data_8YLF
# 
_entry.id   8YLF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YLF         pdb_00008ylf 10.2210/pdb8ylf/pdb 
WWPDB D_1300045757 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-13 
2 'Structure model' 1 1 2024-12-04 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YLF 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sungil@kangwon.ac.kr 
_pdbx_contact_author.name_first         Sung-il 
_pdbx_contact_author.name_last          Yoon 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0777-0457 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Song, W.S.' 1 0000-0002-8104-8027 
'Yoon, S.I.' 2 0000-0003-0777-0457 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            52 
_citation.language                  ? 
_citation.page_first                13192 
_citation.page_last                 13205 
_citation.title                     'Structural basis of transcriptional regulation by UrtR in response to uric acid.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkae922 
_citation.pdbx_database_id_PubMed   39484741 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Song, W.S.' 1 ?                   
primary 'Ki, D.U.'   2 ?                   
primary 'Cho, H.Y.'  3 ?                   
primary 'Kwon, O.H.' 4 ?                   
primary 'Cho, H.'    5 ?                   
primary 'Yoon, S.I.' 6 0000-0003-0777-0457 
# 
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 'MarR family transcriptional regulator' 18337.809 1  ? ? ? ? 
2 water   nat water                                   18.015    16 ? ? ? ? 
# 
_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       
;SAKDPMDRAAHAVEQWRSERPDLDPSSMIVLGRLQEAALVIARDRLNPLFARYGLQPGEFDVLATLRRSGAPYALTPTAL
YDAAMISSGSMTNRIDRLEKAGWVERRANPADGRGTLVALTSAGRALIDDAVVAHVDNQRRVLSALSAAEQRQLAKLLDK
LLQGQAAEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SAKDPMDRAAHAVEQWRSERPDLDPSSMIVLGRLQEAALVIARDRLNPLFARYGLQPGEFDVLATLRRSGAPYALTPTAL
YDAAMISSGSMTNRIDRLEKAGWVERRANPADGRGTLVALTSAGRALIDDAVVAHVDNQRRVLSALSAAEQRQLAKLLDK
LLQGQAAEG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ALA n 
1 3   LYS n 
1 4   ASP n 
1 5   PRO n 
1 6   MET n 
1 7   ASP n 
1 8   ARG n 
1 9   ALA n 
1 10  ALA n 
1 11  HIS n 
1 12  ALA n 
1 13  VAL n 
1 14  GLU n 
1 15  GLN n 
1 16  TRP n 
1 17  ARG n 
1 18  SER n 
1 19  GLU n 
1 20  ARG n 
1 21  PRO n 
1 22  ASP n 
1 23  LEU n 
1 24  ASP n 
1 25  PRO n 
1 26  SER n 
1 27  SER n 
1 28  MET n 
1 29  ILE n 
1 30  VAL n 
1 31  LEU n 
1 32  GLY n 
1 33  ARG n 
1 34  LEU n 
1 35  GLN n 
1 36  GLU n 
1 37  ALA n 
1 38  ALA n 
1 39  LEU n 
1 40  VAL n 
1 41  ILE n 
1 42  ALA n 
1 43  ARG n 
1 44  ASP n 
1 45  ARG n 
1 46  LEU n 
1 47  ASN n 
1 48  PRO n 
1 49  LEU n 
1 50  PHE n 
1 51  ALA n 
1 52  ARG n 
1 53  TYR n 
1 54  GLY n 
1 55  LEU n 
1 56  GLN n 
1 57  PRO n 
1 58  GLY n 
1 59  GLU n 
1 60  PHE n 
1 61  ASP n 
1 62  VAL n 
1 63  LEU n 
1 64  ALA n 
1 65  THR n 
1 66  LEU n 
1 67  ARG n 
1 68  ARG n 
1 69  SER n 
1 70  GLY n 
1 71  ALA n 
1 72  PRO n 
1 73  TYR n 
1 74  ALA n 
1 75  LEU n 
1 76  THR n 
1 77  PRO n 
1 78  THR n 
1 79  ALA n 
1 80  LEU n 
1 81  TYR n 
1 82  ASP n 
1 83  ALA n 
1 84  ALA n 
1 85  MET n 
1 86  ILE n 
1 87  SER n 
1 88  SER n 
1 89  GLY n 
1 90  SER n 
1 91  MET n 
1 92  THR n 
1 93  ASN n 
1 94  ARG n 
1 95  ILE n 
1 96  ASP n 
1 97  ARG n 
1 98  LEU n 
1 99  GLU n 
1 100 LYS n 
1 101 ALA n 
1 102 GLY n 
1 103 TRP n 
1 104 VAL n 
1 105 GLU n 
1 106 ARG n 
1 107 ARG n 
1 108 ALA n 
1 109 ASN n 
1 110 PRO n 
1 111 ALA n 
1 112 ASP n 
1 113 GLY n 
1 114 ARG n 
1 115 GLY n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 ALA n 
1 120 LEU n 
1 121 THR n 
1 122 SER n 
1 123 ALA n 
1 124 GLY n 
1 125 ARG n 
1 126 ALA n 
1 127 LEU n 
1 128 ILE n 
1 129 ASP n 
1 130 ASP n 
1 131 ALA n 
1 132 VAL n 
1 133 VAL n 
1 134 ALA n 
1 135 HIS n 
1 136 VAL n 
1 137 ASP n 
1 138 ASN n 
1 139 GLN n 
1 140 ARG n 
1 141 ARG n 
1 142 VAL n 
1 143 LEU n 
1 144 SER n 
1 145 ALA n 
1 146 LEU n 
1 147 SER n 
1 148 ALA n 
1 149 ALA n 
1 150 GLU n 
1 151 GLN n 
1 152 ARG n 
1 153 GLN n 
1 154 LEU n 
1 155 ALA n 
1 156 LYS n 
1 157 LEU n 
1 158 LEU n 
1 159 ASP n 
1 160 LYS n 
1 161 LEU n 
1 162 LEU n 
1 163 GLN n 
1 164 GLY n 
1 165 GLN n 
1 166 ALA n 
1 167 ALA n 
1 168 GLU n 
1 169 GLY 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                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 A8H32_16025 
_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      'Burkholderia thailandensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     57975 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   -4  ?   ?   ?   A . n 
A 1 2   ALA 2   -3  ?   ?   ?   A . n 
A 1 3   LYS 3   -2  ?   ?   ?   A . n 
A 1 4   ASP 4   -1  ?   ?   ?   A . n 
A 1 5   PRO 5   0   ?   ?   ?   A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   ASP 7   2   2   ASP ASP A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  ALA 10  5   5   ALA ALA A . n 
A 1 11  HIS 11  6   6   HIS HIS A . n 
A 1 12  ALA 12  7   7   ALA ALA A . n 
A 1 13  VAL 13  8   8   VAL VAL A . n 
A 1 14  GLU 14  9   9   GLU GLU A . n 
A 1 15  GLN 15  10  10  GLN GLN A . n 
A 1 16  TRP 16  11  11  TRP TRP A . n 
A 1 17  ARG 17  12  12  ARG ARG A . n 
A 1 18  SER 18  13  13  SER SER A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  ARG 20  15  15  ARG ARG A . n 
A 1 21  PRO 21  16  16  PRO PRO A . n 
A 1 22  ASP 22  17  17  ASP ASP A . n 
A 1 23  LEU 23  18  18  LEU LEU A . n 
A 1 24  ASP 24  19  19  ASP ASP A . n 
A 1 25  PRO 25  20  20  PRO PRO A . n 
A 1 26  SER 26  21  21  SER SER A . n 
A 1 27  SER 27  22  22  SER SER A . n 
A 1 28  MET 28  23  23  MET MET A . n 
A 1 29  ILE 29  24  24  ILE ILE A . n 
A 1 30  VAL 30  25  25  VAL VAL A . n 
A 1 31  LEU 31  26  26  LEU LEU A . n 
A 1 32  GLY 32  27  27  GLY GLY A . n 
A 1 33  ARG 33  28  28  ARG ARG A . n 
A 1 34  LEU 34  29  29  LEU LEU A . n 
A 1 35  GLN 35  30  30  GLN GLN A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  ALA 37  32  32  ALA ALA A . n 
A 1 38  ALA 38  33  33  ALA ALA A . n 
A 1 39  LEU 39  34  34  LEU LEU A . n 
A 1 40  VAL 40  35  35  VAL VAL A . n 
A 1 41  ILE 41  36  36  ILE ILE A . n 
A 1 42  ALA 42  37  37  ALA ALA A . n 
A 1 43  ARG 43  38  38  ARG ARG A . n 
A 1 44  ASP 44  39  39  ASP ASP A . n 
A 1 45  ARG 45  40  40  ARG ARG A . n 
A 1 46  LEU 46  41  41  LEU LEU A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  PRO 48  43  43  PRO PRO A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  PHE 50  45  45  PHE PHE A . n 
A 1 51  ALA 51  46  46  ALA ALA A . n 
A 1 52  ARG 52  47  47  ARG ARG A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  GLY 54  49  49  GLY GLY A . n 
A 1 55  LEU 55  50  50  LEU LEU A . n 
A 1 56  GLN 56  51  51  GLN GLN A . n 
A 1 57  PRO 57  52  52  PRO PRO A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLU 59  54  54  GLU GLU A . n 
A 1 60  PHE 60  55  55  PHE PHE A . n 
A 1 61  ASP 61  56  56  ASP ASP A . n 
A 1 62  VAL 62  57  57  VAL VAL A . n 
A 1 63  LEU 63  58  58  LEU LEU A . n 
A 1 64  ALA 64  59  59  ALA ALA A . n 
A 1 65  THR 65  60  60  THR THR A . n 
A 1 66  LEU 66  61  61  LEU LEU A . n 
A 1 67  ARG 67  62  62  ARG ARG A . n 
A 1 68  ARG 68  63  63  ARG ARG A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  GLY 70  65  65  GLY GLY A . n 
A 1 71  ALA 71  66  66  ALA ALA A . n 
A 1 72  PRO 72  67  67  PRO PRO A . n 
A 1 73  TYR 73  68  68  TYR TYR A . n 
A 1 74  ALA 74  69  69  ALA ALA A . n 
A 1 75  LEU 75  70  70  LEU LEU A . n 
A 1 76  THR 76  71  71  THR THR A . n 
A 1 77  PRO 77  72  72  PRO PRO A . n 
A 1 78  THR 78  73  73  THR THR A . n 
A 1 79  ALA 79  74  74  ALA ALA A . n 
A 1 80  LEU 80  75  75  LEU LEU A . n 
A 1 81  TYR 81  76  76  TYR TYR A . n 
A 1 82  ASP 82  77  77  ASP ASP A . n 
A 1 83  ALA 83  78  78  ALA ALA A . n 
A 1 84  ALA 84  79  79  ALA ALA A . n 
A 1 85  MET 85  80  80  MET MET A . n 
A 1 86  ILE 86  81  81  ILE ILE A . n 
A 1 87  SER 87  82  82  SER SER A . n 
A 1 88  SER 88  83  83  SER SER A . n 
A 1 89  GLY 89  84  84  GLY GLY A . n 
A 1 90  SER 90  85  85  SER SER A . n 
A 1 91  MET 91  86  86  MET MET A . n 
A 1 92  THR 92  87  87  THR THR A . n 
A 1 93  ASN 93  88  88  ASN ASN A . n 
A 1 94  ARG 94  89  89  ARG ARG A . n 
A 1 95  ILE 95  90  90  ILE ILE A . n 
A 1 96  ASP 96  91  91  ASP ASP A . n 
A 1 97  ARG 97  92  92  ARG ARG A . n 
A 1 98  LEU 98  93  93  LEU LEU A . n 
A 1 99  GLU 99  94  94  GLU GLU A . n 
A 1 100 LYS 100 95  95  LYS LYS A . n 
A 1 101 ALA 101 96  96  ALA ALA A . n 
A 1 102 GLY 102 97  97  GLY GLY A . n 
A 1 103 TRP 103 98  98  TRP TRP A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 GLU 105 100 100 GLU GLU A . n 
A 1 106 ARG 106 101 101 ARG ARG A . n 
A 1 107 ARG 107 102 102 ARG ARG A . n 
A 1 108 ALA 108 103 103 ALA ALA A . n 
A 1 109 ASN 109 104 ?   ?   ?   A . n 
A 1 110 PRO 110 105 ?   ?   ?   A . n 
A 1 111 ALA 111 106 ?   ?   ?   A . n 
A 1 112 ASP 112 107 ?   ?   ?   A . n 
A 1 113 GLY 113 108 ?   ?   ?   A . n 
A 1 114 ARG 114 109 ?   ?   ?   A . n 
A 1 115 GLY 115 110 ?   ?   ?   A . n 
A 1 116 THR 116 111 111 THR THR A . n 
A 1 117 LEU 117 112 112 LEU LEU A . n 
A 1 118 VAL 118 113 113 VAL VAL A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 LEU 120 115 115 LEU LEU A . n 
A 1 121 THR 121 116 116 THR THR A . n 
A 1 122 SER 122 117 117 SER SER A . n 
A 1 123 ALA 123 118 118 ALA ALA A . n 
A 1 124 GLY 124 119 119 GLY GLY A . n 
A 1 125 ARG 125 120 120 ARG ARG A . n 
A 1 126 ALA 126 121 121 ALA ALA A . n 
A 1 127 LEU 127 122 122 LEU LEU A . n 
A 1 128 ILE 128 123 123 ILE ILE A . n 
A 1 129 ASP 129 124 124 ASP ASP A . n 
A 1 130 ASP 130 125 125 ASP ASP A . n 
A 1 131 ALA 131 126 126 ALA ALA A . n 
A 1 132 VAL 132 127 127 VAL VAL A . n 
A 1 133 VAL 133 128 128 VAL VAL A . n 
A 1 134 ALA 134 129 129 ALA ALA A . n 
A 1 135 HIS 135 130 130 HIS HIS A . n 
A 1 136 VAL 136 131 131 VAL VAL A . n 
A 1 137 ASP 137 132 132 ASP ASP A . n 
A 1 138 ASN 138 133 133 ASN ASN A . n 
A 1 139 GLN 139 134 134 GLN GLN A . n 
A 1 140 ARG 140 135 135 ARG ARG A . n 
A 1 141 ARG 141 136 136 ARG ARG A . n 
A 1 142 VAL 142 137 137 VAL VAL A . n 
A 1 143 LEU 143 138 138 LEU LEU A . n 
A 1 144 SER 144 139 139 SER SER A . n 
A 1 145 ALA 145 140 140 ALA ALA A . n 
A 1 146 LEU 146 141 141 LEU LEU A . n 
A 1 147 SER 147 142 142 SER SER A . n 
A 1 148 ALA 148 143 143 ALA ALA A . n 
A 1 149 ALA 149 144 144 ALA ALA A . n 
A 1 150 GLU 150 145 145 GLU GLU A . n 
A 1 151 GLN 151 146 146 GLN GLN A . n 
A 1 152 ARG 152 147 147 ARG ARG A . n 
A 1 153 GLN 153 148 148 GLN GLN A . n 
A 1 154 LEU 154 149 149 LEU LEU A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 LYS 156 151 151 LYS LYS A . n 
A 1 157 LEU 157 152 152 LEU LEU A . n 
A 1 158 LEU 158 153 153 LEU LEU A . n 
A 1 159 ASP 159 154 154 ASP ASP A . n 
A 1 160 LYS 160 155 155 LYS LYS A . n 
A 1 161 LEU 161 156 156 LEU LEU A . n 
A 1 162 LEU 162 157 157 LEU LEU A . n 
A 1 163 GLN 163 158 158 GLN GLN A . n 
A 1 164 GLY 164 159 159 GLY GLY A . n 
A 1 165 GLN 165 160 160 GLN GLN A . n 
A 1 166 ALA 166 161 ?   ?   ?   A . n 
A 1 167 ALA 167 162 ?   ?   ?   A . n 
A 1 168 GLU 168 163 ?   ?   ?   A . n 
A 1 169 GLY 169 164 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1  201 25 HOH HOH A . 
B 2 HOH 2  202 27 HOH HOH A . 
B 2 HOH 3  203 6  HOH HOH A . 
B 2 HOH 4  204 17 HOH HOH A . 
B 2 HOH 5  205 11 HOH HOH A . 
B 2 HOH 6  206 2  HOH HOH A . 
B 2 HOH 7  207 9  HOH HOH A . 
B 2 HOH 8  208 7  HOH HOH A . 
B 2 HOH 9  209 1  HOH HOH A . 
B 2 HOH 10 210 14 HOH HOH A . 
B 2 HOH 11 211 12 HOH HOH A . 
B 2 HOH 12 212 5  HOH HOH A . 
B 2 HOH 13 213 23 HOH HOH A . 
B 2 HOH 14 214 21 HOH HOH A . 
B 2 HOH 15 215 15 HOH HOH A . 
B 2 HOH 16 216 24 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 95  ? CD  ? A LYS 100 CD  
2  1 Y 1 A LYS 95  ? CE  ? A LYS 100 CE  
3  1 Y 1 A LYS 95  ? NZ  ? A LYS 100 NZ  
4  1 Y 1 A ARG 102 ? CG  ? A ARG 107 CG  
5  1 Y 1 A ARG 102 ? CD  ? A ARG 107 CD  
6  1 Y 1 A ARG 102 ? NE  ? A ARG 107 NE  
7  1 Y 1 A ARG 102 ? CZ  ? A ARG 107 CZ  
8  1 Y 1 A ARG 102 ? NH1 ? A ARG 107 NH1 
9  1 Y 1 A ARG 102 ? NH2 ? A ARG 107 NH2 
10 1 Y 1 A THR 111 ? OG1 ? A THR 116 OG1 
11 1 Y 1 A THR 111 ? CG2 ? A THR 116 CG2 
12 1 Y 1 A ARG 135 ? CD  ? A ARG 140 CD  
13 1 Y 1 A ARG 135 ? NE  ? A ARG 140 NE  
14 1 Y 1 A ARG 135 ? CZ  ? A ARG 140 CZ  
15 1 Y 1 A ARG 135 ? NH1 ? A ARG 140 NH1 
16 1 Y 1 A ARG 135 ? NH2 ? A ARG 140 NH2 
17 1 Y 1 A ARG 136 ? NE  ? A ARG 141 NE  
18 1 Y 1 A ARG 136 ? CZ  ? A ARG 141 CZ  
19 1 Y 1 A ARG 136 ? NH1 ? A ARG 141 NH1 
20 1 Y 1 A ARG 136 ? NH2 ? A ARG 141 NH2 
21 1 Y 1 A ARG 147 ? CG  ? A ARG 152 CG  
22 1 Y 1 A ARG 147 ? CD  ? A ARG 152 CD  
23 1 Y 1 A ARG 147 ? NE  ? A ARG 152 NE  
24 1 Y 1 A ARG 147 ? CZ  ? A ARG 152 CZ  
25 1 Y 1 A ARG 147 ? NH1 ? A ARG 152 NH1 
26 1 Y 1 A ARG 147 ? NH2 ? A ARG 152 NH2 
27 1 Y 1 A LYS 151 ? CG  ? A LYS 156 CG  
28 1 Y 1 A LYS 151 ? CD  ? A LYS 156 CD  
29 1 Y 1 A LYS 151 ? CE  ? A LYS 156 CE  
30 1 Y 1 A LYS 151 ? NZ  ? A LYS 156 NZ  
31 1 Y 1 A GLN 158 ? CD  ? A GLN 163 CD  
32 1 Y 1 A GLN 158 ? OE1 ? A GLN 163 OE1 
33 1 Y 1 A GLN 158 ? NE2 ? A GLN 163 NE2 
# 
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   ? ? ? 1.15.2_3472 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YLF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.389 
_cell.length_a_esd                 ? 
_cell.length_b                     62.389 
_cell.length_b_esd                 ? 
_cell.length_c                     77.254 
_cell.length_c_esd                 ? 
_cell.volume                       260415.995 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8YLF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YLF 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.03 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'imidazole, sodium citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 270' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-11-02 
_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   0.9793 
_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                        'PAL/PLS BEAMLINE 7A (6B, 6C1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '7A (6B, 6C1)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YLF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.01 
_reflns.d_resolution_low                               30.00 
_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                                     11986 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          53.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.01 
_reflns_shell.d_res_low                                     2.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             549 
_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                               8.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.912 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          94.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               46.12 
_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                                 8YLF 
_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                            2.01 
_refine.ls_d_res_low                             28.93 
_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                     11952 
_refine.ls_number_reflns_R_free                  581 
_refine.ls_number_reflns_R_work                  11371 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2175 
_refine.ls_R_factor_R_free                       0.2355 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2166 
_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                          1.33 
_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                      'in-house Se-SAD model' 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.0034 
_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                            0.1818 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.01 
_refine_hist.d_res_low                        28.93 
_refine_hist.number_atoms_solvent             16 
_refine_hist.number_atoms_total               1164 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0059  ? 1163 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7959  ? 1579 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0447  ? 187  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0046  ? 207  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 10.3026 ? 715  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.01 2.21  . . 165 2760 99.86 . . . . 0.2373 . . . . . . . . . . . 0.3019 
'X-RAY DIFFRACTION' 2.21 2.53  . . 139 2802 99.90 . . . . 0.2213 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 2.53 3.19  . . 131 2855 99.87 . . . . 0.2494 . . . . . . . . . . . 0.2787 
'X-RAY DIFFRACTION' 3.19 28.93 . . 146 2954 99.68 . . . . 0.1996 . . . . . . . . . . . 0.2019 
# 
_struct.entry_id                     8YLF 
_struct.title                        'Crystal structure of Burkholderia thailandensis MftR' 
_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        8YLF 
_struct_keywords.text            'Transcription factor, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2N8QSC4_BURTH 
_struct_ref.pdbx_db_accession          A0A2N8QSC4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDRAAHAVEQWRSERPDLDPSSMIVLGRLQEAALVIARDRLNPLFARYGLQPGEFDVLATLRRSGAPYALTPTALYDAAM
ISSGSMTNRIDRLEKAGWVERRANPADGRGTLVALTSAGRALIDDAVVAHVDNQRRVLSALSAAEQRQLAKLLDKLLQGQ
AAEG
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YLF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 6 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 169 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A2N8QSC4 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  164 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       164 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YLF SER A 1 ? UNP A0A2N8QSC4 ? ? 'expression tag' -4 1 
1 8YLF ALA A 2 ? UNP A0A2N8QSC4 ? ? 'expression tag' -3 2 
1 8YLF LYS A 3 ? UNP A0A2N8QSC4 ? ? 'expression tag' -2 3 
1 8YLF ASP A 4 ? UNP A0A2N8QSC4 ? ? 'expression tag' -1 4 
1 8YLF PRO A 5 ? UNP A0A2N8QSC4 ? ? 'expression tag' 0  5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6880  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  13050 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z          1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 6_555 -x,-x+y,-z+1/3 -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 
0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 25.7513333333 
# 
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 ASP A 7   ? ARG A 20  ? ASP A 2   ARG A 15  1 ? 14 
HELX_P HELX_P2 AA2 SER A 27  ? ARG A 45  ? SER A 22  ARG A 40  1 ? 19 
HELX_P HELX_P3 AA3 ARG A 45  ? TYR A 53  ? ARG A 40  TYR A 48  1 ? 9  
HELX_P HELX_P4 AA4 GLN A 56  ? SER A 69  ? GLN A 51  SER A 64  1 ? 14 
HELX_P HELX_P5 AA5 THR A 76  ? ALA A 84  ? THR A 71  ALA A 79  1 ? 9  
HELX_P HELX_P6 AA6 SER A 90  ? ALA A 101 ? SER A 85  ALA A 96  1 ? 12 
HELX_P HELX_P7 AA7 THR A 121 ? SER A 144 ? THR A 116 SER A 139 1 ? 24 
HELX_P HELX_P8 AA8 SER A 147 ? GLY A 164 ? SER A 142 GLY A 159 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ALA 
_struct_mon_prot_cis.label_seq_id           71 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ALA 
_struct_mon_prot_cis.auth_seq_id            66 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    72 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     67 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.12 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
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 
# 
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 ALA A 74  ? LEU A 75  ? ALA A 69  LEU A 70  
AA1 2 LEU A 117 ? LEU A 120 ? LEU A 112 LEU A 115 
AA1 3 VAL A 104 ? ARG A 107 ? VAL A 99  ARG A 102 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 75  ? N LEU A 70  O VAL A 118 ? O VAL A 113 
AA1 2 3 O LEU A 117 ? O LEU A 112 N ARG A 107 ? N ARG A 102 
# 
_pdbx_entry_details.entry_id                   8YLF 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 40 ? ? -124.08 -56.08 
2 1 SER A 82 ? ? -92.20  51.01  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+1/3   
3 -x+y,-x,z+2/3  
4 x-y,-y,-z+2/3  
5 -x,-x+y,-z+1/3 
6 y,x,-z         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -10.8535204907 16.4304255535 11.1413475565 0.288050312453 ? 0.0262122036872  ? 0.0141000194499  ? 
0.155428865449 ? 0.00428193819878 ? 0.244995798636 ? 8.17808946804 ? 2.46642388651  ? 1.46622418791 ? 1.32806022165 ? 
0.621220377365  ? 2.00355659143 ? -0.182407673822 ? 0.0161682227276  ? -0.105174617321 ? -0.102343695749  ? 0.0750741752826 ? 
-0.113030693336  ? 0.0877539415842 ? 0.0252013272817 ? 0.0520363336999 ? 
2 'X-RAY DIFFRACTION' ? refined -22.0861852061 11.9098071957 7.99719792633 0.311627180875 ? -0.0233572993869 ? 0.00218748138914 ? 
0.247721385655 ? -0.037049491522  ? 0.215792134646 ? 5.67252928842 ? 0.412178891285 ? 2.26588676318 ? 1.42843947578 ? 
-0.573228930835 ? 3.36950621219 ? -0.092193256866 ? -0.0452943175978 ? -0.244415106877 ? -0.0943423460629 ? 0.034020613608  ? 
-0.0520868515675 ? 0.0116662917864 ? -0.40572955572  ? 0.061997507146  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 78 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 79 through 160 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER -4  ? A SER 1   
2  1 Y 1 A ALA -3  ? A ALA 2   
3  1 Y 1 A LYS -2  ? A LYS 3   
4  1 Y 1 A ASP -1  ? A ASP 4   
5  1 Y 1 A PRO 0   ? A PRO 5   
6  1 Y 1 A ASN 104 ? A ASN 109 
7  1 Y 1 A PRO 105 ? A PRO 110 
8  1 Y 1 A ALA 106 ? A ALA 111 
9  1 Y 1 A ASP 107 ? A ASP 112 
10 1 Y 1 A GLY 108 ? A GLY 113 
11 1 Y 1 A ARG 109 ? A ARG 114 
12 1 Y 1 A GLY 110 ? A GLY 115 
13 1 Y 1 A ALA 161 ? A ALA 166 
14 1 Y 1 A ALA 162 ? A ALA 167 
15 1 Y 1 A GLU 163 ? A GLU 168 
16 1 Y 1 A GLY 164 ? A GLY 169 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TRP N    N N N 307 
TRP CA   C N S 308 
TRP C    C N N 309 
TRP O    O N N 310 
TRP CB   C N N 311 
TRP CG   C Y N 312 
TRP CD1  C Y N 313 
TRP CD2  C Y N 314 
TRP NE1  N Y N 315 
TRP CE2  C Y N 316 
TRP CE3  C Y N 317 
TRP CZ2  C Y N 318 
TRP CZ3  C Y N 319 
TRP CH2  C Y N 320 
TRP OXT  O N N 321 
TRP H    H N N 322 
TRP H2   H N N 323 
TRP HA   H N N 324 
TRP HB2  H N N 325 
TRP HB3  H N N 326 
TRP HD1  H N N 327 
TRP HE1  H N N 328 
TRP HE3  H N N 329 
TRP HZ2  H N N 330 
TRP HZ3  H N N 331 
TRP HH2  H N N 332 
TRP HXT  H N N 333 
TYR N    N N N 334 
TYR CA   C N S 335 
TYR C    C N N 336 
TYR O    O N N 337 
TYR CB   C N N 338 
TYR CG   C Y N 339 
TYR CD1  C Y N 340 
TYR CD2  C Y N 341 
TYR CE1  C Y N 342 
TYR CE2  C Y N 343 
TYR CZ   C Y N 344 
TYR OH   O N N 345 
TYR OXT  O N N 346 
TYR H    H N N 347 
TYR H2   H N N 348 
TYR HA   H N N 349 
TYR HB2  H N N 350 
TYR HB3  H N N 351 
TYR HD1  H N N 352 
TYR HD2  H N N 353 
TYR HE1  H N N 354 
TYR HE2  H N N 355 
TYR HH   H N N 356 
TYR HXT  H N N 357 
VAL N    N N N 358 
VAL CA   C N S 359 
VAL C    C N N 360 
VAL O    O N N 361 
VAL CB   C N N 362 
VAL CG1  C N N 363 
VAL CG2  C N N 364 
VAL OXT  O N N 365 
VAL H    H N N 366 
VAL H2   H N N 367 
VAL HA   H N N 368 
VAL HB   H N N 369 
VAL HG11 H N N 370 
VAL HG12 H N N 371 
VAL HG13 H N N 372 
VAL HG21 H N N 373 
VAL HG22 H N N 374 
VAL HG23 H N N 375 
VAL HXT  H N N 376 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' RS-2023-00208153    1 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' 2022R1I1A1A01068105 2 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'in-house Selenomethionine-incorporated MftR model(SAD)' 
# 
_space_group.name_H-M_alt     'P 31 2 1' 
_space_group.name_Hall        
;P 31 2"
;
_space_group.IT_number        152 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YLF 
_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]   0.016028 
_atom_sites.fract_transf_matrix[1][2]   0.009254 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018508 
_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]   0.012944 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 6   ? 10.29824  16.37374 5.25106  1.000 61.56054 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 6   ? 9.61725   16.63202 6.52147  1.000 59.65729 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 6   ? 8.34283   17.45328 6.33031  1.000 58.21854 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 6   ? 8.32266   18.40497 5.54947  1.000 59.11823 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 6   ? 10.54685  17.36141 7.49844  1.000 59.87615 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 6   ? 11.61933  16.48886 8.14229  1.000 67.33211 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 6   ? 12.31314  17.22965 9.64717  1.000 71.56071 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 6   ? 13.38575  15.90449 10.21325 1.000 70.26800 ? 1   MET A CE  1 
ATOM   9    N N   . ASP A 1 7   ? 7.28857   17.09357 7.06370  1.000 54.91066 ? 2   ASP A N   1 
ATOM   10   C CA  . ASP A 1 7   ? 6.02337   17.80882 7.00108  1.000 43.89536 ? 2   ASP A CA  1 
ATOM   11   C C   . ASP A 1 7   ? 6.01391   18.91102 8.06331  1.000 40.95990 ? 2   ASP A C   1 
ATOM   12   O O   . ASP A 1 7   ? 7.03056   19.19651 8.70384  1.000 46.22604 ? 2   ASP A O   1 
ATOM   13   C CB  . ASP A 1 7   ? 4.85361   16.82750 7.14517  1.000 41.10796 ? 2   ASP A CB  1 
ATOM   14   C CG  . ASP A 1 7   ? 4.84971   16.09811 8.49746  1.000 43.36985 ? 2   ASP A CG  1 
ATOM   15   O OD1 . ASP A 1 7   ? 5.89026   16.07211 9.18582  1.000 41.22624 ? 2   ASP A OD1 1 
ATOM   16   O OD2 . ASP A 1 7   ? 3.80208   15.53095 8.86376  1.000 47.27633 ? 2   ASP A OD2 1 
ATOM   17   N N   . ARG A 1 8   ? 4.85757   19.55570 8.25283  1.000 39.57739 ? 3   ARG A N   1 
ATOM   18   C CA  . ARG A 1 8   ? 4.74874   20.61596 9.25301  1.000 41.91675 ? 3   ARG A CA  1 
ATOM   19   C C   . ARG A 1 8   ? 5.15083   20.11091 10.62865 1.000 38.23476 ? 3   ARG A C   1 
ATOM   20   O O   . ARG A 1 8   ? 5.94885   20.74475 11.33087 1.000 38.21824 ? 3   ARG A O   1 
ATOM   21   C CB  . ARG A 1 8   ? 3.31587   21.15831 9.30117  1.000 43.30268 ? 3   ARG A CB  1 
ATOM   22   C CG  . ARG A 1 8   ? 2.87985   21.89074 8.03277  1.000 43.24443 ? 3   ARG A CG  1 
ATOM   23   C CD  . ARG A 1 8   ? 1.40741   22.27772 8.05760  1.000 48.72248 ? 3   ARG A CD  1 
ATOM   24   N NE  . ARG A 1 8   ? 1.11070   23.19364 6.95978  1.000 52.97057 ? 3   ARG A NE  1 
ATOM   25   C CZ  . ARG A 1 8   ? 1.27365   24.51221 7.03057  1.000 54.63191 ? 3   ARG A CZ  1 
ATOM   26   N NH1 . ARG A 1 8   ? 1.71617   25.07020 8.15468  1.000 47.62147 ? 3   ARG A NH1 1 
ATOM   27   N NH2 . ARG A 1 8   ? 0.99733   25.27620 5.98033  1.000 56.17546 ? 3   ARG A NH2 1 
ATOM   28   N N   . ALA A 1 9   ? 4.60557   18.95892 11.02301 1.000 34.78700 ? 4   ALA A N   1 
ATOM   29   C CA  . ALA A 1 9   ? 4.77137   18.47633 12.39008 1.000 38.40881 ? 4   ALA A CA  1 
ATOM   30   C C   . ALA A 1 9   ? 6.22496   18.11698 12.69144 1.000 35.99855 ? 4   ALA A C   1 
ATOM   31   O O   . ALA A 1 9   ? 6.74087   18.45570 13.76276 1.000 36.19619 ? 4   ALA A O   1 
ATOM   32   C CB  . ALA A 1 9   ? 3.85454   17.28058 12.63027 1.000 36.51293 ? 4   ALA A CB  1 
