.501 1.00 10.27  ? 128 ALA   B N   1 
ATOM   950  C CA  . ALA   A 1 128 ? 12.057  -19.901 36.441 1.00 12.24  ? 128 ALA   B CA  1 
ATOM   951  C C   . ALA   A 1 128 ? 12.935  -20.203 35.232 1.00 10.51  ? 128 ALA   B C   1 
ATOM   952  O O   . ALA   A 1 128 ? 12.755  -21.231 34.555 1.00 8.28   ? 128 ALA   B O   1 
ATOM   953  C CB  . ALA   A 1 128 ? 10.864  -19.030 36.009 1.00 9.75   ? 128 ALA   B CB  1 
ATOM   954  N N   . ILE   A 1 129 ? 13.848  -19.285 34.903 1.00 10.53  ? 129 ILE   B N   1 
ATOM   955  C CA  . ILE   A 1 129 ? 14.573  -19.390 33.633 1.00 11.57  ? 129 ILE   B CA  1 
ATOM   956  C C   . ILE   A 1 129 ? 16.029  -19.852 33.798 1.00 10.49  ? 129 ILE   B C   1 
ATOM   957  O O   . ILE   A 1 129 ? 16.776  -19.883 32.811 1.00 9.90   ? 129 ILE   B O   1 
ATOM   958  C CB  . ILE   A 1 129 ? 14.504  -18.053 32.887 1.00 9.76   ? 129 ILE   B CB  1 
ATOM   959  C CG1 . ILE   A 1 129 ? 15.278  -16.999 33.667 1.00 12.61  ? 129 ILE   B CG1 1 
ATOM   960  C CG2 . ILE   A 1 129 ? 13.062  -17.586 32.771 1.00 11.39  ? 129 ILE   B CG2 1 
ATOM   961  C CD1 . ILE   A 1 129 ? 15.130  -15.622 33.065 1.00 11.48  ? 129 ILE   B CD1 1 
ATOM   962  N N   . ARG   A 1 130 ? 16.443  -20.222 34.997 1.00 9.28   ? 130 ARG   B N   1 
ATOM   963  C CA  . ARG   A 1 130 ? 17.842  -20.561 35.230 1.00 11.00  ? 130 ARG   B CA  1 
ATOM   964  C C   . ARG   A 1 130 ? 18.270  -21.764 34.392 1.00 10.60  ? 130 ARG   B C   1 
ATOM   965  O O   . ARG   A 1 130 ? 17.568  -22.780 34.317 1.00 10.77  ? 130 ARG   B O   1 
ATOM   966  C CB  . ARG   A 1 130 ? 18.095  -20.833 36.719 1.00 10.52  ? 130 ARG   B CB  1 
ATOM   967  C CG  . ARG   A 1 130 ? 19.594  -21.014 37.047 1.00 13.63  ? 130 ARG   B CG  1 
ATOM   968  C CD  . ARG   A 1 130 ? 19.860  -21.117 38.548 1.00 16.29  ? 130 ARG   B CD  1 
ATOM   969  N NE  . ARG   A 1 130 ? 19.575  -19.838 39.196 1.00 14.11  ? 130 ARG   B NE  1 
ATOM   970  C CZ  . ARG   A 1 130 ? 18.480  -19.593 39.907 1.00 17.78  ? 130 ARG   B CZ  1 
ATOM   971  N NH1 . ARG   A 1 130 ? 17.569  -20.554 40.088 1.00 13.41  ? 130 ARG   B NH1 1 
ATOM   972  N NH2 . ARG   A 1 130 ? 18.304  -18.384 40.448 1.00 16.76  ? 130 ARG   B NH2 1 
ATOM   973  N N   . GLY   A 1 131 ? 19.428  -21.635 33.739 1.00 14.05  ? 131 GLY   B N   1 
ATOM   974  C CA  . GLY   A 1 131 ? 19.953  -22.679 32.869 1.00 14.14  ? 131 GLY   B CA  1 
ATOM   975  C C   . GLY   A 1 131 ? 19.410  -22.681 31.455 1.00 17.96  ? 131 GLY   B C   1 
ATOM   976  O O   . GLY   A 1 131 ? 20.028  -23.282 30.566 1.00 16.45  ? 131 GLY   B O   1 
ATOM   977  N N   . ASN   A 1 132 ? 18.262  -22.054 31.206 1.00 17.68  ? 132 ASN   B N   1 
ATOM   978  C CA  . ASN   A 1 132 ? 17.756  -21.959 29.848 1.00 13.97  ? 132 ASN   B CA  1 
ATOM   979  C C   . ASN   A 1 132 ? 18.092  -20.614 29.220 1.00 14.99  ? 132 ASN   B C   1 
ATOM   980  O O   . ASN   A 1 132 ? 18.575  -20.549 28.097 1.00 18.86  ? 132 ASN   B O   1 
ATOM   981  C CB  . ASN   A 1 132 ? 16.237  -22.189 29.827 1.00 12.91  ? 132 ASN   B CB  1 
ATOM   982  C CG  . ASN   A 1 132 ? 15.848  -23.509 30.455 1.00 18.73  ? 132 ASN   B CG  1 
ATOM   983  O OD1 . ASN   A 1 132 ? 16.354  -24.567 30.078 1.00 19.47  ? 132 ASN   B OD1 1 
ATOM   984  N ND2 . ASN   A 1 132 ? 14.957  -23.451 31.443 1.00 19.33  ? 132 ASN   B ND2 1 
ATOM   985  N N   . ILE   A 1 133 ? 17.801  -19.530 29.908 1.00 22.17  ? 133 ILE   B N   1 
ATOM   986  C CA  . ILE   A 1 133 ? 18.283  -18.221 29.520 1.00 17.50  ? 133 ILE   B CA  1 
ATOM   987  C C   . ILE   A 1 133 ? 19.414  -17.884 30.475 1.00 20.27  ? 133 ILE   B C   1 
ATOM   988  O O   . ILE   A 1 133 ? 19.269  -18.041 31.702 1.00 18.40  ? 133 ILE   B O   1 
ATOM   989  C CB  . ILE   A 1 133 ? 17.172  -17.162 29.582 1.00 15.32  ? 133 ILE   B CB  1 
ATOM   990  C CG1 . ILE   A 1 133 ? 16.000  -17.521 28.658 1.00 21.95  ? 133 ILE   B CG1 1 
ATOM   991  C CG2 . ILE   A 1 133 ? 17.739  -15.799 29.253 1.00 11.89  ? 133 ILE   B CG2 1 
ATOM   992  C CD1 . ILE   A 1 133 ? 14.747  -16.653 28.939 1.00 20.29  ? 133 ILE   B CD1 1 
ATOM   993  N N   . GLN   A 1 134 ? 20.547  -17.452 29.915 1.00 16.59  ? 134 GLN   B N   1 
ATOM   994  C CA  . GLN   A 1 134 ? 21.714  -17.064 30.692 1.00 15.15  ? 134 GLN   B CA  1 
ATOM   995  C C   . GLN   A 1 134 ? 21.579  -15.560 30.890 1.00 17.52  ? 134 GLN   B C   1 
ATOM   996  O O   . GLN   A 1 134 ? 21.975  -14.767 30.029 1.00 18.79  ? 134 GLN   B O   1 
ATOM   997  C CB  . GLN   A 1 134 ? 23.006  -17.439 29.963 1.00 21.34  ? 134 GLN   B CB  1 
ATOM   998  C CG  . GLN   A 1 134 ? 23.297  -18.960 29.773 1.00 24.97  ? 134 GLN   B CG  1 
ATOM   999  C CD  . GLN   A 1 134 ? 23.230  -19.799 31.053 1.00 27.26  ? 134 GLN   B CD  1 
ATOM   1000 O OE1 . GLN   A 1 134 ? 23.469  -19.309 32.156 1.00 27.62  ? 134 GLN   B OE1 1 
ATOM   1001 N NE2 . GLN   A 1 134 ? 22.863  -21.066 30.901 1.00 22.43  ? 134 GLN   B NE2 1 
ATOM   1002 N N   . VAL   A 1 135 ? 20.980  -15.166 32.018 1.00 14.90  ? 135 VAL   B N   1 
ATOM   1003 C CA  . VAL   A 1 135 ? 20.748  -13.757 32.309 1.00 17.47  ? 135 VAL   B CA  1 
ATOM   1004 C C   . VAL   A 1 135 ? 22.066  -13.060 32.619 1.00 15.01  ? 135 VAL   B C   1 
ATOM   1005 O O   . VAL   A 1 135 ? 22.839  -13.503 33.474 1.00 19.12  ? 135 VAL   B O   1 
ATOM   1006 C CB  . VAL   A 1 135 ? 19.772  -13.601 33.489 1.00 22.81  ? 135 VAL   B CB  1 
ATOM   1007 C CG1 . VAL   A 1 135 ? 19.484  -12.105 33.748 1.00 13.89  ? 135 VAL   B CG1 1 
ATOM   1008 C CG2 . VAL   A 1 135 ? 18.468  -14.324 33.198 1.00 13.74  ? 135 VAL   B CG2 1 
ATOM   1009 N N   . SER   A 1 136 ? 22.320  -11.942 31.956 1.00 16.45  ? 136 SER   B N   1 
ATOM   1010 C CA  . SER   A 1 136 ? 23.406  -11.058 32.357 1.00 11.84  ? 136 SER   B CA  1 
ATOM   1011 C C   . SER   A 1 136 ? 22.846  -9.886  33.167 1.00 13.86  ? 136 SER   B C   1 
ATOM   1012 O O   . SER   A 1 136 ? 21.730  -9.428  32.933 1.00 16.36  ? 136 SER   B O   1 
ATOM   1013 C CB  . SER   A 1 136 ? 24.170  -10.523 31.136 1.00 15.71  ? 136 SER   B CB  1 
ATOM   1014 O OG  . SER   A 1 136 ? 23.284  -9.780  30.300 1.00 18.88  ? 136 SER   B OG  1 
ATOM   1015 N N   . THR   A 1 137 ? 23.661  -9.364  34.086 1.00 14.70  ? 137 THR   B N   1 
ATOM   1016 C CA  . THR   A 1 137 ? 23.238  -8.350  35.046 1.00 14.40  ? 137 THR   B CA  1 
ATOM   1017 C C   . THR   A 1 137 ? 24.368  -7.344  35.246 1.00 15.69  ? 137 THR   B C   1 
ATOM   1018 O O   . THR   A 1 137 ? 25.522  -7.741  35.443 1.00 14.73  ? 137 THR   B O   1 
ATOM   1019 C CB  . THR   A 1 137 ? 22.880  -8.996  36.407 1.00 17.29  ? 137 THR   B CB  1 
ATOM   1020 O OG1 . THR   A 1 137 ? 21.851  -9.991  36.232 1.00 14.61  ? 137 THR   B OG1 1 
ATOM   1021 C CG2 . THR   A 1 137 ? 22.423  -7.941  37.413 1.00 13.86  ? 137 THR   B CG2 1 
ATOM   1022 N N   . THR   A 1 138 ? 24.044  -6.054  35.200 1.00 13.77  ? 138 THR   B N   1 
ATOM   1023 C CA  . THR   A 1 138 ? 24.977  -4.996  35.578 1.00 12.66  ? 138 THR   B CA  1 
ATOM   1024 C C   . THR   A 1 138 ? 24.363  -4.151  36.693 1.00 15.87  ? 138 THR   B C   1 
ATOM   1025 O O   . THR   A 1 138 ? 23.182  -3.801  36.632 1.00 14.07  ? 138 THR   B O   1 
ATOM   1026 C CB  . THR   A 1 138 ? 25.331  -4.105  34.376 1.00 15.91  ? 138 THR   B CB  1 
ATOM   1027 O OG1 . THR   A 1 138 ? 25.803  -4.915  33.292 1.00 20.38  ? 138 THR   B OG1 1 
ATOM   1028 C CG2 . THR   A 1 138 ? 26.403  -3.077  34.751 1.00 13.96  ? 138 THR   B CG2 1 
ATOM   1029 N N   . VAL   A 1 139 ? 25.172  -3.823  37.699 1.00 14.71  ? 139 VAL   B N   1 
ATOM   1030 C CA  . VAL   A 1 139 ? 24.718  -3.185  38.929 1.00 12.96  ? 139 VAL   B CA  1 
ATOM   1031 C C   . VAL   A 1 139 ? 25.328  -1.790  39.007 1.00 16.15  ? 139 VAL   B C   1 
ATOM   1032 O O   . VAL   A 1 139 ? 26.557  -1.640  38.957 1.00 10.31  ? 139 VAL   B O   1 
ATOM   1033 C CB  . VAL   A 1 139 ? 25.121  -3.993  40.169 1.00 12.75  ? 139 VAL   B CB  1 
ATOM   1034 C CG1 . VAL   A 1 139 ? 24.728  -3.256  41.448 1.00 11.86  ? 139 VAL   B CG1 1 
ATOM   1035 C CG2 . VAL   A 1 139 ? 24.585  -5.426  40.097 1.00 11.82  ? 139 VAL   B CG2 1 
ATOM   1036 N N   . TYR   A 1 140 ? 24.473  -0.787  39.166 1.00 13.66  ? 140 TYR   B N   1 
ATOM   1037 C CA  . TYR   A 1 140 ? 24.853  0.605   39.298 1.00 16.02  ? 140 TYR   B CA  1 
ATOM   1038 C C   . TYR   A 1 140 ? 24.335  1.139   40.620 1.00 16.48  ? 140 TYR   B C   1 
ATOM   1039 O O   . TYR   A 1 140 ? 23.284  0.706   41.109 1.00 15.81  ? 140 TYR   B O   1 
ATOM   1040 C CB  . TYR   A 1 140 ? 24.263  1.448   38.169 1.00 17.26  ? 140 TYR   B CB  1 
ATOM   1041 C CG  . TYR   A 1 140 ? 24.695  1.050   36.792 1.00 22.67  ? 140 TYR   B CG  1 
ATOM   1042 C CD1 . TYR   A 1 140 ? 25.907  1.485   36.283 1.00 20.72  ? 140 TYR   B CD1 1 
ATOM   1043 C CD2 . TYR   A 1 140 ? 23.892  0.239   35.996 1.00 17.63  ? 140 TYR   B CD2 1 
ATOM   1044 C CE1 . TYR   A 1 140 ? 26.305  1.132   35.026 1.00 26.49  ? 140 TYR   B CE1 1 
ATOM   1045 C CE2 . TYR   A 1 140 ? 24.283  -0.111  34.715 1.00 22.81  ? 140 TYR   B CE2 1 
ATOM   1046 C CZ  . TYR   A 1 140 ? 25.495  0.347   34.245 1.00 25.81  ? 140 TYR   B CZ  1 
ATOM   1047 O OH  . TYR   A 1 140 ? 25.931  0.016   32.990 1.00 27.99  ? 140 TYR   B OH  1 
ATOM   1048 N N   . THR   A 1 141 ? 25.083  2.070   41.196 1.00 15.89  ? 141 THR   B N   1 
ATOM   1049 C CA  . THR   A 1 141 ? 24.662  2.852   42.351 1.00 18.77  ? 141 THR   B CA  1 
ATOM   1050 C C   . THR   A 1 141 ? 24.746  4.341   42.002 1.00 23.57  ? 141 THR   B C   1 
ATOM   1051 O O   . THR   A 1 141 ? 25.625  4.762   41.240 1.00 29.55  ? 141 THR   B O   1 
ATOM   1052 C CB  . THR   A 1 141 ? 25.518  2.534   43.585 1.00 18.45  ? 141 THR   B CB  1 
ATOM   1053 O OG1 . THR   A 1 141 ? 26.900  2.731   43.281 1.00 18.94  ? 141 THR   B OG1 1 
ATOM   1054 C CG2 . THR   A 1 141 ? 25.309  1.079   44.045 1.00 13.21  ? 141 THR   B CG2 1 
ATOM   1055 N N   . LYS   A 1 142 ? 23.838  5.146   42.560 1.00 22.59  ? 142 LYS   B N   1 
ATOM   1056 C CA  . LYS   A 1 142 ? 23.770  6.550   42.114 1.00 26.86  ? 142 LYS   B CA  1 
ATOM   1057 C C   . LYS   A 1 142 ? 23.403  7.589   43.175 1.00 27.21  ? 142 LYS   B C   1 
ATOM   1058 O O   . LYS   A 1 142 ? 22.967  7.237   44.263 1.00 28.20  ? 142 LYS   B O   1 
ATOM   1059 C CB  . LYS   A 1 142 ? 22.787  6.663   40.951 1.00 28.14  ? 142 LYS   B CB  1 
ATOM   1060 C CG  . LYS   A 1 142 ? 21.324  6.477   41.314 1.00 30.40  ? 142 LYS   B CG  1 
ATOM   1061 C CD  . LYS   A 1 142 ? 20.431  7.047   40.201 1.00 30.84  ? 142 LYS   B CD  1 
ATOM   1062 C CE  . LYS   A 1 142 ? 18.948  6.814   40.463 1.00 32.36  ? 142 LYS   B CE  1 
ATOM   1063 N NZ  . LYS   A 1 142 ? 18.153  6.851   39.190 1.00 41.60  ? 142 LYS   B NZ  1 
ATOM   1064 N N   . SER   B 1 2   ? 21.489  -14.268 15.683 1.00 53.83  ? 2   SER   A N   1 
ATOM   1065 C CA  . SER   B 1 2   ? 21.416  -12.817 15.878 1.00 60.10  ? 2   SER   A CA  1 
ATOM   1066 C C   . SER   B 1 2   ? 20.045  -12.372 16.370 1.00 49.32  ? 2   SER   A C   1 
ATOM   1067 O O   . SER   B 1 2   ? 19.037  -13.032 16.112 1.00 43.35  ? 2   SER   A O   1 
ATOM   1068 C CB  . SER   B 1 2   ? 21.754  -12.073 14.586 1.00 59.73  ? 2   SER   A CB  1 
ATOM   1069 O OG  . SER   B 1 2   ? 23.150  -11.914 14.447 1.00 72.97  ? 2   SER   A OG  1 
ATOM   1070 N N   . THR   B 1 3   ? 20.026  -11.223 17.046 1.00 50.31  ? 3   THR   A N   1 
ATOM   1071 C CA  . THR   B 1 3   ? 18.832  -10.728 17.726 1.00 42.52  ? 3   THR   A CA  1 
ATOM   1072 C C   . THR   B 1 3   ? 17.849  -10.078 16.749 1.00 37.26  ? 3   THR   A C   1 
ATOM   1073 O O   . THR   B 1 3   ? 18.152  -9.059  16.125 1.00 35.60  ? 3   THR   A O   1 
ATOM   1074 C CB  . THR   B 1 3   ? 19.246  -9.780  18.850 1.00 44.28  ? 3   THR   A CB  1 
ATOM   1075 O OG1 . THR   B 1 3   ? 18.074  -9.246  19.489 1.00 38.21  ? 3   THR   A OG1 1 
ATOM   1076 C CG2 . THR   B 1 3   ? 20.207  -8.683  18.375 1.00 48.83  ? 3   THR   A CG2 1 
ATOM   1077 N N   . LEU   B 1 4   ? 16.651  -10.666 16.637 1.00 32.34  ? 4   LEU   A N   1 
ATOM   1078 C CA  . LEU   B 1 4   ? 15.665  -10.217 15.657 1.00 33.58  ? 4   LEU   A CA  1 
ATOM   1079 C C   . LEU   B 1 4   ? 14.890  -9.009  16.161 1.00 36.14  ? 4   LEU   A C   1 
ATOM   1080 O O   . LEU   B 1 4   ? 14.476  -8.147  15.374 1.00 29.59  ? 4   LEU   A O   1 
ATOM   1081 C CB  . LEU   B 1 4   ? 14.705  -11.361 15.334 1.00 29.58  ? 4   LEU   A CB  1 
ATOM   1082 C CG  . LEU   B 1 4   ? 15.332  -12.526 14.567 1.00 36.98  ? 4   LEU   A CG  1 
ATOM   1083 C CD1 . LEU   B 1 4   ? 14.712  -13.824 15.006 1.00 35.32  ? 4   LEU   A CD1 1 
ATOM   1084 C CD2 . LEU   B 1 4   ? 15.147  -12.341 13.069 1.00 40.60  ? 4   LEU   A CD2 1 
ATOM   1085 N N   . TYR   B 1 5   ? 14.676  -8.941  17.472 1.00 29.60  ? 5   TYR   A N   1 
ATOM   1086 C CA  . TYR   B 1 5   ? 13.915  -7.865  18.084 1.00 23.24  ? 5   TYR   A CA  1 
ATOM   1087 C C   . TYR   B 1 5   ? 14.351  -7.760  19.531 1.00 21.93  ? 5   TYR   A C   1 
ATOM   1088 O O   . TYR   B 1 5   ? 14.513  -8.770  20.212 1.00 21.45  ? 5   TYR   A O   1 
ATOM   1089 C CB  . TYR   B 1 5   ? 12.406  -8.110  18.004 1.00 19.44  ? 5   TYR   A CB  1 
ATOM   1090 C CG  . TYR   B 1 5   ? 11.576  -7.133  18.816 1.00 31.22  ? 5   TYR   A CG  1 
ATOM   1091 C CD1 . TYR   B 1 5   ? 11.465  -5.782  18.449 1.00 27.63  ? 5   TYR   A CD1 1 
ATOM   1092 C CD2 . TYR   B 1 5   ? 10.907  -7.559  19.971 1.00 26.53  ? 5   TYR   A CD2 1 
ATOM   1093 C CE1 . TYR   B 1 5   ? 10.701  -4.886  19.216 1.00 22.54  ? 5   TYR   A CE1 1 
ATOM   1094 C CE2 . TYR   B 1 5   ? 10.147  -6.689  20.726 1.00 21.67  ? 5   TYR   A CE2 1 
ATOM   1095 C CZ  . TYR   B 1 5   ? 10.043  -5.355  20.355 1.00 30.38  ? 5   TYR   A CZ  1 
ATOM   1096 O OH  . TYR   B 1 5   ? 9.265   -4.516  21.141 1.00 29.14  ? 5   TYR   A OH  1 
ATOM   1097 N N   . SER   B 1 6   ? 14.523  -6.544  20.000 1.00 21.35  ? 6   SER   A N   1 
ATOM   1098 C CA  . SER   B 1 6   ? 14.942  -6.337  21.371 1.00 22.89  ? 6   SER   A CA  1 
ATOM   1099 C C   . SER   B 1 6   ? 14.112  -5.204  21.945 1.00 25.41  ? 6   SER   A C   1 
ATOM   1100 O O   . SER   B 1 6   ? 13.767  -4.262  21.226 1.00 24.31  ? 6   SER   A O   1 
ATOM   1101 C CB  . SER   B 1 6   ? 16.433  -6.032  21.416 1.00 26.60  ? 6   SER   A CB  1 
ATOM   1102 O OG  . SER   B 1 6   ? 16.886  -5.889  22.734 1.00 29.79  ? 6   SER   A OG  1 
ATOM   1103 N N   . THR   B 1 7   ? 13.763  -5.297  23.229 1.00 18.30  ? 7   THR   A N   1 
ATOM   1104 C CA  . THR   B 1 7   ? 12.953  -4.258  23.848 1.00 20.18  ? 7   THR   A CA  1 
ATOM   1105 C C   . THR   B 1 7   ? 13.435  -4.024  25.270 1.00 22.82  ? 7   THR   A C   1 
ATOM   1106 O O   . THR   B 1 7   ? 13.958  -4.931  25.917 1.00 20.15  ? 7   THR   A O   1 
ATOM   1107 C CB  . THR   B 1 7   ? 11.439  -4.619  23.832 1.00 25.20  ? 7   THR   A CB  1 
ATOM   1108 O OG1 . THR   B 1 7   ? 10.657  -3.523  24.333 1.00 22.03  ? 7   THR   A OG1 1 
ATOM   1109 C CG2 . THR   B 1 7   ? 11.131  -5.883  24.663 1.00 17.96  ? 7   THR   A CG2 1 
ATOM   1110 N N   . GLN   B 1 8   ? 13.255  -2.793  25.756 1.00 16.80  ? 8   GLN   A N   1 
ATOM   1111 C CA  . GLN   B 1 8   ? 13.641  -2.437  27.115 1.00 20.27  ? 8   GLN   A CA  1 
ATOM   1112 C C   . GLN   B 1 8   ? 12.440  -1.906  27.888 1.00 21.65  ? 8   GLN   A C   1 
ATOM   1113 O O   . GLN   B 1 8   ? 11.644  -1.123  27.358 1.00 21.84  ? 8   GLN   A O   1 
ATOM   1114 C CB  . GLN   B 1 8   ? 14.756  -1.387  27.131 1.00 19.66  ? 8   GLN   A CB  1 
ATOM   1115 C CG  . GLN   B 1 8   ? 16.012  -1.788  26.445 1.00 18.87  ? 8   GLN   A CG  1 
ATOM   1116 C CD  . GLN   B 1 8   ? 17.119  -0.753  26.648 1.00 25.69  ? 8   GLN   A CD  1 
ATOM   1117 O OE1 . GLN   B 1 8   ? 16.894  0.451   26.512 1.00 32.28  ? 8   GLN   A OE1 1 
ATOM   1118 N NE2 . GLN   B 1 8   ? 18.305  -1.220  27.020 1.00 29.25  ? 8   GLN   A NE2 1 
ATOM   1119 N N   . VAL   B 1 9   ? 12.321  -2.326  29.146 1.00 18.95  ? 9   VAL   A N   1 
ATOM   1120 C CA  . VAL   B 1 9   ? 11.286  -1.844  30.050 1.00 18.04  ? 9   VAL   A CA  1 
ATOM   1121 C C   . VAL   B 1 9   ? 11.956  -1.423  31.346 1.00 19.91  ? 9   VAL   A C   1 
ATOM   1122 O O   . VAL   B 1 9   ? 12.795  -2.171  31.877 1.00 15.17  ? 9   VAL   A O   1 
ATOM   1123 C CB  . VAL   B 1 9   ? 10.210  -2.918  30.325 1.00 15.55  ? 9   VAL   A CB  1 
ATOM   1124 C CG1 . VAL   B 1 9   ? 9.118   -2.354  31.241 1.00 14.90  ? 9   VAL   A CG1 1 
ATOM   1125 C CG2 . VAL   B 1 9   ? 9.591   -3.415  29.015 1.00 13.67  ? 9   VAL   A CG2 1 
ATOM   1126 N N   . LYS   B 1 10  ? 11.586  -0.231  31.857 1.00 14.34  ? 10  LYS   A N   1 
ATOM   1127 C CA  . LYS   B 1 10  ? 12.095  0.282   33.127 1.00 12.90  ? 10  LYS   A CA  1 
ATOM   1128 C C   . LYS   B 1 10  ? 11.063  0.079   34.231 1.00 16.40  ? 10  LYS   A C   1 
ATOM   1129 O O   . LYS   B 1 10  ? 9.914   0.484   34.082 1.00 17.12  ? 10  LYS   A O   1 
ATOM   1130 C CB  . LYS   B 1 10  ? 12.431  1.768   33.029 1.00 14.52  ? 10  LYS   A CB  1 
ATOM   1131 C CG  . LYS   B 1 10  ? 12.934  2.339   34.359 1.00 19.63  ? 10  LYS   A CG  1 
ATOM   1132 C CD  . LYS   B 1 10  ? 13.109  3.865   34.343 1.00 29.96  ? 10  LYS   A CD  1 
ATOM   1133 C CE  . LYS   B 1 10  ? 13.818  4.363   33.094 1.00 29.36  ? 10  LYS   A CE  1 
ATOM   1134 N NZ  . LYS   B 1 10  ? 14.076  5.855   33.127 1.00 38.04  ? 10  LYS   A NZ  1 
ATOM   1135 N N   . ALA   B 1 11  ? 11.472  -0.532  35.341 1.00 18.11  ? 11  ALA   A N   1 
ATOM   1136 C CA  . ALA   B 1 11  ? 10.570  -0.783  36.460 1.00 16.55  ? 11  ALA   A CA  1 
ATOM   1137 C C   . ALA   B 1 11  ? 11.131  -0.102  37.699 1.00 17.76  ? 11  ALA   A C   1 
ATOM   1138 O O   . ALA   B 1 11  ? 12.284  -0.347  38.075 1.00 19.25  ? 11  ALA   A O   1 
ATOM   1139 C CB  . ALA   B 1 11  ? 10.388  -2.284  36.703 1.00 14.75  ? 11  ALA   A CB  1 
ATOM   1140 N N   . VAL   B 1 12  ? 10.325  0.758   38.322 1.00 18.77  ? 12  VAL   A N   1 
ATOM   1141 C CA  . VAL   B 1 12  ? 10.756  1.538   39.484 1.00 18.78  ? 12  VAL   A CA  1 
ATOM   1142 C C   . VAL   B 1 12  ? 9.878   1.172   40.665 1.00 15.29  ? 12  VAL   A C   1 
ATOM   1143 O O   . VAL   B 1 12  ? 8.652   1.294   40.585 1.00 17.74  ? 12  VAL   A O   1 
ATOM   1144 C CB  . VAL   B 1 12  ? 10.671  3.053   39.234 1.00 20.04  ? 12  VAL   A CB  1 
ATOM   1145 C CG1 . VAL   B 1 12  ? 11.108  3.802   40.492 1.00 23.45  ? 12  VAL   A CG1 1 
ATOM   1146 C CG2 . VAL   B 1 12  ? 11.522  3.462   38.046 1.00 18.77  ? 12  VAL   A CG2 1 
ATOM   1147 N N   . GLY   B 1 13  ? 10.493  0.760   41.764 1.00 17.61  ? 13  GLY   A N   1 
ATOM   1148 C CA  . GLY   B 1 13  ? 9.769   0.599   43.014 1.00 22.66  ? 13  GLY   A CA  1 
ATOM   1149 C C   . GLY   B 1 13  ? 9.053   -0.724  43.234 1.00 18.78  ? 13  GLY   A C   1 
ATOM   1150 O O   . GLY   B 1 13  ? 8.205   -0.802  44.142 1.00 18.06  ? 13  GLY   A O   1 
ATOM   1151 N N   . GLY   B 1 14  ? 9.382   -1.770  42.467 1.00 15.20  ? 14  GLY   A N   1 
ATOM   1152 C CA  . GLY   B 1 14  ? 8.886   -3.115  42.791 1.00 12.38  ? 14  GLY   A CA  1 
ATOM   1153 C C   . GLY   B 1 14  ? 7.391   -3.259  42.561 1.00 13.34  ? 14  GLY   A C   1 
ATOM   1154 O O   . GLY   B 1 14  ? 6.809   -2.595  41.698 1.00 16.62  ? 14  GLY   A O   1 
ATOM   1155 N N   . ARG   B 1 15  ? 6.740   -4.108  43.367 1.00 14.62  ? 15  ARG   A N   1 
ATOM   1156 C CA  . ARG   B 1 15  ? 5.370   -4.523  43.054 1.00 15.93  ? 15  ARG   A CA  1 
ATOM   1157 C C   . ARG   B 1 15  ? 4.306   -3.469  43.378 1.00 21.99  ? 15  ARG   A C   1 
ATOM   1158 O O   . ARG   B 1 15  ? 3.138   -3.674  43.023 1.00 18.59  ? 15  ARG   A O   1 
ATOM   1159 C CB  . ARG   B 1 15  ? 5.041   -5.832  43.780 1.00 13.96  ? 15  ARG   A CB  1 
ATOM   1160 C CG  . ARG   B 1 15  ? 5.667   -7.065  43.088 1.00 12.93  ? 15  ARG   A CG  1 
ATOM   1161 C CD  . ARG   B 1 15  ? 5.622   -8.266  44.028 1.00 19.97  ? 15  ARG   A CD  1 
ATOM   1162 N NE  . ARG   B 1 15  ? 6.268   -9.432  43.430 1.00 21.77  ? 15  ARG   A NE  1 
ATOM   1163 C CZ  . ARG   B 1 15  ? 5.645   -10.321 42.664 1.00 20.52  ? 15  ARG   A CZ  1 
ATOM   1164 N NH1 . ARG   B 1 15  ? 4.340   -10.191 42.393 1.00 20.60  ? 15  ARG   A NH1 1 
ATOM   1165 N NH2 . ARG   B 1 15  ? 6.330   -11.343 42.173 1.00 17.44  ? 15  ARG   A NH2 1 
ATOM   1166 N N   . SER   B 1 16  ? 4.684   -2.366  44.034 1.00 22.89  ? 16  SER   A N   1 
ATOM   1167 C CA  . SER   B 1 16  ? 3.830   -1.203  44.295 1.00 25.03  ? 16  SER   A CA  1 
ATOM   1168 C C   . SER   B 1 16  ? 4.132   -0.025  43.382 1.00 26.08  ? 16  SER   A C   1 
ATOM   1169 O O   . SER   B 1 16  ? 3.640   1.084   43.644 1.00 24.14  ? 16  SER   A O   1 
ATOM   1170 C CB  . SER   B 1 16  ? 4.004   -0.711  45.740 1.00 20.51  ? 16  SER   A CB  1 
ATOM   1171 O OG  . SER   B 1 16  ? 3.200   -1.446  46.617 1.00 36.73  ? 16  SER   A OG  1 
ATOM   1172 N N   . GLY   B 1 17  ? 4.943   -0.223  42.342 1.00 22.61  ? 17  GLY   A N   1 
ATOM   1173 C CA  . GLY   B 1 17  ? 5.520   0.886   41.605 1.00 18.05  ? 17  GLY   A CA  1 
ATOM   1174 C C   . GLY   B 1 17  ? 5.074   0.971   40.163 1.00 23.64  ? 17  GLY   A C   1 
ATOM   1175 O O   . GLY   B 1 17  ? 3.880   0.884   39.873 1.00 24.71  ? 17  GLY   A O   1 
ATOM   1176 N N   . THR   B 1 18  ? 6.004   1.139   39.236 1.00 16.51  ? 18  THR   A N   1 
ATOM   1177 C CA  . THR   B 1 18  ? 5.621   1.433   37.864 1.00 16.57  ? 18  THR   A CA  1 
ATOM   1178 C C   . THR   B 1 18  ? 6.490   0.670   36.864 1.00 22.10  ? 18  THR   A C   1 
ATOM   1179 O O   . THR   B 1 18  ? 7.620   0.260   37.167 1.00 20.62  ? 18  THR   A O   1 
ATOM   1180 C CB  . THR   B 1 18  ? 5.700   2.944   37.629 1.00 18.31  ? 18  THR   A CB  1 
ATOM   1181 O OG1 . THR   B 1 18  ? 5.241   3.255   36.308 1.00 45.71  ? 18  THR   A OG1 1 
ATOM   1182 C CG2 . THR   B 1 18  ? 7.104   3.444   37.838 1.00 18.21  ? 18  THR   A CG2 1 
ATOM   1183 N N   . ILE   B 1 19  ? 5.941   0.466   35.664 1.00 22.01  ? 19  ILE   A N   1 
ATOM   1184 C CA  . ILE   B 1 19  ? 6.705   -0.030  34.522 1.00 23.96  ? 19  ILE   A CA  1 
ATOM   1185 C C   . ILE   B 1 19  ? 6.481   0.919   33.368 1.00 23.20  ? 19  ILE   A C   1 
ATOM   1186 O O   . ILE   B 1 19  ? 5.379   1.459   33.206 1.00 18.93  ? 19  ILE   A O   1 
ATOM   1187 C CB  . ILE   B 1 19  ? 6.300   -1.444  34.057 1.00 24.24  ? 19  ILE   A CB  1 
ATOM   1188 C CG1 . ILE   B 1 19  ? 4.859   -1.422  33.541 1.00 24.36  ? 19  ILE   A CG1 1 
ATOM   1189 C CG2 . ILE   B 1 19  ? 6.605   -2.472  35.166 1.00 16.61  ? 19  ILE   A CG2 1 
ATOM   1190 C CD1 . ILE   B 1 19  ? 4.412   -2.615  32.729 1.00 35.02  ? 19  ILE   A CD1 1 
ATOM   1191 N N   . ARG   B 1 20  ? 7.504   1.072   32.531 1.00 21.55  ? 20  ARG   A N   1 
ATOM   1192 C CA  . ARG   B 1 20  ? 7.371   1.899   31.334 1.00 20.12  ? 20  ARG   A CA  1 
ATOM   1193 C C   . ARG   B 1 20  ? 8.355   1.379   30.304 1.00 15.11  ? 20  ARG   A C   1 
ATOM   1194 O O   . ARG   B 1 20  ? 9.563   1.423   30.541 1.00 17.61  ? 20  ARG   A O   1 
ATOM   1195 C CB  . ARG   B 1 20  ? 7.629   3.377   31.623 1.00 20.60  ? 20  ARG   A CB  1 
ATOM   1196 C CG  . ARG   B 1 20  ? 7.427   4.221   30.364 1.00 30.30  ? 20  ARG   A CG  1 
ATOM   1197 C CD  . ARG   B 1 20  ? 7.743   5.711   30.547 1.00 30.94  ? 20  ARG   A CD  1 
ATOM   1198 N NE  . ARG   B 1 20  ? 7.585   6.427   29.280 1.00 34.37  ? 20  ARG   A NE  1 
ATOM   1199 C CZ  . ARG   B 1 20  ? 8.472   6.450   28.287 1.00 30.75  ? 20  ARG   A CZ  1 
ATOM   1200 N NH1 . ARG   B 1 20  ? 9.641   5.825   28.393 1.00 31.75  ? 20  ARG   A NH1 1 
ATOM   1201 N NH2 . ARG   B 1 20  ? 8.191   7.121   27.180 1.00 30.77  ? 20  ARG   A NH2 1 
ATOM   1202 N N   . SER   B 1 21  ? 7.852   0.855   29.193 1.00 16.32  ? 21  SER   A N   1 
ATOM   1203 C CA  . SER   B 1 21  ? 8.754   0.480   28.121 1.00 21.30  ? 21  SER   A CA  1 
ATOM   1204 C C   . SER   B 1 21  ? 9.401   1.735   27.554 1.00 25.43  ? 21  SER   A C   1 
ATOM   1205 O O   . SER   B 1 21  ? 8.830   2.832   27.603 1.00 27.80  ? 21  SER   A O   1 
ATOM   1206 C CB  . SER   B 1 21  ? 8.010   -0.289  27.028 1.00 23.12  ? 21  SER   A CB  1 
ATOM   1207 O OG  . SER   B 1 21  ? 7.057   0.534   26.370 1.00 24.99  ? 21  SER   A OG  1 
ATOM   1208 N N   . GLU   B 1 22  ? 10.626  1.581   27.056 1.00 21.18  ? 22  GLU   A N   1 
ATOM   1209 C CA  . GLU   B 1 22  ? 11.373  2.759   26.627 1.00 30.31  ? 22  GLU   A CA  1 
ATOM   1210 C C   . GLU   B 1 22  ? 10.678  3.478   25.476 1.00 29.34  ? 22  GLU   A C   1 
ATOM   1211 O O   . GLU   B 1 22  ? 10.722  4.711   25.395 1.00 32.17  ? 22  GLU   A O   1 
ATOM   1212 C CB  . GLU   B 1 22  ? 12.803  2.372   26.241 1.00 26.40  ? 22  GLU   A CB  1 
ATOM   1213 C CG  . GLU   B 1 22  ? 13.741  2.015   27.410 1.00 35.27  ? 22  GLU   A CG  1 
ATOM   1214 C CD  . GLU   B 1 22  ? 13.968  3.134   28.440 1.00 39.79  ? 22  GLU   A CD  1 
ATOM   1215 O OE1 . GLU   B 1 22  ? 13.184  4.096   28.532 1.00 47.30  ? 22  GLU   A OE1 1 
ATOM   1216 O OE2 . GLU   B 1 22  ? 14.976  3.048   29.166 1.00 52.69  ? 22  GLU   A OE2 1 
ATOM   1217 N N   . ASP   B 1 23  ? 10.015  2.735   24.597 1.00 25.23  ? 23  ASP   A N   1 
ATOM   1218 C CA  . ASP   B 1 23  ? 9.276   3.336   23.492 1.00 33.36  ? 23  ASP   A CA  1 
ATOM   1219 C C   . ASP   B 1 23  ? 7.889   3.848   23.899 1.00 32.66  ? 23  ASP   A C   1 
ATOM   1220 O O   . ASP   B 1 23  ? 7.129   4.281   23.029 1.00 37.76  ? 23  ASP   A O   1 
ATOM   1221 C CB  . ASP   B 1 23  ? 9.188   2.327   22.330 1.00 30.04  ? 23  ASP   A CB  1 
ATOM   1222 C CG  . ASP   B 1 23  ? 8.352   1.083   22.664 1.00 34.14  ? 23  ASP   A CG  1 
ATOM   1223 O OD1 . ASP   B 1 23  ? 7.815   0.963   23.799 1.00 31.36  ? 23  ASP   A OD1 1 
ATOM   1224 O OD2 . ASP   B 1 23  ? 8.270   0.191   21.780 1.00 33.39  ? 23  ASP   A OD2 1 
ATOM   1225 N N   . GLY   B 1 24  ? 7.549   3.830   25.190 1.00 27.97  ? 24  GLY   A N   1 
ATOM   1226 C CA  . GLY   B 1 24  ? 6.311   4.409   25.674 1.00 28.33  ? 24  GLY   A CA  1 
ATOM   1227 C C   . GLY   B 1 24  ? 5.057   3.585   25.453 1.00 31.62  ? 24  GLY   A C   1 
ATOM   1228 O O   . GLY   B 1 24  ? 3.996   3.952   25.984 1.00 28.91  ? 24  GLY   A O   1 
ATOM   1229 N N   . ILE   B 1 25  ? 5.142   2.472   24.723 1.00 26.66  ? 25  ILE   A N   1 
ATOM   1230 C CA  . ILE   B 1 25  ? 3.937   1.745   24.330 1.00 29.68  ? 25  ILE   A CA  1 
ATOM   1231 C C   . ILE   B 1 25  ? 3.300   1.028   25.516 1.00 26.79  ? 25  ILE   A C   1 
ATOM   1232 O O   . ILE   B 1 25  ? 2.071   0.927   25.610 1.00 31.38  ? 25  ILE   A O   1 
ATOM   1233 C CB  . ILE   B 1 25  ? 4.261   0.785   23.170 1.00 37.69  ? 25  ILE   A CB  1 
ATOM   1234 C CG1 . ILE   B 1 25  ? 4.446   1.583   21.874 1.00 38.09  ? 25  ILE   A CG1 1 
ATOM   1235 C CG2 . ILE   B 1 25  ? 3.199   -0.284  23.026 1.00 31.29  ? 25  ILE   A CG2 1 
ATOM   1236 C CD1 . ILE   B 1 25  ? 5.474   1.029   20.953 1.00 42.89  ? 25  ILE   A CD1 1 
ATOM   1237 N N   . LEU   B 1 26  ? 4.103   0.524   26.443 1.00 28.94  ? 26  LEU   A N   1 
ATOM   1238 C CA  . LEU   B 1 26  ? 3.584   -0.157  27.625 1.00 27.20  ? 26  LEU   A CA  1 
ATOM   1239 C C   . LEU   B 1 26  ? 3.907   0.707   28.839 1.00 24.46  ? 26  LEU   A C   1 
ATOM   1240 O O   . LEU   B 1 26  ? 5.080   0.897   29.181 1.00 28.26  ? 26  LEU   A O   1 
ATOM   1241 C CB  . LEU   B 1 26  ? 4.182   -1.562  27.739 1.00 25.96  ? 26  LEU   A CB  1 
ATOM   1242 C CG  . LEU   B 1 26  ? 3.693   -2.451  28.879 1.00 24.49  ? 26  LEU   A CG  1 
ATOM   1243 C CD1 . LEU   B 1 26  ? 2.206   -2.778  28.727 1.00 29.08  ? 26  LEU   A CD1 1 
ATOM   1244 C CD2 . LEU   B 1 26  ? 4.531   -3.738  28.992 1.00 17.78  ? 26  LEU   A CD2 1 
ATOM   1245 N N   . GLU   B 1 27  ? 2.882   1.261   29.479 1.00 23.47  ? 27  GLU   A N   1 
ATOM   1246 C CA  . GLU   B 1 27  ? 3.111   2.131   30.632 1.00 29.66  ? 27  GLU   A CA  1 
ATOM   1247 C C   . GLU   B 1 27  ? 2.021   1.875   31.660 1.00 27.57  ? 27  GLU   A C   1 
ATOM   1248 O O   . GLU   B 1 27  ? 0.848   2.191   31.424 1.00 28.34  ? 27  GLU   A O   1 
ATOM   1249 C CB  . GLU   B 1 27  ? 3.152   3.601   30.232 1.00 31.49  ? 27  GLU   A CB  1 
ATOM   1250 C CG  . GLU   B 1 27  ? 3.315   4.509   31.441 1.00 35.95  ? 27  GLU   A CG  1 
ATOM   1251 C CD  . GLU   B 1 27  ? 3.909   5.856   31.080 1.00 40.78  ? 27  GLU   A CD  1 
ATOM   1252 O OE1 . GLU   B 1 27  ? 4.007   6.154   29.862 1.00 41.34  ? 27  GLU   A OE1 1 
ATOM   1253 O OE2 . GLU   B 1 27  ? 4.278   6.610   32.014 1.00 42.13  ? 27  GLU   A OE2 1 
ATOM   1254 N N   . LEU   B 1 28  ? 2.400   1.312   32.805 1.00 28.41  ? 28  LEU   A N   1 
ATOM   1255 C CA  . LEU   B 1 28  ? 1.393   0.802   33.718 1.00 22.39  ? 28  LEU   A CA  1 
ATOM   1256 C C   . LEU   B 1 28  ? 1.827   0.985   35.160 1.00 27.60  ? 28  LEU   A C   1 
ATOM   1257 O O   . LEU   B 1 28  ? 3.014   0.904   35.497 1.00 23.50  ? 28  LEU   A O   1 
ATOM   1258 C CB  . LEU   B 1 28  ? 1.087   -0.685  33.439 1.00 28.34  ? 28  LEU   A CB  1 
ATOM   1259 C CG  . LEU   B 1 28  ? 0.450   -1.089  32.090 1.00 29.01  ? 28  LEU   A CG  1 
ATOM   1260 C CD1 . LEU   B 1 28  ? 0.215   -2.602  32.031 1.00 30.45  ? 28  LEU   A CD1 1 
ATOM   1261 C CD2 . LEU   B 1 28  ? -0.866  -0.337  31.838 1.00 30.31  ? 28  LEU   A CD2 1 
ATOM   1262 N N   . LYS   B 1 29  ? 0.834   1.247   36.002 1.00 23.89  ? 29  LYS   A N   1 
ATOM   1263 C CA  . LYS   B 1 29  ? 0.974   1.182   37.447 1.00 25.78  ? 29  LYS   A CA  1 
ATOM   1264 C C   . LYS   B 1 29  ? 0.819   -0.271  37.905 1.00 23.44  ? 29  LYS   A C   1 
ATOM   1265 O O   . LYS   B 1 29  ? 0.118   -1.067  37.277 1.00 27.18  ? 29  LYS   A O   1 
ATOM   1266 C CB  . LYS   B 1 29  ? -0.081  2.086   38.092 1.00 23.94  ? 29  LYS   A CB  1 
ATOM   1267 C CG  . LYS   B 1 29  ? 0.047   2.332   39.581 1.00 38.27  ? 29  LYS   A CG  1 
ATOM   1268 C CD  . LYS   B 1 29  ? 1.316   3.067   39.977 1.00 38.50  ? 29  LYS   A CD  1 
ATOM   1269 C CE  . LYS   B 1 29  ? 1.601   2.890   41.465 1.00 36.42  ? 29  LYS   A CE  1 
ATOM   1270 N NZ  . LYS   B 1 29  ? 2.918   3.472   41.844 1.00 44.11  ? 29  LYS   A NZ  1 
ATOM   1271 N N   . LEU   B 1 30  ? 1.466   -0.617  39.014 1.00 19.40  ? 30  LEU   A N   1 
ATOM   1272 C CA  . LEU   B 1 30  ? 1.372   -1.959  39.569 1.00 19.91  ? 30  LEU   A CA  1 
ATOM   1273 C C   . LEU   B 1 30  ? 0.869   -1.897  41.000 1.00 19.49  ? 30  LEU   A C   1 
ATOM   1274 O O   . LEU   B 1 30  ? 1.164   -0.952  41.735 1.00 23.37  ? 30  LEU   A O   1 
ATOM   1275 C CB  . LEU   B 1 30  ? 2.731   -2.671  39.563 1.00 18.22  ? 30  LEU   A CB  1 
ATOM   1276 C CG  . LEU   B 1 30  ? 3.073   -3.568  38.387 1.00 28.37  ? 30  LEU   A CG  1 
ATOM   1277 C CD1 . LEU   B 1 30  ? 2.895   -2.841  37.074 1.00 23.17  ? 30  LEU   A CD1 1 
ATOM   1278 C CD2 . LEU   B 1 30  ? 4.517   -4.027  38.559 1.00 19.24  ? 30  LEU   A CD2 1 
ATOM   1279 N N   . ALA   B 1 31  ? 0.171   -2.954  41.420 1.00 16.60  ? 31  ALA   A N   1 
ATOM   1280 C CA  . ALA   B 1 31  ? -0.251  -3.058  42.802 1.00 13.90  ? 31  ALA   A CA  1 
ATOM   1281 C C   . ALA   B 1 31  ? -0.152  -4.496  43.281 1.00 19.21  ? 31  ALA   A C   1 
ATOM   1282 O O   . ALA   B 1 31  ? -0.282  -5.449  42.502 1.00 18.13  ? 31  ALA   A O   1 
ATOM   1283 C CB  . ALA   B 1 31  ? -1.689  -2.554  42.980 1.00 21.10  ? 31  ALA   A CB  1 
ATOM   1284 N N   . LEU   B 1 32  ? 0.029   -4.625  44.585 1.00 13.86  ? 32  LEU   A N   1 
ATOM   1285 C CA  . LEU   B 1 32  ? -0.099  -5.899  45.259 1.00 21.37  ? 32  LEU   A CA  1 
ATOM   1286 C C   . LEU   B 1 32  ? -1.552  -6.342  45.201 1.00 21.91  ? 32  LEU   A C   1 
ATOM   1287 O O   . LEU   B 1 32  ? -2.450  -5.509  45.361 1.00 17.64  ? 32  LEU   A O   1 
ATOM   1288 C CB  . LEU   B 1 32  ? 0.333   -5.766  46.711 1.00 20.58  ? 32  LEU   A CB  1 
ATOM   1289 C CG  . LEU   B 1 32  ? 1.817   -5.814  46.971 1.00 29.84  ? 32  LEU   A CG  1 
ATOM   1290 C CD1 . LEU   B 1 32  ? 2.013   -5.500  48.437 1.00 28.96  ? 32  LEU   A CD1 1 
ATOM   1291 C CD2 . LEU   B 1 32  ? 2.378   -7.188  46.627 1.00 23.16  ? 32  LEU   A CD2 1 
ATOM   1292 N N   . PRO   B 1 33  ? -1.827  -7.618  44.933 1.00 23.60  ? 33  PRO   A N   1 
ATOM   1293 C CA  . PRO   B 1 33  ? -3.225  -8.068  44.881 1.00 19.36  ? 33  PRO   A CA  1 
ATOM   1294 C C   . PRO   B 1 33  ? -3.846  -8.097  46.266 1.00 26.83  ? 33  PRO   A C   1 
ATOM   1295 O O   . PRO   B 1 33  ? -3.163  -8.054  47.296 1.00 22.72  ? 33  PRO   A O   1 
ATOM   1296 C CB  . PRO   B 1 33  ? -3.138  -9.478  44.287 1.00 21.14  ? 33  PRO   A CB  1 
ATOM   1297 C CG  . PRO   B 1 33  ? -1.722  -9.913  44.466 1.00 15.28  ? 33  PRO   A CG  1 
ATOM   1298 C CD  . PRO   B 1 33  ? -0.871  -8.661  44.526 1.00 19.85  ? 33  PRO   A CD  1 
ATOM   1299 N N   . LYS   B 1 34  ? -5.179  -8.189  46.283 1.00 26.04  ? 34  LYS   A N   1 
ATOM   1300 C CA  . LYS   B 1 34  ? -5.897  -8.196  47.555 1.00 28.18  ? 34  LYS   A CA  1 
ATOM   1301 C C   . LYS   B 1 34  ? -5.524  -9.413  48.410 1.00 31.49  ? 34  LYS   A C   1 
ATOM   1302 O O   . LYS   B 1 34  ? -5.405  -9.301  49.636 1.00 27.71  ? 34  LYS   A O   1 
ATOM   1303 C CB  . LYS   B 1 34  ? -7.407  -8.119  47.292 1.00 36.93  ? 34  LYS   A CB  1 
ATOM   1304 C CG  . LYS   B 1 34  ? -7.901  -6.685  46.986 1.00 40.69  ? 34  LYS   A CG  1 
ATOM   1305 C CD  . LYS   B 1 34  ? -9.443  -6.545  46.970 1.00 51.07  ? 34  LYS   A CD  1 
ATOM   1306 C CE  . LYS   B 1 34  ? -10.035 -6.778  45.573 1.00 49.11  ? 34  LYS   A CE  1 
ATOM   1307 N NZ  . LYS   B 1 34  ? -11.516 -7.030  45.531 1.00 55.44  ? 34  LYS   A NZ  1 
ATOM   1308 N N   . GLU   B 1 35  ? -5.315  -10.579 47.784 1.00 33.17  ? 35  GLU   A N   1 
ATOM   1309 C CA  . GLU   B 1 35  ? -4.864  -11.763 48.530 1.00 36.63  ? 35  GLU   A CA  1 
ATOM   1310 C C   . GLU   B 1 35  ? -3.590  -11.502 49.332 1.00 24.85  ? 35  GLU   A C   1 
ATOM   1311 O O   . GLU   B 1 35  ? -3.411  -12.067 50.419 1.00 27.72  ? 35  GLU   A O   1 
ATOM   1312 C CB  . GLU   B 1 35  ? -4.643  -12.953 47.583 1.00 27.05  ? 35  GLU   A CB  1 
ATOM   1313 C CG  . GLU   B 1 35  ? -5.892  -13.438 46.884 1.00 31.41  ? 35  GLU   A CG  1 
ATOM   1314 C CD  . GLU   B 1 35  ? -6.105  -12.814 45.498 1.00 40.93  ? 35  GLU   A CD  1 
ATOM   1315 O OE1 . GLU   B 1 35  ? -5.994  -11.565 45.354 1.00 29.51  ? 35  GLU   A OE1 1 
ATOM   1316 O OE2 . GLU   B 1 35  ? -6.413  -13.586 44.556 1.00 36.71  ? 35  GLU   A OE2 1 
ATOM   1317 N N   . LEU   B 1 36  ? -2.709  -10.632 48.842 1.00 28.55  ? 36  LEU   A N   1 
ATOM   1318 C CA  . LEU   B 1 36  ? -1.520  -10.251 49.595 1.00 27.16  ? 36  LEU   A CA  1 
ATOM   1319 C C   . LEU   B 1 36  ? -1.716  -8.974  50.400 1.00 27.61  ? 36  LEU   A C   1 
ATOM   1320 O O   . LEU   B 1 36  ? -0.736  -8.390  50.870 1.00 28.68  ? 36  LEU   A O   1 
ATOM   1321 C CB  . LEU   B 1 36  ? -0.328  -10.108 48.655 1.00 23.45  ? 36  LEU   A CB  1 
ATOM   1322 C CG  . LEU   B 1 36  ? -0.221  -11.369 47.789 1.00 30.71  ? 36  LEU   A CG  1 
ATOM   1323 C CD1 . LEU   B 1 36  ? 0.911   -11.278 46.763 1.00 19.36  ? 36  LEU   A CD1 1 
ATOM   1324 C CD2 . LEU   B 1 36  ? -0.061  -12.596 48.672 1.00 30.18  ? 36  LEU   A CD2 1 
ATOM   1325 N N   . GLY   B 1 37  ? -2.954  -8.529  50.576 1.00 32.31  ? 37  GLY   A N   1 
ATOM   1326 C CA  . GLY   B 1 37  ? -3.211  -7.380  51.422 1.00 39.41  ? 37  GLY   A CA  1 
ATOM   1327 C C   . GLY   B 1 37  ? -3.159  -6.035  50.734 1.00 37.39  ? 37  GLY   A C   1 
ATOM   1328 O O   . GLY   B 1 37  ? -3.326  -5.009  51.410 1.00 43.71  ? 37  GLY   A O   1 
ATOM   1329 N N   . GLY   B 1 38  ? -2.938  -6.003  49.419 1.00 28.12  ? 38  GLY   A N   1 
ATOM   1330 C CA  . GLY   B 1 38  ? -2.959  -4.769  48.664 1.00 22.35  ? 38  GLY   A CA  1 
ATOM   1331 C C   . GLY   B 1 38  ? -4.356  -4.411  48.200 1.00 27.99  ? 38  GLY   A C   1 
ATOM   1332 O O   . GLY   B 1 38  ? -5.356  -5.057  48.536 1.00 25.52  ? 38  GLY   A O   1 
ATOM   1333 N N   . LYS   B 1 39  ? -4.422  -3.361  47.388 1.00 35.64  ? 39  LYS   A N   1 
ATOM   1334 C CA  . LYS   B 1 39  ? -5.720  -2.927  46.898 1.00 32.40  ? 39  LYS   A CA  1 
ATOM   1335 C C   . LYS   B 1 39  ? -6.119  -3.596  45.590 1.00 36.20  ? 39  LYS   A C   1 
ATOM   1336 O O   . LYS   B 1 39  ? -7.316  -3.675  45.305 1.00 29.51  ? 39  LYS   A O   1 
ATOM   1337 C CB  . LYS   B 1 39  ? -5.750  -1.395  46.807 1.00 33.56  ? 39  LYS   A CB  1 
ATOM   1338 C CG  . LYS   B 1 39  ? -5.690  -0.785  48.242 1.00 44.67  ? 39  LYS   A CG  1 
ATOM   1339 C CD  . LYS   B 1 39  ? -5.724  0.744   48.288 1.00 50.75  ? 39  LYS   A CD  1 
ATOM   1340 C CE  . LYS   B 1 39  ? -4.383  1.369   47.843 1.00 58.17  ? 39  LYS   A CE  1 
ATOM   1341 N NZ  . LYS   B 1 39  ? -3.250  1.139   48.778 1.00 54.46  ? 39  LYS   A NZ  1 
ATOM   1342 N N   . GLY   B 1 40  ? -5.172  -4.144  44.830 1.00 32.31  ? 40  GLY   A N   1 
ATOM   1343 C CA  . GLY   B 1 40  ? -5.540  -4.910  43.646 1.00 25.10  ? 40  GLY   A CA  1 
ATOM   1344 C C   . GLY   B 1 40  ? -6.179  -4.063  42.573 1.00 31.18  ? 40  GLY   A C   1 
ATOM   1345 O O   . GLY   B 1 40  ? -7.012  -4.555  41.802 1.00 33.77  ? 40  GLY   A O   1 
ATOM   1346 N N   . ASP   B 1 41  ? -5.826  -2.788  42.528 1.00 28.03  ? 41  ASP   A N   1 
ATOM   1347 C CA  . ASP   B 1 41  ? -6.386  -1.862  41.545 1.00 38.68  ? 41  ASP   A CA  1 
ATOM   1348 C C   . ASP   B 1 41  ? -5.471  -1.643  40.334 1.00 36.60  ? 41  ASP   A C   1 
ATOM   1349 O O   . ASP   B 1 41  ? -5.735  -0.731  39.533 1.00 30.88  ? 41  ASP   A O   1 
ATOM   1350 C CB  . ASP   B 1 41  ? -6.770  -0.536  42.245 1.00 37.48  ? 41  ASP   A CB  1 
ATOM   1351 C CG  . ASP   B 1 41  ? -5.633  0.033   43.039 1.00 38.19  ? 41  ASP   A CG  1 
ATOM   1352 O OD1 . ASP   B 1 41  ? -4.605  -0.632  43.083 1.00 39.43  ? 41  ASP   A OD1 1 
ATOM   1353 O OD2 . ASP   B 1 41  ? -5.800  1.103   43.651 1.00 51.57  ? 41  ASP   A OD2 1 
ATOM   1354 N N   . ALA   B 1 42  ? -4.464  -2.513  40.149 1.00 23.36  ? 42  ALA   A N   1 
ATOM   1355 C CA  . ALA   B 1 42  ? -3.529  -2.458  39.028 1.00 23.03  ? 42  ALA   A CA  1 
ATOM   1356 C C   . ALA   B 1 42  ? -2.906  -3.840  38.857 1.00 20.42  ? 42  ALA   A C   1 
ATOM   1357 O O   . ALA   B 1 42  ? -3.044  -4.706  39.721 1.00 19.71  ? 42  ALA   A O   1 
ATOM   1358 C CB  . ALA   B 1 42  ? -2.470  -1.373  39.250 1.00 17.74  ? 42  ALA   A CB  1 
ATOM   1359 N N   . THR   B 1 43  ? -2.226  -4.034  37.725 1.00 16.45  ? 43  THR   A N   1 
ATOM   1360 C CA  . THR   B 1 43  ? -1.667  -5.337  37.372 1.00 25.20  ? 43  THR   A CA  1 
ATOM   1361 C C   . THR   B 1 43  ? -0.419  -5.663  38.199 1.00 16.23  ? 43  THR   A C   1 
ATOM   1362 O O   . THR   B 1 43  ? -0.054  -4.945  39.135 1.00 17.95  ? 43  THR   A O   1 
ATOM   1363 C CB  . THR   B 1 43  ? -1.355  -5.410  35.877 1.00 20.98  ? 43  THR   A CB  1 
ATOM   1364 O OG1 . THR   B 1 43  ? -1.078  -6.773  35.540 1.00 20.08  ? 43  THR   A OG1 1 
ATOM   1365 C CG2 . THR   B 1 43  ? -0.182  -4.539  35.491 1.00 24.08  ? 43  THR   A CG2 1 
ATOM   1366 N N   . ASN   B 1 44  ? 0.223   -6.795  37.876 1.00 18.18  ? 44  ASN   A N   1 
ATOM   1367 C CA  . ASN   B 1 44  ? 1.277   -7.348  38.714 1.00 16.77  ? 44  ASN   A CA  1 
ATOM   1368 C C   . ASN   B 1 44  ? 2.145   -8.285  37.880 1.00 14.65  ? 44  ASN   A C   1 
ATOM   1369 O O   . ASN   B 1 44  ? 1.749   -8.695  36.774 1.00 17.17  ? 44  ASN   A O   1 
ATOM   1370 C CB  . ASN   B 1 44  ? 0.686   -8.067  39.947 1.00 15.00  ? 44  ASN   A CB  1 
ATOM   1371 C CG  . ASN   B 1 44  ? -0.284  -9.187  39.565 1.00 18.68  ? 44  ASN   A CG  1 
ATOM   1372 O OD1 . ASN   B 1 44  ? 0.078   -10.131 38.838 1.00 17.02  ? 44  ASN   A OD1 1 
ATOM   1373 N ND2 . ASN   B 1 44  ? -1.534  -9.071  40.031 1.00 13.86  ? 44  ASN   A ND2 1 
ATOM   1374 N N   . PRO   B 1 45  ? 3.352   -8.622  38.363 1.00 19.23  ? 45  PRO   A N   1 
ATOM   1375 C CA  . PRO   B 1 45  ? 4.263   -9.478  37.565 1.00 18.63  ? 45  PRO   A CA  1 
ATOM   1376 C C   . PRO   B 1 45  ? 3.662   -10.785 37.077 1.00 16.56  ? 45  PRO   A C   1 
ATOM   1377 O O   . PRO   B 1 45  ? 3.914   -11.187 35.936 1.00 15.53  ? 45  PRO   A O   1 
ATOM   1378 C CB  . PRO   B 1 45  ? 5.424   -9.724  38.535 1.00 17.74  ? 45  PRO   A CB  1 
ATOM   1379 C CG  . PRO   B 1 45  ? 5.523   -8.369  39.258 1.00 16.50  ? 45  PRO   A CG  1 
ATOM   1380 C CD  . PRO   B 1 45  ? 4.054   -7.986  39.500 1.00 11.71  ? 45  PRO   A CD  1 
ATOM   1381 N N   . GLU   B 1 46  ? 2.878   -11.461 37.912 1.00 14.03  ? 46  GLU   A N   1 
ATOM   1382 C CA  . GLU   B 1 46  ? 2.292   -12.729 37.491 1.00 14.33  ? 46  GLU   A CA  1 
ATOM   1383 C C   . GLU   B 1 46  ? 1.312   -12.541 36.347 1.00 10.55  ? 46  GLU   A C   1 
ATOM   1384 O O   . GLU   B 1 46  ? 1.288   -13.344 35.431 1.00 15.94  ? 46  GLU   A O   1 
ATOM   1385 C CB  . GLU   B 1 46  ? 1.616   -13.418 38.678 1.00 12.25  ? 46  GLU   A CB  1 
ATOM   1386 C CG  . GLU   B 1 46  ? 2.624   -13.967 39.650 1.00 15.65  ? 46  GLU   A CG  1 
ATOM   1387 C CD  . GLU   B 1 46  ? 3.354   -12.859 40.403 1.00 25.64  ? 46  GLU   A CD  1 
ATOM   1388 O OE1 . GLU   B 1 46  ? 2.678   -11.909 40.874 1.00 18.03  ? 46  GLU   A OE1 1 
ATOM   1389 O OE2 . GLU   B 1 46  ? 4.606   -12.924 40.498 1.00 20.73  ? 46  GLU   A OE2 1 
ATOM   1390 N N   . GLN   B 1 47  ? 0.505   -11.481 36.375 1.00 15.67  ? 47  GLN   A N   1 
ATOM   1391 C CA  . GLN   B 1 47  ? -0.423  -11.223 35.276 1.00 15.89  ? 47  GLN   A CA  1 
ATOM   1392 C C   . GLN   B 1 47  ? 0.308   -10.866 33.990 1.00 13.69  ? 47  GLN   A C   1 
ATOM   1393 O O   . GLN   B 1 47  ? -0.098  -11.284 32.898 1.00 12.08  ? 47  GLN   A O   1 
ATOM   1394 C CB  . GLN   B 1 47  ? -1.390  -10.086 35.639 1.00 17.67  ? 47  GLN   A CB  1 
ATOM   1395 C CG  . GLN   B 1 47  ? -2.556  -10.542 36.475 1.00 21.75  ? 47  GLN   A CG  1 
ATOM   1396 C CD  . GLN   B 1 47  ? -3.638  -9.477  36.623 1.00 31.56  ? 47  GLN   A CD  1 
ATOM   1397 O OE1 . GLN   B 1 47  ? -3.449  -8.307  36.245 1.00 21.05  ? 47  GLN   A OE1 1 
ATOM   1398 N NE2 . GLN   B 1 47  ? -4.796  -9.891  37.151 1.00 29.92  ? 47  GLN   A NE2 1 
ATOM   1399 N N   . LEU   B 1 48  ? 1.371   -10.062 34.096 1.00 12.42  ? 48  LEU   A N   1 
ATOM   1400 C CA  . LEU   B 1 48  ? 2.141   -9.690  32.915 1.00 13.08  ? 48  LEU   A CA  1 
ATOM   1401 C C   . LEU   B 1 48  ? 2.785   -10.927 32.288 1.00 13.58  ? 48  LEU   A C   1 
ATOM   1402 O O   . LEU   B 1 48  ? 2.779   -11.093 31.059 1.00 14.48  ? 48  LEU   A O   1 
ATOM   1403 C CB  . LEU   B 1 48  ? 3.199   -8.642  33.307 1.00 11.12  ? 48  LEU   A CB  1 