ATOM   33   N N   . ALA A 1 10  ? 6.90684   17.43887 11.76576 1.000 39.36180 ? 5   ALA A N   1 
ATOM   34   C CA  . ALA A 1 10  ? 8.29380   17.06095 12.02991 1.000 35.22088 ? 5   ALA A CA  1 
ATOM   35   C C   . ALA A 1 10  ? 9.20467   18.27545 12.02156 1.000 36.52111 ? 5   ALA A C   1 
ATOM   36   O O   . ALA A 1 10  ? 10.15023  18.35534 12.81057 1.000 38.21102 ? 5   ALA A O   1 
ATOM   37   C CB  . ALA A 1 10  ? 8.76847   16.02932 11.00736 1.000 42.37860 ? 5   ALA A CB  1 
ATOM   38   N N   . HIS A 1 11  ? 8.96052   19.21864 11.11139 1.000 42.64733 ? 6   HIS A N   1 
ATOM   39   C CA  . HIS A 1 11  ? 9.77509   20.42466 11.08570 1.000 44.03973 ? 6   HIS A CA  1 
ATOM   40   C C   . HIS A 1 11  ? 9.61463   21.20790 12.38216 1.000 41.58048 ? 6   HIS A C   1 
ATOM   41   O O   . HIS A 1 11  ? 10.58981  21.75419 12.91281 1.000 37.40050 ? 6   HIS A O   1 
ATOM   42   C CB  . HIS A 1 11  ? 9.39974   21.28237 9.87751  1.000 49.46064 ? 6   HIS A CB  1 
ATOM   43   C CG  . HIS A 1 11  ? 10.10115  22.60317 9.83025  1.000 57.04483 ? 6   HIS A CG  1 
ATOM   44   N ND1 . HIS A 1 11  ? 11.44605  22.72374 9.55291  1.000 61.11792 ? 6   HIS A ND1 1 
ATOM   45   C CD2 . HIS A 1 11  ? 9.64289   23.86303 10.02552 1.000 58.62168 ? 6   HIS A CD2 1 
ATOM   46   C CE1 . HIS A 1 11  ? 11.78594  24.00069 9.57670  1.000 61.92157 ? 6   HIS A CE1 1 
ATOM   47   N NE2 . HIS A 1 11  ? 10.70965  24.71321 9.85915  1.000 60.27161 ? 6   HIS A NE2 1 
ATOM   48   N N   . ALA A 1 12  ? 8.39214   21.25456 12.91569 1.000 35.23369 ? 7   ALA A N   1 
ATOM   49   C CA  . ALA A 1 12  ? 8.13793   22.01250 14.13805 1.000 39.08040 ? 7   ALA A CA  1 
ATOM   50   C C   . ALA A 1 12  ? 8.80020   21.36105 15.35156 1.000 42.13681 ? 7   ALA A C   1 
ATOM   51   O O   . ALA A 1 12  ? 9.33962   22.05596 16.22233 1.000 38.82222 ? 7   ALA A O   1 
ATOM   52   C CB  . ALA A 1 12  ? 6.63092   22.13716 14.36420 1.000 38.61224 ? 7   ALA A CB  1 
ATOM   53   N N   . VAL A 1 13  ? 8.73190   20.03189 15.44756 1.000 38.49544 ? 8   VAL A N   1 
ATOM   54   C CA  . VAL A 1 13  ? 9.42731   19.32889 16.52252 1.000 41.29956 ? 8   VAL A CA  1 
ATOM   55   C C   . VAL A 1 13  ? 10.92686  19.58099 16.43446 1.000 44.80465 ? 8   VAL A C   1 
ATOM   56   O O   . VAL A 1 13  ? 11.59416  19.81314 17.45049 1.000 48.70775 ? 8   VAL A O   1 
ATOM   57   C CB  . VAL A 1 13  ? 9.09356   17.82556 16.47454 1.000 43.39222 ? 8   VAL A CB  1 
ATOM   58   C CG1 . VAL A 1 13  ? 10.08754  17.01681 17.30798 1.000 48.03628 ? 8   VAL A CG1 1 
ATOM   59   C CG2 . VAL A 1 13  ? 7.66964   17.59623 16.95978 1.000 45.84837 ? 8   VAL A CG2 1 
ATOM   60   N N   . GLU A 1 14  ? 11.47836  19.55015 15.21831 1.000 41.93485 ? 9   GLU A N   1 
ATOM   61   C CA  . GLU A 1 14  ? 12.89847  19.83118 15.04550 1.000 45.77317 ? 9   GLU A CA  1 
ATOM   62   C C   . GLU A 1 14  ? 13.25204  21.20379 15.59955 1.000 45.43398 ? 9   GLU A C   1 
ATOM   63   O O   . GLU A 1 14  ? 14.23752  21.35514 16.33141 1.000 42.03890 ? 9   GLU A O   1 
ATOM   64   C CB  . GLU A 1 14  ? 13.27481  19.73972 13.56610 1.000 50.73624 ? 9   GLU A CB  1 
ATOM   65   C CG  . GLU A 1 14  ? 14.72192  19.40659 13.31508 1.000 62.95751 ? 9   GLU A CG  1 
ATOM   66   C CD  . GLU A 1 14  ? 15.05310  17.97175 13.67701 1.000 70.07528 ? 9   GLU A CD  1 
ATOM   67   O OE1 . GLU A 1 14  ? 14.13122  17.12410 13.69646 1.000 69.98604 ? 9   GLU A OE1 1 
ATOM   68   O OE2 . GLU A 1 14  ? 16.23719  17.69645 13.94804 1.000 74.04452 ? 9   GLU A OE2 1 
ATOM   69   N N   . GLN A 1 15  ? 12.45197  22.21705 15.26500 1.000 42.17947 ? 10  GLN A N   1 
ATOM   70   C CA  . GLN A 1 15  ? 12.70587  23.55572 15.78080 1.000 39.98595 ? 10  GLN A CA  1 
ATOM   71   C C   . GLN A 1 15  ? 12.57400  23.59806 17.29789 1.000 38.60368 ? 10  GLN A C   1 
ATOM   72   O O   . GLN A 1 15  ? 13.42238  24.18434 17.97880 1.000 49.91716 ? 10  GLN A O   1 
ATOM   73   C CB  . GLN A 1 15  ? 11.75385  24.55186 15.11989 1.000 38.61118 ? 10  GLN A CB  1 
ATOM   74   C CG  . GLN A 1 15  ? 11.98466  24.72054 13.61546 1.000 40.18171 ? 10  GLN A CG  1 
ATOM   75   C CD  . GLN A 1 15  ? 11.24672  25.92184 13.05641 1.000 43.31890 ? 10  GLN A CD  1 
ATOM   76   O OE1 . GLN A 1 15  ? 10.07194  26.13388 13.35518 1.000 42.75731 ? 10  GLN A OE1 1 
ATOM   77   N NE2 . GLN A 1 15  ? 11.94019  26.72584 12.25348 1.000 39.36667 ? 10  GLN A NE2 1 
ATOM   78   N N   . TRP A 1 16  ? 11.52762  22.97209 17.84838 1.000 38.18216 ? 11  TRP A N   1 
ATOM   79   C CA  . TRP A 1 16  ? 11.33868  22.98478 19.29957 1.000 43.02641 ? 11  TRP A CA  1 
ATOM   80   C C   . TRP A 1 16  ? 12.50172  22.30603 20.01230 1.000 46.26961 ? 11  TRP A C   1 
ATOM   81   O O   . TRP A 1 16  ? 13.01668  22.82085 21.01040 1.000 46.11277 ? 11  TRP A O   1 
ATOM   82   C CB  . TRP A 1 16  ? 10.02016  22.30931 19.67557 1.000 38.07922 ? 11  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 16  ? 8.81344   23.22405 19.65353 1.000 33.12206 ? 11  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 16  ? 7.66161   23.05659 18.92112 1.000 31.97556 ? 11  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 16  ? 8.63978   24.44005 20.40165 1.000 29.70348 ? 11  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 16  ? 6.78690   24.09596 19.17376 1.000 36.34038 ? 11  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 16  ? 7.36448   24.95631 20.07507 1.000 33.61026 ? 11  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 16  ? 9.44127   25.14521 21.31121 1.000 38.65934 ? 11  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 16  ? 6.87538   26.14218 20.62730 1.000 35.41742 ? 11  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 16  ? 8.95191   26.32808 21.86049 1.000 35.30691 ? 11  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 16  ? 7.68113   26.80927 21.51795 1.000 34.34786 ? 11  TRP A CH2 1 
ATOM   92   N N   . ARG A 1 17  ? 12.91689  21.13383 19.52261 1.000 48.60141 ? 12  ARG A N   1 
ATOM   93   C CA  . ARG A 1 17  ? 14.07237  20.45733 20.10505 1.000 55.91544 ? 12  ARG A CA  1 
ATOM   94   C C   . ARG A 1 17  ? 15.29248  21.36656 20.10701 1.000 54.63170 ? 12  ARG A C   1 
ATOM   95   O O   . ARG A 1 17  ? 16.07248  21.37433 21.06897 1.000 58.28068 ? 12  ARG A O   1 
ATOM   96   C CB  . ARG A 1 17  ? 14.36511  19.16239 19.34461 1.000 58.13906 ? 12  ARG A CB  1 
ATOM   97   C CG  . ARG A 1 17  ? 13.49493  17.98741 19.76630 1.000 64.79498 ? 12  ARG A CG  1 
ATOM   98   C CD  . ARG A 1 17  ? 13.63468  16.82003 18.80754 1.000 73.99072 ? 12  ARG A CD  1 
ATOM   99   N NE  . ARG A 1 17  ? 12.80176  15.68701 19.20078 1.000 80.73847 ? 12  ARG A NE  1 
ATOM   100  C CZ  . ARG A 1 17  ? 12.43731  14.70734 18.37813 1.000 82.44522 ? 12  ARG A CZ  1 
ATOM   101  N NH1 . ARG A 1 17  ? 12.82700  14.72439 17.10881 1.000 78.22916 ? 12  ARG A NH1 1 
ATOM   102  N NH2 . ARG A 1 17  ? 11.67268  13.71648 18.82152 1.000 85.66605 ? 12  ARG A NH2 1 
ATOM   103  N N   . SER A 1 18  ? 15.45672  22.16152 19.04876 1.000 51.30615 ? 13  SER A N   1 
ATOM   104  C CA  . SER A 1 18  ? 16.56208  23.11210 18.99639 1.000 47.61589 ? 13  SER A CA  1 
ATOM   105  C C   . SER A 1 18  ? 16.36263  24.24703 19.99587 1.000 49.13998 ? 13  SER A C   1 
ATOM   106  O O   . SER A 1 18  ? 17.28824  24.61006 20.72862 1.000 53.79014 ? 13  SER A O   1 
ATOM   107  C CB  . SER A 1 18  ? 16.70493  23.65771 17.57513 1.000 48.30015 ? 13  SER A CB  1 
ATOM   108  O OG  . SER A 1 18  ? 17.51515  24.81679 17.55721 1.000 56.02764 ? 13  SER A OG  1 
ATOM   109  N N   . GLU A 1 19  ? 15.14764  24.80444 20.06178 1.000 45.72769 ? 14  GLU A N   1 
ATOM   110  C CA  . GLU A 1 19  ? 14.92839  26.02453 20.83513 1.000 41.37267 ? 14  GLU A CA  1 
ATOM   111  C C   . GLU A 1 19  ? 14.68702  25.75476 22.31812 1.000 48.27159 ? 14  GLU A C   1 
ATOM   112  O O   . GLU A 1 19  ? 15.08494  26.56832 23.15817 1.000 54.55441 ? 14  GLU A O   1 
ATOM   113  C CB  . GLU A 1 19  ? 13.75006  26.81508 20.26312 1.000 42.32734 ? 14  GLU A CB  1 
ATOM   114  C CG  . GLU A 1 19  ? 14.07885  27.63221 19.02213 1.000 46.43971 ? 14  GLU A CG  1 
ATOM   115  C CD  . GLU A 1 19  ? 15.05927  28.76285 19.30995 1.000 52.00935 ? 14  GLU A CD  1 
ATOM   116  O OE1 . GLU A 1 19  ? 14.97314  29.38133 20.39898 1.000 47.97031 ? 14  GLU A OE1 1 
ATOM   117  O OE2 . GLU A 1 19  ? 15.92100  29.02981 18.44236 1.000 50.73085 ? 14  GLU A OE2 1 
ATOM   118  N N   . ARG A 1 20  ? 14.02121  24.65159 22.65273 1.000 48.13651 ? 15  ARG A N   1 
ATOM   119  C CA  . ARG A 1 20  ? 13.65981  24.30917 24.02858 1.000 50.47295 ? 15  ARG A CA  1 
ATOM   120  C C   . ARG A 1 20  ? 14.13913  22.89519 24.30817 1.000 53.02887 ? 15  ARG A C   1 
ATOM   121  O O   . ARG A 1 20  ? 13.32866  21.97394 24.47993 1.000 51.22481 ? 15  ARG A O   1 
ATOM   122  C CB  . ARG A 1 20  ? 12.15028  24.42117 24.25608 1.000 47.08889 ? 15  ARG A CB  1 
ATOM   123  C CG  . ARG A 1 20  ? 11.59023  25.83805 24.27301 1.000 40.24202 ? 15  ARG A CG  1 
ATOM   124  C CD  . ARG A 1 20  ? 12.17121  26.65108 25.42333 1.000 43.12167 ? 15  ARG A CD  1 
ATOM   125  N NE  . ARG A 1 20  ? 11.85787  26.06686 26.72373 1.000 52.02691 ? 15  ARG A NE  1 
ATOM   126  C CZ  . ARG A 1 20  ? 10.76254  26.33717 27.43380 1.000 55.19468 ? 15  ARG A CZ  1 
ATOM   127  N NH1 . ARG A 1 20  ? 9.84564   27.17860 26.96907 1.000 53.09633 ? 15  ARG A NH1 1 
ATOM   128  N NH2 . ARG A 1 20  ? 10.57584  25.75013 28.61153 1.000 55.84531 ? 15  ARG A NH2 1 
ATOM   129  N N   . PRO A 1 21  ? 15.45463  22.67529 24.36343 1.000 56.53336 ? 16  PRO A N   1 
ATOM   130  C CA  . PRO A 1 21  ? 15.95563  21.31910 24.62228 1.000 57.62856 ? 16  PRO A CA  1 
ATOM   131  C C   . PRO A 1 21  ? 15.51546  20.77107 25.96752 1.000 59.61331 ? 16  PRO A C   1 
ATOM   132  O O   . PRO A 1 21  ? 15.59251  19.55551 26.18487 1.000 63.46450 ? 16  PRO A O   1 
ATOM   133  C CB  . PRO A 1 21  ? 17.47687  21.48482 24.54487 1.000 60.83779 ? 16  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 21  ? 17.71048  22.91770 24.86972 1.000 61.56246 ? 16  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 21  ? 16.54688  23.66528 24.30488 1.000 57.13773 ? 16  PRO A CD  1 
ATOM   136  N N   . ASP A 1 22  ? 15.04373  21.63174 26.87045 1.000 57.99968 ? 17  ASP A N   1 
ATOM   137  C CA  . ASP A 1 22  ? 14.44254  21.19567 28.12374 1.000 60.56829 ? 17  ASP A CA  1 
ATOM   138  C C   . ASP A 1 22  ? 13.08636  20.52695 27.91743 1.000 64.24197 ? 17  ASP A C   1 
ATOM   139  O O   . ASP A 1 22  ? 12.54721  19.95486 28.87417 1.000 63.28622 ? 17  ASP A O   1 
ATOM   140  C CB  . ASP A 1 22  ? 14.29099  22.39511 29.06380 1.000 59.21828 ? 17  ASP A CB  1 
ATOM   141  C CG  . ASP A 1 22  ? 13.36713  23.46922 28.49278 1.000 60.34378 ? 17  ASP A CG  1 
ATOM   142  O OD1 . ASP A 1 22  ? 13.69012  24.03622 27.42324 1.000 57.88395 ? 17  ASP A OD1 1 
ATOM   143  O OD2 . ASP A 1 22  ? 12.30052  23.72127 29.09434 1.000 59.43742 ? 17  ASP A OD2 1 
ATOM   144  N N   . LEU A 1 23  ? 12.53457  20.59185 26.70095 1.000 58.80139 ? 18  LEU A N   1 
ATOM   145  C CA  . LEU A 1 23  ? 11.21487  20.07378 26.36129 1.000 61.00722 ? 18  LEU A CA  1 
ATOM   146  C C   . LEU A 1 23  ? 11.31945  18.71527 25.68542 1.000 57.92556 ? 18  LEU A C   1 
ATOM   147  O O   . LEU A 1 23  ? 12.24866  18.46886 24.91422 1.000 59.03347 ? 18  LEU A O   1 
ATOM   148  C CB  . LEU A 1 23  ? 10.49443  21.01765 25.39612 1.000 65.37898 ? 18  LEU A CB  1 
ATOM   149  C CG  . LEU A 1 23  ? 9.46761   22.03571 25.86541 1.000 65.28615 ? 18  LEU A CG  1 
ATOM   150  C CD1 . LEU A 1 23  ? 8.69249   22.51099 24.65310 1.000 59.59599 ? 18  LEU A CD1 1 
ATOM   151  C CD2 . LEU A 1 23  ? 8.55709   21.41696 26.89120 1.000 67.35183 ? 18  LEU A CD2 1 
ATOM   152  N N   . ASP A 1 24  ? 10.33886  17.84708 25.94397 1.000 52.09818 ? 19  ASP A N   1 
ATOM   153  C CA  . ASP A 1 24  ? 10.17053  16.67428 25.10027 1.000 52.96911 ? 19  ASP A CA  1 
ATOM   154  C C   . ASP A 1 24  ? 8.96171   16.91094 24.20658 1.000 49.60951 ? 19  ASP A C   1 
ATOM   155  O O   . ASP A 1 24  ? 7.81916   16.76304 24.66543 1.000 45.03153 ? 19  ASP A O   1 
ATOM   156  C CB  . ASP A 1 24  ? 9.98668   15.40294 25.92521 1.000 62.39826 ? 19  ASP A CB  1 
ATOM   157  C CG  . ASP A 1 24  ? 10.03375  14.15675 25.06953 1.000 73.30696 ? 19  ASP A CG  1 
ATOM   158  O OD1 . ASP A 1 24  ? 10.55108  14.24816 23.93656 1.000 79.75348 ? 19  ASP A OD1 1 
ATOM   159  O OD2 . ASP A 1 24  ? 9.54188   13.09742 25.51278 1.000 78.83030 ? 19  ASP A OD2 1 
ATOM   160  N N   . PRO A 1 25  ? 9.15049   17.29608 22.94580 1.000 50.02083 ? 20  PRO A N   1 
ATOM   161  C CA  . PRO A 1 25  ? 8.00572   17.66463 22.09752 1.000 46.19048 ? 20  PRO A CA  1 
ATOM   162  C C   . PRO A 1 25  ? 7.48935   16.52259 21.23921 1.000 47.37016 ? 20  PRO A C   1 
ATOM   163  O O   . PRO A 1 25  ? 6.80527   16.76174 20.23817 1.000 50.06095 ? 20  PRO A O   1 
ATOM   164  C CB  . PRO A 1 25  ? 8.58866   18.77592 21.22205 1.000 42.33375 ? 20  PRO A CB  1 
ATOM   165  C CG  . PRO A 1 25  ? 10.01224  18.32676 21.01529 1.000 45.34358 ? 20  PRO A CG  1 
ATOM   166  C CD  . PRO A 1 25  ? 10.43724  17.61562 22.29969 1.000 47.16754 ? 20  PRO A CD  1 
ATOM   167  N N   . SER A 1 26  ? 7.80940   15.28514 21.62141 1.000 50.82084 ? 21  SER A N   1 
ATOM   168  C CA  . SER A 1 26  ? 7.52802   14.13710 20.76402 1.000 57.39256 ? 21  SER A CA  1 
ATOM   169  C C   . SER A 1 26  ? 6.03873   14.01668 20.45816 1.000 53.68197 ? 21  SER A C   1 
ATOM   170  O O   . SER A 1 26  ? 5.64940   13.78092 19.30622 1.000 56.23707 ? 21  SER A O   1 
ATOM   171  C CB  . SER A 1 26  ? 8.05137   12.85912 21.42408 1.000 62.46411 ? 21  SER A CB  1 
ATOM   172  O OG  . SER A 1 26  ? 7.53550   12.71100 22.73680 1.000 68.46715 ? 21  SER A OG  1 
ATOM   173  N N   . SER A 1 27  ? 5.19045   14.20707 21.47276 1.000 44.70317 ? 22  SER A N   1 
ATOM   174  C CA  . SER A 1 27  ? 3.74256   14.09961 21.30244 1.000 40.92657 ? 22  SER A CA  1 
ATOM   175  C C   . SER A 1 27  ? 3.20352   15.00120 20.19967 1.000 38.34689 ? 22  SER A C   1 
ATOM   176  O O   . SER A 1 27  ? 2.06967   14.79703 19.75157 1.000 40.47538 ? 22  SER A O   1 
ATOM   177  C CB  . SER A 1 27  ? 3.04545   14.44095 22.61834 1.000 53.19437 ? 22  SER A CB  1 
ATOM   178  O OG  . SER A 1 27  ? 3.38253   15.75260 23.04394 1.000 51.15963 ? 22  SER A OG  1 
ATOM   179  N N   . MET A 1 28  ? 3.98355   15.99232 19.75863 1.000 37.22525 ? 23  MET A N   1 
ATOM   180  C CA  . MET A 1 28  ? 3.49786   16.94634 18.76313 1.000 44.18939 ? 23  MET A CA  1 
ATOM   181  C C   . MET A 1 28  ? 3.35359   16.31568 17.38404 1.000 40.11728 ? 23  MET A C   1 
ATOM   182  O O   . MET A 1 28  ? 2.52992   16.77404 16.58510 1.000 38.67775 ? 23  MET A O   1 
ATOM   183  C CB  . MET A 1 28  ? 4.43560   18.14822 18.66902 1.000 38.06465 ? 23  MET A CB  1 
ATOM   184  C CG  . MET A 1 28  ? 4.37549   19.08467 19.84189 1.000 40.49029 ? 23  MET A CG  1 
ATOM   185  S SD  . MET A 1 28  ? 5.43855   20.50641 19.53369 1.000 44.21045 ? 23  MET A SD  1 
ATOM   186  C CE  . MET A 1 28  ? 5.06936   21.52339 20.96222 1.000 41.92049 ? 23  MET A CE  1 
ATOM   187  N N   . ILE A 1 29  ? 4.14487   15.28361 17.08309 1.000 37.34561 ? 24  ILE A N   1 
ATOM   188  C CA  . ILE A 1 29  ? 4.10546   14.67830 15.75289 1.000 42.32854 ? 24  ILE A CA  1 
ATOM   189  C C   . ILE A 1 29  ? 2.75213   14.02920 15.50391 1.000 37.90734 ? 24  ILE A C   1 
ATOM   190  O O   . ILE A 1 29  ? 2.04350   14.37638 14.55277 1.000 42.06189 ? 24  ILE A O   1 
ATOM   191  C CB  . ILE A 1 29  ? 5.24437   13.65905 15.58476 1.000 49.27291 ? 24  ILE A CB  1 
ATOM   192  C CG1 . ILE A 1 29  ? 6.59716   14.33019 15.81591 1.000 50.00974 ? 24  ILE A CG1 1 
ATOM   193  C CG2 . ILE A 1 29  ? 5.17716   13.00873 14.20269 1.000 46.82149 ? 24  ILE A CG2 1 
ATOM   194  C CD1 . ILE A 1 29  ? 7.24585   14.79869 14.58192 1.000 54.95982 ? 24  ILE A CD1 1 
ATOM   195  N N   . VAL A 1 30  ? 2.37395   13.07791 16.36221 1.000 34.21347 ? 25  VAL A N   1 
ATOM   196  C CA  . VAL A 1 30  ? 1.15428   12.31077 16.12794 1.000 38.24790 ? 25  VAL A CA  1 
ATOM   197  C C   . VAL A 1 30  ? -0.07470  13.21423 16.20807 1.000 40.53514 ? 25  VAL A C   1 
ATOM   198  O O   . VAL A 1 30  ? -0.96571  13.14282 15.35027 1.000 40.80318 ? 25  VAL A O   1 
ATOM   199  C CB  . VAL A 1 30  ? 1.07564   11.11313 17.10253 1.000 47.81984 ? 25  VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 30  ? 1.21245   11.56380 18.54750 1.000 51.70953 ? 25  VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 30  ? -0.20833  10.31014 16.90537 1.000 43.25102 ? 25  VAL A CG2 1 
ATOM   202  N N   . LEU A 1 31  ? -0.13160  14.10712 17.20555 1.000 33.07691 ? 26  LEU A N   1 
ATOM   203  C CA  . LEU A 1 31  ? -1.33100  14.92916 17.34870 1.000 35.70237 ? 26  LEU A CA  1 
ATOM   204  C C   . LEU A 1 31  ? -1.36202  16.06728 16.32839 1.000 36.30646 ? 26  LEU A C   1 
ATOM   205  O O   . LEU A 1 31  ? -2.44607  16.46293 15.88230 1.000 32.73781 ? 26  LEU A O   1 
ATOM   206  C CB  . LEU A 1 31  ? -1.44563  15.47493 18.77874 1.000 34.10659 ? 26  LEU A CB  1 
ATOM   207  C CG  . LEU A 1 31  ? -1.75882  14.48354 19.91103 1.000 38.15771 ? 26  LEU A CG  1 
ATOM   208  C CD1 . LEU A 1 31  ? -1.95062  15.19396 21.25212 1.000 35.37997 ? 26  LEU A CD1 1 
ATOM   209  C CD2 . LEU A 1 31  ? -2.98672  13.64258 19.58487 1.000 39.10272 ? 26  LEU A CD2 1 
ATOM   210  N N   . GLY A 1 32  ? -0.19626  16.59866 15.94129 1.000 32.10929 ? 27  GLY A N   1 
ATOM   211  C CA  . GLY A 1 32  ? -0.16720  17.57004 14.85760 1.000 31.87922 ? 27  GLY A CA  1 
ATOM   212  C C   . GLY A 1 32  ? -0.58963  16.95935 13.53337 1.000 31.99084 ? 27  GLY A C   1 
ATOM   213  O O   . GLY A 1 32  ? -1.34394  17.57055 12.77014 1.000 32.15884 ? 27  GLY A O   1 
ATOM   214  N N   . ARG A 1 33  ? -0.11860  15.73918 13.24656 1.000 30.42914 ? 28  ARG A N   1 
ATOM   215  C CA  . ARG A 1 33  ? -0.55067  15.06713 12.02231 1.000 32.23352 ? 28  ARG A CA  1 
ATOM   216  C C   . ARG A 1 33  ? -2.01666  14.67464 12.08591 1.000 31.62852 ? 28  ARG A C   1 
ATOM   217  O O   . ARG A 1 33  ? -2.70785  14.71614 11.06093 1.000 33.44315 ? 28  ARG A O   1 
ATOM   218  C CB  . ARG A 1 33  ? 0.30236   13.83204 11.75264 1.000 32.45040 ? 28  ARG A CB  1 
ATOM   219  C CG  . ARG A 1 33  ? 1.63663   14.17200 11.15661 1.000 33.88241 ? 28  ARG A CG  1 
ATOM   220  C CD  . ARG A 1 33  ? 2.48044   12.94574 10.91406 1.000 34.97406 ? 28  ARG A CD  1 
ATOM   221  N NE  . ARG A 1 33  ? 3.84428   13.37552 10.66625 1.000 35.60110 ? 28  ARG A NE  1 
ATOM   222  C CZ  . ARG A 1 33  ? 4.91048   12.60216 10.79286 1.000 41.70069 ? 28  ARG A CZ  1 
ATOM   223  N NH1 . ARG A 1 33  ? 4.77611   11.32931 11.16393 1.000 39.16976 ? 28  ARG A NH1 1 
ATOM   224  N NH2 . ARG A 1 33  ? 6.10873   13.11662 10.55281 1.000 37.05506 ? 28  ARG A NH2 1 
ATOM   225  N N   . LEU A 1 34  ? -2.50342  14.28760 13.27032 1.000 32.47197 ? 29  LEU A N   1 
ATOM   226  C CA  . LEU A 1 34  ? -3.91732  13.95329 13.41777 1.000 30.20491 ? 29  LEU A CA  1 
ATOM   227  C C   . LEU A 1 34  ? -4.79386  15.14006 13.05678 1.000 28.33838 ? 29  LEU A C   1 
ATOM   228  O O   . LEU A 1 34  ? -5.74168  15.01741 12.26805 1.000 27.89176 ? 29  LEU A O   1 
ATOM   229  C CB  . LEU A 1 34  ? -4.20954  13.49527 14.84907 1.000 30.02798 ? 29  LEU A CB  1 
ATOM   230  C CG  . LEU A 1 34  ? -5.68830  13.27514 15.18679 1.000 33.10799 ? 29  LEU A CG  1 
ATOM   231  C CD1 . LEU A 1 34  ? -6.16475  11.96891 14.57902 1.000 39.56410 ? 29  LEU A CD1 1 
ATOM   232  C CD2 . LEU A 1 34  ? -5.91003  13.24349 16.69611 1.000 37.86814 ? 29  LEU A CD2 1 
ATOM   233  N N   . GLN A 1 35  ? -4.50747  16.30536 13.64101 1.000 27.58916 ? 30  GLN A N   1 
ATOM   234  C CA  . GLN A 1 35  ? -5.37379  17.45725 13.40287 1.000 32.98802 ? 30  GLN A CA  1 
ATOM   235  C C   . GLN A 1 35  ? -5.19377  17.99508 11.98748 1.000 29.01155 ? 30  GLN A C   1 
ATOM   236  O O   . GLN A 1 35  ? -6.16204  18.43198 11.35153 1.000 26.79162 ? 30  GLN A O   1 
ATOM   237  C CB  . GLN A 1 35  ? -5.10292  18.54125 14.45088 1.000 38.17730 ? 30  GLN A CB  1 
ATOM   238  C CG  . GLN A 1 35  ? -5.22439  18.02560 15.90214 1.000 54.78688 ? 30  GLN A CG  1 
ATOM   239  C CD  . GLN A 1 35  ? -4.98387  19.10100 16.96307 1.000 67.06116 ? 30  GLN A CD  1 
ATOM   240  O OE1 . GLN A 1 35  ? -5.90367  19.82619 17.34306 1.000 72.21128 ? 30  GLN A OE1 1 
ATOM   241  N NE2 . GLN A 1 35  ? -3.74635  19.19532 17.45218 1.000 65.90240 ? 30  GLN A NE2 1 
ATOM   242  N N   . GLU A 1 36  ? -3.96604  17.98639 11.47601 1.000 29.85354 ? 31  GLU A N   1 
ATOM   243  C CA  . GLU A 1 36  ? -3.76258  18.44316 10.10099 1.000 34.72335 ? 31  GLU A CA  1 
ATOM   244  C C   . GLU A 1 36  ? -4.44415  17.51688 9.09726  1.000 29.92568 ? 31  GLU A C   1 
ATOM   245  O O   . GLU A 1 36  ? -5.04103  17.98356 8.11261  1.000 31.11855 ? 31  GLU A O   1 
ATOM   246  C CB  . GLU A 1 36  ? -2.26597  18.56062 9.80143  1.000 37.55397 ? 31  GLU A CB  1 
ATOM   247  C CG  . GLU A 1 36  ? -1.95017  19.07228 8.40187  1.000 41.56766 ? 31  GLU A CG  1 
ATOM   248  C CD  . GLU A 1 36  ? -2.29096  20.54367 8.22020  1.000 46.27723 ? 31  GLU A CD  1 
ATOM   249  O OE1 . GLU A 1 36  ? -2.88090  21.16133 9.14453  1.000 39.42216 ? 31  GLU A OE1 1 
ATOM   250  O OE2 . GLU A 1 36  ? -1.95150  21.08810 7.14440  1.000 39.74244 ? 31  GLU A OE2 1 
ATOM   251  N N   . ALA A 1 37  ? -4.36460  16.20038 9.31395  1.000 26.88260 ? 32  ALA A N   1 
ATOM   252  C CA  . ALA A 1 37  ? -4.99833  15.28032 8.37512  1.000 26.90159 ? 32  ALA A CA  1 
ATOM   253  C C   . ALA A 1 37  ? -6.51202  15.43932 8.39387  1.000 33.43955 ? 32  ALA A C   1 
ATOM   254  O O   . ALA A 1 37  ? -7.15077  15.44455 7.33869  1.000 26.38936 ? 32  ALA A O   1 
ATOM   255  C CB  . ALA A 1 37  ? -4.59618  13.83160 8.67550  1.000 25.40884 ? 32  ALA A CB  1 
ATOM   256  N N   . ALA A 1 38  ? -7.10686  15.56783 9.58236  1.000 28.32250 ? 33  ALA A N   1 
ATOM   257  C CA  . ALA A 1 38  ? -8.54829  15.76202 9.64635  1.000 27.20970 ? 33  ALA A CA  1 
ATOM   258  C C   . ALA A 1 38  ? -8.94820  17.04487 8.93456  1.000 27.95111 ? 33  ALA A C   1 
ATOM   259  O O   . ALA A 1 38  ? -9.93432  17.07235 8.18882  1.000 28.83553 ? 33  ALA A O   1 
ATOM   260  C CB  . ALA A 1 38  ? -9.01885  15.78543 11.10848 1.000 23.61125 ? 33  ALA A CB  1 
ATOM   261  N N   . LEU A 1 39  ? -8.18367  18.11628 9.14597  1.000 27.44772 ? 34  LEU A N   1 
ATOM   262  C CA  . LEU A 1 39  ? -8.51963  19.41033 8.55922  1.000 31.73552 ? 34  LEU A CA  1 
ATOM   263  C C   . LEU A 1 39  ? -8.39204  19.38706 7.03726  1.000 34.25824 ? 34  LEU A C   1 
ATOM   264  O O   . LEU A 1 39  ? -9.30367  19.82325 6.31988  1.000 33.85670 ? 34  LEU A O   1 
ATOM   265  C CB  . LEU A 1 39  ? -7.62030  20.49135 9.16434  1.000 36.91232 ? 34  LEU A CB  1 
ATOM   266  C CG  . LEU A 1 39  ? -7.75711  21.90838 8.60674  1.000 44.24087 ? 34  LEU A CG  1 
ATOM   267  C CD1 . LEU A 1 39  ? -9.13694  22.47241 8.92010  1.000 44.25137 ? 34  LEU A CD1 1 
ATOM   268  C CD2 . LEU A 1 39  ? -6.64504  22.84179 9.12561  1.000 41.01566 ? 34  LEU A CD2 1 
ATOM   269  N N   . VAL A 1 40  ? -7.25966  18.89638 6.52367  1.000 31.98328 ? 35  VAL A N   1 
ATOM   270  C CA  . VAL A 1 40  ? -7.02058  18.94066 5.07956  1.000 29.59824 ? 35  VAL A CA  1 
ATOM   271  C C   . VAL A 1 40  ? -8.01768  18.05904 4.34565  1.000 34.80952 ? 35  VAL A C   1 
ATOM   272  O O   . VAL A 1 40  ? -8.51910  18.42510 3.26870  1.000 33.91550 ? 35  VAL A O   1 
ATOM   273  C CB  . VAL A 1 40  ? -5.56875  18.53405 4.76373  1.000 32.75277 ? 35  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 40  ? -5.35748  18.42545 3.24766  1.000 41.77523 ? 35  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 40  ? -4.60296  19.54603 5.37577  1.000 34.77902 ? 35  VAL A CG2 1 
ATOM   276  N N   . ILE A 1 41  ? -8.32480  16.88642 4.91383  1.000 30.88960 ? 36  ILE A N   1 
ATOM   277  C CA  . ILE A 1 41  ? -9.26402  15.96861 4.27208  1.000 31.48723 ? 36  ILE A CA  1 
ATOM   278  C C   . ILE A 1 41  ? -10.66389 16.57049 4.24478  1.000 32.46022 ? 36  ILE A C   1 
ATOM   279  O O   . ILE A 1 41  ? -11.35182 16.53574 3.21692  1.000 38.00063 ? 36  ILE A O   1 
ATOM   280  C CB  . ILE A 1 41  ? -9.23998  14.59895 4.97243  1.000 32.20555 ? 36  ILE A CB  1 
ATOM   281  C CG1 . ILE A 1 41  ? -7.90600  13.89683 4.68130  1.000 35.74811 ? 36  ILE A CG1 1 
ATOM   282  C CG2 . ILE A 1 41  ? -10.42157 13.72193 4.51914  1.000 27.51752 ? 36  ILE A CG2 1 
ATOM   283  C CD1 . ILE A 1 41  ? -7.70700  12.60848 5.45612  1.000 39.52910 ? 36  ILE A CD1 1 
ATOM   284  N N   . ALA A 1 42  ? -11.10633 17.13864 5.36858  1.000 33.17042 ? 37  ALA A N   1 
ATOM   285  C CA  . ALA A 1 42  ? -12.39400 17.81903 5.37593  1.000 34.89393 ? 37  ALA A CA  1 
ATOM   286  C C   . ALA A 1 42  ? -12.39532 18.98229 4.39768  1.000 36.72682 ? 37  ALA A C   1 
ATOM   287  O O   . ALA A 1 42  ? -13.24913 19.05329 3.50083  1.000 34.28817 ? 37  ALA A O   1 
ATOM   288  C CB  . ALA A 1 42  ? -12.72886 18.30169 6.78596  1.000 36.79670 ? 37  ALA A CB  1 
ATOM   289  N N   . ARG A 1 43  ? -11.41263 19.88474 4.52575  1.000 30.64575 ? 38  ARG A N   1 
ATOM   290  C CA  . ARG A 1 43  ? -11.42689 21.12224 3.75022  1.000 35.12511 ? 38  ARG A CA  1 
ATOM   291  C C   . ARG A 1 43  ? -11.28674 20.86230 2.25669  1.000 36.06560 ? 38  ARG A C   1 
ATOM   292  O O   . ARG A 1 43  ? -11.99256 21.47564 1.44470  1.000 36.96890 ? 38  ARG A O   1 
ATOM   293  C CB  . ARG A 1 43  ? -10.31095 22.06004 4.20492  1.000 36.35235 ? 38  ARG A CB  1 
ATOM   294  C CG  . ARG A 1 43  ? -10.19314 23.30269 3.31576  1.000 40.02309 ? 38  ARG A CG  1 
ATOM   295  C CD  . ARG A 1 43  ? -9.00041  24.16733 3.69049  1.000 43.74215 ? 38  ARG A CD  1 
ATOM   296  N NE  . ARG A 1 43  ? -7.74228  23.56697 3.26739  1.000 51.95971 ? 38  ARG A NE  1 
ATOM   297  C CZ  . ARG A 1 43  ? -6.68796  23.39212 4.05944  1.000 63.21996 ? 38  ARG A CZ  1 
ATOM   298  N NH1 . ARG A 1 43  ? -6.72137  23.78846 5.33019  1.000 53.69966 ? 38  ARG A NH1 1 
ATOM   299  N NH2 . ARG A 1 43  ? -5.58913  22.83077 3.56908  1.000 72.62434 ? 38  ARG A NH2 1 
ATOM   300  N N   . ASP A 1 44  ? -10.34938 19.99531 1.87119  1.000 37.80737 ? 39  ASP A N   1 
ATOM   301  C CA  . ASP A 1 44  ? -9.96776  19.83902 0.47351  1.000 44.30253 ? 39  ASP A CA  1 
ATOM   302  C C   . ASP A 1 44  ? -10.61592 18.64582 -0.21758 1.000 45.64394 ? 39  ASP A C   1 
ATOM   303  O O   . ASP A 1 44  ? -10.57824 18.57800 -1.45091 1.000 44.68440 ? 39  ASP A O   1 
ATOM   304  C CB  . ASP A 1 44  ? -8.44489  19.70736 0.34803  1.000 48.55977 ? 39  ASP A CB  1 
ATOM   305  C CG  . ASP A 1 44  ? -7.72730  21.02052 0.55302  1.000 53.45245 ? 39  ASP A CG  1 
ATOM   306  O OD1 . ASP A 1 44  ? -8.40597  22.06177 0.71208  1.000 51.62427 ? 39  ASP A OD1 1 
ATOM   307  O OD2 . ASP A 1 44  ? -6.48033  21.00756 0.54681  1.000 56.91345 ? 39  ASP A OD2 1 
ATOM   308  N N   . ARG A 1 45  ? -11.20028 17.70633 0.52580  1.000 41.64223 ? 40  ARG A N   1 
ATOM   309  C CA  . ARG A 1 45  ? -11.69840 16.48225 -0.09734 1.000 42.45440 ? 40  ARG A CA  1 
ATOM   310  C C   . ARG A 1 45  ? -13.17769 16.22989 0.17907  1.000 39.72618 ? 40  ARG A C   1 
ATOM   311  O O   . ARG A 1 45  ? -13.96315 16.04312 -0.75861 1.000 33.40122 ? 40  ARG A O   1 
ATOM   312  C CB  . ARG A 1 45  ? -10.88194 15.27338 0.37635  1.000 42.72909 ? 40  ARG A CB  1 
ATOM   313  C CG  . ARG A 1 45  ? -9.37992  15.39402 0.15258  1.000 42.02537 ? 40  ARG A CG  1 
ATOM   314  C CD  . ARG A 1 45  ? -9.02619  15.43059 -1.32862 1.000 43.97312 ? 40  ARG A CD  1 
ATOM   315  N NE  . ARG A 1 45  ? -9.41141  14.21493 -2.04443 1.000 47.23957 ? 40  ARG A NE  1 
ATOM   316  C CZ  . ARG A 1 45  ? -8.58516  13.20258 -2.30177 1.000 55.99208 ? 40  ARG A CZ  1 
ATOM   317  N NH1 . ARG A 1 45  ? -7.32650  13.24471 -1.88889 1.000 58.43218 ? 40  ARG A NH1 1 
ATOM   318  N NH2 . ARG A 1 45  ? -9.01808  12.14043 -2.96779 1.000 56.89906 ? 40  ARG A NH2 1 
ATOM   319  N N   . LEU A 1 46  ? -13.56733 16.17533 1.45651  1.000 28.22847 ? 41  LEU A N   1 
ATOM   320  C CA  . LEU A 1 46  ? -14.93823 15.79960 1.78005  1.000 34.69728 ? 41  LEU A CA  1 
ATOM   321  C C   . LEU A 1 46  ? -15.89674 16.96139 1.56238  1.000 34.26165 ? 41  LEU A C   1 
ATOM   322  O O   . LEU A 1 46  ? -16.91437 16.81783 0.87610  1.000 34.18059 ? 41  LEU A O   1 
ATOM   323  C CB  . LEU A 1 46  ? -15.02783 15.31400 3.23182  1.000 29.07322 ? 41  LEU A CB  1 
ATOM   324  C CG  . LEU A 1 46  ? -14.15188 14.12707 3.62721  1.000 35.28402 ? 41  LEU A CG  1 
ATOM   325  C CD1 . LEU A 1 46  ? -14.39551 13.77792 5.09075  1.000 36.53243 ? 41  LEU A CD1 1 
ATOM   326  C CD2 . LEU A 1 46  ? -14.43337 12.94039 2.74310  1.000 40.31486 ? 41  LEU A CD2 1 
ATOM   327  N N   . ASN A 1 47  ? -15.58935 18.11547 2.15242  1.000 33.17649 ? 42  ASN A N   1 
ATOM   328  C CA  . ASN A 1 47  ? -16.49691 19.25628 2.05218  1.000 33.58147 ? 42  ASN A CA  1 
ATOM   329  C C   . ASN A 1 47  ? -16.73300 19.73108 0.62965  1.000 33.78378 ? 42  ASN A C   1 
ATOM   330  O O   . ASN A 1 47  ? -17.88404 20.10166 0.33272  1.000 35.57228 ? 42  ASN A O   1 
ATOM   331  C CB  . ASN A 1 47  ? -15.99681 20.40391 2.93143  1.000 40.07758 ? 42  ASN A CB  1 
ATOM   332  C CG  . ASN A 1 47  ? -16.09386 20.06822 4.39439  1.000 37.21822 ? 42  ASN A CG  1 
ATOM   333  O OD1 . ASN A 1 47  ? -16.60511 19.00664 4.75100  1.000 33.80790 ? 42  ASN A OD1 1 
ATOM   334  N ND2 . ASN A 1 47  ? -15.58422 20.94827 5.24991  1.000 33.33377 ? 42  ASN A ND2 1 
ATOM   335  N N   . PRO A 1 48  ? -15.75177 19.75509 -0.28754 1.000 32.92874 ? 43  PRO A N   1 
ATOM   336  C CA  . PRO A 1 48  ? -16.10029 20.06886 -1.68254 1.000 35.57140 ? 43  PRO A CA  1 
ATOM   337  C C   . PRO A 1 48  ? -17.17949 19.16337 -2.23078 1.000 42.08566 ? 43  PRO A C   1 
ATOM   338  O O   . PRO A 1 48  ? -18.10432 19.64840 -2.89182 1.000 44.28334 ? 43  PRO A O   1 
ATOM   339  C CB  . PRO A 1 48  ? -14.77301 19.88840 -2.43043 1.000 42.06986 ? 43  PRO A CB  1 
ATOM   340  C CG  . PRO A 1 48  ? -13.76233 20.26229 -1.42550 1.000 34.94243 ? 43  PRO A CG  1 
ATOM   341  C CD  . PRO A 1 48  ? -14.29135 19.65425 -0.12111 1.000 33.52283 ? 43  PRO A CD  1 
ATOM   342  N N   . LEU A 1 49  ? -17.11396 17.85922 -1.94489 1.000 41.08993 ? 44  LEU A N   1 
ATOM   343  C CA  . LEU A 1 49  ? -18.13655 16.95749 -2.46498 1.000 42.92259 ? 44  LEU A CA  1 
ATOM   344  C C   . LEU A 1 49  ? -19.49952 17.28205 -1.86439 1.000 43.66883 ? 44  LEU A C   1 
ATOM   345  O O   . LEU A 1 49  ? -20.50329 17.34965 -2.58329 1.000 39.45888 ? 44  LEU A O   1 
ATOM   346  C CB  . LEU A 1 49  ? -17.75740 15.49695 -2.19736 1.000 43.09248 ? 44  LEU A CB  1 
ATOM   347  C CG  . LEU A 1 49  ? -18.74864 14.48906 -2.80011 1.000 49.14226 ? 44  LEU A CG  1 
ATOM   348  C CD1 . LEU A 1 49  ? -18.03150 13.37794 -3.53378 1.000 52.19474 ? 44  LEU A CD1 1 
ATOM   349  C CD2 . LEU A 1 49  ? -19.67557 13.90118 -1.75404 1.000 48.50354 ? 44  LEU A CD2 1 
ATOM   350  N N   . PHE A 1 50  ? -19.55528 17.49536 -0.54853 1.000 42.34566 ? 45  PHE A N   1 
ATOM   351  C CA  . PHE A 1 50  ? -20.81684 17.88609 0.06599  1.000 40.23959 ? 45  PHE A CA  1 
ATOM   352  C C   . PHE A 1 50  ? -21.37464 19.15131 -0.57350 1.000 38.53434 ? 45  PHE A C   1 
ATOM   353  O O   . PHE A 1 50  ? -22.58989 19.26193 -0.78264 1.000 37.17366 ? 45  PHE A O   1 
ATOM   354  C CB  . PHE A 1 50  ? -20.63661 18.10299 1.56265  1.000 35.92500 ? 45  PHE A CB  1 
ATOM   355  C CG  . PHE A 1 50  ? -20.15557 16.88587 2.32191  1.000 32.83028 ? 45  PHE A CG  1 
ATOM   356  C CD1 . PHE A 1 50  ? -20.52865 15.60836 1.94755  1.000 33.57439 ? 45  PHE A CD1 1 
ATOM   357  C CD2 . PHE A 1 50  ? -19.33396 17.04126 3.43579  1.000 29.54615 ? 45  PHE A CD2 1 
ATOM   358  C CE1 . PHE A 1 50  ? -20.08079 14.49918 2.66721  1.000 29.18615 ? 45  PHE A CE1 1 
ATOM   359  C CE2 . PHE A 1 50  ? -18.89085 15.93466 4.16365  1.000 30.69008 ? 45  PHE A CE2 1 
ATOM   360  C CZ  . PHE A 1 50  ? -19.26036 14.66970 3.77926  1.000 34.02354 ? 45  PHE A CZ  1 
ATOM   361  N N   . ALA A 1 51  ? -20.50390 20.12545 -0.87293 1.000 35.02022 ? 46  ALA A N   1 
ATOM   362  C CA  . ALA A 1 51  ? -20.96410 21.38940 -1.44960 1.000 44.31166 ? 46  ALA A CA  1 
ATOM   363  C C   . ALA A 1 51  ? -21.54545 21.20220 -2.83964 1.000 51.29141 ? 46  ALA A C   1 
ATOM   364  O O   . ALA A 1 51  ? -22.39918 21.99046 -3.27254 1.000 48.70263 ? 46  ALA A O   1 
ATOM   365  C CB  . ALA A 1 51  ? -19.81466 22.39769 -1.51992 1.000 43.55596 ? 46  ALA A CB  1 
ATOM   366  N N   . ARG A 1 52  ? -21.06361 20.20225 -3.57447 1.000 48.61121 ? 47  ARG A N   1 
ATOM   367  C CA  . ARG A 1 52  ? -21.65586 19.91146 -4.87017 1.000 51.10335 ? 47  ARG A CA  1 
ATOM   368  C C   . ARG A 1 52  ? -23.09448 19.43887 -4.73623 1.000 49.69938 ? 47  ARG A C   1 
ATOM   369  O O   . ARG A 1 52  ? -23.86631 19.57181 -5.69242 1.000 45.29447 ? 47  ARG A O   1 
ATOM   370  C CB  . ARG A 1 52  ? -20.82742 18.86422 -5.60785 1.000 57.12599 ? 47  ARG A CB  1 
ATOM   371  C CG  . ARG A 1 52  ? -19.48449 19.36401 -6.12524 1.000 63.94130 ? 47  ARG A CG  1 
ATOM   372  C CD  . ARG A 1 52  ? -18.75806 18.20951 -6.77299 1.000 76.55197 ? 47  ARG A CD  1 
ATOM   373  N NE  . ARG A 1 52  ? -19.64480 17.50182 -7.69769 1.000 86.41776 ? 47  ARG A NE  1 
ATOM   374  C CZ  . ARG A 1 52  ? -19.74169 16.17738 -7.78433 1.000 89.04215 ? 47  ARG A CZ  1 
ATOM   375  N NH1 . ARG A 1 52  ? -19.00918 15.39948 -6.99429 1.000 83.35268 ? 47  ARG A NH1 1 
ATOM   376  N NH2 . ARG A 1 52  ? -20.57976 15.63014 -8.65677 1.000 93.64899 ? 47  ARG A NH2 1 
ATOM   377  N N   . TYR A 1 53  ? -23.47014 18.90033 -3.57156 1.000 46.88125 ? 48  TYR A N   1 
ATOM   378  C CA  . TYR A 1 53  ? -24.84345 18.50589 -3.29843 1.000 50.60875 ? 48  TYR A CA  1 
ATOM   379  C C   . TYR A 1 53  ? -25.61115 19.57754 -2.54286 1.000 52.13045 ? 48  TYR A C   1 
ATOM   380  O O   . TYR A 1 53  ? -26.74883 19.33542 -2.12610 1.000 48.09180 ? 48  TYR A O   1 
ATOM   381  C CB  . TYR A 1 53  ? -24.87402 17.18471 -2.52993 1.000 41.65047 ? 48  TYR A CB  1 
ATOM   382  C CG  . TYR A 1 53  ? -24.53533 16.01094 -3.41267 1.000 39.38688 ? 48  TYR A CG  1 
ATOM   383  C CD1 . TYR A 1 53  ? -23.22063 15.62928 -3.60028 1.000 38.66800 ? 48  TYR A CD1 1 
ATOM   384  C CD2 . TYR A 1 53  ? -25.52861 15.30520 -4.08866 1.000 43.92667 ? 48  TYR A CD2 1 
ATOM   385  C CE1 . TYR A 1 53  ? -22.89242 14.56360 -4.41794 1.000 50.74387 ? 48  TYR A CE1 1 
ATOM   386  C CE2 . TYR A 1 53  ? -25.21133 14.23731 -4.91226 1.000 45.60857 ? 48  TYR A CE2 1 
ATOM   387  C CZ  . TYR A 1 53  ? -23.88845 13.87597 -5.07111 1.000 54.22238 ? 48  TYR A CZ  1 
ATOM   388  O OH  . TYR A 1 53  ? -23.54747 12.82059 -5.87802 1.000 65.62514 ? 48  TYR A OH  1 
ATOM   389  N N   . GLY A 1 54  ? -25.02567 20.76373 -2.38813 1.000 49.03039 ? 49  GLY A N   1 
ATOM   390  C CA  . GLY A 1 54  ? -25.67732 21.83403 -1.66733 1.000 50.10007 ? 49  GLY A CA  1 
ATOM   391  C C   . GLY A 1 54  ? -25.62917 21.69514 -0.16386 1.000 41.71248 ? 49  GLY A C   1 
ATOM   392  O O   . GLY A 1 54  ? -26.44579 22.31202 0.52545  1.000 42.08934 ? 49  GLY A O   1 
ATOM   393  N N   . LEU A 1 55  ? -24.68236 20.92257 0.36766  1.000 39.08688 ? 50  LEU A N   1 
ATOM   394  C CA  . LEU A 1 55  ? -24.63364 20.57371 1.78446  1.000 36.98720 ? 50  LEU A CA  1 
ATOM   395  C C   . LEU A 1 55  ? -23.33037 21.02375 2.43600  1.000 39.69401 ? 50  LEU A C   1 
ATOM   396  O O   . LEU A 1 55  ? -22.25628 20.91051 1.83541  1.000 40.81429 ? 50  LEU A O   1 
ATOM   397  C CB  . LEU A 1 55  ? -24.75497 19.05794 1.97723  1.000 37.66627 ? 50  LEU A CB  1 
ATOM   398  C CG  . LEU A 1 55  ? -26.08896 18.37725 1.68802  1.000 39.69612 ? 50  LEU A CG  1 
ATOM   399  C CD1 . LEU A 1 55  ? -25.90800 16.87066 1.72259  1.000 36.22700 ? 50  LEU A CD1 1 
ATOM   400  C CD2 . LEU A 1 55  ? -27.11464 18.81110 2.72700  1.000 32.42771 ? 50  LEU A CD2 1 
ATOM   401  N N   . GLN A 1 56  ? -23.43195 21.50159 3.68656  1.000 40.37502 ? 51  GLN A N   1 
ATOM   402  C CA  . GLN A 1 56  ? -22.29776 21.57395 4.59949  1.000 42.37048 ? 51  GLN A CA  1 
ATOM   403  C C   . GLN A 1 56  ? -22.04107 20.20005 5.20796  1.000 38.75870 ? 51  GLN A C   1 
ATOM   404  O O   . GLN A 1 56  ? -22.95384 19.37523 5.29012  1.000 38.67983 ? 51  GLN A O   1 
ATOM   405  C CB  . GLN A 1 56  ? -22.57640 22.58760 5.70356  1.000 49.20888 ? 51  GLN A CB  1 
ATOM   406  C CG  . GLN A 1 56  ? -23.01598 23.95047 5.19537  1.000 62.92707 ? 51  GLN A CG  1 
ATOM   407  C CD  . GLN A 1 56  ? -23.50805 24.86093 6.31166  1.000 76.20927 ? 51  GLN A CD  1 
ATOM   408  O OE1 . GLN A 1 56  ? -23.46473 24.49739 7.48922  1.000 79.06648 ? 51  GLN A OE1 1 
ATOM   409  N NE2 . GLN A 1 56  ? -23.98294 26.05156 5.94411  1.000 79.98191 ? 51  GLN A NE2 1 
ATOM   410  N N   . PRO A 1 57  ? -20.80337 19.91745 5.64935  1.000 43.17915 ? 52  PRO A N   1 
ATOM   411  C CA  . PRO A 1 57  ? -20.53399 18.56816 6.18906  1.000 37.25099 ? 52  PRO A CA  1 
ATOM   412  C C   . PRO A 1 57  ? -21.43590 18.20733 7.34878  1.000 42.47409 ? 52  PRO A C   1 
ATOM   413  O O   . PRO A 1 57  ? -21.93913 17.07404 7.41366  1.000 37.09974 ? 52  PRO A O   1 
ATOM   414  C CB  . PRO A 1 57  ? -19.06203 18.63615 6.61605  1.000 33.54272 ? 52  PRO A CB  1 
ATOM   415  C CG  . PRO A 1 57  ? -18.78252 20.11271 6.78339  1.000 43.91902 ? 52  PRO A CG  1 
ATOM   416  C CD  . PRO A 1 57  ? -19.61665 20.78901 5.73274  1.000 46.63173 ? 52  PRO A CD  1 
ATOM   417  N N   . GLY A 1 58  ? -21.66038 19.15152 8.26524  1.000 37.80220 ? 53  GLY A N   1 
ATOM   418  C CA  . GLY A 1 58  ? -22.59525 18.89623 9.34676  1.000 35.31403 ? 53  GLY A CA  1 
ATOM   419  C C   . GLY A 1 58  ? -23.97871 18.55828 8.82506  1.000 35.90615 ? 53  GLY A C   1 
ATOM   420  O O   . GLY A 1 58  ? -24.64743 17.67305 9.35544  1.000 37.56785 ? 53  GLY A O   1 
ATOM   421  N N   . GLU A 1 59  ? -24.42224 19.25647 7.76720  1.000 32.80938 ? 54  GLU A N   1 
ATOM   422  C CA  . GLU A 1 59  ? -25.74836 18.99469 7.20545  1.000 29.84042 ? 54  GLU A CA  1 
ATOM   423  C C   . GLU A 1 59  ? -25.81431 17.61561 6.56058  1.000 31.67573 ? 54  GLU A C   1 
ATOM   424  O O   . GLU A 1 59  ? -26.83866 16.93258 6.65546  1.000 30.18384 ? 54  GLU A O   1 
ATOM   425  C CB  . GLU A 1 59  ? -26.12119 20.07764 6.18488  1.000 31.87083 ? 54  GLU A CB  1 
ATOM   426  C CG  . GLU A 1 59  ? -26.29790 21.46728 6.78738  1.000 31.62678 ? 54  GLU A CG  1 
ATOM   427  C CD  . GLU A 1 59  ? -26.47808 22.53805 5.73216  1.000 40.89974 ? 54  GLU A CD  1 
ATOM   428  O OE1 . GLU A 1 59  ? -26.09021 22.29171 4.57067  1.000 39.44908 ? 54  GLU A OE1 1 
ATOM   429  O OE2 . GLU A 1 59  ? -27.00536 23.61785 6.06585  1.000 38.93977 ? 54  GLU A OE2 1 
ATOM   430  N N   . PHE A 1 60  ? -24.73644 17.19273 5.88932  1.000 30.59929 ? 55  PHE A N   1 
ATOM   431  C CA  . PHE A 1 60  ? -24.67445 15.82734 5.37274  1.000 29.08151 ? 55  PHE A CA  1 
ATOM   432  C C   . PHE A 1 60  ? -24.87992 14.81016 6.49184  1.000 28.03132 ? 55  PHE A C   1 
ATOM   433  O O   . PHE A 1 60  ? -25.61519 13.83108 6.32741  1.000 26.91866 ? 55  PHE A O   1 
ATOM   434  C CB  . PHE A 1 60  ? -23.32986 15.58157 4.68142  1.000 23.18007 ? 55  PHE A CB  1 
ATOM   435  C CG  . PHE A 1 60  ? -23.16320 14.17035 4.15497  1.000 24.49578 ? 55  PHE A CG  1 
ATOM   436  C CD1 . PHE A 1 60  ? -22.62142 13.18314 4.94746  1.000 28.25658 ? 55  PHE A CD1 1 
ATOM   437  C CD2 . PHE A 1 60  ? -23.54425 13.84701 2.85433  1.000 31.64831 ? 55  PHE A CD2 1 
ATOM   438  C CE1 . PHE A 1 60  ? -22.47986 11.88283 4.48810  1.000 30.53224 ? 55  PHE A CE1 1 
ATOM   439  C CE2 . PHE A 1 60  ? -23.40255 12.54691 2.37068  1.000 29.97151 ? 55  PHE A CE2 1 
ATOM   440  C CZ  . PHE A 1 60  ? -22.86295 11.56115 3.18181  1.000 29.90049 ? 55  PHE A CZ  1 
ATOM   441  N N   . ASP A 1 61  ? -24.20600 15.01980 7.63105  1.000 27.03835 ? 56  ASP A N   1 
ATOM   442  C CA  . ASP A 1 61  ? -24.29382 14.08358 8.75377  1.000 25.75621 ? 56  ASP A CA  1 
ATOM   443  C C   . ASP A 1 61  ? -25.72763 13.94633 9.25932  1.000 25.42980 ? 56  ASP A C   1 
ATOM   444  O O   . ASP A 1 61  ? -26.17997 12.84277 9.59838  1.000 26.03782 ? 56  ASP A O   1 
ATOM   445  C CB  . ASP A 1 61  ? -23.36851 14.56539 9.88356  1.000 26.38375 ? 56  ASP A CB  1 
ATOM   446  C CG  . ASP A 1 61  ? -23.05626 13.46570 10.90796 1.000 36.73327 ? 56  ASP A CG  1 
ATOM   447  O OD1 . ASP A 1 61  ? -23.48199 12.30380 10.70132 1.000 32.55316 ? 56  ASP A OD1 1 
ATOM   448  O OD2 . ASP A 1 61  ? -22.37061 13.76620 11.92062 1.000 38.28265 ? 56  ASP A OD2 1 
ATOM   449  N N   . VAL A 1 62  ? -26.44753 15.06399 9.36391  1.000 23.21801 ? 57  VAL A N   1 
ATOM   450  C CA  . VAL A 1 62  ? -27.83212 14.99574 9.81984  1.000 23.65434 ? 57  VAL A CA  1 
ATOM   451  C C   . VAL A 1 62  ? -28.64997 14.15043 8.86627  1.000 27.91816 ? 57  VAL A C   1 
ATOM   452  O O   . VAL A 1 62  ? -29.34962 13.22045 9.27920  1.000 27.26541 ? 57  VAL A O   1 
ATOM   453  C CB  . VAL A 1 62  ? -28.43174 16.40498 9.96660  1.000 29.21982 ? 57  VAL A CB  1 
ATOM   454  C CG1 . VAL A 1 62  ? -29.94719 16.30241 10.10884 1.000 29.80992 ? 57  VAL A CG1 1 
ATOM   455  C CG2 . VAL A 1 62  ? -27.83778 17.09884 11.17843 1.000 32.83720 ? 57  VAL A CG2 1 
ATOM   456  N N   . LEU A 1 63  ? -28.55901 14.44891 7.56428  1.000 30.85973 ? 58  LEU A N   1 
ATOM   457  C CA  . LEU A 1 63  ? -29.33584 13.68595 6.59308  1.000 28.89539 ? 58  LEU A CA  1 
ATOM   458  C C   . LEU A 1 63  ? -28.91359 12.22281 6.58273  1.000 32.11110 ? 58  LEU A C   1 
ATOM   459  O O   . LEU A 1 63  ? -29.76126 11.31988 6.54036  1.000 28.66548 ? 58  LEU A O   1 
ATOM   460  C CB  . LEU A 1 63  ? -29.18737 14.29752 5.19765  1.000 26.97118 ? 58  LEU A CB  1 
ATOM   461  C CG  . LEU A 1 63  ? -29.57743 15.76597 4.95909  1.000 25.97116 ? 58  LEU A CG  1 
ATOM   462  C CD1 . LEU A 1 63  ? -29.54825 16.04880 3.42345  1.000 26.90494 ? 58  LEU A CD1 1 
ATOM   463  C CD2 . LEU A 1 63  ? -30.95316 16.07398 5.51494  1.000 26.49503 ? 58  LEU A CD2 1 
ATOM   464  N N   . ALA A 1 64  ? -27.60233 11.96521 6.62231  1.000 25.82466 ? 59  ALA A N   1 
ATOM   465  C CA  . ALA A 1 64  ? -27.12797 10.58425 6.63639  1.000 28.21876 ? 59  ALA A CA  1 
ATOM   466  C C   . ALA A 1 64  ? -27.59914 9.85182  7.88490  1.000 28.49172 ? 59  ALA A C   1 
ATOM   467  O O   . ALA A 1 64  ? -27.96006 8.67144  7.82781  1.000 34.26453 ? 59  ALA A O   1 
ATOM   468  C CB  . ALA A 1 64  ? -25.60349 10.55254 6.55476  1.000 29.88598 ? 59  ALA A CB  1 
ATOM   469  N N   . THR A 1 65  ? -27.60139 10.53286 9.02350  1.000 28.42415 ? 60  THR A N   1 
ATOM   470  C CA  . THR A 1 65  ? -28.04530 9.88335  10.25053 1.000 27.47246 ? 60  THR A CA  1 
ATOM   471  C C   . THR A 1 65  ? -29.52473 9.52340  10.17852 1.000 29.97247 ? 60  THR A C   1 
ATOM   472  O O   . THR A 1 65  ? -29.91636 8.41588  10.56021 1.000 30.07545 ? 60  THR A O   1 
ATOM   473  C CB  . THR A 1 65  ? -27.73989 10.78954 11.43081 1.000 26.36210 ? 60  THR A CB  1 
ATOM   474  O OG1 . THR A 1 65  ? -26.32560 11.02209 11.45082 1.000 31.53564 ? 60  THR A OG1 1 
ATOM   475  C CG2 . THR A 1 65  ? -28.18048 10.14678 12.76727 1.000 29.04226 ? 60  THR A CG2 1 
ATOM   476  N N   . LEU A 1 66  ? -30.35359 10.42505 9.64759  1.000 30.46394 ? 61  LEU A N   1 
ATOM   477  C CA  . LEU A 1 66  ? -31.77879 10.13211 9.51565  1.000 30.04077 ? 61  LEU A CA  1 
ATOM   478  C C   . LEU A 1 66  ? -32.00695 8.97925  8.55209  1.000 36.65173 ? 61  LEU A C   1 
ATOM   479  O O   . LEU A 1 66  ? -32.76445 8.04817  8.85348  1.000 33.30219 ? 61  LEU A O   1 
ATOM   480  C CB  . LEU A 1 66  ? -32.53682 11.38087 9.05663  1.000 25.96147 ? 61  LEU A CB  1 
ATOM   481  C CG  . LEU A 1 66  ? -32.51043 12.54093 10.06106 1.000 29.56360 ? 61  LEU A CG  1 
ATOM   482  C CD1 . LEU A 1 66  ? -32.92555 13.86067 9.43518  1.000 30.02270 ? 61  LEU A CD1 1 
ATOM   483  C CD2 . LEU A 1 66  ? -33.44324 12.21159 11.20758 1.000 31.10386 ? 61  LEU A CD2 1 
ATOM   484  N N   . ARG A 1 67  ? -31.34754 9.01838  7.38758  1.000 32.20949 ? 62  ARG A N   1 
ATOM   485  C CA  . ARG A 1 67  ? -31.52780 7.96199  6.39582  1.000 35.13267 ? 62  ARG A CA  1 
ATOM   486  C C   . ARG A 1 67  ? -31.14361 6.60429  6.96262  1.000 37.11622 ? 62  ARG A C   1 
ATOM   487  O O   . ARG A 1 67  ? -31.88029 5.62211  6.80646  1.000 37.47494 ? 62  ARG A O   1 
ATOM   488  C CB  . ARG A 1 67  ? -30.70049 8.25929  5.14494  1.000 27.85501 ? 62  ARG A CB  1 
ATOM   489  C CG  . ARG A 1 67  ? -30.69059 7.11396  4.13202  1.000 35.85320 ? 62  ARG A CG  1 
ATOM   490  C CD  . ARG A 1 67  ? -32.03885 6.99339  3.41157  1.000 37.93297 ? 62  ARG A CD  1 
ATOM   491  N NE  . ARG A 1 67  ? -32.09174 5.85290  2.48945  1.000 37.35240 ? 62  ARG A NE  1 
ATOM   492  C CZ  . ARG A 1 67  ? -32.24699 4.59704  2.89750  1.000 40.49086 ? 62  ARG A CZ  1 
ATOM   493  N NH1 . ARG A 1 67  ? -32.34334 4.32347  4.20594  1.000 35.15636 ? 62  ARG A NH1 1 
ATOM   494  N NH2 . ARG A 1 67  ? -32.29461 3.61460  2.01581  1.000 37.95698 ? 62  ARG A NH2 1 
ATOM   495  N N   . ARG A 1 68  ? -29.98096 6.51622  7.61325  1.000 32.48037 ? 63  ARG A N   1 
ATOM   496  C CA  . ARG A 1 68  ? -29.55977 5.18436  8.01552  1.000 37.05364 ? 63  ARG A CA  1 
ATOM   497  C C   . ARG A 1 68  ? -30.29271 4.70065  9.24939  1.000 34.71963 ? 63  ARG A C   1 
ATOM   498  O O   . ARG A 1 68  ? -30.16901 3.52367  9.59832  1.000 34.00288 ? 63  ARG A O   1 
ATOM   499  C CB  . ARG A 1 68  ? -28.04692 5.12232  8.23993  1.000 39.17637 ? 63  ARG A CB  1 
ATOM   500  C CG  . ARG A 1 68  ? -27.52810 5.91104  9.39451  1.000 42.32938 ? 63  ARG A CG  1 
ATOM   501  C CD  . ARG A 1 68  ? -26.03250 5.67052  9.54867  1.000 46.23490 ? 63  ARG A CD  1 
ATOM   502  N NE  . ARG A 1 68  ? -25.35956 6.88223  9.99090  1.000 45.21747 ? 63  ARG A NE  1 
ATOM   503  C CZ  . ARG A 1 68  ? -25.24336 7.24701  11.26698 1.000 38.39479 ? 63  ARG A CZ  1 
ATOM   504  N NH1 . ARG A 1 68  ? -25.73769 6.47886  12.23391 1.000 38.04924 ? 63  ARG A NH1 1 
ATOM   505  N NH2 . ARG A 1 68  ? -24.62820 8.38213  11.57001 1.000 36.49515 ? 63  ARG A NH2 1 
ATOM   506  N N   . SER A 1 69  ? -31.08201 5.55817  9.89516  1.000 31.57066 ? 64  SER A N   1 
ATOM   507  C CA  . SER A 1 69  ? -31.90013 5.05938  10.99066 1.000 40.86500 ? 64  SER A CA  1 
ATOM   508  C C   . SER A 1 69  ? -33.08453 4.24645  10.49262 1.000 45.25072 ? 64  SER A C   1 
ATOM   509  O O   . SER A 1 69  ? -33.82604 3.70721  11.31693 1.000 38.87427 ? 64  SER A O   1 
ATOM   510  C CB  . SER A 1 69  ? -32.38914 6.22101  11.86426 1.000 41.62215 ? 64  SER A CB  1 
ATOM   511  O OG  . SER A 1 69  ? -33.37481 6.97902  11.17356 1.000 45.53070 ? 64  SER A OG  1 
ATOM   512  N N   . GLY A 1 70  ? -33.28487 4.15394  9.17844  1.000 41.64294 ? 65  GLY A N   1 
ATOM   513  C CA  . GLY A 1 70  ? -34.36346 3.36720  8.61715  1.000 48.10035 ? 65  GLY A CA  1 
ATOM   514  C C   . GLY A 1 70  ? -35.68419 4.11822  8.57836  1.000 45.17988 ? 65  GLY A C   1 
ATOM   515  O O   . GLY A 1 70  ? -35.89712 5.11533  9.27025  1.000 38.90963 ? 65  GLY A O   1 
ATOM   516  N N   . ALA A 1 71  ? -36.59004 3.61453  7.74687  1.000 44.27024 ? 66  ALA A N   1 
ATOM   517  C CA  . ALA A 1 71  ? -37.87672 4.26759  7.57474  1.000 44.64282 ? 66  ALA A CA  1 
ATOM   518  C C   . ALA A 1 71  ? -38.61408 4.31891  8.91104  1.000 46.90579 ? 66  ALA A C   1 
ATOM   519  O O   . ALA A 1 71  ? -38.50577 3.38271  9.71427  1.000 53.79103 ? 66  ALA A O   1 
ATOM   520  C CB  . ALA A 1 71  ? -38.71739 3.53151  6.52750  1.000 48.70078 ? 66  ALA A CB  1 
ATOM   521  N N   . PRO A 1 72  ? -39.37021 5.39553  9.19397  1.000 47.31854 ? 67  PRO A N   1 
ATOM   522  C CA  . PRO A 1 72  ? -39.64415 6.57382  8.35816  1.000 50.60720 ? 67  PRO A CA  1 
ATOM   523  C C   . PRO A 1 72  ? -38.56594 7.65549  8.39929  1.000 51.92876 ? 67  PRO A C   1 
ATOM   524  O O   . PRO A 1 72  ? -38.87060 8.79845  8.05033  1.000 43.61548 ? 67  PRO A O   1 
ATOM   525  C CB  . PRO A 1 72  ? -40.93913 7.12011  8.96037  1.000 46.25775 ? 67  PRO A CB  1 
ATOM   526  C CG  . PRO A 1 72  ? -40.80057 6.80318  10.41071 1.000 46.63337 ? 67  PRO A CG  1 
ATOM   527  C CD  . PRO A 1 72  ? -40.09361 5.46612  10.47857 1.000 47.08997 ? 67  PRO A CD  1 
ATOM   528  N N   . TYR A 1 73  ? -37.35057 7.31072  8.83851  1.000 46.71798 ? 68  TYR A N   1 
ATOM   529  C CA  . TYR A 1 73  ? -36.21702 8.23798  8.81727  1.000 41.61441 ? 68  TYR A CA  1 
ATOM   530  C C   . TYR A 1 73  ? -36.49950 9.44405  9.70148  1.000 39.49318 ? 68  TYR A C   1 
ATOM   531  O O   . TYR A 1 73  ? -36.30955 10.59394 9.29900  1.000 39.86574 ? 68  TYR A O   1 
ATOM   532  C CB  . TYR A 1 73  ? -35.88522 8.69038  7.38668  1.000 35.90928 ? 68  TYR A CB  1 
ATOM   533  C CG  . TYR A 1 73  ? -36.01528 7.60499  6.34673  1.000 41.40166 ? 68  TYR A CG  1 
ATOM   534  C CD1 . TYR A 1 73  ? -35.10780 6.55507  6.28816  1.000 41.08518 ? 68  TYR A CD1 1 
ATOM   535  C CD2 . TYR A 1 73  ? -37.04487 7.63749  5.41087  1.000 44.13620 ? 68  TYR A CD2 1 
ATOM   536  C CE1 . TYR A 1 73  ? -35.23289 5.54675  5.32442  1.000 44.82108 ? 68  TYR A CE1 1 
ATOM   537  C CE2 . TYR A 1 73  ? -37.17623 6.64671  4.45159  1.000 47.58223 ? 68  TYR A CE2 1 
ATOM   538  C CZ  . TYR A 1 73  ? -36.26946 5.60372  4.41050  1.000 47.41055 ? 68  TYR A CZ  1 
ATOM   539  O OH  . TYR A 1 73  ? -36.40925 4.61671  3.45620  1.000 50.04194 ? 68  TYR A OH  1 
ATOM   540  N N   . ALA A 1 74  ? -36.96223 9.16969  10.92064 1.000 38.35706 ? 69  ALA A N   1 
ATOM   541  C CA  . ALA A 1 74  ? -37.38616 10.19873 11.85387 1.000 40.37177 ? 69  ALA A CA  1 
ATOM   542  C C   . ALA A 1 74  ? -36.77443 9.92226  13.22200 1.000 39.67890 ? 69  ALA A C   1 
ATOM   543  O O   . ALA A 1 74  ? -36.90791 8.81509  13.75542 1.000 39.94127 ? 69  ALA A O   1 
ATOM   544  C CB  . ALA A 1 74  ? -38.91793 10.24404 11.95377 1.000 44.14668 ? 69  ALA A CB  1 
ATOM   545  N N   . LEU A 1 75  ? -36.09301 10.91853 13.78011 1.000 37.93267 ? 70  LEU A N   1 
ATOM   546  C CA  . LEU A 1 75  ? -35.47372 10.78145 15.09234 1.000 36.24491 ? 70  LEU A CA  1 
ATOM   547  C C   . LEU A 1 75  ? -35.70212 12.04635 15.89670 1.000 41.79111 ? 70  LEU A C   1 
ATOM   548  O O   . LEU A 1 75  ? -35.77413 13.14436 15.33879 1.000 39.49445 ? 70  LEU A O   1 
ATOM   549  C CB  . LEU A 1 75  ? -33.96082 10.55066 14.99119 1.000 34.99378 ? 70  LEU A CB  1 
ATOM   550  C CG  . LEU A 1 75  ? -33.42211 9.39384  14.15948 1.000 37.04918 ? 70  LEU A CG  1 
ATOM   551  C CD1 . LEU A 1 75  ? -31.93025 9.58136  13.95272 1.000 33.74714 ? 70  LEU A CD1 1 
ATOM   552  C CD2 . LEU A 1 75  ? -33.71127 8.08717  14.91546 1.000 47.43697 ? 70  LEU A CD2 1 
ATOM   553  N N   . THR A 1 76  ? -35.75197 11.88819 17.22387 1.000 48.72793 ? 71  THR A N   1 
ATOM   554  C CA  . THR A 1 76  ? -35.70649 13.03982 18.10619 1.000 47.66383 ? 71  THR A CA  1 
ATOM   555  C C   . THR A 1 76  ? -34.36548 13.74905 17.92475 1.000 48.21755 ? 71  THR A C   1 
ATOM   556  O O   . THR A 1 76  ? -33.36980 13.11349 17.56102 1.000 41.59260 ? 71  THR A O   1 
ATOM   557  C CB  . THR A 1 76  ? -35.86776 12.60737 19.56735 1.000 49.92365 ? 71  THR A CB  1 
ATOM   558  O OG1 . THR A 1 76  ? -34.80118 11.71026 19.90583 1.000 45.69415 ? 71  THR A OG1 1 
ATOM   559  C CG2 . THR A 1 76  ? -37.18927 11.89747 19.78057 1.000 50.33446 ? 71  THR A CG2 1 
ATOM   560  N N   . PRO A 1 77  ? -34.29680 15.06122 18.18171 1.000 55.88820 ? 72  PRO A N   1 
ATOM   561  C CA  . PRO A 1 77  ? -32.99709 15.74424 18.04895 1.000 52.67494 ? 72  PRO A CA  1 
ATOM   562  C C   . PRO A 1 77  ? -31.92987 15.12331 18.93267 1.000 48.38451 ? 72  PRO A C   1 
ATOM   563  O O   . PRO A 1 77  ? -30.75205 15.09327 18.55536 1.000 50.92223 ? 72  PRO A O   1 
ATOM   564  C CB  . PRO A 1 77  ? -33.30469 17.19503 18.45968 1.000 60.67710 ? 72  PRO A CB  1 
ATOM   565  C CG  . PRO A 1 77  ? -34.80385 17.31515 18.43893 1.000 63.58940 ? 72  PRO A CG  1 
ATOM   566  C CD  . PRO A 1 77  ? -35.33380 15.94517 18.74215 1.000 62.87012 ? 72  PRO A CD  1 
ATOM   567  N N   . THR A 1 78  ? -32.31770 14.58742 20.08925 1.000 37.12728 ? 73  THR A N   1 
ATOM   568  C CA  . THR A 1 78  ? -31.33644 13.93759 20.95443 1.000 49.63838 ? 73  THR A CA  1 
ATOM   569  C C   . THR A 1 78  ? -30.86376 12.60968 20.36716 1.000 44.79891 ? 73  THR A C   1 
ATOM   570  O O   . THR A 1 78  ? -29.66790 12.31094 20.39497 1.000 42.86068 ? 73  THR A O   1 
ATOM   571  C CB  . THR A 1 78  ? -31.91948 13.72993 22.34694 1.000 51.27428 ? 73  THR A CB  1 
ATOM   572  O OG1 . THR A 1 78  ? -32.27472 15.00219 22.90609 1.000 53.67897 ? 73  THR A OG1 1 
ATOM   573  C CG2 . THR A 1 78  ? -30.89260 13.05847 23.25974 1.000 50.20726 ? 73  THR A CG2 1 
ATOM   574  N N   . ALA A 1 79  ? -31.78566 11.78279 19.86533 1.000 45.41773 ? 74  ALA A N   1 
ATOM   575  C CA  . ALA A 1 79  ? -31.36185 10.56335 19.18635 1.000 41.04126 ? 74  ALA A CA  1 
ATOM   576  C C   . ALA A 1 79  ? -30.49639 10.89869 17.98736 1.000 43.03023 ? 74  ALA A C   1 
ATOM   577  O O   . ALA A 1 79  ? -29.54359 10.17529 17.67948 1.000 45.13180 ? 74  ALA A O   1 
ATOM   578  C CB  . ALA A 1 79  ? -32.56933 9.72973  18.74670 1.000 39.28351 ? 74  ALA A CB  1 
ATOM   579  N N   . LEU A 1 80  ? -30.79814 12.01597 17.32115 1.000 36.59238 ? 75  LEU A N   1 
ATOM   580  C CA  . LEU A 1 80  ? -30.02480 12.44015 16.15720 1.000 40.98498 ? 75  LEU A CA  1 
ATOM   581  C C   . LEU A 1 80  ? -28.57128 12.71532 16.53483 1.000 40.81820 ? 75  LEU A C   1 
ATOM   582  O O   . LEU A 1 80  ? -27.64157 12.22974 15.87549 1.000 36.08423 ? 75  LEU A O   1 
ATOM   583  C CB  . LEU A 1 80  ? -30.68930 13.67696 15.54422 1.000 44.20322 ? 75  LEU A CB  1 
ATOM   584  C CG  . LEU A 1 80  ? -30.19670 14.25856 14.21974 1.000 42.72377 ? 75  LEU A CG  1 
ATOM   585  C CD1 . LEU A 1 80  ? -30.00815 13.17647 13.20273 1.000 27.06839 ? 75  LEU A CD1 1 
ATOM   586  C CD2 . LEU A 1 80  ? -31.20604 15.28232 13.72467 1.000 42.31722 ? 75  LEU A CD2 1 
ATOM   587  N N   . TYR A 1 81  ? -28.35769 13.46868 17.61667 1.000 40.75451 ? 76  TYR A N   1 
ATOM   588  C CA  . TYR A 1 81  ? -26.99856 13.75038 18.07735 1.000 45.91384 ? 76  TYR A CA  1 
ATOM   589  C C   . TYR A 1 81  ? -26.24233 12.47176 18.43469 1.000 43.89321 ? 76  TYR A C   1 
ATOM   590  O O   . TYR A 1 81  ? -25.07454 12.30578 18.06500 1.000 42.19282 ? 76  TYR A O   1 
ATOM   591  C CB  . TYR A 1 81  ? -27.01967 14.68477 19.29142 1.000 35.74215 ? 76  TYR A CB  1 
ATOM   592  C CG  . TYR A 1 81  ? -25.63060 14.88905 19.86157 1.000 38.06195 ? 76  TYR A CG  1 
ATOM   593  C CD1 . TYR A 1 81  ? -24.75311 15.81174 19.30121 1.000 42.76262 ? 76  TYR A CD1 1 
ATOM   594  C CD2 . TYR A 1 81  ? -25.18637 14.14905 20.95291 1.000 50.02326 ? 76  TYR A CD2 1 
ATOM   595  C CE1 . TYR A 1 81  ? -23.47314 15.99727 19.81833 1.000 45.07638 ? 76  TYR A CE1 1 
ATOM   596  C CE2 . TYR A 1 81  ? -23.91220 14.32763 21.47396 1.000 50.54066 ? 76  TYR A CE2 1 
ATOM   597  C CZ  . TYR A 1 81  ? -23.06491 15.25315 20.90460 1.000 51.83638 ? 76  TYR A CZ  1 
ATOM   598  O OH  . TYR A 1 81  ? -21.80278 15.42415 21.42265 1.000 58.16152 ? 76  TYR A OH  1 