ATOM   1404 C CG  . LEU   B 1 48  ? 2.643   -7.277  33.699 1.00 12.89  ? 48  LEU   A CG  1 
ATOM   1405 C CD1 . LEU   B 1 48  ? 3.695   -6.350  34.395 1.00 10.40  ? 48  LEU   A CD1 1 
ATOM   1406 C CD2 . LEU   B 1 48  ? 2.106   -6.602  32.463 1.00 14.51  ? 48  LEU   A CD2 1 
ATOM   1407 N N   . PHE   B 1 49  ? 3.298   -11.827 33.133 1.00 15.31  ? 49  PHE   A N   1 
ATOM   1408 C CA  . PHE   B 1 49  ? 3.899   -13.065 32.646 1.00 13.38  ? 49  PHE   A CA  1 
ATOM   1409 C C   . PHE   B 1 49  ? 2.848   -13.988 32.038 1.00 17.88  ? 49  PHE   A C   1 
ATOM   1410 O O   . PHE   B 1 49  ? 3.051   -14.546 30.953 1.00 13.88  ? 49  PHE   A O   1 
ATOM   1411 C CB  . PHE   B 1 49  ? 4.620   -13.782 33.792 1.00 15.27  ? 49  PHE   A CB  1 
ATOM   1412 C CG  . PHE   B 1 49  ? 5.347   -15.013 33.344 1.00 17.86  ? 49  PHE   A CG  1 
ATOM   1413 C CD1 . PHE   B 1 49  ? 6.567   -14.905 32.695 1.00 21.68  ? 49  PHE   A CD1 1 
ATOM   1414 C CD2 . PHE   B 1 49  ? 4.792   -16.274 33.522 1.00 19.29  ? 49  PHE   A CD2 1 
ATOM   1415 C CE1 . PHE   B 1 49  ? 7.244   -16.057 32.246 1.00 30.17  ? 49  PHE   A CE1 1 
ATOM   1416 C CE2 . PHE   B 1 49  ? 5.456   -17.423 33.085 1.00 23.15  ? 49  PHE   A CE2 1 
ATOM   1417 C CZ  . PHE   B 1 49  ? 6.684   -17.314 32.442 1.00 19.24  ? 49  PHE   A CZ  1 
ATOM   1418 N N   . ALA   B 1 50  ? 1.738   -14.203 32.756 1.00 16.73  ? 50  ALA   A N   1 
ATOM   1419 C CA  . ALA   B 1 50  ? 0.629   -14.987 32.213 1.00 15.35  ? 50  ALA   A CA  1 
ATOM   1420 C C   . ALA   B 1 50  ? 0.227   -14.482 30.831 1.00 17.14  ? 50  ALA   A C   1 
ATOM   1421 O O   . ALA   B 1 50  ? -0.003  -15.282 29.913 1.00 14.03  ? 50  ALA   A O   1 
ATOM   1422 C CB  . ALA   B 1 50  ? -0.569  -14.931 33.171 1.00 9.31   ? 50  ALA   A CB  1 
ATOM   1423 N N   . ALA   B 1 51  ? 0.176   -13.152 30.651 1.00 12.56  ? 51  ALA   A N   1 
ATOM   1424 C CA  . ALA   B 1 51  ? -0.235  -12.577 29.372 1.00 11.58  ? 51  ALA   A CA  1 
ATOM   1425 C C   . ALA   B 1 51  ? 0.812   -12.799 28.279 1.00 17.23  ? 51  ALA   A C   1 
ATOM   1426 O O   . ALA   B 1 51  ? 0.477   -13.190 27.149 1.00 15.73  ? 51  ALA   A O   1 
ATOM   1427 C CB  . ALA   B 1 51  ? -0.490  -11.079 29.541 1.00 14.18  ? 51  ALA   A CB  1 
ATOM   1428 N N   . GLY   B 1 52  ? 2.078   -12.475 28.573 1.00 15.21  ? 52  GLY   A N   1 
ATOM   1429 C CA  . GLY   B 1 52  ? 3.135   -12.725 27.606 1.00 12.01  ? 52  GLY   A CA  1 
ATOM   1430 C C   . GLY   B 1 52  ? 3.174   -14.174 27.156 1.00 12.34  ? 52  GLY   A C   1 
ATOM   1431 O O   . GLY   B 1 52  ? 3.282   -14.478 25.958 1.00 15.52  ? 52  GLY   A O   1 
ATOM   1432 N N   . TYR   B 1 53  ? 3.035   -15.095 28.097 1.00 13.76  ? 53  TYR   A N   1 
ATOM   1433 C CA  . TYR   B 1 53  ? 3.159   -16.503 27.730 1.00 15.35  ? 53  TYR   A CA  1 
ATOM   1434 C C   . TYR   B 1 53  ? 1.916   -17.028 27.019 1.00 15.32  ? 53  TYR   A C   1 
ATOM   1435 O O   . TYR   B 1 53  ? 2.034   -17.718 25.999 1.00 15.82  ? 53  TYR   A O   1 
ATOM   1436 C CB  . TYR   B 1 53  ? 3.583   -17.305 28.958 1.00 21.40  ? 53  TYR   A CB  1 
ATOM   1437 C CG  . TYR   B 1 53  ? 3.744   -18.810 28.840 1.00 18.29  ? 53  TYR   A CG  1 
ATOM   1438 C CD1 . TYR   B 1 53  ? 4.319   -19.373 27.718 1.00 23.92  ? 53  TYR   A CD1 1 
ATOM   1439 C CD2 . TYR   B 1 53  ? 3.826   -19.555 30.006 1.00 22.74  ? 53  TYR   A CD2 1 
ATOM   1440 C CE1 . TYR   B 1 53  ? 4.621   -20.731 27.648 1.00 23.50  ? 53  TYR   A CE1 1 
ATOM   1441 C CE2 . TYR   B 1 53  ? 4.162   -20.915 29.979 1.00 23.11  ? 53  TYR   A CE2 1 
ATOM   1442 C CZ  . TYR   B 1 53  ? 4.569   -21.491 28.789 1.00 16.38  ? 53  TYR   A CZ  1 
ATOM   1443 O OH  . TYR   B 1 53  ? 4.924   -22.812 28.717 1.00 14.29  ? 53  TYR   A OH  1 
ATOM   1444 N N   . ALA   B 1 54  ? 0.720   -16.631 27.453 1.00 14.75  ? 54  ALA   A N   1 
ATOM   1445 C CA  . ALA   B 1 54  ? -0.469  -17.050 26.717 1.00 14.91  ? 54  ALA   A CA  1 
ATOM   1446 C C   . ALA   B 1 54  ? -0.417  -16.544 25.277 1.00 18.98  ? 54  ALA   A C   1 
ATOM   1447 O O   . ALA   B 1 54  ? -0.688  -17.302 24.334 1.00 24.59  ? 54  ALA   A O   1 
ATOM   1448 C CB  . ALA   B 1 54  ? -1.729  -16.549 27.419 1.00 15.34  ? 54  ALA   A CB  1 
ATOM   1449 N N   . ALA   B 1 55  ? -0.010  -15.279 25.084 1.00 15.73  ? 55  ALA   A N   1 
ATOM   1450 C CA  . ALA   B 1 55  ? 0.059   -14.709 23.739 1.00 15.34  ? 55  ALA   A CA  1 
ATOM   1451 C C   . ALA   B 1 55  ? 1.132   -15.388 22.890 1.00 17.45  ? 55  ALA   A C   1 
ATOM   1452 O O   . ALA   B 1 55  ? 0.886   -15.761 21.731 1.00 20.85  ? 55  ALA   A O   1 
ATOM   1453 C CB  . ALA   B 1 55  ? 0.324   -13.209 23.830 1.00 12.61  ? 55  ALA   A CB  1 
ATOM   1454 N N   . CYS   B 1 56  ? 2.337   -15.560 23.436 1.00 18.87  ? 56  CYS   A N   1 
ATOM   1455 C CA  . CYS   B 1 56  ? 3.381   -16.196 22.639 1.00 15.57  ? 56  CYS   A CA  1 
ATOM   1456 C C   . CYS   B 1 56  ? 2.996   -17.626 22.290 1.00 18.20  ? 56  CYS   A C   1 
ATOM   1457 O O   . CYS   B 1 56  ? 3.192   -18.078 21.149 1.00 19.46  ? 56  CYS   A O   1 
ATOM   1458 C CB  . CYS   B 1 56  ? 4.725   -16.165 23.372 1.00 20.97  ? 56  CYS   A CB  1 
ATOM   1459 S SG  . CYS   B 1 56  ? 6.071   -17.070 22.491 1.00 30.71  ? 56  CYS   A SG  1 
ATOM   1460 N N   . PHE   B 1 57  ? 2.420   -18.349 23.248 1.00 18.37  ? 57  PHE   A N   1 
ATOM   1461 C CA  . PHE   B 1 57  ? 2.072   -19.740 22.997 1.00 18.22  ? 57  PHE   A CA  1 
ATOM   1462 C C   . PHE   B 1 57  ? 0.971   -19.843 21.959 1.00 22.48  ? 57  PHE   A C   1 
ATOM   1463 O O   . PHE   B 1 57  ? 1.033   -20.694 21.067 1.00 22.81  ? 57  PHE   A O   1 
ATOM   1464 C CB  . PHE   B 1 57  ? 1.655   -20.442 24.289 1.00 12.74  ? 57  PHE   A CB  1 
ATOM   1465 C CG  . PHE   B 1 57  ? 1.644   -21.949 24.179 1.00 16.14  ? 57  PHE   A CG  1 
ATOM   1466 C CD1 . PHE   B 1 57  ? 0.504   -22.618 23.738 1.00 13.77  ? 57  PHE   A CD1 1 
ATOM   1467 C CD2 . PHE   B 1 57  ? 2.772   -22.689 24.489 1.00 18.93  ? 57  PHE   A CD2 1 
ATOM   1468 C CE1 . PHE   B 1 57  ? 0.485   -24.008 23.631 1.00 17.32  ? 57  PHE   A CE1 1 
ATOM   1469 C CE2 . PHE   B 1 57  ? 2.770   -24.085 24.398 1.00 21.16  ? 57  PHE   A CE2 1 
ATOM   1470 C CZ  . PHE   B 1 57  ? 1.624   -24.752 23.967 1.00 20.85  ? 57  PHE   A CZ  1 
ATOM   1471 N N   . GLY   B 1 58  ? -0.065  -19.009 22.079 1.00 19.88  ? 58  GLY   A N   1 
ATOM   1472 C CA  . GLY   B 1 58  ? -1.109  -19.012 21.077 1.00 16.16  ? 58  GLY   A CA  1 
ATOM   1473 C C   . GLY   B 1 58  ? -0.569  -18.708 19.694 1.00 20.73  ? 58  GLY   A C   1 
ATOM   1474 O O   . GLY   B 1 58  ? -0.943  -19.357 18.707 1.00 23.67  ? 58  GLY   A O   1 
ATOM   1475 N N   . ASN   B 1 59  ? 0.364   -17.761 19.611 1.00 16.27  ? 59  ASN   A N   1 
ATOM   1476 C CA  . ASN   B 1 59  ? 0.960   -17.443 18.321 1.00 20.73  ? 59  ASN   A CA  1 
ATOM   1477 C C   . ASN   B 1 59  ? 1.715   -18.637 17.743 1.00 26.60  ? 59  ASN   A C   1 
ATOM   1478 O O   . ASN   B 1 59  ? 1.632   -18.931 16.535 1.00 26.10  ? 59  ASN   A O   1 
ATOM   1479 C CB  . ASN   B 1 59  ? 1.894   -16.249 18.451 1.00 18.09  ? 59  ASN   A CB  1 
ATOM   1480 C CG  . ASN   B 1 59  ? 2.173   -15.634 17.120 1.00 30.84  ? 59  ASN   A CG  1 
ATOM   1481 O OD1 . ASN   B 1 59  ? 1.393   -14.806 16.630 1.00 23.02  ? 59  ASN   A OD1 1 
ATOM   1482 N ND2 . ASN   B 1 59  ? 3.241   -16.087 16.479 1.00 29.29  ? 59  ASN   A ND2 1 
ATOM   1483 N N   . ALA   B 1 60  ? 2.480   -19.328 18.588 1.00 19.19  ? 60  ALA   A N   1 
ATOM   1484 C CA  . ALA   B 1 60  ? 3.230   -20.470 18.085 1.00 23.87  ? 60  ALA   A CA  1 
ATOM   1485 C C   . ALA   B 1 60  ? 2.285   -21.607 17.691 1.00 26.22  ? 60  ALA   A C   1 
ATOM   1486 O O   . ALA   B 1 60  ? 2.571   -22.362 16.757 1.00 30.75  ? 60  ALA   A O   1 
ATOM   1487 C CB  . ALA   B 1 60  ? 4.265   -20.922 19.121 1.00 17.57  ? 60  ALA   A CB  1 
ATOM   1488 N N   . VAL   B 1 61  ? 1.154   -21.746 18.389 1.00 26.70  ? 61  VAL   A N   1 
ATOM   1489 C CA  . VAL   B 1 61  ? 0.160   -22.737 17.986 1.00 27.06  ? 61  VAL   A CA  1 
ATOM   1490 C C   . VAL   B 1 61  ? -0.334  -22.415 16.589 1.00 34.53  ? 61  VAL   A C   1 
ATOM   1491 O O   . VAL   B 1 61  ? -0.491  -23.310 15.751 1.00 27.38  ? 61  VAL   A O   1 
ATOM   1492 C CB  . VAL   B 1 61  ? -1.008  -22.799 18.991 1.00 22.30  ? 61  VAL   A CB  1 
ATOM   1493 C CG1 . VAL   B 1 61  ? -2.185  -23.623 18.423 1.00 28.60  ? 61  VAL   A CG1 1 
ATOM   1494 C CG2 . VAL   B 1 61  ? -0.568  -23.393 20.309 1.00 20.56  ? 61  VAL   A CG2 1 
ATOM   1495 N N   . ILE   B 1 62  ? -0.595  -21.129 16.317 1.00 29.48  ? 62  ILE   A N   1 
ATOM   1496 C CA  . ILE   B 1 62  ? -1.018  -20.742 14.971 1.00 35.74  ? 62  ILE   A CA  1 
ATOM   1497 C C   . ILE   B 1 62  ? 0.016   -21.194 13.954 1.00 33.92  ? 62  ILE   A C   1 
ATOM   1498 O O   . ILE   B 1 62  ? -0.314  -21.810 12.929 1.00 38.46  ? 62  ILE   A O   1 
ATOM   1499 C CB  . ILE   B 1 62  ? -1.252  -19.222 14.876 1.00 31.09  ? 62  ILE   A CB  1 
ATOM   1500 C CG1 . ILE   B 1 62  ? -2.495  -18.797 15.646 1.00 25.51  ? 62  ILE   A CG1 1 
ATOM   1501 C CG2 . ILE   B 1 62  ? -1.352  -18.766 13.424 1.00 30.35  ? 62  ILE   A CG2 1 
ATOM   1502 C CD1 . ILE   B 1 62  ? -2.523  -17.312 15.940 1.00 23.69  ? 62  ILE   A CD1 1 
ATOM   1503 N N   . HIS   B 1 63  ? 1.284   -20.881 14.226 1.00 31.86  ? 63  HIS   A N   1 
ATOM   1504 C CA  . HIS   B 1 63  ? 2.349   -21.221 13.284 1.00 39.19  ? 63  HIS   A CA  1 
ATOM   1505 C C   . HIS   B 1 63  ? 2.476   -22.741 13.084 1.00 43.97  ? 63  HIS   A C   1 
ATOM   1506 O O   . HIS   B 1 63  ? 2.751   -23.206 11.977 1.00 38.67  ? 63  HIS   A O   1 
ATOM   1507 C CB  . HIS   B 1 63  ? 3.676   -20.616 13.742 1.00 32.25  ? 63  HIS   A CB  1 
ATOM   1508 C CG  . HIS   B 1 63  ? 4.850   -21.050 12.917 1.00 50.21  ? 63  HIS   A CG  1 
ATOM   1509 N ND1 . HIS   B 1 63  ? 5.177   -20.461 11.711 1.00 48.00  ? 63  HIS   A ND1 1 
ATOM   1510 C CD2 . HIS   B 1 63  ? 5.774   -22.022 13.119 1.00 52.25  ? 63  HIS   A CD2 1 
ATOM   1511 C CE1 . HIS   B 1 63  ? 6.247   -21.052 11.208 1.00 48.84  ? 63  HIS   A CE1 1 
ATOM   1512 N NE2 . HIS   B 1 63  ? 6.631   -22.002 12.043 1.00 51.06  ? 63  HIS   A NE2 1 
ATOM   1513 N N   . VAL   B 1 64  ? 2.281   -23.539 14.137 1.00 40.20  ? 64  VAL   A N   1 
ATOM   1514 C CA  . VAL   B 1 64  ? 2.412   -24.996 13.991 1.00 37.79  ? 64  VAL   A CA  1 
ATOM   1515 C C   . VAL   B 1 64  ? 1.237   -25.572 13.201 1.00 46.51  ? 64  VAL   A C   1 
ATOM   1516 O O   . VAL   B 1 64  ? 1.404   -26.495 12.374 1.00 40.44  ? 64  VAL   A O   1 
ATOM   1517 C CB  . VAL   B 1 64  ? 2.530   -25.668 15.371 1.00 32.47  ? 64  VAL   A CB  1 
ATOM   1518 C CG1 . VAL   B 1 64  ? 2.370   -27.172 15.246 1.00 32.15  ? 64  VAL   A CG1 1 
ATOM   1519 C CG2 . VAL   B 1 64  ? 3.845   -25.315 16.023 1.00 32.10  ? 64  VAL   A CG2 1 
ATOM   1520 N N   . THR   B 1 65  ? 0.027   -25.043 13.450 1.00 38.46  ? 65  THR   A N   1 
ATOM   1521 C CA  . THR   B 1 65  ? -1.167  -25.519 12.752 1.00 44.59  ? 65  THR   A CA  1 
ATOM   1522 C C   . THR   B 1 65  ? -1.076  -25.236 11.259 1.00 47.90  ? 65  THR   A C   1 
ATOM   1523 O O   . THR   B 1 65  ? -1.378  -26.109 10.431 1.00 49.24  ? 65  THR   A O   1 
ATOM   1524 C CB  . THR   B 1 65  ? -2.427  -24.864 13.317 1.00 42.33  ? 65  THR   A CB  1 
ATOM   1525 O OG1 . THR   B 1 65  ? -2.506  -25.075 14.731 1.00 34.18  ? 65  THR   A OG1 1 
ATOM   1526 C CG2 . THR   B 1 65  ? -3.647  -25.472 12.665 1.00 44.87  ? 65  THR   A CG2 1 
ATOM   1527 N N   . ARG   B 1 66  ? -0.698  -24.009 10.897 1.00 49.25  ? 66  ARG   A N   1 
ATOM   1528 C CA  . ARG   B 1 66  ? -0.142  -23.784 9.567  1.00 51.63  ? 66  ARG   A CA  1 
ATOM   1529 C C   . ARG   B 1 66  ? 1.185   -24.535 9.484  1.00 58.98  ? 66  ARG   A C   1 
ATOM   1530 O O   . ARG   B 1 66  ? 1.748   -24.921 10.501 1.00 72.49  ? 66  ARG   A O   1 
ATOM   1531 C CB  . ARG   B 1 66  ? 0.026   -22.283 9.312  1.00 45.07  ? 66  ARG   A CB  1 
ATOM   1532 C CG  . ARG   B 1 66  ? -1.324  -21.561 9.310  1.00 49.19  ? 66  ARG   A CG  1 
ATOM   1533 C CD  . ARG   B 1 66  ? -1.240  -20.045 9.403  1.00 48.14  ? 66  ARG   A CD  1 
ATOM   1534 N NE  . ARG   B 1 66  ? -2.546  -19.508 9.771  1.00 48.43  ? 66  ARG   A NE  1 
ATOM   1535 C CZ  . ARG   B 1 66  ? -2.765  -18.266 10.192 1.00 52.52  ? 66  ARG   A CZ  1 
ATOM   1536 N NH1 . ARG   B 1 66  ? -1.755  -17.409 10.295 1.00 48.66  ? 66  ARG   A NH1 1 
ATOM   1537 N NH2 . ARG   B 1 66  ? -3.999  -17.887 10.523 1.00 47.20  ? 66  ARG   A NH2 1 
ATOM   1538 N N   . SER   B 1 67  ? 1.661   -24.797 8.271  1.00 68.67  ? 67  SER   A N   1 
ATOM   1539 C CA  . SER   B 1 67  ? 2.860   -25.621 8.075  1.00 70.27  ? 67  SER   A CA  1 
ATOM   1540 C C   . SER   B 1 67  ? 2.597   -27.107 8.324  1.00 68.73  ? 67  SER   A C   1 
ATOM   1541 O O   . SER   B 1 67  ? 3.072   -27.929 7.533  1.00 72.30  ? 67  SER   A O   1 
ATOM   1542 C CB  . SER   B 1 67  ? 4.040   -25.171 8.950  1.00 64.53  ? 67  SER   A CB  1 
ATOM   1543 O OG  . SER   B 1 67  ? 3.924   -25.695 10.261 1.00 67.63  ? 67  SER   A OG  1 
ATOM   1544 N N   . ASN   B 1 68  ? 1.869   -27.499 9.391  1.00 68.50  ? 68  ASN   A N   1 
ATOM   1545 C CA  . ASN   B 1 68  ? 1.318   -28.856 9.331  1.00 70.80  ? 68  ASN   A CA  1 
ATOM   1546 C C   . ASN   B 1 68  ? 0.439   -29.022 8.092  1.00 67.89  ? 68  ASN   A C   1 
ATOM   1547 O O   . ASN   B 1 68  ? 0.321   -30.129 7.548  1.00 68.05  ? 68  ASN   A O   1 
ATOM   1548 C CB  . ASN   B 1 68  ? 0.535   -29.201 10.603 1.00 67.72  ? 68  ASN   A CB  1 
ATOM   1549 C CG  . ASN   B 1 68  ? 1.425   -29.780 11.709 1.00 64.73  ? 68  ASN   A CG  1 
ATOM   1550 O OD1 . ASN   B 1 68  ? 2.631   -29.977 11.522 1.00 57.40  ? 68  ASN   A OD1 1 
ATOM   1551 N ND2 . ASN   B 1 68  ? 0.824   -30.073 12.858 1.00 61.35  ? 68  ASN   A ND2 1 
ATOM   1552 N N   . LYS   B 1 69  ? -0.178  -27.925 7.640  1.00 64.78  ? 69  LYS   A N   1 
ATOM   1553 C CA  . LYS   B 1 69  ? -0.805  -27.808 6.321  1.00 64.69  ? 69  LYS   A CA  1 
ATOM   1554 C C   . LYS   B 1 69  ? -1.971  -28.773 6.134  1.00 64.53  ? 69  LYS   A C   1 
ATOM   1555 O O   . LYS   B 1 69  ? -2.286  -29.176 5.010  1.00 62.99  ? 69  LYS   A O   1 
ATOM   1556 C CB  . LYS   B 1 69  ? 0.222   -27.982 5.201  1.00 63.51  ? 69  LYS   A CB  1 
ATOM   1557 C CG  . LYS   B 1 69  ? 1.061   -26.740 4.960  1.00 69.32  ? 69  LYS   A CG  1 
ATOM   1558 C CD  . LYS   B 1 69  ? 1.984   -26.913 3.767  1.00 71.19  ? 69  LYS   A CD  1 
ATOM   1559 C CE  . LYS   B 1 69  ? 2.961   -25.758 3.661  1.00 72.34  ? 69  LYS   A CE  1 
ATOM   1560 N NZ  . LYS   B 1 69  ? 3.951   -25.981 2.574  1.00 69.87  ? 69  LYS   A NZ  1 
ATOM   1561 N N   . GLU   B 1 70  ? -2.635  -29.138 7.227  1.00 64.34  ? 70  GLU   A N   1 
ATOM   1562 C CA  . GLU   B 1 70  ? -3.869  -29.904 7.141  1.00 65.65  ? 70  GLU   A CA  1 
ATOM   1563 C C   . GLU   B 1 70  ? -5.110  -29.045 7.317  1.00 66.03  ? 70  GLU   A C   1 
ATOM   1564 O O   . GLU   B 1 70  ? -6.165  -29.388 6.774  1.00 75.06  ? 70  GLU   A O   1 
ATOM   1565 C CB  . GLU   B 1 70  ? -3.886  -31.014 8.198  1.00 65.99  ? 70  GLU   A CB  1 
ATOM   1566 C CG  . GLU   B 1 70  ? -3.063  -32.234 7.840  1.00 69.21  ? 70  GLU   A CG  1 
ATOM   1567 C CD  . GLU   B 1 70  ? -2.428  -32.891 9.058  1.00 72.07  ? 70  GLU   A CD  1 
ATOM   1568 O OE1 . GLU   B 1 70  ? -2.857  -32.609 10.202 1.00 71.26  ? 70  GLU   A OE1 1 
ATOM   1569 O OE2 . GLU   B 1 70  ? -1.484  -33.683 8.868  1.00 72.01  ? 70  GLU   A OE2 1 
ATOM   1570 N N   . TYR   B 1 71  ? -5.006  -27.931 8.045  1.00 54.92  ? 71  TYR   A N   1 
ATOM   1571 C CA  . TYR   B 1 71  ? -6.155  -27.138 8.455  1.00 52.75  ? 71  TYR   A CA  1 
ATOM   1572 C C   . TYR   B 1 71  ? -6.019  -25.685 8.016  1.00 55.22  ? 71  TYR   A C   1 
ATOM   1573 O O   . TYR   B 1 71  ? -4.920  -25.127 8.009  1.00 58.20  ? 71  TYR   A O   1 
ATOM   1574 C CB  . TYR   B 1 71  ? -6.320  -27.171 9.969  1.00 52.85  ? 71  TYR   A CB  1 
ATOM   1575 C CG  . TYR   B 1 71  ? -6.797  -28.473 10.556 1.00 43.16  ? 71  TYR   A CG  1 
ATOM   1576 C CD1 . TYR   B 1 71  ? -8.161  -28.755 10.641 1.00 43.55  ? 71  TYR   A CD1 1 
ATOM   1577 C CD2 . TYR   B 1 71  ? -5.889  -29.405 11.073 1.00 47.80  ? 71  TYR   A CD2 1 
ATOM   1578 C CE1 . TYR   B 1 71  ? -8.619  -29.941 11.203 1.00 40.04  ? 71  TYR   A CE1 1 
ATOM   1579 C CE2 . TYR   B 1 71  ? -6.330  -30.597 11.644 1.00 42.96  ? 71  TYR   A CE2 1 
ATOM   1580 C CZ  . TYR   B 1 71  ? -7.706  -30.860 11.708 1.00 43.75  ? 71  TYR   A CZ  1 
ATOM   1581 O OH  . TYR   B 1 71  ? -8.175  -32.027 12.278 1.00 36.44  ? 71  TYR   A OH  1 
ATOM   1582 N N   . LYS   B 1 72  ? -7.156  -25.062 7.686  1.00 57.56  ? 72  LYS   A N   1 
ATOM   1583 C CA  . LYS   B 1 72  ? -7.206  -23.653 7.286  1.00 60.52  ? 72  LYS   A CA  1 
ATOM   1584 C C   . LYS   B 1 72  ? -7.898  -22.862 8.394  1.00 58.55  ? 72  LYS   A C   1 
ATOM   1585 O O   . LYS   B 1 72  ? -9.122  -22.702 8.416  1.00 58.23  ? 72  LYS   A O   1 
ATOM   1586 C CB  . LYS   B 1 72  ? -7.871  -23.470 5.924  1.00 63.77  ? 72  LYS   A CB  1 
ATOM   1587 C CG  . LYS   B 1 72  ? -7.092  -24.155 4.798  1.00 70.82  ? 72  LYS   A CG  1 
ATOM   1588 C CD  . LYS   B 1 72  ? -7.168  -23.370 3.492  1.00 75.88  ? 72  LYS   A CD  1 
ATOM   1589 C CE  . LYS   B 1 72  ? -6.045  -23.784 2.536  1.00 78.57  ? 72  LYS   A CE  1 
ATOM   1590 N NZ  . LYS   B 1 72  ? -5.529  -22.653 1.707  1.00 79.21  ? 72  LYS   A NZ  1 
ATOM   1591 N N   . ILE   B 1 73  ? -7.070  -22.350 9.285  1.00 56.44  ? 73  ILE   A N   1 
ATOM   1592 C CA  . ILE   B 1 73  ? -7.396  -21.695 10.541 1.00 57.75  ? 73  ILE   A CA  1 
ATOM   1593 C C   . ILE   B 1 73  ? -7.116  -20.201 10.453 1.00 48.05  ? 73  ILE   A C   1 
ATOM   1594 O O   . ILE   B 1 73  ? -6.186  -19.762 9.773  1.00 49.63  ? 73  ILE   A O   1 
ATOM   1595 C CB  . ILE   B 1 73  ? -6.564  -22.354 11.668 1.00 53.68  ? 73  ILE   A CB  1 
ATOM   1596 C CG1 . ILE   B 1 73  ? -6.734  -21.609 12.993 1.00 56.28  ? 73  ILE   A CG1 1 
ATOM   1597 C CG2 . ILE   B 1 73  ? -5.124  -22.615 11.213 1.00 57.51  ? 73  ILE   A CG2 1 
ATOM   1598 C CD1 . ILE   B 1 73  ? -6.115  -22.276 14.172 1.00 53.05  ? 73  ILE   A CD1 1 
ATOM   1599 N N   . ARG   B 1 74  ? -7.935  -19.416 11.139 1.00 40.12  ? 74  ARG   A N   1 
ATOM   1600 C CA  . ARG   B 1 74  ? -7.640  -18.008 11.360 1.00 52.29  ? 74  ARG   A CA  1 
ATOM   1601 C C   . ARG   B 1 74  ? -7.320  -17.692 12.819 1.00 45.36  ? 74  ARG   A C   1 
ATOM   1602 O O   . ARG   B 1 74  ? -7.689  -18.426 13.742 1.00 39.40  ? 74  ARG   A O   1 
ATOM   1603 C CB  . ARG   B 1 74  ? -8.780  -17.138 10.834 1.00 52.86  ? 74  ARG   A CB  1 
ATOM   1604 C CG  . ARG   B 1 74  ? -10.151 -17.458 11.345 1.00 53.39  ? 74  ARG   A CG  1 
ATOM   1605 C CD  . ARG   B 1 74  ? -11.053 -16.492 10.589 1.00 64.29  ? 74  ARG   A CD  1 
ATOM   1606 N NE  . ARG   B 1 74  ? -12.474 -16.760 10.703 1.00 79.92  ? 74  ARG   A NE  1 
ATOM   1607 C CZ  . ARG   B 1 74  ? -13.412 -15.970 10.177 1.00 84.14  ? 74  ARG   A CZ  1 
ATOM   1608 N NH1 . ARG   B 1 74  ? -13.074 -14.810 9.591  1.00 75.26  ? 74  ARG   A NH1 1 
ATOM   1609 N NH2 . ARG   B 1 74  ? -14.701 -16.299 10.294 1.00 84.03  ? 74  ARG   A NH2 1 
ATOM   1610 N N   . ASP   B 1 75  ? -6.584  -16.582 12.983 1.00 42.89  ? 75  ASP   A N   1 
ATOM   1611 C CA  . ASP   B 1 75  ? -5.947  -16.201 14.240 1.00 40.91  ? 75  ASP   A CA  1 
ATOM   1612 C C   . ASP   B 1 75  ? -6.840  -16.459 15.442 1.00 38.29  ? 75  ASP   A C   1 
ATOM   1613 O O   . ASP   B 1 75  ? -6.459  -17.163 16.385 1.00 36.17  ? 75  ASP   A O   1 
ATOM   1614 C CB  . ASP   B 1 75  ? -5.543  -14.715 14.205 1.00 47.31  ? 75  ASP   A CB  1 
ATOM   1615 C CG  . ASP   B 1 75  ? -4.301  -14.446 13.348 1.00 51.33  ? 75  ASP   A CG  1 
ATOM   1616 O OD1 . ASP   B 1 75  ? -3.749  -15.408 12.762 1.00 39.94  ? 75  ASP   A OD1 1 
ATOM   1617 O OD2 . ASP   B 1 75  ? -3.878  -13.261 13.278 1.00 45.54  ? 75  ASP   A OD2 1 
ATOM   1618 N N   . ASN   B 1 76  ? -8.052  -15.928 15.399 1.00 29.02  ? 76  ASN   A N   1 
ATOM   1619 C CA  . ASN   B 1 76  ? -8.908  -15.998 16.568 1.00 35.98  ? 76  ASN   A CA  1 
ATOM   1620 C C   . ASN   B 1 76  ? -9.496  -17.385 16.801 1.00 33.09  ? 76  ASN   A C   1 
ATOM   1621 O O   . ASN   B 1 76  ? -10.276 -17.541 17.748 1.00 35.81  ? 76  ASN   A O   1 
ATOM   1622 C CB  . ASN   B 1 76  ? -9.996  -14.940 16.437 1.00 39.84  ? 76  ASN   A CB  1 
ATOM   1623 C CG  . ASN   B 1 76  ? -9.410  -13.567 16.180 1.00 50.09  ? 76  ASN   A CG  1 
ATOM   1624 O OD1 . ASN   B 1 76  ? -8.965  -12.883 17.104 1.00 40.64  ? 76  ASN   A OD1 1 
ATOM   1625 N ND2 . ASN   B 1 76  ? -9.344  -13.185 14.905 1.00 58.67  ? 76  ASN   A ND2 1 
ATOM   1626 N N   . ASP   B 1 77  ? -9.124  -18.396 16.008 1.00 25.12  ? 77  ASP   A N   1 
ATOM   1627 C CA  . ASP   B 1 77  ? -9.497  -19.771 16.320 1.00 33.11  ? 77  ASP   A CA  1 
ATOM   1628 C C   . ASP   B 1 77  ? -8.602  -20.389 17.389 1.00 37.21  ? 77  ASP   A C   1 
ATOM   1629 O O   . ASP   B 1 77  ? -8.707  -21.599 17.639 1.00 31.21  ? 77  ASP   A O   1 
ATOM   1630 C CB  . ASP   B 1 77  ? -9.462  -20.639 15.057 1.00 34.45  ? 77  ASP   A CB  1 
ATOM   1631 C CG  . ASP   B 1 77  ? -10.460 -20.176 13.991 1.00 50.10  ? 77  ASP   A CG  1 
ATOM   1632 O OD1 . ASP   B 1 77  ? -11.504 -19.580 14.349 1.00 44.64  ? 77  ASP   A OD1 1 
ATOM   1633 O OD2 . ASP   B 1 77  ? -10.206 -20.426 12.784 1.00 57.95  ? 77  ASP   A OD2 1 
ATOM   1634 N N   . VAL   B 1 78  ? -7.720  -19.596 17.999 1.00 27.66  ? 78  VAL   A N   1 
ATOM   1635 C CA  . VAL   B 1 78  ? -6.797  -20.053 19.029 1.00 26.14  ? 78  VAL   A CA  1 
ATOM   1636 C C   . VAL   B 1 78  ? -6.967  -19.160 20.245 1.00 21.40  ? 78  VAL   A C   1 
ATOM   1637 O O   . VAL   B 1 78  ? -6.756  -17.944 20.169 1.00 22.94  ? 78  VAL   A O   1 
ATOM   1638 C CB  . VAL   B 1 78  ? -5.335  -20.023 18.565 1.00 27.36  ? 78  VAL   A CB  1 
ATOM   1639 C CG1 . VAL   B 1 78  ? -4.444  -20.602 19.669 1.00 24.28  ? 78  VAL   A CG1 1 
ATOM   1640 C CG2 . VAL   B 1 78  ? -5.164  -20.785 17.276 1.00 33.58  ? 78  VAL   A CG2 1 
ATOM   1641 N N   . GLU   B 1 79  ? -7.336  -19.762 21.359 1.00 22.10  ? 79  GLU   A N   1 
ATOM   1642 C CA  . GLU   B 1 79  ? -7.383  -19.086 22.643 1.00 22.75  ? 79  GLU   A CA  1 
ATOM   1643 C C   . GLU   B 1 79  ? -6.466  -19.824 23.600 1.00 20.19  ? 79  GLU   A C   1 
ATOM   1644 O O   . GLU   B 1 79  ? -6.439  -21.055 23.608 1.00 20.43  ? 79  GLU   A O   1 
ATOM   1645 C CB  . GLU   B 1 79  ? -8.798  -19.062 23.203 1.00 24.15  ? 79  GLU   A CB  1 
ATOM   1646 C CG  . GLU   B 1 79  ? -8.865  -18.488 24.601 1.00 29.73  ? 79  GLU   A CG  1 
ATOM   1647 C CD  . GLU   B 1 79  ? -10.181 -18.787 25.283 1.00 46.16  ? 79  GLU   A CD  1 
ATOM   1648 O OE1 . GLU   B 1 79  ? -10.162 -19.251 26.461 1.00 39.05  ? 79  GLU   A OE1 1 
ATOM   1649 O OE2 . GLU   B 1 79  ? -11.235 -18.541 24.639 1.00 47.34  ? 79  GLU   A OE2 1 
ATOM   1650 N N   . VAL   B 1 80  ? -5.693  -19.080 24.383 1.00 16.83  ? 80  VAL   A N   1 
ATOM   1651 C CA  . VAL   B 1 80  ? -4.890  -19.653 25.456 1.00 16.62  ? 80  VAL   A CA  1 
ATOM   1652 C C   . VAL   B 1 80  ? -5.277  -18.938 26.742 1.00 17.80  ? 80  VAL   A C   1 
ATOM   1653 O O   . VAL   B 1 80  ? -5.247  -17.704 26.811 1.00 17.71  ? 80  VAL   A O   1 
ATOM   1654 C CB  . VAL   B 1 80  ? -3.379  -19.528 25.192 1.00 18.81  ? 80  VAL   A CB  1 
ATOM   1655 C CG1 . VAL   B 1 80  ? -2.585  -20.092 26.388 1.00 15.94  ? 80  VAL   A CG1 1 
ATOM   1656 C CG2 . VAL   B 1 80  ? -3.008  -20.244 23.920 1.00 16.87  ? 80  VAL   A CG2 1 
ATOM   1657 N N   . LEU   B 1 81  ? -5.661  -19.708 27.742 1.00 17.81  ? 81  LEU   A N   1 
ATOM   1658 C CA  . LEU   B 1 81  ? -5.937  -19.209 29.079 1.00 18.00  ? 81  LEU   A CA  1 
ATOM   1659 C C   . LEU   B 1 81  ? -4.805  -19.709 29.953 1.00 21.64  ? 81  LEU   A C   1 
ATOM   1660 O O   . LEU   B 1 81  ? -4.693  -20.915 30.194 1.00 16.62  ? 81  LEU   A O   1 
ATOM   1661 C CB  . LEU   B 1 81  ? -7.279  -19.707 29.609 1.00 17.08  ? 81  LEU   A CB  1 
ATOM   1662 C CG  . LEU   B 1 81  ? -7.623  -19.151 30.996 1.00 22.00  ? 81  LEU   A CG  1 
ATOM   1663 C CD1 . LEU   B 1 81  ? -7.891  -17.666 30.942 1.00 21.22  ? 81  LEU   A CD1 1 
ATOM   1664 C CD2 . LEU   B 1 81  ? -8.822  -19.886 31.608 1.00 25.40  ? 81  LEU   A CD2 1 
ATOM   1665 N N   . SER   B 1 82  ? -3.967  -18.791 30.420 1.00 13.83  ? 82  SER   A N   1 
ATOM   1666 C CA  . SER   B 1 82  ? -2.886  -19.150 31.313 1.00 13.83  ? 82  SER   A CA  1 
ATOM   1667 C C   . SER   B 1 82  ? -3.304  -18.855 32.750 1.00 16.79  ? 82  SER   A C   1 
ATOM   1668 O O   . SER   B 1 82  ? -3.928  -17.824 33.027 1.00 18.08  ? 82  SER   A O   1 
ATOM   1669 C CB  . SER   B 1 82  ? -1.602  -18.391 30.951 1.00 14.92  ? 82  SER   A CB  1 
ATOM   1670 O OG  . SER   B 1 82  ? -1.853  -16.998 30.853 1.00 21.31  ? 82  SER   A OG  1 
ATOM   1671 N N   . THR   B 1 83  ? -2.973  -19.781 33.650 1.00 15.41  ? 83  THR   A N   1 
ATOM   1672 C CA  . THR   B 1 83  ? -3.073  -19.615 35.088 1.00 14.60  ? 83  THR   A CA  1 
ATOM   1673 C C   . THR   B 1 83  ? -1.650  -19.615 35.626 1.00 21.01  ? 83  THR   A C   1 
ATOM   1674 O O   . THR   B 1 83  ? -0.933  -20.614 35.470 1.00 12.64  ? 83  THR   A O   1 
ATOM   1675 C CB  . THR   B 1 83  ? -3.876  -20.752 35.728 1.00 18.57  ? 83  THR   A CB  1 
ATOM   1676 O OG1 . THR   B 1 83  ? -5.178  -20.835 35.124 1.00 17.64  ? 83  THR   A OG1 1 
ATOM   1677 C CG2 . THR   B 1 83  ? -4.027  -20.496 37.215 1.00 21.35  ? 83  THR   A CG2 1 
ATOM   1678 N N   . VAL   B 1 84  ? -1.238  -18.500 36.234 1.00 13.25  ? 84  VAL   A N   1 
ATOM   1679 C CA  . VAL   B 1 84  ? 0.100   -18.351 36.793 1.00 11.23  ? 84  VAL   A CA  1 
ATOM   1680 C C   . VAL   B 1 84  ? -0.036  -18.061 38.279 1.00 11.49  ? 84  VAL   A C   1 
ATOM   1681 O O   . VAL   B 1 84  ? -0.787  -17.161 38.676 1.00 11.31  ? 84  VAL   A O   1 
ATOM   1682 C CB  . VAL   B 1 84  ? 0.906   -17.242 36.089 1.00 9.17   ? 84  VAL   A CB  1 
ATOM   1683 C CG1 . VAL   B 1 84  ? 2.217   -16.992 36.848 1.00 11.19  ? 84  VAL   A CG1 1 
ATOM   1684 C CG2 . VAL   B 1 84  ? 1.200   -17.614 34.630 1.00 11.93  ? 84  VAL   A CG2 1 
ATOM   1685 N N   . GLY   B 1 85  ? 0.668   -18.838 39.086 1.00 10.79  ? 85  GLY   A N   1 
ATOM   1686 C CA  . GLY   B 1 85  ? 0.682   -18.644 40.515 1.00 14.10  ? 85  GLY   A CA  1 
ATOM   1687 C C   . GLY   B 1 85  ? 2.084   -18.462 41.064 1.00 15.46  ? 85  GLY   A C   1 
ATOM   1688 O O   . GLY   B 1 85  ? 3.061   -18.827 40.412 1.00 15.44  ? 85  GLY   A O   1 
ATOM   1689 N N   . ILE   B 1 86  ? 2.198   -17.887 42.259 1.00 15.21  ? 86  ILE   A N   1 
ATOM   1690 C CA  . ILE   B 1 86  ? 3.480   -17.687 42.920 1.00 15.76  ? 86  ILE   A CA  1 
ATOM   1691 C C   . ILE   B 1 86  ? 3.447   -18.399 44.263 1.00 18.92  ? 86  ILE   A C   1 
ATOM   1692 O O   . ILE   B 1 86  ? 2.471   -18.273 45.015 1.00 16.62  ? 86  ILE   A O   1 
ATOM   1693 C CB  . ILE   B 1 86  ? 3.837   -16.193 43.068 1.00 14.60  ? 86  ILE   A CB  1 
ATOM   1694 C CG1 . ILE   B 1 86  ? 5.206   -16.064 43.747 1.00 19.44  ? 86  ILE   A CG1 1 
ATOM   1695 C CG2 . ILE   B 1 86  ? 2.756   -15.404 43.772 1.00 19.91  ? 86  ILE   A CG2 1 
ATOM   1696 C CD1 . ILE   B 1 86  ? 5.826   -14.698 43.644 1.00 20.96  ? 86  ILE   A CD1 1 
ATOM   1697 N N   . VAL   B 1 87  ? 4.509   -19.161 44.545 1.00 14.90  ? 87  VAL   A N   1 
ATOM   1698 C CA  . VAL   B 1 87  ? 4.607   -19.997 45.739 1.00 17.20  ? 87  VAL   A CA  1 
ATOM   1699 C C   . VAL   B 1 87  ? 6.028   -19.914 46.290 1.00 21.70  ? 87  VAL   A C   1 
ATOM   1700 O O   . VAL   B 1 87  ? 6.989   -19.735 45.541 1.00 19.62  ? 87  VAL   A O   1 
ATOM   1701 C CB  . VAL   B 1 87  ? 4.248   -21.466 45.415 1.00 20.62  ? 87  VAL   A CB  1 
ATOM   1702 C CG1 . VAL   B 1 87  ? 5.186   -22.034 44.342 1.00 15.91  ? 87  VAL   A CG1 1 
ATOM   1703 C CG2 . VAL   B 1 87  ? 4.285   -22.319 46.673 1.00 30.92  ? 87  VAL   A CG2 1 
ATOM   1704 N N   . ALA   B 1 88  ? 6.175   -20.052 47.606 1.00 20.26  ? 88  ALA   A N   1 
ATOM   1705 C CA  . ALA   B 1 88  ? 7.510   -20.156 48.183 1.00 19.19  ? 88  ALA   A CA  1 
ATOM   1706 C C   . ALA   B 1 88  ? 8.145   -21.489 47.795 1.00 25.21  ? 88  ALA   A C   1 
ATOM   1707 O O   . ALA   B 1 88  ? 7.468   -22.528 47.757 1.00 19.30  ? 88  ALA   A O   1 
ATOM   1708 C CB  . ALA   B 1 88  ? 7.445   -20.013 49.707 1.00 24.35  ? 88  ALA   A CB  1 
ATOM   1709 N N   . ASN   B 1 89  ? 9.451   -21.464 47.488 1.00 16.70  ? 89  ASN   A N   1 
ATOM   1710 C CA  . ASN   B 1 89  ? 10.095  -22.646 46.911 1.00 17.58  ? 89  ASN   A CA  1 
ATOM   1711 C C   . ASN   B 1 89  ? 10.762  -23.555 47.935 1.00 26.76  ? 89  ASN   A C   1 
ATOM   1712 O O   . ASN   B 1 89  ? 11.428  -24.522 47.536 1.00 34.05  ? 89  ASN   A O   1 
ATOM   1713 C CB  . ASN   B 1 89  ? 11.126  -22.255 45.819 1.00 14.05  ? 89  ASN   A CB  1 
ATOM   1714 C CG  . ASN   B 1 89  ? 12.289  -21.398 46.335 1.00 18.33  ? 89  ASN   A CG  1 
ATOM   1715 O OD1 . ASN   B 1 89  ? 12.456  -21.188 47.536 1.00 20.73  ? 89  ASN   A OD1 1 
ATOM   1716 N ND2 . ASN   B 1 89  ? 13.106  -20.905 45.408 1.00 17.01  ? 89  ASN   A ND2 1 
ATOM   1717 N N   . GLY   B 1 90  ? 10.598  -23.286 49.230 1.00 28.16  ? 90  GLY   A N   1 
ATOM   1718 C CA  . GLY   B 1 90  ? 11.253  -24.075 50.247 1.00 30.60  ? 90  GLY   A CA  1 
ATOM   1719 C C   . GLY   B 1 90  ? 12.724  -23.776 50.458 1.00 32.24  ? 90  GLY   A C   1 
ATOM   1720 O O   . GLY   B 1 90  ? 13.354  -24.443 51.284 1.00 31.23  ? 90  GLY   A O   1 
ATOM   1721 N N   . ASN   B 1 91  ? 13.290  -22.793 49.752 1.00 30.42  ? 91  ASN   A N   1 
ATOM   1722 C CA  . ASN   B 1 91  ? 14.709  -22.437 49.830 1.00 30.59  ? 91  ASN   A CA  1 
ATOM   1723 C C   . ASN   B 1 91  ? 14.884  -20.920 49.896 1.00 29.62  ? 91  ASN   A C   1 
ATOM   1724 O O   . ASN   B 1 91  ? 15.776  -20.344 49.262 1.00 29.42  ? 91  ASN   A O   1 
ATOM   1725 C CB  . ASN   B 1 91  ? 15.482  -23.045 48.653 1.00 29.47  ? 91  ASN   A CB  1 
ATOM   1726 C CG  . ASN   B 1 91  ? 17.003  -22.994 48.844 1.00 43.44  ? 91  ASN   A CG  1 
ATOM   1727 O OD1 . ASN   B 1 91  ? 17.509  -22.913 49.974 1.00 35.78  ? 91  ASN   A OD1 1 
ATOM   1728 N ND2 . ASN   B 1 91  ? 17.739  -23.032 47.725 1.00 42.52  ? 91  ASN   A ND2 1 
ATOM   1729 N N   . GLY   B 1 92  ? 14.016  -20.252 50.657 1.00 27.83  ? 92  GLY   A N   1 
ATOM   1730 C CA  . GLY   B 1 92  ? 14.138  -18.819 50.886 1.00 29.40  ? 92  GLY   A CA  1 
ATOM   1731 C C   . GLY   B 1 92  ? 13.833  -17.940 49.687 1.00 27.00  ? 92  GLY   A C   1 
ATOM   1732 O O   . GLY   B 1 92  ? 14.310  -16.800 49.624 1.00 23.74  ? 92  GLY   A O   1 
ATOM   1733 N N   . GLY   B 1 93  ? 13.055  -18.435 48.729 1.00 17.87  ? 93  GLY   A N   1 
ATOM   1734 C CA  . GLY   B 1 93  ? 12.708  -17.649 47.557 1.00 16.80  ? 93  GLY   A CA  1 
ATOM   1735 C C   . GLY   B 1 93  ? 11.365  -18.086 47.022 1.00 18.24  ? 93  GLY   A C   1 
ATOM   1736 O O   . GLY   B 1 93  ? 10.659  -18.829 47.711 1.00 16.58  ? 93  GLY   A O   1 
ATOM   1737 N N   . PHE   B 1 94  ? 11.002  -17.672 45.804 1.00 15.98  ? 94  PHE   A N   1 
ATOM   1738 C CA  . PHE   B 1 94  ? 9.697   -17.995 45.240 1.00 16.36  ? 94  PHE   A CA  1 
ATOM   1739 C C   . PHE   B 1 94  ? 9.844   -18.638 43.866 1.00 13.80  ? 94  PHE   A C   1 
ATOM   1740 O O   . PHE   B 1 94  ? 10.877  -18.509 43.216 1.00 15.69  ? 94  PHE   A O   1 
ATOM   1741 C CB  . PHE   B 1 94  ? 8.836   -16.738 45.187 1.00 15.80  ? 94  PHE   A CB  1 
ATOM   1742 C CG  . PHE   B 1 94  ? 8.629   -16.121 46.545 1.00 20.09  ? 94  PHE   A CG  1 
ATOM   1743 C CD1 . PHE   B 1 94  ? 7.572   -16.524 47.356 1.00 18.07  ? 94  PHE   A CD1 1 
ATOM   1744 C CD2 . PHE   B 1 94  ? 9.542   -15.217 47.046 1.00 19.46  ? 94  PHE   A CD2 1 
ATOM   1745 C CE1 . PHE   B 1 94  ? 7.399   -15.981 48.630 1.00 23.49  ? 94  PHE   A CE1 1 
ATOM   1746 C CE2 . PHE   B 1 94  ? 9.388   -14.675 48.332 1.00 25.50  ? 94  PHE   A CE2 1 
ATOM   1747 C CZ  . PHE   B 1 94  ? 8.302   -15.051 49.118 1.00 23.46  ? 94  PHE   A CZ  1 
ATOM   1748 N N   . ALA   B 1 95  ? 8.832   -19.403 43.478 1.00 14.57  ? 95  ALA   A N   1 
ATOM   1749 C CA  . ALA   B 1 95  ? 8.707   -20.038 42.176 1.00 16.68  ? 95  ALA   A CA  1 
ATOM   1750 C C   . ALA   B 1 95  ? 7.352   -19.676 41.568 1.00 15.93  ? 95  ALA   A C   1 
ATOM   1751 O O   . ALA   B 1 95  ? 6.401   -19.343 42.280 1.00 16.28  ? 95  ALA   A O   1 
ATOM   1752 C CB  . ALA   B 1 95  ? 8.840   -21.571 42.284 1.00 14.62  ? 95  ALA   A CB  1 
ATOM   1753 N N   . LEU   B 1 96  ? 7.276   -19.727 40.242 1.00 14.13  ? 96  LEU   A N   1 
ATOM   1754 C CA  . LEU   B 1 96  ? 6.002   -19.649 39.547 1.00 13.96  ? 96  LEU   A CA  1 
ATOM   1755 C C   . LEU   B 1 96  ? 5.472   -21.051 39.281 1.00 12.76  ? 96  LEU   A C   1 
ATOM   1756 O O   . LEU   B 1 96  ? 6.240   -22.003 39.124 1.00 11.24  ? 96  LEU   A O   1 
ATOM   1757 C CB  . LEU   B 1 96  ? 6.149   -18.896 38.228 1.00 12.24  ? 96  LEU   A CB  1 
ATOM   1758 C CG  . LEU   B 1 96  ? 6.654   -17.461 38.370 1.00 12.41  ? 96  LEU   A CG  1 
ATOM   1759 C CD1 . LEU   B 1 96  ? 6.752   -16.854 37.005 1.00 18.99  ? 96  LEU   A CD1 1 
ATOM   1760 C CD2 . LEU   B 1 96  ? 5.733   -16.601 39.262 1.00 19.21  ? 96  LEU   A CD2 1 
ATOM   1761 N N   . THR   B 1 97  ? 4.149   -21.166 39.255 1.00 11.81  ? 97  THR   A N   1 
ATOM   1762 C CA  . THR   B 1 97  ? 3.430   -22.307 38.681 1.00 13.52  ? 97  THR   A CA  1 
ATOM   1763 C C   . THR   B 1 97  ? 2.667   -21.837 37.444 1.00 14.23  ? 97  THR   A C   1 
ATOM   1764 O O   . THR   B 1 97  ? 2.167   -20.699 37.412 1.00 11.15  ? 97  THR   A O   1 
ATOM   1765 C CB  . THR   B 1 97  ? 2.447   -22.930 39.698 1.00 12.56  ? 97  THR   A CB  1 
ATOM   1766 O OG1 . THR   B 1 97  ? 1.468   -21.960 40.077 1.00 14.72  ? 97  THR   A OG1 1 
ATOM   1767 C CG2 . THR   B 1 97  ? 3.144   -23.350 40.954 1.00 14.12  ? 97  THR   A CG2 1 
ATOM   1768 N N   . VAL   B 1 98  ? 2.567   -22.708 36.427 1.00 13.08  ? 98  VAL   A N   1 
ATOM   1769 C CA  . VAL   B 1 98  ? 1.899   -22.345 35.178 1.00 15.11  ? 98  VAL   A CA  1 
ATOM   1770 C C   . VAL   B 1 98  ? 0.984   -23.485 34.728 1.00 18.61  ? 98  VAL   A C   1 
ATOM   1771 O O   . VAL   B 1 98  ? 1.395   -24.651 34.687 1.00 13.55  ? 98  VAL   A O   1 
ATOM   1772 C CB  . VAL   B 1 98  ? 2.881   -22.002 34.039 1.00 19.49  ? 98  VAL   A CB  1 
ATOM   1773 C CG1 . VAL   B 1 98  ? 2.084   -21.527 32.827 1.00 13.02  ? 98  VAL   A CG1 1 
ATOM   1774 C CG2 . VAL   B 1 98  ? 3.950   -20.954 34.451 1.00 11.23  ? 98  VAL   A CG2 1 
ATOM   1775 N N   . HIS   B 1 99  ? -0.254  -23.146 34.395 1.00 14.93  ? 99  HIS   A N   1 
ATOM   1776 C CA  . HIS   B 1 99  ? -1.165  -24.056 33.713 1.00 17.86  ? 99  HIS   A CA  1 
ATOM   1777 C C   . HIS   B 1 99  ? -1.687  -23.359 32.466 1.00 12.38  ? 99  HIS   A C   1 
ATOM   1778 O O   . HIS   B 1 99  ? -1.944  -22.154 32.481 1.00 15.69  ? 99  HIS   A O   1 
ATOM   1779 C CB  . HIS   B 1 99  ? -2.330  -24.490 34.623 1.00 18.99  ? 99  HIS   A CB  1 
ATOM   1780 C CG  . HIS   B 1 99  ? -3.313  -25.385 33.932 1.00 19.42  ? 99  HIS   A CG  1 
ATOM   1781 N ND1 . HIS   B 1 99  ? -3.132  -26.748 33.821 1.00 16.19  ? 99  HIS   A ND1 1 
ATOM   1782 C CD2 . HIS   B 1 99  ? -4.453  -25.101 33.263 1.00 19.02  ? 99  HIS   A CD2 1 
ATOM   1783 C CE1 . HIS   B 1 99  ? -4.130  -27.266 33.126 1.00 27.55  ? 99  HIS   A CE1 1 
ATOM   1784 N NE2 . HIS   B 1 99  ? -4.948  -26.288 32.779 1.00 23.99  ? 99  HIS   A NE2 1 
ATOM   1785 N N   . LEU   B 1 100 ? -1.811  -24.097 31.375 1.00 14.76  ? 100 LEU   A N   1 
ATOM   1786 C CA  . LEU   B 1 100 ? -2.368  -23.563 30.135 1.00 20.46  ? 100 LEU   A CA  1 
ATOM   1787 C C   . LEU   B 1 100 ? -3.611  -24.376 29.741 1.00 19.48  ? 100 LEU   A C   1 
ATOM   1788 O O   . LEU   B 1 100 ? -3.538  -25.598 29.616 1.00 18.81  ? 100 LEU   A O   1 
ATOM   1789 C CB  . LEU   B 1 100 ? -1.334  -23.604 29.015 1.00 16.36  ? 100 LEU   A CB  1 
ATOM   1790 C CG  . LEU   B 1 100 ? 0.017   -22.894 29.178 1.00 22.51  ? 100 LEU   A CG  1 
ATOM   1791 C CD1 . LEU   B 1 100 ? 0.831   -23.189 27.940 1.00 13.82  ? 100 LEU   A CD1 1 
ATOM   1792 C CD2 . LEU   B 1 100 ? -0.103  -21.373 29.411 1.00 19.20  ? 100 LEU   A CD2 1 
ATOM   1793 N N   . ASP   B 1 101 ? -4.745  -23.700 29.573 1.00 17.96  ? 101 ASP   A N   1 
ATOM   1794 C CA  . ASP   B 1 101 ? -5.899  -24.249 28.865 1.00 19.75  ? 101 ASP   A CA  1 
ATOM   1795 C C   . ASP   B 1 101 ? -5.853  -23.708 27.436 1.00 16.16  ? 101 ASP   A C   1 
ATOM   1796 O O   . ASP   B 1 101 ? -5.971  -22.503 27.217 1.00 19.16  ? 101 ASP   A O   1 
ATOM   1797 C CB  . ASP   B 1 101 ? -7.207  -23.862 29.560 1.00 23.03  ? 101 ASP   A CB  1 
ATOM   1798 C CG  . ASP   B 1 101 ? -7.330  -24.453 30.970 1.00 28.94  ? 101 ASP   A CG  1 
ATOM   1799 O OD1 . ASP   B 1 101 ? -7.214  -25.688 31.103 1.00 27.37  ? 101 ASP   A OD1 1 
ATOM   1800 O OD2 . ASP   B 1 101 ? -7.525  -23.690 31.953 1.00 33.71  ? 101 ASP   A OD2 1 
ATOM   1801 N N   . VAL   B 1 102 ? -5.689  -24.590 26.462 1.00 19.53  ? 102 VAL   A N   1 
ATOM   1802 C CA  . VAL   B 1 102 ? -5.577  -24.201 25.063 1.00 17.55  ? 102 VAL   A CA  1 
ATOM   1803 C C   . VAL   B 1 102 ? -6.825  -24.665 24.323 1.00 18.93  ? 102 VAL   A C   1 
ATOM   1804 O O   . VAL   B 1 102 ? -7.139  -25.860 24.308 1.00 18.12  ? 102 VAL   A O   1 
ATOM   1805 C CB  . VAL   B 1 102 ? -4.316  -24.782 24.419 1.00 22.41  ? 102 VAL   A CB  1 
ATOM   1806 C CG1 . VAL   B 1 102 ? -4.209  -24.300 22.996 1.00 16.42  ? 102 VAL   A CG1 1 
ATOM   1807 C CG2 . VAL   B 1 102 ? -3.064  -24.372 25.236 1.00 19.56  ? 102 VAL   A CG2 1 
ATOM   1808 N N   . THR   B 1 103 ? -7.517  -23.730 23.676 1.00 18.89  ? 103 THR   A N   1 
ATOM   1809 C CA  . THR   B 1 103 ? -8.740  -24.038 22.944 1.00 24.08  ? 103 THR   A CA  1 
ATOM   1810 C C   . THR   B 1 103 ? -8.535  -23.706 21.475 1.00 23.09  ? 103 THR   A C   1 
ATOM   1811 O O   . THR   B 1 103 ? -8.241  -22.556 21.121 1.00 23.27  ? 103 THR   A O   1 
ATOM   1812 C CB  . THR   B 1 103 ? -9.938  -23.268 23.497 1.00 23.12  ? 103 THR   A CB  1 
ATOM   1813 O OG1 . THR   B 1 103 ? -10.131 -23.622 24.867 1.00 26.40  ? 103 THR   A OG1 1 
ATOM   1814 C CG2 . THR   B 1 103 ? -11.207 -23.637 22.710 1.00 26.95  ? 103 THR   A CG2 1 
ATOM   1815 N N   . LEU   B 1 104 ? -8.702  -24.709 20.627 1.00 23.97  ? 104 LEU   A N   1 
ATOM   1816 C CA  . LEU   B 1 104 ? -8.578  -24.561 19.184 1.00 26.61  ? 104 LEU   A CA  1 
ATOM   1817 C C   . LEU   B 1 104 ? -9.948  -24.792 18.550 1.00 34.19  ? 104 LEU   A C   1 
ATOM   1818 O O   . LEU   B 1 104 ? -10.600 -25.801 18.838 1.00 23.14  ? 104 LEU   A O   1 
ATOM   1819 C CB  . LEU   B 1 104 ? -7.558  -25.562 18.630 1.00 20.17  ? 104 LEU   A CB  1 
ATOM   1820 C CG  . LEU   B 1 104 ? -6.140  -25.566 19.216 1.00 32.11  ? 104 LEU   A CG  1 
ATOM   1821 C CD1 . LEU   B 1 104 ? -5.165  -26.200 18.233 1.00 23.22  ? 104 LEU   A CD1 1 
ATOM   1822 C CD2 . LEU   B 1 104 ? -5.703  -24.147 19.560 1.00 27.80  ? 104 LEU   A CD2 1 
ATOM   1823 N N   . SER   B 1 105 ? -10.377 -23.871 17.687 1.00 28.93  ? 105 SER   A N   1 
ATOM   1824 C CA  . SER   B 1 105 ? -11.660 -24.001 17.009 1.00 35.97  ? 105 SER   A CA  1 
ATOM   1825 C C   . SER   B 1 105 ? -11.485 -24.719 15.679 1.00 30.36  ? 105 SER   A C   1 
ATOM   1826 O O   . SER   B 1 105 ? -10.572 -24.402 14.910 1.00 25.85  ? 105 SER   A O   1 
ATOM   1827 C CB  . SER   B 1 105 ? -12.299 -22.631 16.770 1.00 35.31  ? 105 SER   A CB  1 
ATOM   1828 O OG  . SER   B 1 105 ? -12.616 -22.008 17.994 1.00 35.56  ? 105 SER   A OG  1 
ATOM   1829 N N   . GLY   B 1 106 ? -12.359 -25.691 15.426 1.00 28.28  ? 106 GLY   A N   1 
ATOM   1830 C CA  . GLY   B 1 106 ? -12.455 -26.304 14.126 1.00 21.99  ? 106 GLY   A CA  1 
ATOM   1831 C C   . GLY   B 1 106 ? -11.449 -27.386 13.804 1.00 32.38  ? 106 GLY   A C   1 
ATOM   1832 O O   . GLY   B 1 106 ? -11.230 -27.658 12.618 1.00 28.24  ? 106 GLY   A O   1 
ATOM   1833 N N   . ILE   B 1 107 ? -10.816 -28.022 14.798 1.00 28.66  ? 107 ILE   A N   1 
ATOM   1834 C CA  . ILE   B 1 107 ? -9.986  -29.176 14.475 1.00 25.33  ? 107 ILE   A CA  1 
ATOM   1835 C C   . ILE   B 1 107 ? -10.297 -30.276 15.474 1.00 22.98  ? 107 ILE   A C   1 
ATOM   1836 O O   . ILE   B 1 107 ? -10.831 -30.027 16.563 1.00 23.29  ? 107 ILE   A O   1 
ATOM   1837 C CB  . ILE   B 1 107 ? -8.471  -28.886 14.477 1.00 37.33  ? 107 ILE   A CB  1 
ATOM   1838 C CG1 . ILE   B 1 107 ? -7.936  -28.748 15.867 1.00 33.73  ? 107 ILE   A CG1 1 
ATOM   1839 C CG2 . ILE   B 1 107 ? -8.160  -27.513 13.858 1.00 33.35  ? 107 ILE   A CG2 1 
ATOM   1840 C CD1 . ILE   B 1 107 ? -6.459  -28.735 15.805 1.00 42.92  ? 107 ILE   A CD1 1 
ATOM   1841 N N   . SER   B 1 108 ? -9.943  -31.506 15.103 1.00 24.40  ? 108 SER   A N   1 
ATOM   1842 C CA  . SER   B 1 108 ? -10.306 -32.638 15.939 1.00 26.32  ? 108 SER   A CA  1 
ATOM   1843 C C   . SER   B 1 108 ? -9.477  -32.638 17.217 1.00 24.40  ? 108 SER   A C   1 
ATOM   1844 O O   . SER   B 1 108 ? -8.452  -31.956 17.326 1.00 26.35  ? 108 SER   A O   1 
ATOM   1845 C CB  . SER   B 1 108 ? -10.134 -33.960 15.187 1.00 22.34  ? 108 SER   A CB  1 
ATOM   1846 O OG  . SER   B 1 108 ? -8.766  -34.244 14.910 1.00 22.79  ? 108 SER   A OG  1 
ATOM   1847 N N   . GLN   B 1 109 ? -9.963  -33.386 18.209 1.00 24.44  ? 109 GLN   A N   1 
ATOM   1848 C CA  . GLN   B 1 109 ? -9.312  -33.402 19.517 1.00 28.32  ? 109 GLN   A CA  1 
ATOM   1849 C C   . GLN   B 1 109 ? -7.901  -33.972 19.411 1.00 33.72  ? 109 GLN   A C   1 
ATOM   1850 O O   . GLN   B 1 109 ? -6.942  -33.388 19.946 1.00 22.91  ? 109 GLN   A O   1 
ATOM   1851 C CB  . GLN   B 1 109 ? -10.156 -34.200 20.517 1.00 17.79  ? 109 GLN   A CB  1 
ATOM   1852 C CG  . GLN   B 1 109 ? -9.651  -34.190 21.991 1.00 22.40  ? 109 GLN   A CG  1 
ATOM   1853 C CD  . GLN   B 1 109 ? -9.587  -32.782 22.613 1.00 24.82  ? 109 GLN   A CD  1 
ATOM   1854 O OE1 . GLN   B 1 109 ? -10.334 -31.883 22.234 1.00 23.57  ? 109 GLN   A OE1 1 
ATOM   1855 N NE2 . GLN   B 1 109 ? -8.713  -32.610 23.606 1.00 16.81  ? 109 GLN   A NE2 1 
ATOM   1856 N N   . ALA   B 1 110 ? -7.754  -35.097 18.689 1.00 25.46  ? 110 ALA   A N   1 
ATOM   1857 C CA  . ALA   B 1 110 ? -6.443  -35.721 18.516 1.00 23.35  ? 110 ALA   A CA  1 
ATOM   1858 C C   . ALA   B 1 110 ? -5.458  -34.777 17.832 1.00 27.42  ? 110 ALA   A C   1 