ATOM   599  N N   . ASP A 1 82  ? -26.87280 11.57597 19.20105 1.000 43.38596 ? 77  ASP A N   1 
ATOM   600  C CA  . ASP A 1 82  ? -26.16944 10.36555 19.62270 1.000 42.98420 ? 77  ASP A CA  1 
ATOM   601  C C   . ASP A 1 82  ? -25.81820 9.45732  18.44104 1.000 44.13123 ? 77  ASP A C   1 
ATOM   602  O O   . ASP A 1 82  ? -24.81323 8.74380  18.49783 1.000 43.52385 ? 77  ASP A O   1 
ATOM   603  C CB  . ASP A 1 82  ? -27.00200 9.59930  20.64943 1.000 40.28314 ? 77  ASP A CB  1 
ATOM   604  C CG  . ASP A 1 82  ? -26.92204 10.21568 22.03077 1.000 44.86383 ? 77  ASP A CG  1 
ATOM   605  O OD1 . ASP A 1 82  ? -25.81762 10.62958 22.43466 1.000 48.80404 ? 77  ASP A OD1 1 
ATOM   606  O OD2 . ASP A 1 82  ? -27.96672 10.29811 22.70039 1.000 51.98884 ? 77  ASP A OD2 1 
ATOM   607  N N   . ALA A 1 83  ? -26.61100 9.47214  17.36833 1.000 40.69188 ? 78  ALA A N   1 
ATOM   608  C CA  . ALA A 1 83  ? -26.37293 8.57659  16.23640 1.000 39.08109 ? 78  ALA A CA  1 
ATOM   609  C C   . ALA A 1 83  ? -25.50194 9.19668  15.15938 1.000 43.87500 ? 78  ALA A C   1 
ATOM   610  O O   . ALA A 1 83  ? -25.17397 8.50908  14.17507 1.000 41.58812 ? 78  ALA A O   1 
ATOM   611  C CB  . ALA A 1 83  ? -27.70114 8.12625  15.62437 1.000 40.05812 ? 78  ALA A CB  1 
ATOM   612  N N   . ALA A 1 84  ? -25.12893 10.46795 15.31450 1.000 36.09989 ? 79  ALA A N   1 
ATOM   613  C CA  . ALA A 1 84  ? -24.36320 11.14792 14.28294 1.000 41.17107 ? 79  ALA A CA  1 
ATOM   614  C C   . ALA A 1 84  ? -22.98884 10.50746 14.14290 1.000 42.66576 ? 79  ALA A C   1 
ATOM   615  O O   . ALA A 1 84  ? -22.46597 9.89214  15.07781 1.000 36.19032 ? 79  ALA A O   1 
ATOM   616  C CB  . ALA A 1 84  ? -24.22591 12.63697 14.60467 1.000 43.25455 ? 79  ALA A CB  1 
ATOM   617  N N   . MET A 1 85  ? -22.41987 10.62121 12.94270 1.000 34.15538 ? 80  MET A N   1 
ATOM   618  C CA  . MET A 1 85  ? -21.04336 10.17762 12.75179 1.000 38.91075 ? 80  MET A CA  1 
ATOM   619  C C   . MET A 1 85  ? -20.07766 11.01725 13.58113 1.000 39.17997 ? 80  MET A C   1 
ATOM   620  O O   . MET A 1 85  ? -19.12140 10.48454 14.15834 1.000 34.69423 ? 80  MET A O   1 
ATOM   621  C CB  . MET A 1 85  ? -20.66713 10.24465 11.27355 1.000 40.30162 ? 80  MET A CB  1 
ATOM   622  C CG  . MET A 1 85  ? -19.23308 9.82103  10.99442 1.000 45.76197 ? 80  MET A CG  1 
ATOM   623  S SD  . MET A 1 85  ? -18.93754 8.07044  11.36757 1.000 45.90387 ? 80  MET A SD  1 
ATOM   624  C CE  . MET A 1 85  ? -19.88635 7.30567  10.04331 1.000 42.83966 ? 80  MET A CE  1 
ATOM   625  N N   . ILE A 1 86  ? -20.32064 12.33003 13.65936 1.000 38.57662 ? 81  ILE A N   1 
ATOM   626  C CA  . ILE A 1 86  ? -19.43343 13.28835 14.31239 1.000 38.09661 ? 81  ILE A CA  1 
ATOM   627  C C   . ILE A 1 86  ? -20.20725 14.04789 15.38665 1.000 37.90033 ? 81  ILE A C   1 
ATOM   628  O O   . ILE A 1 86  ? -21.34966 14.46154 15.16756 1.000 37.08755 ? 81  ILE A O   1 
ATOM   629  C CB  . ILE A 1 86  ? -18.83164 14.28383 13.30005 1.000 39.54968 ? 81  ILE A CB  1 
ATOM   630  C CG1 . ILE A 1 86  ? -18.25093 13.54981 12.07953 1.000 42.00958 ? 81  ILE A CG1 1 
ATOM   631  C CG2 . ILE A 1 86  ? -17.76132 15.13916 13.98341 1.000 43.98515 ? 81  ILE A CG2 1 
ATOM   632  C CD1 . ILE A 1 86  ? -17.00346 12.76635 12.39388 1.000 39.69277 ? 81  ILE A CD1 1 
ATOM   633  N N   . SER A 1 87  ? -19.56727 14.27840 16.52540 1.000 39.56075 ? 82  SER A N   1 
ATOM   634  C CA  . SER A 1 87  ? -20.24361 14.92937 17.64976 1.000 39.07379 ? 82  SER A CA  1 
ATOM   635  C C   . SER A 1 87  ? -20.05577 16.45123 17.63765 1.000 40.70435 ? 82  SER A C   1 
ATOM   636  O O   . SER A 1 87  ? -19.68142 17.06143 18.64241 1.000 49.92984 ? 82  SER A O   1 
ATOM   637  C CB  . SER A 1 87  ? -19.75990 14.31627 18.95805 1.000 43.76497 ? 82  SER A CB  1 
ATOM   638  O OG  . SER A 1 87  ? -18.40886 14.64802 19.21798 1.000 40.69514 ? 82  SER A OG  1 
ATOM   639  N N   . SER A 1 88  ? -20.33554 17.08449 16.49777 1.000 41.71245 ? 83  SER A N   1 
ATOM   640  C CA  . SER A 1 88  ? -20.22942 18.53540 16.39415 1.000 50.71939 ? 83  SER A CA  1 
ATOM   641  C C   . SER A 1 88  ? -21.47178 19.22457 16.97424 1.000 55.97140 ? 83  SER A C   1 
ATOM   642  O O   . SER A 1 88  ? -22.54492 18.62852 17.11526 1.000 46.96455 ? 83  SER A O   1 
ATOM   643  C CB  . SER A 1 88  ? -20.01292 18.96446 14.93826 1.000 55.23283 ? 83  SER A CB  1 
ATOM   644  O OG  . SER A 1 88  ? -20.79859 18.20477 14.02748 1.000 54.13310 ? 83  SER A OG  1 
ATOM   645  N N   . GLY A 1 89  ? -21.30850 20.50069 17.31953 1.000 61.28057 ? 84  GLY A N   1 
ATOM   646  C CA  . GLY A 1 89  ? -22.37788 21.29972 17.88820 1.000 61.88831 ? 84  GLY A CA  1 
ATOM   647  C C   . GLY A 1 89  ? -23.16385 22.07453 16.84533 1.000 66.40753 ? 84  GLY A C   1 
ATOM   648  O O   . GLY A 1 89  ? -23.18265 21.73576 15.65857 1.000 64.38496 ? 84  GLY A O   1 
ATOM   649  N N   . SER A 1 90  ? -23.83285 23.13629 17.31478 1.000 64.92721 ? 85  SER A N   1 
ATOM   650  C CA  . SER A 1 90  ? -24.62977 24.02996 16.46125 1.000 62.22698 ? 85  SER A CA  1 
ATOM   651  C C   . SER A 1 90  ? -25.65717 23.26074 15.63113 1.000 64.18109 ? 85  SER A C   1 
ATOM   652  O O   . SER A 1 90  ? -25.90681 23.58597 14.46665 1.000 60.32444 ? 85  SER A O   1 
ATOM   653  C CB  . SER A 1 90  ? -23.73267 24.87559 15.55357 1.000 60.18909 ? 85  SER A CB  1 
ATOM   654  O OG  . SER A 1 90  ? -23.01900 25.84559 16.30235 1.000 69.57427 ? 85  SER A OG  1 
ATOM   655  N N   . MET A 1 91  ? -26.26746 22.23649 16.23449 1.000 65.51399 ? 86  MET A N   1 
ATOM   656  C CA  . MET A 1 91  ? -27.16987 21.37740 15.47523 1.000 65.50387 ? 86  MET A CA  1 
ATOM   657  C C   . MET A 1 91  ? -28.53892 22.01089 15.27453 1.000 57.45975 ? 86  MET A C   1 
ATOM   658  O O   . MET A 1 91  ? -29.16301 21.80610 14.22646 1.000 54.37363 ? 86  MET A O   1 
ATOM   659  C CB  . MET A 1 91  ? -27.32721 20.01600 16.15086 1.000 66.77891 ? 86  MET A CB  1 
ATOM   660  C CG  . MET A 1 91  ? -28.39507 19.15507 15.47986 1.000 63.43436 ? 86  MET A CG  1 
ATOM   661  S SD  . MET A 1 91  ? -28.14001 17.39466 15.69995 1.000 63.15561 ? 86  MET A SD  1 
ATOM   662  C CE  . MET A 1 91  ? -26.78037 17.11516 14.57301 1.000 57.74512 ? 86  MET A CE  1 
ATOM   663  N N   . THR A 1 92  ? -29.03100 22.76829 16.25822 1.000 48.53656 ? 87  THR A N   1 
ATOM   664  C CA  . THR A 1 92  ? -30.37952 23.31678 16.14026 1.000 59.11046 ? 87  THR A CA  1 
ATOM   665  C C   . THR A 1 92  ? -30.48696 24.23615 14.92901 1.000 65.73584 ? 87  THR A C   1 
ATOM   666  O O   . THR A 1 92  ? -31.44926 24.15617 14.15499 1.000 59.63558 ? 87  THR A O   1 
ATOM   667  C CB  . THR A 1 92  ? -30.77684 24.05016 17.42394 1.000 63.16282 ? 87  THR A CB  1 
ATOM   668  O OG1 . THR A 1 92  ? -30.96281 23.09601 18.47759 1.000 59.11995 ? 87  THR A OG1 1 
ATOM   669  C CG2 . THR A 1 92  ? -32.08971 24.82970 17.21984 1.000 69.38224 ? 87  THR A CG2 1 
ATOM   670  N N   . ASN A 1 93  ? -29.49143 25.10506 14.73454 1.000 65.15923 ? 88  ASN A N   1 
ATOM   671  C CA  . ASN A 1 93  ? -29.50857 25.96807 13.56149 1.000 64.97348 ? 88  ASN A CA  1 
ATOM   672  C C   . ASN A 1 93  ? -29.25407 25.16773 12.29319 1.000 61.10587 ? 88  ASN A C   1 
ATOM   673  O O   . ASN A 1 93  ? -29.72633 25.54361 11.21576 1.000 66.44181 ? 88  ASN A O   1 
ATOM   674  C CB  . ASN A 1 93  ? -28.47900 27.08983 13.70957 1.000 69.22130 ? 88  ASN A CB  1 
ATOM   675  C CG  . ASN A 1 93  ? -28.78103 28.02679 14.88765 1.000 73.62034 ? 88  ASN A CG  1 
ATOM   676  O OD1 . ASN A 1 93  ? -27.90735 28.77182 15.33415 1.000 78.56333 ? 88  ASN A OD1 1 
ATOM   677  N ND2 . ASN A 1 93  ? -30.01449 27.98665 15.39202 1.000 68.39293 ? 88  ASN A ND2 1 
ATOM   678  N N   . ARG A 1 94  ? -28.51762 24.06185 12.40524 1.000 56.71869 ? 89  ARG A N   1 
ATOM   679  C CA  . ARG A 1 94  ? -28.31719 23.17597 11.26535 1.000 52.46356 ? 89  ARG A CA  1 
ATOM   680  C C   . ARG A 1 94  ? -29.62823 22.52935 10.84021 1.000 48.37495 ? 89  ARG A C   1 
ATOM   681  O O   . ARG A 1 94  ? -29.91971 22.42935 9.64027  1.000 59.39243 ? 89  ARG A O   1 
ATOM   682  C CB  . ARG A 1 94  ? -27.26962 22.13374 11.63283 1.000 51.66741 ? 89  ARG A CB  1 
ATOM   683  C CG  . ARG A 1 94  ? -26.92912 21.15708 10.58455 1.000 51.17066 ? 89  ARG A CG  1 
ATOM   684  C CD  . ARG A 1 94  ? -25.80817 20.24884 11.06641 1.000 50.72591 ? 89  ARG A CD  1 
ATOM   685  N NE  . ARG A 1 94  ? -24.66198 20.99848 11.56761 1.000 52.20333 ? 89  ARG A NE  1 
ATOM   686  C CZ  . ARG A 1 94  ? -24.20344 20.90596 12.81351 1.000 59.80448 ? 89  ARG A CZ  1 
ATOM   687  N NH1 . ARG A 1 94  ? -24.79015 20.08102 13.67226 1.000 54.53287 ? 89  ARG A NH1 1 
ATOM   688  N NH2 . ARG A 1 94  ? -23.15568 21.62975 13.19923 1.000 64.08926 ? 89  ARG A NH2 1 
ATOM   689  N N   . ILE A 1 95  ? -30.44667 22.10811 11.80713 1.000 44.74473 ? 90  ILE A N   1 
ATOM   690  C CA  . ILE A 1 95  ? -31.77973 21.60604 11.48051 1.000 47.32817 ? 90  ILE A CA  1 
ATOM   691  C C   . ILE A 1 95  ? -32.63400 22.71692 10.88125 1.000 51.62377 ? 90  ILE A C   1 
ATOM   692  O O   . ILE A 1 95  ? -33.35144 22.50592 9.89125  1.000 47.94269 ? 90  ILE A O   1 
ATOM   693  C CB  . ILE A 1 95  ? -32.43024 20.97830 12.72769 1.000 45.27128 ? 90  ILE A CB  1 
ATOM   694  C CG1 . ILE A 1 95  ? -31.75349 19.64358 13.05332 1.000 43.87567 ? 90  ILE A CG1 1 
ATOM   695  C CG2 . ILE A 1 95  ? -33.90993 20.76908 12.52462 1.000 47.30008 ? 90  ILE A CG2 1 
ATOM   696  C CD1 . ILE A 1 95  ? -31.92559 19.20871 14.49936 1.000 43.60967 ? 90  ILE A CD1 1 
ATOM   697  N N   . ASP A 1 96  ? -32.55511 23.92207 11.45288 1.000 49.61108 ? 91  ASP A N   1 
ATOM   698  C CA  . ASP A 1 96  ? -33.30395 25.05150 10.90684 1.000 56.98786 ? 91  ASP A CA  1 
ATOM   699  C C   . ASP A 1 96  ? -33.00933 25.23396 9.42282  1.000 53.47442 ? 91  ASP A C   1 
ATOM   700  O O   . ASP A 1 96  ? -33.92672 25.35112 8.60230  1.000 57.26303 ? 91  ASP A O   1 
ATOM   701  C CB  . ASP A 1 96  ? -32.96930 26.33312 11.67725 1.000 61.48812 ? 91  ASP A CB  1 
ATOM   702  C CG  . ASP A 1 96  ? -33.56387 26.35529 13.07546 1.000 72.22644 ? 91  ASP A CG  1 
ATOM   703  O OD1 . ASP A 1 96  ? -34.51488 25.59063 13.33771 1.000 74.32160 ? 91  ASP A OD1 1 
ATOM   704  O OD2 . ASP A 1 96  ? -33.08367 27.15200 13.91123 1.000 76.75127 ? 91  ASP A OD2 1 
ATOM   705  N N   . ARG A 1 97  ? -31.72262 25.24000 9.06561  1.000 53.53467 ? 92  ARG A N   1 
ATOM   706  C CA  . ARG A 1 97  ? -31.32363 25.39663 7.66904  1.000 56.54678 ? 92  ARG A CA  1 
ATOM   707  C C   . ARG A 1 97  ? -31.87827 24.27753 6.79971  1.000 55.95170 ? 92  ARG A C   1 
ATOM   708  O O   . ARG A 1 97  ? -32.34944 24.52537 5.68137  1.000 53.96560 ? 92  ARG A O   1 
ATOM   709  C CB  . ARG A 1 97  ? -29.79727 25.44207 7.56776  1.000 55.46304 ? 92  ARG A CB  1 
ATOM   710  C CG  . ARG A 1 97  ? -29.21697 26.84436 7.67712  1.000 65.24174 ? 92  ARG A CG  1 
ATOM   711  C CD  . ARG A 1 97  ? -27.69804 26.85307 7.60269  1.000 71.57310 ? 92  ARG A CD  1 
ATOM   712  N NE  . ARG A 1 97  ? -27.07145 26.53183 8.88689  1.000 80.59626 ? 92  ARG A NE  1 
ATOM   713  C CZ  . ARG A 1 97  ? -26.35709 25.43414 9.12795  1.000 81.84677 ? 92  ARG A CZ  1 
ATOM   714  N NH1 . ARG A 1 97  ? -26.16330 24.53659 8.17007  1.000 78.80210 ? 92  ARG A NH1 1 
ATOM   715  N NH2 . ARG A 1 97  ? -25.82504 25.23822 10.32728 1.000 82.66207 ? 92  ARG A NH2 1 
ATOM   716  N N   . LEU A 1 98  ? -31.82135 23.03725 7.29506  1.000 53.15019 ? 93  LEU A N   1 
ATOM   717  C CA  . LEU A 1 98  ? -32.26705 21.89565 6.50486  1.000 47.65468 ? 93  LEU A CA  1 
ATOM   718  C C   . LEU A 1 98  ? -33.77408 21.93544 6.27887  1.000 45.14993 ? 93  LEU A C   1 
ATOM   719  O O   . LEU A 1 98  ? -34.25695 21.57117 5.19997  1.000 41.59827 ? 93  LEU A O   1 
ATOM   720  C CB  . LEU A 1 98  ? -31.84411 20.59463 7.19204  1.000 39.13664 ? 93  LEU A CB  1 
ATOM   721  C CG  . LEU A 1 98  ? -30.33338 20.35902 7.20566  1.000 42.00197 ? 93  LEU A CG  1 
ATOM   722  C CD1 . LEU A 1 98  ? -29.96388 19.10554 7.98719  1.000 42.10441 ? 93  LEU A CD1 1 
ATOM   723  C CD2 . LEU A 1 98  ? -29.78616 20.28486 5.80501  1.000 44.78427 ? 93  LEU A CD2 1 
ATOM   724  N N   . GLU A 1 99  ? -34.53542 22.38181 7.27789  1.000 46.82318 ? 94  GLU A N   1 
ATOM   725  C CA  . GLU A 1 99  ? -35.97145 22.55412 7.07405  1.000 49.25970 ? 94  GLU A CA  1 
ATOM   726  C C   . GLU A 1 99  ? -36.25064 23.63170 6.03202  1.000 49.99880 ? 94  GLU A C   1 
ATOM   727  O O   . GLU A 1 99  ? -37.10336 23.45331 5.15434  1.000 49.46965 ? 94  GLU A O   1 
ATOM   728  C CB  . GLU A 1 99  ? -36.65395 22.89635 8.40010  1.000 53.97649 ? 94  GLU A CB  1 
ATOM   729  C CG  . GLU A 1 99  ? -38.14808 23.11287 8.25436  1.000 59.49797 ? 94  GLU A CG  1 
ATOM   730  C CD  . GLU A 1 99  ? -38.88133 23.10555 9.58228  1.000 67.82124 ? 94  GLU A CD  1 
ATOM   731  O OE1 . GLU A 1 99  ? -38.28159 23.51831 10.60511 1.000 63.75411 ? 94  GLU A OE1 1 
ATOM   732  O OE2 . GLU A 1 99  ? -40.06180 22.68143 9.59343  1.000 71.19358 ? 94  GLU A OE2 1 
ATOM   733  N N   . LYS A 1 100 ? -35.52614 24.75405 6.10304  1.000 50.87695 ? 95  LYS A N   1 
ATOM   734  C CA  . LYS A 1 100 ? -35.72623 25.83236 5.13750  1.000 54.58104 ? 95  LYS A CA  1 
ATOM   735  C C   . LYS A 1 100 ? -35.37764 25.39426 3.71912  1.000 53.91157 ? 95  LYS A C   1 
ATOM   736  O O   . LYS A 1 100 ? -35.95583 25.90021 2.75215  1.000 52.35882 ? 95  LYS A O   1 
ATOM   737  C CB  . LYS A 1 100 ? -34.88905 27.04674 5.53810  1.000 52.07930 ? 95  LYS A CB  1 
ATOM   738  C CG  . LYS A 1 100 ? -35.12202 28.28535 4.69377  1.000 53.81617 ? 95  LYS A CG  1 
ATOM   739  N N   . ALA A 1 101 ? -34.43341 24.46780 3.57339  1.000 55.90655 ? 96  ALA A N   1 
ATOM   740  C CA  . ALA A 1 101 ? -34.02878 23.97901 2.26140  1.000 54.98445 ? 96  ALA A CA  1 
ATOM   741  C C   . ALA A 1 101 ? -34.97844 22.93086 1.69877  1.000 52.95372 ? 96  ALA A C   1 
ATOM   742  O O   . ALA A 1 101 ? -34.84494 22.56471 0.52401  1.000 46.26170 ? 96  ALA A O   1 
ATOM   743  C CB  . ALA A 1 101 ? -32.61412 23.39686 2.33289  1.000 51.98832 ? 96  ALA A CB  1 
ATOM   744  N N   . GLY A 1 102 ? -35.92298 22.44317 2.50167  1.000 50.30819 ? 97  GLY A N   1 
ATOM   745  C CA  . GLY A 1 102 ? -36.86344 21.42911 2.06264  1.000 44.95520 ? 97  GLY A CA  1 
ATOM   746  C C   . GLY A 1 102 ? -36.42806 19.99766 2.28241  1.000 40.99905 ? 97  GLY A C   1 
ATOM   747  O O   . GLY A 1 102 ? -37.06780 19.08748 1.74272  1.000 43.99480 ? 97  GLY A O   1 
ATOM   748  N N   . TRP A 1 103 ? -35.36726 19.76281 3.06335  1.000 34.99222 ? 98  TRP A N   1 
ATOM   749  C CA  . TRP A 1 103 ? -34.79159 18.42753 3.19803  1.000 31.85636 ? 98  TRP A CA  1 
ATOM   750  C C   . TRP A 1 103 ? -35.17453 17.69916 4.47046  1.000 41.54918 ? 98  TRP A C   1 
ATOM   751  O O   . TRP A 1 103 ? -35.10745 16.46704 4.49655  1.000 34.41944 ? 98  TRP A O   1 
ATOM   752  C CB  . TRP A 1 103 ? -33.27007 18.50169 3.11200  1.000 35.44151 ? 98  TRP A CB  1 
ATOM   753  C CG  . TRP A 1 103 ? -32.85011 19.01275 1.76632  1.000 43.04491 ? 98  TRP A CG  1 
ATOM   754  C CD1 . TRP A 1 103 ? -33.49636 18.81151 0.56879  1.000 46.31129 ? 98  TRP A CD1 1 
ATOM   755  C CD2 . TRP A 1 103 ? -31.72572 19.83773 1.47939  1.000 46.68839 ? 98  TRP A CD2 1 
ATOM   756  N NE1 . TRP A 1 103 ? -32.82485 19.45286 -0.44226 1.000 41.29997 ? 98  TRP A NE1 1 
ATOM   757  C CE2 . TRP A 1 103 ? -31.73421 20.09058 0.09048  1.000 41.79311 ? 98  TRP A CE2 1 
ATOM   758  C CE3 . TRP A 1 103 ? -30.70595 20.38893 2.26142  1.000 46.18421 ? 98  TRP A CE3 1 
ATOM   759  C CZ2 . TRP A 1 103 ? -30.76298 20.86603 -0.52610 1.000 47.64675 ? 98  TRP A CZ2 1 
ATOM   760  C CZ3 . TRP A 1 103 ? -29.74245 21.15778 1.64720  1.000 45.38140 ? 98  TRP A CZ3 1 
ATOM   761  C CH2 . TRP A 1 103 ? -29.77359 21.38545 0.26726  1.000 44.65681 ? 98  TRP A CH2 1 
ATOM   762  N N   . VAL A 1 104 ? -35.53513 18.41142 5.53357  1.000 42.95287 ? 99  VAL A N   1 
ATOM   763  C CA  . VAL A 1 104 ? -36.05508 17.78025 6.73423  1.000 40.25174 ? 99  VAL A CA  1 
ATOM   764  C C   . VAL A 1 104 ? -37.36771 18.45964 7.08146  1.000 43.40194 ? 99  VAL A C   1 
ATOM   765  O O   . VAL A 1 104 ? -37.70938 19.51874 6.55061  1.000 42.93496 ? 99  VAL A O   1 
ATOM   766  C CB  . VAL A 1 104 ? -35.07987 17.83297 7.92988  1.000 42.33218 ? 99  VAL A CB  1 
ATOM   767  C CG1 . VAL A 1 104 ? -33.73248 17.23837 7.54520  1.000 39.94395 ? 99  VAL A CG1 1 
ATOM   768  C CG2 . VAL A 1 104 ? -34.94838 19.25715 8.45386  1.000 34.12283 ? 99  VAL A CG2 1 
ATOM   769  N N   . GLU A 1 105 ? -38.09968 17.82028 7.98487  1.000 49.91184 ? 100 GLU A N   1 
ATOM   770  C CA  . GLU A 1 105 ? -39.40356 18.27243 8.43207  1.000 53.28662 ? 100 GLU A CA  1 
ATOM   771  C C   . GLU A 1 105 ? -39.50021 18.02513 9.92340  1.000 48.54704 ? 100 GLU A C   1 
ATOM   772  O O   . GLU A 1 105 ? -39.09376 16.96179 10.39438 1.000 48.90830 ? 100 GLU A O   1 
ATOM   773  C CB  . GLU A 1 105 ? -40.50243 17.50615 7.71597  1.000 53.56360 ? 100 GLU A CB  1 
ATOM   774  C CG  . GLU A 1 105 ? -41.77926 18.25220 7.53826  1.000 69.23806 ? 100 GLU A CG  1 
ATOM   775  C CD  . GLU A 1 105 ? -42.60598 17.63567 6.44542  1.000 74.59443 ? 100 GLU A CD  1 
ATOM   776  O OE1 . GLU A 1 105 ? -42.49201 16.40407 6.26229  1.000 76.24495 ? 100 GLU A OE1 1 
ATOM   777  O OE2 . GLU A 1 105 ? -43.34059 18.37924 5.76132  1.000 76.88226 ? 100 GLU A OE2 1 
ATOM   778  N N   . ARG A 1 106 ? -40.03725 18.99706 10.66063 1.000 56.19657 ? 101 ARG A N   1 
ATOM   779  C CA  . ARG A 1 106 ? -40.26473 18.82703 12.09196 1.000 62.96095 ? 101 ARG A CA  1 
ATOM   780  C C   . ARG A 1 106 ? -41.68006 18.32061 12.33129 1.000 63.84231 ? 101 ARG A C   1 
ATOM   781  O O   . ARG A 1 106 ? -42.64807 18.91812 11.85444 1.000 63.03520 ? 101 ARG A O   1 
ATOM   782  C CB  . ARG A 1 106 ? -40.03349 20.13473 12.84315 1.000 67.29970 ? 101 ARG A CB  1 
ATOM   783  C CG  . ARG A 1 106 ? -38.62843 20.26966 13.40415 1.000 71.13541 ? 101 ARG A CG  1 
ATOM   784  C CD  . ARG A 1 106 ? -38.10567 21.67585 13.22581 1.000 74.33726 ? 101 ARG A CD  1 
ATOM   785  N NE  . ARG A 1 106 ? -36.91166 21.91597 14.02983 1.000 77.34601 ? 101 ARG A NE  1 
ATOM   786  C CZ  . ARG A 1 106 ? -36.14841 22.99777 13.91827 1.000 79.02730 ? 101 ARG A CZ  1 
ATOM   787  N NH1 . ARG A 1 106 ? -36.45784 23.93284 13.02763 1.000 76.59231 ? 101 ARG A NH1 1 
ATOM   788  N NH2 . ARG A 1 106 ? -35.07461 23.14265 14.69092 1.000 78.03579 ? 101 ARG A NH2 1 
ATOM   789  N N   . ARG A 1 107 ? -41.78892 17.20567 13.05008 1.000 62.12402 ? 102 ARG A N   1 
ATOM   790  C CA  . ARG A 1 107 ? -43.07282 16.57471 13.32736 1.000 67.92298 ? 102 ARG A CA  1 
ATOM   791  C C   . ARG A 1 107 ? -43.11809 16.17051 14.80252 1.000 68.11464 ? 102 ARG A C   1 
ATOM   792  O O   . ARG A 1 107 ? -42.17566 16.45599 15.55163 1.000 64.44430 ? 102 ARG A O   1 
ATOM   793  C CB  . ARG A 1 107 ? -43.28691 15.38076 12.38168 1.000 63.29206 ? 102 ARG A CB  1 
ATOM   794  N N   . ALA A 1 108 ? -44.19551 15.52667 15.24613 1.000 72.99106 ? 103 ALA A N   1 
ATOM   795  C CA  . ALA A 1 108 ? -44.33557 15.22868 16.67309 1.000 69.73483 ? 103 ALA A CA  1 
ATOM   796  C C   . ALA A 1 108 ? -44.36020 13.72342 16.96763 1.000 67.29441 ? 103 ALA A C   1 
ATOM   797  O O   . ALA A 1 108 ? -43.80825 13.26346 17.97729 1.000 64.49335 ? 103 ALA A O   1 
ATOM   798  C CB  . ALA A 1 108 ? -45.58563 15.89825 17.22004 1.000 80.65110 ? 103 ALA A CB  1 
ATOM   799  N N   . THR A 1 116 ? -41.43317 15.62013 19.62819 1.000 83.32351 ? 111 THR A N   1 
ATOM   800  C CA  . THR A 1 116 ? -40.84743 16.30651 18.47702 1.000 78.05819 ? 111 THR A CA  1 
ATOM   801  C C   . THR A 1 116 ? -39.86405 15.41077 17.73968 1.000 70.93479 ? 111 THR A C   1 
ATOM   802  O O   . THR A 1 116 ? -38.95115 14.84654 18.34480 1.000 63.42109 ? 111 THR A O   1 
ATOM   803  C CB  . THR A 1 116 ? -40.11749 17.59913 18.89068 1.000 79.02478 ? 111 THR A CB  1 
ATOM   804  N N   . LEU A 1 117 ? -40.05390 15.29313 16.42788 1.000 67.11655 ? 112 LEU A N   1 
ATOM   805  C CA  . LEU A 1 117 ? -39.21815 14.47012 15.56985 1.000 64.96953 ? 112 LEU A CA  1 
ATOM   806  C C   . LEU A 1 117 ? -38.65309 15.30513 14.42772 1.000 57.08816 ? 112 LEU A C   1 
ATOM   807  O O   . LEU A 1 117 ? -39.27337 16.27565 13.98092 1.000 57.58480 ? 112 LEU A O   1 
ATOM   808  C CB  . LEU A 1 117 ? -40.01278 13.29309 14.98183 1.000 67.85737 ? 112 LEU A CB  1 
ATOM   809  C CG  . LEU A 1 117 ? -40.61526 12.28074 15.95529 1.000 71.20994 ? 112 LEU A CG  1 
ATOM   810  C CD1 . LEU A 1 117 ? -41.50372 11.29810 15.20308 1.000 73.18096 ? 112 LEU A CD1 1 
ATOM   811  C CD2 . LEU A 1 117 ? -39.51577 11.54098 16.69052 1.000 67.82396 ? 112 LEU A CD2 1 
ATOM   812  N N   . VAL A 1 118 ? -37.46983 14.91529 13.96072 1.000 45.72579 ? 113 VAL A N   1 
ATOM   813  C CA  . VAL A 1 118 ? -36.87801 15.43566 12.73349 1.000 45.53195 ? 113 VAL A CA  1 
ATOM   814  C C   . VAL A 1 118 ? -36.89971 14.29840 11.72055 1.000 41.83240 ? 113 VAL A C   1 
ATOM   815  O O   . VAL A 1 118 ? -36.38346 13.20911 11.99390 1.000 42.82167 ? 113 VAL A O   1 
ATOM   816  C CB  . VAL A 1 118 ? -35.45272 15.96280 12.96906 1.000 47.95858 ? 113 VAL A CB  1 
ATOM   817  C CG1 . VAL A 1 118 ? -34.81524 16.43163 11.65866 1.000 44.95979 ? 113 VAL A CG1 1 
ATOM   818  C CG2 . VAL A 1 118 ? -35.47311 17.09433 13.98588 1.000 55.06149 ? 113 VAL A CG2 1 
ATOM   819  N N   . ALA A 1 119 ? -37.52182 14.53247 10.56776 1.000 42.25495 ? 114 ALA A N   1 
ATOM   820  C CA  . ALA A 1 119 ? -37.70328 13.49131 9.56211  1.000 44.16733 ? 114 ALA A CA  1 
ATOM   821  C C   . ALA A 1 119 ? -37.24350 13.99367 8.20327  1.000 45.44203 ? 114 ALA A C   1 
ATOM   822  O O   . ALA A 1 119 ? -37.44016 15.16770 7.88125  1.000 45.53117 ? 114 ALA A O   1 
ATOM   823  C CB  . ALA A 1 119 ? -39.18303 13.04516 9.47530  1.000 39.93052 ? 114 ALA A CB  1 
ATOM   824  N N   . LEU A 1 120 ? -36.64254 13.09992 7.40645  1.000 45.20044 ? 115 LEU A N   1 
ATOM   825  C CA  . LEU A 1 120 ? -36.34382 13.42069 6.01339  1.000 42.09978 ? 115 LEU A CA  1 
ATOM   826  C C   . LEU A 1 120 ? -37.61773 13.74610 5.26528  1.000 43.79779 ? 115 LEU A C   1 
ATOM   827  O O   . LEU A 1 120 ? -38.64534 13.08863 5.44195  1.000 40.73720 ? 115 LEU A O   1 
ATOM   828  C CB  . LEU A 1 120 ? -35.66188 12.24957 5.29793  1.000 39.22489 ? 115 LEU A CB  1 
ATOM   829  C CG  . LEU A 1 120 ? -34.22951 11.92687 5.69353  1.000 40.08877 ? 115 LEU A CG  1 
ATOM   830  C CD1 . LEU A 1 120 ? -33.79747 10.64087 5.02120  1.000 37.60746 ? 115 LEU A CD1 1 
ATOM   831  C CD2 . LEU A 1 120 ? -33.32037 13.08556 5.30677  1.000 36.84722 ? 115 LEU A CD2 1 
ATOM   832  N N   . THR A 1 121 ? -37.54925 14.76142 4.42242  1.000 46.45331 ? 116 THR A N   1 
ATOM   833  C CA  . THR A 1 121 ? -38.55287 14.85465 3.38200  1.000 45.15638 ? 116 THR A CA  1 
ATOM   834  C C   . THR A 1 121 ? -38.19815 13.87997 2.26664  1.000 41.84514 ? 116 THR A C   1 
ATOM   835  O O   . THR A 1 121 ? -37.12085 13.27696 2.25354  1.000 37.93981 ? 116 THR A O   1 
ATOM   836  C CB  . THR A 1 121 ? -38.63629 16.27069 2.83168  1.000 44.98111 ? 116 THR A CB  1 
ATOM   837  O OG1 . THR A 1 121 ? -37.41344 16.56810 2.14487  1.000 47.81339 ? 116 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 121 ? -38.84640 17.27352 3.97758  1.000 39.92831 ? 116 THR A CG2 1 
ATOM   839  N N   . SER A 1 122 ? -39.12020 13.71356 1.31510  1.000 39.18382 ? 117 SER A N   1 
ATOM   840  C CA  . SER A 1 122 ? -38.77974 12.89823 0.15835  1.000 39.29283 ? 117 SER A CA  1 
ATOM   841  C C   . SER A 1 122 ? -37.59884 13.50467 -0.59277 1.000 39.31982 ? 117 SER A C   1 
ATOM   842  O O   . SER A 1 122 ? -36.67250 12.78696 -0.99192 1.000 42.35825 ? 117 SER A O   1 
ATOM   843  C CB  . SER A 1 122 ? -39.99896 12.72390 -0.75357 1.000 48.74998 ? 117 SER A CB  1 
ATOM   844  O OG  . SER A 1 122 ? -40.68796 13.94299 -0.95681 1.000 54.94361 ? 117 SER A OG  1 
ATOM   845  N N   . ALA A 1 123 ? -37.59199 14.83251 -0.75757 1.000 40.24893 ? 118 ALA A N   1 
ATOM   846  C CA  . ALA A 1 123 ? -36.46479 15.48682 -1.41600 1.000 38.71344 ? 118 ALA A CA  1 
ATOM   847  C C   . ALA A 1 123 ? -35.17441 15.27018 -0.64109 1.000 40.01915 ? 118 ALA A C   1 
ATOM   848  O O   . ALA A 1 123 ? -34.11059 15.05766 -1.23615 1.000 35.36341 ? 118 ALA A O   1 
ATOM   849  C CB  . ALA A 1 123 ? -36.74532 16.97703 -1.57782 1.000 43.80242 ? 118 ALA A CB  1 
ATOM   850  N N   . GLY A 1 124 ? -35.24722 15.32311 0.69289  1.000 31.95234 ? 119 GLY A N   1 
ATOM   851  C CA  . GLY A 1 124 ? -34.06266 15.06396 1.49155  1.000 30.80178 ? 119 GLY A CA  1 
ATOM   852  C C   . GLY A 1 124 ? -33.60725 13.62145 1.39782  1.000 33.02150 ? 119 GLY A C   1 
ATOM   853  O O   . GLY A 1 124 ? -32.40511 13.34046 1.36732  1.000 31.46606 ? 119 GLY A O   1 
ATOM   854  N N   . ARG A 1 125 ? -34.55285 12.68208 1.36494  1.000 33.27208 ? 120 ARG A N   1 
ATOM   855  C CA  . ARG A 1 125 ? -34.14771 11.28822 1.22957  1.000 33.28577 ? 120 ARG A CA  1 
ATOM   856  C C   . ARG A 1 125 ? -33.49047 11.03337 -0.12313 1.000 32.15444 ? 120 ARG A C   1 
ATOM   857  O O   . ARG A 1 125 ? -32.46214 10.34756 -0.20708 1.000 33.60176 ? 120 ARG A O   1 
ATOM   858  C CB  . ARG A 1 125 ? -35.34536 10.36402 1.40383  1.000 36.67850 ? 120 ARG A CB  1 
ATOM   859  C CG  . ARG A 1 125 ? -34.94532 8.92737  1.22091  1.000 44.19426 ? 120 ARG A CG  1 
ATOM   860  C CD  . ARG A 1 125 ? -36.13460 8.01310  1.10582  1.000 57.86147 ? 120 ARG A CD  1 
ATOM   861  N NE  . ARG A 1 125 ? -35.71108 6.69217  0.66019  1.000 56.57552 ? 120 ARG A NE  1 
ATOM   862  C CZ  . ARG A 1 125 ? -36.54531 5.71319  0.34719  1.000 52.40006 ? 120 ARG A CZ  1 
ATOM   863  N NH1 . ARG A 1 125 ? -37.85411 5.91456  0.41683  1.000 52.38741 ? 120 ARG A NH1 1 
ATOM   864  N NH2 . ARG A 1 125 ? -36.06692 4.54363  -0.04820 1.000 50.05533 ? 120 ARG A NH2 1 
ATOM   865  N N   . ALA A 1 126 ? -34.07164 11.57209 -1.19286 1.000 31.13053 ? 121 ALA A N   1 
ATOM   866  C CA  . ALA A 1 126 ? -33.46188 11.39078 -2.50806 1.000 31.64167 ? 121 ALA A CA  1 
ATOM   867  C C   . ALA A 1 126 ? -32.06979 11.99913 -2.53466 1.000 38.67602 ? 121 ALA A C   1 
ATOM   868  O O   . ALA A 1 126 ? -31.12813 11.39014 -3.05505 1.000 36.37760 ? 121 ALA A O   1 
ATOM   869  C CB  . ALA A 1 126 ? -34.34675 12.01238 -3.58523 1.000 37.36966 ? 121 ALA A CB  1 
ATOM   870  N N   . LEU A 1 127 ? -31.91335 13.17717 -1.92144 1.000 39.43468 ? 122 LEU A N   1 
ATOM   871  C CA  . LEU A 1 127 ? -30.62510 13.85730 -1.92671 1.000 37.15844 ? 122 LEU A CA  1 
ATOM   872  C C   . LEU A 1 127 ? -29.55429 13.01252 -1.24709 1.000 29.97124 ? 122 LEU A C   1 
ATOM   873  O O   . LEU A 1 127 ? -28.49226 12.75582 -1.82877 1.000 34.14511 ? 122 LEU A O   1 
ATOM   874  C CB  . LEU A 1 127 ? -30.75082 15.22624 -1.25375 1.000 36.70407 ? 122 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 127 ? -29.40860 15.94116 -1.07635 1.000 38.75482 ? 122 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 127 ? -28.75759 16.12377 -2.42978 1.000 50.51914 ? 122 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 127 ? -29.60241 17.27423 -0.39149 1.000 41.50938 ? 122 LEU A CD2 1 
ATOM   878  N N   . ILE A 1 128 ? -29.81732 12.55741 -0.01582 1.000 28.48275 ? 123 ILE A N   1 
ATOM   879  C CA  . ILE A 1 128 ? -28.80263 11.81293 0.72883  1.000 28.29549 ? 123 ILE A CA  1 
ATOM   880  C C   . ILE A 1 128 ? -28.56978 10.42288 0.13196  1.000 29.12869 ? 123 ILE A C   1 
ATOM   881  O O   . ILE A 1 128 ? -27.45222 9.89049  0.21809  1.000 32.51317 ? 123 ILE A O   1 
ATOM   882  C CB  . ILE A 1 128 ? -29.17776 11.74605 2.22864  1.000 31.68448 ? 123 ILE A CB  1 
ATOM   883  C CG1 . ILE A 1 128 ? -27.98122 11.27172 3.04393  1.000 31.76758 ? 123 ILE A CG1 1 
ATOM   884  C CG2 . ILE A 1 128 ? -30.39988 10.84877 2.47875  1.000 35.43630 ? 123 ILE A CG2 1 
ATOM   885  C CD1 . ILE A 1 128 ? -26.80285 12.21848 2.91517  1.000 33.66531 ? 123 ILE A CD1 1 
ATOM   886  N N   . ASP A 1 129 ? -29.59731 9.81768  -0.48611 1.000 31.60894 ? 124 ASP A N   1 
ATOM   887  C CA  . ASP A 1 129 ? -29.40716 8.57131  -1.23103 1.000 33.83162 ? 124 ASP A CA  1 
ATOM   888  C C   . ASP A 1 129 ? -28.43311 8.76172  -2.39632 1.000 38.39270 ? 124 ASP A C   1 
ATOM   889  O O   . ASP A 1 129 ? -27.60550 7.88938  -2.67594 1.000 31.15539 ? 124 ASP A O   1 
ATOM   890  C CB  . ASP A 1 129 ? -30.75187 8.05648  -1.76466 1.000 39.71687 ? 124 ASP A CB  1 
ATOM   891  C CG  . ASP A 1 129 ? -31.50581 7.18460  -0.76267 1.000 42.74740 ? 124 ASP A CG  1 
ATOM   892  O OD1 . ASP A 1 129 ? -30.88734 6.69001  0.19563  1.000 39.64322 ? 124 ASP A OD1 1 
ATOM   893  O OD2 . ASP A 1 129 ? -32.72268 6.96150  -0.96692 1.000 46.10821 ? 124 ASP A OD2 1 
ATOM   894  N N   . ASP A 1 130 ? -28.54683 9.88391  -3.10819 1.000 44.63102 ? 125 ASP A N   1 
ATOM   895  C CA  . ASP A 1 130 ? -27.55848 10.26875 -4.12056 1.000 37.13021 ? 125 ASP A CA  1 
ATOM   896  C C   . ASP A 1 130 ? -26.19632 10.55970 -3.48409 1.000 38.92745 ? 125 ASP A C   1 
ATOM   897  O O   . ASP A 1 130 ? -25.16816 9.99041  -3.87685 1.000 36.68901 ? 125 ASP A O   1 
ATOM   898  C CB  . ASP A 1 130 ? -28.07489 11.50955 -4.84635 1.000 49.21538 ? 125 ASP A CB  1 
ATOM   899  C CG  . ASP A 1 130 ? -27.56658 11.63093 -6.26832 1.000 65.47372 ? 125 ASP A CG  1 
ATOM   900  O OD1 . ASP A 1 130 ? -26.56815 10.97149 -6.62634 1.000 82.67786 ? 125 ASP A OD1 1 
ATOM   901  O OD2 . ASP A 1 130 ? -28.18059 12.41506 -7.01986 1.000 64.63756 ? 125 ASP A OD2 1 
ATOM   902  N N   . ALA A 1 131 ? -26.17592 11.44175 -2.48579 1.000 32.39245 ? 126 ALA A N   1 
ATOM   903  C CA  . ALA A 1 131 ? -24.90874 11.96245 -1.97273 1.000 39.08849 ? 126 ALA A CA  1 
ATOM   904  C C   . ALA A 1 131 ? -24.06966 10.88493 -1.29437 1.000 37.23369 ? 126 ALA A C   1 
ATOM   905  O O   . ALA A 1 131 ? -22.83472 10.91447 -1.37987 1.000 36.71435 ? 126 ALA A O   1 
ATOM   906  C CB  . ALA A 1 131 ? -25.16187 13.11530 -1.00114 1.000 33.10324 ? 126 ALA A CB  1 
ATOM   907  N N   . VAL A 1 132 ? -24.70431 9.93324  -0.60290 1.000 37.66989 ? 127 VAL A N   1 
ATOM   908  C CA  . VAL A 1 132 ? -23.90097 8.98191  0.16188  1.000 38.54726 ? 127 VAL A CA  1 
ATOM   909  C C   . VAL A 1 132 ? -23.07315 8.08460  -0.76068 1.000 34.58675 ? 127 VAL A C   1 
ATOM   910  O O   . VAL A 1 132 ? -21.96896 7.66202  -0.39536 1.000 38.72918 ? 127 VAL A O   1 
ATOM   911  C CB  . VAL A 1 132 ? -24.77606 8.15145  1.11705  1.000 36.71995 ? 127 VAL A CB  1 
ATOM   912  C CG1 . VAL A 1 132 ? -25.68787 7.21741  0.34667  1.000 34.93051 ? 127 VAL A CG1 1 
ATOM   913  C CG2 . VAL A 1 132 ? -23.89719 7.37094  2.06189  1.000 43.99434 ? 127 VAL A CG2 1 
ATOM   914  N N   . VAL A 1 133 ? -23.57466 7.77622  -1.95721 1.000 36.86246 ? 128 VAL A N   1 
ATOM   915  C CA  . VAL A 1 133 ? -22.78132 7.00102  -2.91496 1.000 36.37011 ? 128 VAL A CA  1 
ATOM   916  C C   . VAL A 1 133 ? -21.54676 7.78866  -3.33991 1.000 42.88708 ? 128 VAL A C   1 
ATOM   917  O O   . VAL A 1 133 ? -20.42157 7.26996  -3.33613 1.000 40.39870 ? 128 VAL A O   1 
ATOM   918  C CB  . VAL A 1 133 ? -23.63710 6.59766  -4.12788 1.000 39.54673 ? 128 VAL A CB  1 
ATOM   919  C CG1 . VAL A 1 133 ? -22.75087 6.01408  -5.23910 1.000 42.42934 ? 128 VAL A CG1 1 
ATOM   920  C CG2 . VAL A 1 133 ? -24.68092 5.58555  -3.70996 1.000 45.41697 ? 128 VAL A CG2 1 
ATOM   921  N N   . ALA A 1 134 ? -21.73436 9.06070  -3.70712 1.000 41.87202 ? 129 ALA A N   1 
ATOM   922  C CA  . ALA A 1 134 ? -20.58715 9.87562  -4.09468 1.000 45.27683 ? 129 ALA A CA  1 
ATOM   923  C C   . ALA A 1 134 ? -19.63858 10.05916 -2.92134 1.000 40.24184 ? 129 ALA A C   1 
ATOM   924  O O   . ALA A 1 134 ? -18.41252 10.08952 -3.09538 1.000 40.85188 ? 129 ALA A O   1 
ATOM   925  C CB  . ALA A 1 134 ? -21.05230 11.23155 -4.63361 1.000 47.45969 ? 129 ALA A CB  1 
ATOM   926  N N   . HIS A 1 135 ? -20.19384 10.17089 -1.71543 1.000 34.97742 ? 130 HIS A N   1 
ATOM   927  C CA  . HIS A 1 135 ? -19.37489 10.32799 -0.51926 1.000 37.13364 ? 130 HIS A CA  1 
ATOM   928  C C   . HIS A 1 135 ? -18.43797 9.14148  -0.32713 1.000 35.35913 ? 130 HIS A C   1 
ATOM   929  O O   . HIS A 1 135 ? -17.23367 9.32247  -0.11746 1.000 35.31724 ? 130 HIS A O   1 
ATOM   930  C CB  . HIS A 1 135 ? -20.27519 10.50925 0.70486  1.000 32.29612 ? 130 HIS A CB  1 
ATOM   931  C CG  . HIS A 1 135 ? -19.52754 10.58360 1.99346  1.000 34.77410 ? 130 HIS A CG  1 
ATOM   932  N ND1 . HIS A 1 135 ? -18.55651 11.53096 2.23136  1.000 36.14084 ? 130 HIS A ND1 1 
ATOM   933  C CD2 . HIS A 1 135 ? -19.61685 9.83959  3.12091  1.000 38.03517 ? 130 HIS A CD2 1 
ATOM   934  C CE1 . HIS A 1 135 ? -18.08532 11.37797 3.45840  1.000 37.26698 ? 130 HIS A CE1 1 
ATOM   935  N NE2 . HIS A 1 135 ? -18.70913 10.35674 4.01965  1.000 35.95712 ? 130 HIS A NE2 1 
ATOM   936  N N   . VAL A 1 136 ? -18.96837 7.91326  -0.39316 1.000 31.17124 ? 131 VAL A N   1 
ATOM   937  C CA  . VAL A 1 136 ? -18.12109 6.76167  -0.10120 1.000 36.63342 ? 131 VAL A CA  1 
ATOM   938  C C   . VAL A 1 136 ? -17.07111 6.58830  -1.18806 1.000 38.30883 ? 131 VAL A C   1 
ATOM   939  O O   . VAL A 1 136 ? -15.91606 6.26228  -0.89467 1.000 42.50433 ? 131 VAL A O   1 
ATOM   940  C CB  . VAL A 1 136 ? -18.95155 5.47972  0.10502  1.000 41.98329 ? 131 VAL A CB  1 
ATOM   941  C CG1 . VAL A 1 136 ? -19.72383 5.54775  1.42068  1.000 41.82983 ? 131 VAL A CG1 1 
ATOM   942  C CG2 . VAL A 1 136 ? -19.87907 5.22648  -1.06306 1.000 50.51165 ? 131 VAL A CG2 1 
ATOM   943  N N   . ASP A 1 137 ? -17.44745 6.80258  -2.45510 1.000 42.34480 ? 132 ASP A N   1 
ATOM   944  C CA  . ASP A 1 137 ? -16.44765 6.82917  -3.52258 1.000 45.27369 ? 132 ASP A CA  1 
ATOM   945  C C   . ASP A 1 137 ? -15.36685 7.86001  -3.22216 1.000 44.70880 ? 132 ASP A C   1 
ATOM   946  O O   . ASP A 1 137 ? -14.16984 7.58551  -3.36362 1.000 47.93914 ? 132 ASP A O   1 
ATOM   947  C CB  . ASP A 1 137 ? -17.10859 7.12609  -4.86830 1.000 51.78815 ? 132 ASP A CB  1 
ATOM   948  C CG  . ASP A 1 137 ? -17.80797 5.91787  -5.44760 1.000 68.32694 ? 132 ASP A CG  1 
ATOM   949  O OD1 . ASP A 1 137 ? -17.81460 4.85795  -4.77937 1.000 69.65934 ? 132 ASP A OD1 1 
ATOM   950  O OD2 . ASP A 1 137 ? -18.34500 6.02195  -6.57373 1.000 80.26558 ? 132 ASP A OD2 1 
ATOM   951  N N   . ASN A 1 138 ? -15.77699 9.05536  -2.79639 1.000 41.72954 ? 133 ASN A N   1 
ATOM   952  C CA  . ASN A 1 138 ? -14.80768 10.08617 -2.44169 1.000 42.71227 ? 133 ASN A CA  1 
ATOM   953  C C   . ASN A 1 138 ? -13.89163 9.61032  -1.32007 1.000 43.65163 ? 133 ASN A C   1 
ATOM   954  O O   . ASN A 1 138 ? -12.67253 9.81623  -1.37672 1.000 43.63899 ? 133 ASN A O   1 
ATOM   955  C CB  . ASN A 1 138 ? -15.54217 11.36498 -2.03949 1.000 41.62463 ? 133 ASN A CB  1 
ATOM   956  C CG  . ASN A 1 138 ? -14.62584 12.57760 -1.96870 1.000 42.05016 ? 133 ASN A CG  1 
ATOM   957  O OD1 . ASN A 1 138 ? -13.68888 12.72004 -2.75794 1.000 37.49838 ? 133 ASN A OD1 1 
ATOM   958  N ND2 . ASN A 1 138 ? -14.89855 13.45986 -1.01819 1.000 36.75177 ? 133 ASN A ND2 1 
ATOM   959  N N   . GLN A 1 139 ? -14.46201 8.95388  -0.30068 1.000 39.00896 ? 134 GLN A N   1 
ATOM   960  C CA  . GLN A 1 139 ? -13.66442 8.48558  0.83449  1.000 34.77859 ? 134 GLN A CA  1 
ATOM   961  C C   . GLN A 1 139 ? -12.62591 7.45564  0.39847  1.000 41.73190 ? 134 GLN A C   1 
ATOM   962  O O   . GLN A 1 139 ? -11.48606 7.46464  0.88131  1.000 39.66257 ? 134 GLN A O   1 
ATOM   963  C CB  . GLN A 1 139 ? -14.57320 7.88787  1.90922  1.000 31.21601 ? 134 GLN A CB  1 
ATOM   964  C CG  . GLN A 1 139 ? -15.45915 8.88126  2.64882  1.000 30.60707 ? 134 GLN A CG  1 
ATOM   965  C CD  . GLN A 1 139 ? -15.92318 8.34652  4.00089  1.000 38.73623 ? 134 GLN A CD  1 
ATOM   966  O OE1 . GLN A 1 139 ? -15.89227 9.05694  5.00835  1.000 38.07950 ? 134 GLN A OE1 1 
ATOM   967  N NE2 . GLN A 1 139 ? -16.36116 7.09177  4.02285  1.000 35.97268 ? 134 GLN A NE2 1 
ATOM   968  N N   . ARG A 1 140 ? -13.00451 6.54668  -0.50194 1.000 39.77619 ? 135 ARG A N   1 
ATOM   969  C CA  . ARG A 1 140 ? -12.06272 5.52050  -0.93149 1.000 41.99078 ? 135 ARG A CA  1 
ATOM   970  C C   . ARG A 1 140 ? -10.86172 6.13741  -1.63875 1.000 42.22762 ? 135 ARG A C   1 
ATOM   971  O O   . ARG A 1 140 ? -9.72716  5.67944  -1.46214 1.000 49.66675 ? 135 ARG A O   1 
ATOM   972  C CB  . ARG A 1 140 ? -12.76575 4.50672  -1.83854 1.000 52.85819 ? 135 ARG A CB  1 
ATOM   973  C CG  . ARG A 1 140 ? -13.68845 3.55254  -1.10697 1.000 56.08356 ? 135 ARG A CG  1 
ATOM   974  N N   . ARG A 1 141 ? -11.08938 7.17016  -2.45601 1.000 41.27322 ? 136 ARG A N   1 
ATOM   975  C CA  . ARG A 1 141 ? -9.96960  7.84288  -3.10957 1.000 44.03524 ? 136 ARG A CA  1 
ATOM   976  C C   . ARG A 1 141 ? -9.10712  8.57487  -2.08430 1.000 46.14615 ? 136 ARG A C   1 
ATOM   977  O O   . ARG A 1 141 ? -7.87619  8.60400  -2.21101 1.000 47.30788 ? 136 ARG A O   1 
ATOM   978  C CB  . ARG A 1 141 ? -10.48633 8.80587  -4.18627 1.000 48.52031 ? 136 ARG A CB  1 
ATOM   979  C CG  . ARG A 1 141 ? -11.29954 8.13000  -5.31225 1.000 52.50643 ? 136 ARG A CG  1 
ATOM   980  C CD  . ARG A 1 141 ? -11.76457 9.12797  -6.37639 1.000 52.98651 ? 136 ARG A CD  1 
ATOM   981  N N   . VAL A 1 142 ? -9.73751  9.14776  -1.04912 1.000 41.24285 ? 137 VAL A N   1 
ATOM   982  C CA  . VAL A 1 142 ? -8.98941  9.79185  0.03122  1.000 35.43045 ? 137 VAL A CA  1 
ATOM   983  C C   . VAL A 1 142 ? -8.05014  8.79295  0.69547  1.000 37.72628 ? 137 VAL A C   1 
ATOM   984  O O   . VAL A 1 142 ? -6.91783  9.12833  1.06162  1.000 44.66360 ? 137 VAL A O   1 
ATOM   985  C CB  . VAL A 1 142 ? -9.95420  10.41748 1.05979  1.000 39.29466 ? 137 VAL A CB  1 
ATOM   986  C CG1 . VAL A 1 142 ? -9.17954  10.88507 2.29292  1.000 33.13023 ? 137 VAL A CG1 1 
ATOM   987  C CG2 . VAL A 1 142 ? -10.72330 11.57986 0.45204  1.000 43.48446 ? 137 VAL A CG2 1 
ATOM   988  N N   . LEU A 1 143 ? -8.50393  7.55377  0.86399  1.000 36.05035 ? 138 LEU A N   1 
ATOM   989  C CA  . LEU A 1 143 ? -7.78178  6.54417  1.63156  1.000 39.68097 ? 138 LEU A CA  1 
ATOM   990  C C   . LEU A 1 143 ? -6.87502  5.67703  0.77577  1.000 46.05036 ? 138 LEU A C   1 
ATOM   991  O O   . LEU A 1 143 ? -6.18536  4.80288  1.31426  1.000 51.73702 ? 138 LEU A O   1 
ATOM   992  C CB  . LEU A 1 143 ? -8.77436  5.64725  2.36496  1.000 41.39495 ? 138 LEU A CB  1 
ATOM   993  C CG  . LEU A 1 143 ? -9.50109  6.34906  3.50769  1.000 43.06614 ? 138 LEU A CG  1 
ATOM   994  C CD1 . LEU A 1 143 ? -10.77368 5.59841  3.83161  1.000 44.04402 ? 138 LEU A CD1 1 
ATOM   995  C CD2 . LEU A 1 143 ? -8.59601  6.41868  4.72187  1.000 43.24898 ? 138 LEU A CD2 1 
ATOM   996  N N   . SER A 1 144 ? -6.85326  5.90474  -0.53604 1.000 48.27215 ? 139 SER A N   1 
ATOM   997  C CA  . SER A 1 144 ? -6.27307  4.93174  -1.45165 1.000 51.13196 ? 139 SER A CA  1 
ATOM   998  C C   . SER A 1 144 ? -4.76645  4.79708  -1.29413 1.000 54.47175 ? 139 SER A C   1 
ATOM   999  O O   . SER A 1 144 ? -4.19859  3.80257  -1.75656 1.000 55.28169 ? 139 SER A O   1 
ATOM   1000 C CB  . SER A 1 144 ? -6.61784  5.30766  -2.89158 1.000 51.39603 ? 139 SER A CB  1 
ATOM   1001 O OG  . SER A 1 144 ? -6.09171  6.58167  -3.21851 1.000 54.07580 ? 139 SER A OG  1 
ATOM   1002 N N   . ALA A 1 145 ? -4.10298  5.76677  -0.66012 1.000 52.93122 ? 140 ALA A N   1 
ATOM   1003 C CA  . ALA A 1 145 ? -2.67081  5.63332  -0.41418 1.000 58.22896 ? 140 ALA A CA  1 
ATOM   1004 C C   . ALA A 1 145 ? -2.36038  4.60644  0.67008  1.000 57.38000 ? 140 ALA A C   1 
ATOM   1005 O O   . ALA A 1 145 ? -1.21898  4.14479  0.76233  1.000 60.79651 ? 140 ALA A O   1 
ATOM   1006 C CB  . ALA A 1 145 ? -2.06939  6.98489  -0.03154 1.000 58.70644 ? 140 ALA A CB  1 
ATOM   1007 N N   . LEU A 1 146 ? -3.33993  4.24327  1.49060  1.000 49.86938 ? 141 LEU A N   1 
ATOM   1008 C CA  . LEU A 1 146 ? -3.16951  3.20896  2.49908  1.000 47.08475 ? 141 LEU A CA  1 
ATOM   1009 C C   . LEU A 1 146 ? -3.72036  1.88753  1.99089  1.000 53.27206 ? 141 LEU A C   1 
ATOM   1010 O O   . LEU A 1 146 ? -4.81336  1.84041  1.41847  1.000 52.92361 ? 141 LEU A O   1 
ATOM   1011 C CB  . LEU A 1 146 ? -3.88767  3.57907  3.79588  1.000 42.32300 ? 141 LEU A CB  1 
ATOM   1012 C CG  . LEU A 1 146 ? -3.52144  4.92946  4.39061  1.000 41.86959 ? 141 LEU A CG  1 
ATOM   1013 C CD1 . LEU A 1 146 ? -4.20932  5.08348  5.74087  1.000 42.32362 ? 141 LEU A CD1 1 
ATOM   1014 C CD2 . LEU A 1 146 ? -2.02485  5.04386  4.52572  1.000 41.04629 ? 141 LEU A CD2 1 
ATOM   1015 N N   . SER A 1 147 ? -2.97531  0.81010  2.22654  1.000 57.15457 ? 142 SER A N   1 
ATOM   1016 C CA  . SER A 1 147 ? -3.49236  -0.50305 1.88106  1.000 61.44584 ? 142 SER A CA  1 
ATOM   1017 C C   . SER A 1 147 ? -4.66822  -0.85216 2.79057  1.000 60.45032 ? 142 SER A C   1 
ATOM   1018 O O   . SER A 1 147 ? -4.95987  -0.15830 3.76638  1.000 56.73546 ? 142 SER A O   1 
ATOM   1019 C CB  . SER A 1 147 ? -2.40390  -1.55950 2.00770  1.000 62.69329 ? 142 SER A CB  1 
ATOM   1020 O OG  . SER A 1 147 ? -2.22621  -1.89065 3.36921  1.000 65.02635 ? 142 SER A OG  1 
ATOM   1021 N N   . ALA A 1 148 ? -5.35211  -1.94978 2.46054  1.000 62.60891 ? 143 ALA A N   1 
ATOM   1022 C CA  . ALA A 1 148 ? -6.47851  -2.38490 3.28164  1.000 58.56567 ? 143 ALA A CA  1 
ATOM   1023 C C   . ALA A 1 148 ? -6.04259  -2.62265 4.72267  1.000 57.80820 ? 143 ALA A C   1 
ATOM   1024 O O   . ALA A 1 148 ? -6.66548  -2.11893 5.66468  1.000 50.22406 ? 143 ALA A O   1 
ATOM   1025 C CB  . ALA A 1 148 ? -7.10849  -3.64509 2.69143  1.000 59.97592 ? 143 ALA A CB  1 
ATOM   1026 N N   . ALA A 1 149 ? -4.95488  -3.37570 4.90983  1.000 61.11070 ? 144 ALA A N   1 
ATOM   1027 C CA  . ALA A 1 149 ? -4.44748  -3.62679 6.25494  1.000 60.31962 ? 144 ALA A CA  1 
ATOM   1028 C C   . ALA A 1 149 ? -4.01365  -2.33874 6.94503  1.000 59.94425 ? 144 ALA A C   1 
ATOM   1029 O O   . ALA A 1 149 ? -4.14678  -2.22028 8.16755  1.000 61.19188 ? 144 ALA A O   1 
ATOM   1030 C CB  . ALA A 1 149 ? -3.28572  -4.62036 6.20556  1.000 62.21616 ? 144 ALA A CB  1 
ATOM   1031 N N   . GLU A 1 150 ? -3.49340  -1.36645 6.18810  1.000 57.81925 ? 145 GLU A N   1 
ATOM   1032 C CA  . GLU A 1 150 ? -3.11877  -0.08608 6.78743  1.000 54.07435 ? 145 GLU A CA  1 
ATOM   1033 C C   . GLU A 1 150 ? -4.34779  0.68066  7.26528  1.000 54.70893 ? 145 GLU A C   1 
ATOM   1034 O O   . GLU A 1 150 ? -4.32519  1.30892  8.33196  1.000 53.03803 ? 145 GLU A O   1 
ATOM   1035 C CB  . GLU A 1 150 ? -2.31689  0.74980  5.78898  1.000 53.58807 ? 145 GLU A CB  1 
ATOM   1036 C CG  . GLU A 1 150 ? -0.85674  0.33339  5.66714  1.000 58.46546 ? 145 GLU A CG  1 
ATOM   1037 C CD  . GLU A 1 150 ? -0.15171  0.98955  4.49348  1.000 59.22302 ? 145 GLU A CD  1 
ATOM   1038 O OE1 . GLU A 1 150 ? -0.80938  1.23875  3.46262  1.000 60.42889 ? 145 GLU A OE1 1 
ATOM   1039 O OE2 . GLU A 1 150 ? 1.06371   1.25146  4.60083  1.000 63.75606 ? 145 GLU A OE2 1 
ATOM   1040 N N   . GLN A 1 151 ? -5.43412  0.63394  6.49686  1.000 55.35431 ? 146 GLN A N   1 
ATOM   1041 C CA  . GLN A 1 151 ? -6.66146  1.29063  6.92616  1.000 46.80069 ? 146 GLN A CA  1 
ATOM   1042 C C   . GLN A 1 151 ? -7.23445  0.62229  8.17206  1.000 48.38669 ? 146 GLN A C   1 
ATOM   1043 O O   . GLN A 1 151 ? -7.59214  1.30360  9.13949  1.000 47.74101 ? 146 GLN A O   1 
ATOM   1044 C CB  . GLN A 1 151 ? -7.66706  1.30107  5.77646  1.000 48.46096 ? 146 GLN A CB  1 
ATOM   1045 C CG  . GLN A 1 151 ? -7.14763  2.06616  4.56929  1.000 47.09748 ? 146 GLN A CG  1 
ATOM   1046 C CD  . GLN A 1 151 ? -8.12948  2.10344  3.42316  1.000 49.63611 ? 146 GLN A CD  1 
ATOM   1047 O OE1 . GLN A 1 151 ? -9.34211  2.16392  3.63419  1.000 51.04853 ? 146 GLN A OE1 1 
ATOM   1048 N NE2 . GLN A 1 151 ? -7.60954  2.06214  2.19169  1.000 47.48874 ? 146 GLN A NE2 1 
ATOM   1049 N N   . ARG A 1 152 ? -7.30503  -0.71409 8.18475  1.000 48.99417 ? 147 ARG A N   1 
ATOM   1050 C CA  . ARG A 1 152 ? -7.75151  -1.40044 9.39600  1.000 47.29521 ? 147 ARG A CA  1 
ATOM   1051 C C   . ARG A 1 152 ? -6.86773  -1.03439 10.58159 1.000 49.65009 ? 147 ARG A C   1 
ATOM   1052 O O   . ARG A 1 152 ? -7.35727  -0.82696 11.69876 1.000 48.44725 ? 147 ARG A O   1 
ATOM   1053 C CB  . ARG A 1 152 ? -7.75235  -2.91638 9.18531  1.000 51.19708 ? 147 ARG A CB  1 
ATOM   1054 N N   . GLN A 1 153 ? -5.56072  -0.94562 10.34148 1.000 49.67166 ? 148 GLN A N   1 
ATOM   1055 C CA  . GLN A 1 153 ? -4.59698  -0.60925 11.38198 1.000 53.56352 ? 148 GLN A CA  1 
ATOM   1056 C C   . GLN A 1 153 ? -4.82714  0.80122  11.90677 1.000 53.42821 ? 148 GLN A C   1 
ATOM   1057 O O   . GLN A 1 153 ? -4.79128  1.04246  13.12010 1.000 52.32289 ? 148 GLN A O   1 
ATOM   1058 C CB  . GLN A 1 153 ? -3.19812  -0.74486 10.79390 1.000 57.81193 ? 148 GLN A CB  1 
ATOM   1059 C CG  . GLN A 1 153 ? -2.04720  -0.77175 11.72776 1.000 66.48388 ? 148 GLN A CG  1 
ATOM   1060 C CD  . GLN A 1 153 ? -0.78335  -1.07386 10.95172 1.000 80.12234 ? 148 GLN A CD  1 
ATOM   1061 O OE1 . GLN A 1 153 ? -0.73859  -0.88779 9.73382  1.000 85.39241 ? 148 GLN A OE1 1 
ATOM   1062 N NE2 . GLN A 1 153 ? 0.23545   -1.56713 11.63484 1.000 84.62508 ? 148 GLN A NE2 1 
ATOM   1063 N N   . LEU A 1 154 ? -5.05255  1.75298  10.99648 1.000 47.21679 ? 149 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 154 ? -5.30188  3.12773  11.41298 1.000 45.60156 ? 149 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 154 ? -6.60119  3.23259  12.20016 1.000 46.56068 ? 149 LEU A C   1 
ATOM   1066 O O   . LEU A 1 154 ? -6.67574  3.97665  13.18340 1.000 42.80621 ? 149 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 154 ? -5.32513  4.04777  10.19170 1.000 45.05458 ? 149 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 154 ? -5.50984  5.55023  10.40785 1.000 43.09841 ? 149 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 154 ? -4.49778  6.05924  11.39913 1.000 41.61975 ? 149 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 154 ? -5.34139  6.28584  9.08867  1.000 41.09265 ? 149 LEU A CD2 1 
ATOM   1071 N N   . ALA A 1 155 ? -7.63133  2.47945  11.79511 1.000 46.77312 ? 150 ALA A N   1 
ATOM   1072 C CA  . ALA A 1 155 ? -8.90767  2.52980  12.50383 1.000 44.00893 ? 150 ALA A CA  1 
ATOM   1073 C C   . ALA A 1 155 ? -8.78880  1.94007  13.90752 1.000 47.40453 ? 150 ALA A C   1 
ATOM   1074 O O   . ALA A 1 155 ? -9.46523  2.39575  14.83919 1.000 40.99931 ? 150 ALA A O   1 
ATOM   1075 C CB  . ALA A 1 155 ? -9.98712  1.79914  11.70127 1.000 42.58948 ? 150 ALA A CB  1 
ATOM   1076 N N   . LYS A 1 156 ? -7.94573  0.91947  14.07931 1.000 47.19057 ? 151 LYS A N   1 
ATOM   1077 C CA  . LYS A 1 156 ? -7.75735  0.34840  15.40932 1.000 46.14246 ? 151 LYS A CA  1 
ATOM   1078 C C   . LYS A 1 156 ? -7.04087  1.32623  16.33531 1.000 47.28977 ? 151 LYS A C   1 
ATOM   1079 O O   . LYS A 1 156 ? -7.44122  1.49678  17.49206 1.000 46.26089 ? 151 LYS A O   1 
ATOM   1080 C CB  . LYS A 1 156 ? -6.98513  -0.97091 15.32094 1.000 44.39077 ? 151 LYS A CB  1 
ATOM   1081 N N   . LEU A 1 157 ? -5.98712  1.98689  15.84516 1.000 47.57603 ? 152 LEU A N   1 
ATOM   1082 C CA  . LEU A 1 157 ? -5.26874  2.94941  16.67903 1.000 46.78789 ? 152 LEU A CA  1 
ATOM   1083 C C   . LEU A 1 157 ? -6.14739  4.14895  17.03824 1.000 44.85365 ? 152 LEU A C   1 
ATOM   1084 O O   . LEU A 1 157 ? -6.16890  4.58583  18.19820 1.000 40.02676 ? 152 LEU A O   1 
ATOM   1085 C CB  . LEU A 1 157 ? -3.99137  3.40102  15.96923 1.000 41.95775 ? 152 LEU A CB  1 
ATOM   1086 C CG  . LEU A 1 157 ? -2.95066  2.30465  15.73728 1.000 44.85292 ? 152 LEU A CG  1 
ATOM   1087 C CD1 . LEU A 1 157 ? -1.84543  2.80935  14.84751 1.000 47.21257 ? 152 LEU A CD1 1 
ATOM   1088 C CD2 . LEU A 1 157 ? -2.37964  1.81345  17.06189 1.000 50.39157 ? 152 LEU A CD2 1 
ATOM   1089 N N   . LEU A 1 158 ? -6.88543  4.69079  16.06341 1.000 39.18532 ? 153 LEU A N   1 
ATOM   1090 C CA  . LEU A 1 158 ? -7.78766  5.80225  16.35985 1.000 36.53895 ? 153 LEU A CA  1 
ATOM   1091 C C   . LEU A 1 158 ? -8.88094  5.38915  17.33730 1.000 40.70184 ? 153 LEU A C   1 
ATOM   1092 O O   . LEU A 1 158 ? -9.31413  6.19953  18.16651 1.000 48.06380 ? 153 LEU A O   1 
ATOM   1093 C CB  . LEU A 1 158 ? -8.40427  6.34324  15.06606 1.000 28.53633 ? 153 LEU A CB  1 
ATOM   1094 C CG  . LEU A 1 158 ? -7.41850  7.06132  14.15498 1.000 36.14881 ? 153 LEU A CG  1 
ATOM   1095 C CD1 . LEU A 1 158 ? -8.03871  7.31308  12.78333 1.000 34.47269 ? 153 LEU A CD1 1 
ATOM   1096 C CD2 . LEU A 1 158 ? -6.96189  8.36979  14.80339 1.000 39.54758 ? 153 LEU A CD2 1 
ATOM   1097 N N   . ASP A 1 159 ? -9.32660  4.13301  17.27476 1.000 39.94914 ? 154 ASP A N   1 
ATOM   1098 C CA  . ASP A 1 159 ? -10.32755 3.66447  18.22511 1.000 36.47538 ? 154 ASP A CA  1 
ATOM   1099 C C   . ASP A 1 159 ? -9.76699  3.66839  19.64565 1.000 45.97421 ? 154 ASP A C   1 
ATOM   1100 O O   . ASP A 1 159 ? -10.42507 4.12164  20.58883 1.000 44.74880 ? 154 ASP A O   1 
ATOM   1101 C CB  . ASP A 1 159 ? -10.80566 2.27011  17.81677 1.000 43.53310 ? 154 ASP A CB  1 
ATOM   1102 C CG  . ASP A 1 159 ? -11.79345 1.67082  18.80366 1.000 50.59752 ? 154 ASP A CG  1 
ATOM   1103 O OD1 . ASP A 1 159 ? -12.69985 2.39718  19.26677 1.000 49.32650 ? 154 ASP A OD1 1 
ATOM   1104 O OD2 . ASP A 1 159 ? -11.68089 0.45917  19.08568 1.000 54.26527 ? 154 ASP A OD2 1 
ATOM   1105 N N   . LYS A 1 160 ? -8.53552  3.18849  19.81013 1.000 45.07854 ? 155 LYS A N   1 
ATOM   1106 C CA  . LYS A 1 160 ? -7.91980  3.14964  21.13298 1.000 50.22250 ? 155 LYS A CA  1 
ATOM   1107 C C   . LYS A 1 160 ? -7.63223  4.55267  21.65813 1.000 48.61792 ? 155 LYS A C   1 
ATOM   1108 O O   . LYS A 1 160 ? -7.84754  4.83496  22.84339 1.000 52.96476 ? 155 LYS A O   1 
ATOM   1109 C CB  . LYS A 1 160 ? -6.63879  2.32318  21.07199 1.000 50.92932 ? 155 LYS A CB  1 
ATOM   1110 C CG  . LYS A 1 160 ? -6.04829  1.97471  22.40231 1.000 51.28304 ? 155 LYS A CG  1 
ATOM   1111 C CD  . LYS A 1 160 ? -4.92422  0.96286  22.22416 1.000 57.68397 ? 155 LYS A CD  1 
ATOM   1112 C CE  . LYS A 1 160 ? -4.29972  0.59165  23.55482 1.000 60.31171 ? 155 LYS A CE  1 
ATOM   1113 N NZ  . LYS A 1 160 ? -3.10496  -0.28592 23.37656 1.000 66.48448 ? 155 LYS A NZ  1 
ATOM   1114 N N   . LEU A 1 161 ? -7.13264  5.43998  20.79784 1.000 46.63598 ? 156 LEU A N   1 
ATOM   1115 C CA  . LEU A 1 161 ? -6.93985  6.83071  21.19724 1.000 40.66132 ? 156 LEU A CA  1 
ATOM   1116 C C   . LEU A 1 161 ? -8.25634  7.44430  21.65585 1.000 45.06774 ? 156 LEU A C   1 
ATOM   1117 O O   . LEU A 1 161 ? -8.32528  8.10245  22.70244 1.000 45.17949 ? 156 LEU A O   1 
ATOM   1118 C CB  . LEU A 1 161 ? -6.35274  7.62228  20.03002 1.000 35.96718 ? 156 LEU A CB  1 
ATOM   1119 C CG  . LEU A 1 161 ? -6.01600  9.09776  20.23848 1.000 40.41504 ? 156 LEU A CG  1 
ATOM   1120 C CD1 . LEU A 1 161 ? -5.02911  9.27407  21.38219 1.000 40.99534 ? 156 LEU A CD1 1 
ATOM   1121 C CD2 . LEU A 1 161 ? -5.46553  9.71080  18.94281 1.000 39.98033 ? 156 LEU A CD2 1 
ATOM   1122 N N   . LEU A 1 162 ? -9.32181  7.20146  20.89249 1.000 44.35922 ? 157 LEU A N   1 
ATOM   1123 C CA  . LEU A 1 162 ? -10.61526 7.81796  21.16463 1.000 48.49582 ? 157 LEU A CA  1 
ATOM   1124 C C   . LEU A 1 162 ? -11.16417 7.38639  22.51631 1.000 51.28919 ? 157 LEU A C   1 
ATOM   1125 O O   . LEU A 1 162 ? -11.63828 8.21969  23.29657 1.000 47.81552 ? 157 LEU A O   1 
ATOM   1126 C CB  . LEU A 1 162 ? -11.60155 7.45475  20.05546 1.000 49.76737 ? 157 LEU A CB  1 
ATOM   1127 C CG  . LEU A 1 162 ? -12.04258 8.49710  19.04308 1.000 50.81603 ? 157 LEU A CG  1 
ATOM   1128 C CD1 . LEU A 1 162 ? -13.07706 7.86568  18.11549 1.000 51.97021 ? 157 LEU A CD1 1 
ATOM   1129 C CD2 . LEU A 1 162 ? -12.62771 9.70316  19.75692 1.000 47.18072 ? 157 LEU A CD2 1 
ATOM   1130 N N   . GLN A 1 163 ? -11.13729 6.07751  22.79594 1.000 54.15470 ? 158 GLN A N   1 
ATOM   1131 C CA  . GLN A 1 163 ? -11.64517 5.57411  24.07011 1.000 59.53829 ? 158 GLN A CA  1 
ATOM   1132 C C   . GLN A 1 163 ? -10.80125 6.06114  25.23425 1.000 70.47391 ? 158 GLN A C   1 
ATOM   1133 O O   . GLN A 1 163 ? -11.31434 6.21247  26.34757 1.000 77.57783 ? 158 GLN A O   1 
ATOM   1134 C CB  . GLN A 1 163 ? -11.70599 4.04712  24.05432 1.000 57.77347 ? 158 GLN A CB  1 
ATOM   1135 C CG  . GLN A 1 163 ? -12.87260 3.48756  23.23265 1.000 58.79354 ? 158 GLN A CG  1 
ATOM   1136 N N   . GLY A 1 164 ? -9.51417  6.31390  24.99770 1.000 69.21175 ? 159 GLY A N   1 
ATOM   1137 C CA  . GLY A 1 164 ? -8.66892  6.95281  25.98746 1.000 64.17416 ? 159 GLY A CA  1 
ATOM   1138 C C   . GLY A 1 164 ? -9.07123  8.37075  26.33234 1.000 62.86392 ? 159 GLY A C   1 
ATOM   1139 O O   . GLY A 1 164 ? -8.50617  8.93926  27.27161 1.000 71.18337 ? 159 GLY A O   1 
ATOM   1140 N N   . GLN A 1 165 ? -10.02156 8.95020  25.60340 1.000 60.94317 ? 160 GLN A N   1 
ATOM   1141 C CA  . GLN A 1 165 ? -10.51180 10.29776 25.88764 1.000 58.50841 ? 160 GLN A CA  1 
ATOM   1142 C C   . GLN A 1 165 ? -11.78558 10.21805 26.71332 1.000 58.39194 ? 160 GLN A C   1 
ATOM   1143 O O   . GLN A 1 165 ? -11.82591 9.51746  27.72390 1.000 57.71850 ? 160 GLN A O   1 
ATOM   1144 C CB  . GLN A 1 165 ? -10.76811 11.08646 24.59148 1.000 53.20928 ? 160 GLN A CB  1 
ATOM   1145 C CG  . GLN A 1 165 ? -9.61888  11.06094 23.59418 1.000 46.43364 ? 160 GLN A CG  1 
ATOM   1146 C CD  . GLN A 1 165 ? -8.27714  11.38219 24.22908 1.000 50.31269 ? 160 GLN A CD  1 
ATOM   1147 O OE1 . GLN A 1 165 ? -8.09855  12.44928 24.81585 1.000 54.03657 ? 160 GLN A OE1 1 
ATOM   1148 N NE2 . GLN A 1 165 ? -7.32482  10.45423 24.11883 1.000 46.80943 ? 160 GLN A NE2 1 
HETATM 1149 O O   . HOH B 2 .   ? -0.56345  19.95816 5.64679  1.000 45.63376 ? 201 HOH A O   1 
HETATM 1150 O O   . HOH B 2 .   ? -13.64334 23.30089 1.58211  1.000 41.58270 ? 202 HOH A O   1 
HETATM 1151 O O   . HOH B 2 .   ? -33.43179 4.58306  -0.41524 1.000 44.96339 ? 203 HOH A O   1 
HETATM 1152 O O   . HOH B 2 .   ? -9.22617  3.23547  -0.44539 1.000 45.11927 ? 204 HOH A O   1 
HETATM 1153 O O   . HOH B 2 .   ? -19.57167 21.30456 2.41967  1.000 40.69676 ? 205 HOH A O   1 
HETATM 1154 O O   . HOH B 2 .   ? -17.27651 13.41557 0.59933  1.000 35.55721 ? 206 HOH A O   1 
HETATM 1155 O O   . HOH B 2 .   ? 0.80420   18.79372 11.35168 1.000 45.64699 ? 207 HOH A O   1 
HETATM 1156 O O   . HOH B 2 .   ? -14.64510 23.43278 4.21232  1.000 44.40471 ? 208 HOH A O   1 
HETATM 1157 O O   . HOH B 2 .   ? 4.34978   24.09318 17.55312 1.000 29.41131 ? 209 HOH A O   1 
HETATM 1158 O O   . HOH B 2 .   ? -15.81820 17.06723 6.82259  1.000 43.11732 ? 210 HOH A O   1 
HETATM 1159 O O   . HOH B 2 .   ? -17.34364 10.78369 -5.79043 1.000 41.15854 ? 211 HOH A O   1 
HETATM 1160 O O   . HOH B 2 .   ? -19.36174 9.32589  6.76310  1.000 34.05715 ? 212 HOH A O   1 
HETATM 1161 O O   . HOH B 2 .   ? 2.10418   17.98333 9.34679  1.000 38.52758 ? 213 HOH A O   1 
HETATM 1162 O O   . HOH B 2 .   ? 9.16395   27.47777 30.66717 1.000 49.10126 ? 214 HOH A O   1 
HETATM 1163 O O   . HOH B 2 .   ? -17.00667 8.68487  7.81042  1.000 40.05609 ? 215 HOH A O   1 