ATOM   1859 O O   . ALA   B 1 110 ? -4.328  -34.595 18.303 1.00 28.50  ? 110 ALA   A O   1 
ATOM   1860 C CB  . ALA   B 1 110 ? -6.572  -37.021 17.717 1.00 22.11  ? 110 ALA   A CB  1 
ATOM   1861 N N   . ASP   B 1 111 ? -5.864  -34.153 16.728 1.00 24.85  ? 111 ASP   A N   1 
ATOM   1862 C CA  . ASP   B 1 111 ? -4.939  -33.241 16.058 1.00 16.54  ? 111 ASP   A CA  1 
ATOM   1863 C C   . ASP   B 1 111 ? -4.593  -32.045 16.951 1.00 19.50  ? 111 ASP   A C   1 
ATOM   1864 O O   . ASP   B 1 111 ? -3.444  -31.593 16.974 1.00 19.13  ? 111 ASP   A O   1 
ATOM   1865 C CB  . ASP   B 1 111 ? -5.528  -32.750 14.736 1.00 22.97  ? 111 ASP   A CB  1 
ATOM   1866 C CG  . ASP   B 1 111 ? -5.680  -33.857 13.697 1.00 30.81  ? 111 ASP   A CG  1 
ATOM   1867 O OD1 . ASP   B 1 111 ? -5.057  -34.943 13.836 1.00 36.61  ? 111 ASP   A OD1 1 
ATOM   1868 O OD2 . ASP   B 1 111 ? -6.449  -33.636 12.740 1.00 29.49  ? 111 ASP   A OD2 1 
ATOM   1869 N N   . ALA   B 1 112 ? -5.577  -31.504 17.674 1.00 21.63  ? 112 ALA   A N   1 
ATOM   1870 C CA  . ALA   B 1 112 ? -5.313  -30.363 18.550 1.00 24.41  ? 112 ALA   A CA  1 
ATOM   1871 C C   . ALA   B 1 112 ? -4.265  -30.709 19.600 1.00 20.77  ? 112 ALA   A C   1 
ATOM   1872 O O   . ALA   B 1 112 ? -3.339  -29.925 19.859 1.00 22.88  ? 112 ALA   A O   1 
ATOM   1873 C CB  . ALA   B 1 112 ? -6.608  -29.904 19.213 1.00 19.67  ? 112 ALA   A CB  1 
ATOM   1874 N N   . GLU   B 1 113 ? -4.380  -31.901 20.193 1.00 21.65  ? 113 GLU   A N   1 
ATOM   1875 C CA  . GLU   B 1 113 ? -3.413  -32.342 21.202 1.00 27.48  ? 113 GLU   A CA  1 
ATOM   1876 C C   . GLU   B 1 113 ? -2.018  -32.513 20.599 1.00 23.78  ? 113 GLU   A C   1 
ATOM   1877 O O   . GLU   B 1 113 ? -1.008  -32.117 21.199 1.00 16.78  ? 113 GLU   A O   1 
ATOM   1878 C CB  . GLU   B 1 113 ? -3.899  -33.650 21.826 1.00 21.77  ? 113 GLU   A CB  1 
ATOM   1879 C CG  . GLU   B 1 113 ? -5.040  -33.492 22.831 1.00 27.27  ? 113 GLU   A CG  1 
ATOM   1880 C CD  . GLU   B 1 113 ? -5.568  -34.841 23.246 1.00 37.92  ? 113 GLU   A CD  1 
ATOM   1881 O OE1 . GLU   B 1 113 ? -6.747  -34.978 23.662 1.00 36.32  ? 113 GLU   A OE1 1 
ATOM   1882 O OE2 . GLU   B 1 113 ? -4.757  -35.785 23.148 1.00 53.82  ? 113 GLU   A OE2 1 
ATOM   1883 N N   . LYS   B 1 114 ? -1.945  -33.088 19.399 1.00 21.84  ? 114 LYS   A N   1 
ATOM   1884 C CA  . LYS   B 1 114 ? -0.635  -33.222 18.758 1.00 25.31  ? 114 LYS   A CA  1 
ATOM   1885 C C   . LYS   B 1 114 ? -0.009  -31.867 18.426 1.00 22.01  ? 114 LYS   A C   1 
ATOM   1886 O O   . LYS   B 1 114 ? 1.208   -31.684 18.583 1.00 23.26  ? 114 LYS   A O   1 
ATOM   1887 C CB  . LYS   B 1 114 ? -0.719  -34.076 17.503 1.00 27.08  ? 114 LYS   A CB  1 
ATOM   1888 C CG  . LYS   B 1 114 ? -0.591  -35.579 17.779 1.00 43.38  ? 114 LYS   A CG  1 
ATOM   1889 C CD  . LYS   B 1 114 ? -1.959  -36.139 18.335 1.00 48.55  ? 114 LYS   A CD  1 
ATOM   1890 C CE  . LYS   B 1 114 ? -1.995  -37.584 18.578 1.00 56.21  ? 114 LYS   A CE  1 
ATOM   1891 N NZ  . LYS   B 1 114 ? -3.257  -37.921 19.182 1.00 58.10  ? 114 LYS   A NZ  1 
ATOM   1892 N N   . ILE   B 1 115 ? -0.826  -30.911 17.983 1.00 19.56  ? 115 ILE   A N   1 
ATOM   1893 C CA  . ILE   B 1 115 ? -0.347  -29.559 17.697 1.00 19.25  ? 115 ILE   A CA  1 
ATOM   1894 C C   . ILE   B 1 115 ? 0.164   -28.880 18.967 1.00 22.26  ? 115 ILE   A C   1 
ATOM   1895 O O   . ILE   B 1 115 ? 1.200   -28.208 18.959 1.00 20.40  ? 115 ILE   A O   1 
ATOM   1896 C CB  . ILE   B 1 115 ? -1.463  -28.716 17.052 1.00 24.43  ? 115 ILE   A CB  1 
ATOM   1897 C CG1 . ILE   B 1 115 ? -1.668  -29.080 15.580 1.00 27.41  ? 115 ILE   A CG1 1 
ATOM   1898 C CG2 . ILE   B 1 115 ? -1.151  -27.206 17.173 1.00 20.85  ? 115 ILE   A CG2 1 
ATOM   1899 C CD1 . ILE   B 1 115 ? -2.974  -28.578 15.048 1.00 24.11  ? 115 ILE   A CD1 1 
ATOM   1900 N N   . VAL   B 1 116 ? -0.583  -28.985 20.064 1.00 18.16  ? 116 VAL   A N   1 
ATOM   1901 C CA  . VAL   B 1 116 ? -0.127  -28.344 21.296 1.00 19.23  ? 116 VAL   A CA  1 
ATOM   1902 C C   . VAL   B 1 116 ? 1.180   -28.979 21.775 1.00 20.26  ? 116 VAL   A C   1 
ATOM   1903 O O   . VAL   B 1 116 ? 2.101   -28.276 22.219 1.00 19.57  ? 116 VAL   A O   1 
ATOM   1904 C CB  . VAL   B 1 116 ? -1.233  -28.383 22.363 1.00 14.91  ? 116 VAL   A CB  1 
ATOM   1905 C CG1 . VAL   B 1 116 ? -0.695  -27.931 23.737 1.00 13.44  ? 116 VAL   A CG1 1 
ATOM   1906 C CG2 . VAL   B 1 116 ? -2.399  -27.452 21.931 1.00 12.85  ? 116 VAL   A CG2 1 
ATOM   1907 N N   . GLU   B 1 117 ? 1.306   -30.302 21.654 1.00 18.78  ? 117 GLU   A N   1 
ATOM   1908 C CA  . GLU   B 1 117 ? 2.570   -30.941 22.021 1.00 20.21  ? 117 GLU   A CA  1 
ATOM   1909 C C   . GLU   B 1 117 ? 3.726   -30.421 21.163 1.00 26.76  ? 117 GLU   A C   1 
ATOM   1910 O O   . GLU   B 1 117 ? 4.797   -30.089 21.682 1.00 29.76  ? 117 GLU   A O   1 
ATOM   1911 C CB  . GLU   B 1 117 ? 2.442   -32.464 21.921 1.00 26.63  ? 117 GLU   A CB  1 
ATOM   1912 C CG  . GLU   B 1 117 ? 3.648   -33.223 22.448 1.00 30.16  ? 117 GLU   A CG  1 
ATOM   1913 C CD  . GLU   B 1 117 ? 3.358   -34.701 22.733 1.00 48.36  ? 117 GLU   A CD  1 
ATOM   1914 O OE1 . GLU   B 1 117 ? 4.263   -35.550 22.498 1.00 53.03  ? 117 GLU   A OE1 1 
ATOM   1915 O OE2 . GLU   B 1 117 ? 2.238   -35.011 23.216 1.00 50.03  ? 117 GLU   A OE2 1 
ATOM   1916 N N   . GLN   B 1 118 ? 3.526   -30.316 19.845 1.00 20.27  ? 118 GLN   A N   1 
ATOM   1917 C CA  . GLN   B 1 118 ? 4.583   -29.754 19.004 1.00 19.93  ? 118 GLN   A CA  1 
ATOM   1918 C C   . GLN   B 1 118 ? 4.924   -28.336 19.421 1.00 28.41  ? 118 GLN   A C   1 
ATOM   1919 O O   . GLN   B 1 118 ? 6.102   -27.943 19.418 1.00 22.52  ? 118 GLN   A O   1 
ATOM   1920 C CB  . GLN   B 1 118 ? 4.178   -29.749 17.532 1.00 21.28  ? 118 GLN   A CB  1 
ATOM   1921 C CG  . GLN   B 1 118 ? 4.123   -31.109 16.863 1.00 24.84  ? 118 GLN   A CG  1 
ATOM   1922 C CD  . GLN   B 1 118 ? 3.507   -31.002 15.476 1.00 35.08  ? 118 GLN   A CD  1 
ATOM   1923 O OE1 . GLN   B 1 118 ? 2.355   -31.363 15.275 1.00 43.36  ? 118 GLN   A OE1 1 
ATOM   1924 N NE2 . GLN   B 1 118 ? 4.263   -30.468 14.528 1.00 29.43  ? 118 GLN   A NE2 1 
ATOM   1925 N N   . THR   B 1 119 ? 3.898   -27.541 19.745 1.00 19.96  ? 119 THR   A N   1 
ATOM   1926 C CA  . THR   B 1 119 ? 4.124   -26.142 20.080 1.00 23.27  ? 119 THR   A CA  1 
ATOM   1927 C C   . THR   B 1 119 ? 4.960   -26.009 21.344 1.00 23.78  ? 119 THR   A C   1 
ATOM   1928 O O   . THR   B 1 119 ? 5.795   -25.098 21.447 1.00 26.21  ? 119 THR   A O   1 
ATOM   1929 C CB  . THR   B 1 119 ? 2.793   -25.392 20.240 1.00 28.42  ? 119 THR   A CB  1 
ATOM   1930 O OG1 . THR   B 1 119 ? 1.952   -25.592 19.092 1.00 32.69  ? 119 THR   A OG1 1 
ATOM   1931 C CG2 . THR   B 1 119 ? 3.045   -23.912 20.400 1.00 32.67  ? 119 THR   A CG2 1 
ATOM   1932 N N   . HIS   B 1 120 ? 4.772   -26.908 22.313 1.00 21.52  ? 120 HIS   A N   1 
ATOM   1933 C CA  . HIS   B 1 120 ? 5.570   -26.781 23.536 1.00 27.05  ? 120 HIS   A CA  1 
ATOM   1934 C C   . HIS   B 1 120 ? 7.067   -26.874 23.261 1.00 28.06  ? 120 HIS   A C   1 
ATOM   1935 O O   . HIS   B 1 120 ? 7.868   -26.339 24.033 1.00 21.96  ? 120 HIS   A O   1 
ATOM   1936 C CB  . HIS   B 1 120 ? 5.158   -27.824 24.577 1.00 23.61  ? 120 HIS   A CB  1 
ATOM   1937 C CG  . HIS   B 1 120 ? 4.108   -27.331 25.528 1.00 29.53  ? 120 HIS   A CG  1 
ATOM   1938 N ND1 . HIS   B 1 120 ? 4.296   -26.225 26.335 1.00 21.98  ? 120 HIS   A ND1 1 
ATOM   1939 C CD2 . HIS   B 1 120 ? 2.852   -27.771 25.781 1.00 23.76  ? 120 HIS   A CD2 1 
ATOM   1940 C CE1 . HIS   B 1 120 ? 3.209   -26.015 27.054 1.00 22.21  ? 120 HIS   A CE1 1 
ATOM   1941 N NE2 . HIS   B 1 120 ? 2.317   -26.939 26.736 1.00 29.39  ? 120 HIS   A NE2 1 
ATOM   1942 N N   . GLN   B 1 121 ? 7.471   -27.521 22.161 1.00 25.16  ? 121 GLN   A N   1 
ATOM   1943 C CA  . GLN   B 1 121 ? 8.894   -27.573 21.852 1.00 23.99  ? 121 GLN   A CA  1 
ATOM   1944 C C   . GLN   B 1 121 ? 9.382   -26.341 21.118 1.00 25.13  ? 121 GLN   A C   1 
ATOM   1945 O O   . GLN   B 1 121 ? 10.598  -26.129 21.037 1.00 29.83  ? 121 GLN   A O   1 
ATOM   1946 C CB  . GLN   B 1 121 ? 9.251   -28.810 21.028 1.00 26.68  ? 121 GLN   A CB  1 
ATOM   1947 C CG  . GLN   B 1 121 ? 9.038   -30.091 21.781 1.00 34.00  ? 121 GLN   A CG  1 
ATOM   1948 C CD  . GLN   B 1 121 ? 9.744   -30.060 23.153 1.00 48.15  ? 121 GLN   A CD  1 
ATOM   1949 O OE1 . GLN   B 1 121 ? 9.079   -30.115 24.201 1.00 44.57  ? 121 GLN   A OE1 1 
ATOM   1950 N NE2 . GLN   B 1 121 ? 11.071  -29.870 23.150 1.00 41.26  ? 121 GLN   A NE2 1 
ATOM   1951 N N   . VAL   B 1 122 ? 8.468   -25.523 20.615 1.00 23.11  ? 122 VAL   A N   1 
ATOM   1952 C CA  . VAL   B 1 122 ? 8.797   -24.388 19.767 1.00 29.71  ? 122 VAL   A CA  1 
ATOM   1953 C C   . VAL   B 1 122 ? 8.764   -23.083 20.541 1.00 25.47  ? 122 VAL   A C   1 
ATOM   1954 O O   . VAL   B 1 122 ? 9.577   -22.192 20.291 1.00 26.64  ? 122 VAL   A O   1 
ATOM   1955 C CB  . VAL   B 1 122 ? 7.827   -24.338 18.566 1.00 26.97  ? 122 VAL   A CB  1 
ATOM   1956 C CG1 . VAL   B 1 122 ? 7.877   -22.969 17.881 1.00 42.32  ? 122 VAL   A CG1 1 
ATOM   1957 C CG2 . VAL   B 1 122 ? 8.147   -25.439 17.602 1.00 32.11  ? 122 VAL   A CG2 1 
ATOM   1958 N N   . CYS   B 1 123 ? 7.819   -22.962 21.457 1.00 26.57  ? 123 CYS   A N   1 
ATOM   1959 C CA  . CYS   B 1 123 ? 7.520   -21.669 22.056 1.00 29.71  ? 123 CYS   A CA  1 
ATOM   1960 C C   . CYS   B 1 123 ? 8.715   -21.199 22.881 1.00 21.38  ? 123 CYS   A C   1 
ATOM   1961 O O   . CYS   B 1 123 ? 9.229   -21.964 23.698 1.00 17.00  ? 123 CYS   A O   1 
ATOM   1962 C CB  . CYS   B 1 123 ? 6.263   -21.773 22.920 1.00 22.63  ? 123 CYS   A CB  1 
ATOM   1963 S SG  . CYS   B 1 123 ? 5.906   -20.322 23.889 1.00 27.13  ? 123 CYS   A SG  1 
ATOM   1964 N N   . PRO   B 1 124 ? 9.198   -19.974 22.665 1.00 21.13  ? 124 PRO   A N   1 
ATOM   1965 C CA  . PRO   B 1 124 ? 10.351  -19.485 23.448 1.00 20.93  ? 124 PRO   A CA  1 
ATOM   1966 C C   . PRO   B 1 124 ? 10.132  -19.550 24.952 1.00 21.41  ? 124 PRO   A C   1 
ATOM   1967 O O   . PRO   B 1 124 ? 11.066  -19.832 25.707 1.00 17.56  ? 124 PRO   A O   1 
ATOM   1968 C CB  . PRO   B 1 124 ? 10.488  -18.017 23.001 1.00 17.46  ? 124 PRO   A CB  1 
ATOM   1969 C CG  . PRO   B 1 124 ? 9.881   -17.948 21.684 1.00 28.79  ? 124 PRO   A CG  1 
ATOM   1970 C CD  . PRO   B 1 124 ? 8.785   -19.020 21.621 1.00 25.22  ? 124 PRO   A CD  1 
ATOM   1971 N N   . TYR   B 1 125 ? 8.914   -19.274 25.413 1.00 13.81  ? 125 TYR   A N   1 
ATOM   1972 C CA  . TYR   B 1 125 ? 8.668   -19.208 26.849 1.00 21.80  ? 125 TYR   A CA  1 
ATOM   1973 C C   . TYR   B 1 125 ? 8.647   -20.608 27.452 1.00 14.63  ? 125 TYR   A C   1 
ATOM   1974 O O   . TYR   B 1 125 ? 9.245   -20.857 28.505 1.00 14.98  ? 125 TYR   A O   1 
ATOM   1975 C CB  . TYR   B 1 125 ? 7.356   -18.449 27.113 1.00 21.49  ? 125 TYR   A CB  1 
ATOM   1976 C CG  . TYR   B 1 125 ? 7.449   -16.992 26.714 1.00 31.94  ? 125 TYR   A CG  1 
ATOM   1977 C CD1 . TYR   B 1 125 ? 7.712   -16.633 25.393 1.00 35.77  ? 125 TYR   A CD1 1 
ATOM   1978 C CD2 . TYR   B 1 125 ? 7.260   -15.979 27.647 1.00 36.12  ? 125 TYR   A CD2 1 
ATOM   1979 C CE1 . TYR   B 1 125 ? 7.816   -15.328 25.017 1.00 42.90  ? 125 TYR   A CE1 1 
ATOM   1980 C CE2 . TYR   B 1 125 ? 7.355   -14.662 27.277 1.00 42.94  ? 125 TYR   A CE2 1 
ATOM   1981 C CZ  . TYR   B 1 125 ? 7.636   -14.345 25.960 1.00 47.37  ? 125 TYR   A CZ  1 
ATOM   1982 O OH  . TYR   B 1 125 ? 7.737   -13.039 25.572 1.00 63.78  ? 125 TYR   A OH  1 
ATOM   1983 N N   . SER   B 1 126 ? 7.986   -21.546 26.767 1.00 14.93  ? 126 SER   A N   1 
ATOM   1984 C CA  . SER   B 1 126 ? 8.039   -22.942 27.193 1.00 18.84  ? 126 SER   A CA  1 
ATOM   1985 C C   . SER   B 1 126 ? 9.485   -23.417 27.329 1.00 16.12  ? 126 SER   A C   1 
ATOM   1986 O O   . SER   B 1 126 ? 9.840   -24.067 28.322 1.00 14.65  ? 126 SER   A O   1 
ATOM   1987 C CB  . SER   B 1 126 ? 7.264   -23.843 26.216 1.00 14.42  ? 126 SER   A CB  1 
ATOM   1988 O OG  . SER   B 1 126 ? 5.872   -23.649 26.365 1.00 14.75  ? 126 SER   A OG  1 
ATOM   1989 N N   . ASN   B 1 127 ? 10.342  -23.081 26.353 1.00 14.55  ? 127 ASN   A N   1 
ATOM   1990 C CA  . ASN   B 1 127 ? 11.743  -23.500 26.465 1.00 19.21  ? 127 ASN   A CA  1 
ATOM   1991 C C   . ASN   B 1 127 ? 12.473  -22.721 27.557 1.00 16.41  ? 127 ASN   A C   1 
ATOM   1992 O O   . ASN   B 1 127 ? 13.426  -23.230 28.162 1.00 12.14  ? 127 ASN   A O   1 
ATOM   1993 C CB  . ASN   B 1 127 ? 12.472  -23.339 25.121 1.00 21.47  ? 127 ASN   A CB  1 
ATOM   1994 C CG  . ASN   B 1 127 ? 11.964  -24.309 24.044 1.00 24.65  ? 127 ASN   A CG  1 
ATOM   1995 O OD1 . ASN   B 1 127 ? 11.562  -25.443 24.352 1.00 25.04  ? 127 ASN   A OD1 1 
ATOM   1996 N ND2 . ASN   B 1 127 ? 11.972  -23.861 22.783 1.00 20.23  ? 127 ASN   A ND2 1 
ATOM   1997 N N   . ALA   B 1 128 ? 12.031  -21.500 27.841 1.00 12.26  ? 128 ALA   A N   1 
ATOM   1998 C CA  . ALA   B 1 128 ? 12.706  -20.703 28.860 1.00 13.54  ? 128 ALA   A CA  1 
ATOM   1999 C C   . ALA   B 1 128 ? 12.527  -21.288 30.259 1.00 12.33  ? 128 ALA   A C   1 
ATOM   2000 O O   . ALA   B 1 128 ? 13.363  -21.053 31.133 1.00 9.73   ? 128 ALA   A O   1 
ATOM   2001 C CB  . ALA   B 1 128 ? 12.181  -19.262 28.834 1.00 14.43  ? 128 ALA   A CB  1 
ATOM   2002 N N   . ILE   B 1 129 ? 11.458  -22.045 30.505 1.00 11.53  ? 129 ILE   A N   1 
ATOM   2003 C CA  . ILE   B 1 129 ? 11.203  -22.500 31.870 1.00 12.25  ? 129 ILE   A CA  1 
ATOM   2004 C C   . ILE   B 1 129 ? 11.386  -24.005 32.061 1.00 12.36  ? 129 ILE   A C   1 
ATOM   2005 O O   . ILE   B 1 129 ? 11.250  -24.481 33.194 1.00 8.79   ? 129 ILE   A O   1 
ATOM   2006 C CB  . ILE   B 1 129 ? 9.805   -22.066 32.361 1.00 12.22  ? 129 ILE   A CB  1 
ATOM   2007 C CG1 . ILE   B 1 129 ? 8.699   -22.754 31.572 1.00 9.28   ? 129 ILE   A CG1 1 
ATOM   2008 C CG2 . ILE   B 1 129 ? 9.639   -20.547 32.290 1.00 10.59  ? 129 ILE   A CG2 1 
ATOM   2009 C CD1 . ILE   B 1 129 ? 7.292   -22.103 31.894 1.00 19.43  ? 129 ILE   A CD1 1 
ATOM   2010 N N   . ARG   B 1 130 ? 11.703  -24.761 31.007 1.00 11.58  ? 130 ARG   A N   1 
ATOM   2011 C CA  . ARG   B 1 130 ? 11.764  -26.218 31.102 1.00 13.52  ? 130 ARG   A CA  1 
ATOM   2012 C C   . ARG   B 1 130 ? 12.844  -26.657 32.086 1.00 15.21  ? 130 ARG   A C   1 
ATOM   2013 O O   . ARG   B 1 130 ? 13.948  -26.101 32.111 1.00 16.23  ? 130 ARG   A O   1 
ATOM   2014 C CB  . ARG   B 1 130 ? 12.009  -26.835 29.712 1.00 18.27  ? 130 ARG   A CB  1 
ATOM   2015 C CG  . ARG   B 1 130 ? 11.803  -28.360 29.668 1.00 24.76  ? 130 ARG   A CG  1 
ATOM   2016 C CD  . ARG   B 1 130 ? 11.877  -28.928 28.253 1.00 29.49  ? 130 ARG   A CD  1 
ATOM   2017 N NE  . ARG   B 1 130 ? 10.688  -28.532 27.497 1.00 33.66  ? 130 ARG   A NE  1 
ATOM   2018 C CZ  . ARG   B 1 130 ? 10.706  -27.645 26.511 1.00 27.06  ? 130 ARG   A CZ  1 
ATOM   2019 N NH1 . ARG   B 1 130 ? 11.850  -27.081 26.152 1.00 25.42  ? 130 ARG   A NH1 1 
ATOM   2020 N NH2 . ARG   B 1 130 ? 9.581   -27.312 25.899 1.00 27.48  ? 130 ARG   A NH2 1 
ATOM   2021 N N   . GLY   B 1 131 ? 12.512  -27.643 32.914 1.00 11.98  ? 131 GLY   A N   1 
ATOM   2022 C CA  . GLY   B 1 131 ? 13.403  -28.111 33.962 1.00 12.03  ? 131 GLY   A CA  1 
ATOM   2023 C C   . GLY   B 1 131 ? 13.335  -27.334 35.269 1.00 13.28  ? 131 GLY   A C   1 
ATOM   2024 O O   . GLY   B 1 131 ? 13.911  -27.785 36.277 1.00 10.55  ? 131 GLY   A O   1 
ATOM   2025 N N   . ASN   B 1 132 ? 12.685  -26.162 35.279 1.00 12.51  ? 132 ASN   A N   1 
ATOM   2026 C CA  . ASN   B 1 132 ? 12.471  -25.411 36.514 1.00 15.86  ? 132 ASN   A CA  1 
ATOM   2027 C C   . ASN   B 1 132 ? 11.012  -25.372 36.917 1.00 13.78  ? 132 ASN   A C   1 
ATOM   2028 O O   . ASN   B 1 132 ? 10.691  -25.550 38.093 1.00 13.15  ? 132 ASN   A O   1 
ATOM   2029 C CB  . ASN   B 1 132 ? 12.963  -23.977 36.366 1.00 13.51  ? 132 ASN   A CB  1 
ATOM   2030 C CG  . ASN   B 1 132 ? 14.451  -23.907 36.109 1.00 13.60  ? 132 ASN   A CG  1 
ATOM   2031 O OD1 . ASN   B 1 132 ? 15.247  -24.493 36.865 1.00 9.46   ? 132 ASN   A OD1 1 
ATOM   2032 N ND2 . ASN   B 1 132 ? 14.843  -23.164 35.061 1.00 8.39   ? 132 ASN   A ND2 1 
ATOM   2033 N N   . ILE   B 1 133 ? 10.135  -25.154 35.952 1.00 12.01  ? 133 ILE   A N   1 
ATOM   2034 C CA  . ILE   B 1 133 ? 8.693   -25.223 36.138 1.00 14.82  ? 133 ILE   A CA  1 
ATOM   2035 C C   . ILE   B 1 133 ? 8.159   -26.342 35.250 1.00 14.39  ? 133 ILE   A C   1 
ATOM   2036 O O   . ILE   B 1 133 ? 8.427   -26.364 34.037 1.00 15.40  ? 133 ILE   A O   1 
ATOM   2037 C CB  . ILE   B 1 133 ? 8.012   -23.886 35.784 1.00 13.31  ? 133 ILE   A CB  1 
ATOM   2038 C CG1 . ILE   B 1 133 ? 8.544   -22.749 36.673 1.00 12.93  ? 133 ILE   A CG1 1 
ATOM   2039 C CG2 . ILE   B 1 133 ? 6.485   -24.025 35.830 1.00 15.27  ? 133 ILE   A CG2 1 
ATOM   2040 C CD1 . ILE   B 1 133 ? 8.137   -21.388 36.182 1.00 16.51  ? 133 ILE   A CD1 1 
ATOM   2041 N N   . GLN   B 1 134 ? 7.361   -27.222 35.838 1.00 12.16  ? 134 GLN   A N   1 
ATOM   2042 C CA  . GLN   B 1 134 ? 6.618   -28.227 35.090 1.00 14.76  ? 134 GLN   A CA  1 
ATOM   2043 C C   . GLN   B 1 134 ? 5.267   -27.645 34.692 1.00 17.69  ? 134 GLN   A C   1 
ATOM   2044 O O   . GLN   B 1 134 ? 4.332   -27.595 35.494 1.00 16.76  ? 134 GLN   A O   1 
ATOM   2045 C CB  . GLN   B 1 134 ? 6.459   -29.493 35.922 1.00 24.77  ? 134 GLN   A CB  1 
ATOM   2046 C CG  . GLN   B 1 134 ? 5.730   -30.596 35.197 1.00 31.30  ? 134 GLN   A CG  1 
ATOM   2047 C CD  . GLN   B 1 134 ? 6.293   -30.854 33.796 1.00 41.55  ? 134 GLN   A CD  1 
ATOM   2048 O OE1 . GLN   B 1 134 ? 5.623   -30.588 32.784 1.00 37.07  ? 134 GLN   A OE1 1 
ATOM   2049 N NE2 . GLN   B 1 134 ? 7.527   -31.363 33.731 1.00 40.46  ? 134 GLN   A NE2 1 
ATOM   2050 N N   . VAL   B 1 135 ? 5.166   -27.214 33.437 1.00 16.63  ? 135 VAL   A N   1 
ATOM   2051 C CA  . VAL   B 1 135 ? 3.940   -26.642 32.928 1.00 12.87  ? 135 VAL   A CA  1 
ATOM   2052 C C   . VAL   B 1 135 ? 2.927   -27.759 32.722 1.00 19.65  ? 135 VAL   A C   1 
ATOM   2053 O O   . VAL   B 1 135 ? 3.264   -28.841 32.242 1.00 18.28  ? 135 VAL   A O   1 
ATOM   2054 C CB  . VAL   B 1 135 ? 4.200   -25.886 31.616 1.00 16.06  ? 135 VAL   A CB  1 
ATOM   2055 C CG1 . VAL   B 1 135 ? 2.898   -25.250 31.106 1.00 13.36  ? 135 VAL   A CG1 1 
ATOM   2056 C CG2 . VAL   B 1 135 ? 5.259   -24.806 31.831 1.00 18.45  ? 135 VAL   A CG2 1 
ATOM   2057 N N   . SER   B 1 136 ? 1.683   -27.505 33.099 1.00 15.77  ? 136 SER   A N   1 
ATOM   2058 C CA  . SER   B 1 136 ? 0.606   -28.443 32.820 1.00 17.94  ? 136 SER   A CA  1 
ATOM   2059 C C   . SER   B 1 136 ? -0.307  -27.804 31.784 1.00 16.52  ? 136 SER   A C   1 
ATOM   2060 O O   . SER   B 1 136 ? -0.425  -26.573 31.723 1.00 14.31  ? 136 SER   A O   1 
ATOM   2061 C CB  . SER   B 1 136 ? -0.160  -28.818 34.089 1.00 14.17  ? 136 SER   A CB  1 
ATOM   2062 O OG  . SER   B 1 136 ? -0.839  -27.701 34.631 1.00 20.71  ? 136 SER   A OG  1 
ATOM   2063 N N   . THR   B 1 137 ? -0.899  -28.644 30.938 1.00 14.73  ? 137 THR   A N   1 
ATOM   2064 C CA  . THR   B 1 137 ? -1.653  -28.211 29.770 1.00 20.95  ? 137 THR   A CA  1 
ATOM   2065 C C   . THR   B 1 137 ? -2.899  -29.084 29.620 1.00 27.09  ? 137 THR   A C   1 
ATOM   2066 O O   . THR   B 1 137 ? -2.827  -30.317 29.754 1.00 17.24  ? 137 THR   A O   1 
ATOM   2067 C CB  . THR   B 1 137 ? -0.791  -28.298 28.495 1.00 20.94  ? 137 THR   A CB  1 
ATOM   2068 O OG1 . THR   B 1 137 ? 0.386   -27.500 28.652 1.00 19.34  ? 137 THR   A OG1 1 
ATOM   2069 C CG2 . THR   B 1 137 ? -1.551  -27.776 27.276 1.00 20.38  ? 137 THR   A CG2 1 
ATOM   2070 N N   . THR   B 1 138 ? -4.035  -28.437 29.351 1.00 21.03  ? 138 THR   A N   1 
ATOM   2071 C CA  . THR   B 1 138 ? -5.259  -29.101 28.913 1.00 20.57  ? 138 THR   A CA  1 
ATOM   2072 C C   . THR   B 1 138 ? -5.672  -28.524 27.564 1.00 18.63  ? 138 THR   A C   1 
ATOM   2073 O O   . THR   B 1 138 ? -5.603  -27.300 27.352 1.00 17.96  ? 138 THR   A O   1 
ATOM   2074 C CB  . THR   B 1 138 ? -6.370  -28.941 29.960 1.00 18.84  ? 138 THR   A CB  1 
ATOM   2075 O OG1 . THR   B 1 138 ? -5.876  -29.326 31.247 1.00 22.69  ? 138 THR   A OG1 1 
ATOM   2076 C CG2 . THR   B 1 138 ? -7.587  -29.816 29.636 1.00 24.96  ? 138 THR   A CG2 1 
ATOM   2077 N N   . VAL   B 1 139 ? -6.066  -29.405 26.643 1.00 18.42  ? 139 VAL   A N   1 
ATOM   2078 C CA  . VAL   B 1 139 ? -6.412  -29.031 25.271 1.00 15.51  ? 139 VAL   A CA  1 
ATOM   2079 C C   . VAL   B 1 139 ? -7.914  -29.210 25.051 1.00 17.92  ? 139 VAL   A C   1 
ATOM   2080 O O   . VAL   B 1 139 ? -8.464  -30.279 25.333 1.00 18.89  ? 139 VAL   A O   1 
ATOM   2081 C CB  . VAL   B 1 139 ? -5.612  -29.860 24.255 1.00 17.87  ? 139 VAL   A CB  1 
ATOM   2082 C CG1 . VAL   B 1 139 ? -5.994  -29.455 22.835 1.00 14.08  ? 139 VAL   A CG1 1 
ATOM   2083 C CG2 . VAL   B 1 139 ? -4.114  -29.673 24.489 1.00 19.26  ? 139 VAL   A CG2 1 
ATOM   2084 N N   . TYR   B 1 140 ? -8.561  -28.173 24.512 1.00 21.93  ? 140 TYR   A N   1 
ATOM   2085 C CA  . TYR   B 1 140 ? -9.994  -28.133 24.224 1.00 19.84  ? 140 TYR   A CA  1 
ATOM   2086 C C   . TYR   B 1 140 ? -10.208 -27.814 22.745 1.00 25.98  ? 140 TYR   A C   1 
ATOM   2087 O O   . TYR   B 1 140 ? -9.376  -27.135 22.132 1.00 20.35  ? 140 TYR   A O   1 
ATOM   2088 C CB  . TYR   B 1 140 ? -10.657 -27.053 25.083 1.00 16.55  ? 140 TYR   A CB  1 
ATOM   2089 C CG  . TYR   B 1 140 ? -10.664 -27.388 26.548 1.00 19.53  ? 140 TYR   A CG  1 
ATOM   2090 C CD1 . TYR   B 1 140 ? -11.465 -28.406 27.041 1.00 27.47  ? 140 TYR   A CD1 1 
ATOM   2091 C CD2 . TYR   B 1 140 ? -9.828  -26.721 27.438 1.00 26.05  ? 140 TYR   A CD2 1 
ATOM   2092 C CE1 . TYR   B 1 140 ? -11.471 -28.726 28.396 1.00 29.63  ? 140 TYR   A CE1 1 
ATOM   2093 C CE2 . TYR   B 1 140 ? -9.818  -27.031 28.792 1.00 22.25  ? 140 TYR   A CE2 1 
ATOM   2094 C CZ  . TYR   B 1 140 ? -10.647 -28.036 29.270 1.00 34.92  ? 140 TYR   A CZ  1 
ATOM   2095 O OH  . TYR   B 1 140 ? -10.651 -28.358 30.621 1.00 26.54  ? 140 TYR   A OH  1 
ATOM   2096 N N   . THR   B 1 141 ? -11.337 -28.282 22.159 1.00 20.23  ? 141 THR   A N   1 
ATOM   2097 C CA  . THR   B 1 141 ? -11.578 -28.052 20.726 1.00 25.11  ? 141 THR   A CA  1 
ATOM   2098 C C   . THR   B 1 141 ? -12.865 -27.328 20.295 1.00 33.87  ? 141 THR   A C   1 
ATOM   2099 O O   . THR   B 1 141 ? -12.956 -26.960 19.117 1.00 41.81  ? 141 THR   A O   1 
ATOM   2100 C CB  . THR   B 1 141 ? -11.461 -29.372 19.935 1.00 24.67  ? 141 THR   A CB  1 
ATOM   2101 O OG1 . THR   B 1 141 ? -12.276 -30.393 20.528 1.00 26.32  ? 141 THR   A OG1 1 
ATOM   2102 C CG2 . THR   B 1 141 ? -10.011 -29.838 19.852 1.00 22.88  ? 141 THR   A CG2 1 
ATOM   2103 N N   . LYS   B 1 142 ? -13.839 -27.078 21.157 1.00 30.41  ? 142 LYS   A N   1 
ATOM   2104 C CA  . LYS   B 1 142 ? -14.839 -26.031 20.782 1.00 37.83  ? 142 LYS   A CA  1 
ATOM   2105 C C   . LYS   B 1 142 ? -15.587 -26.240 19.445 1.00 40.36  ? 142 LYS   A C   1 
ATOM   2106 O O   . LYS   B 1 142 ? -15.245 -25.665 18.385 1.00 25.52  ? 142 LYS   A O   1 
ATOM   2107 C CB  . LYS   B 1 142 ? -14.151 -24.652 20.743 1.00 40.96  ? 142 LYS   A CB  1 
ATOM   2108 C CG  . LYS   B 1 142 ? -15.077 -23.451 20.758 1.00 47.40  ? 142 LYS   A CG  1 
ATOM   2109 C CD  . LYS   B 1 142 ? -14.339 -22.178 21.180 1.00 47.13  ? 142 LYS   A CD  1 
ATOM   2110 C CE  . LYS   B 1 142 ? -15.301 -21.095 21.652 1.00 55.10  ? 142 LYS   A CE  1 
ATOM   2111 N NZ  . LYS   B 1 142 ? -14.606 -19.929 22.270 1.00 54.97  ? 142 LYS   A NZ  1 
ATOM   2112 N N   . MET   C 1 1   ? -10.869 -15.247 50.337 1.00 71.92  ? 1   MET   C N   1 
ATOM   2113 C CA  . MET   C 1 1   ? -9.412  -15.285 50.455 1.00 74.93  ? 1   MET   C CA  1 
ATOM   2114 C C   . MET   C 1 1   ? -8.959  -16.530 51.210 1.00 70.10  ? 1   MET   C C   1 
ATOM   2115 O O   . MET   C 1 1   ? -9.545  -16.898 52.234 1.00 64.66  ? 1   MET   C O   1 
ATOM   2116 C CB  . MET   C 1 1   ? -8.892  -14.032 51.163 1.00 76.43  ? 1   MET   C CB  1 
ATOM   2117 C CG  . MET   C 1 1   ? -9.487  -12.743 50.638 1.00 82.43  ? 1   MET   C CG  1 
ATOM   2118 S SD  . MET   C 1 1   ? -8.792  -12.139 49.088 1.00 85.59  ? 1   MET   C SD  1 
ATOM   2119 C CE  . MET   C 1 1   ? -8.995  -10.388 49.383 1.00 83.94  ? 1   MET   C CE  1 
ATOM   2120 N N   . SER   C 1 2   ? -7.905  -17.165 50.708 1.00 61.38  ? 2   SER   C N   1 
ATOM   2121 C CA  . SER   C 1 2   ? -7.384  -18.379 51.314 1.00 56.18  ? 2   SER   C CA  1 
ATOM   2122 C C   . SER   C 1 2   ? -6.238  -18.058 52.273 1.00 58.66  ? 2   SER   C C   1 
ATOM   2123 O O   . SER   C 1 2   ? -5.553  -17.036 52.139 1.00 49.91  ? 2   SER   C O   1 
ATOM   2124 C CB  . SER   C 1 2   ? -6.924  -19.354 50.231 1.00 51.89  ? 2   SER   C CB  1 
ATOM   2125 O OG  . SER   C 1 2   ? -5.586  -19.089 49.862 1.00 54.93  ? 2   SER   C OG  1 
ATOM   2126 N N   . THR   C 1 3   ? -6.044  -18.948 53.254 1.00 48.52  ? 3   THR   C N   1 
ATOM   2127 C CA  . THR   C 1 3   ? -5.091  -18.714 54.337 1.00 43.71  ? 3   THR   C CA  1 
ATOM   2128 C C   . THR   C 1 3   ? -3.665  -18.608 53.810 1.00 37.45  ? 3   THR   C C   1 
ATOM   2129 O O   . THR   C 1 3   ? -3.198  -19.489 53.084 1.00 38.77  ? 3   THR   C O   1 
ATOM   2130 C CB  . THR   C 1 3   ? -5.193  -19.844 55.363 1.00 47.88  ? 3   THR   C CB  1 
ATOM   2131 O OG1 . THR   C 1 3   ? -6.471  -19.802 56.011 1.00 49.42  ? 3   THR   C OG1 1 
ATOM   2132 C CG2 . THR   C 1 3   ? -4.105  -19.726 56.396 1.00 38.61  ? 3   THR   C CG2 1 
ATOM   2133 N N   . LEU   C 1 4   ? -2.970  -17.532 54.195 1.00 32.47  ? 4   LEU   C N   1 
ATOM   2134 C CA  . LEU   C 1 4   ? -1.590  -17.327 53.753 1.00 25.17  ? 4   LEU   C CA  1 
ATOM   2135 C C   . LEU   C 1 4   ? -0.612  -18.197 54.537 1.00 33.39  ? 4   LEU   C C   1 
ATOM   2136 O O   . LEU   C 1 4   ? 0.406   -18.655 53.995 1.00 28.62  ? 4   LEU   C O   1 
ATOM   2137 C CB  . LEU   C 1 4   ? -1.198  -15.857 53.906 1.00 24.28  ? 4   LEU   C CB  1 
ATOM   2138 C CG  . LEU   C 1 4   ? -1.750  -14.780 52.978 1.00 31.68  ? 4   LEU   C CG  1 
ATOM   2139 C CD1 . LEU   C 1 4   ? -1.213  -13.433 53.404 1.00 27.93  ? 4   LEU   C CD1 1 
ATOM   2140 C CD2 . LEU   C 1 4   ? -1.362  -15.073 51.530 1.00 32.04  ? 4   LEU   C CD2 1 
ATOM   2141 N N   . TYR   C 1 5   ? -0.878  -18.401 55.823 1.00 34.13  ? 5   TYR   C N   1 
ATOM   2142 C CA  . TYR   C 1 5   ? 0.021   -19.160 56.681 1.00 29.20  ? 5   TYR   C CA  1 
ATOM   2143 C C   . TYR   C 1 5   ? -0.778  -19.694 57.853 1.00 25.40  ? 5   TYR   C C   1 
ATOM   2144 O O   . TYR   C 1 5   ? -1.665  -19.002 58.366 1.00 25.17  ? 5   TYR   C O   1 
ATOM   2145 C CB  . TYR   C 1 5   ? 1.192   -18.312 57.195 1.00 24.08  ? 5   TYR   C CB  1 
ATOM   2146 C CG  . TYR   C 1 5   ? 1.969   -18.974 58.317 1.00 29.48  ? 5   TYR   C CG  1 
ATOM   2147 C CD1 . TYR   C 1 5   ? 2.800   -20.067 58.065 1.00 29.39  ? 5   TYR   C CD1 1 
ATOM   2148 C CD2 . TYR   C 1 5   ? 1.904   -18.482 59.633 1.00 26.06  ? 5   TYR   C CD2 1 
ATOM   2149 C CE1 . TYR   C 1 5   ? 3.528   -20.680 59.098 1.00 30.42  ? 5   TYR   C CE1 1 
ATOM   2150 C CE2 . TYR   C 1 5   ? 2.624   -19.087 60.665 1.00 24.64  ? 5   TYR   C CE2 1 
ATOM   2151 C CZ  . TYR   C 1 5   ? 3.435   -20.179 60.392 1.00 24.30  ? 5   TYR   C CZ  1 
ATOM   2152 O OH  . TYR   C 1 5   ? 4.153   -20.777 61.404 1.00 26.54  ? 5   TYR   C OH  1 
ATOM   2153 N N   . SER   C 1 6   ? -0.430  -20.907 58.288 1.00 22.70  ? 6   SER   C N   1 
ATOM   2154 C CA  . SER   C 1 6   ? -1.149  -21.591 59.349 1.00 22.10  ? 6   SER   C CA  1 
ATOM   2155 C C   . SER   C 1 6   ? -0.171  -22.390 60.198 1.00 27.03  ? 6   SER   C C   1 
ATOM   2156 O O   . SER   C 1 6   ? 0.748   -23.020 59.664 1.00 23.18  ? 6   SER   C O   1 
ATOM   2157 C CB  . SER   C 1 6   ? -2.219  -22.508 58.766 1.00 25.21  ? 6   SER   C CB  1 
ATOM   2158 O OG  . SER   C 1 6   ? -3.037  -23.002 59.802 1.00 35.61  ? 6   SER   C OG  1 
ATOM   2159 N N   . THR   C 1 7   ? -0.358  -22.349 61.517 1.00 23.18  ? 7   THR   C N   1 
ATOM   2160 C CA  . THR   C 1 7   ? 0.545   -23.017 62.443 1.00 25.66  ? 7   THR   C CA  1 
ATOM   2161 C C   . THR   C 1 7   ? -0.267  -23.692 63.539 1.00 21.99  ? 7   THR   C C   1 
ATOM   2162 O O   . THR   C 1 7   ? -1.380  -23.273 63.853 1.00 23.43  ? 7   THR   C O   1 
ATOM   2163 C CB  . THR   C 1 7   ? 1.562   -22.027 63.057 1.00 24.40  ? 7   THR   C CB  1 
ATOM   2164 O OG1 . THR   C 1 7   ? 2.490   -22.744 63.877 1.00 33.99  ? 7   THR   C OG1 1 
ATOM   2165 C CG2 . THR   C 1 7   ? 0.856   -20.969 63.902 1.00 18.66  ? 7   THR   C CG2 1 
ATOM   2166 N N   . GLN   C 1 8   ? 0.309   -24.733 64.129 1.00 18.71  ? 8   GLN   C N   1 
ATOM   2167 C CA  . GLN   C 1 8   ? -0.316  -25.472 65.212 1.00 25.96  ? 8   GLN   C CA  1 
ATOM   2168 C C   . GLN   C 1 8   ? 0.619   -25.546 66.410 1.00 25.44  ? 8   GLN   C C   1 
ATOM   2169 O O   . GLN   C 1 8   ? 1.819   -25.819 66.261 1.00 29.58  ? 8   GLN   C O   1 
ATOM   2170 C CB  . GLN   C 1 8   ? -0.702  -26.888 64.778 1.00 27.40  ? 8   GLN   C CB  1 
ATOM   2171 C CG  . GLN   C 1 8   ? -1.730  -26.960 63.676 1.00 24.60  ? 8   GLN   C CG  1 
ATOM   2172 C CD  . GLN   C 1 8   ? -2.173  -28.393 63.421 1.00 39.44  ? 8   GLN   C CD  1 
ATOM   2173 O OE1 . GLN   C 1 8   ? -3.019  -28.931 64.129 1.00 37.57  ? 8   GLN   C OE1 1 
ATOM   2174 N NE2 . GLN   C 1 8   ? -1.555  -29.032 62.431 1.00 42.55  ? 8   GLN   C NE2 1 
ATOM   2175 N N   . VAL   C 1 9   ? 0.063   -25.304 67.594 1.00 24.60  ? 9   VAL   C N   1 
ATOM   2176 C CA  . VAL   C 1 9   ? 0.787   -25.410 68.856 1.00 20.10  ? 9   VAL   C CA  1 
ATOM   2177 C C   . VAL   C 1 9   ? -0.024  -26.273 69.819 1.00 28.29  ? 9   VAL   C C   1 
ATOM   2178 O O   . VAL   C 1 9   ? -1.217  -26.019 70.038 1.00 23.76  ? 9   VAL   C O   1 
ATOM   2179 C CB  . VAL   C 1 9   ? 1.071   -24.025 69.480 1.00 23.80  ? 9   VAL   C CB  1 
ATOM   2180 C CG1 . VAL   C 1 9   ? 1.821   -24.187 70.819 1.00 18.46  ? 9   VAL   C CG1 1 
ATOM   2181 C CG2 . VAL   C 1 9   ? 1.920   -23.163 68.533 1.00 16.68  ? 9   VAL   C CG2 1 
ATOM   2182 N N   . LYS   C 1 10  ? 0.633   -27.277 70.410 1.00 29.63  ? 10  LYS   C N   1 
ATOM   2183 C CA  . LYS   C 1 10  ? 0.034   -28.113 71.437 1.00 24.00  ? 10  LYS   C CA  1 
ATOM   2184 C C   . LYS   C 1 10  ? 0.428   -27.599 72.817 1.00 24.04  ? 10  LYS   C C   1 
ATOM   2185 O O   . LYS   C 1 10  ? 1.619   -27.440 73.112 1.00 24.31  ? 10  LYS   C O   1 
ATOM   2186 C CB  . LYS   C 1 10  ? 0.464   -29.572 71.282 1.00 32.95  ? 10  LYS   C CB  1 
ATOM   2187 C CG  . LYS   C 1 10  ? -0.331  -30.516 72.182 1.00 35.11  ? 10  LYS   C CG  1 
ATOM   2188 C CD  . LYS   C 1 10  ? 0.373   -31.850 72.386 1.00 40.73  ? 10  LYS   C CD  1 
ATOM   2189 C CE  . LYS   C 1 10  ? 0.332   -32.725 71.137 1.00 39.45  ? 10  LYS   C CE  1 
ATOM   2190 N NZ  . LYS   C 1 10  ? 0.989   -34.060 71.383 1.00 47.40  ? 10  LYS   C NZ  1 
ATOM   2191 N N   . ALA   C 1 11  ? -0.569  -27.350 73.656 1.00 20.08  ? 11  ALA   C N   1 
ATOM   2192 C CA  . ALA   C 1 11  ? -0.353  -26.916 75.028 1.00 26.43  ? 11  ALA   C CA  1 
ATOM   2193 C C   . ALA   C 1 11  ? -0.889  -27.987 75.965 1.00 33.50  ? 11  ALA   C C   1 
ATOM   2194 O O   . ALA   C 1 11  ? -2.075  -28.331 75.905 1.00 29.98  ? 11  ALA   C O   1 
ATOM   2195 C CB  . ALA   C 1 11  ? -1.039  -25.582 75.300 1.00 23.27  ? 11  ALA   C CB  1 
ATOM   2196 N N   . VAL   C 1 12  ? -0.018  -28.499 76.832 1.00 38.24  ? 12  VAL   C N   1 
ATOM   2197 C CA  . VAL   C 1 12  ? -0.380  -29.537 77.795 1.00 36.17  ? 12  VAL   C CA  1 
ATOM   2198 C C   . VAL   C 1 12  ? -0.277  -28.964 79.199 1.00 26.06  ? 12  VAL   C C   1 
ATOM   2199 O O   . VAL   C 1 12  ? 0.739   -28.355 79.556 1.00 32.66  ? 12  VAL   C O   1 
ATOM   2200 C CB  . VAL   C 1 12  ? 0.509   -30.788 77.654 1.00 34.49  ? 12  VAL   C CB  1 
ATOM   2201 C CG1 . VAL   C 1 12  ? 0.014   -31.892 78.595 1.00 39.77  ? 12  VAL   C CG1 1 
ATOM   2202 C CG2 . VAL   C 1 12  ? 0.514   -31.289 76.221 1.00 30.90  ? 12  VAL   C CG2 1 
ATOM   2203 N N   . GLY   C 1 13  ? -1.336  -29.144 79.984 1.00 30.36  ? 13  GLY   C N   1 
ATOM   2204 C CA  . GLY   C 1 13  ? -1.285  -28.894 81.414 1.00 30.15  ? 13  GLY   C CA  1 
ATOM   2205 C C   . GLY   C 1 13  ? -1.430  -27.457 81.864 1.00 32.84  ? 13  GLY   C C   1 
ATOM   2206 O O   . GLY   C 1 13  ? -0.930  -27.111 82.936 1.00 29.13  ? 13  GLY   C O   1 
ATOM   2207 N N   . GLY   C 1 14  ? -2.085  -26.599 81.070 1.00 28.27  ? 14  GLY   C N   1 
ATOM   2208 C CA  . GLY   C 1 14  ? -2.418  -25.270 81.567 1.00 23.83  ? 14  GLY   C CA  1 
ATOM   2209 C C   . GLY   C 1 14  ? -1.197  -24.389 81.802 1.00 22.82  ? 14  GLY   C C   1 
ATOM   2210 O O   . GLY   C 1 14  ? -0.149  -24.537 81.162 1.00 29.22  ? 14  GLY   C O   1 
ATOM   2211 N N   . ARG   C 1 15  ? -1.333  -23.464 82.760 1.00 26.09  ? 15  ARG   C N   1 
ATOM   2212 C CA  . ARG   C 1 15  ? -0.315  -22.446 83.000 1.00 26.95  ? 15  ARG   C CA  1 
ATOM   2213 C C   . ARG   C 1 15  ? 0.939   -22.973 83.694 1.00 27.33  ? 15  ARG   C C   1 
ATOM   2214 O O   . ARG   C 1 15  ? 1.941   -22.252 83.736 1.00 27.92  ? 15  ARG   C O   1 
ATOM   2215 C CB  . ARG   C 1 15  ? -0.915  -21.296 83.805 1.00 25.19  ? 15  ARG   C CB  1 
ATOM   2216 C CG  . ARG   C 1 15  ? -1.892  -20.438 83.002 1.00 26.24  ? 15  ARG   C CG  1 
ATOM   2217 C CD  . ARG   C 1 15  ? -2.560  -19.428 83.899 1.00 27.92  ? 15  ARG   C CD  1 
ATOM   2218 N NE  . ARG   C 1 15  ? -3.518  -18.598 83.185 1.00 34.51  ? 15  ARG   C NE  1 
ATOM   2219 C CZ  . ARG   C 1 15  ? -3.241  -17.400 82.681 1.00 34.10  ? 15  ARG   C CZ  1 
ATOM   2220 N NH1 . ARG   C 1 15  ? -2.014  -16.887 82.794 1.00 25.91  ? 15  ARG   C NH1 1 
ATOM   2221 N NH2 . ARG   C 1 15  ? -4.197  -16.719 82.054 1.00 32.87  ? 15  ARG   C NH2 1 
ATOM   2222 N N   . SER   C 1 16  ? 0.943   -24.202 84.209 1.00 25.40  ? 16  SER   C N   1 
ATOM   2223 C CA  . SER   C 1 16  ? 2.169   -24.781 84.752 1.00 25.36  ? 16  SER   C CA  1 
ATOM   2224 C C   . SER   C 1 16  ? 2.700   -25.932 83.899 1.00 36.34  ? 16  SER   C C   1 
ATOM   2225 O O   . SER   C 1 16  ? 3.563   -26.697 84.361 1.00 28.46  ? 16  SER   C O   1 
ATOM   2226 C CB  . SER   C 1 16  ? 1.952   -25.244 86.195 1.00 28.15  ? 16  SER   C CB  1 
ATOM   2227 O OG  . SER   C 1 16  ? 1.095   -26.369 86.203 1.00 38.45  ? 16  SER   C OG  1 
ATOM   2228 N N   . GLY   C 1 17  ? 2.215   -26.067 82.656 1.00 26.96  ? 17  GLY   C N   1 
ATOM   2229 C CA  . GLY   C 1 17  ? 2.677   -27.125 81.782 1.00 27.54  ? 17  GLY   C CA  1 
ATOM   2230 C C   . GLY   C 1 17  ? 3.636   -26.661 80.705 1.00 31.91  ? 17  GLY   C C   1 
ATOM   2231 O O   . GLY   C 1 17  ? 4.627   -25.975 80.999 1.00 26.46  ? 17  GLY   C O   1 
ATOM   2232 N N   . THR   C 1 18  ? 3.332   -27.002 79.448 1.00 27.74  ? 18  THR   C N   1 
ATOM   2233 C CA  . THR   C 1 18  ? 4.259   -26.838 78.331 1.00 29.82  ? 18  THR   C CA  1 
ATOM   2234 C C   . THR   C 1 18  ? 3.505   -26.419 77.062 1.00 34.16  ? 18  THR   C C   1 
ATOM   2235 O O   . THR   C 1 18  ? 2.290   -26.624 76.951 1.00 23.40  ? 18  THR   C O   1 
ATOM   2236 C CB  . THR   C 1 18  ? 5.032   -28.153 78.100 1.00 30.76  ? 18  THR   C CB  1 
ATOM   2237 O OG1 . THR   C 1 18  ? 6.126   -27.928 77.200 1.00 46.23  ? 18  THR   C OG1 1 
ATOM   2238 C CG2 . THR   C 1 18  ? 4.129   -29.212 77.544 1.00 22.46  ? 18  THR   C CG2 1 
ATOM   2239 N N   . ILE   C 1 19  ? 4.247   -25.798 76.111 1.00 27.07  ? 19  ILE   C N   1 
ATOM   2240 C CA  . ILE   C 1 19  ? 3.793   -25.584 74.733 1.00 26.88  ? 19  ILE   C CA  1 
ATOM   2241 C C   . ILE   C 1 19  ? 4.838   -26.146 73.792 1.00 25.26  ? 19  ILE   C C   1 
ATOM   2242 O O   . ILE   C 1 19  ? 6.043   -26.087 74.079 1.00 25.06  ? 19  ILE   C O   1 
ATOM   2243 C CB  . ILE   C 1 19  ? 3.584   -24.107 74.323 1.00 22.36  ? 19  ILE   C CB  1 
ATOM   2244 C CG1 . ILE   C 1 19  ? 4.938   -23.391 74.275 1.00 25.89  ? 19  ILE   C CG1 1 
ATOM   2245 C CG2 . ILE   C 1 19  ? 2.617   -23.440 75.239 1.00 19.23  ? 19  ILE   C CG2 1 
ATOM   2246 C CD1 . ILE   C 1 19  ? 4.986   -22.049 73.608 1.00 35.43  ? 19  ILE   C CD1 1 
ATOM   2247 N N   . ARG   C 1 20  ? 4.376   -26.606 72.627 1.00 24.61  ? 20  ARG   C N   1 
ATOM   2248 C CA  . ARG   C 1 20  ? 5.271   -27.074 71.573 1.00 29.83  ? 20  ARG   C CA  1 
ATOM   2249 C C   . ARG   C 1 20  ? 4.601   -26.872 70.219 1.00 26.69  ? 20  ARG   C C   1 
ATOM   2250 O O   . ARG   C 1 20  ? 3.497   -27.375 69.979 1.00 25.27  ? 20  ARG   C O   1 
ATOM   2251 C CB  . ARG   C 1 20  ? 5.662   -28.550 71.779 1.00 31.91  ? 20  ARG   C CB  1 
ATOM   2252 C CG  . ARG   C 1 20  ? 6.758   -29.011 70.836 1.00 36.18  ? 20  ARG   C CG  1 
ATOM   2253 C CD  . ARG   C 1 20  ? 7.153   -30.480 71.009 1.00 35.47  ? 20  ARG   C CD  1 
ATOM   2254 N NE  . ARG   C 1 20  ? 8.218   -30.832 70.066 1.00 37.06  ? 20  ARG   C NE  1 
ATOM   2255 C CZ  . ARG   C 1 20  ? 8.011   -31.118 68.782 1.00 42.03  ? 20  ARG   C CZ  1 
ATOM   2256 N NH1 . ARG   C 1 20  ? 6.779   -31.109 68.287 1.00 36.17  ? 20  ARG   C NH1 1 
ATOM   2257 N NH2 . ARG   C 1 20  ? 9.032   -31.420 67.990 1.00 41.53  ? 20  ARG   C NH2 1 
ATOM   2258 N N   . SER   C 1 21  ? 5.244   -26.111 69.348 1.00 22.50  ? 21  SER   C N   1 
ATOM   2259 C CA  . SER   C 1 21  ? 4.711   -25.951 68.002 1.00 30.92  ? 21  SER   C CA  1 
ATOM   2260 C C   . SER   C 1 21  ? 4.992   -27.213 67.194 1.00 32.41  ? 21  SER   C C   1 
ATOM   2261 O O   . SER   C 1 21  ? 6.000   -27.901 67.397 1.00 37.20  ? 21  SER   C O   1 
ATOM   2262 C CB  . SER   C 1 21  ? 5.336   -24.743 67.303 1.00 23.97  ? 21  SER   C CB  1 
ATOM   2263 O OG  . SER   C 1 21  ? 6.706   -24.984 67.039 1.00 29.86  ? 21  SER   C OG  1 
ATOM   2264 N N   . GLU   C 1 22  ? 4.085   -27.526 66.279 1.00 30.43  ? 22  GLU   C N   1 
ATOM   2265 C CA  . GLU   C 1 22  ? 4.189   -28.825 65.633 1.00 40.22  ? 22  GLU   C CA  1 
ATOM   2266 C C   . GLU   C 1 22  ? 5.425   -28.927 64.747 1.00 32.68  ? 22  GLU   C C   1 
ATOM   2267 O O   . GLU   C 1 22  ? 5.875   -30.041 64.472 1.00 39.38  ? 22  GLU   C O   1 
ATOM   2268 C CB  . GLU   C 1 22  ? 2.908   -29.130 64.852 1.00 35.35  ? 22  GLU   C CB  1 
ATOM   2269 C CG  . GLU   C 1 22  ? 1.683   -29.407 65.762 1.00 43.20  ? 22  GLU   C CG  1 
ATOM   2270 C CD  . GLU   C 1 22  ? 1.836   -30.640 66.690 1.00 48.40  ? 22  GLU   C CD  1 
ATOM   2271 O OE1 . GLU   C 1 22  ? 1.334   -31.730 66.332 1.00 54.35  ? 22  GLU   C OE1 1 
ATOM   2272 O OE2 . GLU   C 1 22  ? 2.424   -30.524 67.792 1.00 46.25  ? 22  GLU   C OE2 1 
ATOM   2273 N N   . ASP   C 1 23  ? 6.021   -27.806 64.344 1.00 35.37  ? 23  ASP   C N   1 
ATOM   2274 C CA  . ASP   C 1 23  ? 7.293   -27.847 63.629 1.00 32.78  ? 23  ASP   C CA  1 
ATOM   2275 C C   . ASP   C 1 23  ? 8.495   -27.820 64.569 1.00 31.97  ? 23  ASP   C C   1 
ATOM   2276 O O   . ASP   C 1 23  ? 9.632   -27.722 64.098 1.00 37.90  ? 23  ASP   C O   1 
ATOM   2277 C CB  . ASP   C 1 23  ? 7.378   -26.700 62.599 1.00 33.96  ? 23  ASP   C CB  1 
ATOM   2278 C CG  . ASP   C 1 23  ? 7.422   -25.303 63.243 1.00 46.56  ? 23  ASP   C CG  1 
ATOM   2279 O OD1 . ASP   C 1 23  ? 7.098   -25.171 64.446 1.00 34.81  ? 23  ASP   C OD1 1 
ATOM   2280 O OD2 . ASP   C 1 23  ? 7.779   -24.328 62.527 1.00 46.19  ? 23  ASP   C OD2 1 
ATOM   2281 N N   . GLY   C 1 24  ? 8.274   -27.910 65.880 1.00 31.36  ? 24  GLY   C N   1 
ATOM   2282 C CA  . GLY   C 1 24  ? 9.346   -27.980 66.847 1.00 30.59  ? 24  GLY   C CA  1 
ATOM   2283 C C   . GLY   C 1 24  ? 10.083  -26.689 67.121 1.00 29.27  ? 24  GLY   C C   1 
ATOM   2284 O O   . GLY   C 1 24  ? 10.875  -26.648 68.070 1.00 28.67  ? 24  GLY   C O   1 
ATOM   2285 N N   . ILE   C 1 25  ? 9.858   -25.629 66.337 1.00 28.58  ? 25  ILE   C N   1 
ATOM   2286 C CA  . ILE   C 1 25  ? 10.653  -24.402 66.495 1.00 28.70  ? 25  ILE   C CA  1 
ATOM   2287 C C   . ILE   C 1 25  ? 10.339  -23.663 67.799 1.00 28.98  ? 25  ILE   C C   1 
ATOM   2288 O O   . ILE   C 1 25  ? 11.218  -23.001 68.364 1.00 30.85  ? 25  ILE   C O   1 
ATOM   2289 C CB  . ILE   C 1 25  ? 10.491  -23.485 65.264 1.00 28.95  ? 25  ILE   C CB  1 
ATOM   2290 C CG1 . ILE   C 1 25  ? 11.131  -24.121 64.020 1.00 32.94  ? 25  ILE   C CG1 1 
ATOM   2291 C CG2 . ILE   C 1 25  ? 11.049  -22.093 65.522 1.00 31.77  ? 25  ILE   C CG2 1 
ATOM   2292 C CD1 . ILE   C 1 25  ? 12.645  -24.332 64.177 1.00 35.68  ? 25  ILE   C CD1 1 
ATOM   2293 N N   . LEU   C 1 26  ? 9.118   -23.767 68.323 1.00 26.96  ? 26  LEU   C N   1 
ATOM   2294 C CA  . LEU   C 1 26  ? 8.765   -23.100 69.577 1.00 23.39  ? 26  LEU   C CA  1 
ATOM   2295 C C   . LEU   C 1 26  ? 8.408   -24.161 70.611 1.00 24.10  ? 26  LEU   C C   1 
ATOM   2296 O O   . LEU   C 1 26  ? 7.374   -24.826 70.503 1.00 25.30  ? 26  LEU   C O   1 
ATOM   2297 C CB  . LEU   C 1 26  ? 7.611   -22.127 69.371 1.00 23.63  ? 26  LEU   C CB  1 
ATOM   2298 C CG  . LEU   C 1 26  ? 7.122   -21.321 70.579 1.00 23.72  ? 26  LEU   C CG  1 
ATOM   2299 C CD1 . LEU   C 1 26  ? 8.170   -20.299 71.054 1.00 17.70  ? 26  LEU   C CD1 1 
ATOM   2300 C CD2 . LEU   C 1 26  ? 5.788   -20.666 70.274 1.00 20.99  ? 26  LEU   C CD2 1 
ATOM   2301 N N   . GLU   C 1 27  ? 9.245   -24.310 71.627 1.00 27.03  ? 27  GLU   C N   1 
ATOM   2302 C CA  . GLU   C 1 27  ? 9.049   -25.397 72.585 1.00 30.42  ? 27  GLU   C CA  1 
ATOM   2303 C C   . GLU   C 1 27  ? 9.516   -24.897 73.939 1.00 27.28  ? 27  GLU   C C   1 
ATOM   2304 O O   . GLU   C 1 27  ? 10.704  -24.622 74.116 1.00 32.85  ? 27  GLU   C O   1 
ATOM   2305 C CB  . GLU   C 1 27  ? 9.818   -26.647 72.156 1.00 24.67  ? 27  GLU   C CB  1 
ATOM   2306 C CG  . GLU   C 1 27  ? 9.743   -27.798 73.132 1.00 35.08  ? 27  GLU   C CG  1 
ATOM   2307 C CD  . GLU   C 1 27  ? 10.540  -29.003 72.639 1.00 46.18  ? 27  GLU   C CD  1 
ATOM   2308 O OE1 . GLU   C 1 27  ? 11.675  -28.806 72.145 1.00 45.61  ? 27  GLU   C OE1 1 
ATOM   2309 O OE2 . GLU   C 1 27  ? 10.031  -30.141 72.732 1.00 52.05  ? 27  GLU   C OE2 1 
ATOM   2310 N N   . LEU   C 1 28  ? 8.599   -24.779 74.889 1.00 29.19  ? 28  LEU   C N   1 
ATOM   2311 C CA  . LEU   C 1 28  ? 9.015   -24.210 76.156 1.00 30.60  ? 28  LEU   C CA  1 
ATOM   2312 C C   . LEU   C 1 28  ? 8.032   -24.500 77.278 1.00 27.36  ? 28  LEU   C C   1 
ATOM   2313 O O   . LEU   C 1 28  ? 6.861   -24.841 77.062 1.00 27.81  ? 28  LEU   C O   1 
ATOM   2314 C CB  . LEU   C 1 28  ? 9.316   -22.717 75.962 1.00 38.13  ? 28  LEU   C CB  1 
ATOM   2315 C CG  . LEU   C 1 28  ? 8.357   -21.786 75.231 1.00 34.07  ? 28  LEU   C CG  1 
ATOM   2316 C CD1 . LEU   C 1 28  ? 7.256   -21.333 76.124 1.00 47.38  ? 28  LEU   C CD1 1 
ATOM   2317 C CD2 . LEU   C 1 28  ? 9.130   -20.591 74.714 1.00 31.76  ? 28  LEU   C CD2 1 
ATOM   2318 N N   . LYS   C 1 29  ? 8.581   -24.427 78.494 1.00 31.54  ? 29  LYS   C N   1 
ATOM   2319 C CA  . LYS   C 1 29  ? 7.831   -24.544 79.733 1.00 29.25  ? 29  LYS   C CA  1 
ATOM   2320 C C   . LYS   C 1 29  ? 7.086   -23.259 80.057 1.00 20.90  ? 29  LYS   C C   1 
ATOM   2321 O O   . LYS   C 1 29  ? 7.474   -22.171 79.631 1.00 25.96  ? 29  LYS   C O   1 
ATOM   2322 C CB  . LYS   C 1 29  ? 8.743   -24.841 80.913 1.00 32.07  ? 29  LYS   C CB  1 
ATOM   2323 C CG  . LYS   C 1 29  ? 9.383   -26.157 80.936 1.00 47.29  ? 29  LYS   C CG  1 
ATOM   2324 C CD  . LYS   C 1 29  ? 10.109  -26.339 82.274 1.00 52.55  ? 29  LYS   C CD  1 
ATOM   2325 C CE  . LYS   C 1 29  ? 10.584  -27.783 82.373 1.00 57.19  ? 29  LYS   C CE  1 
ATOM   2326 N NZ  . LYS   C 1 29  ? 11.633  -28.035 81.235 1.00 62.82  ? 29  LYS   C NZ  1 
ATOM   2327 N N   . LEU   C 1 30  ? 5.986   -23.401 80.783 1.00 21.93  ? 30  LEU   C N   1 
ATOM   2328 C CA  . LEU   C 1 30  ? 5.281   -22.268 81.363 1.00 20.86  ? 30  LEU   C CA  1 
ATOM   2329 C C   . LEU   C 1 30  ? 5.327   -22.341 82.875 1.00 22.94  ? 30  LEU   C C   1 
ATOM   2330 O O   . LEU   C 1 30  ? 5.401   -23.421 83.465 1.00 25.46  ? 30  LEU   C O   1 
ATOM   2331 C CB  . LEU   C 1 30  ? 3.822   -22.227 80.918 1.00 23.07  ? 30  LEU   C CB  1 
ATOM   2332 C CG  . LEU   C 1 30  ? 3.542   -22.378 79.424 1.00 32.16  ? 30  LEU   C CG  1 
ATOM   2333 C CD1 . LEU   C 1 30  ? 2.120   -21.990 79.196 1.00 30.71  ? 30  LEU   C CD1 1 
ATOM   2334 C CD2 . LEU   C 1 30  ? 4.465   -21.489 78.608 1.00 28.73  ? 30  LEU   C CD2 1 
ATOM   2335 N N   . ALA   C 1 31  ? 5.217   -21.181 83.502 1.00 18.39  ? 31  ALA   C N   1 
ATOM   2336 C CA  . ALA   C 1 31  ? 5.125   -21.144 84.951 1.00 25.46  ? 31  ALA   C CA  1 
ATOM   2337 C C   . ALA   C 1 31  ? 4.190   -20.009 85.336 1.00 25.38  ? 31  ALA   C C   1 
ATOM   2338 O O   . ALA   C 1 31  ? 4.148   -18.975 84.660 1.00 25.11  ? 31  ALA   C O   1 
ATOM   2339 C CB  . ALA   C 1 31  ? 6.503   -20.960 85.606 1.00 17.16  ? 31  ALA   C CB  1 
ATOM   2340 N N   . LEU   C 1 32  ? 3.400   -20.240 86.380 1.00 27.97  ? 32  LEU   C N   1 
ATOM   2341 C CA  . LEU   C 1 32  ? 2.657   -19.169 87.024 1.00 22.34  ? 32  LEU   C CA  1 
ATOM   2342 C C   . LEU   C 1 32  ? 3.634   -18.101 87.506 1.00 23.90  ? 32  LEU   C C   1 
ATOM   2343 O O   . LEU   C 1 32  ? 4.715   -18.447 88.013 1.00 23.32  ? 32  LEU   C O   1 
ATOM   2344 C CB  . LEU   C 1 32  ? 1.856   -19.726 88.206 1.00 26.96  ? 32  LEU   C CB  1 
ATOM   2345 C CG  . LEU   C 1 32  ? 0.548   -20.472 87.894 1.00 32.95  ? 32  LEU   C CG  1 
ATOM   2346 C CD1 . LEU   C 1 32  ? 0.012   -21.104 89.159 1.00 23.67  ? 32  LEU   C CD1 1 
ATOM   2347 C CD2 . LEU   C 1 32  ? -0.490  -19.506 87.331 1.00 24.04  ? 32  LEU   C CD2 1 
ATOM   2348 N N   . PRO   C 1 33  ? 3.335   -16.817 87.344 1.00 24.98  ? 33  PRO   C N   1 
ATOM   2349 C CA  . PRO   C 1 33  ? 4.218   -15.790 87.896 1.00 23.98  ? 33  PRO   C CA  1 
ATOM   2350 C C   . PRO   C 1 33  ? 4.047   -15.716 89.410 1.00 29.15  ? 33  PRO   C C   1 
ATOM   2351 O O   . PRO   C 1 33  ? 3.121   -16.287 89.986 1.00 21.34  ? 33  PRO   C O   1 
ATOM   2352 C CB  . PRO   C 1 33  ? 3.766   -14.501 87.206 1.00 24.61  ? 33  PRO   C CB  1 
ATOM   2353 C CG  . PRO   C 1 33  ? 2.383   -14.778 86.760 1.00 19.61  ? 33  PRO   C CG  1 
ATOM   2354 C CD  . PRO   C 1 33  ? 2.273   -16.236 86.491 1.00 23.44  ? 33  PRO   C CD  1 
ATOM   2355 N N   . LYS   C 1 34  ? 4.986   -15.017 90.052 1.00 31.26  ? 34  LYS   C N   1 
ATOM   2356 C CA  . LYS   C 1 34  ? 4.959   -14.848 91.510 1.00 30.45  ? 34  LYS   C CA  1 
ATOM   2357 C C   . LYS   C 1 34  ? 3.658   -14.230 91.965 1.00 38.99  ? 34  LYS   C C   1 
ATOM   2358 O O   . LYS   C 1 34  ? 3.124   -14.593 93.018 1.00 31.10  ? 34  LYS   C O   1 
ATOM   2359 C CB  . LYS   C 1 34  ? 6.100   -13.947 91.960 1.00 33.96  ? 34  LYS   C CB  1 
ATOM   2360 C CG  . LYS   C 1 34  ? 7.483   -14.468 91.645 1.00 49.45  ? 34  LYS   C CG  1 
ATOM   2361 C CD  . LYS   C 1 34  ? 7.901   -15.612 92.548 1.00 55.49  ? 34  LYS   C CD  1 
ATOM   2362 C CE  . LYS   C 1 34  ? 9.256   -16.168 92.154 1.00 53.06  ? 34  LYS   C CE  1 
ATOM   2363 N NZ  . LYS   C 1 34  ? 10.434  -15.207 92.290 1.00 54.15  ? 34  LYS   C NZ  1 
ATOM   2364 N N   . GLU   C 1 35  ? 3.128   -13.295 91.169 1.00 36.13  ? 35  GLU   C N   1 
ATOM   2365 C CA  . GLU   C 1 35  ? 1.913   -12.580 91.539 1.00 31.80  ? 35  GLU   C CA  1 
ATOM   2366 C C   . GLU   C 1 35  ? 0.710   -13.496 91.528 1.00 33.06  ? 35  GLU   C C   1 
ATOM   2367 O O   . GLU   C 1 35  ? -0.284  -13.217 92.204 1.00 38.34  ? 35  GLU   C O   1 
ATOM   2368 C CB  . GLU   C 1 35  ? 1.686   -11.388 90.601 1.00 28.56  ? 35  GLU   C CB  1 
ATOM   2369 C CG  . GLU   C 1 35  ? 2.825   -10.380 90.644 1.00 31.20  ? 35  GLU   C CG  1 
ATOM   2370 C CD  . GLU   C 1 35  ? 3.852   -10.626 89.562 1.00 40.23  ? 35  GLU   C CD  1 
ATOM   2371 O OE1 . GLU   C 1 35  ? 4.362   -9.630  88.997 1.00 43.12  ? 35  GLU   C OE1 1 
ATOM   2372 O OE2 . GLU   C 1 35  ? 4.146   -11.815 89.266 1.00 31.31  ? 35  GLU   C OE2 1 
ATOM   2373 N N   . LEU   C 1 36  ? 0.779   -14.594 90.780 1.00 32.18  ? 36  LEU   C N   1 
ATOM   2374 C CA  . LEU   C 1 36  ? -0.284  -15.587 90.769 1.00 29.83  ? 36  LEU   C CA  1 
ATOM   2375 C C   . LEU   C 1 36  ? 0.083   -16.845 91.565 1.00 31.35  ? 36  LEU   C C   1 
ATOM   2376 O O   . LEU   C 1 36  ? -0.594  -17.871 91.432 1.00 34.64  ? 36  LEU   C O   1 
ATOM   2377 C CB  . LEU   C 1 36  ? -0.651  -15.939 89.320 1.00 34.05  ? 36  LEU   C CB  1 
ATOM   2378 C CG  . LEU   C 1 36  ? -0.916  -14.775 88.341 1.00 29.54  ? 36  LEU   C CG  1 
ATOM   2379 C CD1 . LEU   C 1 36  ? -1.561  -15.276 87.044 1.00 35.66  ? 36  LEU   C CD1 1 
ATOM   2380 C CD2 . LEU   C 1 36  ? -1.760  -13.656 88.956 1.00 31.04  ? 36  LEU   C CD2 1 
ATOM   2381 N N   . GLY   C 1 37  ? 1.146   -16.795 92.366 1.00 28.36  ? 37  GLY   C N   1 
ATOM   2382 C CA  . GLY   C 1 37  ? 1.507   -17.925 93.216 1.00 40.86  ? 37  GLY   C CA  1 
ATOM   2383 C C   . GLY   C 1 37  ? 2.427   -18.972 92.612 1.00 45.75  ? 37  GLY   C C   1 
ATOM   2384 O O   . GLY   C 1 37  ? 2.339   -20.157 92.975 1.00 43.44  ? 37  GLY   C O   1 
ATOM   2385 N N   . GLY   C 1 38  ? 3.315   -18.573 91.703 1.00 34.94  ? 38  GLY   C N   1 
ATOM   2386 C CA  . GLY   C 1 38  ? 4.250   -19.492 91.095 1.00 22.44  ? 38  GLY   C CA  1 
ATOM   2387 C C   . GLY   C 1 38  ? 5.669   -18.974 91.171 1.00 31.89  ? 38  GLY   C C   1 
ATOM   2388 O O   . GLY   C 1 38  ? 5.935   -17.966 91.843 1.00 33.75  ? 38  GLY   C O   1 
ATOM   2389 N N   . LYS   C 1 39  ? 6.594   -19.652 90.495 1.00 19.23  ? 39  LYS   C N   1 
ATOM   2390 C CA  . LYS   C 1 39  ? 7.994   -19.276 90.549 1.00 25.09  ? 39  LYS   C CA  1 
ATOM   2391 C C   . LYS   C 1 39  ? 8.368   -18.203 89.526 1.00 32.66  ? 39  LYS   C C   1 
ATOM   2392 O O   . LYS   C 1 39  ? 9.429   -17.579 89.665 1.00 25.13  ? 39  LYS   C O   1 
ATOM   2393 C CB  . LYS   C 1 39  ? 8.880   -20.509 90.314 1.00 22.27  ? 39  LYS   C CB  1 
ATOM   2394 C CG  . LYS   C 1 39  ? 8.833   -21.577 91.410 1.00 21.99  ? 39  LYS   C CG  1 
ATOM   2395 C CD  . LYS   C 1 39  ? 9.884   -22.641 91.131 1.00 25.10  ? 39  LYS   C CD  1 
ATOM   2396 C CE  . LYS   C 1 39  ? 9.908   -23.723 92.200 1.00 25.76  ? 39  LYS   C CE  1 
ATOM   2397 N NZ  . LYS   C 1 39  ? 8.617   -24.488 92.247 1.00 27.46  ? 39  LYS   C NZ  1 
ATOM   2398 N N   . GLY   C 1 40  ? 7.555   -18.013 88.484 1.00 24.89  ? 40  GLY   C N   1 
ATOM   2399 C CA  . GLY   C 1 40  ? 7.903   -17.086 87.412 1.00 26.07  ? 40  GLY   C CA  1 
ATOM   2400 C C   . GLY   C 1 40  ? 9.253   -17.349 86.778 1.00 21.11  ? 40  GLY   C C   1 
ATOM   2401 O O   . GLY   C 1 40  ? 9.886   -16.414 86.282 1.00 22.69  ? 40  GLY   C O   1 
ATOM   2402 N N   . ASP   C 1 41  ? 9.723   -18.594 86.794 1.00 20.09  ? 41  ASP   C N   1 
ATOM   2403 C CA  . ASP   C 1 41  ? 10.993  -18.954 86.176 1.00 18.48  ? 41  ASP   C CA  1 
ATOM   2404 C C   . ASP   C 1 41  ? 10.828  -19.433 84.737 1.00 27.01  ? 41  ASP   C C   1 
ATOM   2405 O O   . ASP   C 1 41  ? 11.754  -20.056 84.191 1.00 22.64  ? 41  ASP   C O   1 
ATOM   2406 C CB  . ASP   C 1 41  ? 11.690  -20.037 86.999 1.00 19.08  ? 41  ASP   C CB  1 
ATOM   2407 C CG  . ASP   C 1 41  ? 10.879  -21.336 87.065 1.00 27.21  ? 41  ASP   C CG  1 
ATOM   2408 O OD1 . ASP   C 1 41  ? 9.625   -21.283 87.037 1.00 27.15  ? 41  ASP   C OD1 1 
ATOM   2409 O OD2 . ASP   C 1 41  ? 11.492  -22.415 87.155 1.00 26.82  ? 41  ASP   C OD2 1 
ATOM   2410 N N   . ALA   C 1 42  ? 9.649   -19.217 84.149 1.00 21.63  ? 42  ALA   C N   1 
ATOM   2411 C CA  . ALA   C 1 42  ? 9.345   -19.545 82.760 1.00 26.93  ? 42  ALA   C CA  1 
ATOM   2412 C C   . ALA   C 1 42  ? 8.217   -18.611 82.315 1.00 21.93  ? 42  ALA   C C   1 
ATOM   2413 O O   . ALA   C 1 42  ? 7.665   -17.859 83.127 1.00 17.04  ? 42  ALA   C O   1 
ATOM   2414 C CB  . ALA   C 1 42  ? 8.985   -21.031 82.600 1.00 18.32  ? 42  ALA   C CB  1 
ATOM   2415 N N   . THR   C 1 43  ? 7.924   -18.622 81.005 1.00 21.29  ? 43  THR   C N   1 
ATOM   2416 C CA  . THR   C 1 43  ? 6.990   -17.668 80.405 1.00 16.11  ? 43  THR   C CA  1 
ATOM   2417 C C   . THR   C 1 43  ? 5.546   -18.084 80.703 1.00 20.51  ? 43  THR   C C   1 
ATOM   2418 O O   . THR   C 1 43  ? 5.285   -19.105 81.345 1.00 18.73  ? 43  THR   C O   1 
ATOM   2419 C CB  . THR   C 1 43  ? 7.232   -17.556 78.896 1.00 29.61  ? 43  THR   C CB  1 
ATOM   2420 O OG1 . THR   C 1 43  ? 6.646   -16.337 78.376 1.00 18.50  ? 43  THR   C OG1 1 
ATOM   2421 C CG2 . THR   C 1 43  ? 6.606   -18.751 78.178 1.00 21.79  ? 43  THR   C CG2 1 
ATOM   2422 N N   . ASN   C 1 44  ? 4.586   -17.293 80.223 1.00 16.81  ? 44  ASN   C N   1 
ATOM   2423 C CA  . ASN   C 1 44  ? 3.190   -17.474 80.585 1.00 20.37  ? 44  ASN   C CA  1 
ATOM   2424 C C   . ASN   C 1 44  ? 2.310   -17.005 79.434 1.00 24.82  ? 44  ASN   C C   1 
ATOM   2425 O O   . ASN   C 1 44  ? 2.805   -16.386 78.482 1.00 17.43  ? 44  ASN   C O   1 
ATOM   2426 C CB  . ASN   C 1 44  ? 2.850   -16.712 81.878 1.00 19.77  ? 44  ASN   C CB  1 
ATOM   2427 C CG  . ASN   C 1 44  ? 3.153   -15.223 81.793 1.00 19.98  ? 44  ASN   C CG  1 
ATOM   2428 O OD1 . ASN   C 1 44  ? 2.490   -14.466 81.069 1.00 17.32  ? 44  ASN   C OD1 1 
ATOM   2429 N ND2 . ASN   C 1 44  ? 4.134   -14.783 82.584 1.00 19.28  ? 44  ASN   C ND2 1 
ATOM   2430 N N   . PRO   C 1 45  ? 0.996   -17.275 79.486 1.00 20.00  ? 45  PRO   C N   1 
ATOM   2431 C CA  . PRO   C 1 45  ? 0.135   -16.860 78.355 1.00 25.09  ? 45  PRO   C CA  1 
ATOM   2432 C C   . PRO   C 1 45  ? 0.162   -15.365 78.059 1.00 20.20  ? 45  PRO   C C   1 
ATOM   2433 O O   . PRO   C 1 45  ? 0.155   -14.976 76.883 1.00 21.72  ? 45  PRO   C O   1 
ATOM   2434 C CB  . PRO   C 1 45  ? -1.267  -17.329 78.787 1.00 21.67  ? 45  PRO   C CB  1 
ATOM   2435 C CG  . PRO   C 1 45  ? -0.970  -18.558 79.622 1.00 20.10  ? 45  PRO   C CG  1 
ATOM   2436 C CD  . PRO   C 1 45  ? 0.237   -18.104 80.447 1.00 20.72  ? 45  PRO   C CD  1 
ATOM   2437 N N   . GLU   C 1 46  ? 0.201   -14.515 79.088 1.00 17.57  ? 46  GLU   C N   1 
ATOM   2438 C CA  . GLU   C 1 46  ? 0.191   -13.068 78.873 1.00 14.79  ? 46  GLU   C CA  1 
ATOM   2439 C C   . GLU   C 1 46  ? 1.457   -12.586 78.175 1.00 22.04  ? 46  GLU   C C   1 
ATOM   2440 O O   . GLU   C 1 46  ? 1.389   -11.697 77.316 1.00 14.85  ? 46  GLU   C O   1 
ATOM   2441 C CB  . GLU   C 1 46  ? 0.015   -12.323 80.200 1.00 18.86  ? 46  GLU   C CB  1 
ATOM   2442 C CG  . GLU   C 1 46  ? -1.406  -12.363 80.749 1.00 23.39  ? 46  GLU   C CG  1 
ATOM   2443 C CD  . GLU   C 1 46  ? -1.842  -13.783 81.098 1.00 27.01  ? 46  GLU   C CD  1 
ATOM   2444 O OE1 . GLU   C 1 46  ? -1.100  -14.464 81.847 1.00 24.78  ? 46  GLU   C OE1 1 
ATOM   2445 O OE2 . GLU   C 1 46  ? -2.890  -14.229 80.582 1.00 23.71  ? 46  GLU   C OE2 1 
ATOM   2446 N N   . GLN   C 1 47  ? 2.621   -13.124 78.561 1.00 15.71  ? 47  GLN   C N   1 
ATOM   2447 C CA  . GLN   C 1 47  ? 3.870   -12.776 77.884 1.00 20.39  ? 47  GLN   C CA  1 
ATOM   2448 C C   . GLN   C 1 47  ? 3.873   -13.251 76.436 1.00 14.55  ? 47  GLN   C C   1 
ATOM   2449 O O   . GLN   C 1 47  ? 4.388   -12.554 75.557 1.00 15.66  ? 47  GLN   C O   1 
ATOM   2450 C CB  . GLN   C 1 47  ? 5.090   -13.399 78.584 1.00 22.04  ? 47  GLN   C CB  1 
ATOM   2451 C CG  . GLN   C 1 47  ? 5.613   -12.680 79.765 1.00 25.58  ? 47  GLN   C CG  1 
ATOM   2452 C CD  . GLN   C 1 47  ? 6.954   -13.232 80.274 1.00 21.67  ? 47  GLN   C CD  1 
ATOM   2453 O OE1 . GLN   C 1 47  ? 7.392   -14.324 79.896 1.00 19.33  ? 47  GLN   C OE1 1 
ATOM   2454 N NE2 . GLN   C 1 47  ? 7.596   -12.471 81.151 1.00 22.40  ? 47  GLN   C NE2 1 
ATOM   2455 N N   . LEU   C 1 48  ? 3.368   -14.461 76.180 1.00 13.95  ? 48  LEU   C N   1 
ATOM   2456 C CA  . LEU   C 1 48  ? 3.285   -14.945 74.804 1.00 14.53  ? 48  LEU   C CA  1 
ATOM   2457 C C   . LEU   C 1 48  ? 2.422   -14.007 73.963 1.00 15.13  ? 48  LEU   C C   1 
ATOM   2458 O O   . LEU   C 1 48  ? 2.828   -13.573 72.870 1.00 13.41  ? 48  LEU   C O   1 
ATOM   2459 C CB  . LEU   C 1 48  ? 2.729   -16.372 74.781 1.00 13.24  ? 48  LEU   C CB  1 
ATOM   2460 C CG  . LEU   C 1 48  ? 3.641   -17.420 75.439 1.00 19.23  ? 48  LEU   C CG  1 
ATOM   2461 C CD1 . LEU   C 1 48  ? 2.889   -18.740 75.641 1.00 18.42  ? 48  LEU   C CD1 1 
ATOM   2462 C CD2 . LEU   C 1 48  ? 4.912   -17.621 74.658 1.00 14.26  ? 48  LEU   C CD2 1 
ATOM   2463 N N   . PHE   C 1 49  ? 1.247   -13.646 74.483 1.00 12.77  ? 49  PHE   C N   1 
ATOM   2464 C CA  . PHE   C 1 49  ? 0.376   -12.715 73.767 1.00 11.81  ? 49  PHE   C CA  1 
ATOM   2465 C C   . PHE   C 1 49  ? 1.062   -11.372 73.547 1.00 17.20  ? 49  PHE   C C   1 
ATOM   2466 O O   . PHE   C 1 49  ? 1.027   -10.824 72.435 1.00 17.40  ? 49  PHE   C O   1 
ATOM   2467 C CB  . PHE   C 1 49  ? -0.939  -12.522 74.519 1.00 16.36  ? 49  PHE   C CB  1 
ATOM   2468 C CG  . PHE   C 1 49  ? -1.934  -11.622 73.806 1.00 22.65  ? 49  PHE   C CG  1 
ATOM   2469 C CD1 . PHE   C 1 49  ? -2.528  -12.010 72.607 1.00 22.95  ? 49  PHE   C CD1 1 
ATOM   2470 C CD2 . PHE   C 1 49  ? -2.292  -10.405 74.340 1.00 17.59  ? 49  PHE   C CD2 1 
ATOM   2471 C CE1 . PHE   C 1 49  ? -3.452  -11.173 71.956 1.00 15.49  ? 49  PHE   C CE1 1 
ATOM   2472 C CE2 . PHE   C 1 49  ? -3.211  -9.569  73.679 1.00 22.14  ? 49  PHE   C CE2 1 
ATOM   2473 C CZ  . PHE   C 1 49  ? -3.791  -9.966  72.497 1.00 19.09  ? 49  PHE   C CZ  1 
ATOM   2474 N N   . ALA   C 1 50  ? 1.678   -10.821 74.602 1.00 14.25  ? 50  ALA   C N   1 
ATOM   2475 C CA  . ALA   C 1 50  ? 2.356   -9.533  74.489 1.00 14.86  ? 50  ALA   C CA  1 
ATOM   2476 C C   . ALA   C 1 50  ? 3.413   -9.577  73.403 1.00 17.29  ? 50  ALA   C C   1 
ATOM   2477 O O   . ALA   C 1 50  ? 3.545   -8.640  72.605 1.00 13.03  ? 50  ALA   C O   1 
ATOM   2478 C CB  . ALA   C 1 50  ? 2.991   -9.131  75.827 1.00 11.76  ? 50  ALA   C CB  1 
ATOM   2479 N N   . ALA   C 1 51  ? 4.188   -10.670 73.364 1.00 18.30  ? 51  ALA   C N   1 
ATOM   2480 C CA  . ALA   C 1 51  ? 5.252   -10.784 72.370 1.00 20.61  ? 51  ALA   C CA  1 
ATOM   2481 C C   . ALA   C 1 51  ? 4.676   -10.825 70.964 1.00 12.99  ? 51  ALA   C C   1 
ATOM   2482 O O   . ALA   C 1 51  ? 5.122   -10.093 70.065 1.00 16.93  ? 51  ALA   C O   1 
ATOM   2483 C CB  . ALA   C 1 51  ? 6.091   -12.038 72.652 1.00 16.04  ? 51  ALA   C CB  1 
ATOM   2484 N N   . GLY   C 1 52  ? 3.682   -11.683 70.755 1.00 12.77  ? 52  GLY   C N   1 
ATOM   2485 C CA  . GLY   C 1 52  ? 3.119   -11.820 69.426 1.00 13.71  ? 52  GLY   C CA  1 
ATOM   2486 C C   . GLY   C 1 52  ? 2.515   -10.518 68.931 1.00 19.69  ? 52  GLY   C C   1 
ATOM   2487 O O   . GLY   C 1 52  ? 2.707   -10.119 67.766 1.00 16.69  ? 52  GLY   C O   1 
ATOM   2488 N N   . TYR   C 1 53  ? 1.825   -9.806  69.822 1.00 14.62  ? 53  TYR   C N   1 
ATOM   2489 C CA  . TYR   C 1 53  ? 1.159   -8.579  69.396 1.00 17.85  ? 53  TYR   C CA  1 
ATOM   2490 C C   . TYR   C 1 53  ? 2.133   -7.417  69.227 1.00 18.30  ? 53  TYR   C C   1 
ATOM   2491 O O   . TYR   C 1 53  ? 2.032   -6.670  68.253 1.00 21.12  ? 53  TYR   C O   1 
ATOM   2492 C CB  . TYR   C 1 53  ? -0.031  -8.285  70.319 1.00 16.69  ? 53  TYR   C CB  1 
ATOM   2493 C CG  . TYR   C 1 53  ? -0.821  -7.003  70.116 1.00 14.05  ? 53  TYR   C CG  1 
ATOM   2494 C CD1 . TYR   C 1 53  ? -1.105  -6.538  68.848 1.00 21.09  ? 53  TYR   C CD1 1 
ATOM   2495 C CD2 . TYR   C 1 53  ? -1.688  -6.593  71.118 1.00 18.98  ? 53  TYR   C CD2 1 
ATOM   2496 C CE1 . TYR   C 1 53  ? -1.936  -5.451  68.632 1.00 18.21  ? 53  TYR   C CE1 1 
ATOM   2497 C CE2 . TYR   C 1 53  ? -2.583  -5.532  70.916 1.00 24.77  ? 53  TYR   C CE2 1 
ATOM   2498 C CZ  . TYR   C 1 53  ? -2.698  -4.969  69.653 1.00 21.70  ? 53  TYR   C CZ  1 
ATOM   2499 O OH  . TYR   C 1 53  ? -3.564  -3.923  69.402 1.00 21.34  ? 53  TYR   C OH  1 
ATOM   2500 N N   . ALA   C 1 54  ? 3.151   -7.304  70.069 1.00 14.49  ? 54  ALA   C N   1 
ATOM   2501 C CA  . ALA   C 1 54  ? 4.124   -6.250  69.815 1.00 11.63  ? 54  ALA   C CA  1 
ATOM   2502 C C   . ALA   C 1 54  ? 4.873   -6.498  68.502 1.00 18.30  ? 54  ALA   C C   1 
ATOM   2503 O O   . ALA   C 1 54  ? 5.126   -5.556  67.743 1.00 14.65  ? 54  ALA   C O   1 
ATOM   2504 C CB  . ALA   C 1 54  ? 5.098   -6.122  70.983 1.00 13.13  ? 54  ALA   C CB  1 
ATOM   2505 N N   . ALA   C 1 55  ? 5.207   -7.766  68.196 1.00 14.52  ? 55  ALA   C N   1 
ATOM   2506 C CA  . ALA   C 1 55  ? 5.960   -8.045  66.977 1.00 16.50  ? 55  ALA   C CA  1 
ATOM   2507 C C   . ALA   C 1 55  ? 5.117   -7.776  65.734 1.00 17.03  ? 55  ALA   C C   1 
ATOM   2508 O O   . ALA   C 1 55  ? 5.563   -7.095  64.806 1.00 15.16  ? 55  ALA   C O   1 
ATOM   2509 C CB  . ALA   C 1 55  ? 6.473   -9.484  66.965 1.00 11.52  ? 55  ALA   C CB  1 
ATOM   2510 N N   . CYS   C 1 56  ? 3.891   -8.303  65.704 1.00 18.27  ? 56  CYS   C N   1 
ATOM   2511 C CA  . CYS   C 1 56  ? 3.018   -8.083  64.561 1.00 16.88  ? 56  CYS   C CA  1 
ATOM   2512 C C   . CYS   C 1 56  ? 2.663   -6.608  64.398 1.00 23.83  ? 56  CYS   C C   1 
ATOM   2513 O O   . CYS   C 1 56  ? 2.558   -6.108  63.268 1.00 16.30  ? 56  CYS   C O   1 
ATOM   2514 C CB  . CYS   C 1 56  ? 1.747   -8.916  64.706 1.00 17.04  ? 56  CYS   C CB  1 
ATOM   2515 S SG  . CYS   C 1 56  ? 0.516   -8.508  63.454 1.00 26.84  ? 56  CYS   C SG  1 
ATOM   2516 N N   . PHE   C 1 57  ? 2.474   -5.887  65.508 1.00 18.65  ? 57  PHE   C N   1 
ATOM   2517 C CA  . PHE   C 1 57  ? 2.184   -4.465  65.379 1.00 18.36  ? 57  PHE   C CA  1 
ATOM   2518 C C   . PHE   C 1 57  ? 3.378   -3.714  64.801 1.00 18.96  ? 57  PHE   C C   1 
ATOM   2519 O O   . PHE   C 1 57  ? 3.213   -2.852  63.930 1.00 16.06  ? 57  PHE   C O   1 
ATOM   2520 C CB  . PHE   C 1 57  ? 1.771   -3.866  66.724 1.00 11.88  ? 57  PHE   C CB  1 
ATOM   2521 C CG  . PHE   C 1 57  ? 1.081   -2.540  66.596 1.00 15.17  ? 57  PHE   C CG  1 
ATOM   2522 C CD1 . PHE   C 1 57  ? -0.296  -2.474  66.429 1.00 17.42  ? 57  PHE   C CD1 1 
ATOM   2523 C CD2 . PHE   C 1 57  ? 1.810   -1.350  66.619 1.00 18.17  ? 57  PHE   C CD2 1 
ATOM   2524 C CE1 . PHE   C 1 57  ? -0.941  -1.259  66.307 1.00 13.26  ? 57  PHE   C CE1 1 
ATOM   2525 C CE2 . PHE   C 1 57  ? 1.160   -0.122  66.492 1.00 15.32  ? 57  PHE   C CE2 1 
ATOM   2526 C CZ  . PHE   C 1 57  ? -0.217  -0.088  66.344 1.00 17.11  ? 57  PHE   C CZ  1 
ATOM   2527 N N   . GLY   C 1 58  ? 4.587   -4.012  65.282 1.00 16.39  ? 58  GLY   C N   1 
ATOM   2528 C CA  . GLY   C 1 58  ? 5.756   -3.364  64.717 1.00 13.90  ? 58  GLY   C CA  1 
ATOM   2529 C C   . GLY   C 1 58  ? 5.905   -3.657  63.236 1.00 16.66  ? 58  GLY   C C   1 
ATOM   2530 O O   . GLY   C 1 58  ? 6.260   -2.775  62.438 1.00 14.65  ? 58  GLY   C O   1 
ATOM   2531 N N   . ASN   C 1 59  ? 5.636   -4.911  62.847 1.00 20.25  ? 59  ASN   C N   1 
ATOM   2532 C CA  . ASN   C 1 59  ? 5.678   -5.262  61.428 1.00 20.75  ? 59  ASN   C CA  1 
ATOM   2533 C C   . ASN   C 1 59  ? 4.682   -4.441  60.636 1.00 16.57  ? 59  ASN   C C   1 
ATOM   2534 O O   . ASN   C 1 59  ? 4.989   -3.939  59.548 1.00 18.32  ? 59  ASN   C O   1 
ATOM   2535 C CB  . ASN   C 1 59  ? 5.384   -6.739  61.213 1.00 21.04  ? 59  ASN   C CB  1 
ATOM   2536 C CG  . ASN   C 1 59  ? 5.874   -7.213  59.867 1.00 17.86  ? 59  ASN   C CG  1 
ATOM   2537 O OD1 . ASN   C 1 59  ? 7.064   -7.470  59.698 1.00 22.09  ? 59  ASN   C OD1 1 
ATOM   2538 N ND2 . ASN   C 1 59  ? 4.977   -7.260  58.889 1.00 18.96  ? 59  ASN   C ND2 1 
ATOM   2539 N N   . ALA   C 1 60  ? 3.469   -4.311  61.162 1.00 19.69  ? 60  ALA   C N   1 
ATOM   2540 C CA  . ALA   C 1 60  ? 2.463   -3.542  60.461 1.00 17.90  ? 60  ALA   C CA  1 
ATOM   2541 C C   . ALA   C 1 60  ? 2.837   -2.070  60.385 1.00 23.01  ? 60  ALA   C C   1 
ATOM   2542 O O   . ALA   C 1 60  ? 2.486   -1.396  59.408 1.00 19.85  ? 60  ALA   C O   1 
ATOM   2543 C CB  . ALA   C 1 60  ? 1.114   -3.713  61.146 1.00 15.02  ? 60  ALA   C CB  1 
ATOM   2544 N N   . VAL   C 1 61  ? 3.513   -1.541  61.417 1.00 18.16  ? 61  VAL   C N   1 
ATOM   2545 C CA  . VAL   C 1 61  ? 3.983   -0.160  61.356 1.00 15.90  ? 61  VAL   C CA  1 
ATOM   2546 C C   . VAL   C 1 61  ? 4.957   -0.006  60.200 1.00 22.17  ? 61  VAL   C C   1 
ATOM   2547 O O   . VAL   C 1 61  ? 4.860   0.951   59.424 1.00 18.90  ? 61  VAL   C O   1 
ATOM   2548 C CB  . VAL   C 1 61  ? 4.629   0.294   62.682 1.00 13.71  ? 61  VAL   C CB  1 
ATOM   2549 C CG1 . VAL   C 1 61  ? 5.444   1.565   62.442 1.00 22.24  ? 61  VAL   C CG1 1 
ATOM   2550 C CG2 . VAL   C 1 61  ? 3.591   0.574   63.755 1.00 11.68  ? 61  VAL   C CG2 1 
ATOM   2551 N N   . ILE   C 1 62  ? 5.909   -0.943  60.069 1.00 16.40  ? 62  ILE   C N   1 
ATOM   2552 C CA  . ILE   C 1 62  ? 6.876   -0.887  58.971 1.00 16.42  ? 62  ILE   C CA  1 
ATOM   2553 C C   . ILE   C 1 62  ? 6.145   -0.896  57.634 1.00 30.21  ? 62  ILE   C C   1 
ATOM   2554 O O   . ILE   C 1 62  ? 6.387   -0.054  56.758 1.00 30.13  ? 62  ILE   C O   1 
ATOM   2555 C CB  . ILE   C 1 62  ? 7.871   -2.060  59.049 1.00 29.90  ? 62  ILE   C CB  1 
ATOM   2556 C CG1 . ILE   C 1 62  ? 8.752   -1.993  60.295 1.00 23.28  ? 62  ILE   C CG1 1 
ATOM   2557 C CG2 . ILE   C 1 62  ? 8.725   -2.156  57.764 1.00 29.29  ? 62  ILE   C CG2 1 
ATOM   2558 C CD1 . ILE   C 1 62  ? 9.430   -3.325  60.600 1.00 20.44  ? 62  ILE   C CD1 1 
ATOM   2559 N N   . HIS   C 1 63  ? 5.252   -1.874  57.465 1.00 24.42  ? 63  HIS   C N   1 
ATOM   2560 C CA  . HIS   C 1 63  ? 4.490   -2.031  56.234 1.00 25.20  ? 63  HIS   C CA  1 
ATOM   2561 C C   . HIS   C 1 63  ? 3.730   -0.750  55.882 1.00 31.32  ? 63  HIS   C C   1 
ATOM   2562 O O   . HIS   C 1 63  ? 3.753   -0.304  54.731 1.00 31.70  ? 63  HIS   C O   1 
ATOM   2563 C CB  . HIS   C 1 63  ? 3.564   -3.245  56.392 1.00 30.41  ? 63  HIS   C CB  1 
ATOM   2564 C CG  . HIS   C 1 63  ? 2.498   -3.371  55.343 1.00 45.17  ? 63  HIS   C CG  1 
ATOM   2565 N ND1 . HIS   C 1 63  ? 1.419   -2.512  55.266 1.00 41.72  ? 63  HIS   C ND1 1 
ATOM   2566 C CD2 . HIS   C 1 63  ? 2.317   -4.285  54.358 1.00 47.69  ? 63  HIS   C CD2 1 
ATOM   2567 C CE1 . HIS   C 1 63  ? 0.638   -2.871  54.264 1.00 43.48  ? 63  HIS   C CE1 1 
ATOM   2568 N NE2 . HIS   C 1 63  ? 1.162   -3.943  53.694 1.00 53.98  ? 63  HIS   C NE2 1 
ATOM   2569 N N   . VAL   C 1 64  ? 3.111   -0.099  56.874 1.00 30.65  ? 64  VAL   C N   1 
ATOM   2570 C CA  . VAL   C 1 64  ? 2.366   1.133   56.608 1.00 22.47  ? 64  VAL   C CA  1 
ATOM   2571 C C   . VAL   C 1 64  ? 3.302   2.282   56.234 1.00 37.71  ? 64  VAL   C C   1 
ATOM   2572 O O   . VAL   C 1 64  ? 3.023   3.055   55.301 1.00 31.82  ? 64  VAL   C O   1 
ATOM   2573 C CB  . VAL   C 1 64  ? 1.490   1.505   57.814 1.00 29.10  ? 64  VAL   C CB  1 
ATOM   2574 C CG1 . VAL   C 1 64  ? 0.996   2.944   57.701 1.00 25.10  ? 64  VAL   C CG1 1 
ATOM   2575 C CG2 . VAL   C 1 64  ? 0.299   0.544   57.921 1.00 22.48  ? 64  VAL   C CG2 1 
ATOM   2576 N N   . THR   C 1 65  ? 4.405   2.440   56.969 1.00 24.37  ? 65  THR   C N   1 
ATOM   2577 C CA  . THR   C 1 65  ? 5.340   3.509   56.646 1.00 28.33  ? 65  THR   C CA  1 
ATOM   2578 C C   . THR   C 1 65  ? 5.872   3.350   55.222 1.00 37.83  ? 65  THR   C C   1 
ATOM   2579 O O   . THR   C 1 65  ? 5.999   4.330   54.475 1.00 40.33  ? 65  THR   C O   1 
ATOM   2580 C CB  . THR   C 1 65  ? 6.499   3.534   57.644 1.00 27.00  ? 65  THR   C CB  1 
ATOM   2581 O OG1 . THR   C 1 65  ? 5.999   3.558   58.987 1.00 23.41  ? 65  THR   C OG1 1 
ATOM   2582 C CG2 . THR   C 1 65  ? 7.341   4.795   57.426 1.00 33.42  ? 65  THR   C CG2 1 
ATOM   2583 N N   . ARG   C 1 66  ? 6.168   2.114   54.814 1.00 35.63  ? 66  ARG   C N   1 
ATOM   2584 C CA  . ARG   C 1 66  ? 6.788   1.919   53.508 1.00 34.64  ? 66  ARG   C CA  1 
ATOM   2585 C C   . ARG   C 1 66  ? 5.767   1.964   52.381 1.00 41.17  ? 66  ARG   C C   1 
ATOM   2586 O O   . ARG   C 1 66  ? 6.092   2.369   51.256 1.00 39.33  ? 66  ARG   C O   1 
ATOM   2587 C CB  . ARG   C 1 66  ? 7.571   0.619   53.505 1.00 43.95  ? 66  ARG   C CB  1 
ATOM   2588 C CG  . ARG   C 1 66  ? 8.831   0.744   54.304 1.00 44.37  ? 66  ARG   C CG  1 
ATOM   2589 C CD  . ARG   C 1 66  ? 9.525   -0.571  54.496 1.00 46.05  ? 66  ARG   C CD  1 
ATOM   2590 N NE  . ARG   C 1 66  ? 10.696  -0.352  55.333 1.00 53.50  ? 66  ARG   C NE  1 
ATOM   2591 C CZ  . ARG   C 1 66  ? 11.478  -1.313  55.806 1.00 50.94  ? 66  ARG   C CZ  1 
ATOM   2592 N NH1 . ARG   C 1 66  ? 11.213  -2.586  55.535 1.00 52.17  ? 66  ARG   C NH1 1 
ATOM   2593 N NH2 . ARG   C 1 66  ? 12.522  -0.996  56.564 1.00 57.36  ? 66  ARG   C NH2 1 
ATOM   2594 N N   . SER   C 1 67  ? 4.529   1.562   52.658 1.00 46.53  ? 67  SER   C N   1 
ATOM   2595 C CA  . SER   C 1 67  ? 3.477   1.730   51.671 1.00 45.58  ? 67  SER   C CA  1 
ATOM   2596 C C   . SER   C 1 67  ? 3.083   3.193   51.521 1.00 42.66  ? 67  SER   C C   1 
ATOM   2597 O O   . SER   C 1 67  ? 2.511   3.569   50.492 1.00 45.59  ? 67  SER   C O   1 
ATOM   2598 C CB  . SER   C 1 67  ? 2.268   0.886   52.059 1.00 44.38  ? 67  SER   C CB  1 
ATOM   2599 O OG  . SER   C 1 67  ? 1.410   1.635   52.899 1.00 56.84  ? 67  SER   C OG  1 
ATOM   2600 N N   . ASN   C 1 68  ? 3.391   4.034   52.517 1.00 36.71  ? 68  ASN   C N   1 
ATOM   2601 C CA  . ASN   C 1 68  ? 3.028   5.449   52.424 1.00 42.75  ? 68  ASN   C CA  1 
ATOM   2602 C C   . ASN   C 1 68  ? 3.901   6.232   51.448 1.00 45.90  ? 68  ASN   C C   1 
ATOM   2603 O O   . ASN   C 1 68  ? 3.479   7.300   50.986 1.00 52.90  ? 68  ASN   C O   1 
ATOM   2604 C CB  . ASN   C 1 68  ? 3.095   6.109   53.804 1.00 47.02  ? 68  ASN   C CB  1 
ATOM   2605 C CG  . ASN   C 1 68  ? 1.838   5.866   54.627 1.00 44.71  ? 68  ASN   C CG  1 
ATOM   2606 O OD1 . ASN   C 1 68  ? 0.888   5.218   54.162 1.00 42.46  ? 68  ASN   C OD1 1 
ATOM   2607 N ND2 . ASN   C 1 68  ? 1.821   6.389   55.850 1.00 37.67  ? 68  ASN   C ND2 1 
ATOM   2608 N N   . LYS   C 1 69  ? 5.127   5.764   51.187 1.00 51.72  ? 69  LYS   C N   1 
ATOM   2609 C CA  . LYS   C 1 69  ? 6.054   6.152   50.114 1.00 51.89  ? 69  LYS   C CA  1 
ATOM   2610 C C   . LYS   C 1 69  ? 6.992   7.300   50.479 1.00 53.16  ? 69  LYS   C C   1 
ATOM   2611 O O   . LYS   C 1 69  ? 7.903   7.603   49.705 1.00 52.48  ? 69  LYS   C O   1 
ATOM   2612 C CB  . LYS   C 1 69  ? 5.343   6.510   48.796 1.00 51.27  ? 69  LYS   C CB  1 
ATOM   2613 C CG  . LYS   C 1 69  ? 4.698   5.339   48.056 1.00 51.81  ? 69  LYS   C CG  1 
ATOM   2614 C CD  . LYS   C 1 69  ? 5.617   4.139   47.880 1.00 47.94  ? 69  LYS   C CD  1 
ATOM   2615 C CE  . LYS   C 1 69  ? 5.409   3.491   46.529 1.00 52.16  ? 69  LYS   C CE  1 
ATOM   2616 N NZ  . LYS   C 1 69  ? 3.986   3.127   46.251 1.00 49.41  ? 69  LYS   C NZ  1 
ATOM   2617 N N   . GLU   C 1 70  ? 6.826   7.929   51.629 1.00 52.46  ? 70  GLU   C N   1 
ATOM   2618 C CA  . GLU   C 1 70  ? 7.527   9.180   51.845 1.00 50.45  ? 70  GLU   C CA  1 
ATOM   2619 C C   . GLU   C 1 70  ? 8.908   8.824   52.390 1.00 52.17  ? 70  GLU   C C   1 
ATOM   2620 O O   . GLU   C 1 70  ? 9.950   9.074   51.765 1.00 52.31  ? 70  GLU   C O   1 
ATOM   2621 C CB  . GLU   C 1 70  ? 6.735   10.004  52.847 1.00 52.88  ? 70  GLU   C CB  1 
ATOM   2622 C CG  . GLU   C 1 70  ? 5.280   10.024  52.454 1.00 59.80  ? 70  GLU   C CG  1 
ATOM   2623 C CD  . GLU   C 1 70  ? 4.428   10.885  53.344 1.00 71.31  ? 70  GLU   C CD  1 
ATOM   2624 O OE1 . GLU   C 1 70  ? 4.982   11.461  54.276 1.00 69.74  ? 70  GLU   C OE1 1 
ATOM   2625 O OE2 . GLU   C 1 70  ? 3.197   10.882  53.203 1.00 73.02  ? 70  GLU   C OE2 1 
ATOM   2626 N N   . TYR   C 1 71  ? 8.882   8.121   53.524 1.00 46.26  ? 71  TYR   C N   1 
ATOM   2627 C CA  . TYR   C 1 71  ? 10.003  7.984   54.438 1.00 38.33  ? 71  TYR   C CA  1 
ATOM   2628 C C   . TYR   C 1 71  ? 10.855  6.769   54.115 1.00 38.18  ? 71  TYR   C C   1 
ATOM   2629 O O   . TYR   C 1 71  ? 10.333  5.700   53.791 1.00 40.66  ? 71  TYR   C O   1 
ATOM   2630 C CB  . TYR   C 1 71  ? 9.482   7.846   55.865 1.00 47.87  ? 71  TYR   C CB  1 
ATOM   2631 C CG  . TYR   C 1 71  ? 9.072   9.125   56.557 1.00 50.15  ? 71  TYR   C CG  1 
ATOM   2632 C CD1 . TYR   C 1 71  ? 10.041  9.996   57.081 1.00 53.48  ? 71  TYR   C CD1 1 
ATOM   2633 C CD2 . TYR   C 1 71  ? 7.728   9.438   56.747 1.00 45.00  ? 71  TYR   C CD2 1 
ATOM   2634 C CE1 . TYR   C 1 71  ? 9.682   11.159  57.752 1.00 51.05  ? 71  TYR   C CE1 1 
ATOM   2635 C CE2 . TYR   C 1 71  ? 7.357   10.595  57.410 1.00 54.05  ? 71  TYR   C CE2 1 
ATOM   2636 C CZ  . TYR   C 1 71  ? 8.340   11.455  57.916 1.00 53.79  ? 71  TYR   C CZ  1 
ATOM   2637 O OH  . TYR   C 1 71  ? 7.975   12.604  58.583 1.00 40.59  ? 71  TYR   C OH  1 
ATOM   2638 N N   . LYS   C 1 72  ? 12.170  6.945   54.224 1.00 32.75  ? 72  LYS   C N   1 
ATOM   2639 C CA  . LYS   C 1 72  ? 13.117  5.839   54.246 1.00 33.84  ? 72  LYS   C CA  1 
ATOM   2640 C C   . LYS   C 1 72  ? 13.175  5.327   55.682 1.00 40.42  ? 72  LYS   C C   1 
ATOM   2641 O O   . LYS   C 1 72  ? 13.501  6.081   56.606 1.00 44.05  ? 72  LYS   C O   1 
ATOM   2642 C CB  . LYS   C 1 72  ? 14.508  6.299   53.817 1.00 32.55  ? 72  LYS   C CB  1 
ATOM   2643 C CG  . LYS   C 1 72  ? 14.549  7.248   52.650 1.00 42.39  ? 72  LYS   C CG  1 
ATOM   2644 C CD  . LYS   C 1 72  ? 15.960  7.806   52.414 1.00 44.99  ? 72  LYS   C CD  1 
ATOM   2645 C CE  . LYS   C 1 72  ? 16.971  6.714   52.121 1.00 43.34  ? 72  LYS   C CE  1 
ATOM   2646 N NZ  . LYS   C 1 72  ? 18.184  7.203   51.375 1.00 51.68  ? 72  LYS   C NZ  1 
ATOM   2647 N N   . ILE   C 1 73  ? 12.889  4.053   55.888 1.00 29.83  ? 73  ILE   C N   1 
ATOM   2648 C CA  . ILE   C 1 73  ? 13.025  3.482   57.216 1.00 36.79  ? 73  ILE   C CA  1 
ATOM   2649 C C   . ILE   C 1 73  ? 13.686  2.116   57.088 1.00 33.43  ? 73  ILE   C C   1 
ATOM   2650 O O   . ILE   C 1 73  ? 13.639  1.471   56.039 1.00 36.33  ? 73  ILE   C O   1 
ATOM   2651 C CB  . ILE   C 1 73  ? 11.659  3.398   57.935 1.00 33.61  ? 73  ILE   C CB  1 
ATOM   2652 C CG1 . ILE   C 1 73  ? 11.848  3.100   59.410 1.00 39.66  ? 73  ILE   C CG1 1 
ATOM   2653 C CG2 . ILE   C 1 73  ? 10.766  2.368   57.296 1.00 41.62  ? 73  ILE   C CG2 1 
ATOM   2654 C CD1 . ILE   C 1 73  ? 10.552  3.069   60.179 1.00 46.21  ? 73  ILE   C CD1 1 
ATOM   2655 N N   . ARG   C 1 74  ? 14.355  1.696   58.155 1.00 31.81  ? 74  ARG   C N   1 
ATOM   2656 C CA  . ARG   C 1 74  ? 14.825  0.324   58.245 1.00 29.93  ? 74  ARG   C CA  1 
ATOM   2657 C C   . ARG   C 1 74  ? 14.059  -0.384  59.352 1.00 27.82  ? 74  ARG   C C   1 
ATOM   2658 O O   . ARG   C 1 74  ? 13.630  0.242   60.326 1.00 24.48  ? 74  ARG   C O   1 
ATOM   2659 C CB  . ARG   C 1 74  ? 16.334  0.238   58.472 1.00 24.34  ? 74  ARG   C CB  1 
ATOM   2660 C CG  . ARG   C 1 74  ? 16.864  0.998   59.655 1.00 29.08  ? 74  ARG   C CG  1 
ATOM   2661 C CD  . ARG   C 1 74  ? 18.394  0.941   59.670 1.00 30.79  ? 74  ARG   C CD  1 
ATOM   2662 N NE  . ARG   C 1 74  ? 18.990  1.953   60.543 1.00 46.26  ? 74  ARG   C NE  1 
ATOM   2663 C CZ  . ARG   C 1 74  ? 18.826  2.035   61.870 1.00 56.21  ? 74  ARG   C CZ  1 
ATOM   2664 N NH1 . ARG   C 1 74  ? 18.089  1.145   62.541 1.00 48.10  ? 74  ARG   C NH1 1 
ATOM   2665 N NH2 . ARG   C 1 74  ? 19.422  3.017   62.539 1.00 53.16  ? 74  ARG   C NH2 1 
ATOM   2666 N N   . ASP   C 1 75  ? 13.865  -1.696  59.169 1.00 27.03  ? 75  ASP   C N   1 
ATOM   2667 C CA  . ASP   C 1 75  ? 13.004  -2.453  60.077 1.00 32.03  ? 75  ASP   C CA  1 
ATOM   2668 C C   . ASP   C 1 75  ? 13.352  -2.171  61.530 1.00 25.44  ? 75  ASP   C C   1 
ATOM   2669 O O   . ASP   C 1 75  ? 12.460  -2.034  62.369 1.00 23.95  ? 75  ASP   C O   1 
ATOM   2670 C CB  . ASP   C 1 75  ? 13.103  -3.965  59.836 1.00 26.63  ? 75  ASP   C CB  1 
ATOM   2671 C CG  . ASP   C 1 75  ? 12.609  -4.385  58.471 1.00 31.40  ? 75  ASP   C CG  1 
ATOM   2672 O OD1 . ASP   C 1 75  ? 11.612  -3.817  58.002 1.00 33.61  ? 75  ASP   C OD1 1 
ATOM   2673 O OD2 . ASP   C 1 75  ? 13.179  -5.341  57.892 1.00 43.50  ? 75  ASP   C OD2 1 
ATOM   2674 N N   . ASN   C 1 76  ? 14.644  -2.056  61.844 1.00 21.80  ? 76  ASN   C N   1 
ATOM   2675 C CA  . ASN   C 1 76  ? 14.994  -1.876  63.245 1.00 24.92  ? 76  ASN   C CA  1 
ATOM   2676 C C   . ASN   C 1 76  ? 14.720  -0.467  63.753 1.00 31.50  ? 76  ASN   C C   1 
ATOM   2677 O O   . ASN   C 1 76  ? 14.977  -0.219  64.938 1.00 26.54  ? 76  ASN   C O   1 
ATOM   2678 C CB  . ASN   C 1 76  ? 16.457  -2.248  63.479 1.00 23.58  ? 76  ASN   C CB  1 
ATOM   2679 C CG  . ASN   C 1 76  ? 16.682  -3.753  63.450 1.00 29.42  ? 76  ASN   C CG  1 
ATOM   2680 O OD1 . ASN   C 1 76  ? 15.731  -4.539  63.455 1.00 31.13  ? 76  ASN   C OD1 1 
ATOM   2681 N ND2 . ASN   C 1 76  ? 17.940  -4.158  63.369 1.00 37.65  ? 76  ASN   C ND2 1 
ATOM   2682 N N   . ASP   C 1 77  ? 14.214  0.454   62.915 1.00 25.13  ? 77  ASP   C N   1 
ATOM   2683 C CA  . ASP   C 1 77  ? 13.793  1.775   63.394 1.00 27.77  ? 77  ASP   C CA  1 
ATOM   2684 C C   . ASP   C 1 77  ? 12.446  1.753   64.120 1.00 25.98  ? 77  ASP   C C   1 
ATOM   2685 O O   . ASP   C 1 77  ? 12.001  2.809   64.585 1.00 23.98  ? 77  ASP   C O   1 
ATOM   2686 C CB  . ASP   C 1 77  ? 13.666  2.782   62.238 1.00 31.20  ? 77  ASP   C CB  1 
ATOM   2687 C CG  . ASP   C 1 77  ? 15.012  3.208   61.634 1.00 39.76  ? 77  ASP   C CG  1 
ATOM   2688 O OD1 . ASP   C 1 77  ? 16.024  3.257   62.365 1.00 37.92  ? 77  ASP   C OD1 1 
ATOM   2689 O OD2 . ASP   C 1 77  ? 15.038  3.523   60.410 1.00 35.57  ? 77  ASP   C OD2 1 
ATOM   2690 N N   . VAL   C 1 78  ? 11.763  0.607   64.172 1.00 22.19  ? 78  VAL   C N   1 
ATOM   2691 C CA  . VAL   C 1 78  ? 10.446  0.469   64.801 1.00 25.58  ? 78  VAL   C CA  1 
ATOM   2692 C C   . VAL   C 1 78  ? 10.578  -0.412  66.042 1.00 22.36  ? 78  VAL   C C   1 
ATOM   2693 O O   . VAL   C 1 78  ? 10.984  -1.577  65.944 1.00 23.75  ? 78  VAL   C O   1 
ATOM   2694 C CB  . VAL   C 1 78  ? 9.415   -0.117  63.820 1.00 22.92  ? 78  VAL   C CB  1 
ATOM   2695 C CG1 . VAL   C 1 78  ? 8.068   -0.350  64.505 1.00 17.03  ? 78  VAL   C CG1 1 
ATOM   2696 C CG2 . VAL   C 1 78  ? 9.230   0.834   62.643 1.00 18.07  ? 78  VAL   C CG2 1 
ATOM   2697 N N   . GLU   C 1 79  ? 10.229  0.129   67.207 1.00 18.48  ? 79  GLU   C N   1 
ATOM   2698 C CA  . GLU   C 1 79  ? 10.168  -0.653  68.441 1.00 18.60  ? 79  GLU   C CA  1 
ATOM   2699 C C   . GLU   C 1 79  ? 8.748   -0.602  69.000 1.00 16.99  ? 79  GLU   C C   1 
ATOM   2700 O O   . GLU   C 1 79  ? 8.146   0.470   69.048 1.00 20.73  ? 79  GLU   C O   1 
ATOM   2701 C CB  . GLU   C 1 79  ? 11.167  -0.115  69.483 1.00 17.48  ? 79  GLU   C CB  1 
ATOM   2702 C CG  . GLU   C 1 79  ? 10.878  -0.620  70.898 1.00 25.12  ? 79  GLU   C CG  1 
ATOM   2703 C CD  . GLU   C 1 79  ? 11.818  -0.039  71.941 1.00 44.62  ? 79  GLU   C CD  1 
ATOM   2704 O OE1 . GLU   C 1 79  ? 11.296  0.298   73.043 1.00 35.36  ? 79  GLU   C OE1 1 
ATOM   2705 O OE2 . GLU   C 1 79  ? 13.048  0.075   71.663 1.00 37.63  ? 79  GLU   C OE2 1 
ATOM   2706 N N   . VAL   C 1 80  ? 8.198   -1.744  69.413 1.00 17.71  ? 80  VAL   C N   1 
ATOM   2707 C CA  . VAL   C 1 80  ? 6.904   -1.772  70.097 1.00 11.37  ? 80  VAL   C CA  1 
ATOM   2708 C C   . VAL   C 1 80  ? 7.095   -2.481  71.433 1.00 16.40  ? 80  VAL   C C   1 
ATOM   2709 O O   . VAL   C 1 80  ? 7.587   -3.616  71.482 1.00 14.38  ? 80  VAL   C O   1 
ATOM   2710 C CB  . VAL   C 1 80  ? 5.815   -2.454  69.258 1.00 14.82  ? 80  VAL   C CB  1 
ATOM   2711 C CG1 . VAL   C 1 80  ? 4.473   -2.473  70.001 1.00 12.34  ? 80  VAL   C CG1 1 
ATOM   2712 C CG2 . VAL   C 1 80  ? 5.672   -1.755  67.912 1.00 14.28  ? 80  VAL   C CG2 1 
ATOM   2713 N N   . LEU   C 1 81  ? 6.744   -1.792  72.514 1.00 15.41  ? 81  LEU   C N   1 
ATOM   2714 C CA  . LEU   C 1 81  ? 6.765   -2.325  73.873 1.00 13.12  ? 81  LEU   C CA  1 
ATOM   2715 C C   . LEU   C 1 81  ? 5.315   -2.514  74.291 1.00 13.88  ? 81  LEU   C C   1 
ATOM   2716 O O   . LEU   C 1 81  ? 4.596   -1.532  74.522 1.00 13.65  ? 81  LEU   C O   1 
ATOM   2717 C CB  . LEU   C 1 81  ? 7.507   -1.379  74.821 1.00 17.72  ? 81  LEU   C CB  1 
ATOM   2718 C CG  . LEU   C 1 81  ? 7.635   -1.862  76.279 1.00 30.63  ? 81  LEU   C CG  1 
ATOM   2719 C CD1 . LEU   C 1 81  ? 8.689   -2.977  76.389 1.00 21.66  ? 81  LEU   C CD1 1 
ATOM   2720 C CD2 . LEU   C 1 81  ? 7.988   -0.689  77.229 1.00 25.59  ? 81  LEU   C CD2 1 
ATOM   2721 N N   . SER   C 1 82  ? 4.866   -3.761  74.326 1.00 12.07  ? 82  SER   C N   1 
ATOM   2722 C CA  . SER   C 1 82  ? 3.505   -4.055  74.750 1.00 14.04  ? 82  SER   C CA  1 
ATOM   2723 C C   . SER   C 1 82  ? 3.497   -4.347  76.242 1.00 21.13  ? 82  SER   C C   1 
ATOM   2724 O O   . SER   C 1 82  ? 4.382   -5.056  76.739 1.00 17.03  ? 82  SER   C O   1 
ATOM   2725 C CB  . SER   C 1 82  ? 2.950   -5.258  74.001 1.00 10.67  ? 82  SER   C CB  1 
ATOM   2726 O OG  . SER   C 1 82  ? 3.870   -6.319  74.183 1.00 15.48  ? 82  SER   C OG  1 
ATOM   2727 N N   . THR   C 1 83  ? 2.485   -3.831  76.940 1.00 18.86  ? 83  THR   C N   1 
ATOM   2728 C CA  . THR   C 1 83  ? 2.185   -4.177  78.331 1.00 18.95  ? 83  THR   C CA  1 
ATOM   2729 C C   . THR   C 1 83  ? 0.850   -4.899  78.373 1.00 15.54  ? 83  THR   C C   1 
ATOM   2730 O O   . THR   C 1 83  ? -0.171  -4.345  77.957 1.00 18.69  ? 83  THR   C O   1 
ATOM   2731 C CB  . THR   C 1 83  ? 2.139   -2.928  79.201 1.00 16.49  ? 83  THR   C CB  1 
ATOM   2732 O OG1 . THR   C 1 83  ? 3.382   -2.252  79.066 1.00 24.22  ? 83  THR   C OG1 1 
ATOM   2733 C CG2 . THR   C 1 83  ? 1.931   -3.293  80.669 1.00 18.91  ? 83  THR   C CG2 1 
ATOM   2734 N N   . VAL   C 1 84  ? 0.850   -6.136  78.841 1.00 16.65  ? 84  VAL   C N   1 
ATOM   2735 C CA  . VAL   C 1 84  ? -0.362  -6.949  78.865 1.00 14.10  ? 84  VAL   C CA  1 
ATOM   2736 C C   . VAL   C 1 84  ? -0.661  -7.327  80.304 1.00 20.95  ? 84  VAL   C C   1 
ATOM   2737 O O   . VAL   C 1 84  ? 0.204   -7.863  81.008 1.00 19.29  ? 84  VAL   C O   1 
ATOM   2738 C CB  . VAL   C 1 84  ? -0.228  -8.200  77.987 1.00 17.50  ? 84  VAL   C CB  1 
ATOM   2739 C CG1 . VAL   C 1 84  ? -1.405  -9.170  78.262 1.00 14.46  ? 84  VAL   C CG1 1 
ATOM   2740 C CG2 . VAL   C 1 84  ? -0.172  -7.794  76.503 1.00 11.75  ? 84  VAL   C CG2 1 
ATOM   2741 N N   . GLY   C 1 85  ? -1.878  -7.031  80.740 1.00 19.31  ? 85  GLY   C N   1 
ATOM   2742 C CA  . GLY   C 1 85  ? -2.271  -7.298  82.110 1.00 28.69  ? 85  GLY   C CA  1 
ATOM   2743 C C   . GLY   C 1 85  ? -3.469  -8.224  82.148 1.00 26.65  ? 85  GLY   C C   1 
ATOM   2744 O O   . GLY   C 1 85  ? -4.118  -8.436  81.115 1.00 18.39  ? 85  GLY   C O   1 
ATOM   2745 N N   . ILE   C 1 86  ? -3.768  -8.792  83.314 1.00 23.32  ? 86  ILE   C N   1 
ATOM   2746 C CA  . ILE   C 1 86  ? -4.938  -9.641  83.490 1.00 25.49  ? 86  ILE   C CA  1 
ATOM   2747 C C   . ILE   C 1 86  ? -5.697  -9.170  84.728 1.00 26.27  ? 86  ILE   C C   1 
ATOM   2748 O O   . ILE   C 1 86  ? -5.087  -8.849  85.753 1.00 25.05  ? 86  ILE   C O   1 
ATOM   2749 C CB  . ILE   C 1 86  ? -4.560  -11.134 83.563 1.00 27.05  ? 86  ILE   C CB  1 
ATOM   2750 C CG1 . ILE   C 1 86  ? -5.819  -11.994 83.638 1.00 31.37  ? 86  ILE   C CG1 1 
ATOM   2751 C CG2 . ILE   C 1 86  ? -3.574  -11.407 84.660 1.00 31.25  ? 86  ILE   C CG2 1 
ATOM   2752 C CD1 . ILE   C 1 86  ? -5.589  -13.458 83.429 1.00 39.99  ? 86  ILE   C CD1 1 
ATOM   2753 N N   . VAL   C 1 87  ? -7.025  -9.063  84.598 1.00 32.10  ? 87  VAL   C N   1 
ATOM   2754 C CA  . VAL   C 1 87  ? -7.923  -8.511  85.608 1.00 35.88  ? 87  VAL   C CA  1 
ATOM   2755 C C   . VAL   C 1 87  ? -9.161  -9.396  85.680 1.00 35.77  ? 87  VAL   C C   1 
ATOM   2756 O O   . VAL   C 1 87  ? -9.495  -10.100 84.726 1.00 36.42  ? 87  VAL   C O   1 
ATOM   2757 C CB  . VAL   C 1 87  ? -8.347  -7.054  85.293 1.00 38.99  ? 87  VAL   C CB  1 
ATOM   2758 C CG1 . VAL   C 1 87  ? -7.138  -6.134  85.189 1.00 35.07  ? 87  VAL   C CG1 1 
ATOM   2759 C CG2 . VAL   C 1 87  ? -9.153  -7.009  84.015 1.00 30.95  ? 87  VAL   C CG2 1 
ATOM   2760 N N   . ALA   C 1 88  ? -9.856  -9.361  86.810 1.00 43.99  ? 88  ALA   C N   1 
ATOM   2761 C CA  . ALA   C 1 88  ? -11.108 -10.104 86.891 1.00 48.59  ? 88  ALA   C CA  1 
ATOM   2762 C C   . ALA   C 1 88  ? -12.237 -9.231  86.368 1.00 49.39  ? 88  ALA   C C   1 
ATOM   2763 O O   . ALA   C 1 88  ? -12.336 -8.056  86.732 1.00 52.43  ? 88  ALA   C O   1 
ATOM   2764 C CB  . ALA   C 1 88  ? -11.388 -10.543 88.329 1.00 54.62  ? 88  ALA   C CB  1 
ATOM   2765 N N   . ASN   C 1 89  ? -13.049 -9.775  85.472 1.00 52.18  ? 89  ASN   C N   1 
ATOM   2766 C CA  . ASN   C 1 89  ? -14.334 -9.133  85.292 1.00 56.32  ? 89  ASN   C CA  1 
ATOM   2767 C C   . ASN   C 1 89  ? -15.260 -9.616  86.402 1.00 63.80  ? 89  ASN   C C   1 