HETATM 1164 O O   . HOH B 2 .   ? 11.29409  15.62971 13.89689 1.000 47.59444 ? 216 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 6   ? 0.60859 0.93355 0.79688 -0.01660 0.11421  -0.17427 1   MET A N   
2    C CA  . MET A 6   ? 0.61157 0.86807 0.78707 -0.00015 0.09708  -0.13881 1   MET A CA  
3    C C   . MET A 6   ? 0.62024 0.84637 0.74543 -0.01551 0.08962  -0.11154 1   MET A C   
4    O O   . MET A 6   ? 0.63335 0.88573 0.72715 -0.04224 0.08991  -0.10036 1   MET A O   
5    C CB  . MET A 6   ? 0.61459 0.86772 0.79271 0.00381  0.08718  -0.11798 1   MET A CB  
6    C CG  . MET A 6   ? 0.68646 0.95190 0.91996 0.02674  0.08724  -0.13374 1   MET A CG  
7    S SD  . MET A 6   ? 0.74644 0.99444 0.97811 0.03457  0.07071  -0.10152 1   MET A SD  
8    C CE  . MET A 6   ? 0.69943 0.96422 1.00622 0.06249  0.06882  -0.11892 1   MET A CE  
9    N N   . ASP A 7   ? 0.59706 0.77053 0.71877 0.00034  0.08117  -0.09856 2   ASP A N   
10   C CA  . ASP A 7   ? 0.48082 0.62352 0.56348 -0.01000 0.07298  -0.07522 2   ASP A CA  
11   C C   . ASP A 7   ? 0.45817 0.57187 0.52624 -0.00877 0.05819  -0.04631 2   ASP A C   
12   O O   . ASP A 7   ? 0.51707 0.64064 0.59868 -0.00448 0.05538  -0.04373 2   ASP A O   
13   C CB  . ASP A 7   ? 0.45473 0.56439 0.54280 0.00374  0.07334  -0.08121 2   ASP A CB  
14   C CG  . ASP A 7   ? 0.48608 0.56073 0.60105 0.02900  0.06547  -0.07420 2   ASP A CG  
15   O OD1 . ASP A 7   ? 0.44838 0.53202 0.58601 0.03813  0.06226  -0.07206 2   ASP A OD1 
16   O OD2 . ASP A 7   ? 0.54651 0.58919 0.66059 0.03757  0.06151  -0.06862 2   ASP A OD2 
17   N N   . ARG A 8   ? 0.45936 0.54067 0.50373 -0.01294 0.04856  -0.02768 3   ARG A N   
18   C CA  . ARG A 8   ? 0.49922 0.55611 0.53731 -0.01186 0.03504  -0.00856 3   ARG A CA  
19   C C   . ARG A 8   ? 0.45018 0.49659 0.50597 0.00826  0.03209  -0.01024 3   ARG A C   
20   O O   . ARG A 8   ? 0.44527 0.49970 0.50715 0.00760  0.02665  -0.00538 3   ARG A O   
21   C CB  . ARG A 8   ? 0.53307 0.55782 0.55441 -0.01469 0.02584  0.00423  3   ARG A CB  
22   C CG  . ARG A 8   ? 0.53380 0.56942 0.53987 -0.03781 0.02254  0.01586  3   ARG A CG  
23   C CD  . ARG A 8   ? 0.61643 0.62090 0.61390 -0.03755 0.01256  0.02726  3   ARG A CD  
24   N NE  . ARG A 8   ? 0.66900 0.68496 0.65868 -0.06185 0.00339  0.04717  3   ARG A NE  
25   C CZ  . ARG A 8   ? 0.68912 0.69667 0.68998 -0.07403 -0.01242 0.06710  3   ARG A CZ  
26   N NH1 . ARG A 8   ? 0.60062 0.58979 0.61899 -0.06337 -0.01823 0.06300  3   ARG A NH1 
27   N NH2 . ARG A 8   ? 0.70528 0.72555 0.70358 -0.09868 -0.02395 0.09200  3   ARG A NH2 
28   N N   . ALA A 9   ? 0.40802 0.43989 0.47385 0.02390  0.03422  -0.01491 4   ALA A N   
29   C CA  . ALA A 9   ? 0.45141 0.47579 0.53216 0.03901  0.02741  -0.00768 4   ALA A CA  
30   C C   . ALA A 9   ? 0.40266 0.45353 0.51159 0.04539  0.02845  -0.01173 4   ALA A C   
31   O O   . ALA A 9   ? 0.40121 0.45973 0.51434 0.04824  0.02036  -0.00167 4   ALA A O   
32   C CB  . ALA A 9   ? 0.43112 0.43565 0.52056 0.05047  0.02727  -0.00652 4   ALA A CB  
33   N N   . ALA A 10  ? 0.43108 0.50209 0.56240 0.04693  0.03841  -0.02922 5   ALA A N   
34   C CA  . ALA A 10  ? 0.35771 0.45671 0.52381 0.05476  0.03901  -0.03573 5   ALA A CA  
35   C C   . ALA A 10  ? 0.37080 0.49406 0.52277 0.04097  0.03842  -0.03268 5   ALA A C   
36   O O   . ALA A 10  ? 0.38100 0.52047 0.55038 0.04634  0.03282  -0.02737 5   ALA A O   
37   C CB  . ALA A 10  ? 0.42929 0.54959 0.63132 0.06016  0.05098  -0.06351 5   ALA A CB  
38   N N   . HIS A 11  ? 0.45602 0.58464 0.57974 0.02133  0.04261  -0.03369 6   HIS A N   
39   C CA  . HIS A 11  ? 0.47027 0.61879 0.58424 0.00519  0.03962  -0.02711 6   HIS A CA  
40   C C   . HIS A 11  ? 0.44842 0.57670 0.55475 0.00765  0.02654  -0.01186 6   HIS A C   
41   O O   . HIS A 11  ? 0.38631 0.53371 0.50104 0.00404  0.02265  -0.00987 6   HIS A O   
42   C CB  . HIS A 11  ? 0.54473 0.70084 0.63371 -0.01934 0.04206  -0.02295 6   HIS A CB  
43   C CG  . HIS A 11  ? 0.63817 0.80874 0.72053 -0.03935 0.03539  -0.01039 6   HIS A CG  
44   N ND1 . HIS A 11  ? 0.67095 0.88489 0.76636 -0.04825 0.04093  -0.01743 6   HIS A ND1 
45   C CD2 . HIS A 11  ? 0.66979 0.81717 0.74040 -0.05262 0.02250  0.00789  6   HIS A CD2 
46   C CE1 . HIS A 11  ? 0.68288 0.89876 0.77109 -0.06791 0.03161  -0.00126 6   HIS A CE1 
47   N NE2 . HIS A 11  ? 0.67989 0.85377 0.75638 -0.07038 0.01962  0.01387  6   HIS A NE2 
48   N N   . ALA A 12  ? 0.38359 0.47918 0.47595 0.01280  0.02037  -0.00456 7   ALA A N   
49   C CA  . ALA A 12  ? 0.43741 0.52295 0.52452 0.01310  0.00957  0.00223  7   ALA A CA  
50   C C   . ALA A 12  ? 0.46438 0.56865 0.56797 0.02553  0.00557  0.00511  7   ALA A C   
51   O O   . ALA A 12  ? 0.41644 0.53668 0.52195 0.02095  -0.00097 0.00602  7   ALA A O   
52   C CB  . ALA A 12  ? 0.44681 0.50174 0.51854 0.01514  0.00547  0.00489  7   ALA A CB  
53   N N   . VAL A 13  ? 0.41309 0.51710 0.53246 0.03988  0.00746  0.00788  8   VAL A N   
54   C CA  . VAL A 13  ? 0.43390 0.55892 0.57638 0.05017  -0.00001 0.01796  8   VAL A CA  
55   C C   . VAL A 13  ? 0.46089 0.61826 0.62322 0.04831  0.00107  0.01310  8   VAL A C   
56   O O   . VAL A 13  ? 0.49993 0.68157 0.66917 0.04754  -0.00736 0.02126  8   VAL A O   
57   C CB  . VAL A 13  ? 0.45557 0.56960 0.62354 0.06522  -0.00090 0.02422  8   VAL A CB  
58   C CG1 . VAL A 13  ? 0.49313 0.63207 0.69996 0.07573  -0.01098 0.03807  8   VAL A CG1 
59   C CG2 . VAL A 13  ? 0.50129 0.59155 0.64918 0.06503  -0.00521 0.03451  8   VAL A CG2 
60   N N   . GLU A 14  ? 0.41890 0.58435 0.59009 0.04527  0.01173  -0.00132 9   GLU A N   
61   C CA  . GLU A 14  ? 0.44916 0.65085 0.63917 0.04137  0.01421  -0.00830 9   GLU A CA  
62   C C   . GLU A 14  ? 0.44843 0.65931 0.61855 0.02575  0.00833  -0.00346 9   GLU A C   
63   O O   . GLU A 14  ? 0.39109 0.63022 0.57598 0.02621  0.00285  -0.00045 9   GLU A O   
64   C CB  . GLU A 14  ? 0.50482 0.72252 0.70041 0.03411  0.02826  -0.02729 9   GLU A CB  
65   C CG  . GLU A 14  ? 0.63296 0.89494 0.86420 0.03725  0.03326  -0.04062 9   GLU A CG  
66   C CD  . GLU A 14  ? 0.70450 0.97140 0.98664 0.06158  0.03044  -0.04560 9   GLU A CD  
67   O OE1 . GLU A 14  ? 0.71079 0.94792 1.00045 0.07305  0.02875  -0.04360 9   GLU A OE1 
68   O OE2 . GLU A 14  ? 0.73113 1.03146 1.05076 0.06889  0.02824  -0.05024 9   GLU A OE2 
69   N N   . GLN A 15  ? 0.42419 0.61192 0.56652 0.01165  0.00795  -0.00318 10  GLN A N   
70   C CA  . GLN A 15  ? 0.39804 0.58948 0.53177 -0.00316 0.00071  -0.00222 10  GLN A CA  
71   C C   . GLN A 15  ? 0.37767 0.57670 0.51240 0.00265  -0.00881 0.00037  10  GLN A C   
72   O O   . GLN A 15  ? 0.50967 0.73505 0.65191 -0.00421 -0.01379 -0.00213 10  GLN A O   
73   C CB  . GLN A 15  ? 0.39673 0.55742 0.51290 -0.01735 -0.00126 -0.00102 10  GLN A CB  
74   C CG  . GLN A 15  ? 0.41602 0.58277 0.52793 -0.03163 0.00577  0.00124  10  GLN A CG  
75   C CD  . GLN A 15  ? 0.46733 0.60882 0.56977 -0.05016 -0.00221 0.01070  10  GLN A CD  
76   O OE1 . GLN A 15  ? 0.47296 0.58188 0.56975 -0.04530 -0.00819 0.01198  10  GLN A OE1 
77   N NE2 . GLN A 15  ? 0.41047 0.56946 0.51582 -0.07265 -0.00403 0.01908  10  GLN A NE2 
78   N N   . TRP A 16  ? 0.38024 0.56350 0.50701 0.01260  -0.01140 0.00512  11  TRP A N   
79   C CA  . TRP A 16  ? 0.43570 0.63896 0.56015 0.01335  -0.02023 0.00819  11  TRP A CA  
80   C C   . TRP A 16  ? 0.45674 0.70005 0.60125 0.01887  -0.02550 0.01926  11  TRP A C   
81   O O   . TRP A 16  ? 0.44329 0.72043 0.58836 0.01078  -0.03234 0.01783  11  TRP A O   
82   C CB  . TRP A 16  ? 0.38271 0.56880 0.49533 0.02045  -0.02177 0.01457  11  TRP A CB  
83   C CG  . TRP A 16  ? 0.33335 0.49588 0.42926 0.01312  -0.02153 0.00109  11  TRP A CG  
84   C CD1 . TRP A 16  ? 0.33410 0.46102 0.41980 0.01655  -0.01762 0.00058  11  TRP A CD1 
85   C CD2 . TRP A 16  ? 0.28598 0.46141 0.38120 0.00173  -0.02626 -0.01681 11  TRP A CD2 
86   N NE1 . TRP A 16  ? 0.39460 0.51056 0.47560 0.00927  -0.02072 -0.01430 11  TRP A NE1 
87   C CE2 . TRP A 16  ? 0.34759 0.49216 0.43728 0.00057  -0.02579 -0.02756 11  TRP A CE2 
88   C CE3 . TRP A 16  ? 0.38429 0.59683 0.48776 -0.00784 -0.03114 -0.02783 11  TRP A CE3 
89   C CZ2 . TRP A 16  ? 0.36620 0.51413 0.46538 -0.00800 -0.03042 -0.05131 11  TRP A CZ2 
90   C CZ3 . TRP A 16  ? 0.33828 0.55552 0.44770 -0.01804 -0.03455 -0.05357 11  TRP A CZ3 
91   C CH2 . TRP A 16  ? 0.33675 0.52100 0.44731 -0.01714 -0.03435 -0.06619 11  TRP A CH2 
92   N N   . ARG A 17  ? 0.47911 0.72190 0.64562 0.03251  -0.02346 0.02887  12  ARG A N   
93   C CA  . ARG A 17  ? 0.54928 0.82892 0.74633 0.03967  -0.03094 0.04111  12  ARG A CA  
94   C C   . ARG A 17  ? 0.52135 0.83125 0.72316 0.02934  -0.02989 0.03100  12  ARG A C   
95   O O   . ARG A 17  ? 0.55057 0.89966 0.76417 0.02710  -0.03938 0.03988  12  ARG A O   
96   C CB  . ARG A 17  ? 0.56852 0.83883 0.80167 0.05705  -0.02800 0.04433  12  ARG A CB  
97   C CG  . ARG A 17  ? 0.65468 0.90725 0.89998 0.06829  -0.03607 0.06333  12  ARG A CG  
98   C CD  . ARG A 17  ? 0.76318 0.99832 1.04980 0.08488  -0.03122 0.05664  12  ARG A CD  
99   N NE  . ARG A 17  ? 0.84953 1.06383 1.15434 0.09432  -0.04099 0.07660  12  ARG A NE  
100  C CZ  . ARG A 17  ? 0.86992 1.05753 1.20509 0.10664  -0.03634 0.06731  12  ARG A CZ  
101  N NH1 . ARG A 17  ? 0.81307 0.99870 1.16058 0.11014  -0.02051 0.03546  12  ARG A NH1 
102  N NH2 . ARG A 17  ? 0.91098 1.07881 1.26513 0.11285  -0.04760 0.08888  12  ARG A NH2 
103  N N   . SER A 18  ? 0.48690 0.78298 0.67952 0.02013  -0.01974 0.01499  13  SER A N   
104  C CA  . SER A 18  ? 0.42969 0.75301 0.62649 0.00660  -0.01918 0.00665  13  SER A CA  
105  C C   . SER A 18  ? 0.45176 0.78297 0.63236 -0.00798 -0.02680 0.00155  13  SER A C   
106  O O   . SER A 18  ? 0.49489 0.86390 0.68498 -0.01466 -0.03246 0.00033  13  SER A O   
107  C CB  . SER A 18  ? 0.44451 0.75485 0.63583 -0.00418 -0.00835 -0.00374 13  SER A CB  
108  O OG  . SER A 18  ? 0.53626 0.86550 0.72703 -0.02285 -0.00989 -0.00893 13  SER A OG  
109  N N   . GLU A 19  ? 0.42572 0.72540 0.58633 -0.01298 -0.02723 -0.00486 14  GLU A N   
110  C CA  . GLU A 19  ? 0.37028 0.67642 0.52528 -0.02769 -0.03302 -0.01992 14  GLU A CA  
111  C C   . GLU A 19  ? 0.44715 0.78935 0.59760 -0.02718 -0.04043 -0.02042 14  GLU A C   
112  O O   . GLU A 19  ? 0.51481 0.88910 0.66891 -0.04010 -0.04525 -0.03537 14  GLU A O   
113  C CB  . GLU A 19  ? 0.40035 0.66125 0.54664 -0.03335 -0.03190 -0.02999 14  GLU A CB  
114  C CG  . GLU A 19  ? 0.45803 0.69566 0.61080 -0.04562 -0.02992 -0.02924 14  GLU A CG  
115  C CD  . GLU A 19  ? 0.51627 0.77406 0.68578 -0.06294 -0.03549 -0.03892 14  GLU A CD  
116  O OE1 . GLU A 19  ? 0.45741 0.73038 0.63487 -0.06806 -0.04179 -0.05641 14  GLU A OE1 
117  O OE2 . GLU A 19  ? 0.49602 0.75957 0.67196 -0.07337 -0.03323 -0.03097 14  GLU A OE2 
118  N N   . ARG A 20  ? 0.44780 0.78979 0.59137 -0.01549 -0.04198 -0.00464 15  ARG A N   
119  C CA  . ARG A 20  ? 0.46616 0.84964 0.60195 -0.01932 -0.05007 0.00092  15  ARG A CA  
120  C C   . ARG A 20  ? 0.48703 0.89153 0.63629 -0.00775 -0.05719 0.03350  15  ARG A C   
121  O O   . ARG A 20  ? 0.46857 0.86358 0.61416 -0.00067 -0.06035 0.05130  15  ARG A O   
122  C CB  . ARG A 20  ? 0.43560 0.80021 0.55335 -0.02065 -0.04814 -0.00888 15  ARG A CB  
123  C CG  . ARG A 20  ? 0.35340 0.70556 0.47006 -0.03201 -0.04528 -0.04366 15  ARG A CG  
124  C CD  . ARG A 20  ? 0.36898 0.77781 0.49164 -0.04829 -0.05012 -0.06545 15  ARG A CD  
125  N NE  . ARG A 20  ? 0.46604 0.93528 0.57547 -0.05518 -0.05522 -0.05965 15  ARG A NE  
126  C CZ  . ARG A 20  ? 0.50193 0.99333 0.60188 -0.06322 -0.05405 -0.08111 15  ARG A CZ  
127  N NH1 . ARG A 20  ? 0.48596 0.93753 0.59393 -0.06171 -0.04873 -0.11134 15  ARG A NH1 
128  N NH2 . ARG A 20  ? 0.49260 1.05124 0.57803 -0.07419 -0.05934 -0.07099 15  ARG A NH2 
129  N N   . PRO A 21  ? 0.51449 0.94784 0.68568 -0.00574 -0.06159 0.04318  16  PRO A N   
130  C CA  . PRO A 21  ? 0.51321 0.96509 0.71132 0.00700  -0.07190 0.07539  16  PRO A CA  
131  C C   . PRO A 21  ? 0.52614 1.02128 0.71762 -0.00096 -0.08656 0.10052  16  PRO A C   
132  O O   . PRO A 21  ? 0.56463 1.06562 0.78112 0.00876  -0.09849 0.13402  16  PRO A O   
133  C CB  . PRO A 21  ? 0.53460 1.01828 0.75868 0.00736  -0.07433 0.07486  16  PRO A CB  
134  C CG  . PRO A 21  ? 0.54449 1.04712 0.74748 -0.01191 -0.07022 0.04852  16  PRO A CG  
135  C CD  . PRO A 21  ? 0.51270 0.96764 0.69063 -0.01623 -0.05974 0.02612  16  PRO A CD  
136  N N   . ASP A 22  ? 0.50378 1.03334 0.66661 -0.02019 -0.08689 0.08468  17  ASP A N   
137  C CA  . ASP A 22  ? 0.52391 1.10458 0.67283 -0.03364 -0.09864 0.10495  17  ASP A CA  
138  C C   . ASP A 22  ? 0.58612 1.13162 0.72317 -0.02814 -0.09673 0.11560  17  ASP A C   
139  O O   . ASP A 22  ? 0.56295 1.15080 0.69083 -0.03996 -0.10776 0.14029  17  ASP A O   
140  C CB  . ASP A 22  ? 0.49721 1.13121 0.62160 -0.05720 -0.09601 0.07263  17  ASP A CB  
141  C CG  . ASP A 22  ? 0.53151 1.12079 0.64049 -0.05798 -0.08059 0.02838  17  ASP A CG  
142  O OD1 . ASP A 22  ? 0.51457 1.05123 0.63352 -0.04855 -0.07178 0.01126  17  ASP A OD1 
143  O OD2 . ASP A 22  ? 0.51947 1.12907 0.60982 -0.06892 -0.07845 0.01251  17  ASP A OD2 
144  N N   . LEU A 23  ? 0.54078 1.01617 0.67724 -0.01339 -0.08375 0.09925  18  LEU A N   
145  C CA  . LEU A 23  ? 0.58540 1.02258 0.71002 -0.00798 -0.07986 0.10364  18  LEU A CA  
146  C C   . LEU A 23  ? 0.54864 0.94904 0.70323 0.01055  -0.08478 0.13320  18  LEU A C   
147  O O   . LEU A 23  ? 0.55977 0.94056 0.74268 0.02408  -0.08269 0.13230  18  LEU A O   
148  C CB  . LEU A 23  ? 0.66338 1.04869 0.77203 -0.00469 -0.06393 0.06699  18  LEU A CB  
149  C CG  . LEU A 23  ? 0.66661 1.06252 0.75145 -0.01788 -0.05851 0.03626  18  LEU A CG  
150  C CD1 . LEU A 23  ? 0.61747 0.94805 0.69885 -0.00884 -0.04753 0.01634  18  LEU A CD1 
151  C CD2 . LEU A 23  ? 0.68435 1.12048 0.75424 -0.02799 -0.06498 0.05150  18  LEU A CD2 
152  N N   . ASP A 24  ? 0.47819 0.87089 0.63041 0.01035  -0.09078 0.15566  19  ASP A N   
153  C CA  . ASP A 24  ? 0.49507 0.83914 0.67837 0.02857  -0.09234 0.17247  19  ASP A CA  
154  C C   . ASP A 24  ? 0.47758 0.76997 0.63738 0.03280  -0.07703 0.14838  19  ASP A C   
155  O O   . ASP A 24  ? 0.42554 0.72155 0.56391 0.02403  -0.07856 0.15503  19  ASP A O   
156  C CB  . ASP A 24  ? 0.59866 0.96522 0.80697 0.02540  -0.11322 0.22043  19  ASP A CB  
157  C CG  . ASP A 24  ? 0.73699 1.05373 0.99461 0.04594  -0.11735 0.23466  19  ASP A CG  
158  O OD1 . ASP A 24  ? 0.82434 1.10547 1.10046 0.06232  -0.10461 0.20697  19  ASP A OD1 
159  O OD2 . ASP A 24  ? 0.79944 1.11589 1.07986 0.04389  -0.13336 0.27167  19  ASP A OD2 
160  N N   . PRO A 25  ? 0.49589 0.74649 0.65818 0.04351  -0.06274 0.12142  20  PRO A N   
161  C CA  . PRO A 25  ? 0.46969 0.67756 0.60777 0.04454  -0.04977 0.10001  20  PRO A CA  
162  C C   . PRO A 25  ? 0.49155 0.65873 0.64958 0.05747  -0.04744 0.10710  20  PRO A C   
163  O O   . PRO A 25  ? 0.54203 0.67389 0.68617 0.05999  -0.03564 0.08780  20  PRO A O   
164  C CB  . PRO A 25  ? 0.42747 0.62272 0.55830 0.04373  -0.03827 0.07158  20  PRO A CB  
165  C CG  . PRO A 25  ? 0.44904 0.66029 0.61352 0.05166  -0.04110 0.07812  20  PRO A CG  
166  C CD  . PRO A 25  ? 0.45254 0.70424 0.63537 0.05036  -0.05790 0.10812  20  PRO A CD  
167  N N   . SER A 26  ? 0.52074 0.69425 0.71597 0.06457  -0.06022 0.13510  21  SER A N   
168  C CA  . SER A 26  ? 0.60532 0.74066 0.83468 0.07839  -0.05892 0.13675  21  SER A CA  
169  C C   . SER A 26  ? 0.57726 0.68276 0.77965 0.07442  -0.05278 0.13227  21  SER A C   
170  O O   . SER A 26  ? 0.61972 0.69055 0.82648 0.08178  -0.04130 0.11187  21  SER A O   
171  C CB  . SER A 26  ? 0.64738 0.79480 0.93117 0.08510  -0.07906 0.17254  21  SER A CB  
172  O OG  . SER A 26  ? 0.71821 0.89695 0.98628 0.06994  -0.09491 0.20797  21  SER A OG  
173  N N   . SER A 27  ? 0.46635 0.59216 0.64001 0.06088  -0.05965 0.14877  22  SER A N   
174  C CA  . SER A 27  ? 0.43388 0.53822 0.58292 0.05594  -0.05474 0.14541  22  SER A CA  
175  C C   . SER A 27  ? 0.42032 0.49486 0.54183 0.05801  -0.03739 0.10997  22  SER A C   
176  O O   . SER A 27  ? 0.45976 0.50968 0.56844 0.05738  -0.03231 0.10451  22  SER A O   
177  C CB  . SER A 27  ? 0.58490 0.73214 0.70411 0.03785  -0.06234 0.16044  22  SER A CB  
178  O OG  . SER A 27  ? 0.55752 0.73576 0.65055 0.02971  -0.05717 0.13870  22  SER A OG  
179  N N   . MET A 28  ? 0.40719 0.48575 0.52145 0.05854  -0.03006 0.08923  23  MET A N   
180  C CA  . MET A 28  ? 0.51093 0.56597 0.60210 0.05651  -0.01792 0.06322  23  MET A CA  
181  C C   . MET A 28  ? 0.46583 0.48914 0.56930 0.06425  -0.00899 0.05320  23  MET A C   
182  O O   . MET A 28  ? 0.46094 0.46423 0.54442 0.06057  -0.00172 0.04014  23  MET A O   
183  C CB  . MET A 28  ? 0.43021 0.50013 0.51594 0.05165  -0.01532 0.04894  23  MET A CB  
184  C CG  . MET A 28  ? 0.45561 0.55627 0.52656 0.04131  -0.02103 0.04576  23  MET A CG  
185  S SD  . MET A 28  ? 0.49957 0.60864 0.57159 0.03479  -0.01843 0.02695  23  MET A SD  
186  C CE  . MET A 28  ? 0.46189 0.60783 0.52306 0.02247  -0.02451 0.01384  23  MET A CE  
187  N N   . ILE A 29  ? 0.41852 0.44142 0.55902 0.07418  -0.01005 0.05699  24  ILE A N   
188  C CA  . ILE A 29  ? 0.48244 0.48588 0.63997 0.08008  0.00027  0.03858  24  ILE A CA  
189  C C   . ILE A 29  ? 0.43739 0.41469 0.58822 0.07991  0.00130  0.04034  24  ILE A C   
190  O O   . ILE A 29  ? 0.50175 0.46572 0.63069 0.07482  0.01083  0.02443  24  ILE A O   
191  C CB  . ILE A 29  ? 0.54931 0.56184 0.76100 0.09249  -0.00196 0.03617  24  ILE A CB  
192  C CG1 . ILE A 29  ? 0.54661 0.58914 0.76439 0.09187  -0.00261 0.03384  24  ILE A CG1 
193  C CG2 . ILE A 29  ? 0.51449 0.51615 0.74836 0.09707  0.01067  0.00780  24  ILE A CG2 
194  C CD1 . ILE A 29  ? 0.60589 0.65980 0.82253 0.08852  0.01171  0.00592  24  ILE A CD1 
195  N N   . VAL A 30  ? 0.38543 0.35837 0.55616 0.08324  -0.01012 0.06294  25  VAL A N   
196  C CA  . VAL A 30  ? 0.44442 0.39301 0.61581 0.08249  -0.01005 0.06582  25  VAL A CA  
197  C C   . VAL A 30  ? 0.49105 0.43652 0.61258 0.07183  -0.00589 0.06290  25  VAL A C   
198  O O   . VAL A 30  ? 0.50491 0.43120 0.61423 0.06994  0.00187  0.04937  25  VAL A O   
199  C CB  . VAL A 30  ? 0.55365 0.50140 0.76188 0.08492  -0.02668 0.09757  25  VAL A CB  
200  C CG1 . VAL A 30  ? 0.59805 0.57880 0.78787 0.07556  -0.03927 0.12645  25  VAL A CG1 
201  C CG2 . VAL A 30  ? 0.50329 0.42609 0.71396 0.08177  -0.02769 0.10257  25  VAL A CG2 
202  N N   . LEU A 31  ? 0.39748 0.36561 0.49369 0.06449  -0.01098 0.07186  26  LEU A N   
203  C CA  . LEU A 31  ? 0.44259 0.41046 0.50348 0.05615  -0.00817 0.06469  26  LEU A CA  
204  C C   . LEU A 31  ? 0.45983 0.41640 0.50325 0.05458  0.00061  0.04214  26  LEU A C   
205  O O   . LEU A 31  ? 0.42469 0.36832 0.45088 0.05094  0.00364  0.03404  26  LEU A O   
206  C CB  . LEU A 31  ? 0.41512 0.41905 0.46172 0.04736  -0.01599 0.07473  26  LEU A CB  
207  C CG  . LEU A 31  ? 0.45604 0.48277 0.51100 0.04090  -0.02725 0.10385  26  LEU A CG  
208  C CD1 . LEU A 31  ? 0.41083 0.48828 0.44517 0.02719  -0.03226 0.10636  26  LEU A CD1 
209  C CD2 . LEU A 31  ? 0.47544 0.48014 0.53014 0.03931  -0.02659 0.11046  26  LEU A CD2 
210  N N   . GLY A 32  ? 0.40199 0.36569 0.45232 0.05567  0.00306  0.03487  27  GLY A N   
211  C CA  . GLY A 32  ? 0.40597 0.36127 0.44402 0.05038  0.00893  0.02056  27  GLY A CA  
212  C C   . GLY A 32  ? 0.41228 0.35212 0.45110 0.05005  0.01696  0.01238  27  GLY A C   
213  O O   . GLY A 32  ? 0.42300 0.35394 0.44496 0.04275  0.01871  0.00769  27  GLY A O   
214  N N   . ARG A 33  ? 0.38434 0.32393 0.44790 0.05724  0.02076  0.00948  28  ARG A N   
215  C CA  . ARG A 33  ? 0.40825 0.33988 0.47660 0.05572  0.02960  -0.00523 28  ARG A CA  
216  C C   . ARG A 33  ? 0.41120 0.32337 0.46717 0.05440  0.02796  -0.00081 28  ARG A C   
217  O O   . ARG A 33  ? 0.43968 0.34808 0.48292 0.04754  0.03389  -0.01139 28  ARG A O   
218  C CB  . ARG A 33  ? 0.39513 0.33213 0.50571 0.06518  0.03351  -0.01647 28  ARG A CB  
219  C CG  . ARG A 33  ? 0.40041 0.36382 0.52314 0.06364  0.04008  -0.03119 28  ARG A CG  
220  C CD  . ARG A 33  ? 0.39372 0.36569 0.56945 0.07525  0.04359  -0.04826 28  ARG A CD  
221  N NE  . ARG A 33  ? 0.38726 0.39019 0.57523 0.07449  0.04799  -0.05897 28  ARG A NE  
222  C CZ  . ARG A 33  ? 0.44271 0.45956 0.68217 0.08677  0.04756  -0.06999 28  ARG A CZ  
223  N NH1 . ARG A 33  ? 0.40018 0.39860 0.68950 0.10117  0.04083  -0.06960 28  ARG A NH1 
224  N NH2 . ARG A 33  ? 0.37079 0.42045 0.61669 0.08403  0.05228  -0.08009 28  ARG A NH2 
225  N N   . LEU A 34  ? 0.42288 0.32905 0.48185 0.05835  0.01960  0.01582  29  LEU A N   
226  C CA  . LEU A 34  ? 0.40272 0.29566 0.44927 0.05522  0.01791  0.02080  29  LEU A CA  
227  C C   . LEU A 34  ? 0.38956 0.28182 0.40535 0.04778  0.01889  0.01528  29  LEU A C   
228  O O   . LEU A 34  ? 0.39038 0.27294 0.39644 0.04356  0.02237  0.00895  29  LEU A O   
229  C CB  . LEU A 34  ? 0.39647 0.29610 0.44835 0.05572  0.00782  0.04256  29  LEU A CB  
230  C CG  . LEU A 34  ? 0.44214 0.33742 0.47839 0.04960  0.00573  0.04890  29  LEU A CG  
231  C CD1 . LEU A 34  ? 0.52391 0.39781 0.58153 0.05089  0.00736  0.04879  29  LEU A CD1 
232  C CD2 . LEU A 34  ? 0.49552 0.41606 0.52723 0.04387  -0.00384 0.06943  29  LEU A CD2 
233  N N   . GLN A 35  ? 0.37966 0.28308 0.38552 0.04587  0.01433  0.01713  30  GLN A N   
234  C CA  . GLN A 35  ? 0.45419 0.35450 0.44470 0.04042  0.01156  0.01216  30  GLN A CA  
235  C C   . GLN A 35  ? 0.40701 0.30248 0.39282 0.03355  0.01427  0.00766  30  GLN A C   
236  O O   . GLN A 35  ? 0.38396 0.27258 0.36142 0.02807  0.01185  0.00760  30  GLN A O   
237  C CB  . GLN A 35  ? 0.51461 0.42943 0.50652 0.04005  0.00502  0.01025  30  GLN A CB  
238  C CG  . GLN A 35  ? 0.71770 0.65325 0.71071 0.04148  0.00212  0.01587  30  GLN A CG  
239  C CD  . GLN A 35  ? 0.86393 0.82492 0.85918 0.03857  -0.00277 0.00645  30  GLN A CD  
240  O OE1 . GLN A 35  ? 0.92629 0.89580 0.92161 0.03623  -0.00503 -0.00712 30  GLN A OE1 
241  N NE2 . GLN A 35  ? 0.84182 0.81871 0.84345 0.03861  -0.00437 0.01010  30  GLN A NE2 
242  N N   . GLU A 36  ? 0.41236 0.31742 0.40452 0.03162  0.01828  0.00546  31  GLU A N   
243  C CA  . GLU A 36  ? 0.47371 0.38664 0.45898 0.01966  0.02094  0.00347  31  GLU A CA  
244  C C   . GLU A 36  ? 0.41427 0.32839 0.39438 0.01550  0.02851  -0.00453 31  GLU A C   
245  O O   . GLU A 36  ? 0.43158 0.35195 0.39884 0.00299  0.02682  -0.00144 31  GLU A O   
246  C CB  . GLU A 36  ? 0.50015 0.43276 0.49397 0.01644  0.02526  -0.00006 31  GLU A CB  
247  C CG  . GLU A 36  ? 0.54691 0.50080 0.53167 -0.00147 0.02781  0.00022  31  GLU A CG  
248  C CD  . GLU A 36  ? 0.61041 0.55915 0.58876 -0.01362 0.01456  0.01790  31  GLU A CD  
249  O OE1 . GLU A 36  ? 0.52885 0.45583 0.51319 -0.00588 0.00484  0.02283  31  GLU A OE1 
250  O OE2 . GLU A 36  ? 0.52246 0.49311 0.49447 -0.03252 0.01290  0.02644  31  GLU A OE2 
251  N N   . ALA A 37  ? 0.37227 0.28254 0.36661 0.02439  0.03527  -0.01407 32  ALA A N   
252  C CA  . ALA A 37  ? 0.37142 0.28386 0.36686 0.01997  0.04291  -0.02741 32  ALA A CA  
253  C C   . ALA A 37  ? 0.46451 0.36275 0.44329 0.01686  0.03791  -0.01983 32  ALA A C   
254  O O   . ALA A 37  ? 0.37585 0.28397 0.34285 0.00560  0.04059  -0.02503 32  ALA A O   
255  C CB  . ALA A 37  ? 0.34397 0.25014 0.37131 0.03116  0.04825  -0.03968 32  ALA A CB  
256  N N   . ALA A 38  ? 0.40524 0.28750 0.38339 0.02497  0.03066  -0.00855 33  ALA A N   
257  C CA  . ALA A 38  ? 0.39800 0.27195 0.36389 0.02237  0.02620  -0.00413 33  ALA A CA  
258  C C   . ALA A 38  ? 0.40939 0.28908 0.36354 0.01317  0.01948  0.00153  33  ALA A C   
259  O O   . ALA A 38  ? 0.42286 0.30429 0.36848 0.00580  0.01792  0.00235  33  ALA A O   
260  C CB  . ALA A 38  ? 0.35332 0.22210 0.32171 0.02988  0.02033  0.00381  33  ALA A CB  
261  N N   . LEU A 39  ? 0.40056 0.28386 0.35847 0.01234  0.01349  0.00764  34  LEU A N   
262  C CA  . LEU A 39  ? 0.45425 0.33933 0.41222 0.00304  0.00230  0.01841  34  LEU A CA  
263  C C   . LEU A 39  ? 0.48357 0.38777 0.43032 -0.01419 0.00408  0.02371  34  LEU A C   
264  O O   . LEU A 39  ? 0.47848 0.38654 0.42138 -0.02397 -0.00419 0.03429  34  LEU A O   
265  C CB  . LEU A 39  ? 0.51586 0.39972 0.48693 0.00475  -0.00509 0.02270  34  LEU A CB  
266  C CG  . LEU A 39  ? 0.60508 0.48704 0.58884 -0.00571 -0.02052 0.03737  34  LEU A CG  
267  C CD1 . LEU A 39  ? 0.60440 0.47325 0.60370 -0.00055 -0.03189 0.03752  34  LEU A CD1 
268  C CD2 . LEU A 39  ? 0.55900 0.44055 0.55886 -0.00612 -0.02636 0.03928  34  LEU A CD2 
269  N N   . VAL A 40  ? 0.44943 0.37282 0.39297 -0.01977 0.01428  0.01594  35  VAL A N   
270  C CA  . VAL A 40  ? 0.41200 0.36900 0.34360 -0.04094 0.01718  0.01799  35  VAL A CA  
271  C C   . VAL A 40  ? 0.47807 0.44517 0.39937 -0.04681 0.02351  0.00750  35  VAL A C   
272  O O   . VAL A 40  ? 0.46253 0.45509 0.37102 -0.06637 0.01845  0.01807  35  VAL A O   
273  C CB  . VAL A 40  ? 0.44193 0.42547 0.37705 -0.04499 0.02917  0.00392  35  VAL A CB  
274  C CG1 . VAL A 40  ? 0.54420 0.57760 0.46548 -0.07047 0.03542  -0.00073 35  VAL A CG1 
275  C CG2 . VAL A 40  ? 0.46667 0.44443 0.41034 -0.04320 0.02132  0.01708  35  VAL A CG2 
276  N N   . ILE A 41  ? 0.43161 0.38157 0.36049 -0.03219 0.03296  -0.01105 36  ILE A N   
277  C CA  . ILE A 41  ? 0.43842 0.39594 0.36201 -0.03767 0.03939  -0.02448 36  ILE A CA  
278  C C   . ILE A 41  ? 0.45756 0.40485 0.37093 -0.04098 0.02714  -0.00680 36  ILE A C   
279  O O   . ILE A 41  ? 0.52400 0.49476 0.42509 -0.05698 0.02607  -0.00554 36  ILE A O   
280  C CB  . ILE A 41  ? 0.44795 0.38470 0.39102 -0.02186 0.04887  -0.04409 36  ILE A CB  
281  C CG1 . ILE A 41  ? 0.48022 0.43467 0.44338 -0.02028 0.06064  -0.06669 36  ILE A CG1 
282  C CG2 . ILE A 41  ? 0.38940 0.32543 0.33072 -0.02646 0.05277  -0.05578 36  ILE A CG2 
283  C CD1 . ILE A 41  ? 0.52525 0.45536 0.52132 -0.00346 0.06503  -0.08028 36  ILE A CD1 
284  N N   . ALA A 42  ? 0.47361 0.39199 0.39472 -0.02691 0.01754  0.00493  37  ALA A N   
285  C CA  . ALA A 42  ? 0.49782 0.40942 0.41857 -0.02823 0.00483  0.01844  37  ALA A CA  
286  C C   . ALA A 42  ? 0.51530 0.44542 0.43473 -0.04506 -0.00904 0.04023  37  ALA A C   
287  O O   . ALA A 42  ? 0.48106 0.42857 0.39317 -0.05846 -0.01509 0.04943  37  ALA A O   
288  C CB  . ALA A 42  ? 0.52505 0.41263 0.46043 -0.01126 -0.00178 0.01997  37  ALA A CB  
289  N N   . ARG A 43  ? 0.43548 0.36532 0.36360 -0.04710 -0.01568 0.05158  38  ARG A N   
290  C CA  . ARG A 43  ? 0.48532 0.42818 0.42110 -0.06403 -0.03418 0.08002  38  ARG A CA  
291  C C   . ARG A 43  ? 0.48937 0.47772 0.40324 -0.09132 -0.03183 0.08907  38  ARG A C   
292  O O   . ARG A 43  ? 0.49456 0.50030 0.40979 -0.10822 -0.04800 0.11462  38  ARG A O   
293  C CB  . ARG A 43  ? 0.49846 0.43252 0.45024 -0.06277 -0.04111 0.08920  38  ARG A CB  
294  C CG  . ARG A 43  ? 0.53575 0.48471 0.50023 -0.08474 -0.06258 0.12426  38  ARG A CG  
295  C CD  . ARG A 43  ? 0.57957 0.52178 0.56066 -0.08666 -0.06876 0.13282  38  ARG A CD  
296  N NE  . ARG A 43  ? 0.68146 0.65456 0.63821 -0.09741 -0.05175 0.12326  38  ARG A NE  
297  C CZ  . ARG A 43  ? 0.82605 0.79047 0.78555 -0.08528 -0.04096 0.10592  38  ARG A CZ  
298  N NH1 . ARG A 43  ? 0.70998 0.63916 0.69120 -0.06438 -0.04510 0.09685  38  ARG A NH1 