ATOM   2768 O O   . ASN   C 1 89  ? -14.950 -10.559 87.140 1.00 67.74  ? 89  ASN   C O   1 
ATOM   2769 C CB  . ASN   C 1 89  ? -14.908 -9.393  83.891 1.00 48.60  ? 89  ASN   C CB  1 
ATOM   2770 C CG  . ASN   C 1 89  ? -15.064 -10.872 83.570 1.00 51.09  ? 89  ASN   C CG  1 
ATOM   2771 O OD1 . ASN   C 1 89  ? -15.430 -11.671 84.427 1.00 66.81  ? 89  ASN   C OD1 1 
ATOM   2772 N ND2 . ASN   C 1 89  ? -14.794 -11.240 82.325 1.00 45.49  ? 89  ASN   C ND2 1 
ATOM   2773 N N   . GLY   C 1 90  ? -16.390 -8.939  86.544 1.00 67.51  ? 90  GLY   C N   1 
ATOM   2774 C CA  . GLY   C 1 90  ? -17.286 -9.249  87.646 1.00 66.69  ? 90  GLY   C CA  1 
ATOM   2775 C C   . GLY   C 1 90  ? -18.332 -10.295 87.283 1.00 66.88  ? 90  GLY   C C   1 
ATOM   2776 O O   . GLY   C 1 90  ? -19.516 -10.142 87.601 1.00 67.59  ? 90  GLY   C O   1 
ATOM   2777 N N   . ASN   C 1 91  ? -17.910 -11.389 86.630 1.00 70.26  ? 91  ASN   C N   1 
ATOM   2778 C CA  . ASN   C 1 91  ? -18.844 -12.376 86.083 1.00 73.08  ? 91  ASN   C CA  1 
ATOM   2779 C C   . ASN   C 1 91  ? -18.096 -13.681 85.753 1.00 73.03  ? 91  ASN   C C   1 
ATOM   2780 O O   . ASN   C 1 91  ? -18.312 -14.302 84.708 1.00 76.44  ? 91  ASN   C O   1 
ATOM   2781 C CB  . ASN   C 1 91  ? -19.758 -11.613 85.023 1.00 78.21  ? 91  ASN   C CB  1 
ATOM   2782 C CG  . ASN   C 1 91  ? -20.611 -12.497 84.153 1.00 83.78  ? 91  ASN   C CG  1 
ATOM   2783 O OD1 . ASN   C 1 91  ? -20.326 -13.646 83.930 1.00 88.98  ? 91  ASN   C OD1 1 
ATOM   2784 N ND2 . ASN   C 1 91  ? -21.815 -12.021 83.906 1.00 84.66  ? 91  ASN   C ND2 1 
ATOM   2785 N N   . GLY   C 1 92  ? -17.330 -14.179 86.723 1.00 74.29  ? 92  GLY   C N   1 
ATOM   2786 C CA  . GLY   C 1 92  ? -16.833 -15.538 86.686 1.00 71.49  ? 92  GLY   C CA  1 
ATOM   2787 C C   . GLY   C 1 92  ? -15.549 -15.738 85.920 1.00 73.73  ? 92  GLY   C C   1 
ATOM   2788 O O   . GLY   C 1 92  ? -14.931 -16.801 86.056 1.00 67.93  ? 92  GLY   C O   1 
ATOM   2789 N N   . GLY   C 1 93  ? -15.127 -14.764 85.123 1.00 64.05  ? 93  GLY   C N   1 
ATOM   2790 C CA  . GLY   C 1 93  ? -13.950 -14.937 84.306 1.00 57.48  ? 93  GLY   C CA  1 
ATOM   2791 C C   . GLY   C 1 93  ? -12.925 -13.847 84.516 1.00 51.63  ? 93  GLY   C C   1 
ATOM   2792 O O   . GLY   C 1 93  ? -12.866 -13.189 85.563 1.00 54.24  ? 93  GLY   C O   1 
ATOM   2793 N N   . PHE   C 1 94  ? -12.103 -13.652 83.500 1.00 48.25  ? 94  PHE   C N   1 
ATOM   2794 C CA  . PHE   C 1 94  ? -11.022 -12.691 83.563 1.00 45.97  ? 94  PHE   C CA  1 
ATOM   2795 C C   . PHE   C 1 94  ? -10.914 -12.050 82.193 1.00 39.35  ? 94  PHE   C C   1 
ATOM   2796 O O   . PHE   C 1 94  ? -11.365 -12.611 81.191 1.00 41.87  ? 94  PHE   C O   1 
ATOM   2797 C CB  . PHE   C 1 94  ? -9.695  -13.368 83.954 1.00 38.57  ? 94  PHE   C CB  1 
ATOM   2798 C CG  . PHE   C 1 94  ? -9.681  -13.941 85.352 1.00 42.42  ? 94  PHE   C CG  1 
ATOM   2799 C CD1 . PHE   C 1 94  ? -10.118 -15.242 85.594 1.00 45.50  ? 94  PHE   C CD1 1 
ATOM   2800 C CD2 . PHE   C 1 94  ? -9.211  -13.191 86.419 1.00 42.23  ? 94  PHE   C CD2 1 
ATOM   2801 C CE1 . PHE   C 1 94  ? -10.097 -15.773 86.877 1.00 44.24  ? 94  PHE   C CE1 1 
ATOM   2802 C CE2 . PHE   C 1 94  ? -9.184  -13.720 87.702 1.00 47.23  ? 94  PHE   C CE2 1 
ATOM   2803 C CZ  . PHE   C 1 94  ? -9.627  -15.010 87.930 1.00 42.81  ? 94  PHE   C CZ  1 
ATOM   2804 N N   . ALA   C 1 95  ? -10.319 -10.865 82.160 1.00 37.94  ? 95  ALA   C N   1 
ATOM   2805 C CA  . ALA   C 1 95  ? -10.090 -10.132 80.925 1.00 33.01  ? 95  ALA   C CA  1 
ATOM   2806 C C   . ALA   C 1 95  ? -8.643  -9.661  80.861 1.00 27.66  ? 95  ALA   C C   1 
ATOM   2807 O O   . ALA   C 1 95  ? -7.951  -9.571  81.879 1.00 24.04  ? 95  ALA   C O   1 
ATOM   2808 C CB  . ALA   C 1 95  ? -11.036 -8.930  80.793 1.00 29.27  ? 95  ALA   C CB  1 
ATOM   2809 N N   . LEU   C 1 96  ? -8.200  -9.376  79.637 1.00 26.62  ? 96  LEU   C N   1 
ATOM   2810 C CA  . LEU   C 1 96  ? -6.878  -8.842  79.334 1.00 23.95  ? 96  LEU   C CA  1 
ATOM   2811 C C   . LEU   C 1 96  ? -6.944  -7.330  79.158 1.00 22.42  ? 96  LEU   C C   1 
ATOM   2812 O O   . LEU   C 1 96  ? -7.940  -6.783  78.689 1.00 23.59  ? 96  LEU   C O   1 
ATOM   2813 C CB  . LEU   C 1 96  ? -6.326  -9.479  78.052 1.00 18.78  ? 96  LEU   C CB  1 
ATOM   2814 C CG  . LEU   C 1 96  ? -6.197  -10.996 78.027 1.00 28.18  ? 96  LEU   C CG  1 
ATOM   2815 C CD1 . LEU   C 1 96  ? -5.505  -11.463 76.753 1.00 27.08  ? 96  LEU   C CD1 1 
ATOM   2816 C CD2 . LEU   C 1 96  ? -5.425  -11.454 79.257 1.00 25.64  ? 96  LEU   C CD2 1 
ATOM   2817 N N   . THR   C 1 97  ? -5.865  -6.661  79.532 1.00 20.29  ? 97  THR   C N   1 
ATOM   2818 C CA  . THR   C 1 97  ? -5.657  -5.268  79.186 1.00 20.21  ? 97  THR   C CA  1 
ATOM   2819 C C   . THR   C 1 97  ? -4.380  -5.173  78.361 1.00 22.91  ? 97  THR   C C   1 
ATOM   2820 O O   . THR   C 1 97  ? -3.454  -5.961  78.555 1.00 15.56  ? 97  THR   C O   1 
ATOM   2821 C CB  . THR   C 1 97  ? -5.533  -4.375  80.435 1.00 24.81  ? 97  THR   C CB  1 
ATOM   2822 O OG1 . THR   C 1 97  ? -4.273  -4.628  81.069 1.00 27.99  ? 97  THR   C OG1 1 
ATOM   2823 C CG2 . THR   C 1 97  ? -6.662  -4.663  81.422 1.00 24.81  ? 97  THR   C CG2 1 
ATOM   2824 N N   . VAL   C 1 98  ? -4.327  -4.203  77.442 1.00 19.76  ? 98  VAL   C N   1 
ATOM   2825 C CA  . VAL   C 1 98  ? -3.174  -4.019  76.566 1.00 17.31  ? 98  VAL   C CA  1 
ATOM   2826 C C   . VAL   C 1 98  ? -2.859  -2.535  76.459 1.00 20.04  ? 98  VAL   C C   1 
ATOM   2827 O O   . VAL   C 1 98  ? -3.758  -1.725  76.217 1.00 23.44  ? 98  VAL   C O   1 
ATOM   2828 C CB  . VAL   C 1 98  ? -3.407  -4.596  75.151 1.00 21.35  ? 98  VAL   C CB  1 
ATOM   2829 C CG1 . VAL   C 1 98  ? -2.137  -4.462  74.320 1.00 13.34  ? 98  VAL   C CG1 1 
ATOM   2830 C CG2 . VAL   C 1 98  ? -3.858  -6.059  75.212 1.00 19.93  ? 98  VAL   C CG2 1 
ATOM   2831 N N   . HIS   C 1 99  ? -1.586  -2.180  76.623 1.00 15.60  ? 99  HIS   C N   1 
ATOM   2832 C CA  . HIS   C 1 99  ? -1.059  -0.875  76.254 1.00 16.50  ? 99  HIS   C CA  1 
ATOM   2833 C C   . HIS   C 1 99  ? 0.137   -1.095  75.330 1.00 19.87  ? 99  HIS   C C   1 
ATOM   2834 O O   . HIS   C 1 99  ? 0.882   -2.063  75.507 1.00 16.32  ? 99  HIS   C O   1 
ATOM   2835 C CB  . HIS   C 1 99  ? -0.650  -0.071  77.507 1.00 19.16  ? 99  HIS   C CB  1 
ATOM   2836 C CG  . HIS   C 1 99  ? 0.014   1.235   77.199 1.00 20.77  ? 99  HIS   C CG  1 
ATOM   2837 N ND1 . HIS   C 1 99  ? -0.694  2.377   76.884 1.00 19.40  ? 99  HIS   C ND1 1 
ATOM   2838 C CD2 . HIS   C 1 99  ? 1.321   1.581   77.144 1.00 20.23  ? 99  HIS   C CD2 1 
ATOM   2839 C CE1 . HIS   C 1 99  ? 0.148   3.368   76.657 1.00 21.44  ? 99  HIS   C CE1 1 
ATOM   2840 N NE2 . HIS   C 1 99  ? 1.377   2.913   76.810 1.00 18.74  ? 99  HIS   C NE2 1 
ATOM   2841 N N   . LEU   C 1 100 ? 0.315   -0.221  74.333 1.00 15.71  ? 100 LEU   C N   1 
ATOM   2842 C CA  . LEU   C 1 100 ? 1.436   -0.290  73.398 1.00 17.57  ? 100 LEU   C CA  1 
ATOM   2843 C C   . LEU   C 1 100 ? 2.191   1.031   73.424 1.00 21.42  ? 100 LEU   C C   1 
ATOM   2844 O O   . LEU   C 1 100 ? 1.600   2.081   73.157 1.00 21.07  ? 100 LEU   C O   1 
ATOM   2845 C CB  . LEU   C 1 100 ? 0.954   -0.563  71.967 1.00 13.99  ? 100 LEU   C CB  1 
ATOM   2846 C CG  . LEU   C 1 100 ? 0.066   -1.782  71.648 1.00 19.66  ? 100 LEU   C CG  1 
ATOM   2847 C CD1 . LEU   C 1 100 ? -0.247  -1.843  70.141 1.00 11.23  ? 100 LEU   C CD1 1 
ATOM   2848 C CD2 . LEU   C 1 100 ? 0.741   -3.070  72.131 1.00 9.71   ? 100 LEU   C CD2 1 
ATOM   2849 N N   . ASP   C 1 101 ? 3.494   0.982   73.713 1.00 18.72  ? 101 ASP   C N   1 
ATOM   2850 C CA  . ASP   C 1 101 ? 4.394   2.099   73.432 1.00 16.68  ? 101 ASP   C CA  1 
ATOM   2851 C C   . ASP   C 1 101 ? 5.084   1.820   72.104 1.00 20.82  ? 101 ASP   C C   1 
ATOM   2852 O O   . ASP   C 1 101 ? 5.745   0.784   71.948 1.00 14.36  ? 101 ASP   C O   1 
ATOM   2853 C CB  . ASP   C 1 101 ? 5.444   2.287   74.531 1.00 17.55  ? 101 ASP   C CB  1 
ATOM   2854 C CG  . ASP   C 1 101 ? 4.841   2.680   75.863 1.00 27.93  ? 101 ASP   C CG  1 
ATOM   2855 O OD1 . ASP   C 1 101 ? 3.963   3.588   75.891 1.00 20.04  ? 101 ASP   C OD1 1 
ATOM   2856 O OD2 . ASP   C 1 101 ? 5.242   2.063   76.888 1.00 30.95  ? 101 ASP   C OD2 1 
ATOM   2857 N N   . VAL   C 1 102 ? 4.932   2.733   71.151 1.00 18.63  ? 102 VAL   C N   1 
ATOM   2858 C CA  . VAL   C 1 102 ? 5.481   2.569   69.808 1.00 18.90  ? 102 VAL   C CA  1 
ATOM   2859 C C   . VAL   C 1 102 ? 6.508   3.671   69.584 1.00 18.90  ? 102 VAL   C C   1 
ATOM   2860 O O   . VAL   C 1 102 ? 6.176   4.859   69.674 1.00 17.60  ? 102 VAL   C O   1 
ATOM   2861 C CB  . VAL   C 1 102 ? 4.385   2.622   68.731 1.00 21.53  ? 102 VAL   C CB  1 
ATOM   2862 C CG1 . VAL   C 1 102 ? 4.996   2.333   67.370 1.00 13.96  ? 102 VAL   C CG1 1 
ATOM   2863 C CG2 . VAL   C 1 102 ? 3.265   1.637   69.047 1.00 15.33  ? 102 VAL   C CG2 1 
ATOM   2864 N N   . THR   C 1 103 ? 7.754   3.281   69.314 1.00 15.01  ? 103 THR   C N   1 
ATOM   2865 C CA  . THR   C 1 103 ? 8.834   4.218   69.025 1.00 18.76  ? 103 THR   C CA  1 
ATOM   2866 C C   . THR   C 1 103 ? 9.299   4.062   67.578 1.00 23.10  ? 103 THR   C C   1 
ATOM   2867 O O   . THR   C 1 103 ? 9.639   2.956   67.146 1.00 23.36  ? 103 THR   C O   1 
ATOM   2868 C CB  . THR   C 1 103 ? 9.987   4.012   70.002 1.00 21.45  ? 103 THR   C CB  1 
ATOM   2869 O OG1 . THR   C 1 103 ? 9.469   4.115   71.337 1.00 19.24  ? 103 THR   C OG1 1 
ATOM   2870 C CG2 . THR   C 1 103 ? 11.090  5.079   69.796 1.00 21.51  ? 103 THR   C CG2 1 
ATOM   2871 N N   . LEU   C 1 104 ? 9.306   5.168   66.837 1.00 18.64  ? 104 LEU   C N   1 
ATOM   2872 C CA  . LEU   C 1 104 ? 9.834   5.219   65.480 1.00 19.62  ? 104 LEU   C CA  1 
ATOM   2873 C C   . LEU   C 1 104 ? 11.013  6.179   65.429 1.00 27.79  ? 104 LEU   C C   1 
ATOM   2874 O O   . LEU   C 1 104 ? 10.901  7.317   65.887 1.00 26.81  ? 104 LEU   C O   1 
ATOM   2875 C CB  . LEU   C 1 104 ? 8.748   5.664   64.499 1.00 20.35  ? 104 LEU   C CB  1 
ATOM   2876 C CG  . LEU   C 1 104 ? 7.400   4.936   64.574 1.00 20.76  ? 104 LEU   C CG  1 
ATOM   2877 C CD1 . LEU   C 1 104 ? 6.535   5.332   63.400 1.00 32.95  ? 104 LEU   C CD1 1 
ATOM   2878 C CD2 . LEU   C 1 104 ? 7.630   3.461   64.582 1.00 22.96  ? 104 LEU   C CD2 1 
ATOM   2879 N N   . SER   C 1 105 ? 12.134  5.726   64.866 1.00 26.53  ? 105 SER   C N   1 
ATOM   2880 C CA  . SER   C 1 105 ? 13.313  6.566   64.676 1.00 30.11  ? 105 SER   C CA  1 
ATOM   2881 C C   . SER   C 1 105 ? 13.283  7.229   63.301 1.00 36.92  ? 105 SER   C C   1 
ATOM   2882 O O   . SER   C 1 105 ? 12.940  6.588   62.302 1.00 35.01  ? 105 SER   C O   1 
ATOM   2883 C CB  . SER   C 1 105 ? 14.589  5.734   64.809 1.00 30.06  ? 105 SER   C CB  1 
ATOM   2884 O OG  . SER   C 1 105 ? 14.619  5.027   66.035 1.00 36.39  ? 105 SER   C OG  1 
ATOM   2885 N N   . GLY   C 1 106 ? 13.653  8.506   63.247 1.00 36.32  ? 106 GLY   C N   1 
ATOM   2886 C CA  . GLY   C 1 106 ? 13.771  9.185   61.972 1.00 27.95  ? 106 GLY   C CA  1 
ATOM   2887 C C   . GLY   C 1 106 ? 12.461  9.621   61.357 1.00 38.09  ? 106 GLY   C C   1 
ATOM   2888 O O   . GLY   C 1 106 ? 12.425  9.932   60.162 1.00 39.95  ? 106 GLY   C O   1 
ATOM   2889 N N   . ILE   C 1 107 ? 11.380  9.649   62.135 1.00 35.80  ? 107 ILE   C N   1 
ATOM   2890 C CA  . ILE   C 1 107 ? 10.056  10.051  61.673 1.00 29.37  ? 107 ILE   C CA  1 
ATOM   2891 C C   . ILE   C 1 107 ? 9.599   11.143  62.625 1.00 28.91  ? 107 ILE   C C   1 
ATOM   2892 O O   . ILE   C 1 107 ? 9.845   11.047  63.831 1.00 29.92  ? 107 ILE   C O   1 
ATOM   2893 C CB  . ILE   C 1 107 ? 9.043   8.880   61.719 1.00 35.76  ? 107 ILE   C CB  1 
ATOM   2894 C CG1 . ILE   C 1 107 ? 9.523   7.654   60.934 1.00 38.28  ? 107 ILE   C CG1 1 
ATOM   2895 C CG2 . ILE   C 1 107 ? 7.695   9.332   61.185 1.00 36.45  ? 107 ILE   C CG2 1 
ATOM   2896 C CD1 . ILE   C 1 107 ? 9.232   7.698   59.492 1.00 44.24  ? 107 ILE   C CD1 1 
ATOM   2897 N N   . SER   C 1 108 ? 8.903   12.153  62.117 1.00 33.33  ? 108 SER   C N   1 
ATOM   2898 C CA  . SER   C 1 108 ? 8.404   13.195  63.007 1.00 32.05  ? 108 SER   C CA  1 
ATOM   2899 C C   . SER   C 1 108 ? 7.203   12.708  63.814 1.00 35.79  ? 108 SER   C C   1 
ATOM   2900 O O   . SER   C 1 108 ? 6.461   11.815  63.393 1.00 30.75  ? 108 SER   C O   1 
ATOM   2901 C CB  . SER   C 1 108 ? 7.990   14.427  62.216 1.00 26.92  ? 108 SER   C CB  1 
ATOM   2902 O OG  . SER   C 1 108 ? 6.704   14.226  61.648 1.00 40.20  ? 108 SER   C OG  1 
ATOM   2903 N N   . GLN   C 1 109 ? 6.991   13.349  64.967 1.00 31.91  ? 109 GLN   C N   1 
ATOM   2904 C CA  . GLN   C 1 109 ? 5.940   12.938  65.901 1.00 30.79  ? 109 GLN   C CA  1 
ATOM   2905 C C   . GLN   C 1 109 ? 4.559   12.909  65.244 1.00 32.93  ? 109 GLN   C C   1 
ATOM   2906 O O   . GLN   C 1 109 ? 3.790   11.952  65.422 1.00 34.14  ? 109 GLN   C O   1 
ATOM   2907 C CB  . GLN   C 1 109 ? 5.932   13.875  67.120 1.00 32.35  ? 109 GLN   C CB  1 
ATOM   2908 C CG  . GLN   C 1 109 ? 4.975   13.490  68.253 1.00 26.50  ? 109 GLN   C CG  1 
ATOM   2909 C CD  . GLN   C 1 109 ? 5.343   12.193  68.922 1.00 31.61  ? 109 GLN   C CD  1 
ATOM   2910 O OE1 . GLN   C 1 109 ? 6.502   11.790  68.910 1.00 27.03  ? 109 GLN   C OE1 1 
ATOM   2911 N NE2 . GLN   C 1 109 ? 4.355   11.531  69.526 1.00 24.88  ? 109 GLN   C NE2 1 
ATOM   2912 N N   . ALA   C 1 110 ? 4.217   13.952  64.485 1.00 27.49  ? 110 ALA   C N   1 
ATOM   2913 C CA  . ALA   C 1 110 ? 2.887   14.011  63.877 1.00 35.31  ? 110 ALA   C CA  1 
ATOM   2914 C C   . ALA   C 1 110 ? 2.699   12.897  62.843 1.00 31.20  ? 110 ALA   C C   1 
ATOM   2915 O O   . ALA   C 1 110 ? 1.669   12.197  62.829 1.00 31.94  ? 110 ALA   C O   1 
ATOM   2916 C CB  . ALA   C 1 110 ? 2.668   15.390  63.247 1.00 39.41  ? 110 ALA   C CB  1 
ATOM   2917 N N   . ASP   C 1 111 ? 3.691   12.715  61.965 1.00 23.81  ? 111 ASP   C N   1 
ATOM   2918 C CA  . ASP   C 1 111 ? 3.598   11.651  60.970 1.00 29.83  ? 111 ASP   C CA  1 
ATOM   2919 C C   . ASP   C 1 111 ? 3.538   10.284  61.641 1.00 31.97  ? 111 ASP   C C   1 
ATOM   2920 O O   . ASP   C 1 111 ? 2.791   9.404   61.202 1.00 26.86  ? 111 ASP   C O   1 
ATOM   2921 C CB  . ASP   C 1 111 ? 4.783   11.709  60.003 1.00 37.05  ? 111 ASP   C CB  1 
ATOM   2922 C CG  . ASP   C 1 111 ? 4.726   12.920  59.059 1.00 46.31  ? 111 ASP   C CG  1 
ATOM   2923 O OD1 . ASP   C 1 111 ? 3.651   13.576  58.996 1.00 37.16  ? 111 ASP   C OD1 1 
ATOM   2924 O OD2 . ASP   C 1 111 ? 5.761   13.199  58.386 1.00 39.20  ? 111 ASP   C OD2 1 
ATOM   2925 N N   . ALA   C 1 112 ? 4.307   10.099  62.714 1.00 31.39  ? 112 ALA   C N   1 
ATOM   2926 C CA  . ALA   C 1 112 ? 4.323   8.816   63.400 1.00 23.11  ? 112 ALA   C CA  1 
ATOM   2927 C C   . ALA   C 1 112 ? 2.967   8.520   64.028 1.00 23.59  ? 112 ALA   C C   1 
ATOM   2928 O O   . ALA   C 1 112 ? 2.488   7.381   63.985 1.00 22.62  ? 112 ALA   C O   1 
ATOM   2929 C CB  . ALA   C 1 112 ? 5.436   8.808   64.440 1.00 17.36  ? 112 ALA   C CB  1 
ATOM   2930 N N   . GLU   C 1 113 ? 2.316   9.545   64.588 1.00 24.58  ? 113 GLU   C N   1 
ATOM   2931 C CA  . GLU   C 1 113 ? 0.983   9.364   65.175 1.00 30.16  ? 113 GLU   C CA  1 
ATOM   2932 C C   . GLU   C 1 113 ? -0.058  8.973   64.120 1.00 28.55  ? 113 GLU   C C   1 
ATOM   2933 O O   . GLU   C 1 113 ? -0.871  8.055   64.340 1.00 22.06  ? 113 GLU   C O   1 
ATOM   2934 C CB  . GLU   C 1 113 ? 0.589   10.642  65.921 1.00 27.00  ? 113 GLU   C CB  1 
ATOM   2935 C CG  . GLU   C 1 113 ? 1.300   10.769  67.287 1.00 28.07  ? 113 GLU   C CG  1 
ATOM   2936 C CD  . GLU   C 1 113 ? 0.959   12.058  68.047 1.00 40.00  ? 113 GLU   C CD  1 
ATOM   2937 O OE1 . GLU   C 1 113 ? -0.020  12.746  67.673 1.00 47.64  ? 113 GLU   C OE1 1 
ATOM   2938 O OE2 . GLU   C 1 113 ? 1.692   12.392  69.007 1.00 41.78  ? 113 GLU   C OE2 1 
ATOM   2939 N N   . LYS   C 1 114 ? -0.033  9.637   62.959 1.00 24.31  ? 114 LYS   C N   1 
ATOM   2940 C CA  . LYS   C 1 114 ? -0.849  9.184   61.825 1.00 27.83  ? 114 LYS   C CA  1 
ATOM   2941 C C   . LYS   C 1 114 ? -0.552  7.732   61.440 1.00 30.12  ? 114 LYS   C C   1 
ATOM   2942 O O   . LYS   C 1 114 ? -1.477  6.936   61.222 1.00 24.13  ? 114 LYS   C O   1 
ATOM   2943 C CB  . LYS   C 1 114 ? -0.638  10.120  60.624 1.00 37.38  ? 114 LYS   C CB  1 
ATOM   2944 C CG  . LYS   C 1 114 ? -1.341  11.462  60.793 1.00 43.98  ? 114 LYS   C CG  1 
ATOM   2945 C CD  . LYS   C 1 114 ? -1.174  12.517  59.683 1.00 53.42  ? 114 LYS   C CD  1 
ATOM   2946 C CE  . LYS   C 1 114 ? 0.183   13.177  59.910 1.00 54.61  ? 114 LYS   C CE  1 
ATOM   2947 N NZ  . LYS   C 1 114 ? 0.453   14.443  59.194 1.00 61.59  ? 114 LYS   C NZ  1 
ATOM   2948 N N   . ILE   C 1 115 ? 0.736   7.376   61.326 1.00 22.00  ? 115 ILE   C N   1 
ATOM   2949 C CA  . ILE   C 1 115 ? 1.102   6.024   60.905 1.00 25.76  ? 115 ILE   C CA  1 
ATOM   2950 C C   . ILE   C 1 115 ? 0.558   4.982   61.883 1.00 26.11  ? 115 ILE   C C   1 
ATOM   2951 O O   . ILE   C 1 115 ? -0.006  3.953   61.476 1.00 22.02  ? 115 ILE   C O   1 
ATOM   2952 C CB  . ILE   C 1 115 ? 2.629   5.895   60.746 1.00 24.82  ? 115 ILE   C CB  1 
ATOM   2953 C CG1 . ILE   C 1 115 ? 3.093   6.595   59.457 1.00 28.57  ? 115 ILE   C CG1 1 
ATOM   2954 C CG2 . ILE   C 1 115 ? 3.035   4.421   60.761 1.00 19.73  ? 115 ILE   C CG2 1 
ATOM   2955 C CD1 . ILE   C 1 115 ? 4.614   6.745   59.300 1.00 18.68  ? 115 ILE   C CD1 1 
ATOM   2956 N N   . VAL   C 1 116 ? 0.718   5.233   63.190 1.00 24.71  ? 116 VAL   C N   1 
ATOM   2957 C CA  . VAL   C 1 116 ? 0.289   4.269   64.203 1.00 26.01  ? 116 VAL   C CA  1 
ATOM   2958 C C   . VAL   C 1 116 ? -1.232  4.114   64.169 1.00 24.76  ? 116 VAL   C C   1 
ATOM   2959 O O   . VAL   C 1 116 ? -1.772  2.997   64.305 1.00 27.41  ? 116 VAL   C O   1 
ATOM   2960 C CB  . VAL   C 1 116 ? 0.812   4.693   65.600 1.00 20.69  ? 116 VAL   C CB  1 
ATOM   2961 C CG1 . VAL   C 1 116 ? 0.173   3.883   66.697 1.00 24.76  ? 116 VAL   C CG1 1 
ATOM   2962 C CG2 . VAL   C 1 116 ? 2.321   4.529   65.682 1.00 17.51  ? 116 VAL   C CG2 1 
ATOM   2963 N N   . GLU   C 1 117 ? -1.951  5.221   63.940 1.00 24.04  ? 117 GLU   C N   1 
ATOM   2964 C CA  . GLU   C 1 117 ? -3.402  5.115   63.781 1.00 26.87  ? 117 GLU   C CA  1 
ATOM   2965 C C   . GLU   C 1 117 ? -3.777  4.247   62.579 1.00 30.91  ? 117 GLU   C C   1 
ATOM   2966 O O   . GLU   C 1 117 ? -4.661  3.387   62.678 1.00 30.68  ? 117 GLU   C O   1 
ATOM   2967 C CB  . GLU   C 1 117 ? -4.032  6.497   63.651 1.00 38.03  ? 117 GLU   C CB  1 
ATOM   2968 C CG  . GLU   C 1 117 ? -5.490  6.506   64.083 1.00 42.30  ? 117 GLU   C CG  1 
ATOM   2969 C CD  . GLU   C 1 117 ? -6.266  7.678   63.513 1.00 55.78  ? 117 GLU   C CD  1 
ATOM   2970 O OE1 . GLU   C 1 117 ? -5.650  8.487   62.770 1.00 48.51  ? 117 GLU   C OE1 1 
ATOM   2971 O OE2 . GLU   C 1 117 ? -7.481  7.791   63.818 1.00 64.90  ? 117 GLU   C OE2 1 
ATOM   2972 N N   . GLN   C 1 118 ? -3.143  4.471   61.420 1.00 26.10  ? 118 GLN   C N   1 
ATOM   2973 C CA  . GLN   C 1 118 ? -3.400  3.587   60.283 1.00 27.28  ? 118 GLN   C CA  1 
ATOM   2974 C C   . GLN   C 1 118 ? -3.083  2.139   60.635 1.00 31.65  ? 118 GLN   C C   1 
ATOM   2975 O O   . GLN   C 1 118 ? -3.767  1.214   60.173 1.00 26.71  ? 118 GLN   C O   1 
ATOM   2976 C CB  . GLN   C 1 118 ? -2.575  3.981   59.059 1.00 22.11  ? 118 GLN   C CB  1 
ATOM   2977 C CG  . GLN   C 1 118 ? -2.906  5.310   58.422 1.00 33.18  ? 118 GLN   C CG  1 
ATOM   2978 C CD  . GLN   C 1 118 ? -1.907  5.658   57.318 1.00 40.48  ? 118 GLN   C CD  1 
ATOM   2979 O OE1 . GLN   C 1 118 ? -0.787  6.111   57.591 1.00 33.82  ? 118 GLN   C OE1 1 
ATOM   2980 N NE2 . GLN   C 1 118 ? -2.295  5.406   56.068 1.00 38.44  ? 118 GLN   C NE2 1 
ATOM   2981 N N   . THR   C 1 119 ? -2.024  1.925   61.424 1.00 26.81  ? 119 THR   C N   1 
ATOM   2982 C CA  . THR   C 1 119 ? -1.562  0.570   61.704 1.00 20.54  ? 119 THR   C CA  1 
ATOM   2983 C C   . THR   C 1 119 ? -2.621  -0.218  62.454 1.00 19.77  ? 119 THR   C C   1 
ATOM   2984 O O   . THR   C 1 119 ? -2.763  -1.428  62.255 1.00 21.71  ? 119 THR   C O   1 
ATOM   2985 C CB  . THR   C 1 119 ? -0.265  0.610   62.506 1.00 22.02  ? 119 THR   C CB  1 
ATOM   2986 O OG1 . THR   C 1 119 ? 0.751   1.288   61.756 1.00 21.86  ? 119 THR   C OG1 1 
ATOM   2987 C CG2 . THR   C 1 119 ? 0.221   -0.805  62.847 1.00 17.68  ? 119 THR   C CG2 1 
ATOM   2988 N N   . HIS   C 1 120 ? -3.373  0.451   63.326 1.00 21.83  ? 120 HIS   C N   1 
ATOM   2989 C CA  . HIS   C 1 120 ? -4.395  -0.301  64.054 1.00 27.42  ? 120 HIS   C CA  1 
ATOM   2990 C C   . HIS   C 1 120 ? -5.402  -0.988  63.127 1.00 33.36  ? 120 HIS   C C   1 
ATOM   2991 O O   . HIS   C 1 120 ? -6.026  -1.978  63.530 1.00 26.34  ? 120 HIS   C O   1 
ATOM   2992 C CB  . HIS   C 1 120 ? -5.107  0.608   65.043 1.00 23.30  ? 120 HIS   C CB  1 
ATOM   2993 C CG  . HIS   C 1 120 ? -4.435  0.656   66.380 1.00 18.82  ? 120 HIS   C CG  1 
ATOM   2994 N ND1 . HIS   C 1 120 ? -4.264  -0.469  67.166 1.00 27.24  ? 120 HIS   C ND1 1 
ATOM   2995 C CD2 . HIS   C 1 120 ? -3.867  1.678   67.059 1.00 22.26  ? 120 HIS   C CD2 1 
ATOM   2996 C CE1 . HIS   C 1 120 ? -3.643  -0.134  68.280 1.00 25.56  ? 120 HIS   C CE1 1 
ATOM   2997 N NE2 . HIS   C 1 120 ? -3.384  1.162   68.239 1.00 27.95  ? 120 HIS   C NE2 1 
ATOM   2998 N N   . GLN   C 1 121 ? -5.553  -0.506  61.888 1.00 27.62  ? 121 GLN   C N   1 
ATOM   2999 C CA  . GLN   C 1 121 ? -6.407  -1.155  60.897 1.00 23.01  ? 121 GLN   C CA  1 
ATOM   3000 C C   . GLN   C 1 121 ? -5.733  -2.337  60.204 1.00 25.96  ? 121 GLN   C C   1 
ATOM   3001 O O   . GLN   C 1 121 ? -6.418  -3.244  59.711 1.00 30.73  ? 121 GLN   C O   1 
ATOM   3002 C CB  . GLN   C 1 121 ? -6.828  -0.124  59.844 1.00 32.43  ? 121 GLN   C CB  1 
ATOM   3003 C CG  . GLN   C 1 121 ? -7.753  0.967   60.371 1.00 31.02  ? 121 GLN   C CG  1 
ATOM   3004 C CD  . GLN   C 1 121 ? -8.775  0.396   61.330 1.00 43.80  ? 121 GLN   C CD  1 
ATOM   3005 O OE1 . GLN   C 1 121 ? -9.815  -0.130  60.908 1.00 40.33  ? 121 GLN   C OE1 1 
ATOM   3006 N NE2 . GLN   C 1 121 ? -8.483  0.484   62.636 1.00 43.54  ? 121 GLN   C NE2 1 
ATOM   3007 N N   . VAL   C 1 122 ? -4.415  -2.317  60.084 1.00 23.94  ? 122 VAL   C N   1 
ATOM   3008 C CA  . VAL   C 1 122 ? -3.712  -3.370  59.356 1.00 31.47  ? 122 VAL   C CA  1 
ATOM   3009 C C   . VAL   C 1 122 ? -3.477  -4.593  60.231 1.00 30.40  ? 122 VAL   C C   1 
ATOM   3010 O O   . VAL   C 1 122 ? -3.655  -5.732  59.777 1.00 21.23  ? 122 VAL   C O   1 
ATOM   3011 C CB  . VAL   C 1 122 ? -2.383  -2.810  58.812 1.00 24.86  ? 122 VAL   C CB  1 
ATOM   3012 C CG1 . VAL   C 1 122 ? -1.511  -3.934  58.223 1.00 27.45  ? 122 VAL   C CG1 1 
ATOM   3013 C CG2 . VAL   C 1 122 ? -2.659  -1.728  57.814 1.00 25.91  ? 122 VAL   C CG2 1 
ATOM   3014 N N   . CYS   C 1 123 ? -3.063  -4.352  61.480 1.00 26.18  ? 123 CYS   C N   1 
ATOM   3015 C CA  . CYS   C 1 123 ? -2.560  -5.405  62.345 1.00 20.20  ? 123 CYS   C CA  1 
ATOM   3016 C C   . CYS   C 1 123 ? -3.670  -6.388  62.678 1.00 17.58  ? 123 CYS   C C   1 
ATOM   3017 O O   . CYS   C 1 123 ? -4.704  -5.971  63.204 1.00 14.54  ? 123 CYS   C O   1 
ATOM   3018 C CB  . CYS   C 1 123 ? -1.996  -4.800  63.621 1.00 22.39  ? 123 CYS   C CB  1 
ATOM   3019 S SG  . CYS   C 1 123 ? -1.506  -6.061  64.808 1.00 23.45  ? 123 CYS   C SG  1 
ATOM   3020 N N   . PRO   C 1 124 ? -3.509  -7.683  62.394 1.00 21.71  ? 124 PRO   C N   1 
ATOM   3021 C CA  . PRO   C 1 124 ? -4.595  -8.634  62.695 1.00 21.54  ? 124 PRO   C CA  1 
ATOM   3022 C C   . PRO   C 1 124 ? -4.907  -8.763  64.190 1.00 20.16  ? 124 PRO   C C   1 
ATOM   3023 O O   . PRO   C 1 124 ? -6.029  -9.142  64.539 1.00 18.16  ? 124 PRO   C O   1 
ATOM   3024 C CB  . PRO   C 1 124 ? -4.079  -9.959  62.109 1.00 19.58  ? 124 PRO   C CB  1 
ATOM   3025 C CG  . PRO   C 1 124 ? -2.598  -9.801  62.014 1.00 21.58  ? 124 PRO   C CG  1 
ATOM   3026 C CD  . PRO   C 1 124 ? -2.377  -8.332  61.712 1.00 21.80  ? 124 PRO   C CD  1 
ATOM   3027 N N   . TYR   C 1 125 ? -3.974  -8.421  65.084 1.00 22.45  ? 125 TYR   C N   1 
ATOM   3028 C CA  . TYR   C 1 125 ? -4.255  -8.538  66.518 1.00 19.28  ? 125 TYR   C CA  1 
ATOM   3029 C C   . TYR   C 1 125 ? -5.158  -7.410  66.986 1.00 20.00  ? 125 TYR   C C   1 
ATOM   3030 O O   . TYR   C 1 125 ? -6.121  -7.643  67.736 1.00 15.41  ? 125 TYR   C O   1 
ATOM   3031 C CB  . TYR   C 1 125 ? -2.954  -8.584  67.306 1.00 16.64  ? 125 TYR   C CB  1 
ATOM   3032 C CG  . TYR   C 1 125 ? -2.214  -9.850  66.963 1.00 20.78  ? 125 TYR   C CG  1 
ATOM   3033 C CD1 . TYR   C 1 125 ? -1.488  -9.941  65.781 1.00 26.07  ? 125 TYR   C CD1 1 
ATOM   3034 C CD2 . TYR   C 1 125 ? -2.300  -10.971 67.773 1.00 34.06  ? 125 TYR   C CD2 1 
ATOM   3035 C CE1 . TYR   C 1 125 ? -0.853  -11.102 65.414 1.00 37.69  ? 125 TYR   C CE1 1 
ATOM   3036 C CE2 . TYR   C 1 125 ? -1.660  -12.151 67.421 1.00 39.29  ? 125 TYR   C CE2 1 
ATOM   3037 C CZ  . TYR   C 1 125 ? -0.938  -12.211 66.233 1.00 38.41  ? 125 TYR   C CZ  1 
ATOM   3038 O OH  . TYR   C 1 125 ? -0.286  -13.376 65.840 1.00 39.28  ? 125 TYR   C OH  1 
ATOM   3039 N N   . SER   C 1 126 ? -4.869  -6.182  66.526 1.00 17.78  ? 126 SER   C N   1 
ATOM   3040 C CA  . SER   C 1 126 ? -5.738  -5.039  66.802 1.00 14.81  ? 126 SER   C CA  1 
ATOM   3041 C C   . SER   C 1 126 ? -7.149  -5.295  66.282 1.00 18.08  ? 126 SER   C C   1 
ATOM   3042 O O   . SER   C 1 126 ? -8.130  -4.987  66.960 1.00 19.90  ? 126 SER   C O   1 
ATOM   3043 C CB  . SER   C 1 126 ? -5.168  -3.767  66.160 1.00 15.19  ? 126 SER   C CB  1 
ATOM   3044 O OG  . SER   C 1 126 ? -3.884  -3.417  66.670 1.00 22.75  ? 126 SER   C OG  1 
ATOM   3045 N N   . ASN   C 1 127 ? -7.263  -5.843  65.066 1.00 21.84  ? 127 ASN   C N   1 
ATOM   3046 C CA  . ASN   C 1 127 ? -8.569  -6.194  64.508 1.00 22.15  ? 127 ASN   C CA  1 
ATOM   3047 C C   . ASN   C 1 127 ? -9.254  -7.280  65.327 1.00 20.46  ? 127 ASN   C C   1 
ATOM   3048 O O   . ASN   C 1 127 ? -10.472 -7.232  65.534 1.00 22.07  ? 127 ASN   C O   1 
ATOM   3049 C CB  . ASN   C 1 127 ? -8.417  -6.660  63.058 1.00 21.25  ? 127 ASN   C CB  1 
ATOM   3050 C CG  . ASN   C 1 127 ? -8.136  -5.514  62.104 1.00 31.21  ? 127 ASN   C CG  1 
ATOM   3051 O OD1 . ASN   C 1 127 ? -8.580  -4.385  62.333 1.00 29.96  ? 127 ASN   C OD1 1 
ATOM   3052 N ND2 . ASN   C 1 127 ? -7.416  -5.800  61.013 1.00 29.39  ? 127 ASN   C ND2 1 
ATOM   3053 N N   . ALA   C 1 128 ? -8.484  -8.268  65.799 1.00 23.54  ? 128 ALA   C N   1 
ATOM   3054 C CA  . ALA   C 1 128 ? -9.054  -9.365  66.584 1.00 21.05  ? 128 ALA   C CA  1 
ATOM   3055 C C   . ALA   C 1 128 ? -9.678  -8.880  67.895 1.00 17.27  ? 128 ALA   C C   1 
ATOM   3056 O O   . ALA   C 1 128 ? -10.719 -9.392  68.317 1.00 18.35  ? 128 ALA   C O   1 
ATOM   3057 C CB  . ALA   C 1 128 ? -7.979  -10.407 66.875 1.00 20.15  ? 128 ALA   C CB  1 
ATOM   3058 N N   . ILE   C 1 129 ? -9.060  -7.907  68.572 1.00 18.13  ? 129 ILE   C N   1 
ATOM   3059 C CA  . ILE   C 1 129 ? -9.536  -7.570  69.918 1.00 22.04  ? 129 ILE   C CA  1 
ATOM   3060 C C   . ILE   C 1 129 ? -10.406 -6.306  69.968 1.00 22.22  ? 129 ILE   C C   1 
ATOM   3061 O O   . ILE   C 1 129 ? -10.897 -5.949  71.057 1.00 21.12  ? 129 ILE   C O   1 
ATOM   3062 C CB  . ILE   C 1 129 ? -8.346  -7.469  70.894 1.00 20.40  ? 129 ILE   C CB  1 
ATOM   3063 C CG1 . ILE   C 1 129 ? -7.385  -6.345  70.495 1.00 26.53  ? 129 ILE   C CG1 1 
ATOM   3064 C CG2 . ILE   C 1 129 ? -7.604  -8.824  70.933 1.00 24.02  ? 129 ILE   C CG2 1 
ATOM   3065 C CD1 . ILE   C 1 129 ? -6.274  -6.122  71.530 1.00 19.55  ? 129 ILE   C CD1 1 
ATOM   3066 N N   . ARG   C 1 130 ? -10.628 -5.635  68.833 1.00 17.56  ? 130 ARG   C N   1 
ATOM   3067 C CA  . ARG   C 1 130 ? -11.402 -4.386  68.809 1.00 22.02  ? 130 ARG   C CA  1 
ATOM   3068 C C   . ARG   C 1 130 ? -12.759 -4.538  69.504 1.00 20.34  ? 130 ARG   C C   1 
ATOM   3069 O O   . ARG   C 1 130 ? -13.495 -5.486  69.242 1.00 23.52  ? 130 ARG   C O   1 
ATOM   3070 C CB  . ARG   C 1 130 ? -11.605 -3.948  67.352 1.00 18.66  ? 130 ARG   C CB  1 
ATOM   3071 C CG  . ARG   C 1 130 ? -12.333 -2.604  67.182 1.00 24.61  ? 130 ARG   C CG  1 
ATOM   3072 C CD  . ARG   C 1 130 ? -12.141 -2.051  65.743 1.00 24.78  ? 130 ARG   C CD  1 
ATOM   3073 N NE  . ARG   C 1 130 ? -10.732 -1.877  65.391 1.00 21.21  ? 130 ARG   C NE  1 
ATOM   3074 C CZ  . ARG   C 1 130 ? -10.091 -2.595  64.468 1.00 28.97  ? 130 ARG   C CZ  1 
ATOM   3075 N NH1 . ARG   C 1 130 ? -10.724 -3.536  63.762 1.00 28.45  ? 130 ARG   C NH1 1 
ATOM   3076 N NH2 . ARG   C 1 130 ? -8.811  -2.355  64.228 1.00 30.13  ? 130 ARG   C NH2 1 
ATOM   3077 N N   . GLY   C 1 131 ? -13.089 -3.601  70.401 1.00 25.96  ? 131 GLY   C N   1 
ATOM   3078 C CA  . GLY   C 1 131 ? -14.357 -3.619  71.121 1.00 26.75  ? 131 GLY   C CA  1 
ATOM   3079 C C   . GLY   C 1 131 ? -14.388 -4.454  72.396 1.00 28.85  ? 131 GLY   C C   1 
ATOM   3080 O O   . GLY   C 1 131 ? -15.264 -4.244  73.245 1.00 24.16  ? 131 GLY   C O   1 
ATOM   3081 N N   . ASN   C 1 132 ? -13.491 -5.418  72.540 1.00 23.94  ? 132 ASN   C N   1 
ATOM   3082 C CA  . ASN   C 1 132 ? -13.420 -6.248  73.733 1.00 23.32  ? 132 ASN   C CA  1 
ATOM   3083 C C   . ASN   C 1 132 ? -12.339 -5.746  74.666 1.00 28.61  ? 132 ASN   C C   1 
ATOM   3084 O O   . ASN   C 1 132 ? -12.580 -5.500  75.847 1.00 32.24  ? 132 ASN   C O   1 
ATOM   3085 C CB  . ASN   C 1 132 ? -13.112 -7.693  73.342 1.00 24.70  ? 132 ASN   C CB  1 
ATOM   3086 C CG  . ASN   C 1 132 ? -14.183 -8.291  72.474 1.00 29.27  ? 132 ASN   C CG  1 
ATOM   3087 O OD1 . ASN   C 1 132 ? -15.378 -8.207  72.785 1.00 30.37  ? 132 ASN   C OD1 1 
ATOM   3088 N ND2 . ASN   C 1 132 ? -13.773 -8.851  71.345 1.00 24.61  ? 132 ASN   C ND2 1 
ATOM   3089 N N   . ILE   C 1 133 ? -11.136 -5.576  74.132 1.00 28.07  ? 133 ILE   C N   1 
ATOM   3090 C CA  . ILE   C 1 133 ? -10.041 -4.917  74.826 1.00 23.58  ? 133 ILE   C CA  1 
ATOM   3091 C C   . ILE   C 1 133 ? -9.894  -3.521  74.243 1.00 29.55  ? 133 ILE   C C   1 
ATOM   3092 O O   . ILE   C 1 133 ? -9.833  -3.356  73.023 1.00 31.33  ? 133 ILE   C O   1 
ATOM   3093 C CB  . ILE   C 1 133 ? -8.726  -5.703  74.696 1.00 20.89  ? 133 ILE   C CB  1 
ATOM   3094 C CG1 . ILE   C 1 133 ? -8.950  -7.166  75.111 1.00 21.33  ? 133 ILE   C CG1 1 
ATOM   3095 C CG2 . ILE   C 1 133 ? -7.643  -5.069  75.580 1.00 24.14  ? 133 ILE   C CG2 1 
ATOM   3096 C CD1 . ILE   C 1 133 ? -7.678  -8.046  74.944 1.00 24.60  ? 133 ILE   C CD1 1 
ATOM   3097 N N   . GLN   C 1 134 ? -9.881  -2.520  75.104 1.00 26.78  ? 134 GLN   C N   1 
ATOM   3098 C CA  . GLN   C 1 134 ? -9.664  -1.128  74.725 1.00 34.89  ? 134 GLN   C CA  1 
ATOM   3099 C C   . GLN   C 1 134 ? -8.167  -0.809  74.803 1.00 32.38  ? 134 GLN   C C   1 
ATOM   3100 O O   . GLN   C 1 134 ? -7.625  -0.402  75.841 1.00 29.16  ? 134 GLN   C O   1 
ATOM   3101 C CB  . GLN   C 1 134 ? -10.505 -0.248  75.637 1.00 43.24  ? 134 GLN   C CB  1 
ATOM   3102 C CG  . GLN   C 1 134 ? -10.368 1.281   75.423 1.00 57.66  ? 134 GLN   C CG  1 
ATOM   3103 C CD  . GLN   C 1 134 ? -10.697 1.736   73.974 1.00 69.23  ? 134 GLN   C CD  1 
ATOM   3104 O OE1 . GLN   C 1 134 ? -9.808  2.160   73.221 1.00 69.18  ? 134 GLN   C OE1 1 
ATOM   3105 N NE2 . GLN   C 1 134 ? -11.984 1.572   73.576 1.00 68.24  ? 134 GLN   C NE2 1 
ATOM   3106 N N   . VAL   C 1 135 ? -7.497  -0.956  73.666 1.00 23.56  ? 135 VAL   C N   1 
ATOM   3107 C CA  . VAL   C 1 135 ? -6.059  -0.777  73.611 1.00 27.49  ? 135 VAL   C CA  1 
ATOM   3108 C C   . VAL   C 1 135 ? -5.694  0.698   73.728 1.00 27.94  ? 135 VAL   C C   1 
ATOM   3109 O O   . VAL   C 1 135 ? -6.249  1.559   73.030 1.00 31.28  ? 135 VAL   C O   1 
ATOM   3110 C CB  . VAL   C 1 135 ? -5.506  -1.369  72.313 1.00 18.57  ? 135 VAL   C CB  1 
ATOM   3111 C CG1 . VAL   C 1 135 ? -3.987  -1.257  72.322 1.00 21.08  ? 135 VAL   C CG1 1 
ATOM   3112 C CG2 . VAL   C 1 135 ? -5.926  -2.790  72.183 1.00 25.10  ? 135 VAL   C CG2 1 
ATOM   3113 N N   . SER   C 1 136 ? -4.716  0.988   74.570 1.00 20.31  ? 136 SER   C N   1 
ATOM   3114 C CA  . SER   C 1 136 ? -4.161  2.328   74.666 1.00 17.32  ? 136 SER   C CA  1 
ATOM   3115 C C   . SER   C 1 136 ? -2.796  2.332   73.993 1.00 22.05  ? 136 SER   C C   1 
ATOM   3116 O O   . SER   C 1 136 ? -2.101  1.309   73.995 1.00 17.88  ? 136 SER   C O   1 
ATOM   3117 C CB  . SER   C 1 136 ? -4.057  2.792   76.122 1.00 23.49  ? 136 SER   C CB  1 
ATOM   3118 O OG  . SER   C 1 136 ? -3.270  1.908   76.892 1.00 21.79  ? 136 SER   C OG  1 
ATOM   3119 N N   . THR   C 1 137 ? -2.436  3.476   73.393 1.00 18.62  ? 137 THR   C N   1 
ATOM   3120 C CA  . THR   C 1 137 ? -1.208  3.631   72.621 1.00 21.79  ? 137 THR   C CA  1 
ATOM   3121 C C   . THR   C 1 137 ? -0.537  4.960   72.949 1.00 25.67  ? 137 THR   C C   1 
ATOM   3122 O O   . THR   C 1 137 ? -1.192  6.011   72.954 1.00 23.28  ? 137 THR   C O   1 
ATOM   3123 C CB  . THR   C 1 137 ? -1.499  3.569   71.107 1.00 29.40  ? 137 THR   C CB  1 
ATOM   3124 O OG1 . THR   C 1 137 ? -2.245  2.383   70.798 1.00 22.41  ? 137 THR   C OG1 1 
ATOM   3125 C CG2 . THR   C 1 137 ? -0.206  3.558   70.323 1.00 22.88  ? 137 THR   C CG2 1 
ATOM   3126 N N   . THR   C 1 138 ? 0.773   4.924   73.158 1.00 19.24  ? 138 THR   C N   1 
ATOM   3127 C CA  . THR   C 1 138 ? 1.591   6.124   73.229 1.00 20.01  ? 138 THR   C CA  1 
ATOM   3128 C C   . THR   C 1 138 ? 2.709   6.033   72.201 1.00 26.01  ? 138 THR   C C   1 
ATOM   3129 O O   . THR   C 1 138 ? 3.393   5.007   72.111 1.00 22.54  ? 138 THR   C O   1 
ATOM   3130 C CB  . THR   C 1 138 ? 2.165   6.321   74.636 1.00 19.84  ? 138 THR   C CB  1 
ATOM   3131 O OG1 . THR   C 1 138 ? 1.102   6.236   75.593 1.00 20.38  ? 138 THR   C OG1 1 
ATOM   3132 C CG2 . THR   C 1 138 ? 2.863   7.692   74.743 1.00 19.92  ? 138 THR   C CG2 1 
ATOM   3133 N N   . VAL   C 1 139 ? 2.902   7.116   71.451 1.00 19.34  ? 139 VAL   C N   1 
ATOM   3134 C CA  . VAL   C 1 139 ? 3.790   7.154   70.296 1.00 23.01  ? 139 VAL   C CA  1 
ATOM   3135 C C   . VAL   C 1 139 ? 5.004   8.014   70.638 1.00 26.01  ? 139 VAL   C C   1 
ATOM   3136 O O   . VAL   C 1 139 ? 4.857   9.168   71.060 1.00 25.86  ? 139 VAL   C O   1 
ATOM   3137 C CB  . VAL   C 1 139 ? 3.051   7.699   69.059 1.00 22.96  ? 139 VAL   C CB  1 
ATOM   3138 C CG1 . VAL   C 1 139 ? 4.016   7.897   67.903 1.00 24.17  ? 139 VAL   C CG1 1 
ATOM   3139 C CG2 . VAL   C 1 139 ? 1.938   6.758   68.654 1.00 20.54  ? 139 VAL   C CG2 1 
ATOM   3140 N N   . TYR   C 1 140 ? 6.200   7.460   70.459 1.00 17.47  ? 140 TYR   C N   1 
ATOM   3141 C CA  . TYR   C 1 140 ? 7.440   8.188   70.691 1.00 21.08  ? 140 TYR   C CA  1 
ATOM   3142 C C   . TYR   C 1 140 ? 8.259   8.267   69.410 1.00 27.84  ? 140 TYR   C C   1 
ATOM   3143 O O   . TYR   C 1 140 ? 8.205   7.363   68.569 1.00 22.85  ? 140 TYR   C O   1 
ATOM   3144 C CB  . TYR   C 1 140 ? 8.304   7.530   71.781 1.00 19.55  ? 140 TYR   C CB  1 
ATOM   3145 C CG  . TYR   C 1 140 ? 7.645   7.438   73.131 1.00 22.94  ? 140 TYR   C CG  1 
ATOM   3146 C CD1 . TYR   C 1 140 ? 7.767   8.479   74.047 1.00 28.71  ? 140 TYR   C CD1 1 
ATOM   3147 C CD2 . TYR   C 1 140 ? 6.901   6.324   73.499 1.00 24.75  ? 140 TYR   C CD2 1 
ATOM   3148 C CE1 . TYR   C 1 140 ? 7.182   8.407   75.289 1.00 24.69  ? 140 TYR   C CE1 1 
ATOM   3149 C CE2 . TYR   C 1 140 ? 6.297   6.252   74.743 1.00 19.24  ? 140 TYR   C CE2 1 
ATOM   3150 C CZ  . TYR   C 1 140 ? 6.449   7.296   75.631 1.00 19.13  ? 140 TYR   C CZ  1 
ATOM   3151 O OH  . TYR   C 1 140 ? 5.865   7.218   76.868 1.00 22.75  ? 140 TYR   C OH  1 
ATOM   3152 N N   . THR   C 1 141 ? 9.039   9.343   69.271 1.00 19.85  ? 141 THR   C N   1 
ATOM   3153 C CA  . THR   C 1 141 ? 9.913   9.533   68.113 1.00 27.49  ? 141 THR   C CA  1 
ATOM   3154 C C   . THR   C 1 141 ? 11.272  9.959   68.640 1.00 37.27  ? 141 THR   C C   1 
ATOM   3155 O O   . THR   C 1 141 ? 11.397  10.969  69.335 1.00 40.71  ? 141 THR   C O   1 
ATOM   3156 C CB  . THR   C 1 141 ? 9.371   10.565  67.124 1.00 28.11  ? 141 THR   C CB  1 
ATOM   3157 O OG1 . THR   C 1 141 ? 8.963   11.753  67.815 1.00 32.41  ? 141 THR   C OG1 1 
ATOM   3158 C CG2 . THR   C 1 141 ? 8.175   9.991   66.350 1.00 24.16  ? 141 THR   C CG2 1 
ATOM   3159 N N   . LYS   C 1 142 ? 12.274  9.187   68.291 1.00 36.48  ? 142 LYS   C N   1 
ATOM   3160 C CA  . LYS   C 1 142 ? 13.544  9.156   68.971 1.00 46.57  ? 142 LYS   C CA  1 
ATOM   3161 C C   . LYS   C 1 142 ? 14.489  10.058  68.234 1.00 51.47  ? 142 LYS   C C   1 
ATOM   3162 O O   . LYS   C 1 142 ? 14.485  10.038  66.993 1.00 42.53  ? 142 LYS   C O   1 
ATOM   3163 C CB  . LYS   C 1 142 ? 14.073  7.717   68.976 1.00 53.44  ? 142 LYS   C CB  1 
ATOM   3164 C CG  . LYS   C 1 142 ? 15.288  7.358   69.782 1.00 58.99  ? 142 LYS   C CG  1 
ATOM   3165 C CD  . LYS   C 1 142 ? 15.443  5.839   69.683 1.00 50.36  ? 142 LYS   C CD  1 
ATOM   3166 C CE  . LYS   C 1 142 ? 16.066  5.191   70.901 1.00 62.70  ? 142 LYS   C CE  1 
ATOM   3167 N NZ  . LYS   C 1 142 ? 15.814  3.726   70.806 1.00 59.62  ? 142 LYS   C NZ  1 
ATOM   3168 N N   . MET   D 1 1   ? -11.911 -4.084  89.739 1.00 96.44  ? 1   MET   D N   1 
ATOM   3169 C CA  . MET   D 1 1   ? -10.898 -5.133  89.884 1.00 91.48  ? 1   MET   D CA  1 
ATOM   3170 C C   . MET   D 1 1   ? -9.530  -4.737  89.326 1.00 83.45  ? 1   MET   D C   1 
ATOM   3171 O O   . MET   D 1 1   ? -9.354  -4.597  88.118 1.00 82.66  ? 1   MET   D O   1 
ATOM   3172 C CB  . MET   D 1 1   ? -11.382 -6.441  89.236 1.00 97.89  ? 1   MET   D CB  1 
ATOM   3173 C CG  . MET   D 1 1   ? -12.356 -7.271  90.079 1.00 104.16 ? 1   MET   D CG  1 
ATOM   3174 S SD  . MET   D 1 1   ? -14.043 -6.659  90.261 1.00 116.87 ? 1   MET   D SD  1 
ATOM   3175 C CE  . MET   D 1 1   ? -14.765 -7.036  88.665 1.00 103.73 ? 1   MET   D CE  1 
ATOM   3176 N N   . SER   D 1 2   ? -8.566  -4.584  90.237 1.00 79.47  ? 2   SER   D N   1 
ATOM   3177 C CA  . SER   D 1 2   ? -7.214  -4.181  89.881 1.00 67.81  ? 2   SER   D CA  1 
ATOM   3178 C C   . SER   D 1 2   ? -6.528  -5.251  89.032 1.00 54.54  ? 2   SER   D C   1 
ATOM   3179 O O   . SER   D 1 2   ? -7.003  -6.374  88.872 1.00 49.17  ? 2   SER   D O   1 
ATOM   3180 C CB  . SER   D 1 2   ? -6.372  -3.925  91.133 1.00 68.09  ? 2   SER   D CB  1 
ATOM   3181 O OG  . SER   D 1 2   ? -6.882  -2.842  91.885 1.00 67.69  ? 2   SER   D OG  1 
ATOM   3182 N N   . THR   D 1 3   ? -5.369  -4.876  88.507 1.00 52.13  ? 3   THR   D N   1 
ATOM   3183 C CA  . THR   D 1 3   ? -4.535  -5.737  87.676 1.00 40.08  ? 3   THR   D CA  1 
ATOM   3184 C C   . THR   D 1 3   ? -3.840  -6.796  88.538 1.00 34.25  ? 3   THR   D C   1 
ATOM   3185 O O   . THR   D 1 3   ? -3.103  -6.474  89.477 1.00 35.75  ? 3   THR   D O   1 
ATOM   3186 C CB  . THR   D 1 3   ? -3.569  -4.836  86.903 1.00 43.12  ? 3   THR   D CB  1 
ATOM   3187 O OG1 . THR   D 1 3   ? -2.752  -5.583  85.981 1.00 37.18  ? 3   THR   D OG1 1 
ATOM   3188 C CG2 . THR   D 1 3   ? -2.746  -3.940  87.843 1.00 46.82  ? 3   THR   D CG2 1 
ATOM   3189 N N   . LEU   D 1 4   ? -4.081  -8.071  88.228 1.00 36.02  ? 4   LEU   D N   1 
ATOM   3190 C CA  . LEU   D 1 4   ? -3.526  -9.145  89.048 1.00 32.38  ? 4   LEU   D CA  1 
ATOM   3191 C C   . LEU   D 1 4   ? -2.087  -9.464  88.640 1.00 39.11  ? 4   LEU   D C   1 
ATOM   3192 O O   . LEU   D 1 4   ? -1.253  -9.798  89.490 1.00 30.08  ? 4   LEU   D O   1 
ATOM   3193 C CB  . LEU   D 1 4   ? -4.381  -10.401 88.920 1.00 33.36  ? 4   LEU   D CB  1 
ATOM   3194 C CG  . LEU   D 1 4   ? -5.833  -10.185 89.361 1.00 44.08  ? 4   LEU   D CG  1 
ATOM   3195 C CD1 . LEU   D 1 4   ? -6.640  -11.454 89.182 1.00 45.07  ? 4   LEU   D CD1 1 
ATOM   3196 C CD2 . LEU   D 1 4   ? -6.050  -9.507  90.727 1.00 45.73  ? 4   LEU   D CD2 1 
ATOM   3197 N N   . TYR   D 1 5   ? -1.768  -9.301  87.357 1.00 29.25  ? 5   TYR   D N   1 
ATOM   3198 C CA  . TYR   D 1 5   ? -0.437  -9.564  86.835 1.00 23.94  ? 5   TYR   D CA  1 
ATOM   3199 C C   . TYR   D 1 5   ? -0.253  -8.762  85.558 1.00 26.10  ? 5   TYR   D C   1 
ATOM   3200 O O   . TYR   D 1 5   ? -1.187  -8.609  84.772 1.00 23.03  ? 5   TYR   D O   1 
ATOM   3201 C CB  . TYR   D 1 5   ? -0.211  -11.060 86.568 1.00 27.75  ? 5   TYR   D CB  1 
ATOM   3202 C CG  . TYR   D 1 5   ? 1.074   -11.339 85.803 1.00 27.25  ? 5   TYR   D CG  1 
ATOM   3203 C CD1 . TYR   D 1 5   ? 2.327   -11.111 86.384 1.00 24.22  ? 5   TYR   D CD1 1 
ATOM   3204 C CD2 . TYR   D 1 5   ? 1.027   -11.829 84.495 1.00 26.84  ? 5   TYR   D CD2 1 
ATOM   3205 C CE1 . TYR   D 1 5   ? 3.492   -11.364 85.683 1.00 22.91  ? 5   TYR   D CE1 1 
ATOM   3206 C CE2 . TYR   D 1 5   ? 2.181   -12.083 83.784 1.00 23.34  ? 5   TYR   D CE2 1 
ATOM   3207 C CZ  . TYR   D 1 5   ? 3.402   -11.861 84.378 1.00 20.76  ? 5   TYR   D CZ  1 
ATOM   3208 O OH  . TYR   D 1 5   ? 4.519   -12.126 83.648 1.00 18.50  ? 5   TYR   D OH  1 
ATOM   3209 N N   . SER   D 1 6   ? 0.957   -8.252  85.375 1.00 26.20  ? 6   SER   D N   1 
ATOM   3210 C CA  . SER   D 1 6   ? 1.285   -7.356  84.290 1.00 23.53  ? 6   SER   D CA  1 
ATOM   3211 C C   . SER   D 1 6   ? 2.679   -7.714  83.779 1.00 27.60  ? 6   SER   D C   1 
ATOM   3212 O O   . SER   D 1 6   ? 3.578   -8.013  84.574 1.00 21.52  ? 6   SER   D O   1 
ATOM   3213 C CB  . SER   D 1 6   ? 1.207   -5.913  84.785 1.00 22.05  ? 6   SER   D CB  1 
ATOM   3214 O OG  . SER   D 1 6   ? 1.258   -5.015  83.710 1.00 30.67  ? 6   SER   D OG  1 
ATOM   3215 N N   . THR   D 1 7   ? 2.857   -7.700  82.452 1.00 18.98  ? 7   THR   D N   1 
ATOM   3216 C CA  . THR   D 1 7   ? 4.129   -8.058  81.835 1.00 18.29  ? 7   THR   D CA  1 
ATOM   3217 C C   . THR   D 1 7   ? 4.341   -7.222  80.580 1.00 22.32  ? 7   THR   D C   1 
ATOM   3218 O O   . THR   D 1 7   ? 3.380   -6.874  79.889 1.00 22.67  ? 7   THR   D O   1 
ATOM   3219 C CB  . THR   D 1 7   ? 4.188   -9.563  81.477 1.00 28.53  ? 7   THR   D CB  1 
ATOM   3220 O OG1 . THR   D 1 7   ? 5.478   -9.886  80.935 1.00 33.06  ? 7   THR   D OG1 1 
ATOM   3221 C CG2 . THR   D 1 7   ? 3.117   -9.926  80.458 1.00 21.37  ? 7   THR   D CG2 1 