299  N NH2 . ARG A 43  ? 0.93962 0.93728 0.88249 -0.09540 -0.02613 0.09574  38  ARG A NH2 
300  N N   . ASP A 44  ? 0.50820 0.52244 0.40588 -0.09755 -0.01301 0.06812  39  ASP A N   
301  C CA  . ASP A 44  ? 0.57772 0.64976 0.45581 -0.12724 -0.00862 0.07085  39  ASP A CA  
302  C C   . ASP A 44  ? 0.59073 0.69009 0.45343 -0.13445 0.00582  0.04508  39  ASP A C   
303  O O   . ASP A 44  ? 0.56512 0.72240 0.41029 -0.16313 0.00771  0.04694  39  ASP A O   
304  C CB  . ASP A 44  ? 0.62400 0.72098 0.50007 -0.13310 0.00377  0.05776  39  ASP A CB  
305  C CG  . ASP A 44  ? 0.68449 0.77504 0.57142 -0.13956 -0.01246 0.08867  39  ASP A CG  
306  O OD1 . ASP A 44  ? 0.66440 0.73164 0.56545 -0.14058 -0.03479 0.12026  39  ASP A OD1 
307  O OD2 . ASP A 44  ? 0.72202 0.83153 0.60889 -0.14369 -0.00359 0.07990  39  ASP A OD2 
308  N N   . ARG A 45  ? 0.54914 0.61400 0.41908 -0.11233 0.01549  0.02125  40  ARG A N   
309  C CA  . ARG A 45  ? 0.55411 0.64239 0.41658 -0.11894 0.03021  -0.00838 40  ARG A CA  
310  C C   . ARG A 45  ? 0.52769 0.59153 0.39020 -0.11129 0.02400  -0.00435 40  ARG A C   
311  O O   . ARG A 45  ? 0.44074 0.53838 0.28998 -0.12992 0.02263  -0.00439 40  ARG A O   
312  C CB  . ARG A 45  ? 0.55576 0.63262 0.43514 -0.10316 0.04978  -0.04661 40  ARG A CB  
313  C CG  . ARG A 45  ? 0.53604 0.63990 0.42083 -0.10823 0.05799  -0.05698 40  ARG A CG  
314  C CD  . ARG A 45  ? 0.54113 0.72052 0.40913 -0.14105 0.06481  -0.06749 40  ARG A CD  
315  N NE  . ARG A 45  ? 0.57037 0.78168 0.44284 -0.14909 0.08074  -0.10862 40  ARG A NE  
316  C CZ  . ARG A 45  ? 0.66501 0.90159 0.56084 -0.14700 0.09989  -0.15528 40  ARG A CZ  
317  N NH1 . ARG A 45  ? 0.69064 0.92461 0.60491 -0.13640 0.10534  -0.16386 40  ARG A NH1 
318  N NH2 . ARG A 45  ? 0.66322 0.92888 0.56980 -0.15512 0.11315  -0.19619 40  ARG A NH2 
319  N N   . LEU A 46  ? 0.39433 0.40704 0.27118 -0.08617 0.02097  -0.00259 41  LEU A N   
320  C CA  . LEU A 46  ? 0.48186 0.47643 0.36004 -0.07938 0.01774  -0.00337 41  LEU A CA  
321  C C   . LEU A 46  ? 0.47533 0.47282 0.35363 -0.08523 -0.00269 0.02697  41  LEU A C   
322  O O   . LEU A 46  ? 0.47019 0.48767 0.34085 -0.09711 -0.00710 0.03079  41  LEU A O   
323  C CB  . LEU A 46  ? 0.42019 0.37095 0.31351 -0.05489 0.02150  -0.01131 41  LEU A CB  
324  C CG  . LEU A 46  ? 0.49834 0.43879 0.40350 -0.04623 0.03673  -0.03518 41  LEU A CG  
325  C CD1 . LEU A 46  ? 0.52167 0.42630 0.44010 -0.02725 0.03515  -0.03163 41  LEU A CD1 
326  C CD2 . LEU A 46  ? 0.55496 0.51503 0.46178 -0.05731 0.04870  -0.06141 41  LEU A CD2 
327  N N   . ASN A 47  ? 0.46311 0.44124 0.35621 -0.07672 -0.01653 0.04750  42  ASN A N   
328  C CA  . ASN A 47  ? 0.46386 0.43900 0.37308 -0.07862 -0.03897 0.07459  42  ASN A CA  
329  C C   . ASN A 47  ? 0.45542 0.47279 0.35541 -0.10646 -0.05196 0.10027  42  ASN A C   
330  O O   . ASN A 47  ? 0.47288 0.49562 0.38309 -0.11011 -0.06716 0.11658  42  ASN A O   
331  C CB  . ASN A 47  ? 0.54632 0.49373 0.48272 -0.06505 -0.05150 0.08630  42  ASN A CB  
332  C CG  . ASN A 47  ? 0.51694 0.43335 0.46383 -0.04057 -0.04261 0.06397  42  ASN A CG  
333  O OD1 . ASN A 47  ? 0.47868 0.39195 0.41391 -0.03448 -0.02960 0.04579  42  ASN A OD1 
334  N ND2 . ASN A 47  ? 0.46620 0.36419 0.43613 -0.02914 -0.05001 0.06554  42  ASN A ND2 
335  N N   . PRO A 48  ? 0.43790 0.49284 0.32041 -0.12869 -0.04813 0.10639  43  PRO A N   
336  C CA  . PRO A 48  ? 0.45778 0.56723 0.32654 -0.16107 -0.06017 0.13187  43  PRO A CA  
337  C C   . PRO A 48  ? 0.53764 0.67119 0.39024 -0.16888 -0.05293 0.11625  43  PRO A C   
338  O O   . PRO A 48  ? 0.55664 0.71399 0.41194 -0.18400 -0.07157 0.14392  43  PRO A O   
339  C CB  . PRO A 48  ? 0.53198 0.68682 0.37967 -0.18331 -0.04830 0.12606  43  PRO A CB  
340  C CG  . PRO A 48  ? 0.45004 0.56365 0.31396 -0.16284 -0.04532 0.12150  43  PRO A CG  
341  C CD  . PRO A 48  ? 0.44634 0.50391 0.32346 -0.12851 -0.03581 0.09494  43  PRO A CD  
342  N N   . LEU A 49  ? 0.53106 0.65770 0.37247 -0.15886 -0.02829 0.07386  44  LEU A N   
343  C CA  . LEU A 49  ? 0.55084 0.69977 0.38026 -0.16752 -0.02106 0.05592  44  LEU A CA  
344  C C   . LEU A 49  ? 0.56552 0.68227 0.41142 -0.15211 -0.03552 0.07042  44  LEU A C   
345  O O   . LEU A 49  ? 0.50389 0.65059 0.34478 -0.16733 -0.04582 0.08326  44  LEU A O   
346  C CB  . LEU A 49  ? 0.55671 0.69730 0.38331 -0.15851 0.00573  0.00767  44  LEU A CB  
347  C CG  . LEU A 49  ? 0.62778 0.79356 0.44584 -0.17014 0.01434  -0.01598 44  LEU A CG  
348  C CD1 . LEU A 49  ? 0.65476 0.86032 0.46809 -0.18462 0.03669  -0.05998 44  LEU A CD1 
349  C CD2 . LEU A 49  ? 0.63195 0.74634 0.46462 -0.14660 0.01642  -0.02561 44  LEU A CD2 
350  N N   . PHE A 50  ? 0.55971 0.62262 0.42661 -0.12344 -0.03653 0.06720  45  PHE A N   
351  C CA  . PHE A 50  ? 0.53373 0.57406 0.42113 -0.10909 -0.04965 0.07656  45  PHE A CA  
352  C C   . PHE A 50  ? 0.49987 0.55833 0.40593 -0.12029 -0.07788 0.11590  45  PHE A C   
353  O O   . PHE A 50  ? 0.47591 0.54384 0.39267 -0.12173 -0.08951 0.12493  45  PHE A O   
354  C CB  . PHE A 50  ? 0.48767 0.48114 0.39617 -0.08092 -0.04723 0.06656  45  PHE A CB  
355  C CG  . PHE A 50  ? 0.45864 0.43289 0.35587 -0.06999 -0.02452 0.03636  45  PHE A CG  
356  C CD1 . PHE A 50  ? 0.46940 0.45459 0.35168 -0.07771 -0.00999 0.01557  45  PHE A CD1 
357  C CD2 . PHE A 50  ? 0.42308 0.36910 0.33044 -0.05286 -0.02005 0.03043  45  PHE A CD2 
358  C CE1 . PHE A 50  ? 0.42065 0.38438 0.30391 -0.06788 0.00647  -0.00719 45  PHE A CE1 
359  C CE2 . PHE A 50  ? 0.44446 0.37434 0.34729 -0.04409 -0.00343 0.00988  45  PHE A CE2 
360  C CZ  . PHE A 50  ? 0.48754 0.42395 0.38125 -0.05123 0.00863  -0.00702 45  PHE A CZ  
361  N N   . ALA A 51  ? 0.45059 0.51399 0.36603 -0.12876 -0.09123 0.14199  46  ALA A N   
362  C CA  . ALA A 51  ? 0.55426 0.63089 0.49850 -0.14034 -0.12308 0.18633  46  ALA A CA  
363  C C   . ALA A 51  ? 0.63001 0.76550 0.55333 -0.17232 -0.13197 0.20803  46  ALA A C   
364  O O   . ALA A 51  ? 0.58396 0.73188 0.53463 -0.17991 -0.15970 0.24368  46  ALA A O   
365  C CB  . ALA A 51  ? 0.54144 0.61296 0.50053 -0.14712 -0.13579 0.21206  46  ALA A CB  
366  N N   . ARG A 52  ? 0.59658 0.77386 0.47656 -0.19277 -0.11031 0.18682  47  ARG A N   
367  C CA  . ARG A 52  ? 0.61381 0.85736 0.47052 -0.22565 -0.11559 0.19971  47  ARG A CA  
368  C C   . ARG A 52  ? 0.59567 0.83400 0.45868 -0.21670 -0.11718 0.18931  47  ARG A C   
369  O O   . ARG A 52  ? 0.52418 0.80901 0.38779 -0.23871 -0.12953 0.20927  47  ARG A O   
370  C CB  . ARG A 52  ? 0.68643 0.97834 0.50575 -0.24652 -0.08762 0.16418  47  ARG A CB  
371  C CG  . ARG A 52  ? 0.76236 1.08198 0.58514 -0.26209 -0.08624 0.17259  47  ARG A CG  
372  C CD  . ARG A 52  ? 0.91425 1.28172 0.71265 -0.27743 -0.05730 0.12630  47  ARG A CD  
373  N NE  . ARG A 52  ? 1.02398 1.44154 0.81797 -0.29607 -0.05143 0.10989  47  ARG A NE  
374  C CZ  . ARG A 52  ? 1.05751 1.48611 0.83958 -0.29463 -0.02616 0.05917  47  ARG A CZ  
375  N NH1 . ARG A 52  ? 0.99988 1.39169 0.77544 -0.27484 -0.00475 0.02029  47  ARG A NH1 
376  N NH2 . ARG A 52  ? 1.09963 1.57537 0.88323 -0.31304 -0.02269 0.04723  47  ARG A NH2 
377  N N   . TYR A 53  ? 0.57389 0.75903 0.44836 -0.18504 -0.10292 0.15682  48  TYR A N   
378  C CA  . TYR A 53  ? 0.62023 0.79833 0.50434 -0.17511 -0.10456 0.14691  48  TYR A CA  
379  C C   . TYR A 53  ? 0.63485 0.77864 0.56723 -0.15263 -0.12845 0.16880  48  TYR A C   
380  O O   . TYR A 53  ? 0.58159 0.71736 0.52833 -0.14041 -0.12959 0.15782  48  TYR A O   
381  C CB  . TYR A 53  ? 0.52083 0.67157 0.39013 -0.15933 -0.07533 0.09928  48  TYR A CB  
382  C CG  . TYR A 53  ? 0.49013 0.68098 0.32541 -0.18220 -0.05447 0.07128  48  TYR A CG  
383  C CD1 . TYR A 53  ? 0.48359 0.68131 0.30431 -0.18817 -0.03815 0.05307  48  TYR A CD1 
384  C CD2 . TYR A 53  ? 0.53988 0.76659 0.36254 -0.19861 -0.05136 0.05960  48  TYR A CD2 
385  C CE1 . TYR A 53  ? 0.62972 0.86914 0.42918 -0.20851 -0.01853 0.01940  48  TYR A CE1 
386  C CE2 . TYR A 53  ? 0.55554 0.82336 0.35402 -0.22046 -0.03177 0.02663  48  TYR A CE2 
387  C CZ  . TYR A 53  ? 0.66545 0.93984 0.45491 -0.22480 -0.01527 0.00479  48  TYR A CZ  
388  O OH  . TYR A 53  ? 0.79975 1.11878 0.57492 -0.24539 0.00487  -0.03589 48  TYR A OH  
389  N N   . GLY A 54  ? 0.59105 0.71815 0.55373 -0.14815 -0.14806 0.19736  49  GLY A N   
390  C CA  . GLY A 54  ? 0.59579 0.69097 0.61681 -0.12579 -0.17145 0.21167  49  GLY A CA  
391  C C   . GLY A 54  ? 0.49965 0.54742 0.53782 -0.09306 -0.15601 0.17441  49  GLY A C   
392  O O   . GLY A 54  ? 0.49420 0.52488 0.58012 -0.07323 -0.16923 0.17062  49  GLY A O   
393  N N   . LEU A 55  ? 0.48294 0.51470 0.48749 -0.08808 -0.12947 0.14656  50  LEU A N   
394  C CA  . LEU A 55  ? 0.46528 0.46334 0.47672 -0.06261 -0.11277 0.11253  50  LEU A CA  
395  C C   . LEU A 55  ? 0.50633 0.47872 0.52314 -0.05330 -0.10849 0.10874  50  LEU A C   
396  O O   . LEU A 55  ? 0.52605 0.50637 0.51834 -0.06747 -0.10345 0.11821  50  LEU A O   
397  C CB  . LEU A 55  ? 0.48624 0.48793 0.45697 -0.06487 -0.08556 0.08319  50  LEU A CB  
398  C CG  . LEU A 55  ? 0.50740 0.52911 0.47176 -0.07047 -0.08371 0.07578  50  LEU A CG  
399  C CD1 . LEU A 55  ? 0.47535 0.49758 0.40353 -0.07699 -0.05826 0.04965  50  LEU A CD1 
400  C CD2 . LEU A 55  ? 0.40678 0.41769 0.40764 -0.05018 -0.09065 0.06573  50  LEU A CD2 
401  N N   . GLN A 56  ? 0.51228 0.46047 0.56132 -0.03075 -0.10920 0.09115  51  GLN A N   
402  C CA  . GLN A 56  ? 0.54553 0.47239 0.59197 -0.02007 -0.09797 0.07628  51  GLN A CA  
403  C C   . GLN A 56  ? 0.51355 0.43821 0.52089 -0.01738 -0.07123 0.05123  51  GLN A C   
404  O O   . GLN A 56  ? 0.51351 0.44741 0.50874 -0.01818 -0.06307 0.04006  51  GLN A O   
405  C CB  . GLN A 56  ? 0.61969 0.53208 0.71794 0.00006  -0.10878 0.06250  51  GLN A CB  
406  C CG  . GLN A 56  ? 0.77518 0.68502 0.93074 0.00053  -0.13934 0.08552  51  GLN A CG  
407  C CD  . GLN A 56  ? 0.92549 0.82606 1.14405 0.02238  -0.14886 0.06007  51  GLN A CD  
408  O OE1 . GLN A 56  ? 0.96299 0.86589 1.17529 0.03456  -0.13110 0.02522  51  GLN A OE1 
409  N NE2 . GLN A 56  ? 0.95319 0.84805 1.23771 0.02590  -0.17817 0.07686  51  GLN A NE2 
410  N N   . PRO A 57  ? 0.57880 0.49146 0.57035 -0.01494 -0.05896 0.04412  52  PRO A N   
411  C CA  . PRO A 57  ? 0.51422 0.42349 0.47766 -0.01326 -0.03754 0.02576  52  PRO A CA  
412  C C   . PRO A 57  ? 0.57733 0.48747 0.54902 -0.00257 -0.03257 0.00921  52  PRO A C   
413  O O   . PRO A 57  ? 0.51371 0.42802 0.46789 -0.00714 -0.02166 0.00196  52  PRO A O   
414  C CB  . PRO A 57  ? 0.47288 0.37011 0.43148 -0.00943 -0.03092 0.02391  52  PRO A CB  
415  C CG  . PRO A 57  ? 0.59615 0.48751 0.58506 -0.00421 -0.04770 0.03386  52  PRO A CG  
416  C CD  . PRO A 57  ? 0.62205 0.52386 0.62588 -0.01366 -0.06552 0.05340  52  PRO A CD  
417  N N   . GLY A 58  ? 0.50801 0.41886 0.50944 0.00966  -0.04062 0.00130  53  GLY A N   
418  C CA  . GLY A 58  ? 0.46849 0.39435 0.47894 0.01634  -0.03585 -0.01709 53  GLY A CA  
419  C C   . GLY A 58  ? 0.47087 0.41080 0.48260 0.01133  -0.03884 -0.01671 53  GLY A C   
420  O O   . GLY A 58  ? 0.49195 0.44462 0.49084 0.00825  -0.02887 -0.02604 53  GLY A O   
421  N N   . GLU A 59  ? 0.42579 0.36648 0.45434 0.00828  -0.05428 -0.00257 54  GLU A N   
422  C CA  . GLU A 59  ? 0.38133 0.33915 0.41332 0.00284  -0.05917 -0.00046 54  GLU A CA  
423  C C   . GLU A 59  ? 0.41769 0.37802 0.40782 -0.01221 -0.04537 0.00252  54  GLU A C   
424  O O   . GLU A 59  ? 0.39605 0.37029 0.38051 -0.01631 -0.04048 -0.00526 54  GLU A O   
425  C CB  . GLU A 59  ? 0.39559 0.35677 0.45859 0.00072  -0.08251 0.02052  54  GLU A CB  
426  C CG  . GLU A 59  ? 0.37391 0.33132 0.49644 0.01694  -0.10010 0.01429  54  GLU A CG  
427  C CD  . GLU A 59  ? 0.47947 0.43482 0.63971 0.01278  -0.12776 0.04426  54  GLU A CD  
428  O OE1 . GLU A 59  ? 0.46981 0.42878 0.60029 -0.00542 -0.13147 0.07264  54  GLU A OE1 
429  O OE2 . GLU A 59  ? 0.43386 0.38819 0.65749 0.02622  -0.14670 0.03915  54  GLU A OE2 
430  N N   . PHE A 60  ? 0.41584 0.36572 0.38107 -0.02124 -0.03896 0.01060  55  PHE A N   
431  C CA  . PHE A 60  ? 0.40586 0.35778 0.34133 -0.03406 -0.02438 0.00455  55  PHE A CA  
432  C C   . PHE A 60  ? 0.39678 0.34104 0.32724 -0.02986 -0.01118 -0.00946 55  PHE A C   
433  O O   . PHE A 60  ? 0.38357 0.33400 0.30522 -0.03868 -0.00473 -0.01548 55  PHE A O   
434  C CB  . PHE A 60  ? 0.33863 0.28472 0.25739 -0.04167 -0.01795 0.00733  55  PHE A CB  
435  C CG  . PHE A 60  ? 0.36054 0.30952 0.26067 -0.05337 -0.00262 -0.00708 55  PHE A CG  
436  C CD1 . PHE A 60  ? 0.41455 0.34363 0.31544 -0.04759 0.00987  -0.01911 55  PHE A CD1 
437  C CD2 . PHE A 60  ? 0.44661 0.42166 0.33422 -0.07147 -0.00239 -0.00896 55  PHE A CD2 
438  C CE1 . PHE A 60  ? 0.44484 0.37265 0.34259 -0.05687 0.02166  -0.03498 55  PHE A CE1 
439  C CE2 . PHE A 60  ? 0.42655 0.40660 0.30563 -0.08221 0.01218  -0.03017 55  PHE A CE2 
440  C CZ  . PHE A 60  ? 0.43163 0.38462 0.31983 -0.07370 0.02390  -0.04437 55  PHE A CZ  
441  N N   . ASP A 61  ? 0.38541 0.31948 0.32245 -0.01907 -0.00826 -0.01252 56  ASP A N   
442  C CA  . ASP A 61  ? 0.37084 0.30426 0.30351 -0.01903 0.00141  -0.01828 56  ASP A CA  
443  C C   . ASP A 61  ? 0.35694 0.31337 0.29591 -0.02176 0.00023  -0.02423 56  ASP A C   
444  O O   . ASP A 61  ? 0.36624 0.32595 0.29713 -0.03102 0.00716  -0.02411 56  ASP A O   
445  C CB  . ASP A 61  ? 0.37757 0.30804 0.31686 -0.00920 0.00192  -0.01883 56  ASP A CB  
446  C CG  . ASP A 61  ? 0.51102 0.44123 0.44344 -0.01350 0.01004  -0.01546 56  ASP A CG  
447  O OD1 . ASP A 61  ? 0.46153 0.38690 0.38844 -0.02338 0.01465  -0.01205 56  ASP A OD1 
448  O OD2 . ASP A 61  ? 0.52741 0.46396 0.46319 -0.00856 0.01017  -0.01449 56  ASP A OD2 
449  N N   . VAL A 62  ? 0.31620 0.29036 0.27562 -0.01411 -0.00953 -0.02987 57  VAL A N   
450  C CA  . VAL A 62  ? 0.30856 0.31163 0.27857 -0.01619 -0.01033 -0.03965 57  VAL A CA  
451  C C   . VAL A 62  ? 0.36645 0.37107 0.32324 -0.02894 -0.00880 -0.03487 57  VAL A C   
452  O O   . VAL A 62  ? 0.35679 0.37370 0.30548 -0.03873 -0.00184 -0.03769 57  VAL A O   
453  C CB  . VAL A 62  ? 0.36056 0.38190 0.36776 -0.00337 -0.02310 -0.05061 57  VAL A CB  
454  C CG1 . VAL A 62  ? 0.35231 0.40655 0.37378 -0.00612 -0.02474 -0.06181 57  VAL A CG1 
455  C CG2 . VAL A 62  ? 0.39748 0.42844 0.42175 0.00689  -0.02177 -0.06522 57  VAL A CG2 
456  N N   . LEU A 63  ? 0.40710 0.40381 0.36161 -0.03198 -0.01586 -0.02654 58  LEU A N   
457  C CA  . LEU A 63  ? 0.38341 0.38913 0.32535 -0.04635 -0.01446 -0.02517 58  LEU A CA  
458  C C   . LEU A 63  ? 0.43599 0.42622 0.35787 -0.05793 -0.00031 -0.02915 58  LEU A C   
459  O O   . LEU A 63  ? 0.39080 0.38966 0.30870 -0.06909 0.00434  -0.03396 58  LEU A O   
460  C CB  . LEU A 63  ? 0.35781 0.36820 0.29877 -0.05177 -0.02533 -0.01341 58  LEU A CB  
461  C CG  . LEU A 63  ? 0.33115 0.35303 0.30260 -0.04252 -0.04537 -0.00185 58  LEU A CG  
462  C CD1 . LEU A 63  ? 0.34073 0.37701 0.30453 -0.05742 -0.05701 0.01760  58  LEU A CD1 
463  C CD2 . LEU A 63  ? 0.32137 0.36533 0.31999 -0.03556 -0.05184 -0.01074 58  LEU A CD2 
464  N N   . ALA A 64  ? 0.36625 0.33330 0.28167 -0.05544 0.00547  -0.02779 59  ALA A N   
465  C CA  . ALA A 64  ? 0.40418 0.35340 0.31460 -0.06407 0.01635  -0.03295 59  ALA A CA  
466  C C   . ALA A 64  ? 0.40574 0.35470 0.32211 -0.06649 0.01943  -0.02924 59  ALA A C   
467  O O   . ALA A 64  ? 0.47988 0.42234 0.39967 -0.07851 0.02393  -0.03118 59  ALA A O   
468  C CB  . ALA A 64  ? 0.43240 0.36037 0.34276 -0.05828 0.02039  -0.03288 59  ALA A CB  
469  N N   . THR A 65  ? 0.39971 0.36029 0.31999 -0.05772 0.01638  -0.02413 60  THR A N   
470  C CA  . THR A 65  ? 0.38235 0.35627 0.30521 -0.06503 0.01860  -0.01756 60  THR A CA  
471  C C   . THR A 65  ? 0.40557 0.40451 0.32873 -0.07671 0.01840  -0.02138 60  THR A C   
472  O O   . THR A 65  ? 0.40629 0.40575 0.33069 -0.09139 0.02096  -0.01359 60  THR A O   
473  C CB  . THR A 65  ? 0.36026 0.35491 0.28647 -0.05572 0.01646  -0.01731 60  THR A CB  
474  O OG1 . THR A 65  ? 0.43408 0.40431 0.35982 -0.04651 0.01665  -0.01274 60  THR A OG1 
475  C CG2 . THR A 65  ? 0.38478 0.40851 0.31018 -0.06858 0.01841  -0.00816 60  THR A CG2 
476  N N   . LEU A 66  ? 0.40385 0.42328 0.33036 -0.07135 0.01359  -0.03125 61  LEU A N   
477  C CA  . LEU A 66  ? 0.38856 0.43537 0.31748 -0.08178 0.01293  -0.03621 61  LEU A CA  
478  C C   . LEU A 66  ? 0.48030 0.51004 0.40226 -0.09680 0.01647  -0.03567 61  LEU A C   
479  O O   . LEU A 66  ? 0.43443 0.47351 0.35739 -0.11191 0.01937  -0.03355 61  LEU A O   
480  C CB  . LEU A 66  ? 0.32430 0.39493 0.26718 -0.07098 0.00397  -0.04551 61  LEU A CB  
481  C CG  . LEU A 66  ? 0.35574 0.44905 0.31849 -0.05608 0.00009  -0.05501 61  LEU A CG  
482  C CD1 . LEU A 66  ? 0.34943 0.45178 0.33952 -0.04185 -0.01312 -0.06149 61  LEU A CD1 
483  C CD2 . LEU A 66  ? 0.35933 0.49593 0.32655 -0.06481 0.00543  -0.06393 61  LEU A CD2 
484  N N   . ARG A 67  ? 0.43248 0.44185 0.34948 -0.09510 0.01637  -0.03939 62  ARG A N   
485  C CA  . ARG A 67  ? 0.47328 0.47392 0.38768 -0.11031 0.02096  -0.04755 62  ARG A CA  
486  C C   . ARG A 67  ? 0.50328 0.47871 0.42826 -0.11974 0.02694  -0.04503 62  ARG A C   
487  O O   . ARG A 67  ? 0.50493 0.48173 0.43722 -0.13537 0.02891  -0.04896 62  ARG A O   
488  C CB  . ARG A 67  ? 0.38572 0.37949 0.29315 -0.10913 0.02133  -0.05496 62  ARG A CB  
489  C CG  . ARG A 67  ? 0.48762 0.47814 0.39650 -0.12580 0.02863  -0.07252 62  ARG A CG  
490  C CD  . ARG A 67  ? 0.50518 0.52734 0.40876 -0.14016 0.02584  -0.07882 62  ARG A CD  
491  N NE  . ARG A 67  ? 0.49562 0.51959 0.40400 -0.15824 0.03368  -0.10149 62  ARG A NE  
492  C CZ  . ARG A 67  ? 0.53602 0.53859 0.46386 -0.16702 0.03930  -0.11029 62  ARG A CZ  
493  N NH1 . ARG A 67  ? 0.47174 0.45367 0.41037 -0.16177 0.03718  -0.09235 62  ARG A NH1 
494  N NH2 . ARG A 67  ? 0.49889 0.50429 0.43901 -0.18301 0.04597  -0.13677 62  ARG A NH2 
495  N N   . ARG A 68  ? 0.45042 0.40222 0.38146 -0.11127 0.02799  -0.03673 63  ARG A N   
496  C CA  . ARG A 68  ? 0.51049 0.43540 0.46198 -0.12051 0.02980  -0.03106 63  ARG A CA  
497  C C   . ARG A 68  ? 0.47475 0.41308 0.43136 -0.13188 0.02592  -0.01077 63  ARG A C   
498  O O   . ARG A 68  ? 0.46484 0.38297 0.44414 -0.14403 0.02359  0.00046  63  ARG A O   
499  C CB  . ARG A 68  ? 0.54308 0.43977 0.50567 -0.10908 0.03044  -0.02727 63  ARG A CB  
500  C CG  . ARG A 68  ? 0.58319 0.48788 0.53726 -0.09818 0.02675  -0.00945 63  ARG A CG  
501  C CD  . ARG A 68  ? 0.63713 0.51354 0.60605 -0.08882 0.02683  -0.00541 63  ARG A CD  
502  N NE  . ARG A 68  ? 0.62595 0.51265 0.57946 -0.07444 0.02574  -0.00148 63  ARG A NE  
503  C CZ  . ARG A 68  ? 0.53539 0.43847 0.48497 -0.07274 0.02179  0.01517  63  ARG A CZ  
504  N NH1 . ARG A 68  ? 0.52468 0.43944 0.48158 -0.08653 0.01789  0.03420  63  ARG A NH1 
505  N NH2 . ARG A 68  ? 0.51149 0.42401 0.45114 -0.05988 0.02119  0.01281  63  ARG A NH2 
506  N N   . SER A 69  ? 0.42746 0.40343 0.36865 -0.13016 0.02421  -0.00648 64  SER A N   
507  C CA  . SER A 69  ? 0.53537 0.53824 0.47907 -0.14641 0.02185  0.01013  64  SER A CA  
508  C C   . SER A 69  ? 0.58649 0.59705 0.53578 -0.16476 0.02234  0.00574  64  SER A C   
509  O O   . SER A 69  ? 0.49654 0.53138 0.44913 -0.18276 0.02002  0.02129  64  SER A O   
510  C CB  . SER A 69  ? 0.53314 0.58412 0.46419 -0.13986 0.02164  0.00773  64  SER A CB  
511  O OG  . SER A 69  ? 0.57616 0.65045 0.50335 -0.13416 0.02205  -0.01170 64  SER A OG  
512  N N   . GLY A 70  ? 0.54516 0.54223 0.49485 -0.16343 0.02508  -0.01459 65  GLY A N   
513  C CA  . GLY A 70  ? 0.62215 0.62719 0.57825 -0.18166 0.02581  -0.02226 65  GLY A CA  
514  C C   . GLY A 70  ? 0.57406 0.62675 0.51582 -0.18331 0.02517  -0.02880 65  GLY A C   
515  O O   . GLY A 70  ? 0.48719 0.57035 0.42085 -0.17283 0.02367  -0.02610 65  GLY A O   
516  N N   . ALA A 71  ? 0.55873 0.62048 0.50286 -0.19682 0.02603  -0.04082 66  ALA A N   
517  C CA  . ALA A 71  ? 0.55077 0.65865 0.48680 -0.19840 0.02410  -0.04796 66  ALA A CA  
518  C C   . ALA A 71  ? 0.56649 0.71175 0.50397 -0.20616 0.02352  -0.03530 66  ALA A C   
519  O O   . ALA A 71  ? 0.65397 0.79158 0.59827 -0.22276 0.02377  -0.01788 66  ALA A O   
520  C CB  . ALA A 71  ? 0.59909 0.71297 0.53834 -0.21597 0.02507  -0.06158 66  ALA A CB  
521  N N   . PRO A 72  ? 0.55696 0.74802 0.49291 -0.19616 0.02165  -0.04361 67  PRO A N   
522  C CA  . PRO A 72  ? 0.59316 0.79822 0.53146 -0.17765 0.01651  -0.05807 67  PRO A CA  
523  C C   . PRO A 72  ? 0.61574 0.80225 0.55506 -0.15363 0.01335  -0.05840 67  PRO A C   
524  O O   . PRO A 72  ? 0.50041 0.70550 0.45128 -0.13799 0.00588  -0.06606 67  PRO A O   
525  C CB  . PRO A 72  ? 0.51435 0.77870 0.46454 -0.17861 0.01475  -0.06675 67  PRO A CB  
526  C CG  . PRO A 72  ? 0.51303 0.79739 0.46143 -0.18778 0.02033  -0.05866 67  PRO A CG  
527  C CD  . PRO A 72  ? 0.53654 0.77742 0.47525 -0.20581 0.02322  -0.03864 67  PRO A CD  
528  N N   . TYR A 73  ? 0.56358 0.71503 0.49646 -0.15125 0.01711  -0.04884 68  TYR A N   
529  C CA  . TYR A 73  ? 0.50596 0.63642 0.43879 -0.13069 0.01461  -0.04865 68  TYR A CA  
530  C C   . TYR A 73  ? 0.46274 0.62860 0.40922 -0.11589 0.01119  -0.05653 68  TYR A C   
531  O O   . TYR A 73  ? 0.46335 0.62887 0.42249 -0.09804 0.00379  -0.06290 68  TYR A O   
532  C CB  . TYR A 73  ? 0.44064 0.55331 0.37044 -0.12367 0.00965  -0.05271 68  TYR A CB  
533  C CG  . TYR A 73  ? 0.51755 0.61642 0.43911 -0.14106 0.01346  -0.05658 68  TYR A CG  
534  C CD1 . TYR A 73  ? 0.52606 0.58890 0.44609 -0.14860 0.02045  -0.05637 68  TYR A CD1 
535  C CD2 . TYR A 73  ? 0.54355 0.66872 0.46470 -0.15011 0.00927  -0.06318 68  TYR A CD2 
536  C CE1 . TYR A 73  ? 0.57605 0.62949 0.49746 -0.16473 0.02457  -0.06833 68  TYR A CE1 
537  C CE2 . TYR A 73  ? 0.59110 0.71054 0.50627 -0.16811 0.01367  -0.07242 68  TYR A CE2 
538  C CZ  . TYR A 73  ? 0.60033 0.68395 0.51711 -0.17526 0.02199  -0.07779 68  TYR A CZ  
539  O OH  . TYR A 73  ? 0.63361 0.71478 0.55298 -0.19319 0.02691  -0.09491 68  TYR A OH  
540  N N   . ALA A 74  ? 0.43608 0.63701 0.38430 -0.12550 0.01582  -0.05686 69  ALA A N   
541  C CA  . ALA A 74  ? 0.43951 0.68882 0.40561 -0.11534 0.01507  -0.07362 69  ALA A CA  
542  C C   . ALA A 74  ? 0.42775 0.69495 0.38492 -0.12374 0.02126  -0.06691 69  ALA A C   
543  O O   . ALA A 74  ? 0.43291 0.70838 0.37629 -0.14660 0.02516  -0.04916 69  ALA A O   
544  C CB  . ALA A 74  ? 0.46452 0.76789 0.44496 -0.12342 0.01486  -0.08788 69  ALA A CB  
545  N N   . LEU A 75  ? 0.39955 0.67454 0.36718 -0.10740 0.02046  -0.07886 70  LEU A N   
546  C CA  . LEU A 75  ? 0.37217 0.67396 0.33102 -0.11624 0.02554  -0.07399 70  LEU A CA  
547  C C   . LEU A 75  ? 0.41592 0.77227 0.39968 -0.10370 0.02667  -0.10725 70  LEU A C   
548  O O   . LEU A 75  ? 0.38114 0.72657 0.39290 -0.08082 0.02055  -0.12815 70  LEU A O   
549  C CB  . LEU A 75  ? 0.37899 0.62621 0.32441 -0.11029 0.02421  -0.05412 70  LEU A CB  
550  C CG  . LEU A 75  ? 0.42947 0.61697 0.36126 -0.11784 0.02295  -0.02860 70  LEU A CG  
551  C CD1 . LEU A 75  ? 0.40425 0.54519 0.33279 -0.10428 0.02141  -0.02050 70  LEU A CD1 
552  C CD2 . LEU A 75  ? 0.55823 0.76256 0.48160 -0.14565 0.02426  -0.00408 70  LEU A CD2 
553  N N   . THR A 76  ? 0.48545 0.90310 0.46289 -0.12041 0.03329  -0.11161 71  THR A N   
554  C CA  . THR A 76  ? 0.44530 0.91825 0.44745 -0.11024 0.03621  -0.14835 71  THR A CA  
555  C C   . THR A 76  ? 0.46719 0.89068 0.47417 -0.08949 0.03186  -0.14823 71  THR A C   
556  O O   . THR A 76  ? 0.41065 0.77713 0.39255 -0.09137 0.02969  -0.11568 71  THR A O   
557  C CB  . THR A 76  ? 0.45133 1.00753 0.43802 -0.13853 0.04476  -0.14921 71  THR A CB  
558  O OG1 . THR A 76  ? 0.41848 0.94523 0.37245 -0.15390 0.04317  -0.10712 71  THR A OG1 
559  C CG2 . THR A 76  ? 0.43992 1.05115 0.42141 -0.16279 0.04897  -0.14728 71  THR A CG2 
560  N N   . PRO A 77  ? 0.54463 0.98987 0.58900 -0.06982 0.03002  -0.18603 72  PRO A N   
561  C CA  . PRO A 77  ? 0.51715 0.91711 0.56715 -0.05254 0.02537  -0.18481 72  PRO A CA  
562  C C   . PRO A 77  ? 0.47167 0.87951 0.48720 -0.06853 0.03092  -0.16341 72  PRO A C   
563  O O   . PRO A 77  ? 0.52671 0.87808 0.53002 -0.06024 0.02716  -0.14288 72  PRO A O   
564  C CB  . PRO A 77  ? 0.58675 1.02665 0.69205 -0.03398 0.02286  -0.23515 72  PRO A CB  
565  C CG  . PRO A 77  ? 0.59719 1.08747 0.73144 -0.03533 0.02365  -0.26097 72  PRO A CG  
566  C CD  . PRO A 77  ? 0.59417 1.11237 0.68224 -0.06442 0.03248  -0.23439 72  PRO A CD  
567  N N   . THR A 78  ? 0.30979 0.79105 0.30983 -0.09365 0.03870  -0.16463 73  THR A N   
568  C CA  . THR A 78  ? 0.47404 0.96877 0.44322 -0.11244 0.04058  -0.13660 73  THR A CA  
569  C C   . THR A 78  ? 0.44388 0.87434 0.38394 -0.12258 0.03563  -0.08364 73  THR A C   
570  O O   . THR A 78  ? 0.43638 0.82788 0.36425 -0.12082 0.03195  -0.05870 73  THR A O   
571  C CB  . THR A 78  ? 0.46182 1.06211 0.42426 -0.14145 0.04761  -0.14769 73  THR A CB  
572  O OG1 . THR A 78  ? 0.46050 1.11078 0.46828 -0.12920 0.04792  -0.19995 73  THR A OG1 
573  C CG2 . THR A 78  ? 0.45230 1.06454 0.39081 -0.16225 0.04311  -0.11004 73  THR A CG2 
574  N N   . ALA A 79  ? 0.45665 0.87844 0.39057 -0.13382 0.03518  -0.06846 74  ALA A N   
575  C CA  . ALA A 79  ? 0.42839 0.78421 0.34678 -0.14083 0.02994  -0.02638 74  ALA A CA  
576  C C   . ALA A 79  ? 0.47882 0.75297 0.40317 -0.11457 0.02633  -0.02695 74  ALA A C   
577  O O   . ALA A 79  ? 0.52478 0.74841 0.44161 -0.11514 0.02281  0.00018  74  ALA A O   
578  C CB  . ALA A 79  ? 0.40541 0.76538 0.32181 -0.15620 0.03020  -0.01725 74  ALA A CB  
579  N N   . LEU A 80  ? 0.39419 0.65944 0.33671 -0.09256 0.02593  -0.05744 75  LEU A N   
580  C CA  . LEU A 80  ? 0.47029 0.66908 0.41787 -0.07158 0.02137  -0.05620 75  LEU A CA  
581  C C   . LEU A 80  ? 0.47645 0.65473 0.41972 -0.06411 0.02050  -0.04873 75  LEU A C   
582  O O   . LEU A 80  ? 0.43692 0.56238 0.37174 -0.06018 0.01869  -0.02967 75  LEU A O   
583  C CB  . LEU A 80  ? 0.50013 0.70425 0.47515 -0.05301 0.01708  -0.08506 75  LEU A CB  
584  C CG  . LEU A 80  ? 0.49691 0.64579 0.48060 -0.03564 0.00937  -0.08169 75  LEU A CG  
585  C CD1 . LEU A 80  ? 0.32050 0.42633 0.28165 -0.04413 0.01027  -0.05818 75  LEU A CD1 
586  C CD2 . LEU A 80  ? 0.47489 0.64039 0.49258 -0.02339 0.00133  -0.10282 75  LEU A CD2 
587  N N   . TYR A 81  ? 0.45728 0.68279 0.40842 -0.06335 0.02237  -0.06673 76  TYR A N   
588  C CA  . TYR A 81  ? 0.52783 0.74175 0.47493 -0.05821 0.02145  -0.06066 76  TYR A CA  
589  C C   . TYR A 81  ? 0.51427 0.71322 0.44025 -0.07412 0.02048  -0.02212 76  TYR A C   
590  O O   . TYR A 81  ? 0.50877 0.66205 0.43232 -0.06584 0.01778  -0.00708 76  TYR A O   
591  C CB  . TYR A 81  ? 0.37234 0.65322 0.33248 -0.05957 0.02456  -0.09075 76  TYR A CB  
592  C CG  . TYR A 81  ? 0.40544 0.68184 0.35890 -0.05798 0.02358  -0.08294 76  TYR A CG  
593  C CD1 . TYR A 81  ? 0.47407 0.70789 0.44282 -0.03713 0.01985  -0.09410 76  TYR A CD1 
594  C CD2 . TYR A 81  ? 0.54999 0.86750 0.48317 -0.07954 0.02462  -0.06058 76  TYR A CD2 
595  C CE1 . TYR A 81  ? 0.50599 0.73762 0.46909 -0.03623 0.01906  -0.08762 76  TYR A CE1 
596  C CE2 . TYR A 81  ? 0.55836 0.87535 0.48660 -0.07864 0.02251  -0.05195 76  TYR A CE2 
597  C CZ  . TYR A 81  ? 0.58439 0.85800 0.52716 -0.05618 0.02068  -0.06774 76  TYR A CZ  