ATOM   3222 N N   . GLN   D 1 8   ? 5.613   -6.904  80.298 1.00 24.00  ? 8   GLN   D N   1 
ATOM   3223 C CA  . GLN   D 1 8   ? 6.028   -6.068  79.169 1.00 22.81  ? 8   GLN   D CA  1 
ATOM   3224 C C   . GLN   D 1 8   ? 6.984   -6.851  78.273 1.00 23.50  ? 8   GLN   D C   1 
ATOM   3225 O O   . GLN   D 1 8   ? 7.879   -7.541  78.772 1.00 24.89  ? 8   GLN   D O   1 
ATOM   3226 C CB  . GLN   D 1 8   ? 6.739   -4.787  79.641 1.00 19.43  ? 8   GLN   D CB  1 
ATOM   3227 C CG  . GLN   D 1 8   ? 5.995   -3.899  80.621 1.00 20.85  ? 8   GLN   D CG  1 
ATOM   3228 C CD  . GLN   D 1 8   ? 6.710   -2.566  80.811 1.00 30.43  ? 8   GLN   D CD  1 
ATOM   3229 O OE1 . GLN   D 1 8   ? 7.917   -2.532  81.058 1.00 31.83  ? 8   GLN   D OE1 1 
ATOM   3230 N NE2 . GLN   D 1 8   ? 5.987   -1.464  80.625 1.00 29.77  ? 8   GLN   D NE2 1 
ATOM   3231 N N   . VAL   D 1 9   ? 6.796   -6.745  76.955 1.00 25.44  ? 9   VAL   D N   1 
ATOM   3232 C CA  . VAL   D 1 9   ? 7.667   -7.371  75.964 1.00 19.91  ? 9   VAL   D CA  1 
ATOM   3233 C C   . VAL   D 1 9   ? 8.071   -6.308  74.960 1.00 17.24  ? 9   VAL   D C   1 
ATOM   3234 O O   . VAL   D 1 9   ? 7.207   -5.589  74.429 1.00 14.78  ? 9   VAL   D O   1 
ATOM   3235 C CB  . VAL   D 1 9   ? 6.989   -8.553  75.236 1.00 18.50  ? 9   VAL   D CB  1 
ATOM   3236 C CG1 . VAL   D 1 9   ? 7.871   -9.041  74.082 1.00 16.28  ? 9   VAL   D CG1 1 
ATOM   3237 C CG2 . VAL   D 1 9   ? 6.691   -9.717  76.220 1.00 16.82  ? 9   VAL   D CG2 1 
ATOM   3238 N N   . LYS   D 1 10  ? 9.372   -6.195  74.716 1.00 14.12  ? 10  LYS   D N   1 
ATOM   3239 C CA  . LYS   D 1 10  ? 9.904   -5.298  73.695 1.00 17.02  ? 10  LYS   D CA  1 
ATOM   3240 C C   . LYS   D 1 10  ? 10.112  -6.069  72.401 1.00 15.85  ? 10  LYS   D C   1 
ATOM   3241 O O   . LYS   D 1 10  ? 10.857  -7.052  72.388 1.00 17.54  ? 10  LYS   D O   1 
ATOM   3242 C CB  . LYS   D 1 10  ? 11.254  -4.735  74.107 1.00 18.26  ? 10  LYS   D CB  1 
ATOM   3243 C CG  . LYS   D 1 10  ? 11.809  -3.673  73.178 1.00 19.30  ? 10  LYS   D CG  1 
ATOM   3244 C CD  . LYS   D 1 10  ? 13.209  -3.279  73.643 1.00 30.14  ? 10  LYS   D CD  1 
ATOM   3245 C CE  . LYS   D 1 10  ? 13.168  -2.610  74.998 1.00 34.03  ? 10  LYS   D CE  1 
ATOM   3246 N NZ  . LYS   D 1 10  ? 12.486  -1.288  74.948 1.00 43.50  ? 10  LYS   D NZ  1 
ATOM   3247 N N   . ALA   D 1 11  ? 9.549   -5.568  71.307 1.00 16.58  ? 11  ALA   D N   1 
ATOM   3248 C CA  . ALA   D 1 11  ? 9.712   -6.162  69.982 1.00 21.63  ? 11  ALA   D CA  1 
ATOM   3249 C C   . ALA   D 1 11  ? 10.378  -5.153  69.048 1.00 17.70  ? 11  ALA   D C   1 
ATOM   3250 O O   . ALA   D 1 11  ? 9.863   -4.048  68.854 1.00 17.40  ? 11  ALA   D O   1 
ATOM   3251 C CB  . ALA   D 1 11  ? 8.360   -6.609  69.423 1.00 22.41  ? 11  ALA   D CB  1 
ATOM   3252 N N   . VAL   D 1 12  ? 11.541  -5.505  68.504 1.00 17.97  ? 12  VAL   D N   1 
ATOM   3253 C CA  . VAL   D 1 12  ? 12.257  -4.616  67.583 1.00 17.98  ? 12  VAL   D CA  1 
ATOM   3254 C C   . VAL   D 1 12  ? 12.238  -5.223  66.186 1.00 18.32  ? 12  VAL   D C   1 
ATOM   3255 O O   . VAL   D 1 12  ? 12.579  -6.400  66.011 1.00 18.74  ? 12  VAL   D O   1 
ATOM   3256 C CB  . VAL   D 1 12  ? 13.709  -4.346  68.024 1.00 24.18  ? 12  VAL   D CB  1 
ATOM   3257 C CG1 . VAL   D 1 12  ? 14.371  -3.428  67.004 1.00 19.75  ? 12  VAL   D CG1 1 
ATOM   3258 C CG2 . VAL   D 1 12  ? 13.758  -3.689  69.415 1.00 23.40  ? 12  VAL   D CG2 1 
ATOM   3259 N N   . GLY   D 1 13  ? 11.820  -4.425  65.197 1.00 20.16  ? 13  GLY   D N   1 
ATOM   3260 C CA  . GLY   D 1 13  ? 12.038  -4.800  63.811 1.00 19.72  ? 13  GLY   D CA  1 
ATOM   3261 C C   . GLY   D 1 13  ? 11.040  -5.744  63.175 1.00 21.46  ? 13  GLY   D C   1 
ATOM   3262 O O   . GLY   D 1 13  ? 11.319  -6.255  62.090 1.00 29.31  ? 13  GLY   D O   1 
ATOM   3263 N N   . GLY   D 1 14  ? 9.888   -6.000  63.801 1.00 18.84  ? 14  GLY   D N   1 
ATOM   3264 C CA  . GLY   D 1 14  ? 8.816   -6.688  63.094 1.00 15.15  ? 14  GLY   D CA  1 
ATOM   3265 C C   . GLY   D 1 14  ? 9.032   -8.190  63.006 1.00 18.90  ? 14  GLY   D C   1 
ATOM   3266 O O   . GLY   D 1 14  ? 9.656   -8.803  63.878 1.00 16.01  ? 14  GLY   D O   1 
ATOM   3267 N N   . ARG   D 1 15  ? 8.508   -8.801  61.934 1.00 19.90  ? 15  ARG   D N   1 
ATOM   3268 C CA  . ARG   D 1 15  ? 8.435   -10.255 61.855 1.00 18.72  ? 15  ARG   D CA  1 
ATOM   3269 C C   . ARG   D 1 15  ? 9.786   -10.915 61.606 1.00 18.30  ? 15  ARG   D C   1 
ATOM   3270 O O   . ARG   D 1 15  ? 9.890   -12.142 61.724 1.00 22.27  ? 15  ARG   D O   1 
ATOM   3271 C CB  . ARG   D 1 15  ? 7.431   -10.656 60.772 1.00 22.94  ? 15  ARG   D CB  1 
ATOM   3272 C CG  . ARG   D 1 15  ? 5.986   -10.469 61.247 1.00 14.41  ? 15  ARG   D CG  1 
ATOM   3273 C CD  . ARG   D 1 15  ? 5.012   -10.665 60.128 1.00 17.73  ? 15  ARG   D CD  1 
ATOM   3274 N NE  . ARG   D 1 15  ? 3.631   -10.495 60.577 1.00 24.41  ? 15  ARG   D NE  1 
ATOM   3275 C CZ  . ARG   D 1 15  ? 2.864   -11.479 61.029 1.00 18.65  ? 15  ARG   D CZ  1 
ATOM   3276 N NH1 . ARG   D 1 15  ? 3.342   -12.708 61.076 1.00 14.27  ? 15  ARG   D NH1 1 
ATOM   3277 N NH2 . ARG   D 1 15  ? 1.618   -11.222 61.427 1.00 17.31  ? 15  ARG   D NH2 1 
ATOM   3278 N N   . SER   D 1 16  ? 10.824  -10.126 61.320 1.00 19.78  ? 16  SER   D N   1 
ATOM   3279 C CA  . SER   D 1 16  ? 12.190  -10.599 61.153 1.00 26.57  ? 16  SER   D CA  1 
ATOM   3280 C C   . SER   D 1 16  ? 13.119  -10.099 62.251 1.00 26.02  ? 16  SER   D C   1 
ATOM   3281 O O   . SER   D 1 16  ? 14.343  -10.254 62.131 1.00 25.81  ? 16  SER   D O   1 
ATOM   3282 C CB  . SER   D 1 16  ? 12.736  -10.152 59.790 1.00 27.96  ? 16  SER   D CB  1 
ATOM   3283 O OG  . SER   D 1 16  ? 11.972  -10.759 58.775 1.00 43.79  ? 16  SER   D OG  1 
ATOM   3284 N N   . GLY   D 1 17  ? 12.583  -9.485  63.298 1.00 30.99  ? 17  GLY   D N   1 
ATOM   3285 C CA  . GLY   D 1 17  ? 13.369  -8.887  64.373 1.00 20.64  ? 17  GLY   D CA  1 
ATOM   3286 C C   . GLY   D 1 17  ? 13.396  -9.777  65.596 1.00 30.18  ? 17  GLY   D C   1 
ATOM   3287 O O   . GLY   D 1 17  ? 13.548  -11.001 65.495 1.00 24.37  ? 17  GLY   D O   1 
ATOM   3288 N N   . THR   D 1 18  ? 13.222  -9.168  66.768 1.00 26.32  ? 18  THR   D N   1 
ATOM   3289 C CA  . THR   D 1 18  ? 13.365  -9.897  68.018 1.00 17.38  ? 18  THR   D CA  1 
ATOM   3290 C C   . THR   D 1 18  ? 12.265  -9.512  68.994 1.00 23.33  ? 18  THR   D C   1 
ATOM   3291 O O   . THR   D 1 18  ? 11.635  -8.453  68.873 1.00 19.72  ? 18  THR   D O   1 
ATOM   3292 C CB  . THR   D 1 18  ? 14.730  -9.613  68.655 1.00 30.64  ? 18  THR   D CB  1 
ATOM   3293 O OG1 . THR   D 1 18  ? 14.863  -8.195  68.807 1.00 20.39  ? 18  THR   D OG1 1 
ATOM   3294 C CG2 . THR   D 1 18  ? 15.881  -10.180 67.779 1.00 23.70  ? 18  THR   D CG2 1 
ATOM   3295 N N   . ILE   D 1 19  ? 12.070  -10.386 69.994 1.00 23.50  ? 19  ILE   D N   1 
ATOM   3296 C CA  . ILE   D 1 19  ? 11.232  -10.104 71.152 1.00 19.42  ? 19  ILE   D CA  1 
ATOM   3297 C C   . ILE   D 1 19  ? 12.020  -10.410 72.416 1.00 28.03  ? 19  ILE   D C   1 
ATOM   3298 O O   . ILE   D 1 19  ? 12.802  -11.370 72.475 1.00 21.85  ? 19  ILE   D O   1 
ATOM   3299 C CB  . ILE   D 1 19  ? 9.917   -10.917 71.163 1.00 21.72  ? 19  ILE   D CB  1 
ATOM   3300 C CG1 . ILE   D 1 19  ? 10.243  -12.403 71.133 1.00 22.17  ? 19  ILE   D CG1 1 
ATOM   3301 C CG2 . ILE   D 1 19  ? 8.988   -10.496 70.013 1.00 20.88  ? 19  ILE   D CG2 1 
ATOM   3302 C CD1 . ILE   D 1 19  ? 9.180   -13.241 71.710 1.00 30.58  ? 19  ILE   D CD1 1 
ATOM   3303 N N   . ARG   D 1 20  ? 11.782  -9.596  73.447 1.00 19.35  ? 20  ARG   D N   1 
ATOM   3304 C CA  . ARG   D 1 20  ? 12.447  -9.777  74.731 1.00 25.20  ? 20  ARG   D CA  1 
ATOM   3305 C C   . ARG   D 1 20  ? 11.540  -9.268  75.843 1.00 18.25  ? 20  ARG   D C   1 
ATOM   3306 O O   . ARG   D 1 20  ? 11.241  -8.067  75.902 1.00 16.20  ? 20  ARG   D O   1 
ATOM   3307 C CB  . ARG   D 1 20  ? 13.800  -9.063  74.761 1.00 22.22  ? 20  ARG   D CB  1 
ATOM   3308 C CG  . ARG   D 1 20  ? 14.653  -9.556  75.928 1.00 28.25  ? 20  ARG   D CG  1 
ATOM   3309 C CD  . ARG   D 1 20  ? 15.908  -8.732  76.152 1.00 37.24  ? 20  ARG   D CD  1 
ATOM   3310 N NE  . ARG   D 1 20  ? 16.496  -9.055  77.450 1.00 44.18  ? 20  ARG   D NE  1 
ATOM   3311 C CZ  . ARG   D 1 20  ? 16.090  -8.525  78.599 1.00 42.73  ? 20  ARG   D CZ  1 
ATOM   3312 N NH1 . ARG   D 1 20  ? 15.108  -7.632  78.605 1.00 37.60  ? 20  ARG   D NH1 1 
ATOM   3313 N NH2 . ARG   D 1 20  ? 16.670  -8.879  79.742 1.00 50.60  ? 20  ARG   D NH2 1 
ATOM   3314 N N   . SER   D 1 21  ? 11.101  -10.172 76.715 1.00 19.30  ? 21  SER   D N   1 
ATOM   3315 C CA  . SER   D 1 21  ? 10.352  -9.742  77.896 1.00 21.38  ? 21  SER   D CA  1 
ATOM   3316 C C   . SER   D 1 21  ? 11.261  -8.942  78.815 1.00 27.45  ? 21  SER   D C   1 
ATOM   3317 O O   . SER   D 1 21  ? 12.478  -9.153  78.860 1.00 23.14  ? 21  SER   D O   1 
ATOM   3318 C CB  . SER   D 1 21  ? 9.784   -10.933 78.660 1.00 19.67  ? 21  SER   D CB  1 
ATOM   3319 O OG  . SER   D 1 21  ? 10.817  -11.854 78.995 1.00 19.99  ? 21  SER   D OG  1 
ATOM   3320 N N   . GLU   D 1 22  ? 10.662  -7.995  79.543 1.00 24.57  ? 22  GLU   D N   1 
ATOM   3321 C CA  . GLU   D 1 22  ? 11.468  -7.105  80.363 1.00 23.45  ? 22  GLU   D CA  1 
ATOM   3322 C C   . GLU   D 1 22  ? 12.086  -7.835  81.549 1.00 29.15  ? 22  GLU   D C   1 
ATOM   3323 O O   . GLU   D 1 22  ? 13.089  -7.367  82.091 1.00 30.06  ? 22  GLU   D O   1 
ATOM   3324 C CB  . GLU   D 1 22  ? 10.627  -5.913  80.839 1.00 25.78  ? 22  GLU   D CB  1 
ATOM   3325 C CG  . GLU   D 1 22  ? 10.338  -4.939  79.684 1.00 26.33  ? 22  GLU   D CG  1 
ATOM   3326 C CD  . GLU   D 1 22  ? 11.554  -4.123  79.277 1.00 35.29  ? 22  GLU   D CD  1 
ATOM   3327 O OE1 . GLU   D 1 22  ? 12.299  -4.547  78.363 1.00 40.50  ? 22  GLU   D OE1 1 
ATOM   3328 O OE2 . GLU   D 1 22  ? 11.748  -3.031  79.841 1.00 46.14  ? 22  GLU   D OE2 1 
ATOM   3329 N N   . ASP   D 1 23  ? 11.515  -8.970  81.961 1.00 32.07  ? 23  ASP   D N   1 
ATOM   3330 C CA  . ASP   D 1 23  ? 12.159  -9.793  82.978 1.00 34.38  ? 23  ASP   D CA  1 
ATOM   3331 C C   . ASP   D 1 23  ? 13.219  -10.737 82.403 1.00 28.56  ? 23  ASP   D C   1 
ATOM   3332 O O   . ASP   D 1 23  ? 13.860  -11.459 83.169 1.00 31.53  ? 23  ASP   D O   1 
ATOM   3333 C CB  . ASP   D 1 23  ? 11.086  -10.567 83.768 1.00 29.01  ? 23  ASP   D CB  1 
ATOM   3334 C CG  . ASP   D 1 23  ? 10.271  -11.527 82.894 1.00 34.83  ? 23  ASP   D CG  1 
ATOM   3335 O OD1 . ASP   D 1 23  ? 10.661  -11.759 81.734 1.00 31.67  ? 23  ASP   D OD1 1 
ATOM   3336 O OD2 . ASP   D 1 23  ? 9.229   -12.055 83.364 1.00 28.50  ? 23  ASP   D OD2 1 
ATOM   3337 N N   . GLY   D 1 24  ? 13.437  -10.745 81.082 1.00 34.17  ? 24  GLY   D N   1 
ATOM   3338 C CA  . GLY   D 1 24  ? 14.440  -11.611 80.476 1.00 27.02  ? 24  GLY   D CA  1 
ATOM   3339 C C   . GLY   D 1 24  ? 14.049  -13.070 80.320 1.00 26.98  ? 24  GLY   D C   1 
ATOM   3340 O O   . GLY   D 1 24  ? 14.846  -13.852 79.791 1.00 27.90  ? 24  GLY   D O   1 
ATOM   3341 N N   . ILE   D 1 25  ? 12.855  -13.463 80.757 1.00 20.29  ? 25  ILE   D N   1 
ATOM   3342 C CA  . ILE   D 1 25  ? 12.442  -14.865 80.669 1.00 28.21  ? 25  ILE   D CA  1 
ATOM   3343 C C   . ILE   D 1 25  ? 12.190  -15.266 79.213 1.00 30.20  ? 25  ILE   D C   1 
ATOM   3344 O O   . ILE   D 1 25  ? 12.673  -16.302 78.741 1.00 28.29  ? 25  ILE   D O   1 
ATOM   3345 C CB  . ILE   D 1 25  ? 11.205  -15.115 81.551 1.00 28.67  ? 25  ILE   D CB  1 
ATOM   3346 C CG1 . ILE   D 1 25  ? 11.502  -14.802 83.024 1.00 32.83  ? 25  ILE   D CG1 1 
ATOM   3347 C CG2 . ILE   D 1 25  ? 10.745  -16.559 81.421 1.00 29.15  ? 25  ILE   D CG2 1 
ATOM   3348 C CD1 . ILE   D 1 25  ? 12.607  -15.663 83.618 1.00 33.07  ? 25  ILE   D CD1 1 
ATOM   3349 N N   . LEU   D 1 26  ? 11.444  -14.455 78.475 1.00 19.97  ? 26  LEU   D N   1 
ATOM   3350 C CA  . LEU   D 1 26  ? 11.167  -14.732 77.070 1.00 19.98  ? 26  LEU   D CA  1 
ATOM   3351 C C   . LEU   D 1 26  ? 12.076  -13.861 76.209 1.00 23.61  ? 26  LEU   D C   1 
ATOM   3352 O O   . LEU   D 1 26  ? 11.969  -12.627 76.237 1.00 25.28  ? 26  LEU   D O   1 
ATOM   3353 C CB  . LEU   D 1 26  ? 9.693   -14.475 76.759 1.00 22.38  ? 26  LEU   D CB  1 
ATOM   3354 C CG  . LEU   D 1 26  ? 9.125   -14.940 75.424 1.00 21.11  ? 26  LEU   D CG  1 
ATOM   3355 C CD1 . LEU   D 1 26  ? 9.198   -16.445 75.324 1.00 22.57  ? 26  LEU   D CD1 1 
ATOM   3356 C CD2 . LEU   D 1 26  ? 7.686   -14.474 75.305 1.00 19.26  ? 26  LEU   D CD2 1 
ATOM   3357 N N   . GLU   D 1 27  ? 12.987  -14.498 75.473 1.00 17.64  ? 27  GLU   D N   1 
ATOM   3358 C CA  . GLU   D 1 27  ? 13.922  -13.791 74.602 1.00 21.60  ? 27  GLU   D CA  1 
ATOM   3359 C C   . GLU   D 1 27  ? 14.135  -14.640 73.355 1.00 30.28  ? 27  GLU   D C   1 
ATOM   3360 O O   . GLU   D 1 27  ? 14.734  -15.721 73.430 1.00 23.13  ? 27  GLU   D O   1 
ATOM   3361 C CB  . GLU   D 1 27  ? 15.242  -13.515 75.323 1.00 22.79  ? 27  GLU   D CB  1 
ATOM   3362 C CG  . GLU   D 1 27  ? 16.204  -12.635 74.550 1.00 27.44  ? 27  GLU   D CG  1 
ATOM   3363 C CD  . GLU   D 1 27  ? 17.365  -12.111 75.415 1.00 45.61  ? 27  GLU   D CD  1 
ATOM   3364 O OE1 . GLU   D 1 27  ? 17.259  -12.115 76.675 1.00 44.78  ? 27  GLU   D OE1 1 
ATOM   3365 O OE2 . GLU   D 1 27  ? 18.385  -11.690 74.824 1.00 47.37  ? 27  GLU   D OE2 1 
ATOM   3366 N N   . LEU   D 1 28  ? 13.637  -14.170 72.211 1.00 25.45  ? 28  LEU   D N   1 
ATOM   3367 C CA  . LEU   D 1 28  ? 13.609  -15.004 71.016 1.00 25.62  ? 28  LEU   D CA  1 
ATOM   3368 C C   . LEU   D 1 28  ? 13.805  -14.169 69.756 1.00 28.48  ? 28  LEU   D C   1 
ATOM   3369 O O   . LEU   D 1 28  ? 13.418  -12.994 69.686 1.00 24.32  ? 28  LEU   D O   1 
ATOM   3370 C CB  . LEU   D 1 28  ? 12.289  -15.782 70.889 1.00 23.48  ? 28  LEU   D CB  1 
ATOM   3371 C CG  . LEU   D 1 28  ? 11.947  -16.834 71.939 1.00 31.73  ? 28  LEU   D CG  1 
ATOM   3372 C CD1 . LEU   D 1 28  ? 10.544  -17.318 71.685 1.00 26.21  ? 28  LEU   D CD1 1 
ATOM   3373 C CD2 . LEU   D 1 28  ? 12.945  -17.990 71.938 1.00 24.24  ? 28  LEU   D CD2 1 
ATOM   3374 N N   . LYS   D 1 29  ? 14.418  -14.809 68.764 1.00 28.11  ? 29  LYS   D N   1 
ATOM   3375 C CA  . LYS   D 1 29  ? 14.471  -14.329 67.393 1.00 24.91  ? 29  LYS   D CA  1 
ATOM   3376 C C   . LYS   D 1 29  ? 13.174  -14.687 66.675 1.00 23.49  ? 29  LYS   D C   1 
ATOM   3377 O O   . LYS   D 1 29  ? 12.518  -15.675 67.009 1.00 26.48  ? 29  LYS   D O   1 
ATOM   3378 C CB  . LYS   D 1 29  ? 15.664  -14.966 66.674 1.00 29.36  ? 29  LYS   D CB  1 
ATOM   3379 C CG  . LYS   D 1 29  ? 15.891  -14.491 65.256 1.00 33.04  ? 29  LYS   D CG  1 
ATOM   3380 C CD  . LYS   D 1 29  ? 16.057  -12.976 65.208 1.00 37.10  ? 29  LYS   D CD  1 
ATOM   3381 C CE  . LYS   D 1 29  ? 15.958  -12.451 63.776 1.00 38.74  ? 29  LYS   D CE  1 
ATOM   3382 N NZ  . LYS   D 1 29  ? 16.630  -11.135 63.602 1.00 43.05  ? 29  LYS   D NZ  1 
ATOM   3383 N N   . LEU   D 1 30  ? 12.803  -13.875 65.682 1.00 18.05  ? 30  LEU   D N   1 
ATOM   3384 C CA  . LEU   D 1 30  ? 11.644  -14.139 64.840 1.00 24.78  ? 30  LEU   D CA  1 
ATOM   3385 C C   . LEU   D 1 30  ? 12.066  -14.288 63.383 1.00 24.27  ? 30  LEU   D C   1 
ATOM   3386 O O   . LEU   D 1 30  ? 13.002  -13.629 62.920 1.00 19.19  ? 30  LEU   D O   1 
ATOM   3387 C CB  . LEU   D 1 30  ? 10.611  -13.013 64.936 1.00 20.04  ? 30  LEU   D CB  1 
ATOM   3388 C CG  . LEU   D 1 30  ? 10.120  -12.665 66.336 1.00 25.80  ? 30  LEU   D CG  1 
ATOM   3389 C CD1 . LEU   D 1 30  ? 9.039   -11.618 66.225 1.00 21.24  ? 30  LEU   D CD1 1 
ATOM   3390 C CD2 . LEU   D 1 30  ? 9.576   -13.905 66.983 1.00 23.65  ? 30  LEU   D CD2 1 
ATOM   3391 N N   . ALA   D 1 31  ? 11.335  -15.124 62.653 1.00 21.67  ? 31  ALA   D N   1 
ATOM   3392 C CA  . ALA   D 1 31  ? 11.569  -15.322 61.230 1.00 25.28  ? 31  ALA   D CA  1 
ATOM   3393 C C   . ALA   D 1 31  ? 10.245  -15.400 60.491 1.00 24.46  ? 31  ALA   D C   1 
ATOM   3394 O O   . ALA   D 1 31  ? 9.254   -15.918 61.016 1.00 19.79  ? 31  ALA   D O   1 
ATOM   3395 C CB  . ALA   D 1 31  ? 12.385  -16.606 60.952 1.00 23.11  ? 31  ALA   D CB  1 
ATOM   3396 N N   . LEU   D 1 32  ? 10.235  -14.894 59.267 1.00 23.86  ? 32  LEU   D N   1 
ATOM   3397 C CA  . LEU   D 1 32  ? 9.161   -15.243 58.355 1.00 19.23  ? 32  LEU   D CA  1 
ATOM   3398 C C   . LEU   D 1 32  ? 9.137   -16.760 58.167 1.00 20.90  ? 32  LEU   D C   1 
ATOM   3399 O O   . LEU   D 1 32  ? 10.198  -17.386 58.054 1.00 21.46  ? 32  LEU   D O   1 
ATOM   3400 C CB  . LEU   D 1 32  ? 9.367   -14.560 57.002 1.00 23.26  ? 32  LEU   D CB  1 
ATOM   3401 C CG  . LEU   D 1 32  ? 8.847   -13.136 56.840 1.00 26.94  ? 32  LEU   D CG  1 
ATOM   3402 C CD1 . LEU   D 1 32  ? 8.982   -12.711 55.369 1.00 32.52  ? 32  LEU   D CD1 1 
ATOM   3403 C CD2 . LEU   D 1 32  ? 7.408   -13.060 57.295 1.00 22.88  ? 32  LEU   D CD2 1 
ATOM   3404 N N   . PRO   D 1 33  ? 7.966   -17.380 58.139 1.00 19.55  ? 33  PRO   D N   1 
ATOM   3405 C CA  . PRO   D 1 33  ? 7.928   -18.821 57.887 1.00 22.23  ? 33  PRO   D CA  1 
ATOM   3406 C C   . PRO   D 1 33  ? 8.241   -19.138 56.427 1.00 31.95  ? 33  PRO   D C   1 
ATOM   3407 O O   . PRO   D 1 33  ? 8.194   -18.285 55.534 1.00 23.30  ? 33  PRO   D O   1 
ATOM   3408 C CB  . PRO   D 1 33  ? 6.490   -19.198 58.236 1.00 23.95  ? 33  PRO   D CB  1 
ATOM   3409 C CG  . PRO   D 1 33  ? 5.722   -17.937 57.954 1.00 23.35  ? 33  PRO   D CG  1 
ATOM   3410 C CD  . PRO   D 1 33  ? 6.627   -16.819 58.363 1.00 17.62  ? 33  PRO   D CD  1 
ATOM   3411 N N   . LYS   D 1 34  ? 8.539   -20.416 56.201 1.00 26.02  ? 34  LYS   D N   1 
ATOM   3412 C CA  . LYS   D 1 34  ? 8.899   -20.919 54.876 1.00 32.08  ? 34  LYS   D CA  1 
ATOM   3413 C C   . LYS   D 1 34  ? 7.799   -20.617 53.875 1.00 25.33  ? 34  LYS   D C   1 
ATOM   3414 O O   . LYS   D 1 34  ? 8.076   -20.162 52.765 1.00 26.16  ? 34  LYS   D O   1 
ATOM   3415 C CB  . LYS   D 1 34  ? 9.103   -22.435 54.958 1.00 27.95  ? 34  LYS   D CB  1 
ATOM   3416 C CG  . LYS   D 1 34  ? 10.420  -22.923 55.537 1.00 26.89  ? 34  LYS   D CG  1 
ATOM   3417 C CD  . LYS   D 1 34  ? 10.291  -22.497 56.997 1.00 44.21  ? 34  LYS   D CD  1 
ATOM   3418 C CE  . LYS   D 1 34  ? 9.106   -23.174 57.736 1.00 44.45  ? 34  LYS   D CE  1 
ATOM   3419 N NZ  . LYS   D 1 34  ? 8.924   -22.730 59.148 1.00 38.97  ? 34  LYS   D NZ  1 
ATOM   3420 N N   . GLU   D 1 35  ? 6.542   -20.870 54.250 1.00 22.54  ? 35  GLU   D N   1 
ATOM   3421 C CA  . GLU   D 1 35  ? 5.431   -20.604 53.341 1.00 28.40  ? 35  GLU   D CA  1 
ATOM   3422 C C   . GLU   D 1 35  ? 5.411   -19.163 52.846 1.00 23.83  ? 35  GLU   D C   1 
ATOM   3423 O O   . GLU   D 1 35  ? 4.779   -18.880 51.824 1.00 26.35  ? 35  GLU   D O   1 
ATOM   3424 C CB  . GLU   D 1 35  ? 4.082   -20.886 54.011 1.00 37.67  ? 35  GLU   D CB  1 
ATOM   3425 C CG  . GLU   D 1 35  ? 3.812   -22.332 54.378 1.00 39.34  ? 35  GLU   D CG  1 
ATOM   3426 C CD  . GLU   D 1 35  ? 4.218   -22.655 55.818 1.00 45.42  ? 35  GLU   D CD  1 
ATOM   3427 O OE1 . GLU   D 1 35  ? 3.405   -23.302 56.529 1.00 46.35  ? 35  GLU   D OE1 1 
ATOM   3428 O OE2 . GLU   D 1 35  ? 5.342   -22.273 56.242 1.00 36.32  ? 35  GLU   D OE2 1 
ATOM   3429 N N   . LEU   D 1 36  ? 6.051   -18.236 53.562 1.00 28.75  ? 36  LEU   D N   1 
ATOM   3430 C CA  . LEU   D 1 36  ? 6.119   -16.838 53.144 1.00 30.63  ? 36  LEU   D CA  1 
ATOM   3431 C C   . LEU   D 1 36  ? 7.509   -16.448 52.671 1.00 25.53  ? 36  LEU   D C   1 
ATOM   3432 O O   . LEU   D 1 36  ? 7.814   -15.257 52.559 1.00 30.54  ? 36  LEU   D O   1 
ATOM   3433 C CB  . LEU   D 1 36  ? 5.664   -15.905 54.267 1.00 32.64  ? 36  LEU   D CB  1 
ATOM   3434 C CG  . LEU   D 1 36  ? 4.199   -16.046 54.690 1.00 35.21  ? 36  LEU   D CG  1 
ATOM   3435 C CD1 . LEU   D 1 36  ? 3.888   -15.083 55.827 1.00 30.63  ? 36  LEU   D CD1 1 
ATOM   3436 C CD2 . LEU   D 1 36  ? 3.279   -15.803 53.509 1.00 29.76  ? 36  LEU   D CD2 1 
ATOM   3437 N N   . GLY   D 1 37  ? 8.350   -17.432 52.376 1.00 28.51  ? 37  GLY   D N   1 
ATOM   3438 C CA  . GLY   D 1 37  ? 9.647   -17.170 51.802 1.00 29.94  ? 37  GLY   D CA  1 
ATOM   3439 C C   . GLY   D 1 37  ? 10.781  -17.026 52.782 1.00 32.72  ? 37  GLY   D C   1 
ATOM   3440 O O   . GLY   D 1 37  ? 11.936  -16.885 52.345 1.00 34.66  ? 37  GLY   D O   1 
ATOM   3441 N N   . GLY   D 1 38  ? 10.498  -17.044 54.080 1.00 26.02  ? 38  GLY   D N   1 
ATOM   3442 C CA  . GLY   D 1 38  ? 11.542  -16.975 55.061 1.00 29.23  ? 38  GLY   D CA  1 
ATOM   3443 C C   . GLY   D 1 38  ? 12.168  -18.342 55.262 1.00 33.29  ? 38  GLY   D C   1 
ATOM   3444 O O   . GLY   D 1 38  ? 11.801  -19.351 54.645 1.00 24.72  ? 38  GLY   D O   1 
ATOM   3445 N N   . LYS   D 1 39  ? 13.136  -18.379 56.176 1.00 32.02  ? 39  LYS   D N   1 
ATOM   3446 C CA  . LYS   D 1 39  ? 13.779  -19.659 56.461 1.00 39.46  ? 39  LYS   D CA  1 
ATOM   3447 C C   . LYS   D 1 39  ? 13.068  -20.448 57.566 1.00 37.53  ? 39  LYS   D C   1 
ATOM   3448 O O   . LYS   D 1 39  ? 13.359  -21.634 57.744 1.00 34.14  ? 39  LYS   D O   1 
ATOM   3449 C CB  . LYS   D 1 39  ? 15.263  -19.474 56.813 1.00 39.61  ? 39  LYS   D CB  1 
ATOM   3450 C CG  . LYS   D 1 39  ? 16.094  -18.980 55.652 1.00 44.73  ? 39  LYS   D CG  1 
ATOM   3451 C CD  . LYS   D 1 39  ? 17.532  -18.993 56.016 1.00 48.21  ? 39  LYS   D CD  1 
ATOM   3452 C CE  . LYS   D 1 39  ? 17.924  -17.908 56.936 1.00 51.51  ? 39  LYS   D CE  1 
ATOM   3453 N NZ  . LYS   D 1 39  ? 19.388  -17.848 57.192 1.00 54.94  ? 39  LYS   D NZ  1 
ATOM   3454 N N   . GLY   D 1 40  ? 12.112  -19.841 58.270 1.00 34.67  ? 40  GLY   D N   1 
ATOM   3455 C CA  . GLY   D 1 40  ? 11.441  -20.509 59.392 1.00 33.59  ? 40  GLY   D CA  1 
ATOM   3456 C C   . GLY   D 1 40  ? 12.388  -21.159 60.368 1.00 27.55  ? 40  GLY   D C   1 
ATOM   3457 O O   . GLY   D 1 40  ? 12.122  -22.264 60.864 1.00 28.01  ? 40  GLY   D O   1 
ATOM   3458 N N   . ASP   D 1 41  ? 13.523  -20.519 60.645 1.00 25.88  ? 41  ASP   D N   1 
ATOM   3459 C CA  . ASP   D 1 41  ? 14.449  -20.986 61.662 1.00 34.30  ? 41  ASP   D CA  1 
ATOM   3460 C C   . ASP   D 1 41  ? 14.064  -20.494 63.051 1.00 32.43  ? 41  ASP   D C   1 
ATOM   3461 O O   . ASP   D 1 41  ? 14.727  -20.860 64.029 1.00 29.30  ? 41  ASP   D O   1 
ATOM   3462 C CB  . ASP   D 1 41  ? 15.870  -20.523 61.315 1.00 41.89  ? 41  ASP   D CB  1 
ATOM   3463 C CG  . ASP   D 1 41  ? 15.985  -19.005 61.237 1.00 49.04  ? 41  ASP   D CG  1 
ATOM   3464 O OD1 . ASP   D 1 41  ? 15.119  -18.374 60.597 1.00 38.83  ? 41  ASP   D OD1 1 
ATOM   3465 O OD2 . ASP   D 1 41  ? 16.936  -18.444 61.831 1.00 66.58  ? 41  ASP   D OD2 1 
ATOM   3466 N N   . ALA   D 1 42  ? 12.999  -19.690 63.145 1.00 29.97  ? 42  ALA   D N   1 
ATOM   3467 C CA  . ALA   D 1 42  ? 12.588  -19.040 64.378 1.00 23.77  ? 42  ALA   D CA  1 
ATOM   3468 C C   . ALA   D 1 42  ? 11.067  -18.857 64.357 1.00 25.45  ? 42  ALA   D C   1 
ATOM   3469 O O   . ALA   D 1 42  ? 10.405  -19.048 63.329 1.00 20.05  ? 42  ALA   D O   1 
ATOM   3470 C CB  . ALA   D 1 42  ? 13.337  -17.712 64.567 1.00 17.67  ? 42  ALA   D CB  1 
ATOM   3471 N N   . THR   D 1 43  ? 10.513  -18.501 65.517 1.00 20.97  ? 43  THR   D N   1 
ATOM   3472 C CA  . THR   D 1 43  ? 9.066   -18.440 65.699 1.00 25.23  ? 43  THR   D CA  1 
ATOM   3473 C C   . THR   D 1 43  ? 8.484   -17.177 65.044 1.00 16.29  ? 43  THR   D C   1 
ATOM   3474 O O   . THR   D 1 43  ? 9.185   -16.415 64.366 1.00 18.75  ? 43  THR   D O   1 
ATOM   3475 C CB  . THR   D 1 43  ? 8.742   -18.565 67.194 1.00 19.34  ? 43  THR   D CB  1 
ATOM   3476 O OG1 . THR   D 1 43  ? 7.360   -18.908 67.378 1.00 19.76  ? 43  THR   D OG1 1 
ATOM   3477 C CG2 . THR   D 1 43  ? 9.086   -17.297 67.977 1.00 14.18  ? 43  THR   D CG2 1 
ATOM   3478 N N   . ASN   D 1 44  ? 7.182   -16.950 65.235 1.00 19.03  ? 44  ASN   D N   1 
ATOM   3479 C CA  . ASN   D 1 44  ? 6.482   -15.866 64.551 1.00 16.06  ? 44  ASN   D CA  1 
ATOM   3480 C C   . ASN   D 1 44  ? 5.232   -15.500 65.361 1.00 15.60  ? 44  ASN   D C   1 
ATOM   3481 O O   . ASN   D 1 44  ? 4.826   -16.244 66.256 1.00 16.58  ? 44  ASN   D O   1 
ATOM   3482 C CB  . ASN   D 1 44  ? 6.119   -16.278 63.108 1.00 12.86  ? 44  ASN   D CB  1 
ATOM   3483 C CG  . ASN   D 1 44  ? 5.230   -17.501 63.063 1.00 18.22  ? 44  ASN   D CG  1 
ATOM   3484 O OD1 . ASN   D 1 44  ? 4.063   -17.443 63.450 1.00 25.41  ? 44  ASN   D OD1 1 
ATOM   3485 N ND2 . ASN   D 1 44  ? 5.763   -18.611 62.547 1.00 18.19  ? 44  ASN   D ND2 1 
ATOM   3486 N N   . PRO   D 1 45  ? 4.580   -14.365 65.051 1.00 21.38  ? 45  PRO   D N   1 
ATOM   3487 C CA  . PRO   D 1 45  ? 3.464   -13.900 65.920 1.00 19.35  ? 45  PRO   D CA  1 
ATOM   3488 C C   . PRO   D 1 45  ? 2.297   -14.864 66.028 1.00 24.29  ? 45  PRO   D C   1 
ATOM   3489 O O   . PRO   D 1 45  ? 1.639   -14.927 67.083 1.00 15.96  ? 45  PRO   D O   1 
ATOM   3490 C CB  . PRO   D 1 45  ? 3.042   -12.587 65.257 1.00 19.91  ? 45  PRO   D CB  1 
ATOM   3491 C CG  . PRO   D 1 45  ? 4.383   -12.049 64.743 1.00 17.44  ? 45  PRO   D CG  1 
ATOM   3492 C CD  . PRO   D 1 45  ? 5.032   -13.289 64.148 1.00 17.24  ? 45  PRO   D CD  1 
ATOM   3493 N N   . GLU   D 1 46  ? 2.024   -15.609 64.957 1.00 18.52  ? 46  GLU   D N   1 
ATOM   3494 C CA  . GLU   D 1 46  ? 0.937   -16.578 64.961 1.00 19.94  ? 46  GLU   D CA  1 
ATOM   3495 C C   . GLU   D 1 46  ? 1.245   -17.754 65.885 1.00 19.09  ? 46  GLU   D C   1 
ATOM   3496 O O   . GLU   D 1 46  ? 0.362   -18.223 66.602 1.00 15.21  ? 46  GLU   D O   1 
ATOM   3497 C CB  . GLU   D 1 46  ? 0.690   -17.045 63.534 1.00 17.49  ? 46  GLU   D CB  1 
ATOM   3498 C CG  . GLU   D 1 46  ? -0.008  -16.009 62.687 1.00 16.20  ? 46  GLU   D CG  1 
ATOM   3499 C CD  . GLU   D 1 46  ? 0.878   -14.812 62.379 1.00 26.57  ? 46  GLU   D CD  1 
ATOM   3500 O OE1 . GLU   D 1 46  ? 2.036   -15.009 61.926 1.00 22.35  ? 46  GLU   D OE1 1 
ATOM   3501 O OE2 . GLU   D 1 46  ? 0.417   -13.671 62.621 1.00 22.29  ? 46  GLU   D OE2 1 
ATOM   3502 N N   . GLN   D 1 47  ? 2.493   -18.240 65.882 1.00 18.40  ? 47  GLN   D N   1 
ATOM   3503 C CA  . GLN   D 1 47  ? 2.882   -19.303 66.811 1.00 19.34  ? 47  GLN   D CA  1 
ATOM   3504 C C   . GLN   D 1 47  ? 2.764   -18.829 68.258 1.00 21.35  ? 47  GLN   D C   1 
ATOM   3505 O O   . GLN   D 1 47  ? 2.199   -19.526 69.107 1.00 16.87  ? 47  GLN   D O   1 
ATOM   3506 C CB  . GLN   D 1 47  ? 4.312   -19.769 66.530 1.00 15.03  ? 47  GLN   D CB  1 
ATOM   3507 C CG  . GLN   D 1 47  ? 4.470   -20.538 65.253 1.00 31.64  ? 47  GLN   D CG  1 
ATOM   3508 C CD  . GLN   D 1 47  ? 5.783   -21.319 65.197 1.00 25.78  ? 47  GLN   D CD  1 
ATOM   3509 O OE1 . GLN   D 1 47  ? 6.740   -21.008 65.913 1.00 21.13  ? 47  GLN   D OE1 1 
ATOM   3510 N NE2 . GLN   D 1 47  ? 5.836   -22.315 64.323 1.00 30.57  ? 47  GLN   D NE2 1 
ATOM   3511 N N   . LEU   D 1 48  ? 3.305   -17.637 68.548 1.00 16.07  ? 48  LEU   D N   1 
ATOM   3512 C CA  . LEU   D 1 48  ? 3.181   -17.034 69.875 1.00 18.80  ? 48  LEU   D CA  1 
ATOM   3513 C C   . LEU   D 1 48  ? 1.727   -16.921 70.325 1.00 17.89  ? 48  LEU   D C   1 
ATOM   3514 O O   . LEU   D 1 48  ? 1.371   -17.328 71.441 1.00 18.31  ? 48  LEU   D O   1 
ATOM   3515 C CB  . LEU   D 1 48  ? 3.851   -15.655 69.883 1.00 12.01  ? 48  LEU   D CB  1 
ATOM   3516 C CG  . LEU   D 1 48  ? 5.365   -15.779 69.750 1.00 13.36  ? 48  LEU   D CG  1 
ATOM   3517 C CD1 . LEU   D 1 48  ? 6.018   -14.444 69.432 1.00 16.21  ? 48  LEU   D CD1 1 
ATOM   3518 C CD2 . LEU   D 1 48  ? 5.933   -16.358 71.060 1.00 12.18  ? 48  LEU   D CD2 1 
ATOM   3519 N N   . PHE   D 1 49  ? 0.873   -16.343 69.484 1.00 17.39  ? 49  PHE   D N   1 
ATOM   3520 C CA  . PHE   D 1 49  ? -0.526  -16.219 69.878 1.00 15.85  ? 49  PHE   D CA  1 
ATOM   3521 C C   . PHE   D 1 49  ? -1.173  -17.597 70.082 1.00 22.07  ? 49  PHE   D C   1 
ATOM   3522 O O   . PHE   D 1 49  ? -1.890  -17.815 71.078 1.00 16.93  ? 49  PHE   D O   1 
ATOM   3523 C CB  . PHE   D 1 49  ? -1.292  -15.398 68.844 1.00 15.62  ? 49  PHE   D CB  1 
ATOM   3524 C CG  . PHE   D 1 49  ? -2.775  -15.323 69.111 1.00 21.41  ? 49  PHE   D CG  1 
ATOM   3525 C CD1 . PHE   D 1 49  ? -3.274  -14.468 70.086 1.00 20.75  ? 49  PHE   D CD1 1 
ATOM   3526 C CD2 . PHE   D 1 49  ? -3.655  -16.120 68.411 1.00 16.28  ? 49  PHE   D CD2 1 
ATOM   3527 C CE1 . PHE   D 1 49  ? -4.633  -14.399 70.343 1.00 26.11  ? 49  PHE   D CE1 1 
ATOM   3528 C CE2 . PHE   D 1 49  ? -5.018  -16.068 68.669 1.00 27.18  ? 49  PHE   D CE2 1 
ATOM   3529 C CZ  . PHE   D 1 49  ? -5.508  -15.201 69.633 1.00 17.91  ? 49  PHE   D CZ  1 
ATOM   3530 N N   . ALA   D 1 50  ? -0.934  -18.536 69.151 1.00 15.95  ? 50  ALA   D N   1 
ATOM   3531 C CA  . ALA   D 1 50  ? -1.456  -19.896 69.288 1.00 20.86  ? 50  ALA   D CA  1 
ATOM   3532 C C   . ALA   D 1 50  ? -1.052  -20.525 70.622 1.00 17.27  ? 50  ALA   D C   1 
ATOM   3533 O O   . ALA   D 1 50  ? -1.862  -21.194 71.271 1.00 19.35  ? 50  ALA   D O   1 
ATOM   3534 C CB  . ALA   D 1 50  ? -0.963  -20.767 68.123 1.00 14.40  ? 50  ALA   D CB  1 
ATOM   3535 N N   . ALA   D 1 51  ? 0.191   -20.309 71.051 1.00 15.79  ? 51  ALA   D N   1 
ATOM   3536 C CA  . ALA   D 1 51  ? 0.664   -20.906 72.299 1.00 20.15  ? 51  ALA   D CA  1 
ATOM   3537 C C   . ALA   D 1 51  ? -0.006  -20.262 73.511 1.00 19.61  ? 51  ALA   D C   1 
ATOM   3538 O O   . ALA   D 1 51  ? -0.498  -20.960 74.418 1.00 22.54  ? 51  ALA   D O   1 
ATOM   3539 C CB  . ALA   D 1 51  ? 2.182   -20.756 72.400 1.00 17.60  ? 51  ALA   D CB  1 
ATOM   3540 N N   . GLY   D 1 52  ? -0.007  -18.928 73.566 1.00 18.48  ? 52  GLY   D N   1 
ATOM   3541 C CA  . GLY   D 1 52  ? -0.652  -18.266 74.696 1.00 16.83  ? 52  GLY   D CA  1 
ATOM   3542 C C   . GLY   D 1 52  ? -2.103  -18.697 74.842 1.00 23.72  ? 52  GLY   D C   1 
ATOM   3543 O O   . GLY   D 1 52  ? -2.584  -18.998 75.940 1.00 22.79  ? 52  GLY   D O   1 
ATOM   3544 N N   . TYR   D 1 53  ? -2.812  -18.804 73.722 1.00 20.62  ? 53  TYR   D N   1 
ATOM   3545 C CA  . TYR   D 1 53  ? -4.228  -19.136 73.814 1.00 20.67  ? 53  TYR   D CA  1 
ATOM   3546 C C   . TYR   D 1 53  ? -4.491  -20.616 74.054 1.00 22.35  ? 53  TYR   D C   1 
ATOM   3547 O O   . TYR   D 1 53  ? -5.351  -20.942 74.874 1.00 24.54  ? 53  TYR   D O   1 
ATOM   3548 C CB  . TYR   D 1 53  ? -4.975  -18.512 72.634 1.00 20.24  ? 53  TYR   D CB  1 
ATOM   3549 C CG  . TYR   D 1 53  ? -6.451  -18.787 72.460 1.00 23.61  ? 53  TYR   D CG  1 
ATOM   3550 C CD1 . TYR   D 1 53  ? -7.344  -18.515 73.481 1.00 31.27  ? 53  TYR   D CD1 1 
ATOM   3551 C CD2 . TYR   D 1 53  ? -6.980  -18.775 71.189 1.00 32.77  ? 53  TYR   D CD2 1 
ATOM   3552 C CE1 . TYR   D 1 53  ? -8.729  -18.611 73.305 1.00 34.14  ? 53  TYR   D CE1 1 
ATOM   3553 C CE2 . TYR   D 1 53  ? -8.374  -18.801 70.960 1.00 34.64  ? 53  TYR   D CE2 1 
ATOM   3554 C CZ  . TYR   D 1 53  ? -9.253  -18.715 72.042 1.00 35.50  ? 53  TYR   D CZ  1 
ATOM   3555 O OH  . TYR   D 1 53  ? -10.623 -18.751 71.860 1.00 28.24  ? 53  TYR   D OH  1 
ATOM   3556 N N   . ALA   D 1 54  ? -3.728  -21.519 73.438 1.00 17.71  ? 54  ALA   D N   1 
ATOM   3557 C CA  . ALA   D 1 54  ? -3.863  -22.932 73.800 1.00 21.59  ? 54  ALA   D CA  1 
ATOM   3558 C C   . ALA   D 1 54  ? -3.621  -23.155 75.295 1.00 25.28  ? 54  ALA   D C   1 
ATOM   3559 O O   . ALA   D 1 54  ? -4.389  -23.865 75.961 1.00 28.08  ? 54  ALA   D O   1 
ATOM   3560 C CB  . ALA   D 1 54  ? -2.896  -23.806 72.984 1.00 24.91  ? 54  ALA   D CB  1 
ATOM   3561 N N   . ALA   D 1 55  ? -2.580  -22.514 75.854 1.00 19.98  ? 55  ALA   D N   1 
ATOM   3562 C CA  . ALA   D 1 55  ? -2.236  -22.738 77.259 1.00 21.45  ? 55  ALA   D CA  1 
ATOM   3563 C C   . ALA   D 1 55  ? -3.262  -22.123 78.205 1.00 24.28  ? 55  ALA   D C   1 
ATOM   3564 O O   . ALA   D 1 55  ? -3.633  -22.742 79.217 1.00 22.85  ? 55  ALA   D O   1 
ATOM   3565 C CB  . ALA   D 1 55  ? -0.851  -22.178 77.572 1.00 14.23  ? 55  ALA   D CB  1 
ATOM   3566 N N   . CYS   D 1 56  ? -3.719  -20.896 77.920 1.00 18.84  ? 56  CYS   D N   1 
ATOM   3567 C CA  . CYS   D 1 56  ? -4.680  -20.280 78.820 1.00 19.65  ? 56  CYS   D CA  1 
ATOM   3568 C C   . CYS   D 1 56  ? -6.016  -21.013 78.768 1.00 28.05  ? 56  CYS   D C   1 
ATOM   3569 O O   . CYS   D 1 56  ? -6.673  -21.194 79.806 1.00 30.43  ? 56  CYS   D O   1 
ATOM   3570 C CB  . CYS   D 1 56  ? -4.856  -18.800 78.492 1.00 24.70  ? 56  CYS   D CB  1 
ATOM   3571 S SG  . CYS   D 1 56  ? -6.248  -17.995 79.354 1.00 40.47  ? 56  CYS   D SG  1 
ATOM   3572 N N   . PHE   D 1 57  ? -6.420  -21.475 77.575 1.00 22.79  ? 57  PHE   D N   1 
ATOM   3573 C CA  . PHE   D 1 57  ? -7.663  -22.233 77.464 1.00 28.96  ? 57  PHE   D CA  1 
ATOM   3574 C C   . PHE   D 1 57  ? -7.571  -23.562 78.200 1.00 26.87  ? 57  PHE   D C   1 
ATOM   3575 O O   . PHE   D 1 57  ? -8.522  -23.970 78.876 1.00 30.11  ? 57  PHE   D O   1 
ATOM   3576 C CB  . PHE   D 1 57  ? -8.032  -22.491 76.001 1.00 25.74  ? 57  PHE   D CB  1 
ATOM   3577 C CG  . PHE   D 1 57  ? -9.493  -22.780 75.811 1.00 34.05  ? 57  PHE   D CG  1 
ATOM   3578 C CD1 . PHE   D 1 57  ? -10.425 -21.743 75.837 1.00 28.98  ? 57  PHE   D CD1 1 
ATOM   3579 C CD2 . PHE   D 1 57  ? -9.950  -24.097 75.704 1.00 34.42  ? 57  PHE   D CD2 1 
ATOM   3580 C CE1 . PHE   D 1 57  ? -11.786 -22.007 75.691 1.00 34.11  ? 57  PHE   D CE1 1 
ATOM   3581 C CE2 . PHE   D 1 57  ? -11.307 -24.371 75.567 1.00 31.79  ? 57  PHE   D CE2 1 
ATOM   3582 C CZ  . PHE   D 1 57  ? -12.226 -23.332 75.555 1.00 33.18  ? 57  PHE   D CZ  1 
ATOM   3583 N N   . GLY   D 1 58  ? -6.457  -24.284 78.036 1.00 25.71  ? 58  GLY   D N   1 
ATOM   3584 C CA  . GLY   D 1 58  ? -6.281  -25.512 78.794 1.00 29.81  ? 58  GLY   D CA  1 
ATOM   3585 C C   . GLY   D 1 58  ? -6.314  -25.270 80.290 1.00 31.75  ? 58  GLY   D C   1 
ATOM   3586 O O   . GLY   D 1 58  ? -6.917  -26.038 81.046 1.00 33.84  ? 58  GLY   D O   1 
ATOM   3587 N N   . ASN   D 1 59  ? -5.678  -24.184 80.738 1.00 23.74  ? 59  ASN   D N   1 
ATOM   3588 C CA  . ASN   D 1 59  ? -5.713  -23.859 82.156 1.00 27.14  ? 59  ASN   D CA  1 
ATOM   3589 C C   . ASN   D 1 59  ? -7.143  -23.668 82.637 1.00 42.94  ? 59  ASN   D C   1 
ATOM   3590 O O   . ASN   D 1 59  ? -7.542  -24.209 83.680 1.00 34.46  ? 59  ASN   D O   1 
ATOM   3591 C CB  . ASN   D 1 59  ? -4.900  -22.602 82.438 1.00 29.56  ? 59  ASN   D CB  1 
ATOM   3592 C CG  . ASN   D 1 59  ? -4.640  -22.415 83.914 1.00 37.74  ? 59  ASN   D CG  1 
ATOM   3593 O OD1 . ASN   D 1 59  ? -3.747  -23.051 84.463 1.00 27.71  ? 59  ASN   D OD1 1 
ATOM   3594 N ND2 . ASN   D 1 59  ? -5.425  -21.565 84.568 1.00 28.25  ? 59  ASN   D ND2 1 
ATOM   3595 N N   . ALA   D 1 60  ? -7.930  -22.876 81.895 1.00 33.16  ? 60  ALA   D N   1 
ATOM   3596 C CA  . ALA   D 1 60  ? -9.293  -22.607 82.334 1.00 37.75  ? 60  ALA   D CA  1 
ATOM   3597 C C   . ALA   D 1 60  ? -10.165 -23.851 82.232 1.00 38.92  ? 60  ALA   D C   1 
ATOM   3598 O O   . ALA   D 1 60  ? -11.117 -24.005 83.002 1.00 38.61  ? 60  ALA   D O   1 
ATOM   3599 C CB  . ALA   D 1 60  ? -9.900  -21.453 81.534 1.00 35.37  ? 60  ALA   D CB  1 
ATOM   3600 N N   . VAL   D 1 61  ? -9.858  -24.751 81.299 1.00 33.54  ? 61  VAL   D N   1 
ATOM   3601 C CA  . VAL   D 1 61  ? -10.564 -26.024 81.262 1.00 37.24  ? 61  VAL   D CA  1 
ATOM   3602 C C   . VAL   D 1 61  ? -10.284 -26.807 82.541 1.00 44.14  ? 61  VAL   D C   1 
ATOM   3603 O O   . VAL   D 1 61  ? -11.194 -27.395 83.136 1.00 41.51  ? 61  VAL   D O   1 
ATOM   3604 C CB  . VAL   D 1 61  ? -10.181 -26.813 79.996 1.00 33.23  ? 61  VAL   D CB  1 
ATOM   3605 C CG1 . VAL   D 1 61  ? -10.616 -28.256 80.112 1.00 39.52  ? 61  VAL   D CG1 1 
ATOM   3606 C CG2 . VAL   D 1 61  ? -10.803 -26.165 78.776 1.00 35.76  ? 61  VAL   D CG2 1 
ATOM   3607 N N   . ILE   D 1 62  ? -9.029  -26.788 83.007 1.00 36.47  ? 62  ILE   D N   1 
ATOM   3608 C CA  . ILE   D 1 62  ? -8.703  -27.409 84.293 1.00 43.80  ? 62  ILE   D CA  1 
ATOM   3609 C C   . ILE   D 1 62  ? -9.493  -26.755 85.427 1.00 45.55  ? 62  ILE   D C   1 
ATOM   3610 O O   . ILE   D 1 62  ? -10.028 -27.435 86.310 1.00 55.96  ? 62  ILE   D O   1 
ATOM   3611 C CB  . ILE   D 1 62  ? -7.187  -27.346 84.563 1.00 38.76  ? 62  ILE   D CB  1 
ATOM   3612 C CG1 . ILE   D 1 62  ? -6.426  -28.216 83.562 1.00 38.66  ? 62  ILE   D CG1 1 
ATOM   3613 C CG2 . ILE   D 1 62  ? -6.869  -27.780 85.999 1.00 44.02  ? 62  ILE   D CG2 1 
ATOM   3614 C CD1 . ILE   D 1 62  ? -4.997  -27.790 83.339 1.00 28.04  ? 62  ILE   D CD1 1 
ATOM   3615 N N   . HIS   D 1 63  ? -9.551  -25.425 85.431 1.00 41.25  ? 63  HIS   D N   1 
ATOM   3616 C CA  . HIS   D 1 63  ? -10.248 -24.692 86.491 1.00 45.88  ? 63  HIS   D CA  1 
ATOM   3617 C C   . HIS   D 1 63  ? -11.741 -25.018 86.524 1.00 52.60  ? 63  HIS   D C   1 
ATOM   3618 O O   . HIS   D 1 63  ? -12.333 -25.176 87.599 1.00 58.33  ? 63  HIS   D O   1 
ATOM   3619 C CB  . HIS   D 1 63  ? -10.031 -23.196 86.289 1.00 46.93  ? 63  HIS   D CB  1 
ATOM   3620 C CG  . HIS   D 1 63  ? -10.516 -22.340 87.416 1.00 52.47  ? 63  HIS   D CG  1 
ATOM   3621 N ND1 . HIS   D 1 63  ? -10.346 -22.678 88.742 1.00 56.38  ? 63  HIS   D ND1 1 
ATOM   3622 C CD2 . HIS   D 1 63  ? -11.124 -21.129 87.413 1.00 58.14  ? 63  HIS   D CD2 1 
ATOM   3623 C CE1 . HIS   D 1 63  ? -10.862 -21.731 89.506 1.00 56.30  ? 63  HIS   D CE1 1 
ATOM   3624 N NE2 . HIS   D 1 63  ? -11.337 -20.777 88.724 1.00 62.47  ? 63  HIS   D NE2 1 
ATOM   3625 N N   . VAL   D 1 64  ? -12.368 -25.113 85.350 1.00 51.91  ? 64  VAL   D N   1 
ATOM   3626 C CA  . VAL   D 1 64  ? -13.805 -25.373 85.268 1.00 54.39  ? 64  VAL   D CA  1 
ATOM   3627 C C   . VAL   D 1 64  ? -14.112 -26.815 85.648 1.00 60.07  ? 64  VAL   D C   1 
ATOM   3628 O O   . VAL   D 1 64  ? -15.103 -27.094 86.333 1.00 64.99  ? 64  VAL   D O   1 
ATOM   3629 C CB  . VAL   D 1 64  ? -14.332 -25.041 83.858 1.00 49.49  ? 64  VAL   D CB  1 
ATOM   3630 C CG1 . VAL   D 1 64  ? -15.684 -25.707 83.603 1.00 51.59  ? 64  VAL   D CG1 1 
ATOM   3631 C CG2 . VAL   D 1 64  ? -14.432 -23.540 83.670 1.00 43.95  ? 64  VAL   D CG2 1 
ATOM   3632 N N   . THR   D 1 65  ? -13.280 -27.756 85.190 1.00 59.72  ? 65  THR   D N   1 
ATOM   3633 C CA  . THR   D 1 65  ? -13.464 -29.157 85.559 1.00 60.31  ? 65  THR   D CA  1 
ATOM   3634 C C   . THR   D 1 65  ? -13.339 -29.351 87.067 1.00 68.51  ? 65  THR   D C   1 
ATOM   3635 O O   . THR   D 1 65  ? -14.249 -29.882 87.718 1.00 70.30  ? 65  THR   D O   1 
ATOM   3636 C CB  . THR   D 1 65  ? -12.458 -30.027 84.813 1.00 57.51  ? 65  THR   D CB  1 
ATOM   3637 O OG1 . THR   D 1 65  ? -12.689 -29.910 83.406 1.00 51.85  ? 65  THR   D OG1 1 
ATOM   3638 C CG2 . THR   D 1 65  ? -12.578 -31.485 85.235 1.00 57.06  ? 65  THR   D CG2 1 
ATOM   3639 N N   . ARG   D 1 66  ? -12.214 -28.932 87.640 1.00 68.62  ? 66  ARG   D N   1 
ATOM   3640 C CA  . ARG   D 1 66  ? -12.103 -28.863 89.087 1.00 71.92  ? 66  ARG   D CA  1 
ATOM   3641 C C   . ARG   D 1 66  ? -13.085 -27.823 89.617 1.00 83.38  ? 66  ARG   D C   1 
ATOM   3642 O O   . ARG   D 1 66  ? -13.765 -27.123 88.858 1.00 86.57  ? 66  ARG   D O   1 
ATOM   3643 C CB  . ARG   D 1 66  ? -10.671 -28.535 89.491 1.00 63.83  ? 66  ARG   D CB  1 
ATOM   3644 C CG  . ARG   D 1 66  ? -9.680  -29.597 89.080 1.00 60.77  ? 66  ARG   D CG  1 
ATOM   3645 C CD  . ARG   D 1 66  ? -8.261  -29.127 89.302 1.00 57.07  ? 66  ARG   D CD  1 
ATOM   3646 N NE  . ARG   D 1 66  ? -7.303  -30.095 88.784 1.00 53.24  ? 66  ARG   D NE  1 
ATOM   3647 C CZ  . ARG   D 1 66  ? -5.990  -29.903 88.762 1.00 48.86  ? 66  ARG   D CZ  1 
ATOM   3648 N NH1 . ARG   D 1 66  ? -5.479  -28.770 89.230 1.00 45.36  ? 66  ARG   D NH1 1 
ATOM   3649 N NH2 . ARG   D 1 66  ? -5.192  -30.840 88.264 1.00 53.24  ? 66  ARG   D NH2 1 
ATOM   3650 N N   . SER   D 1 67  ? -13.163 -27.727 90.942 1.00 91.46  ? 67  SER   D N   1 
ATOM   3651 C CA  . SER   D 1 67  ? -14.170 -26.898 91.609 1.00 95.37  ? 67  SER   D CA  1 
ATOM   3652 C C   . SER   D 1 67  ? -15.580 -27.129 91.037 1.00 96.98  ? 67  SER   D C   1 
ATOM   3653 O O   . SER   D 1 67  ? -16.461 -26.275 91.174 1.00 96.48  ? 67  SER   D O   1 
ATOM   3654 C CB  . SER   D 1 67  ? -13.775 -25.404 91.582 1.00 93.46  ? 67  SER   D CB  1 
ATOM   3655 O OG  . SER   D 1 67  ? -13.885 -24.832 90.292 1.00 86.03  ? 67  SER   D OG  1 
ATOM   3656 N N   . ASN   D 1 68  ? -15.800 -28.284 90.382 1.00 93.63  ? 68  ASN   D N   1 
ATOM   3657 C CA  . ASN   D 1 68  ? -17.136 -28.841 90.195 1.00 94.01  ? 68  ASN   D CA  1 
ATOM   3658 C C   . ASN   D 1 68  ? -17.370 -30.147 90.940 1.00 95.60  ? 68  ASN   D C   1 
ATOM   3659 O O   . ASN   D 1 68  ? -18.527 -30.479 91.203 1.00 97.60  ? 68  ASN   D O   1 
ATOM   3660 C CB  . ASN   D 1 68  ? -17.482 -29.100 88.724 1.00 94.89  ? 68  ASN   D CB  1 
ATOM   3661 C CG  . ASN   D 1 68  ? -17.747 -27.832 87.923 1.00 92.25  ? 68  ASN   D CG  1 
ATOM   3662 O OD1 . ASN   D 1 68  ? -18.362 -26.883 88.396 1.00 90.59  ? 68  ASN   D OD1 1 
ATOM   3663 N ND2 . ASN   D 1 68  ? -17.328 -27.856 86.659 1.00 86.60  ? 68  ASN   D ND2 1 
ATOM   3664 N N   . LYS   D 1 69  ? -16.324 -30.925 91.233 1.00 91.59  ? 69  LYS   D N   1 
ATOM   3665 C CA  . LYS   D 1 69  ? -16.328 -32.068 92.164 1.00 90.32  ? 69  LYS   D CA  1 
ATOM   3666 C C   . LYS   D 1 69  ? -16.891 -33.355 91.551 1.00 86.98  ? 69  LYS   D C   1 
ATOM   3667 O O   . LYS   D 1 69  ? -16.646 -34.441 92.100 1.00 81.99  ? 69  LYS   D O   1 
ATOM   3668 C CB  . LYS   D 1 69  ? -17.081 -31.724 93.459 1.00 91.09  ? 69  LYS   D CB  1 
ATOM   3669 C CG  . LYS   D 1 69  ? -16.476 -30.510 94.203 1.00 92.00  ? 69  LYS   D CG  1 
ATOM   3670 C CD  . LYS   D 1 69  ? -17.547 -29.507 94.646 1.00 91.22  ? 69  LYS   D CD  1 
ATOM   3671 C CE  . LYS   D 1 69  ? -16.954 -28.203 95.197 1.00 92.78  ? 69  LYS   D CE  1 
ATOM   3672 N NZ  . LYS   D 1 69  ? -17.935 -27.073 95.168 1.00 90.57  ? 69  LYS   D NZ  1 
ATOM   3673 N N   . GLU   D 1 70  ? -17.647 -33.269 90.445 1.00 88.15  ? 70  GLU   D N   1 
ATOM   3674 C CA  . GLU   D 1 70  ? -17.702 -34.364 89.461 1.00 87.26  ? 70  GLU   D CA  1 
ATOM   3675 C C   . GLU   D 1 70  ? -16.394 -35.159 89.297 1.00 91.13  ? 70  GLU   D C   1 
ATOM   3676 O O   . GLU   D 1 70  ? -16.384 -36.383 89.512 1.00 90.16  ? 70  GLU   D O   1 
ATOM   3677 C CB  . GLU   D 1 70  ? -18.274 -33.871 88.110 1.00 84.46  ? 70  GLU   D CB  1 
ATOM   3678 C CG  . GLU   D 1 70  ? -17.734 -32.601 87.482 1.00 90.98  ? 70  GLU   D CG  1 
ATOM   3679 C CD  . GLU   D 1 70  ? -18.317 -32.354 86.091 1.00 90.31  ? 70  GLU   D CD  1 
ATOM   3680 O OE1 . GLU   D 1 70  ? -18.956 -33.308 85.539 1.00 86.22  ? 70  GLU   D OE1 1 
ATOM   3681 O OE2 . GLU   D 1 70  ? -18.393 -31.083 85.806 1.00 84.38  ? 70  GLU   D OE2 1 
ATOM   3682 N N   . TYR   D 1 71  ? -15.288 -34.538 88.919 1.00 93.15  ? 71  TYR   D N   1 
ATOM   3683 C CA  . TYR   D 1 71  ? -14.190 -35.395 88.493 1.00 93.00  ? 71  TYR   D CA  1 
ATOM   3684 C C   . TYR   D 1 71  ? -12.883 -35.131 89.223 1.00 90.90  ? 71  TYR   D C   1 
ATOM   3685 O O   . TYR   D 1 71  ? -12.775 -34.289 90.118 1.00 81.92  ? 71  TYR   D O   1 
ATOM   3686 C CB  . TYR   D 1 71  ? -13.938 -35.308 86.984 1.00 96.69  ? 71  TYR   D CB  1 
ATOM   3687 C CG  . TYR   D 1 71  ? -14.994 -35.925 86.077 1.00 101.99 ? 71  TYR   D CG  1 
ATOM   3688 C CD1 . TYR   D 1 71  ? -15.021 -37.305 85.801 1.00 102.79 ? 71  TYR   D CD1 1 
ATOM   3689 C CD2 . TYR   D 1 71  ? -15.963 -35.124 85.490 1.00 102.97 ? 71  TYR   D CD2 1 
ATOM   3690 C CE1 . TYR   D 1 71  ? -15.991 -37.851 84.933 1.00 102.66 ? 71  TYR   D CE1 1 
ATOM   3691 C CE2 . TYR   D 1 71  ? -16.916 -35.654 84.645 1.00 104.12 ? 71  TYR   D CE2 1 
ATOM   3692 C CZ  . TYR   D 1 71  ? -16.937 -37.008 84.364 1.00 102.35 ? 71  TYR   D CZ  1 
ATOM   3693 O OH  . TYR   D 1 71  ? -17.930 -37.454 83.509 1.00 98.24  ? 71  TYR   D OH  1 
ATOM   3694 N N   . LYS   D 1 72  ? -11.911 -35.961 88.857 1.00 95.14  ? 72  LYS   D N   1 
ATOM   3695 C CA  . LYS   D 1 72  ? -10.660 -36.191 89.566 1.00 93.45  ? 72  LYS   D CA  1 
ATOM   3696 C C   . LYS   D 1 72  ? -9.500  -36.101 88.569 1.00 89.26  ? 72  LYS   D C   1 
ATOM   3697 O O   . LYS   D 1 72  ? -8.856  -37.105 88.236 1.00 89.16  ? 72  LYS   D O   1 
ATOM   3698 C CB  . LYS   D 1 72  ? -10.716 -37.577 90.305 1.00 96.63  ? 72  LYS   D CB  1 
ATOM   3699 C CG  . LYS   D 1 72  ? -11.369 -37.460 91.663 1.00 101.24 ? 72  LYS   D CG  1 
ATOM   3700 C CD  . LYS   D 1 72  ? -12.867 -37.351 91.562 1.00 99.33  ? 72  LYS   D CD  1 
ATOM   3701 C CE  . LYS   D 1 72  ? -13.568 -37.340 92.912 1.00 94.22  ? 72  LYS   D CE  1 
ATOM   3702 N NZ  . LYS   D 1 72  ? -14.983 -37.192 92.643 1.00 91.98  ? 72  LYS   D NZ  1 
ATOM   3703 N N   . ILE   D 1 73  ? -9.149  -34.875 88.177 1.00 82.74  ? 73  ILE   D N   1 
ATOM   3704 C CA  . ILE   D 1 73  ? -8.351  -34.654 86.979 1.00 78.30  ? 73  ILE   D CA  1 
ATOM   3705 C C   . ILE   D 1 73  ? -7.024  -33.992 87.351 1.00 70.94  ? 73  ILE   D C   1 
ATOM   3706 O O   . ILE   D 1 73  ? -6.962  -33.148 88.257 1.00 66.58  ? 73  ILE   D O   1 
ATOM   3707 C CB  . ILE   D 1 73  ? -9.139  -33.833 85.937 1.00 76.38  ? 73  ILE   D CB  1 
ATOM   3708 C CG1 . ILE   D 1 73  ? -8.552  -34.161 84.573 1.00 78.86  ? 73  ILE   D CG1 1 
ATOM   3709 C CG2 . ILE   D 1 73  ? -9.049  -32.314 86.224 1.00 70.55  ? 73  ILE   D CG2 1 
ATOM   3710 C CD1 . ILE   D 1 73  ? -8.603  -35.662 84.359 1.00 78.84  ? 73  ILE   D CD1 1 
ATOM   3711 N N   . ARG   D 1 74  ? -5.951  -34.411 86.677 1.00 63.98  ? 74  ARG   D N   1 
ATOM   3712 C CA  . ARG   D 1 74  ? -4.621  -33.887 86.943 1.00 59.72  ? 74  ARG   D CA  1 
ATOM   3713 C C   . ARG   D 1 74  ? -4.256  -32.990 85.766 1.00 55.69  ? 74  ARG   D C   1 
ATOM   3714 O O   . ARG   D 1 74  ? -4.789  -33.151 84.659 1.00 49.46  ? 74  ARG   D O   1 
ATOM   3715 C CB  . ARG   D 1 74  ? -3.594  -35.020 87.083 1.00 63.41  ? 74  ARG   D CB  1 
ATOM   3716 C CG  . ARG   D 1 74  ? -3.196  -35.722 85.786 1.00 65.86  ? 74  ARG   D CG  1 
ATOM   3717 C CD  . ARG   D 1 74  ? -2.238  -36.876 86.088 1.00 76.05  ? 74  ARG   D CD  1 
ATOM   3718 N NE  . ARG   D 1 74  ? -2.945  -37.984 86.729 1.00 82.10  ? 74  ARG   D NE  1 
ATOM   3719 C CZ  . ARG   D 1 74  ? -3.496  -38.975 86.029 1.00 82.87  ? 74  ARG   D CZ  1 
ATOM   3720 N NH1 . ARG   D 1 74  ? -3.336  -39.004 84.713 1.00 78.96  ? 74  ARG   D NH1 1 
ATOM   3721 N NH2 . ARG   D 1 74  ? -4.161  -39.952 86.627 1.00 84.20  ? 74  ARG   D NH2 1 
ATOM   3722 N N   . ASP   D 1 75  ? -3.350  -32.045 86.011 1.00 48.41  ? 75  ASP   D N   1 
ATOM   3723 C CA  . ASP   D 1 75  ? -2.991  -31.063 84.994 1.00 45.75  ? 75  ASP   D CA  1 
ATOM   3724 C C   . ASP   D 1 75  ? -2.738  -31.673 83.610 1.00 42.15  ? 75  ASP   D C   1 
ATOM   3725 O O   . ASP   D 1 75  ? -3.313  -31.195 82.629 1.00 34.31  ? 75  ASP   D O   1 
ATOM   3726 C CB  . ASP   D 1 75  ? -1.780  -30.240 85.464 1.00 40.31  ? 75  ASP   D CB  1 
ATOM   3727 C CG  . ASP   D 1 75  ? -2.137  -29.219 86.555 1.00 47.02  ? 75  ASP   D CG  1 
ATOM   3728 O OD1 . ASP   D 1 75  ? -3.325  -29.150 86.961 1.00 39.72  ? 75  ASP   D OD1 1 
ATOM   3729 O OD2 . ASP   D 1 75  ? -1.238  -28.445 86.977 1.00 42.63  ? 75  ASP   D OD2 1 
ATOM   3730 N N   . ASN   D 1 76  ? -1.919  -32.722 83.494 1.00 39.95  ? 76  ASN   D N   1 
ATOM   3731 C CA  . ASN   D 1 76  ? -1.571  -33.175 82.152 1.00 42.93  ? 76  ASN   D CA  1 
ATOM   3732 C C   . ASN   D 1 76  ? -2.661  -33.979 81.473 1.00 40.81  ? 76  ASN   D C   1 
ATOM   3733 O O   . ASN   D 1 76  ? -2.429  -34.470 80.364 1.00 37.64  ? 76  ASN   D O   1 
ATOM   3734 C CB  . ASN   D 1 76  ? -0.306  -34.020 82.100 1.00 49.15  ? 76  ASN   D CB  1 
ATOM   3735 C CG  . ASN   D 1 76  ? 0.960   -33.232 82.316 1.00 49.42  ? 76  ASN   D CG  1 
ATOM   3736 O OD1 . ASN   D 1 76  ? 1.132   -32.117 81.842 1.00 52.24  ? 76  ASN   D OD1 1 
ATOM   3737 N ND2 . ASN   D 1 76  ? 1.885   -33.859 83.038 1.00 60.02  ? 76  ASN   D ND2 1 
ATOM   3738 N N   . ASP   D 1 77  ? -3.828  -34.145 82.075 1.00 42.08  ? 77  ASP   D N   1 
ATOM   3739 C CA  . ASP   D 1 77  ? -4.855  -34.824 81.301 1.00 43.42  ? 77  ASP   D CA  1 
ATOM   3740 C C   . ASP   D 1 77  ? -5.503  -33.924 80.251 1.00 46.20  ? 77  ASP   D C   1 
ATOM   3741 O O   . ASP   D 1 77  ? -6.200  -34.439 79.366 1.00 49.51  ? 77  ASP   D O   1 
ATOM   3742 C CB  . ASP   D 1 77  ? -5.907  -35.392 82.240 1.00 49.94  ? 77  ASP   D CB  1 
ATOM   3743 C CG  . ASP   D 1 77  ? -5.419  -36.630 82.973 1.00 55.60  ? 77  ASP   D CG  1 
ATOM   3744 O OD1 . ASP   D 1 77  ? -4.763  -37.488 82.332 1.00 48.15  ? 77  ASP   D OD1 1 
ATOM   3745 O OD2 . ASP   D 1 77  ? -5.675  -36.717 84.197 1.00 53.19  ? 77  ASP   D OD2 1 
ATOM   3746 N N   . VAL   D 1 78  ? -5.261  -32.612 80.312 1.00 34.23  ? 78  VAL   D N   1 
ATOM   3747 C CA  . VAL   D 1 78  ? -5.876  -31.624 79.422 1.00 41.51  ? 78  VAL   D CA  1 
ATOM   3748 C C   . VAL   D 1 78  ? -4.855  -31.207 78.365 1.00 34.09  ? 78  VAL   D C   1 
ATOM   3749 O O   . VAL   D 1 78  ? -3.789  -30.672 78.704 1.00 31.88  ? 78  VAL   D O   1 
ATOM   3750 C CB  . VAL   D 1 78  ? -6.366  -30.397 80.214 1.00 36.66  ? 78  VAL   D CB  1 
ATOM   3751 C CG1 . VAL   D 1 78  ? -7.080  -29.406 79.303 1.00 37.76  ? 78  VAL   D CG1 1 
ATOM   3752 C CG2 . VAL   D 1 78  ? -7.262  -30.805 81.345 1.00 39.93  ? 78  VAL   D CG2 1 
ATOM   3753 N N   . GLU   D 1 79  ? -5.178  -31.427 77.085 1.00 32.84  ? 79  GLU   D N   1 
ATOM   3754 C CA  . GLU   D 1 79  ? -4.406  -30.842 75.988 1.00 37.33  ? 79  GLU   D CA  1 
ATOM   3755 C C   . GLU   D 1 79  ? -5.272  -29.915 75.146 1.00 35.07  ? 79  GLU   D C   1 
ATOM   3756 O O   . GLU   D 1 79  ? -6.463  -30.177 74.927 1.00 37.14  ? 79  GLU   D O   1 
ATOM   3757 C CB  . GLU   D 1 79  ? -3.799  -31.879 75.024 1.00 37.06  ? 79  GLU   D CB  1 
ATOM   3758 C CG  . GLU   D 1 79  ? -2.710  -32.800 75.550 1.00 50.12  ? 79  GLU   D CG  1 
ATOM   3759 C CD  . GLU   D 1 79  ? -2.247  -33.747 74.464 1.00 57.95  ? 79  GLU   D CD  1 
ATOM   3760 O OE1 . GLU   D 1 79  ? -2.851  -33.709 73.358 1.00 64.05  ? 79  GLU   D OE1 1 
ATOM   3761 O OE2 . GLU   D 1 79  ? -1.364  -34.597 74.744 1.00 59.94  ? 79  GLU   D OE2 1 
ATOM   3762 N N   . VAL   D 1 80  ? -4.644  -28.865 74.621 1.00 31.21  ? 80  VAL   D N   1 
ATOM   3763 C CA  . VAL   D 1 80  ? -5.268  -27.973 73.648 1.00 31.26  ? 80  VAL   D CA  1 
ATOM   3764 C C   . VAL   D 1 80  ? -4.317  -27.808 72.473 1.00 28.13  ? 80  VAL   D C   1 
ATOM   3765 O O   . VAL   D 1 80  ? -3.180  -27.353 72.641 1.00 35.02  ? 80  VAL   D O   1 
ATOM   3766 C CB  . VAL   D 1 80  ? -5.634  -26.613 74.254 1.00 29.97  ? 80  VAL   D CB  1 
ATOM   3767 C CG1 . VAL   D 1 80  ? -6.248  -25.713 73.190 1.00 21.57  ? 80  VAL   D CG1 1 
ATOM   3768 C CG2 . VAL   D 1 80  ? -6.635  -26.819 75.386 1.00 33.41  ? 80  VAL   D CG2 1 
ATOM   3769 N N   . LEU   D 1 81  ? -4.770  -28.199 71.301 1.00 29.20  ? 81  LEU   D N   1 
ATOM   3770 C CA  . LEU   D 1 81  ? -4.031  -28.025 70.066 1.00 31.58  ? 81  LEU   D CA  1 
ATOM   3771 C C   . LEU   D 1 81  ? -4.634  -26.814 69.369 1.00 31.81  ? 81  LEU   D C   1 
ATOM   3772 O O   . LEU   D 1 81  ? -5.776  -26.864 68.900 1.00 31.19  ? 81  LEU   D O   1 
ATOM   3773 C CB  . LEU   D 1 81  ? -4.116  -29.276 69.202 1.00 26.97  ? 81  LEU   D CB  1 
ATOM   3774 C CG  . LEU   D 1 81  ? -3.281  -29.189 67.936 1.00 34.67  ? 81  LEU   D CG  1 
ATOM   3775 C CD1 . LEU   D 1 81  ? -1.804  -29.386 68.246 1.00 33.97  ? 81  LEU   D CD1 1 
ATOM   3776 C CD2 . LEU   D 1 81  ? -3.787  -30.217 66.943 1.00 36.06  ? 81  LEU   D CD2 1 
ATOM   3777 N N   A SER   D 1 82  ? -3.867  -25.733 69.326 0.50 29.60  ? 82  SER   D N   1 
ATOM   3778 N N   B SER   D 1 82  ? -3.873  -25.724 69.327 0.50 29.58  ? 82  SER   D N   1 
ATOM   3779 C CA  A SER   D 1 82  ? -4.306  -24.486 68.711 0.50 27.52  ? 82  SER   D CA  1 
ATOM   3780 C CA  B SER   D 1 82  ? -4.322  -24.483 68.706 0.50 27.68  ? 82  SER   D CA  1 
ATOM   3781 C C   A SER   D 1 82  ? -3.803  -24.414 67.274 0.50 28.15  ? 82  SER   D C   1 
ATOM   3782 C C   B SER   D 1 82  ? -3.813  -24.420 67.272 0.50 28.24  ? 82  SER   D C   1 
ATOM   3783 O O   A SER   D 1 82  ? -2.590  -24.498 67.037 0.50 27.48  ? 82  SER   D O   1 
ATOM   3784 O O   B SER   D 1 82  ? -2.603  -24.521 67.038 0.50 27.26  ? 82  SER   D O   1 
ATOM   3785 C CB  A SER   D 1 82  ? -3.777  -23.298 69.512 0.50 23.56  ? 82  SER   D CB  1 
ATOM   3786 C CB  B SER   D 1 82  ? -3.807  -23.280 69.493 0.50 23.56  ? 82  SER   D CB  1 
ATOM   3787 O OG  A SER   D 1 82  ? -4.127  -22.080 68.903 0.50 32.65  ? 82  SER   D OG  1 
ATOM   3788 O OG  B SER   D 1 82  ? -2.386  -23.237 69.455 0.50 32.65  ? 82  SER   D OG  1 
ATOM   3789 N N   . THR   D 1 83  ? -4.726  -24.235 66.320 1.00 24.34  ? 83  THR   D N   1 
ATOM   3790 C CA  . THR   D 1 83  ? -4.383  -23.880 64.937 1.00 27.44  ? 83  THR   D CA  1 
ATOM   3791 C C   . THR   D 1 83  ? -4.723  -22.409 64.703 1.00 26.47  ? 83  THR   D C   1 
ATOM   3792 O O   . THR   D 1 83  ? -5.887  -22.019 64.836 1.00 21.95  ? 83  THR   D O   1 
ATOM   3793 C CB  . THR   D 1 83  ? -5.134  -24.748 63.913 1.00 25.50  ? 83  THR   D CB  1 
ATOM   3794 O OG1 . THR   D 1 83  ? -4.862  -26.128 64.152 1.00 27.63  ? 83  THR   D OG1 1 
ATOM   3795 C CG2 . THR   D 1 83  ? -4.702  -24.400 62.471 1.00 20.83  ? 83  THR   D CG2 1 
ATOM   3796 N N   . VAL   D 1 84  ? -3.718  -21.602 64.361 1.00 22.13  ? 84  VAL   D N   1 
ATOM   3797 C CA  . VAL   D 1 84  ? -3.902  -20.180 64.097 1.00 20.49  ? 84  VAL   D CA  1 
ATOM   3798 C C   . VAL   D 1 84  ? -3.418  -19.882 62.681 1.00 23.46  ? 84  VAL   D C   1 
ATOM   3799 O O   . VAL   D 1 84  ? -2.301  -20.254 62.307 1.00 21.46  ? 84  VAL   D O   1 
ATOM   3800 C CB  . VAL   D 1 84  ? -3.173  -19.300 65.129 1.00 17.39  ? 84  VAL   D CB  1 
ATOM   3801 C CG1 . VAL   D 1 84  ? -3.300  -17.813 64.748 1.00 16.81  ? 84  VAL   D CG1 1 
ATOM   3802 C CG2 . VAL   D 1 84  ? -3.765  -19.482 66.505 1.00 20.31  ? 84  VAL   D CG2 1 
ATOM   3803 N N   . GLY   D 1 85  ? -4.265  -19.238 61.897 1.00 17.42  ? 85  GLY   D N   1 
ATOM   3804 C CA  . GLY   D 1 85  ? -3.882  -18.829 60.569 1.00 17.37  ? 85  GLY   D CA  1 
ATOM   3805 C C   . GLY   D 1 85  ? -4.040  -17.341 60.335 1.00 27.45  ? 85  GLY   D C   1 
ATOM   3806 O O   . GLY   D 1 85  ? -4.799  -16.670 61.048 1.00 25.54  ? 85  GLY   D O   1 
ATOM   3807 N N   . ILE   D 1 86  ? -3.330  -16.810 59.335 1.00 25.63  ? 86  ILE   D N   1 
ATOM   3808 C CA  . ILE   D 1 86  ? -3.399  -15.400 58.969 1.00 23.29  ? 86  ILE   D CA  1 
ATOM   3809 C C   . ILE   D 1 86  ? -3.877  -15.320 57.524 1.00 36.89  ? 86  ILE   D C   1 
ATOM   3810 O O   . ILE   D 1 86  ? -3.365  -16.037 56.653 1.00 28.18  ? 86  ILE   D O   1 
ATOM   3811 C CB  . ILE   D 1 86  ? -2.051  -14.676 59.187 1.00 23.10  ? 86  ILE   D CB  1 
ATOM   3812 C CG1 . ILE   D 1 86  ? -2.153  -13.190 58.832 1.00 22.13  ? 86  ILE   D CG1 1 
ATOM   3813 C CG2 . ILE   D 1 86  ? -0.904  -15.320 58.421 1.00 27.51  ? 86  ILE   D CG2 1 
ATOM   3814 C CD1 . ILE   D 1 86  ? -0.924  -12.376 59.277 1.00 24.79  ? 86  ILE   D CD1 1 
ATOM   3815 N N   . VAL   D 1 87  ? -4.894  -14.488 57.286 1.00 26.64  ? 87  VAL   D N   1 
ATOM   3816 C CA  . VAL   D 1 87  ? -5.543  -14.361 55.987 1.00 36.59  ? 87  VAL   D CA  1 
ATOM   3817 C C   . VAL   D 1 87  ? -5.764  -12.878 55.710 1.00 34.21  ? 87  VAL   D C   1 
ATOM   3818 O O   . VAL   D 1 87  ? -5.934  -12.088 56.641 1.00 32.78  ? 87  VAL   D O   1 
ATOM   3819 C CB  . VAL   D 1 87  ? -6.874  -15.153 55.949 1.00 39.46  ? 87  VAL   D CB  1 
ATOM   3820 C CG1 . VAL   D 1 87  ? -7.844  -14.690 57.060 1.00 28.53  ? 87  VAL   D CG1 1 
ATOM   3821 C CG2 . VAL   D 1 87  ? -7.516  -15.039 54.581 1.00 45.01  ? 87  VAL   D CG2 1 
ATOM   3822 N N   . ALA   D 1 88  ? -5.715  -12.480 54.441 1.00 34.52  ? 88  ALA   D N   1 
ATOM   3823 C CA  . ALA   D 1 88  ? -6.066  -11.100 54.125 1.00 37.90  ? 88  ALA   D CA  1 
ATOM   3824 C C   . ALA   D 1 88  ? -7.556  -10.878 54.379 1.00 37.51  ? 88  ALA   D C   1 
ATOM   3825 O O   . ALA   D 1 88  ? -8.393  -11.714 54.017 1.00 39.60  ? 88  ALA   D O   1 
ATOM   3826 C CB  . ALA   D 1 88  ? -5.702  -10.769 52.671 1.00 37.61  ? 88  ALA   D CB  1 
ATOM   3827 N N   . ASN   D 1 89  ? -7.888  -9.774  55.045 1.00 34.55  ? 89  ASN   D N   1 
ATOM   3828 C CA  . ASN   D 1 89  ? -9.286  -9.380  55.129 1.00 37.27  ? 89  ASN   D CA  1 
ATOM   3829 C C   . ASN   D 1 89  ? -9.610  -8.587  53.863 1.00 43.46  ? 89  ASN   D C   1 
ATOM   3830 O O   . ASN   D 1 89  ? -8.719  -8.248  53.079 1.00 50.83  ? 89  ASN   D O   1 
ATOM   3831 C CB  . ASN   D 1 89  ? -9.573  -8.622  56.454 1.00 27.41  ? 89  ASN   D CB  1 
ATOM   3832 C CG  . ASN   D 1 89  ? -8.931  -7.209  56.544 1.00 31.16  ? 89  ASN   D CG  1 
ATOM   3833 O OD1 . ASN   D 1 89  ? -8.652  -6.564  55.549 1.00 30.57  ? 89  ASN   D OD1 1 
ATOM   3834 N ND2 . ASN   D 1 89  ? -8.698  -6.746  57.768 1.00 25.04  ? 89  ASN   D ND2 1 
ATOM   3835 N N   . GLY   D 1 90  ? -10.883 -8.325  53.624 1.00 42.13  ? 90  GLY   D N   1 
ATOM   3836 C CA  . GLY   D 1 90  ? -11.106 -7.676  52.342 1.00 44.40  ? 90  GLY   D CA  1 
ATOM   3837 C C   . GLY   D 1 90  ? -10.679 -6.227  52.236 1.00 39.67  ? 90  GLY   D C   1 
ATOM   3838 O O   . GLY   D 1 90  ? -10.874 -5.605  51.187 1.00 38.78  ? 90  GLY   D O   1 
ATOM   3839 N N   . ASN   D 1 91  ? -10.022 -5.696  53.267 1.00 41.14  ? 91  ASN   D N   1 
ATOM   3840 C CA  . ASN   D 1 91  ? -10.142 -4.292  53.652 1.00 43.86  ? 91  ASN   D CA  1 
ATOM   3841 C C   . ASN   D 1 91  ? -8.782  -3.641  53.951 1.00 39.48  ? 91  ASN   D C   1 
ATOM   3842 O O   . ASN   D 1 91  ? -8.685  -2.749  54.802 1.00 33.95  ? 91  ASN   D O   1 
ATOM   3843 C CB  . ASN   D 1 91  ? -11.076 -4.196  54.863 1.00 51.66  ? 91  ASN   D CB  1 
ATOM   3844 C CG  . ASN   D 1 91  ? -11.687 -2.820  55.055 1.00 50.48  ? 91  ASN   D CG  1 
ATOM   3845 O OD1 . ASN   D 1 91  ? -11.742 -2.003  54.135 1.00 58.92  ? 91  ASN   D OD1 1 
ATOM   3846 N ND2 . ASN   D 1 91  ? -12.159 -2.563  56.269 1.00 52.23  ? 91  ASN   D ND2 1 
ATOM   3847 N N   . GLY   D 1 92  ? -7.713  -4.058  53.265 1.00 36.79  ? 92  GLY   D N   1 
ATOM   3848 C CA  . GLY   D 1 92  ? -6.411  -3.444  53.467 1.00 35.23  ? 92  GLY   D CA  1 
ATOM   3849 C C   . GLY   D 1 92  ? -5.606  -3.991  54.627 1.00 43.45  ? 92  GLY   D C   1 
ATOM   3850 O O   . GLY   D 1 92  ? -4.521  -3.467  54.921 1.00 32.01  ? 92  GLY   D O   1 
ATOM   3851 N N   . GLY   D 1 93  ? -6.105  -5.020  55.300 1.00 37.45  ? 93  GLY   D N   1 
ATOM   3852 C CA  . GLY   D 1 93  ? -5.367  -5.605  56.394 1.00 36.48  ? 93  GLY   D CA  1 
ATOM   3853 C C   . GLY   D 1 93  ? -5.519  -7.107  56.443 1.00 37.63  ? 93  GLY   D C   1 
ATOM   3854 O O   . GLY   D 1 93  ? -5.903  -7.758  55.461 1.00 26.30  ? 93  GLY   D O   1 
ATOM   3855 N N   . PHE   D 1 94  ? -5.232  -7.669  57.603 1.00 32.72  ? 94  PHE   D N   1 
ATOM   3856 C CA  . PHE   D 1 94  ? -5.218  -9.109  57.759 1.00 27.60  ? 94  PHE   D CA  1 
ATOM   3857 C C   . PHE   D 1 94  ? -6.050  -9.475  58.978 1.00 29.16  ? 94  PHE   D C   1 
ATOM   3858 O O   . PHE   D 1 94  ? -6.301  -8.642  59.857 1.00 24.76  ? 94  PHE   D O   1 
ATOM   3859 C CB  . PHE   D 1 94  ? -3.769  -9.607  57.884 1.00 27.12  ? 94  PHE   D CB  1 
ATOM   3860 C CG  . PHE   D 1 94  ? -2.932  -9.291  56.681 1.00 29.60  ? 94  PHE   D CG  1 
ATOM   3861 C CD1 . PHE   D 1 94  ? -2.927  -10.142 55.575 1.00 30.00  ? 94  PHE   D CD1 1 
ATOM   3862 C CD2 . PHE   D 1 94  ? -2.198  -8.106  56.628 1.00 27.15  ? 94  PHE   D CD2 1 
ATOM   3863 C CE1 . PHE   D 1 94  ? -2.172  -9.847  54.452 1.00 33.66  ? 94  PHE   D CE1 1 
ATOM   3864 C CE2 . PHE   D 1 94  ? -1.439  -7.791  55.506 1.00 38.28  ? 94  PHE   D CE2 1 
ATOM   3865 C CZ  . PHE   D 1 94  ? -1.431  -8.660  54.410 1.00 35.77  ? 94  PHE   D CZ  1 
ATOM   3866 N N   . ALA   D 1 95  ? -6.493  -10.730 59.002 1.00 22.27  ? 95  ALA   D N   1 
ATOM   3867 C CA  . ALA   D 1 95  ? -7.312  -11.280 60.069 1.00 25.44  ? 95  ALA   D CA  1 
ATOM   3868 C C   . ALA   D 1 95  ? -6.755  -12.630 60.499 1.00 27.86  ? 95  ALA   D C   1 
ATOM   3869 O O   . ALA   D 1 95  ? -6.148  -13.358 59.706 1.00 25.12  ? 95  ALA   D O   1 
ATOM   3870 C CB  . ALA   D 1 95  ? -8.774  -11.447 59.632 1.00 21.05  ? 95  ALA   D CB  1 
ATOM   3871 N N   . LEU   D 1 96  ? -6.977  -12.960 61.763 1.00 22.29  ? 96  LEU   D N   1 
ATOM   3872 C CA  . LEU   D 1 96  ? -6.602  -14.257 62.294 1.00 22.89  ? 96  LEU   D CA  1 
ATOM   3873 C C   . LEU   D 1 96  ? -7.795  -15.203 62.212 1.00 21.28  ? 96  LEU   D C   1 
ATOM   3874 O O   . LEU   D 1 96  ? -8.950  -14.773 62.330 1.00 21.78  ? 96  LEU   D O   1 
ATOM   3875 C CB  . LEU   D 1 96  ? -6.139  -14.124 63.744 1.00 27.88  ? 96  LEU   D CB  1 
ATOM   3876 C CG  . LEU   D 1 96  ? -4.908  -13.277 64.086 1.00 28.53  ? 96  LEU   D CG  1 
ATOM   3877 C CD1 . LEU   D 1 96  ? -4.690  -13.356 65.586 1.00 30.04  ? 96  LEU   D CD1 1 
ATOM   3878 C CD2 . LEU   D 1 96  ? -3.662  -13.737 63.347 1.00 22.28  ? 96  LEU   D CD2 1 
ATOM   3879 N N   . THR   D 1 97  ? -7.510  -16.473 61.953 1.00 21.68  ? 97  THR   D N   1 
ATOM   3880 C CA  . THR   D 1 97  ? -8.445  -17.580 62.158 1.00 28.34  ? 97  THR   D CA  1 
ATOM   3881 C C   . THR   D 1 97  ? -7.897  -18.461 63.274 1.00 19.81  ? 97  THR   D C   1 
ATOM   3882 O O   . THR   D 1 97  ? -6.675  -18.625 63.396 1.00 19.82  ? 97  THR   D O   1 
ATOM   3883 C CB  . THR   D 1 97  ? -8.646  -18.423 60.882 1.00 21.89  ? 97  THR   D CB  1 
ATOM   3884 O OG1 . THR   D 1 97  ? -7.448  -19.148 60.573 1.00 19.42  ? 97  THR   D OG1 1 
ATOM   3885 C CG2 . THR   D 1 97  ? -9.020  -17.550 59.685 1.00 27.49  ? 97  THR   D CG2 1 
ATOM   3886 N N   . VAL   D 1 98  ? -8.797  -19.022 64.084 1.00 25.62  ? 98  VAL   D N   1 
ATOM   3887 C CA  . VAL   D 1 98  ? -8.440  -19.828 65.257 1.00 25.21  ? 98  VAL   D CA  1 
ATOM   3888 C C   . VAL   D 1 98  ? -9.318  -21.077 65.299 1.00 30.97  ? 98  VAL   D C   1 
ATOM   3889 O O   . VAL   D 1 98  ? -10.555 -20.964 65.339 1.00 26.73  ? 98  VAL   D O   1 
ATOM   3890 C CB  . VAL   D 1 98  ? -8.617  -19.046 66.574 1.00 25.33  ? 98  VAL   D CB  1 
ATOM   3891 C CG1 . VAL   D 1 98  ? -8.267  -19.950 67.748 1.00 20.90  ? 98  VAL   D CG1 1 
ATOM   3892 C CG2 . VAL   D 1 98  ? -7.786  -17.763 66.589 1.00 21.43  ? 98  VAL   D CG2 1 
ATOM   3893 N N   . HIS   D 1 99  ? -8.684  -22.253 65.348 1.00 25.22  ? 99  HIS   D N   1 
ATOM   3894 C CA  . HIS   D 1 99  ? -9.340  -23.515 65.682 1.00 31.47  ? 99  HIS   D CA  1 
ATOM   3895 C C   . HIS   D 1 99  ? -8.696  -24.148 66.923 1.00 29.83  ? 99  HIS   D C   1 
ATOM   3896 O O   . HIS   D 1 99  ? -7.469  -24.129 67.068 1.00 28.34  ? 99  HIS   D O   1 
ATOM   3897 C CB  . HIS   D 1 99  ? -9.281  -24.496 64.506 1.00 30.09  ? 99  HIS   D CB  1 
ATOM   3898 C CG  . HIS   D 1 99  ? -9.929  -25.813 64.801 1.00 32.82  ? 99  HIS   D CG  1 
ATOM   3899 N ND1 . HIS   D 1 99  ? -11.286 -25.943 65.017 1.00 31.37  ? 99  HIS   D ND1 1 
ATOM   3900 C CD2 . HIS   D 1 99  ? -9.401  -27.052 64.973 1.00 38.26  ? 99  HIS   D CD2 1 
ATOM   3901 C CE1 . HIS   D 1 99  ? -11.569 -27.207 65.285 1.00 35.46  ? 99  HIS   D CE1 1 
ATOM   3902 N NE2 . HIS   D 1 99  ? -10.442 -27.901 65.268 1.00 32.55  ? 99  HIS   D NE2 1 
ATOM   3903 N N   . LEU   D 1 100 ? -9.524  -24.714 67.808 1.00 30.82  ? 100 LEU   D N   1 
ATOM   3904 C CA  . LEU   D 1 100 ? -9.070  -25.399 69.022 1.00 32.12  ? 100 LEU   D CA  1 
ATOM   3905 C C   . LEU   D 1 100 ? -9.516  -26.858 69.011 1.00 35.83  ? 100 LEU   D C   1 
ATOM   3906 O O   . LEU   D 1 100 ? -10.706 -27.143 68.837 1.00 36.20  ? 100 LEU   D O   1 
ATOM   3907 C CB  . LEU   D 1 100 ? -9.612  -24.723 70.288 1.00 27.04  ? 100 LEU   D CB  1 
ATOM   3908 C CG  . LEU   D 1 100 ? -9.252  -23.263 70.563 1.00 34.16  ? 100 LEU   D CG  1 
ATOM   3909 C CD1 . LEU   D 1 100 ? -9.799  -22.820 71.919 1.00 29.86  ? 100 LEU   D CD1 1 
ATOM   3910 C CD2 . LEU   D 1 100 ? -7.730  -23.078 70.487 1.00 26.99  ? 100 LEU   D CD2 1 
ATOM   3911 N N   . ASP   D 1 101 ? -8.556  -27.775 69.197 1.00 33.97  ? 101 ASP   D N   1 
ATOM   3912 C CA  . ASP   D 1 101 ? -8.829  -29.188 69.458 1.00 34.48  ? 101 ASP   D CA  1 
ATOM   3913 C C   . ASP   D 1 101 ? -8.547  -29.422 70.934 1.00 35.09  ? 101 ASP   D C   1 
ATOM   3914 O O   . ASP   D 1 101 ? -7.403  -29.285 71.372 1.00 30.17  ? 101 ASP   D O   1 
ATOM   3915 C CB  . ASP   D 1 101 ? -7.949  -30.093 68.599 1.00 34.98  ? 101 ASP   D CB  1 
ATOM   3916 C CG  . ASP   D 1 101 ? -8.304  -30.042 67.125 1.00 34.60  ? 101 ASP   D CG  1 
ATOM   3917 O OD1 . ASP   D 1 101 ? -9.510  -30.118 66.807 1.00 38.65  ? 101 ASP   D OD1 1 
ATOM   3918 O OD2 . ASP   D 1 101 ? -7.375  -29.935 66.284 1.00 36.79  ? 101 ASP   D OD2 1 
ATOM   3919 N N   . VAL   D 1 102 ? -9.579  -29.739 71.709 1.00 30.80  ? 102 VAL   D N   1 
ATOM   3920 C CA  . VAL   D 1 102 ? -9.439  -29.923 73.150 1.00 38.08  ? 102 VAL   D CA  1 
ATOM   3921 C C   . VAL   D 1 102 ? -9.603  -31.408 73.459 1.00 43.12  ? 102 VAL   D C   1 
ATOM   3922 O O   . VAL   D 1 102 ? -10.577 -32.035 73.026 1.00 38.28  ? 102 VAL   D O   1 
ATOM   3923 C CB  . VAL   D 1 102 ? -10.453 -29.070 73.926 1.00 37.14  ? 102 VAL   D CB  1 
ATOM   3924 C CG1 . VAL   D 1 102 ? -10.191 -29.159 75.426 1.00 33.46  ? 102 VAL   D CG1 1 
ATOM   3925 C CG2 . VAL   D 1 102 ? -10.402 -27.611 73.452 1.00 33.20  ? 102 VAL   D CG2 1 
ATOM   3926 N N   . THR   D 1 103 ? -8.639  -31.981 74.178 1.00 36.80  ? 103 THR   D N   1 
ATOM   3927 C CA  . THR   D 1 103 ? -8.687  -33.382 74.586 1.00 39.80  ? 103 THR   D CA  1 
ATOM   3928 C C   . THR   D 1 103 ? -8.620  -33.486 76.103 1.00 45.05  ? 103 THR   D C   1 
ATOM   3929 O O   . THR   D 1 103 ? -7.659  -33.009 76.721 1.00 39.99  ? 103 THR   D O   1 
ATOM   3930 C CB  . THR   D 1 103 ? -7.546  -34.190 73.986 1.00 35.14  ? 103 THR   D CB  1 
ATOM   3931 O OG1 . THR   D 1 103 ? -7.573  -34.085 72.565 1.00 46.52  ? 103 THR   D OG1 1 
ATOM   3932 C CG2 . THR   D 1 103 ? -7.720  -35.653 74.366 1.00 49.07  ? 103 THR   D CG2 1 
ATOM   3933 N N   . LEU   D 1 104 ? -9.618  -34.141 76.694 1.00 40.88  ? 104 LEU   D N   1 
ATOM   3934 C CA  . LEU   D 1 104 ? -9.686  -34.367 78.132 1.00 47.07  ? 104 LEU   D CA  1 
ATOM   3935 C C   . LEU   D 1 104 ? -9.632  -35.873 78.407 1.00 55.50  ? 104 LEU   D C   1 
ATOM   3936 O O   . LEU   D 1 104 ? -10.443 -36.637 77.868 1.00 51.07  ? 104 LEU   D O   1 
ATOM   3937 C CB  . LEU   D 1 104 ? -10.956 -33.740 78.715 1.00 49.81  ? 104 LEU   D CB  1 
ATOM   3938 C CG  . LEU   D 1 104 ? -11.356 -32.345 78.225 1.00 52.56  ? 104 LEU   D CG  1 
ATOM   3939 C CD1 . LEU   D 1 104 ? -12.467 -31.778 79.084 1.00 60.60  ? 104 LEU   D CD1 1 
ATOM   3940 C CD2 . LEU   D 1 104 ? -10.164 -31.404 78.263 1.00 54.96  ? 104 LEU   D CD2 1 
ATOM   3941 N N   . SER   D 1 105 ? -8.665  -36.298 79.222 1.00 51.45  ? 105 SER   D N   1 
ATOM   3942 C CA  . SER   D 1 105 ? -8.525  -37.701 79.590 1.00 53.37  ? 105 SER   D CA  1 
ATOM   3943 C C   . SER   D 1 105 ? -9.358  -37.997 80.827 1.00 54.63  ? 105 SER   D C   1 
ATOM   3944 O O   . SER   D 1 105 ? -9.268  -37.288 81.833 1.00 58.94  ? 105 SER   D O   1 
ATOM   3945 C CB  . SER   D 1 105 ? -7.064  -38.059 79.857 1.00 52.76  ? 105 SER   D CB  1 
ATOM   3946 O OG  . SER   D 1 105 ? -6.311  -38.042 78.659 1.00 62.29  ? 105 SER   D OG  1 
ATOM   3947 N N   . GLY   D 1 106 ? -10.171 -39.041 80.744 1.00 62.39  ? 106 GLY   D N   1 
ATOM   3948 C CA  . GLY   D 1 106 ? -10.852 -39.531 81.922 1.00 58.92  ? 106 GLY   D CA  1 
ATOM   3949 C C   . GLY   D 1 106 ? -12.101 -38.808 82.353 1.00 63.20  ? 106 GLY   D C   1 
ATOM   3950 O O   . GLY   D 1 106 ? -12.464 -38.877 83.537 1.00 68.87  ? 106 GLY   D O   1 
ATOM   3951 N N   . ILE   D 1 107 ? -12.781 -38.118 81.439 1.00 63.73  ? 107 ILE   D N   1 
ATOM   3952 C CA  . ILE   D 1 107 ? -14.136 -37.664 81.729 1.00 67.94  ? 107 ILE   D CA  1 
ATOM   3953 C C   . ILE   D 1 107 ? -15.031 -37.989 80.544 1.00 62.74  ? 107 ILE   D C   1 
ATOM   3954 O O   . ILE   D 1 107 ? -14.569 -38.209 79.422 1.00 56.43  ? 107 ILE   D O   1 
ATOM   3955 C CB  . ILE   D 1 107 ? -14.276 -36.164 82.047 1.00 70.43  ? 107 ILE   D CB  1 
ATOM   3956 C CG1 . ILE   D 1 107 ? -13.950 -35.316 80.844 1.00 68.85  ? 107 ILE   D CG1 1 
ATOM   3957 C CG2 . ILE   D 1 107 ? -13.310 -35.774 83.172 1.00 68.99  ? 107 ILE   D CG2 1 
ATOM   3958 C CD1 . ILE   D 1 107 ? -14.350 -33.912 81.090 1.00 69.56  ? 107 ILE   D CD1 1 
ATOM   3959 N N   . SER   D 1 108 ? -16.332 -37.999 80.799 1.00 62.63  ? 108 SER   D N   1 
ATOM   3960 C CA  . SER   D 1 108 ? -17.267 -38.425 79.764 1.00 59.83  ? 108 SER   D CA  1 
ATOM   3961 C C   . SER   D 1 108 ? -17.371 -37.355 78.670 1.00 61.08  ? 108 SER   D C   1 
ATOM   3962 O O   . SER   D 1 108 ? -17.355 -36.164 78.945 1.00 61.43  ? 108 SER   D O   1 
ATOM   3963 C CB  . SER   D 1 108 ? -18.646 -38.704 80.366 1.00 54.43  ? 108 SER   D CB  1 
ATOM   3964 O OG  . SER   D 1 108 ? -19.262 -37.523 80.829 1.00 58.47  ? 108 SER   D OG  1 
ATOM   3965 N N   . GLN   D 1 109 ? -17.430 -37.782 77.419 1.00 58.95  ? 109 GLN   D N   1 
ATOM   3966 C CA  . GLN   D 1 109 ? -17.513 -36.971 76.205 1.00 55.75  ? 109 GLN   D CA  1 
ATOM   3967 C C   . GLN   D 1 109 ? -18.546 -35.864 76.278 1.00 56.88  ? 109 GLN   D C   1 
ATOM   3968 O O   . GLN   D 1 109 ? -18.302 -34.749 75.804 1.00 56.89  ? 109 GLN   D O   1 
ATOM   3969 C CB  . GLN   D 1 109 ? -17.808 -37.927 75.045 1.00 56.00  ? 109 GLN   D CB  1 
ATOM   3970 C CG  . GLN   D 1 109 ? -17.813 -37.377 73.582 1.00 61.67  ? 109 GLN   D CG  1 
ATOM   3971 C CD  . GLN   D 1 109 ? -16.532 -36.687 73.163 1.00 61.17  ? 109 GLN   D CD  1 
ATOM   3972 O OE1 . GLN   D 1 109 ? -16.528 -35.442 72.977 1.00 60.28  ? 109 GLN   D OE1 1 
ATOM   3973 N NE2 . GLN   D 1 109 ? -15.453 -37.470 73.032 1.00 55.02  ? 109 GLN   D NE2 1 
ATOM   3974 N N   . ALA   D 1 110 ? -19.713 -36.161 76.842 1.00 54.77  ? 110 ALA   D N   1 
ATOM   3975 C CA  . ALA   D 1 110 ? -20.732 -35.123 76.987 1.00 50.39  ? 110 ALA   D CA  1 
ATOM   3976 C C   . ALA   D 1 110 ? -20.322 -34.098 78.047 1.00 58.84  ? 110 ALA   D C   1 
ATOM   3977 O O   . ALA   D 1 110 ? -20.446 -32.872 77.848 1.00 58.30  ? 110 ALA   D O   1 
ATOM   3978 C CB  . ALA   D 1 110 ? -22.079 -35.763 77.337 1.00 47.87  ? 110 ALA   D CB  1 
ATOM   3979 N N   . ASP   D 1 111 ? -19.806 -34.585 79.179 1.00 55.79  ? 111 ASP   D N   1 
ATOM   3980 C CA  . ASP   D 1 111 ? -19.366 -33.670 80.230 1.00 58.38  ? 111 ASP   D CA  1 
ATOM   3981 C C   . ASP   D 1 111 ? -18.259 -32.760 79.733 1.00 52.03  ? 111 ASP   D C   1 
ATOM   3982 O O   . ASP   D 1 111 ? -18.238 -31.567 80.058 1.00 47.90  ? 111 ASP   D O   1 
ATOM   3983 C CB  . ASP   D 1 111 ? -18.879 -34.424 81.470 1.00 62.29  ? 111 ASP   D CB  1 
ATOM   3984 C CG  . ASP   D 1 111 ? -20.007 -35.009 82.280 1.00 69.47  ? 111 ASP   D CG  1 
ATOM   3985 O OD1 . ASP   D 1 111 ? -21.098 -35.228 81.706 1.00 71.71  ? 111 ASP   D OD1 1 
ATOM   3986 O OD2 . ASP   D 1 111 ? -19.798 -35.257 83.488 1.00 74.03  ? 111 ASP   D OD2 1 
ATOM   3987 N N   . ALA   D 1 112 ? -17.313 -33.320 78.974 1.00 48.48  ? 112 ALA   D N   1 
ATOM   3988 C CA  . ALA   D 1 112 ? -16.259 -32.513 78.375 1.00 52.29  ? 112 ALA   D CA  1 
ATOM   3989 C C   . ALA   D 1 112 ? -16.845 -31.429 77.484 1.00 54.47  ? 112 ALA   D C   1 
ATOM   3990 O O   . ALA   D 1 112 ? -16.404 -30.274 77.523 1.00 51.96  ? 112 ALA   D O   1 
ATOM   3991 C CB  . ALA   D 1 112 ? -15.315 -33.397 77.567 1.00 48.54  ? 112 ALA   D CB  1 
ATOM   3992 N N   . GLU   D 1 113 ? -17.833 -31.785 76.653 1.00 54.34  ? 113 GLU   D N   1 
ATOM   3993 C CA  . GLU   D 1 113 ? -18.448 -30.757 75.814 1.00 49.19  ? 113 GLU   D CA  1 
ATOM   3994 C C   . GLU   D 1 113 ? -19.039 -29.619 76.654 1.00 51.19  ? 113 GLU   D C   1 
ATOM   3995 O O   . GLU   D 1 113 ? -18.808 -28.433 76.363 1.00 54.19  ? 113 GLU   D O   1 
ATOM   3996 C CB  . GLU   D 1 113 ? -19.478 -31.404 74.889 1.00 46.44  ? 113 GLU   D CB  1 
ATOM   3997 C CG  . GLU   D 1 113 ? -18.767 -31.974 73.661 1.00 48.97  ? 113 GLU   D CG  1 
ATOM   3998 C CD  . GLU   D 1 113 ? -19.544 -33.047 72.914 1.00 52.60  ? 113 GLU   D CD  1 
ATOM   3999 O OE1 . GLU   D 1 113 ? -20.794 -33.069 73.011 1.00 50.67  ? 113 GLU   D OE1 1 
ATOM   4000 O OE2 . GLU   D 1 113 ? -18.889 -33.875 72.231 1.00 54.21  ? 113 GLU   D OE2 1 
ATOM   4001 N N   . LYS   D 1 114 ? -19.749 -29.950 77.733 1.00 53.58  ? 114 LYS   D N   1 
ATOM   4002 C CA  . LYS   D 1 114 ? -20.318 -28.879 78.558 1.00 51.39  ? 114 LYS   D CA  1 
ATOM   4003 C C   . LYS   D 1 114 ? -19.233 -28.046 79.254 1.00 51.33  ? 114 LYS   D C   1 
ATOM   4004 O O   . LYS   D 1 114 ? -19.369 -26.815 79.362 1.00 51.83  ? 114 LYS   D O   1 
ATOM   4005 C CB  . LYS   D 1 114 ? -21.292 -29.463 79.578 1.00 58.91  ? 114 LYS   D CB  1 
ATOM   4006 C CG  . LYS   D 1 114 ? -22.689 -29.681 79.007 1.00 61.99  ? 114 LYS   D CG  1 
ATOM   4007 C CD  . LYS   D 1 114 ? -23.664 -30.136 80.078 1.00 60.74  ? 114 LYS   D CD  1 
ATOM   4008 C CE  . LYS   D 1 114 ? -25.088 -29.679 79.793 1.00 66.06  ? 114 LYS   D CE  1 
ATOM   4009 N NZ  . LYS   D 1 114 ? -26.061 -30.473 80.609 1.00 65.76  ? 114 LYS   D NZ  1 
ATOM   4010 N N   . ILE   D 1 115 ? -18.152 -28.696 79.716 1.00 52.32  ? 115 ILE   D N   1 
ATOM   4011 C CA  . ILE   D 1 115 ? -17.006 -27.992 80.309 1.00 50.89  ? 115 ILE   D CA  1 
ATOM   4012 C C   . ILE   D 1 115 ? -16.391 -27.003 79.327 1.00 42.20  ? 115 ILE   D C   1 
ATOM   4013 O O   . ILE   D 1 115 ? -16.127 -25.849 79.677 1.00 45.30  ? 115 ILE   D O   1 
ATOM   4014 C CB  . ILE   D 1 115 ? -15.958 -28.998 80.827 1.00 53.76  ? 115 ILE   D CB  1 
ATOM   4015 C CG1 . ILE   D 1 115 ? -16.514 -29.765 82.029 1.00 52.14  ? 115 ILE   D CG1 1 
ATOM   4016 C CG2 . ILE   D 1 115 ? -14.609 -28.320 81.085 1.00 45.61  ? 115 ILE   D CG2 1 
ATOM   4017 C CD1 . ILE   D 1 115 ? -15.700 -30.957 82.433 1.00 46.45  ? 115 ILE   D CD1 1 
ATOM   4018 N N   . VAL   D 1 116 ? -16.135 -27.439 78.097 1.00 38.51  ? 116 VAL   D N   1 
ATOM   4019 C CA  . VAL   D 1 116 ? -15.502 -26.561 77.116 1.00 45.80  ? 116 VAL   D CA  1 
ATOM   4020 C C   . VAL   D 1 116 ? -16.418 -25.384 76.772 1.00 50.42  ? 116 VAL   D C   1 
ATOM   4021 O O   . VAL   D 1 116 ? -15.954 -24.240 76.615 1.00 37.10  ? 116 VAL   D O   1 
ATOM   4022 C CB  . VAL   D 1 116 ? -15.093 -27.378 75.874 1.00 44.00  ? 116 VAL   D CB  1 
ATOM   4023 C CG1 . VAL   D 1 116 ? -14.624 -26.479 74.745 1.00 39.29  ? 116 VAL   D CG1 1 
ATOM   4024 C CG2 . VAL   D 1 116 ? -13.988 -28.372 76.261 1.00 44.64  ? 116 VAL   D CG2 1 
ATOM   4025 N N   . GLU   D 1 117 ? -17.737 -25.629 76.687 1.00 47.46  ? 117 GLU   D N   1 
ATOM   4026 C CA  . GLU   D 1 117 ? -18.648 -24.515 76.431 1.00 41.88  ? 117 GLU   D CA  1 
ATOM   4027 C C   . GLU   D 1 117 ? -18.637 -23.515 77.583 1.00 46.22  ? 117 GLU   D C   1 
ATOM   4028 O O   . GLU   D 1 117 ? -18.724 -22.300 77.354 1.00 49.68  ? 117 GLU   D O   1 
ATOM   4029 C CB  . GLU   D 1 117 ? -20.070 -25.014 76.166 1.00 53.10  ? 117 GLU   D CB  1 
ATOM   4030 C CG  . GLU   D 1 117 ? -21.054 -23.872 75.902 1.00 58.95  ? 117 GLU   D CG  1 
ATOM   4031 C CD  . GLU   D 1 117 ? -22.382 -24.332 75.311 1.00 70.63  ? 117 GLU   D CD  1 
ATOM   4032 O OE1 . GLU   D 1 117 ? -22.514 -24.321 74.063 1.00 72.22  ? 117 GLU   D OE1 1 
ATOM   4033 O OE2 . GLU   D 1 117 ? -23.298 -24.678 76.094 1.00 65.57  ? 117 GLU   D OE2 1 
ATOM   4034 N N   . GLN   D 1 118 ? -18.525 -23.994 78.829 1.00 45.49  ? 118 GLN   D N   1 
ATOM   4035 C CA  . GLN   D 1 118 ? -18.374 -23.055 79.947 1.00 47.64  ? 118 GLN   D CA  1 
ATOM   4036 C C   . GLN   D 1 118 ? -17.046 -22.307 79.878 1.00 41.92  ? 118 GLN   D C   1 
ATOM   4037 O O   . GLN   D 1 118 ? -16.971 -21.130 80.252 1.00 38.82  ? 118 GLN   D O   1 
ATOM   4038 C CB  . GLN   D 1 118 ? -18.469 -23.774 81.294 1.00 50.26  ? 118 GLN   D CB  1 
ATOM   4039 C CG  . GLN   D 1 118 ? -19.834 -24.313 81.645 1.00 59.17  ? 118 GLN   D CG  1 
ATOM   4040 C CD  . GLN   D 1 118 ? -19.763 -25.301 82.790 1.00 55.99  ? 118 GLN   D CD  1 
ATOM   4041 O OE1 . GLN   D 1 118 ? -18.966 -25.138 83.719 1.00 48.77  ? 118 GLN   D OE1 1 
ATOM   4042 N NE2 . GLN   D 1 118 ? -20.576 -26.347 82.717 1.00 54.55  ? 118 GLN   D NE2 1 
ATOM   4043 N N   . THR   D 1 119 ? -15.983 -22.995 79.444 1.00 44.33  ? 119 THR   D N   1 
ATOM   4044 C CA  . THR   D 1 119 ? -14.649 -22.401 79.446 1.00 39.99  ? 119 THR   D CA  1 
ATOM   4045 C C   . THR   D 1 119 ? -14.572 -21.255 78.450 1.00 38.22  ? 119 THR   D C   1 
ATOM   4046 O O   . THR   D 1 119 ? -13.945 -20.225 78.727 1.00 33.92  ? 119 THR   D O   1 
ATOM   4047 C CB  . THR   D 1 119 ? -13.590 -23.459 79.119 1.00 38.35  ? 119 THR   D CB  1 
ATOM   4048 O OG1 . THR   D 1 119 ? -13.674 -24.538 80.055 1.00 40.57  ? 119 THR   D OG1 1 
ATOM   4049 C CG2 . THR   D 1 119 ? -12.182 -22.855 79.195 1.00 34.01  ? 119 THR   D CG2 1 
ATOM   4050 N N   . HIS   D 1 120 ? -15.240 -21.407 77.300 1.00 34.94  ? 120 HIS   D N   1 
ATOM   4051 C CA  . HIS   D 1 120 ? -15.265 -20.330 76.311 1.00 43.10  ? 120 HIS   D CA  1 
ATOM   4052 C C   . HIS   D 1 120 ? -15.772 -19.016 76.889 1.00 43.78  ? 120 HIS   D C   1 
ATOM   4053 O O   . HIS   D 1 120 ? -15.435 -17.945 76.372 1.00 37.11  ? 120 HIS   D O   1 
ATOM   4054 C CB  . HIS   D 1 120 ? -16.108 -20.730 75.105 1.00 37.54  ? 120 HIS   D CB  1 
ATOM   4055 C CG  . HIS   D 1 120 ? -15.330 -21.452 74.052 1.00 33.32  ? 120 HIS   D CG  1 
ATOM   4056 N ND1 . HIS   D 1 120 ? -14.217 -20.903 73.450 1.00 34.62  ? 120 HIS   D ND1 1 
ATOM   4057 C CD2 . HIS   D 1 120 ? -15.500 -22.671 73.490 1.00 37.39  ? 120 HIS   D CD2 1 
ATOM   4058 C CE1 . HIS   D 1 120 ? -13.738 -21.752 72.559 1.00 36.12  ? 120 HIS   D CE1 1 
ATOM   4059 N NE2 . HIS   D 1 120 ? -14.497 -22.835 72.564 1.00 41.26  ? 120 HIS   D NE2 1 
ATOM   4060 N N   . GLN   D 1 121 ? -16.550 -19.066 77.969 1.00 38.48  ? 121 GLN   D N   1 
ATOM   4061 C CA  . GLN   D 1 121 ? -17.000 -17.846 78.630 1.00 42.38  ? 121 GLN   D CA  1 
ATOM   4062 C C   . GLN   D 1 121 ? -16.032 -17.347 79.698 1.00 38.93  ? 121 GLN   D C   1 
ATOM   4063 O O   . GLN   D 1 121 ? -16.191 -16.218 80.176 1.00 43.94  ? 121 GLN   D O   1 
ATOM   4064 C CB  . GLN   D 1 121 ? -18.384 -18.067 79.257 1.00 45.70  ? 121 GLN   D CB  1 
ATOM   4065 C CG  . GLN   D 1 121 ? -19.429 -18.636 78.299 1.00 49.13  ? 121 GLN   D CG  1 
ATOM   4066 C CD  . GLN   D 1 121 ? -19.970 -17.582 77.350 1.00 59.86  ? 121 GLN   D CD  1 
ATOM   4067 O OE1 . GLN   D 1 121 ? -20.506 -16.557 77.786 1.00 65.00  ? 121 GLN   D OE1 1 
ATOM   4068 N NE2 . GLN   D 1 121 ? -19.843 -17.829 76.046 1.00 54.40  ? 121 GLN   D NE2 1 
ATOM   4069 N N   . VAL   D 1 122 ? -15.035 -18.149 80.071 1.00 44.09  ? 122 VAL   D N   1 
ATOM   4070 C CA  . VAL   D 1 122 ? -14.114 -17.821 81.153 1.00 41.99  ? 122 VAL   D CA  1 
ATOM   4071 C C   . VAL   D 1 122 ? -12.760 -17.366 80.629 1.00 33.02  ? 122 VAL   D C   1 
ATOM   4072 O O   . VAL   D 1 122 ? -12.146 -16.454 81.189 1.00 33.01  ? 122 VAL   D O   1 
ATOM   4073 C CB  . VAL   D 1 122 ? -13.944 -19.027 82.109 1.00 42.10  ? 122 VAL   D CB  1 
ATOM   4074 C CG1 . VAL   D 1 122 ? -12.905 -18.726 83.205 1.00 48.76  ? 122 VAL   D CG1 1 
ATOM   4075 C CG2 . VAL   D 1 122 ? -15.267 -19.416 82.707 1.00 46.60  ? 122 VAL   D CG2 1 
ATOM   4076 N N   . CYS   D 1 123 ? -12.267 -18.024 79.589 1.00 35.68  ? 123 CYS   D N   1 
ATOM   4077 C CA  . CYS   D 1 123 ? -10.926 -17.792 79.085 1.00 39.75  ? 123 CYS   D CA  1 
ATOM   4078 C C   . CYS   D 1 123 ? -10.821 -16.364 78.570 1.00 30.18  ? 123 CYS   D C   1 
ATOM   4079 O O   . CYS   D 1 123 ? -11.600 -15.977 77.690 1.00 26.03  ? 123 CYS   D O   1 
ATOM   4080 C CB  . CYS   D 1 123 ? -10.619 -18.808 77.987 1.00 33.95  ? 123 CYS   D CB  1 
ATOM   4081 S SG  . CYS   D 1 123 ? -9.098  -18.523 77.114 1.00 53.78  ? 123 CYS   D SG  1 
ATOM   4082 N N   . PRO   D 1 124 ? -9.906  -15.550 79.099 1.00 32.82  ? 124 PRO   D N   1 
ATOM   4083 C CA  . PRO   D 1 124 ? -9.856  -14.136 78.693 1.00 24.68  ? 124 PRO   D CA  1 
ATOM   4084 C C   . PRO   D 1 124 ? -9.514  -13.953 77.231 1.00 31.92  ? 124 PRO   D C   1 
ATOM   4085 O O   . PRO   D 1 124 ? -9.846  -12.910 76.661 1.00 24.04  ? 124 PRO   D O   1 
ATOM   4086 C CB  . PRO   D 1 124 ? -8.766  -13.545 79.591 1.00 27.68  ? 124 PRO   D CB  1 
ATOM   4087 C CG  . PRO   D 1 124 ? -7.939  -14.739 80.035 1.00 38.10  ? 124 PRO   D CG  1 
ATOM   4088 C CD  . PRO   D 1 124 ? -8.926  -15.870 80.150 1.00 29.41  ? 124 PRO   D CD  1 
ATOM   4089 N N   . TYR   D 1 125 ? -8.873  -14.942 76.606 1.00 19.76  ? 125 TYR   D N   1 
ATOM   4090 C CA  . TYR   D 1 125 ? -8.542  -14.856 75.189 1.00 33.92  ? 125 TYR   D CA  1 
ATOM   4091 C C   . TYR   D 1 125 ? -9.777  -15.053 74.306 1.00 23.80  ? 125 TYR   D C   1 
ATOM   4092 O O   . TYR   D 1 125 ? -9.990  -14.303 73.337 1.00 27.71  ? 125 TYR   D O   1 
ATOM   4093 C CB  . TYR   D 1 125 ? -7.454  -15.879 74.860 1.00 27.32  ? 125 TYR   D CB  1 
ATOM   4094 C CG  . TYR   D 1 125 ? -6.115  -15.557 75.483 1.00 41.91  ? 125 TYR   D CG  1 
ATOM   4095 C CD1 . TYR   D 1 125 ? -5.968  -15.507 76.870 1.00 40.05  ? 125 TYR   D CD1 1 
ATOM   4096 C CD2 . TYR   D 1 125 ? -5.001  -15.281 74.687 1.00 39.44  ? 125 TYR   D CD2 1 
ATOM   4097 C CE1 . TYR   D 1 125 ? -4.768  -15.186 77.444 1.00 43.11  ? 125 TYR   D CE1 1 
ATOM   4098 C CE2 . TYR   D 1 125 ? -3.790  -14.966 75.259 1.00 45.52  ? 125 TYR   D CE2 1 
ATOM   4099 C CZ  . TYR   D 1 125 ? -3.683  -14.920 76.636 1.00 45.84  ? 125 TYR   D CZ  1 
ATOM   4100 O OH  . TYR   D 1 125 ? -2.482  -14.603 77.211 1.00 53.87  ? 125 TYR   D OH  1 
ATOM   4101 N N   . SER   D 1 126 ? -10.592 -16.070 74.610 1.00 26.64  ? 126 SER   D N   1 
ATOM   4102 C CA  . SER   D 1 126 ? -11.884 -16.199 73.936 1.00 31.51  ? 126 SER   D CA  1 
ATOM   4103 C C   . SER   D 1 126 ? -12.696 -14.915 74.051 1.00 25.62  ? 126 SER   D C   1 
ATOM   4104 O O   . SER   D 1 126 ? -13.225 -14.415 73.053 1.00 32.17  ? 126 SER   D O   1 
ATOM   4105 C CB  . SER   D 1 126 ? -12.691 -17.374 74.497 1.00 28.22  ? 126 SER   D CB  1 
ATOM   4106 O OG  . SER   D 1 126 ? -12.020 -18.596 74.311 1.00 30.45  ? 126 SER   D OG  1 
ATOM   4107 N N   . ASN   D 1 127 ? -12.818 -14.376 75.264 1.00 22.99  ? 127 ASN   D N   1 
ATOM   4108 C CA  . ASN   D 1 127 ? -13.574 -13.136 75.431 1.00 21.40  ? 127 ASN   D CA  1 
ATOM   4109 C C   . ASN   D 1 127 ? -12.915 -11.981 74.691 1.00 28.52  ? 127 ASN   D C   1 
ATOM   4110 O O   . ASN   D 1 127 ? -13.608 -11.072 74.217 1.00 25.71  ? 127 ASN   D O   1 
ATOM   4111 C CB  . ASN   D 1 127 ? -13.714 -12.776 76.907 1.00 22.85  ? 127 ASN   D CB  1 
ATOM   4112 C CG  . ASN   D 1 127 ? -14.540 -13.787 77.687 1.00 34.82  ? 127 ASN   D CG  1 
ATOM   4113 O OD1 . ASN   D 1 127 ? -15.260 -14.612 77.110 1.00 36.24  ? 127 ASN   D OD1 1 
ATOM   4114 N ND2 . ASN   D 1 127 ? -14.440 -13.726 79.010 1.00 37.41  ? 127 ASN   D ND2 1 
ATOM   4115 N N   . ALA   D 1 128 ? -11.581 -11.997 74.590 1.00 23.95  ? 128 ALA   D N   1 
ATOM   4116 C CA  . ALA   D 1 128 ? -10.858 -10.942 73.890 1.00 24.97  ? 128 ALA   D CA  1 
ATOM   4117 C C   . ALA   D 1 128 ? -11.201 -10.893 72.407 1.00 27.27  ? 128 ALA   D C   1 
ATOM   4118 O O   . ALA   D 1 128 ? -11.153 -9.813  71.801 1.00 22.29  ? 128 ALA   D O   1 
ATOM   4119 C CB  . ALA   D 1 128 ? -9.353  -11.136 74.040 1.00 18.81  ? 128 ALA   D CB  1 
ATOM   4120 N N   . ILE   D 1 129 ? -11.514 -12.033 71.789 1.00 20.89  ? 129 ILE   D N   1 
ATOM   4121 C CA  . ILE   D 1 129 ? -11.659 -12.047 70.333 1.00 20.64  ? 129 ILE   D CA  1 
ATOM   4122 C C   . ILE   D 1 129 ? -13.096 -12.278 69.858 1.00 22.72  ? 129 ILE   D C   1 
ATOM   4123 O O   . ILE   D 1 129 ? -13.338 -12.246 68.637 1.00 28.50  ? 129 ILE   D O   1 
ATOM   4124 C CB  . ILE   D 1 129 ? -10.701 -13.072 69.692 1.00 15.34  ? 129 ILE   D CB  1 
ATOM   4125 C CG1 . ILE   D 1 129 ? -11.049 -14.487 70.107 1.00 19.73  ? 129 ILE   D CG1 1 
ATOM   4126 C CG2 . ILE   D 1 129 ? -9.244  -12.748 70.079 1.00 15.24  ? 129 ILE   D CG2 1 
ATOM   4127 C CD1 . ILE   D 1 129 ? -10.206 -15.502 69.382 1.00 27.90  ? 129 ILE   D CD1 1 
ATOM   4128 N N   . ARG   D 1 130 ? -14.048 -12.471 70.768 1.00 23.89  ? 130 ARG   D N   1 
ATOM   4129 C CA  . ARG   D 1 130 ? -15.428 -12.768 70.396 1.00 23.60  ? 130 ARG   D CA  1 
ATOM   4130 C C   . ARG   D 1 130 ? -16.088 -11.584 69.679 1.00 22.09  ? 130 ARG   D C   1 
ATOM   4131 O O   . ARG   D 1 130 ? -16.045 -10.443 70.152 1.00 23.29  ? 130 ARG   D O   1 
ATOM   4132 C CB  . ARG   D 1 130 ? -16.239 -13.123 71.642 1.00 29.34  ? 130 ARG   D CB  1 
ATOM   4133 C CG  . ARG   D 1 130 ? -17.641 -13.598 71.301 1.00 34.34  ? 130 ARG   D CG  1 
ATOM   4134 C CD  . ARG   D 1 130 ? -18.398 -14.187 72.483 1.00 43.69  ? 130 ARG   D CD  1 
ATOM   4135 N NE  . ARG   D 1 130 ? -17.659 -15.225 73.204 1.00 42.13  ? 130 ARG   D NE  1 
ATOM   4136 C CZ  . ARG   D 1 130 ? -17.043 -15.024 74.364 1.00 40.77  ? 130 ARG   D CZ  1 
ATOM   4137 N NH1 . ARG   D 1 130 ? -17.098 -13.831 74.951 1.00 33.02  ? 130 ARG   D NH1 1 
ATOM   4138 N NH2 . ARG   D 1 130 ? -16.395 -16.022 74.952 1.00 40.33  ? 130 ARG   D NH2 1 
ATOM   4139 N N   . GLY   D 1 131 ? -16.740 -11.877 68.557 1.00 18.26  ? 131 GLY   D N   1 
ATOM   4140 C CA  . GLY   D 1 131 ? -17.349 -10.878 67.700 1.00 23.79  ? 131 GLY   D CA  1 
ATOM   4141 C C   . GLY   D 1 131 ? -16.476 -10.402 66.558 1.00 25.70  ? 131 GLY   D C   1 
ATOM   4142 O O   . GLY   D 1 131 ? -16.989 -9.788  65.614 1.00 24.02  ? 131 GLY   D O   1 
ATOM   4143 N N   . ASN   D 1 132 ? -15.174 -10.655 66.627 1.00 22.96  ? 132 ASN   D N   1 
ATOM   4144 C CA  . ASN   D 1 132 ? -14.240 -10.370 65.557 1.00 17.10  ? 132 ASN   D CA  1 
ATOM   4145 C C   . ASN   D 1 132 ? -13.750 -11.641 64.888 1.00 26.26  ? 132 ASN   D C   1 
ATOM   4146 O O   . ASN   D 1 132 ? -13.634 -11.706 63.658 1.00 21.22  ? 132 ASN   D O   1 
ATOM   4147 C CB  . ASN   D 1 132 ? -13.062 -9.582  66.135 1.00 22.32  ? 132 ASN   D CB  1 
ATOM   4148 C CG  . ASN   D 1 132 ? -13.477 -8.227  66.598 1.00 22.14  ? 132 ASN   D CG  1 
ATOM   4149 O OD1 . ASN   D 1 132 ? -14.157 -7.501  65.867 1.00 24.07  ? 132 ASN   D OD1 1 
ATOM   4150 N ND2 . ASN   D 1 132 ? -13.156 -7.898  67.837 1.00 17.70  ? 132 ASN   D ND2 1 
ATOM   4151 N N   . ILE   D 1 133 ? -13.436 -12.652 65.691 1.00 23.83  ? 133 ILE   D N   1 
ATOM   4152 C CA  . ILE   D 1 133 ? -13.019 -13.962 65.211 1.00 26.86  ? 133 ILE   D CA  1 
ATOM   4153 C C   . ILE   D 1 133 ? -14.032 -14.981 65.694 1.00 21.17  ? 133 ILE   D C   1 
ATOM   4154 O O   . ILE   D 1 133 ? -14.421 -14.982 66.868 1.00 25.15  ? 133 ILE   D O   1 
ATOM   4155 C CB  . ILE   D 1 133 ? -11.608 -14.338 65.700 1.00 25.29  ? 133 ILE   D CB  1 
ATOM   4156 C CG1 . ILE   D 1 133 ? -10.574 -13.477 64.981 1.00 27.12  ? 133 ILE   D CG1 1 
ATOM   4157 C CG2 . ILE   D 1 133 ? -11.348 -15.826 65.477 1.00 21.71  ? 133 ILE   D CG2 1 
ATOM   4158 C CD1 . ILE   D 1 133 ? -9.319  -13.297 65.742 1.00 24.22  ? 133 ILE   D CD1 1 
ATOM   4159 N N   . GLN   D 1 134 ? -14.468 -15.828 64.785 1.00 29.28  ? 134 GLN   D N   1 
ATOM   4160 C CA  . GLN   D 1 134 ? -15.364 -16.938 65.082 1.00 30.93  ? 134 GLN   D CA  1 
ATOM   4161 C C   . GLN   D 1 134 ? -14.505 -18.180 65.326 1.00 24.69  ? 134 GLN   D C   1 
ATOM   4162 O O   . GLN   D 1 134 ? -14.102 -18.884 64.389 1.00 26.86  ? 134 GLN   D O   1 
ATOM   4163 C CB  . GLN   D 1 134 ? -16.344 -17.064 63.925 1.00 39.73  ? 134 GLN   D CB  1 
ATOM   4164 C CG  . GLN   D 1 134 ? -17.366 -18.200 63.864 1.00 55.85  ? 134 GLN   D CG  1 
ATOM   4165 C CD  . GLN   D 1 134 ? -18.393 -18.306 64.991 1.00 65.52  ? 134 GLN   D CD  1 
ATOM   4166 O OE1 . GLN   D 1 134 ? -18.878 -17.312 65.560 1.00 65.39  ? 134 GLN   D OE1 1 
ATOM   4167 N NE2 . GLN   D 1 134 ? -18.854 -19.543 65.174 1.00 74.14  ? 134 GLN   D NE2 1 
ATOM   4168 N N   . VAL   D 1 135 ? -14.179 -18.416 66.598 1.00 26.03  ? 135 VAL   D N   1 
ATOM   4169 C CA  . VAL   D 1 135 ? -13.404 -19.591 66.988 1.00 27.26  ? 135 VAL   D CA  1 
ATOM   4170 C C   . VAL   D 1 135 ? -14.248 -20.839 66.761 1.00 27.04  ? 135 VAL   D C   1 
ATOM   4171 O O   . VAL   D 1 135 ? -15.417 -20.900 67.163 1.00 31.20  ? 135 VAL   D O   1 
ATOM   4172 C CB  . VAL   D 1 135 ? -12.971 -19.500 68.462 1.00 32.76  ? 135 VAL   D CB  1 
ATOM   4173 C CG1 . VAL   D 1 135 ? -12.078 -20.700 68.835 1.00 29.71  ? 135 VAL   D CG1 1 
ATOM   4174 C CG2 . VAL   D 1 135 ? -12.271 -18.194 68.753 1.00 26.73  ? 135 VAL   D CG2 1 
ATOM   4175 N N   . SER   D 1 136 ? -13.659 -21.836 66.125 1.00 28.63  ? 136 SER   D N   1 
ATOM   4176 C CA  . SER   D 1 136 ? -14.255 -23.158 66.059 1.00 34.32  ? 136 SER   D CA  1 
ATOM   4177 C C   . SER   D 1 136 ? -13.549 -24.064 67.064 1.00 40.66  ? 136 SER   D C   1 
ATOM   4178 O O   . SER   D 1 136 ? -12.395 -23.821 67.443 1.00 33.32  ? 136 SER   D O   1 
ATOM   4179 C CB  . SER   D 1 136 ? -14.192 -23.724 64.630 1.00 35.58  ? 136 SER   D CB  1 
ATOM   4180 O OG  . SER   D 1 136 ? -12.869 -23.771 64.120 1.00 34.74  ? 136 SER   D OG  1 
ATOM   4181 N N   . THR   D 1 137 ? -14.276 -25.081 67.532 1.00 40.30  ? 137 THR   D N   1 
ATOM   4182 C CA  . THR   D 1 137 ? -13.812 -25.989 68.577 1.00 41.66  ? 137 THR   D CA  1 
ATOM   4183 C C   . THR   D 1 137 ? -14.279 -27.407 68.280 1.00 42.76  ? 137 THR   D C   1 
ATOM   4184 O O   . THR   D 1 137 ? -15.465 -27.628 68.017 1.00 39.57  ? 137 THR   D O   1 
ATOM   4185 C CB  . THR   D 1 137 ? -14.328 -25.570 69.960 1.00 36.91  ? 137 THR   D CB  1 
ATOM   4186 O OG1 . THR   D 1 137 ? -14.019 -24.191 70.199 1.00 41.26  ? 137 THR   D OG1 1 
ATOM   4187 C CG2 . THR   D 1 137 ? -13.687 -26.420 71.031 1.00 39.66  ? 137 THR   D CG2 1 
ATOM   4188 N N   . THR   D 1 138 ? -13.344 -28.356 68.330 1.00 41.37  ? 138 THR   D N   1 
ATOM   4189 C CA  . THR   D 1 138 ? -13.624 -29.785 68.329 1.00 38.30  ? 138 THR   D CA  1 
ATOM   4190 C C   . THR   D 1 138 ? -13.129 -30.362 69.650 1.00 43.60  ? 138 THR   D C   1 
ATOM   4191 O O   . THR   D 1 138 ? -12.024 -30.030 70.094 1.00 42.05  ? 138 THR   D O   1 
ATOM   4192 C CB  . THR   D 1 138 ? -12.929 -30.485 67.145 1.00 41.09  ? 138 THR   D CB  1 
ATOM   4193 O OG1 . THR   D 1 138 ? -13.466 -29.992 65.911 1.00 44.93  ? 138 THR   D OG1 1 
ATOM   4194 C CG2 . THR   D 1 138 ? -13.125 -31.994 67.208 1.00 43.33  ? 138 THR   D CG2 1 
ATOM   4195 N N   . VAL   D 1 139 ? -13.945 -31.210 70.286 1.00 45.73  ? 139 VAL   D N   1 
ATOM   4196 C CA  . VAL   D 1 139 ? -13.648 -31.777 71.604 1.00 47.94  ? 139 VAL   D CA  1 
ATOM   4197 C C   . VAL   D 1 139 ? -13.424 -33.287 71.461 1.00 50.72  ? 139 VAL   D C   1 
ATOM   4198 O O   . VAL   D 1 139 ? -14.206 -33.978 70.793 1.00 52.25  ? 139 VAL   D O   1 
ATOM   4199 C CB  . VAL   D 1 139 ? -14.768 -31.477 72.625 1.00 48.47  ? 139 VAL   D CB  1 
ATOM   4200 C CG1 . VAL   D 1 139 ? -14.453 -32.101 73.972 1.00 58.22  ? 139 VAL   D CG1 1 
ATOM   4201 C CG2 . VAL   D 1 139 ? -14.981 -29.985 72.779 1.00 55.04  ? 139 VAL   D CG2 1 
ATOM   4202 N N   . TYR   D 1 140 ? -12.354 -33.791 72.086 1.00 49.21  ? 140 TYR   D N   1 
ATOM   4203 C CA  . TYR   D 1 140 ? -12.021 -35.213 72.148 1.00 45.48  ? 140 TYR   D CA  1 
ATOM   4204 C C   . TYR   D 1 140 ? -11.913 -35.670 73.606 1.00 52.51  ? 140 TYR   D C   1 
ATOM   4205 O O   . TYR   D 1 140 ? -11.487 -34.908 74.485 1.00 46.65  ? 140 TYR   D O   1 
ATOM   4206 C CB  . TYR   D 1 140 ? -10.690 -35.506 71.417 1.00 42.95  ? 140 TYR   D CB  1 
ATOM   4207 C CG  . TYR   D 1 140 ? -10.695 -35.144 69.952 1.00 49.50  ? 140 TYR   D CG  1 
ATOM   4208 C CD1 . TYR   D 1 140 ? -11.204 -36.026 69.005 1.00 38.35  ? 140 TYR   D CD1 1 
ATOM   4209 C CD2 . TYR   D 1 140 ? -10.194 -33.916 69.511 1.00 46.00  ? 140 TYR   D CD2 1 
ATOM   4210 C CE1 . TYR   D 1 140 ? -11.223 -35.700 67.669 1.00 41.01  ? 140 TYR   D CE1 1 
ATOM   4211 C CE2 . TYR   D 1 140 ? -10.206 -33.582 68.165 1.00 46.85  ? 140 TYR   D CE2 1 
ATOM   4212 C CZ  . TYR   D 1 140 ? -10.722 -34.481 67.250 1.00 45.94  ? 140 TYR   D CZ  1 
ATOM   4213 O OH  . TYR   D 1 140 ? -10.737 -34.158 65.912 1.00 49.81  ? 140 TYR   D OH  1 
ATOM   4214 N N   . THR   D 1 141 ? -12.303 -36.922 73.872 1.00 58.14  ? 141 THR   D N   1 
ATOM   4215 C CA  . THR   D 1 141 ? -12.107 -37.536 75.185 1.00 57.16  ? 141 THR   D CA  1 
ATOM   4216 C C   . THR   D 1 141 ? -11.407 -38.875 75.010 1.00 61.23  ? 141 THR   D C   1 
ATOM   4217 O O   . THR   D 1 141 ? -11.913 -39.750 74.302 1.00 66.78  ? 141 THR   D O   1 
ATOM   4218 C CB  . THR   D 1 141 ? -13.426 -37.737 75.947 1.00 59.22  ? 141 THR   D CB  1 
ATOM   4219 O OG1 . THR   D 1 141 ? -14.431 -38.252 75.066 1.00 63.11  ? 141 THR   D OG1 1 
ATOM   4220 C CG2 . THR   D 1 141 ? -13.899 -36.430 76.546 1.00 57.60  ? 141 THR   D CG2 1 
ATOM   4221 N N   . LYS   D 1 142 ? -10.251 -39.028 75.652 1.00 62.79  ? 142 LYS   D N   1 
ATOM   4222 C CA  . LYS   D 1 142 ? -9.488  -40.270 75.617 1.00 59.62  ? 142 LYS   D CA  1 
ATOM   4223 C C   . LYS   D 1 142 ? -10.084 -41.285 76.580 1.00 64.13  ? 142 LYS   D C   1 
ATOM   4224 O O   . LYS   D 1 142 ? -9.651  -41.394 77.731 1.00 59.38  ? 142 LYS   D O   1 
ATOM   4225 C CB  . LYS   D 1 142 ? -8.025  -40.016 75.979 1.00 64.45  ? 142 LYS   D CB  1 
ATOM   4226 C CG  . LYS   D 1 142 ? -7.111  -39.709 74.810 1.00 60.09  ? 142 LYS   D CG  1 
ATOM   4227 C CD  . LYS   D 1 142 ? -5.917  -38.921 75.311 1.00 63.27  ? 142 LYS   D CD  1 
ATOM   4228 C CE  . LYS   D 1 142 ? -4.701  -39.064 74.426 1.00 65.30  ? 142 LYS   D CE  1 
ATOM   4229 N NZ  . LYS   D 1 142 ? -3.514  -38.497 75.126 1.00 66.94  ? 142 LYS   D NZ  1 
HETATM 4230 N N1  . A1EEB E 2 .   ? 6.603   -18.475 17.893 1.00 45.36  ? 201 A1EEB B N1  1 
HETATM 4231 C C1  . A1EEB E 2 .   ? 6.474   -17.213 18.326 1.00 40.31  ? 201 A1EEB B C1  1 
HETATM 4232 C C2  . A1EEB E 2 .   ? 7.480   -17.021 16.166 1.00 58.86  ? 201 A1EEB B C2  1 
HETATM 4233 C C3  . A1EEB E 2 .   ? 8.135   -16.376 15.116 1.00 59.87  ? 201 A1EEB B C3  1 
HETATM 4234 C C4  . A1EEB E 2 .   ? 8.445   -15.052 15.315 1.00 51.38  ? 201 A1EEB B C4  1 
HETATM 4235 C C5  . A1EEB E 2 .   ? 8.150   -14.355 16.463 1.00 55.90  ? 201 A1EEB B C5  1 
HETATM 4236 C C6  . A1EEB E 2 .   ? 7.498   -15.009 17.501 1.00 56.89  ? 201 A1EEB B C6  1 
HETATM 4237 C C7  . A1EEB E 2 .   ? 7.167   -16.345 17.345 1.00 54.59  ? 201 A1EEB B C7  1 
HETATM 4238 O O1  . A1EEB E 2 .   ? 5.902   -16.849 19.325 1.00 34.19  ? 201 A1EEB B O1  1 
HETATM 4239 F F1  . A1EEB E 2 .   ? 9.084   -14.393 14.312 1.00 51.85  ? 201 A1EEB B F1  1 
HETATM 4240 S S1  . A1EEB E 2 .   ? 6.958   -18.672 16.227 1.00 74.35  ? 201 A1EEB B S1  1 
HETATM 4241 N N1  . A1EEB F 2 .   ? 10.341  -11.315 45.966 1.00 53.58  ? 201 A1EEB A N1  1 
HETATM 4242 C C1  . A1EEB F 2 .   ? 9.299   -11.113 45.148 1.00 46.95  ? 201 A1EEB A C1  1 
HETATM 4243 C C2  . A1EEB F 2 .   ? 8.326   -11.487 47.299 1.00 52.49  ? 201 A1EEB A C2  1 
HETATM 4244 C C3  . A1EEB F 2 .   ? 7.299   -11.744 48.208 1.00 51.93  ? 201 A1EEB A C3  1 
HETATM 4245 C C4  . A1EEB F 2 .   ? 6.040   -11.893 47.677 1.00 43.06  ? 201 A1EEB A C4  1 
HETATM 4246 C C5  . A1EEB F 2 .   ? 5.754   -11.802 46.335 1.00 52.09  ? 201 A1EEB A C5  1 
HETATM 4247 C C6  . A1EEB F 2 .   ? 6.786   -11.546 45.440 1.00 53.77  ? 201 A1EEB A C6  1 
HETATM 4248 C C7  . A1EEB F 2 .   ? 8.072   -11.390 45.931 1.00 49.34  ? 201 A1EEB A C7  1 
HETATM 4249 O O1  . A1EEB F 2 .   ? 9.347   -10.769 43.991 1.00 41.83  ? 201 A1EEB A O1  1 
HETATM 4250 F F1  . A1EEB F 2 .   ? 5.016   -12.144 48.535 1.00 45.15  ? 201 A1EEB A F1  1 
HETATM 4251 S S1  . A1EEB F 2 .   ? 10.008  -11.253 47.647 1.00 76.18  ? 201 A1EEB A S1  1 
HETATM 4252 N N1  . A1EEB G 2 .   ? -8.212  -20.050 83.283 1.00 45.94  ? 201 A1EEB D N1  1 
HETATM 4253 C C1  . A1EEB G 2 .   ? -7.587  -18.881 83.090 1.00 58.22  ? 201 A1EEB D C1  1 
HETATM 4254 C C2  . A1EEB G 2 .   ? -7.631  -19.166 85.463 1.00 55.63  ? 201 A1EEB D C2  1 
HETATM 4255 C C3  . A1EEB G 2 .   ? -7.282  -18.898 86.786 1.00 54.84  ? 201 A1EEB D C3  1 
HETATM 4256 C C4  . A1EEB G 2 .   ? -6.381  -17.880 86.984 1.00 48.58  ? 201 A1EEB D C4  1 
HETATM 4257 C C5  . A1EEB G 2 .   ? -5.823  -17.137 85.970 1.00 57.43  ? 201 A1EEB D C5  1 
HETATM 4258 C C6  . A1EEB G 2 .   ? -6.177  -17.415 84.656 1.00 60.89  ? 201 A1EEB D C6  1 
HETATM 4259 C C7  . A1EEB G 2 .   ? -7.083  -18.434 84.410 1.00 63.45  ? 201 A1EEB D C7  1 
HETATM 4260 O O1  . A1EEB G 2 .   ? -7.456  -18.299 82.039 1.00 58.86  ? 201 A1EEB D O1  1 
HETATM 4261 F F1  . A1EEB G 2 .   ? -6.020  -17.591 88.263 1.00 60.79  ? 201 A1EEB D F1  1 
HETATM 4262 S S1  . A1EEB G 2 .   ? -8.730  -20.376 84.886 1.00 46.80  ? 201 A1EEB D S1  1 
HETATM 4263 O O   . HOH   H 3 .   ? -1.045  -3.658  14.515 1.00 51.22  ? 301 HOH   B O   1 
HETATM 4264 O O   . HOH   H 3 .   ? 24.609  -0.963  31.378 1.00 30.14  ? 302 HOH   B O   1 
HETATM 4265 O O   . HOH   H 3 .   ? -1.494  -13.184 15.732 1.00 30.87  ? 303 HOH   B O   1 
HETATM 4266 O O   . HOH   H 3 .   ? 6.953   3.026   43.979 1.00 40.65  ? 304 HOH   B O   1 
HETATM 4267 O O   . HOH   H 3 .   ? 18.767  -17.385 25.299 1.00 22.93  ? 305 HOH   B O   1 
HETATM 4268 O O   . HOH   H 3 .   ? 13.501  -21.306 22.686 1.00 27.78  ? 306 HOH   B O   1 
HETATM 4269 O O   . HOH   H 3 .   ? 22.763  -15.456 42.989 1.00 21.20  ? 307 HOH   B O   1 
HETATM 4270 O O   . HOH   H 3 .   ? -11.427 -18.305 33.962 1.00 41.69  ? 308 HOH   B O   1 
HETATM 4271 O O   . HOH   H 3 .   ? 23.167  -4.773  52.576 1.00 26.08  ? 309 HOH   B O   1 
HETATM 4272 O O   . HOH   H 3 .   ? 24.263  -15.499 33.512 1.00 30.69  ? 310 HOH   B O   1 
HETATM 4273 O O   . HOH   H 3 .   ? 11.564  -21.872 18.529 1.00 38.18  ? 311 HOH   B O   1 
HETATM 4274 O O   . HOH   H 3 .   ? 22.035  -2.290  28.970 1.00 33.41  ? 312 HOH   B O   1 
HETATM 4275 O O   . HOH   H 3 .   ? 21.667  3.552   36.292 1.00 22.59  ? 313 HOH   B O   1 
HETATM 4276 O O   . HOH   H 3 .   ? 1.148   -4.586  13.137 1.00 42.39  ? 314 HOH   B O   1 
HETATM 4277 O O   . HOH   H 3 .   ? 19.504  -10.548 22.312 1.00 34.88  ? 315 HOH   B O   1 
HETATM 4278 O O   . HOH   H 3 .   ? 4.945   -4.568  19.215 1.00 25.42  ? 316 HOH   B O   1 
HETATM 4279 O O   . HOH   H 3 .   ? 27.726  -3.283  54.420 1.00 51.87  ? 317 HOH   B O   1 
HETATM 4280 O O   . HOH   H 3 .   ? 18.182  -19.733 25.686 1.00 29.57  ? 318 HOH   B O   1 
HETATM 4281 O O   . HOH   H 3 .   ? -5.907  -10.504 40.564 1.00 35.98  ? 319 HOH   B O   1 
HETATM 4282 O O   . HOH   H 3 .   ? 15.779  -22.712 23.074 1.00 41.09  ? 320 HOH   B O   1 
HETATM 4283 O O   . HOH   H 3 .   ? 30.120  -7.260  46.741 1.00 19.89  ? 321 HOH   B O   1 
HETATM 4284 O O   . HOH   H 3 .   ? 15.696  -19.842 46.171 1.00 27.23  ? 322 HOH   B O   1 
HETATM 4285 O O   . HOH   H 3 .   ? 7.753   -8.854  19.780 1.00 28.58  ? 323 HOH   B O   1 
HETATM 4286 O O   . HOH   H 3 .   ? 24.242  -13.656 29.306 1.00 37.11  ? 324 HOH   B O   1 
HETATM 4287 O O   . HOH   H 3 .   ? 19.908  -17.307 34.149 1.00 16.84  ? 325 HOH   B O   1 
HETATM 4288 O O   . HOH   H 3 .   ? -1.964  -20.907 40.649 1.00 30.69  ? 326 HOH   B O   1 
HETATM 4289 O O   . HOH   H 3 .   ? 23.224  -12.448 35.870 1.00 20.95  ? 327 HOH   B O   1 
HETATM 4290 O O   . HOH   H 3 .   ? -7.827  -11.794 24.750 1.00 26.99  ? 328 HOH   B O   1 
HETATM 4291 O O   . HOH   H 3 .   ? 18.835  -3.543  30.425 1.00 17.05  ? 329 HOH   B O   1 
HETATM 4292 O O   . HOH   H 3 .   ? 17.240  -25.046 27.613 1.00 35.95  ? 330 HOH   B O   1 
HETATM 4293 O O   . HOH   H 3 .   ? 18.743  0.610   36.013 1.00 19.38  ? 331 HOH   B O   1 
HETATM 4294 O O   . HOH   H 3 .   ? 20.067  -22.489 45.800 1.00 23.77  ? 332 HOH   B O   1 
HETATM 4295 O O   . HOH   H 3 .   ? 20.513  4.420   51.446 1.00 31.22  ? 333 HOH   B O   1 
HETATM 4296 O O   . HOH   H 3 .   ? -2.099  -23.976 46.784 1.00 40.64  ? 334 HOH   B O   1 
HETATM 4297 O O   . HOH   H 3 .   ? 30.490  -2.854  52.414 1.00 27.73  ? 335 HOH   B O   1 
HETATM 4298 O O   . HOH   H 3 .   ? 20.599  -3.455  53.786 1.00 34.98  ? 336 HOH   B O   1 
HETATM 4299 O O   . HOH   H 3 .   ? 15.432  -3.297  57.374 1.00 23.10  ? 337 HOH   B O   1 
HETATM 4300 O O   . HOH   H 3 .   ? 26.236  -3.707  30.881 1.00 36.55  ? 338 HOH   B O   1 
HETATM 4301 O O   . HOH   H 3 .   ? 16.301  6.308   35.289 1.00 40.24  ? 339 HOH   B O   1 
HETATM 4302 O O   . HOH   H 3 .   ? 5.449   -9.888  18.760 1.00 27.38  ? 340 HOH   B O   1 
HETATM 4303 O O   . HOH   H 3 .   ? -0.614  -2.438  23.697 1.00 25.05  ? 341 HOH   B O   1 
HETATM 4304 O O   . HOH   H 3 .   ? 18.079  3.708   41.676 1.00 20.96  ? 342 HOH   B O   1 
HETATM 4305 O O   . HOH   H 3 .   ? 0.510   -7.124  14.478 1.00 34.39  ? 343 HOH   B O   1 
HETATM 4306 O O   . HOH   H 3 .   ? -6.205  -18.124 39.220 1.00 29.84  ? 344 HOH   B O   1 
HETATM 4307 O O   . HOH   H 3 .   ? 22.289  -11.000 27.998 1.00 26.72  ? 345 HOH   B O   1 
HETATM 4308 O O   . HOH   H 3 .   ? 21.312  -19.592 33.990 1.00 21.62  ? 346 HOH   B O   1 
HETATM 4309 O O   . HOH   H 3 .   ? 17.708  -2.697  55.821 1.00 26.16  ? 347 HOH   B O   1 
HETATM 4310 O O   . HOH   H 3 .   ? -10.257 -12.496 30.447 1.00 30.64  ? 348 HOH   B O   1 
HETATM 4311 O O   . HOH   H 3 .   ? 20.355  -13.814 27.935 1.00 16.53  ? 349 HOH   B O   1 
HETATM 4312 O O   . HOH   H 3 .   ? 15.099  4.128   41.155 1.00 30.43  ? 350 HOH   B O   1 
HETATM 4313 O O   . HOH   H 3 .   ? 29.446  -0.116  52.463 1.00 27.34  ? 351 HOH   B O   1 
HETATM 4314 O O   . HOH   H 3 .   ? 18.476  -9.388  25.940 1.00 20.19  ? 352 HOH   B O   1 
HETATM 4315 O O   . HOH   H 3 .   ? -4.823  -11.780 15.775 1.00 34.60  ? 353 HOH   B O   1 
HETATM 4316 O O   . HOH   H 3 .   ? 25.821  -8.715  41.476 1.00 21.48  ? 354 HOH   B O   1 
HETATM 4317 O O   . HOH   H 3 .   ? 17.204  -20.714 43.760 1.00 30.79  ? 355 HOH   B O   1 
HETATM 4318 O O   . HOH   H 3 .   ? 15.941  7.889   49.399 1.00 47.23  ? 356 HOH   B O   1 
HETATM 4319 O O   . HOH   H 3 .   ? 18.251  -16.913 36.254 1.00 16.70  ? 357 HOH   B O   1 
HETATM 4320 O O   . HOH   H 3 .   ? 19.149  -14.843 48.691 1.00 14.66  ? 358 HOH   B O   1 
HETATM 4321 O O   . HOH   H 3 .   ? 8.399   -1.763  16.443 1.00 43.95  ? 359 HOH   B O   1 
HETATM 4322 O O   . HOH   H 3 .   ? -2.834  -16.066 21.769 1.00 23.21  ? 360 HOH   B O   1 
HETATM 4323 O O   . HOH   H 3 .   ? 18.869  -25.750 29.195 1.00 35.13  ? 361 HOH   B O   1 
HETATM 4324 O O   . HOH   H 3 .   ? 29.090  -1.557  37.507 1.00 27.25  ? 362 HOH   B O   1 
HETATM 4325 O O   . HOH   H 3 .   ? 27.709  -5.239  37.997 1.00 19.45  ? 363 HOH   B O   1 
HETATM 4326 O O   . HOH   H 3 .   ? 22.263  -5.110  59.419 1.00 55.28  ? 364 HOH   B O   1 
HETATM 4327 O O   . HOH   H 3 .   ? 2.979   -9.058  19.739 1.00 22.15  ? 365 HOH   B O   1 
HETATM 4328 O O   . HOH   H 3 .   ? -5.659  -2.613  30.869 1.00 35.97  ? 366 HOH   B O   1 
HETATM 4329 O O   . HOH   H 3 .   ? -2.983  -13.100 22.220 1.00 26.47  ? 367 HOH   B O   1 
HETATM 4330 O O   . HOH   H 3 .   ? 9.246   4.881   47.533 1.00 31.78  ? 368 HOH   B O   1 
HETATM 4331 O O   . HOH   H 3 .   ? -7.526  -12.259 36.839 1.00 44.22  ? 369 HOH   B O   1 
HETATM 4332 O O   . HOH   H 3 .   ? -4.433  -1.822  23.803 1.00 30.41  ? 370 HOH   B O   1 
HETATM 4333 O O   . HOH   H 3 .   ? 20.806  4.058   54.413 1.00 31.21  ? 371 HOH   B O   1 
HETATM 4334 O O   . HOH   H 3 .   ? 28.867  -0.428  32.663 1.00 34.15  ? 372 HOH   B O   1 
HETATM 4335 O O   . HOH   H 3 .   ? 20.679  -16.952 26.970 1.00 26.10  ? 373 HOH   B O   1 
HETATM 4336 O O   . HOH   H 3 .   ? 21.661  0.868   31.079 1.00 37.86  ? 374 HOH   B O   1 
HETATM 4337 O O   . HOH   H 3 .   ? 12.352  -7.764  53.879 1.00 40.84  ? 375 HOH   B O   1 
HETATM 4338 O O   . HOH   H 3 .   ? 26.223  -10.942 34.425 1.00 23.22  ? 376 HOH   B O   1 
HETATM 4339 O O   . HOH   H 3 .   ? 27.636  2.615   39.644 1.00 27.26  ? 377 HOH   B O   1 
HETATM 4340 O O   . HOH   H 3 .   ? 19.292  9.664   38.583 1.00 37.26  ? 378 HOH   B O   1 
HETATM 4341 O O   . HOH   H 3 .   ? 29.681  -3.856  38.435 1.00 35.64  ? 379 HOH   B O   1 
HETATM 4342 O O   . HOH   H 3 .   ? 21.070  -4.584  26.964 1.00 37.45  ? 380 HOH   B O   1 
HETATM 4343 O O   . HOH   H 3 .   ? 27.463  -9.046  33.259 1.00 49.60  ? 381 HOH   B O   1 
HETATM 4344 O O   . HOH   H 3 .   ? 28.779  4.293   40.930 1.00 28.99  ? 382 HOH   B O   1 
HETATM 4345 O O   . HOH   H 3 .   ? 24.143  9.896   45.709 1.00 28.96  ? 383 HOH   B O   1 
HETATM 4346 O O   . HOH   H 3 .   ? 24.962  -6.005  51.139 1.00 27.23  ? 384 HOH   B O   1 
HETATM 4347 O O   . HOH   H 3 .   ? 23.214  -22.294 27.878 1.00 35.42  ? 385 HOH   B O   1 
HETATM 4348 O O   . HOH   H 3 .   ? 11.447  -22.183 39.706 1.00 17.98  ? 386 HOH   B O   1 
HETATM 4349 O O   . HOH   H 3 .   ? 20.017  -16.287 37.964 1.00 22.30  ? 387 HOH   B O   1 
HETATM 4350 O O   . HOH   H 3 .   ? 20.880  -25.336 27.928 1.00 39.15  ? 388 HOH   B O   1 
HETATM 4351 O O   . HOH   H 3 .   ? 15.485  -20.591 26.304 1.00 23.14  ? 389 HOH   B O   1 
HETATM 4352 O O   . HOH   H 3 .   ? 22.485  -21.884 46.185 1.00 25.72  ? 390 HOH   B O   1 
HETATM 4353 O O   . HOH   H 3 .   ? 22.969  -19.212 46.534 1.00 30.22  ? 391 HOH   B O   1 
HETATM 4354 O O   . HOH   H 3 .   ? 21.765  -10.515 23.545 1.00 35.08  ? 392 HOH   B O   1 
HETATM 4355 O O   . HOH   H 3 .   ? 23.731  -15.241 47.087 1.00 29.58  ? 393 HOH   B O   1 
HETATM 4356 O O   . HOH   H 3 .   ? 24.469  -10.551 40.050 1.00 29.48  ? 394 HOH   B O   1 
HETATM 4357 O O   . HOH   H 3 .   ? 19.889  8.191   59.398 1.00 45.13  ? 395 HOH   B O   1 
HETATM 4358 O O   . HOH   H 3 .   ? 21.199  -9.352  26.216 1.00 26.93  ? 396 HOH   B O   1 
HETATM 4359 O O   . HOH   H 3 .   ? 20.648  1.931   33.419 1.00 35.42  ? 397 HOH   B O   1 
HETATM 4360 O O   . HOH   H 3 .   ? 3.595   -25.740 44.104 1.00 26.88  ? 398 HOH   B O   1 
HETATM 4361 O O   . HOH   H 3 .   ? 29.903  -8.580  40.176 1.00 35.49  ? 399 HOH   B O   1 
HETATM 4362 O O   . HOH   H 3 .   ? 23.975  -17.010 45.165 1.00 31.42  ? 400 HOH   B O   1 
HETATM 4363 O O   . HOH   H 3 .   ? 21.800  -15.991 48.495 1.00 29.24  ? 401 HOH   B O   1 
HETATM 4364 O O   . HOH   H 3 .   ? 27.818  -7.444  39.654 1.00 25.39  ? 402 HOH   B O   1 
HETATM 4365 O O   . HOH   I 3 .   ? -4.105  -36.434 20.514 1.00 58.77  ? 301 HOH   A O   1 
HETATM 4366 O O   . HOH   I 3 .   ? -13.446 -18.084 25.462 1.00 43.51  ? 302 HOH   A O   1 
HETATM 4367 O O   . HOH   I 3 .   ? 1.535   -1.755  48.331 1.00 37.08  ? 303 HOH   A O   1 
HETATM 4368 O O   . HOH   I 3 .   ? -10.940 -21.238 9.062  1.00 42.73  ? 304 HOH   A O   1 
HETATM 4369 O O   . HOH   I 3 .   ? -8.821  -22.042 26.331 1.00 23.59  ? 305 HOH   A O   1 
HETATM 4370 O O   . HOH   I 3 .   ? -6.912  -11.526 16.522 1.00 39.78  ? 306 HOH   A O   1 
HETATM 4371 O O   . HOH   I 3 .   ? 7.681   -27.094 31.704 1.00 24.42  ? 307 HOH   A O   1 
HETATM 4372 O O   . HOH   I 3 .   ? 6.800   -24.286 40.174 1.00 19.37  ? 308 HOH   A O   1 
HETATM 4373 O O   . HOH   I 3 .   ? -5.366  -21.801 32.736 1.00 20.31  ? 309 HOH   A O   1 
HETATM 4374 O O   . HOH   I 3 .   ? -7.857  -24.536 34.383 1.00 32.52  ? 310 HOH   A O   1 
HETATM 4375 O O   . HOH   I 3 .   ? -2.488  -1.695  46.839 1.00 31.13  ? 311 HOH   A O   1 
HETATM 4376 O O   . HOH   I 3 .   ? -9.057  -27.048 32.382 1.00 33.25  ? 312 HOH   A O   1 
HETATM 4377 O O   . HOH   I 3 .   ? -2.390  -6.734  41.257 1.00 17.00  ? 313 HOH   A O   1 
HETATM 4378 O O   . HOH   I 3 .   ? 0.351   -1.052  25.833 1.00 34.79  ? 314 HOH   A O   1 
HETATM 4379 O O   . HOH   I 3 .   ? 12.862  -27.144 21.936 1.00 35.01  ? 315 HOH   A O   1 
HETATM 4380 O O   . HOH   I 3 .   ? 16.864  -23.448 38.702 1.00 21.36  ? 316 HOH   A O   1 
HETATM 4381 O O   . HOH   I 3 .   ? 12.517  -26.177 53.122 1.00 30.91  ? 317 HOH   A O   1 
HETATM 4382 O O   . HOH   I 3 .   ? 5.550   8.555   30.684 1.00 48.42  ? 318 HOH   A O   1 
HETATM 4383 O O   . HOH   I 3 .   ? 9.848   -24.528 40.424 1.00 21.94  ? 319 HOH   A O   1 
HETATM 4384 O O   . HOH   I 3 .   ? 0.444   1.252   28.352 1.00 37.55  ? 320 HOH   A O   1 
HETATM 4385 O O   . HOH   I 3 .   ? 2.258   -5.901  41.748 1.00 16.20  ? 321 HOH   A O   1 
HETATM 4386 O O   . HOH   I 3 .   ? 8.232   -25.762 29.653 1.00 17.53  ? 322 HOH   A O   1 
HETATM 4387 O O   . HOH   I 3 .   ? 12.484  -28.609 38.407 1.00 21.63  ? 323 HOH   A O   1 
HETATM 4388 O O   . HOH   I 3 .   ? -2.148  -1.702  35.932 1.00 22.38  ? 324 HOH   A O   1 
HETATM 4389 O O   . HOH   I 3 .   ? 0.234   -5.926  51.536 1.00 38.88  ? 325 HOH   A O   1 
HETATM 4390 O O   . HOH   I 3 .   ? -11.594 -14.190 13.725 1.00 54.32  ? 326 HOH   A O   1 
HETATM 4391 O O   . HOH   I 3 .   ? 5.271   4.810   42.225 1.00 32.79  ? 327 HOH   A O   1 
HETATM 4392 O O   . HOH   I 3 .   ? 2.603   -29.346 36.693 1.00 26.78  ? 328 HOH   A O   1 
HETATM 4393 O O   . HOH   I 3 .   ? -2.233  -30.598 11.972 1.00 43.94  ? 329 HOH   A O   1 
HETATM 4394 O O   . HOH   I 3 .   ? 13.682  -19.239 25.028 1.00 16.24  ? 330 HOH   A O   1 
HETATM 4395 O O   . HOH   I 3 .   ? 8.621   2.563   35.377 1.00 25.60  ? 331 HOH   A O   1 
HETATM 4396 O O   . HOH   I 3 .   ? -0.473  -31.324 31.528 1.00 25.58  ? 332 HOH   A O   1 
HETATM 4397 O O   . HOH   I 3 .   ? -5.194  -16.079 44.263 1.00 29.07  ? 333 HOH   A O   1 
HETATM 4398 O O   . HOH   I 3 .   ? 8.139   -1.896  39.339 1.00 17.32  ? 334 HOH   A O   1 
HETATM 4399 O O   . HOH   I 3 .   ? 2.405   -29.286 29.423 1.00 18.15  ? 335 HOH   A O   1 
HETATM 4400 O O   . HOH   I 3 .   ? 0.786   -10.598 42.515 1.00 14.94  ? 336 HOH   A O   1 
HETATM 4401 O O   . HOH   I 3 .   ? 10.906  3.980   30.206 1.00 24.38  ? 337 HOH   A O   1 
HETATM 4402 O O   . HOH   I 3 .   ? -1.070  -32.057 24.041 1.00 24.34  ? 338 HOH   A O   1 
HETATM 4403 O O   . HOH   I 3 .   ? 3.416   -25.449 37.130 1.00 16.20  ? 339 HOH   A O   1 
HETATM 4404 O O   . HOH   I 3 .   ? 11.078  -2.326  40.238 1.00 20.21  ? 340 HOH   A O   1 
HETATM 4405 O O   . HOH   I 3 .   ? -10.595 -21.258 20.110 1.00 26.60  ? 341 HOH   A O   1 
HETATM 4406 O O   . HOH   I 3 .   ? 12.193  -1.890  20.838 1.00 38.26  ? 342 HOH   A O   1 
HETATM 4407 O O   . HOH   I 3 .   ? -7.638  -29.136 33.514 1.00 28.77  ? 343 HOH   A O   1 
HETATM 4408 O O   . HOH   I 3 .   ? 10.289  -21.188 51.176 1.00 33.31  ? 344 HOH   A O   1 
HETATM 4409 O O   . HOH   I 3 .   ? 18.808  -8.002  23.109 1.00 30.50  ? 345 HOH   A O   1 
HETATM 4410 O O   . HOH   I 3 .   ? -10.961 -31.220 30.798 1.00 44.33  ? 346 HOH   A O   1 
HETATM 4411 O O   . HOH   I 3 .   ? 9.908   -20.168 39.146 1.00 9.47   ? 347 HOH   A O   1 
HETATM 4412 O O   . HOH   I 3 .   ? 6.347   -31.281 23.807 1.00 33.55  ? 348 HOH   A O   1 
HETATM 4413 O O   . HOH   I 3 .   ? -5.531  -35.270 10.537 1.00 44.52  ? 349 HOH   A O   1 
HETATM 4414 O O   . HOH   I 3 .   ? 14.952  -4.497  17.990 1.00 29.60  ? 350 HOH   A O   1 
HETATM 4415 O O   . HOH   I 3 .   ? 6.984   -2.245  46.358 1.00 27.47  ? 351 HOH   A O   1 
HETATM 4416 O O   . HOH   I 3 .   ? 0.400   -26.563 37.011 1.00 26.21  ? 352 HOH   A O   1 
HETATM 4417 O O   . HOH   I 3 .   ? -4.056  -2.250  50.806 1.00 40.42  ? 353 HOH   A O   1 
HETATM 4418 O O   . HOH   I 3 .   ? 12.508  -26.566 40.152 1.00 25.51  ? 354 HOH   A O   1 
HETATM 4419 O O   . HOH   I 3 .   ? -0.681  -21.982 38.083 1.00 17.58  ? 355 HOH   A O   1 
HETATM 4420 O O   . HOH   I 3 .   ? -6.643  -8.464  43.745 1.00 26.82  ? 356 HOH   A O   1 
HETATM 4421 O O   . HOH   I 3 .   ? -1.255  -32.367 28.338 1.00 39.83  ? 357 HOH   A O   1 
HETATM 4422 O O   . HOH   I 3 .   ? 9.861   -28.925 33.130 1.00 22.71  ? 358 HOH   A O   1 
HETATM 4423 O O   . HOH   I 3 .   ? 0.116   0.276   44.211 1.00 41.55  ? 359 HOH   A O   1 
HETATM 4424 O O   . HOH   I 3 .   ? 0.036   -2.202  46.295 1.00 27.35  ? 360 HOH   A O   1 
HETATM 4425 O O   . HOH   I 3 .   ? -3.001  -28.569 10.790 1.00 70.71  ? 361 HOH   A O   1 
HETATM 4426 O O   . HOH   I 3 .   ? -1.884  1.942   35.021 1.00 28.96  ? 362 HOH   A O   1 
HETATM 4427 O O   . HOH   I 3 .   ? 3.112   -33.935 19.057 1.00 38.41  ? 363 HOH   A O   1 
HETATM 4428 O O   . HOH   I 3 .   ? 2.281   -8.173  43.270 1.00 16.29  ? 364 HOH   A O   1 
HETATM 4429 O O   . HOH   I 3 .   ? 6.385   -26.599 38.624 1.00 29.65  ? 365 HOH   A O   1 
HETATM 4430 O O   . HOH   I 3 .   ? 6.684   -27.504 27.692 1.00 22.06  ? 366 HOH   A O   1 
HETATM 4431 O O   . HOH   I 3 .   ? -2.667  0.667   45.025 1.00 32.42  ? 367 HOH   A O   1 
HETATM 4432 O O   . HOH   I 3 .   ? 4.134   -3.049  49.047 1.00 38.06  ? 368 HOH   A O   1 
HETATM 4433 O O   . HOH   I 3 .   ? 6.899   -33.979 22.535 1.00 44.36  ? 369 HOH   A O   1 
HETATM 4434 O O   . HOH   I 3 .   ? -7.168  -14.522 10.764 1.00 38.21  ? 370 HOH   A O   1 
HETATM 4435 O O   . HOH   I 3 .   ? -13.678 -21.045 24.991 1.00 41.08  ? 371 HOH   A O   1 
HETATM 4436 O O   . HOH   I 3 .   ? -12.536 -30.506 23.946 1.00 25.18  ? 372 HOH   A O   1 
HETATM 4437 O O   . HOH   I 3 .   ? 9.698   -30.830 31.586 1.00 42.37  ? 373 HOH   A O   1 
HETATM 4438 O O   . HOH   I 3 .   ? 12.727  -22.367 42.698 1.00 20.49  ? 374 HOH   A O   1 
HETATM 4439 O O   . HOH   I 3 .   ? 6.063   5.801   34.438 1.00 36.10  ? 375 HOH   A O   1 
HETATM 4440 O O   . HOH   I 3 .   ? -5.311  -32.402 27.109 1.00 23.71  ? 376 HOH   A O   1 
HETATM 4441 O O   . HOH   I 3 .   ? -8.580  -0.670  38.217 1.00 50.74  ? 377 HOH   A O   1 
HETATM 4442 O O   . HOH   I 3 .   ? -4.721  -32.902 29.479 1.00 31.83  ? 378 HOH   A O   1 
HETATM 4443 O O   . HOH   I 3 .   ? 18.673  -19.070 48.585 1.00 34.04  ? 379 HOH   A O   1 
HETATM 4444 O O   . HOH   I 3 .   ? 5.551   8.863   28.208 1.00 39.89  ? 380 HOH   A O   1 
HETATM 4445 O O   . HOH   I 3 .   ? 17.657  -16.869 49.316 1.00 28.05  ? 381 HOH   A O   1 
HETATM 4446 O O   . HOH   I 3 .   ? 8.963   8.854   31.167 1.00 50.12  ? 382 HOH   A O   1 
HETATM 4447 O O   . HOH   I 3 .   ? -8.800  -14.950 46.523 1.00 46.69  ? 383 HOH   A O   1 
HETATM 4448 O O   . HOH   I 3 .   ? 13.551  -30.959 31.951 1.00 26.08  ? 384 HOH   A O   1 
HETATM 4449 O O   . HOH   I 3 .   ? 13.304  -24.024 40.116 1.00 38.45  ? 385 HOH   A O   1 
HETATM 4450 O O   . HOH   I 3 .   ? -5.111  -7.750  41.716 1.00 34.74  ? 386 HOH   A O   1 
HETATM 4451 O O   . HOH   I 3 .   ? 5.086   -29.293 28.295 1.00 26.05  ? 387 HOH   A O   1 
HETATM 4452 O O   . HOH   I 3 .   ? 0.898   -30.668 25.438 1.00 32.32  ? 388 HOH   A O   1 
HETATM 4453 O O   . HOH   I 3 .   ? -1.337  -24.592 37.962 1.00 29.54  ? 389 HOH   A O   1 
HETATM 4454 O O   . HOH   I 3 .   ? 10.342  -26.608 52.985 1.00 47.50  ? 390 HOH   A O   1 
HETATM 4455 O O   . HOH   I 3 .   ? 3.854   -31.692 25.352 1.00 40.29  ? 391 HOH   A O   1 
HETATM 4456 O O   . HOH   I 3 .   ? 1.051   -31.602 28.420 1.00 44.18  ? 392 HOH   A O   1 
HETATM 4457 O O   . HOH   I 3 .   ? -2.917  -33.051 25.711 1.00 28.16  ? 393 HOH   A O   1 
HETATM 4458 O O   . HOH   I 3 .   ? -4.141  -25.318 37.658 1.00 41.52  ? 394 HOH   A O   1 
HETATM 4459 O O   . HOH   I 3 .   ? 6.259   -25.147 42.721 1.00 19.89  ? 395 HOH   A O   1 
HETATM 4460 O O   . HOH   I 3 .   ? 10.893  -24.520 42.770 1.00 22.76  ? 396 HOH   A O   1 
HETATM 4461 O O   . HOH   I 3 .   ? -9.635  -33.210 30.641 1.00 45.50  ? 397 HOH   A O   1 
HETATM 4462 O O   . HOH   J 3 .   ? 3.935   -30.274 69.314 1.00 39.92  ? 201 HOH   C O   1 
HETATM 4463 O O   . HOH   J 3 .   ? 8.914   4.646   52.458 1.00 42.23  ? 202 HOH   C O   1 
HETATM 4464 O O   . HOH   J 3 .   ? -9.837  -0.787  58.704 1.00 43.38  ? 203 HOH   C O   1 
HETATM 4465 O O   . HOH   J 3 .   ? 4.747   5.463   77.883 1.00 27.39  ? 204 HOH   C O   1 
HETATM 4466 O O   . HOH   J 3 .   ? -8.852  -0.883  66.578 1.00 36.90  ? 205 HOH   C O   1 
HETATM 4467 O O   . HOH   J 3 .   ? -1.261  -25.825 84.991 1.00 36.34  ? 206 HOH   C O   1 
HETATM 4468 O O   . HOH   J 3 .   ? 11.051  -5.075  55.791 1.00 41.34  ? 207 HOH   C O   1 
HETATM 4469 O O   . HOH   J 3 .   ? -8.088  1.279   77.695 1.00 38.00  ? 208 HOH   C O   1 
HETATM 4470 O O   . HOH   J 3 .   ? 8.574   1.910   72.281 1.00 20.53  ? 209 HOH   C O   1 
HETATM 4471 O O   . HOH   J 3 .   ? -10.134 -5.492  78.989 1.00 34.00  ? 210 HOH   C O   1 
HETATM 4472 O O   . HOH   J 3 .   ? 6.404   6.855   54.819 1.00 46.08  ? 211 HOH   C O   1 
HETATM 4473 O O   . HOH   J 3 .   ? -2.021  -3.678  80.130 1.00 17.77  ? 212 HOH   C O   1 
HETATM 4474 O O   . HOH   J 3 .   ? 8.041   -23.300 87.572 1.00 29.57  ? 213 HOH   C O   1 
HETATM 4475 O O   . HOH   J 3 .   ? 3.859   -0.663  77.037 1.00 17.85  ? 214 HOH   C O   1 
HETATM 4476 O O   . HOH   J 3 .   ? 3.774   -22.539 87.604 1.00 26.95  ? 215 HOH   C O   1 
HETATM 4477 O O   . HOH   J 3 .   ? 13.300  2.945   71.048 1.00 45.43  ? 216 HOH   C O   1 
HETATM 4478 O O   . HOH   J 3 .   ? 1.898   -19.775 82.791 1.00 21.09  ? 217 HOH   C O   1 
HETATM 4479 O O   . HOH   J 3 .   ? 4.248   2.307   79.339 1.00 32.78  ? 218 HOH   C O   1 
HETATM 4480 O O   . HOH   J 3 .   ? -4.895  2.614   70.848 1.00 27.27  ? 219 HOH   C O   1 
HETATM 4481 O O   . HOH   J 3 .   ? -7.706  -21.037 53.047 1.00 51.77  ? 220 HOH   C O   1 
HETATM 4482 O O   . HOH   J 3 .   ? 8.924   15.133  65.505 1.00 32.49  ? 221 HOH   C O   1 
HETATM 4483 O O   . HOH   J 3 .   ? -1.619  7.460   66.863 1.00 25.94  ? 222 HOH   C O   1 
HETATM 4484 O O   . HOH   J 3 .   ? 11.634  -20.526 69.359 1.00 28.50  ? 223 HOH   C O   1 
HETATM 4485 O O   . HOH   J 3 .   ? 3.072   -29.027 74.748 1.00 36.32  ? 224 HOH   C O   1 
HETATM 4486 O O   . HOH   J 3 .   ? -2.589  -26.525 78.402 1.00 33.39  ? 225 HOH   C O   1 
HETATM 4487 O O   . HOH   J 3 .   ? 5.041   -18.892 94.254 1.00 50.31  ? 226 HOH   C O   1 
HETATM 4488 O O   . HOH   J 3 .   ? 0.786   -15.065 83.741 1.00 22.17  ? 227 HOH   C O   1 
HETATM 4489 O O   . HOH   J 3 .   ? 6.178   16.285  59.919 1.00 42.77  ? 228 HOH   C O   1 
HETATM 4490 O O   . HOH   J 3 .   ? 5.576   -16.639 84.484 1.00 16.25  ? 229 HOH   C O   1 
HETATM 4491 O O   . HOH   J 3 .   ? 3.112   -24.321 59.161 1.00 34.38  ? 230 HOH   C O   1 
HETATM 4492 O O   . HOH   J 3 .   ? -11.440 -1.460  70.943 1.00 35.75  ? 231 HOH   C O   1 
HETATM 4493 O O   . HOH   J 3 .   ? -12.402 -6.619  78.364 1.00 37.52  ? 232 HOH   C O   1 
HETATM 4494 O O   . HOH   J 3 .   ? -4.311  1.509   57.480 1.00 34.20  ? 233 HOH   C O   1 
HETATM 4495 O O   . HOH   J 3 .   ? 1.389   2.380   45.626 1.00 36.54  ? 234 HOH   C O   1 
HETATM 4496 O O   . HOH   J 3 .   ? -9.650  -3.027  60.162 1.00 48.09  ? 235 HOH   C O   1 
HETATM 4497 O O   . HOH   J 3 .   ? 13.795  8.385   58.168 1.00 49.31  ? 236 HOH   C O   1 
HETATM 4498 O O   . HOH   J 3 .   ? 8.688   2.926   50.367 1.00 33.61  ? 237 HOH   C O   1 
HETATM 4499 O O   . HOH   J 3 .   ? -4.511  5.364   73.566 1.00 27.97  ? 238 HOH   C O   1 
HETATM 4500 O O   . HOH   J 3 .   ? -7.782  -2.916  68.851 1.00 27.01  ? 239 HOH   C O   1 
HETATM 4501 O O   . HOH   J 3 .   ? 12.292  -15.018 94.436 1.00 47.69  ? 240 HOH   C O   1 
HETATM 4502 O O   . HOH   J 3 .   ? -4.714  0.138   78.624 1.00 33.19  ? 241 HOH   C O   1 
HETATM 4503 O O   . HOH   J 3 .   ? 7.536   2.209   78.631 1.00 37.09  ? 242 HOH   C O   1 
HETATM 4504 O O   . HOH   J 3 .   ? 0.254   -17.955 84.291 1.00 21.11  ? 243 HOH   C O   1 
HETATM 4505 O O   . HOH   J 3 .   ? -6.622  -2.411  77.739 1.00 25.40  ? 244 HOH   C O   1 
HETATM 4506 O O   . HOH   J 3 .   ? 9.725   -20.253 79.370 1.00 18.94  ? 245 HOH   C O   1 
HETATM 4507 O O   . HOH   J 3 .   ? -8.954  -1.967  70.596 1.00 30.03  ? 246 HOH   C O   1 
HETATM 4508 O O   . HOH   J 3 .   ? -0.052  -25.469 78.306 1.00 21.70  ? 247 HOH   C O   1 
HETATM 4509 O O   . HOH   J 3 .   ? 4.990   10.796  73.507 1.00 38.12  ? 248 HOH   C O   1 
HETATM 4510 O O   . HOH   J 3 .   ? 0.935   9.294   71.677 1.00 27.30  ? 249 HOH   C O   1 
HETATM 4511 O O   . HOH   J 3 .   ? 5.592   -24.605 86.162 1.00 30.35  ? 250 HOH   C O   1 
HETATM 4512 O O   . HOH   J 3 .   ? 2.568   -7.550  87.875 1.00 27.93  ? 251 HOH   C O   1 
HETATM 4513 O O   . HOH   J 3 .   ? 3.740   -25.404 63.348 1.00 32.43  ? 252 HOH   C O   1 
HETATM 4514 O O   . HOH   J 3 .   ? 6.386   -26.914 83.364 1.00 33.51  ? 253 HOH   C O   1 
HETATM 4515 O O   . HOH   J 3 .   ? 11.437  -23.465 78.505 1.00 32.48  ? 254 HOH   C O   1 
HETATM 4516 O O   . HOH   J 3 .   ? 11.440  -22.241 71.590 1.00 36.35  ? 255 HOH   C O   1 
HETATM 4517 O O   . HOH   J 3 .   ? 3.005   0.257   80.703 1.00 31.63  ? 256 HOH   C O   1 
HETATM 4518 O O   . HOH   J 3 .   ? 8.448   11.583  71.219 1.00 31.94  ? 257 HOH   C O   1 
HETATM 4519 O O   . HOH   J 3 .   ? 16.950  -2.988  60.119 1.00 25.66  ? 258 HOH   C O   1 
HETATM 4520 O O   . HOH   J 3 .   ? -3.235  -29.837 59.848 1.00 46.37  ? 259 HOH   C O   1 
HETATM 4521 O O   . HOH   J 3 .   ? 8.842   -5.928  57.539 1.00 36.97  ? 260 HOH   C O   1 
HETATM 4522 O O   . HOH   J 3 .   ? 4.521   8.179   55.965 1.00 38.80  ? 261 HOH   C O   1 
HETATM 4523 O O   . HOH   J 3 .   ? -3.884  7.725   74.172 1.00 41.73  ? 262 HOH   C O   1 
HETATM 4524 O O   . HOH   J 3 .   ? -10.257 -9.658  62.778 1.00 28.22  ? 263 HOH   C O   1 
HETATM 4525 O O   . HOH   J 3 .   ? -2.628  -1.278  80.485 1.00 29.62  ? 264 HOH   C O   1 
HETATM 4526 O O   . HOH   J 3 .   ? 9.347   -25.514 88.633 1.00 31.54  ? 265 HOH   C O   1 
HETATM 4527 O O   . HOH   J 3 .   ? -2.987  5.212   68.089 1.00 35.81  ? 266 HOH   C O   1 
HETATM 4528 O O   . HOH   J 3 .   ? 4.776   -10.209 93.941 1.00 49.24  ? 267 HOH   C O   1 
HETATM 4529 O O   . HOH   K 3 .   ? -7.536  -8.247  51.206 1.00 32.82  ? 301 HOH   D O   1 
HETATM 4530 O O   . HOH   K 3 .   ? -13.641 -38.222 71.976 1.00 41.74  ? 302 HOH   D O   1 
HETATM 4531 O O   . HOH   K 3 .   ? 14.677  -6.029  81.126 1.00 36.09  ? 303 HOH   D O   1 
HETATM 4532 O O   . HOH   K 3 .   ? 13.238  -6.259  77.024 1.00 22.63  ? 304 HOH   D O   1 
HETATM 4533 O O   . HOH   K 3 .   ? -17.403 -10.640 63.351 1.00 29.11  ? 305 HOH   D O   1 
HETATM 4534 O O   . HOH   K 3 .   ? -11.119 -14.430 61.169 1.00 22.76  ? 306 HOH   D O   1 
HETATM 4535 O O   . HOH   K 3 .   ? -6.080  -27.171 66.053 1.00 29.62  ? 307 HOH   D O   1 
HETATM 4536 O O   . HOH   K 3 .   ? -8.788  -8.109  88.992 1.00 54.80  ? 308 HOH   D O   1 
HETATM 4537 O O   . HOH   K 3 .   ? 15.924  -16.155 59.682 1.00 34.22  ? 309 HOH   D O   1 
HETATM 4538 O O   . HOH   K 3 .   ? 3.994   -15.962 60.630 1.00 21.00  ? 310 HOH   D O   1 
HETATM 4539 O O   . HOH   K 3 .   ? 3.003   -35.329 84.795 1.00 45.08  ? 311 HOH   D O   1 
HETATM 4540 O O   . HOH   K 3 .   ? 10.813  -7.403  59.844 1.00 28.08  ? 312 HOH   D O   1 
HETATM 4541 O O   . HOH   K 3 .   ? 8.541   -18.553 61.535 1.00 22.16  ? 313 HOH   D O   1 
HETATM 4542 O O   . HOH   K 3 .   ? 0.924   -22.555 56.045 1.00 31.19  ? 314 HOH   D O   1 
HETATM 4543 O O   . HOH   K 3 .   ? 7.896   -13.807 62.214 1.00 23.13  ? 315 HOH   D O   1 
HETATM 4544 O O   . HOH   K 3 .   ? 10.148  -13.996 52.304 1.00 34.21  ? 316 HOH   D O   1 
HETATM 4545 O O   . HOH   K 3 .   ? 6.739   -10.674 83.981 1.00 32.65  ? 317 HOH   D O   1 
HETATM 4546 O O   . HOH   K 3 .   ? -17.819 -8.588  70.995 1.00 30.15  ? 318 HOH   D O   1 
HETATM 4547 O O   . HOH   K 3 .   ? -8.790  -32.721 90.210 1.00 51.00  ? 319 HOH   D O   1 
HETATM 4548 O O   . HOH   K 3 .   ? 15.376  -11.117 71.580 1.00 28.67  ? 320 HOH   D O   1 
HETATM 4549 O O   . HOH   K 3 .   ? 7.456   -21.067 60.775 1.00 34.88  ? 321 HOH   D O   1 
HETATM 4550 O O   . HOH   K 3 .   ? 14.002  -16.038 57.335 1.00 27.19  ? 322 HOH   D O   1 
HETATM 4551 O O   . HOH   K 3 .   ? -6.997  -21.322 62.199 1.00 23.83  ? 323 HOH   D O   1 
HETATM 4552 O O   . HOH   K 3 .   ? -10.075 -8.001  59.806 1.00 29.74  ? 324 HOH   D O   1 
HETATM 4553 O O   . HOH   K 3 .   ? -6.326  -6.443  52.934 1.00 42.71  ? 325 HOH   D O   1 
HETATM 4554 O O   . HOH   K 3 .   ? -10.092 -10.317 77.604 1.00 28.51  ? 326 HOH   D O   1 
HETATM 4555 O O   . HOH   K 3 .   ? -15.313 -20.458 62.414 1.00 36.13  ? 327 HOH   D O   1 
HETATM 4556 O O   . HOH   K 3 .   ? -7.943  -10.829 63.323 1.00 21.65  ? 328 HOH   D O   1 
HETATM 4557 O O   . HOH   K 3 .   ? 13.440  -7.202  71.022 1.00 27.12  ? 329 HOH   D O   1 
HETATM 4558 O O   . HOH   K 3 .   ? -11.371 -18.887 62.928 1.00 23.88  ? 330 HOH   D O   1 
HETATM 4559 O O   . HOH   K 3 .   ? -14.357 -16.338 71.299 1.00 30.87  ? 331 HOH   D O   1 
HETATM 4560 O O   . HOH   K 3 .   ? 9.627   -7.820  66.542 1.00 21.64  ? 332 HOH   D O   1 
HETATM 4561 O O   . HOH   K 3 .   ? 4.107   -20.577 49.639 1.00 25.48  ? 333 HOH   D O   1 
HETATM 4562 O O   . HOH   K 3 .   ? -6.075  -31.881 71.552 1.00 29.48  ? 334 HOH   D O   1 
HETATM 4563 O O   . HOH   K 3 .   ? -1.321  -4.057  82.952 1.00 27.61  ? 335 HOH   D O   1 
HETATM 4564 O O   . HOH   K 3 .   ? 8.020   -8.970  81.891 1.00 27.00  ? 336 HOH   D O   1 
HETATM 4565 O O   . HOH   K 3 .   ? -16.140 -22.227 69.610 1.00 36.99  ? 337 HOH   D O   1 
HETATM 4566 O O   . HOH   K 3 .   ? 14.637  -13.708 60.521 1.00 34.96  ? 338 HOH   D O   1 
HETATM 4567 O O   . HOH   K 3 .   ? 12.446  -18.483 67.753 1.00 21.78  ? 339 HOH   D O   1 
HETATM 4568 O O   . HOH   K 3 .   ? -15.598 -16.641 68.961 1.00 39.06  ? 340 HOH   D O   1 
HETATM 4569 O O   . HOH   K 3 .   ? 5.916   -13.837 60.263 1.00 22.97  ? 341 HOH   D O   1 
HETATM 4570 O O   . HOH   K 3 .   ? -6.867  -36.232 70.609 1.00 49.04  ? 342 HOH   D O   1 
HETATM 4571 O O   . HOH   K 3 .   ? 15.796  -17.406 69.399 1.00 27.93  ? 343 HOH   D O   1 
HETATM 4572 O O   . HOH   K 3 .   ? 16.263  -11.716 60.316 1.00 35.15  ? 344 HOH   D O   1 
HETATM 4573 O O   . HOH   K 3 .   ? -7.570  -5.573  50.643 1.00 38.70  ? 345 HOH   D O   1 
HETATM 4574 O O   . HOH   K 3 .   ? 8.453   -4.786  66.271 1.00 18.59  ? 346 HOH   D O   1 
HETATM 4575 O O   . HOH   K 3 .   ? 10.688  -18.485 77.759 1.00 29.69  ? 347 HOH   D O   1 
HETATM 4576 O O   . HOH   K 3 .   ? -10.271 -4.300  92.833 1.00 45.46  ? 348 HOH   D O   1 
HETATM 4577 O O   . HOH   K 3 .   ? 13.059  -13.926 58.244 1.00 24.02  ? 349 HOH   D O   1 
HETATM 4578 O O   . HOH   K 3 .   ? 4.391   -4.506  83.524 1.00 31.76  ? 350 HOH   D O   1 
HETATM 4579 O O   . HOH   K 3 .   ? 18.183  -15.194 58.477 1.00 41.67  ? 351 HOH   D O   1 
HETATM 4580 O O   . HOH   K 3 .   ? 0.334   -36.466 84.366 1.00 52.12  ? 352 HOH   D O   1 
HETATM 4581 O O   . HOH   K 3 .   ? -12.876 -16.447 61.909 1.00 33.35  ? 353 HOH   D O   1 
HETATM 4582 O O   . HOH   K 3 .   ? -12.943 1.394   55.263 1.00 40.41  ? 354 HOH   D O   1 
HETATM 4583 O O   . HOH   K 3 .   ? -11.325 -11.997 57.109 1.00 32.30  ? 355 HOH   D O   1 
HETATM 4584 O O   . HOH   K 3 .   ? -11.787 -10.129 58.543 1.00 30.17  ? 356 HOH   D O   1 
HETATM 4585 O O   . HOH   K 3 .   ? -11.086 -14.335 58.221 1.00 41.18  ? 357 HOH   D O   1 
# 