598  O OH  . TYR A 81  ? 0.66542 0.94077 0.60368 -0.05598 0.01875  -0.05986 76  TYR A OH  
599  N N   . ASP A 82  ? 0.49727 0.73824 0.41296 -0.09814 0.02116  -0.00467 77  ASP A N   
600  C CA  . ASP A 82  ? 0.49951 0.72774 0.40595 -0.11476 0.01573  0.03716  77  ASP A CA  
601  C C   . ASP A 82  ? 0.53761 0.68892 0.45026 -0.10796 0.01221  0.05625  77  ASP A C   
602  O O   . ASP A 82  ? 0.53855 0.65836 0.45680 -0.10957 0.00650  0.08252  77  ASP A O   
603  C CB  . ASP A 82  ? 0.44671 0.73945 0.34442 -0.14610 0.01439  0.05709  77  ASP A CB  
604  C CG  . ASP A 82  ? 0.47861 0.85771 0.36830 -0.16010 0.01693  0.04634  77  ASP A CG  
605  O OD1 . ASP A 82  ? 0.52889 0.90772 0.41772 -0.15344 0.01497  0.04758  77  ASP A OD1 
606  O OD2 . ASP A 82  ? 0.54583 0.99860 0.43091 -0.17888 0.02157  0.03355  77  ASP A OD2 
607  N N   . ALA A 83  ? 0.50170 0.62678 0.41762 -0.10085 0.01512  0.04108  78  ALA A N   
608  C CA  . ALA A 83  ? 0.49918 0.56319 0.42253 -0.09794 0.01348  0.05182  78  ALA A CA  
609  C C   . ALA A 83  ? 0.57399 0.59270 0.50036 -0.07591 0.01524  0.03628  78  ALA A C   
610  O O   . ALA A 83  ? 0.55698 0.53240 0.49078 -0.07371 0.01555  0.03864  78  ALA A O   
611  C CB  . ALA A 83  ? 0.51045 0.57751 0.43407 -0.10720 0.01542  0.04545  78  ALA A CB  
612  N N   . ALA A 84  ? 0.44238 0.56766 0.36160 -0.03269 0.00047  0.01410  79  ALA A N   
613  C CA  . ALA A 84  ? 0.52493 0.60084 0.43855 -0.02292 -0.00035 -0.00201 79  ALA A CA  
614  C C   . ALA A 84  ? 0.55413 0.59070 0.47627 -0.03095 -0.00145 0.00511  79  ALA A C   
615  O O   . ALA A 84  ? 0.46711 0.51176 0.39620 -0.03860 -0.00315 0.01949  79  ALA A O   
616  C CB  . ALA A 84  ? 0.55598 0.63332 0.45418 -0.00219 -0.00259 -0.02069 79  ALA A CB  
617  N N   . MET A 85  ? 0.45860 0.45754 0.38161 -0.02928 -0.00078 -0.00395 80  MET A N   
618  C CA  . MET A 85  ? 0.52649 0.49358 0.45836 -0.03247 -0.00082 -0.00116 80  MET A CA  
619  C C   . MET A 85  ? 0.53329 0.49768 0.45769 -0.02444 -0.00298 -0.00219 80  MET A C   
620  O O   . MET A 85  ? 0.47551 0.43292 0.40979 -0.02895 -0.00451 0.00769  80  MET A O   
621  C CB  . MET A 85  ? 0.55323 0.49310 0.48494 -0.03114 0.00171  -0.01243 80  MET A CB  
622  C CG  . MET A 85  ? 0.62695 0.54227 0.56952 -0.03179 0.00316  -0.01221 80  MET A CG  
623  S SD  . MET A 85  ? 0.62291 0.52887 0.59236 -0.04228 0.00008  -0.00123 80  MET A SD  
624  C CE  . MET A 85  ? 0.58523 0.48396 0.55852 -0.04842 0.00003  -0.01306 80  MET A CE  
625  N N   . ILE A 86  ? 0.52931 0.49800 0.43843 -0.01244 -0.00546 -0.01428 81  ILE A N   
626  C CA  . ILE A 86  ? 0.52843 0.48897 0.43010 -0.00482 -0.01095 -0.01927 81  ILE A CA  
627  C C   . ILE A 86  ? 0.51994 0.51115 0.40894 0.00594  -0.01496 -0.02859 81  ILE A C   
628  O O   . ILE A 86  ? 0.50563 0.51394 0.38959 0.01398  -0.01464 -0.03773 81  ILE A O   
629  C CB  . ILE A 86  ? 0.55814 0.48818 0.45639 0.00001  -0.01467 -0.02734 81  ILE A CB  
630  C CG1 . ILE A 86  ? 0.59184 0.50411 0.50022 -0.00863 -0.00844 -0.02201 81  ILE A CG1 
631  C CG2 . ILE A 86  ? 0.61949 0.53715 0.51460 0.00357  -0.02308 -0.02949 81  ILE A CG2 
632  C CD1 . ILE A 86  ? 0.56060 0.46508 0.48246 -0.01477 -0.00621 -0.01301 81  ILE A CD1 
633  N N   . SER A 87  ? 0.53934 0.54037 0.42342 0.00765  -0.01936 -0.02846 82  SER A N   
634  C CA  . SER A 87  ? 0.52532 0.56345 0.39585 0.01927  -0.02282 -0.04118 82  SER A CA  
635  C C   . SER A 87  ? 0.55619 0.57327 0.41712 0.03612  -0.03402 -0.06477 82  SER A C   
636  O O   . SER A 87  ? 0.67302 0.69975 0.52433 0.04350  -0.04178 -0.07668 82  SER A O   
637  C CB  . SER A 87  ? 0.57544 0.64352 0.44391 0.01123  -0.02302 -0.02878 82  SER A CB  
638  O OG  . SER A 87  ? 0.54549 0.58658 0.41415 0.00936  -0.03017 -0.02840 82  SER A OG  
639  N N   . SER A 88  ? 0.57751 0.56553 0.44185 0.04176  -0.03725 -0.07149 83  SER A N   
640  C CA  . SER A 88  ? 0.70151 0.66362 0.56197 0.05663  -0.05202 -0.09077 83  SER A CA  
641  C C   . SER A 88  ? 0.75981 0.75305 0.61380 0.07797  -0.05603 -0.11388 83  SER A C   
642  O O   . SER A 88  ? 0.63173 0.66725 0.48546 0.07995  -0.04560 -0.11213 83  SER A O   
643  C CB  . SER A 88  ? 0.76933 0.69141 0.63785 0.05254  -0.05624 -0.08410 83  SER A CB  
644  O OG  . SER A 88  ? 0.75010 0.68398 0.62273 0.04673  -0.04507 -0.07449 83  SER A OG  
645  N N   . GLY A 89  ? 0.83469 0.80795 0.68575 0.09441  -0.07276 -0.13650 84  GLY A N   
646  C CA  . GLY A 89  ? 0.83470 0.83458 0.68220 0.12000  -0.07939 -0.16512 84  GLY A CA  
647  C C   . GLY A 89  ? 0.89581 0.87254 0.75483 0.13305  -0.08827 -0.17176 84  GLY A C   
648  O O   . GLY A 89  ? 0.87445 0.83074 0.74115 0.11999  -0.08402 -0.15096 84  GLY A O   
649  N N   . SER A 90  ? 0.87445 0.85721 0.73528 0.16058  -0.10197 -0.20271 85  SER A N   
650  C CA  . SER A 90  ? 0.84263 0.80339 0.71832 0.17772  -0.11522 -0.21155 85  SER A CA  
651  C C   . SER A 90  ? 0.85515 0.84720 0.73624 0.17197  -0.09953 -0.19387 85  SER A C   
652  O O   . SER A 90  ? 0.81213 0.77552 0.70440 0.16979  -0.10670 -0.18217 85  SER A O   
653  C CB  . SER A 90  ? 0.83742 0.72595 0.72355 0.16931  -0.13601 -0.20088 85  SER A CB  
654  O OG  . SER A 90  ? 0.96209 0.82701 0.85440 0.17407  -0.15381 -0.21301 85  SER A OG  
655  N N   . MET A 91  ? 0.85390 0.90762 0.72772 0.16759  -0.07969 -0.18990 86  MET A N   
656  C CA  . MET A 91  ? 0.84203 0.92500 0.72182 0.15701  -0.06586 -0.17060 86  MET A CA  
657  C C   . MET A 91  ? 0.72628 0.83897 0.61796 0.18208  -0.07094 -0.18734 86  MET A C   
658  O O   . MET A 91  ? 0.68459 0.79568 0.58568 0.17626  -0.06955 -0.17293 86  MET A O   
659  C CB  . MET A 91  ? 0.84299 0.97897 0.71533 0.13928  -0.04617 -0.15499 86  MET A CB  
660  C CG  . MET A 91  ? 0.78632 0.95678 0.66712 0.12870  -0.03492 -0.13772 86  MET A CG  
661  S SD  . MET A 91  ? 0.77539 0.97006 0.65417 0.09515  -0.01855 -0.10646 86  MET A SD  
662  C CE  . MET A 91  ? 0.73233 0.85044 0.61128 0.07570  -0.02189 -0.09113 86  MET A CE  
663  N N   . THR A 92  ? 0.60277 0.74649 0.49491 0.21108  -0.07724 -0.21915 87  THR A N   
664  C CA  . THR A 92  ? 0.71879 0.89980 0.62733 0.23649  -0.08120 -0.23463 87  THR A CA  
665  C C   . THR A 92  ? 0.81683 0.93987 0.74096 0.24689  -0.10102 -0.23487 87  THR A C   
666  O O   . THR A 92  ? 0.72887 0.87090 0.66611 0.25007  -0.09990 -0.22579 87  THR A O   
667  C CB  . THR A 92  ? 0.75439 0.97418 0.67133 0.25680  -0.08754 -0.25781 87  THR A CB  
668  O OG1 . THR A 92  ? 0.68318 0.97201 0.59110 0.24511  -0.06829 -0.25010 87  THR A OG1 
669  C CG2 . THR A 92  ? 0.81727 1.06498 0.75396 0.28431  -0.09743 -0.27518 87  THR A CG2 
670  N N   . ASN A 93  ? 0.83235 0.88562 0.75778 0.24809  -0.12101 -0.23961 88  ASN A N   
671  C CA  . ASN A 93  ? 0.84280 0.84028 0.78561 0.25136  -0.14239 -0.23031 88  ASN A CA  
672  C C   . ASN A 93  ? 0.79994 0.78269 0.73912 0.21844  -0.13249 -0.19113 88  ASN A C   
673  O O   . ASN A 93  ? 0.86853 0.83520 0.82076 0.21892  -0.14300 -0.17793 88  ASN A O   
674  C CB  . ASN A 93  ? 0.91658 0.84862 0.86490 0.25230  -0.16765 -0.23666 88  ASN A CB  
675  C CG  . ASN A 93  ? 0.96285 0.91432 0.92006 0.27253  -0.17950 -0.26461 88  ASN A CG  
676  O OD1 . ASN A 93  ? 1.03709 0.95150 0.99646 0.26923  -0.19575 -0.27026 88  ASN A OD1 
677  N ND2 . ASN A 93  ? 0.87433 0.88706 0.83723 0.29327  -0.17198 -0.28232 88  ASN A ND2 
678  N N   . ARG A 94  ? 0.74756 0.73761 0.66988 0.19080  -0.11352 -0.17341 89  ARG A N   
679  C CA  . ARG A 94  ? 0.69725 0.68074 0.61538 0.16203  -0.10248 -0.14249 89  ARG A CA  
680  C C   . ARG A 94  ? 0.62711 0.66034 0.55057 0.16235  -0.09142 -0.13671 89  ARG A C   
681  O O   . ARG A 94  ? 0.76833 0.79229 0.69602 0.15158  -0.09403 -0.11930 89  ARG A O   
682  C CB  . ARG A 94  ? 0.69269 0.67449 0.59594 0.13768  -0.08651 -0.13029 89  ARG A CB  
683  C CG  . ARG A 94  ? 0.69012 0.66508 0.58905 0.11067  -0.07515 -0.10510 89  ARG A CG  
684  C CD  . ARG A 94  ? 0.68967 0.65869 0.57900 0.09203  -0.06301 -0.09678 89  ARG A CD  
685  N NE  . ARG A 94  ? 0.72090 0.65445 0.60814 0.09478  -0.07400 -0.10232 89  ARG A NE  
686  C CZ  . ARG A 94  ? 0.81575 0.75943 0.69712 0.09885  -0.07194 -0.11302 89  ARG A CZ  
687  N NH1 . ARG A 94  ? 0.73470 0.72568 0.61162 0.09978  -0.05860 -0.11647 89  ARG A NH1 
688  N NH2 . ARG A 94  ? 0.88167 0.79143 0.76200 0.09986  -0.08444 -0.11804 89  ARG A NH2 
689  N N   . ILE A 95  ? 0.56172 0.65310 0.48528 0.17362  -0.07997 -0.15017 90  ILE A N   
690  C CA  . ILE A 95  ? 0.57363 0.71839 0.50624 0.17516  -0.07193 -0.14501 90  ILE A CA  
691  C C   . ILE A 95  ? 0.62340 0.76352 0.57455 0.20016  -0.08972 -0.15467 90  ILE A C   
692  O O   . ILE A 95  ? 0.57036 0.72165 0.52959 0.19320  -0.09074 -0.13968 90  ILE A O   
693  C CB  . ILE A 95  ? 0.52450 0.74076 0.45485 0.18080  -0.05665 -0.15473 90  ILE A CB  
694  C CG1 . ILE A 95  ? 0.50928 0.73149 0.42631 0.14963  -0.04067 -0.13466 90  ILE A CG1 
695  C CG2 . ILE A 95  ? 0.52459 0.80314 0.46946 0.18892  -0.05220 -0.15364 90  ILE A CG2 
696  C CD1 . ILE A 95  ? 0.48827 0.76947 0.39922 0.15298  -0.02951 -0.14193 90  ILE A CD1 
697  N N   . ASP A 96  ? 0.60130 0.72267 0.56102 0.22973  -0.10640 -0.18015 91  ASP A N   
698  C CA  . ASP A 96  ? 0.69125 0.80030 0.67373 0.25617  -0.12788 -0.18971 91  ASP A CA  
699  C C   . ASP A 96  ? 0.66155 0.72245 0.64779 0.23687  -0.14003 -0.16051 91  ASP A C   
700  O O   . ASP A 96  ? 0.69913 0.77733 0.69927 0.24092  -0.14591 -0.15041 91  ASP A O   
701  C CB  . ASP A 96  ? 0.75605 0.83239 0.74783 0.28771  -0.14902 -0.22175 91  ASP A CB  
702  C CG  . ASP A 96  ? 0.87191 1.00998 0.86238 0.31284  -0.13965 -0.25526 91  ASP A CG  
703  O OD1 . ASP A 96  ? 0.87338 1.08613 0.86438 0.31467  -0.12051 -0.25456 91  ASP A OD1 
704  O OD2 . ASP A 96  ? 0.93764 1.05318 0.92538 0.31920  -0.15202 -0.27359 91  ASP A OD2 
705  N N   . ARG A 97  ? 0.68450 0.69135 0.65822 0.21476  -0.14359 -0.14544 92  ARG A N   
706  C CA  . ARG A 97  ? 0.73503 0.70423 0.70926 0.19382  -0.15379 -0.11607 92  ARG A CA  
707  C C   . ARG A 97  ? 0.71792 0.72415 0.68384 0.17144  -0.13670 -0.09585 92  ARG A C   
708  O O   . ARG A 97  ? 0.69094 0.69532 0.66419 0.16669  -0.14697 -0.07874 92  ARG A O   
709  C CB  . ARG A 97  ? 0.74219 0.66168 0.70347 0.17244  -0.15598 -0.10401 92  ARG A CB  
710  C CG  . ARG A 97  ? 0.87987 0.74338 0.85564 0.18584  -0.18540 -0.10931 92  ARG A CG  
711  C CD  . ARG A 97  ? 0.97757 0.79964 0.94224 0.16205  -0.18710 -0.09483 92  ARG A CD  
712  N NE  . ARG A 97  ? 1.09439 0.92005 1.04785 0.16560  -0.17649 -0.11593 92  ARG A NE  
713  C CZ  . ARG A 97  ? 1.11104 0.95261 1.04615 0.14456  -0.15351 -0.10843 92  ARG A CZ  
714  N NH1 . ARG A 97  ? 1.07155 0.92504 0.99753 0.12007  -0.13830 -0.08450 92  ARG A NH1 
715  N NH2 . ARG A 97  ? 1.12266 0.96870 1.04943 0.14882  -0.14729 -0.12594 92  ARG A NH2 
716  N N   . LEU A 98  ? 0.67623 0.71543 0.62780 0.15645  -0.11291 -0.09681 93  LEU A N   
717  C CA  . LEU A 98  ? 0.59934 0.66756 0.54377 0.13313  -0.09898 -0.08002 93  LEU A CA  
718  C C   . LEU A 98  ? 0.54636 0.66285 0.50628 0.14598  -0.10162 -0.08197 93  LEU A C   
719  O O   . LEU A 98  ? 0.49772 0.62527 0.45755 0.13153  -0.10277 -0.06607 93  LEU A O   
720  C CB  . LEU A 98  ? 0.48979 0.57644 0.42079 0.11509  -0.07750 -0.08026 93  LEU A CB  
721  C CG  . LEU A 98  ? 0.54519 0.58834 0.46235 0.09874  -0.07363 -0.07443 93  LEU A CG  
722  C CD1 . LEU A 98  ? 0.54328 0.60429 0.45221 0.08409  -0.05554 -0.07426 93  LEU A CD1 
723  C CD2 . LEU A 98  ? 0.59171 0.60776 0.50213 0.07952  -0.07728 -0.05658 93  LEU A CD2 
724  N N   . GLU A 99  ? 0.55162 0.70224 0.52521 0.17366  -0.10291 -0.10243 94  GLU A N   
725  C CA  . GLU A 99  ? 0.55922 0.76024 0.55218 0.18973  -0.10698 -0.10502 94  GLU A CA  
726  C C   . GLU A 99  ? 0.57329 0.74469 0.58175 0.20161  -0.13096 -0.09694 94  GLU A C   
727  O O   . GLU A 99  ? 0.55518 0.75247 0.57197 0.19587  -0.13465 -0.08284 94  GLU A O   
728  C CB  . GLU A 99  ? 0.59866 0.84821 0.60400 0.22070  -0.10326 -0.13196 94  GLU A CB  
729  C CG  . GLU A 99  ? 0.64042 0.95057 0.66967 0.24067  -0.10694 -0.13623 94  GLU A CG  
730  C CD  . GLU A 99  ? 0.71916 1.10008 0.75765 0.26558  -0.09616 -0.16076 94  GLU A CD  
731  O OE1 . GLU A 99  ? 0.67356 1.04390 0.70491 0.28168  -0.09532 -0.18351 94  GLU A OE1 
732  O OE2 . GLU A 99  ? 0.73333 1.18564 0.78606 0.26807  -0.08876 -0.15687 94  GLU A OE2 
733  N N   . LYS A 100 ? 0.60094 0.71745 0.61470 0.21618  -0.14979 -0.10332 95  LYS A N   
734  C CA  . LYS A 100 ? 0.65279 0.73644 0.68460 0.22576  -0.17681 -0.09090 95  LYS A CA  
735  C C   . LYS A 100 ? 0.65381 0.72279 0.67179 0.19192  -0.17739 -0.05760 95  LYS A C   
736  O O   . LYS A 100 ? 0.62934 0.69931 0.66075 0.19370  -0.19468 -0.04074 95  LYS A O   
737  C CB  . LYS A 100 ? 0.63862 0.66063 0.67953 0.24277  -0.19907 -0.10177 95  LYS A CB  
738  C CG  . LYS A 100 ? 0.66480 0.64882 0.73116 0.25555  -0.23260 -0.08837 95  LYS A CG  
739  N N   . ALA A 101 ? 0.69128 0.74971 0.68320 0.16212  -0.15960 -0.04860 96  ALA A N   
740  C CA  . ALA A 101 ? 0.68738 0.73859 0.66319 0.13111  -0.15781 -0.02246 96  ALA A CA  
741  C C   . ALA A 101 ? 0.64651 0.74834 0.61715 0.11695  -0.14531 -0.01697 96  ALA A C   
742  O O   . ALA A 101 ? 0.56539 0.66904 0.52330 0.09395  -0.14610 0.00142  96  ALA A O   
743  C CB  . ALA A 101 ? 0.66662 0.68910 0.61960 0.10814  -0.14422 -0.01893 96  ALA A CB  
744  N N   . GLY A 102 ? 0.59495 0.74143 0.57510 0.12888  -0.13473 -0.03225 97  GLY A N   
745  C CA  . GLY A 102 ? 0.51124 0.70689 0.48997 0.11363  -0.12497 -0.02646 97  GLY A CA  
746  C C   . GLY A 102 ? 0.46464 0.66849 0.42465 0.08715  -0.10382 -0.02786 97  GLY A C   
747  O O   . GLY A 102 ? 0.49301 0.72811 0.45048 0.06876  -0.09882 -0.02141 97  GLY A O   
748  N N   . TRP A 103 ? 0.40160 0.57723 0.35071 0.08449  -0.09354 -0.03591 98  TRP A N   
749  C CA  . TRP A 103 ? 0.36748 0.54139 0.30153 0.05951  -0.07680 -0.03529 98  TRP A CA  
750  C C   . TRP A 103 ? 0.47687 0.68442 0.41739 0.06126  -0.06390 -0.04350 98  TRP A C   
751  O O   . TRP A 103 ? 0.38528 0.60179 0.32071 0.03895  -0.05384 -0.03914 98  TRP A O   
752  C CB  . TRP A 103 ? 0.43477 0.55859 0.35325 0.05119  -0.07402 -0.03435 98  TRP A CB  
753  C CG  . TRP A 103 ? 0.54144 0.64270 0.45137 0.04236  -0.08473 -0.02143 98  TRP A CG  
754  C CD1 . TRP A 103 ? 0.57724 0.69851 0.48386 0.03054  -0.09041 -0.01139 98  TRP A CD1 
755  C CD2 . TRP A 103 ? 0.60291 0.66408 0.50695 0.04293  -0.09243 -0.01453 98  TRP A CD2 
756  N NE1 . TRP A 103 ? 0.52423 0.62351 0.42147 0.02371  -0.10017 0.00206  98  TRP A NE1 
757  C CE2 . TRP A 103 ? 0.54289 0.60538 0.43968 0.03039  -0.10171 0.00181  98  TRP A CE2 
758  C CE3 . TRP A 103 ? 0.60763 0.63503 0.51213 0.05098  -0.09353 -0.01908 98  TRP A CE3 
759  C CZ2 . TRP A 103 ? 0.62823 0.66274 0.51938 0.02456  -0.11142 0.01655  98  TRP A CZ2 
760  C CZ3 . TRP A 103 ? 0.60953 0.60478 0.50998 0.04517  -0.10411 -0.00573 98  TRP A CZ3 
761  C CH2 . TRP A 103 ? 0.60066 0.60111 0.49499 0.03148  -0.11262 0.01331  98  TRP A CH2 
762  N N   . VAL A 104 ? 0.48427 0.71144 0.43631 0.08666  -0.06512 -0.05530 99  VAL A N   
763  C CA  . VAL A 104 ? 0.43184 0.70722 0.39033 0.08836  -0.05315 -0.06047 99  VAL A CA  
764  C C   . VAL A 104 ? 0.44670 0.77695 0.42543 0.11394  -0.05831 -0.06876 99  VAL A C   
765  O O   . VAL A 104 ? 0.44089 0.76076 0.42968 0.13437  -0.07261 -0.07339 99  VAL A O   
766  C CB  . VAL A 104 ? 0.46676 0.72518 0.41649 0.09436  -0.04590 -0.07034 99  VAL A CB  
767  C CG1 . VAL A 104 ? 0.45976 0.66468 0.39325 0.07210  -0.04192 -0.06243 99  VAL A CG1 
768  C CG2 . VAL A 104 ? 0.36551 0.61058 0.32042 0.12737  -0.05647 -0.08921 99  VAL A CG2 
769  N N   . GLU A 105 ? 0.50574 0.89807 0.49261 0.11227  -0.04736 -0.06893 100 GLU A N   
770  C CA  . GLU A 105 ? 0.51824 0.98024 0.52617 0.13543  -0.04850 -0.07694 100 GLU A CA  
771  C C   . GLU A 105 ? 0.44058 0.95504 0.44894 0.14347  -0.03543 -0.08613 100 GLU A C   
772  O O   . GLU A 105 ? 0.44623 0.96712 0.44494 0.11718  -0.02461 -0.07283 100 GLU A O   
773  C CB  . GLU A 105 ? 0.50255 1.00984 0.52278 0.11569  -0.04864 -0.05898 100 GLU A CB  
774  C CG  . GLU A 105 ? 0.67507 1.23600 0.71965 0.14112  -0.05672 -0.06465 100 GLU A CG  
775  C CD  . GLU A 105 ? 0.73299 1.31526 0.78600 0.11819  -0.06230 -0.04507 100 GLU A CD  
776  O OE1 . GLU A 105 ? 0.75648 1.33936 0.80112 0.08268  -0.05594 -0.02928 100 GLU A OE1 
777  O OE2 . GLU A 105 ? 0.75225 1.34774 0.82119 0.13543  -0.07513 -0.04573 100 GLU A OE2 
778  N N   . ARG A 106 ? 0.52027 1.07424 0.54071 0.18011  -0.03767 -0.10902 101 ARG A N   
779  C CA  . ARG A 106 ? 0.58371 1.20466 0.60386 0.19045  -0.02474 -0.12009 101 ARG A CA  
780  C C   . ARG A 106 ? 0.55481 1.27582 0.59509 0.18818  -0.01683 -0.11022 101 ARG A C   
781  O O   . ARG A 106 ? 0.52734 1.27913 0.58858 0.20913  -0.02440 -0.11711 101 ARG A O   
782  C CB  . ARG A 106 ? 0.64031 1.25524 0.66153 0.23317  -0.03142 -0.15588 101 ARG A CB  
783  C CG  . ARG A 106 ? 0.71659 1.27135 0.71488 0.22947  -0.03140 -0.16457 101 ARG A CG  
784  C CD  . ARG A 106 ? 0.77745 1.26853 0.77850 0.26107  -0.05023 -0.19114 101 ARG A CD  
785  N NE  . ARG A 106 ? 0.83500 1.28680 0.81699 0.26275  -0.05068 -0.20502 101 ARG A NE  
786  C CZ  . ARG A 106 ? 0.87955 1.26230 0.86083 0.28083  -0.06861 -0.22347 101 ARG A CZ  
787  N NH1 . ARG A 106 ? 0.85554 1.19961 0.85500 0.29848  -0.08815 -0.22794 101 ARG A NH1 
788  N NH2 . ARG A 106 ? 0.88276 1.23534 0.84690 0.27949  -0.06911 -0.23493 101 ARG A NH2 
789  N N   . ARG A 107 ? 0.51715 1.28983 0.55345 0.16101  -0.00321 -0.09096 102 ARG A N   
790  C CA  . ARG A 107 ? 0.55284 1.42130 0.60662 0.14986  0.00392  -0.07420 102 ARG A CA  
791  C C   . ARG A 107 ? 0.54598 1.46000 0.58207 0.14237  0.01263  -0.07016 102 ARG A C   
792  O O   . ARG A 107 ? 0.51371 1.40087 0.53401 0.15121  0.01387  -0.08407 102 ARG A O   
793  C CB  . ARG A 107 ? 0.49605 1.35202 0.55674 0.10642  0.00108  -0.04030 102 ARG A CB  
794  N N   . ALA A 108 ? 0.58364 1.56675 0.62294 0.12563  0.01560  -0.04990 103 ALA A N   
795  C CA  . ALA A 108 ? 0.52861 1.56571 0.55529 0.12110  0.01863  -0.04488 103 ALA A CA  
796  C C   . ALA A 108 ? 0.48921 1.55088 0.51679 0.07418  0.02111  -0.00224 103 ALA A C   
797  O O   . ALA A 108 ? 0.45253 1.52641 0.47151 0.06173  0.02169  0.00788  103 ALA A O   
798  C CB  . ALA A 108 ? 0.64319 1.74975 0.67143 0.14691  0.01707  -0.06026 103 ALA A CB  
799  N N   . THR A 116 ? 0.72624 1.72248 0.71720 0.13288  0.01923  -0.07299 111 THR A N   
800  C CA  . THR A 116 ? 0.68670 1.60260 0.67655 0.14908  0.01716  -0.09222 111 THR A CA  
801  C C   . THR A 116 ? 0.61764 1.47379 0.60376 0.11816  0.02243  -0.06890 111 THR A C   
802  O O   . THR A 116 ? 0.53186 1.36957 0.50828 0.09995  0.02533  -0.05660 111 THR A O   
803  C CB  . THR A 116 ? 0.71680 1.58863 0.69715 0.18432  0.00979  -0.13123 111 THR A CB  
804  N N   . LEU A 117 ? 0.57614 1.40376 0.57023 0.11259  0.02300  -0.06341 112 LEU A N   
805  C CA  . LEU A 117 ? 0.57404 1.33171 0.56280 0.08182  0.02239  -0.04281 112 LEU A CA  
806  C C   . LEU A 117 ? 0.50640 1.17263 0.49006 0.09769  0.01111  -0.06129 112 LEU A C   
807  O O   . LEU A 117 ? 0.50718 1.18041 0.50038 0.12575  0.00497  -0.08048 112 LEU A O   
808  C CB  . LEU A 117 ? 0.59570 1.38073 0.60184 0.04603  0.02139  -0.00932 112 LEU A CB  
809  C CG  . LEU A 117 ? 0.60781 1.47491 0.62293 0.01980  0.02704  0.02029  112 LEU A CG  
810  C CD1 . LEU A 117 ? 0.61896 1.50692 0.65466 -0.01292 0.02182  0.04980  112 LEU A CD1 
811  C CD2 . LEU A 117 ? 0.57867 1.41678 0.58156 -0.00211 0.02864  0.03669  112 LEU A CD2 
812  N N   . VAL A 118 ? 0.39417 0.97843 0.36478 0.07931  0.00756  -0.05355 113 VAL A N   
813  C CA  . VAL A 118 ? 0.42085 0.92265 0.38650 0.08351  -0.00262 -0.06131 113 VAL A CA  
814  C C   . VAL A 118 ? 0.38159 0.85694 0.35091 0.04909  -0.00450 -0.03770 113 VAL A C   
815  O O   . VAL A 118 ? 0.39861 0.86300 0.36542 0.02236  -0.00080 -0.02033 113 VAL A O   
816  C CB  . VAL A 118 ? 0.47979 0.91425 0.42817 0.09159  -0.00541 -0.07404 113 VAL A CB  
817  C CG1 . VAL A 118 ? 0.46899 0.82626 0.41302 0.09110  -0.01567 -0.07627 113 VAL A CG1 
818  C CG2 . VAL A 118 ? 0.56244 1.02197 0.50768 0.12599  -0.00656 -0.10157 113 VAL A CG2 
819  N N   . ALA A 119 ? 0.38735 0.85410 0.36404 0.05004  -0.01202 -0.03763 114 ALA A N   
820  C CA  . ALA A 119 ? 0.41619 0.86554 0.39642 0.01913  -0.01557 -0.02001 114 ALA A CA  
821  C C   . ALA A 119 ? 0.45576 0.84394 0.42689 0.02202  -0.02450 -0.02703 114 ALA A C   
822  O O   . ALA A 119 ? 0.45826 0.84134 0.43037 0.04710  -0.03095 -0.03908 114 ALA A O   
823  C CB  . ALA A 119 ? 0.33177 0.85349 0.33192 0.00968  -0.01658 -0.00728 114 ALA A CB  
824  N N   . LEU A 120 ? 0.46966 0.81437 0.43338 -0.00344 -0.02615 -0.01931 115 LEU A N   
825  C CA  . LEU A 120 ? 0.44767 0.75003 0.40190 -0.00532 -0.03395 -0.02336 115 LEU A CA  
826  C C   . LEU A 120 ? 0.45288 0.79334 0.41789 -0.00207 -0.04216 -0.02027 115 LEU A C   
827  O O   . LEU A 120 ? 0.39287 0.78262 0.37234 -0.01426 -0.04219 -0.01094 115 LEU A O   
828  C CB  . LEU A 120 ? 0.42680 0.69035 0.37322 -0.03287 -0.03394 -0.01937 115 LEU A CB  
829  C CG  . LEU A 120 ? 0.45681 0.67328 0.39310 -0.03615 -0.02790 -0.02282 115 LEU A CG  
830  C CD1 . LEU A 120 ? 0.43518 0.62326 0.37047 -0.06113 -0.02946 -0.02162 115 LEU A CD1 
831  C CD2 . LEU A 120 ? 0.43271 0.61213 0.35519 -0.01806 -0.02915 -0.03201 115 LEU A CD2 
832  N N   . THR A 121 ? 0.49514 0.81481 0.45507 0.01278  -0.05075 -0.02520 116 THR A N   
833  C CA  . THR A 121 ? 0.46804 0.81283 0.43486 0.00842  -0.06075 -0.01910 116 THR A CA  
834  C C   . THR A 121 ? 0.43936 0.75792 0.39265 -0.02077 -0.06303 -0.01532 116 THR A C   
835  O O   . THR A 121 ? 0.40788 0.68575 0.34791 -0.03293 -0.05720 -0.01928 116 THR A O   
836  C CB  . THR A 121 ? 0.46916 0.80222 0.43770 0.03303  -0.07236 -0.02184 116 THR A CB  
837  O OG1 . THR A 121 ? 0.53072 0.80609 0.47989 0.02812  -0.07492 -0.02205 116 THR A OG1 
838  C CG2 . THR A 121 ? 0.39482 0.74509 0.37718 0.06596  -0.07201 -0.03279 116 THR A CG2 
839  N N   . SER A 122 ? 0.39548 0.74027 0.35305 -0.03104 -0.07244 -0.00958 117 SER A N   
840  C CA  . SER A 122 ? 0.40989 0.73114 0.35192 -0.05600 -0.07647 -0.01122 117 SER A CA  
841  C C   . SER A 122 ? 0.43290 0.70808 0.35299 -0.05074 -0.07687 -0.01615 117 SER A C   
842  O O   . SER A 122 ? 0.48719 0.73021 0.39203 -0.06527 -0.07230 -0.02383 117 SER A O   
843  C CB  . SER A 122 ? 0.51399 0.87522 0.46307 -0.06745 -0.08850 -0.00462 117 SER A CB  
844  O OG  . SER A 122 ? 0.58037 0.96810 0.53914 -0.04537 -0.09665 0.00199  117 SER A OG  
845  N N   . ALA A 123 ? 0.44515 0.71800 0.36612 -0.02958 -0.08332 -0.01128 118 ALA A N   
846  C CA  . ALA A 123 ? 0.44469 0.67854 0.34771 -0.02690 -0.08529 -0.01032 118 ALA A CA  
847  C C   . ALA A 123 ? 0.47642 0.67191 0.37221 -0.02526 -0.07328 -0.01816 118 ALA A C   
848  O O   . ALA A 123 ? 0.43230 0.60031 0.31104 -0.03516 -0.06967 -0.02071 118 ALA A O   
849  C CB  . ALA A 123 ? 0.50575 0.74076 0.41778 -0.00482 -0.09846 -0.00037 118 ALA A CB  
850  N N   . GLY A 124 ? 0.36873 0.56781 0.27750 -0.01254 -0.06696 -0.02206 119 GLY A N   
851  C CA  . GLY A 124 ? 0.36691 0.53354 0.26988 -0.01210 -0.05665 -0.02813 119 GLY A CA  
852  C C   . GLY A 124 ? 0.40034 0.55665 0.29767 -0.03442 -0.04836 -0.03278 119 GLY A C   
853  O O   . GLY A 124 ? 0.39486 0.51825 0.28246 -0.03879 -0.04233 -0.03743 119 GLY A O   
854  N N   . ARG A 125 ? 0.39121 0.57528 0.29770 -0.04865 -0.04969 -0.03148 120 ARG A N   
855  C CA  . ARG A 125 ? 0.39725 0.56491 0.30254 -0.06992 -0.04646 -0.03695 120 ARG A CA  
856  C C   . ARG A 125 ? 0.39639 0.54169 0.28364 -0.07957 -0.04859 -0.04687 120 ARG A C   
857  O O   . ARG A 125 ? 0.42652 0.54197 0.30822 -0.08571 -0.04329 -0.05666 120 ARG A O   
858  C CB  . ARG A 125 ? 0.42370 0.62477 0.34515 -0.08625 -0.05158 -0.03133 120 ARG A CB  
859  C CG  . ARG A 125 ? 0.52613 0.70271 0.45035 -0.10842 -0.05321 -0.03765 120 ARG A CG  
860  C CD  . ARG A 125 ? 0.68430 0.88954 0.62463 -0.12951 -0.06325 -0.03129 120 ARG A CD  
861  N NE  . ARG A 125 ? 0.67825 0.85025 0.62111 -0.15000 -0.06978 -0.04208 120 ARG A NE  
862  C CZ  . ARG A 125 ? 0.61730 0.79995 0.57372 -0.17294 -0.08273 -0.04055 120 ARG A CZ  
863  N NH1 . ARG A 125 ? 0.59691 0.82864 0.56493 -0.17947 -0.08877 -0.02615 120 ARG A NH1 
864  N NH2 . ARG A 125 ? 0.59895 0.74348 0.55944 -0.18866 -0.09112 -0.05451 120 ARG A NH2 
865  N N   . ALA A 126 ? 0.37998 0.54427 0.25857 -0.08028 -0.05663 -0.04469 121 ALA A N   
866  C CA  . ALA A 126 ? 0.39664 0.55077 0.25483 -0.08951 -0.05816 -0.05399 121 ALA A CA  
867  C C   . ALA A 126 ? 0.49873 0.62579 0.34499 -0.07998 -0.05063 -0.05464 121 ALA A C   
868  O O   . ALA A 126 ? 0.47851 0.59018 0.31349 -0.08687 -0.04506 -0.06746 121 ALA A O   
869  C CB  . ALA A 126 ? 0.46126 0.64668 0.31193 -0.09181 -0.06947 -0.04644 121 ALA A CB  
870  N N   . LEU A 127 ? 0.50840 0.63034 0.35960 -0.06350 -0.05123 -0.04228 122 LEU A N   
871  C CA  . LEU A 127 ? 0.49059 0.58808 0.33319 -0.05660 -0.04697 -0.03923 122 LEU A CA  
872  C C   . LEU A 127 ? 0.40734 0.47933 0.25209 -0.05880 -0.03532 -0.05017 122 LEU A C   
873  O O   . LEU A 127 ? 0.46732 0.52881 0.30122 -0.06360 -0.02963 -0.05664 122 LEU A O   
874  C CB  . LEU A 127 ? 0.48366 0.57520 0.33573 -0.03844 -0.05368 -0.02643 122 LEU A CB  
875  C CG  . LEU A 127 ? 0.52071 0.58377 0.36802 -0.03318 -0.05177 -0.02149 122 LEU A CG  
876  C CD1 . LEU A 127 ? 0.67344 0.74224 0.50382 -0.04511 -0.05351 -0.01465 122 LEU A CD1 
877  C CD2 . LEU A 127 ? 0.55532 0.60726 0.41460 -0.01490 -0.06255 -0.01253 122 LEU A CD2 
878  N N   . ILE A 128 ? 0.38510 0.45212 0.24499 -0.05532 -0.03198 -0.05128 123 ILE A N   
879  C CA  . ILE A 128 ? 0.38912 0.43182 0.25416 -0.05676 -0.02328 -0.05757 123 ILE A CA  
880  C C   . ILE A 128 ? 0.40214 0.43749 0.26712 -0.07103 -0.02137 -0.07197 123 ILE A C   
881  O O   . ILE A 128 ? 0.45182 0.46567 0.31787 -0.07105 -0.01517 -0.08029 123 ILE A O   
882  C CB  . ILE A 128 ? 0.42577 0.47192 0.30617 -0.05053 -0.02172 -0.05143 123 ILE A CB  
883  C CG1 . ILE A 128 ? 0.43376 0.45450 0.31876 -0.04985 -0.01459 -0.05329 123 ILE A CG1 
884  C CG2 . ILE A 128 ? 0.46109 0.53138 0.35394 -0.06157 -0.02525 -0.04946 123 ILE A CG2 
885  C CD1 . ILE A 128 ? 0.46718 0.46901 0.34294 -0.04034 -0.01221 -0.05236 123 ILE A CD1 
886  N N   . ASP A 129 ? 0.42757 0.48013 0.29330 -0.08243 -0.02824 -0.07672 124 ASP A N   
887  C CA  . ASP A 129 ? 0.45920 0.50228 0.32397 -0.09513 -0.03021 -0.09539 124 ASP A CA  
888  C C   . ASP A 129 ? 0.52379 0.56617 0.36879 -0.09284 -0.02548 -0.10900 124 ASP A C   
889  O O   . ASP A 129 ? 0.43713 0.46338 0.28325 -0.09421 -0.02192 -0.12784 124 ASP A O   
890  C CB  . ASP A 129 ? 0.52553 0.59032 0.39320 -0.10896 -0.04126 -0.09751 124 ASP A CB  
891  C CG  . ASP A 129 ? 0.55617 0.62004 0.44800 -0.11919 -0.04685 -0.08960 124 ASP A CG  
892  O OD1 . ASP A 129 ? 0.51967 0.56147 0.42512 -0.11798 -0.04311 -0.08642 124 ASP A OD1 
893  O OD2 . ASP A 129 ? 0.58829 0.67708 0.48653 -0.13045 -0.05620 -0.08445 124 ASP A OD2 
894  N N   . ASP A 130 ? 0.60114 0.66495 0.42968 -0.08940 -0.02655 -0.09909 125 ASP A N   
895  C CA  . ASP A 130 ? 0.50937 0.58256 0.31884 -0.08829 -0.02128 -0.10436 125 ASP A CA  
896  C C   . ASP A 130 ? 0.53721 0.59033 0.35152 -0.07883 -0.01141 -0.10077 125 ASP A C   
897  O O   . ASP A 130 ? 0.51073 0.56158 0.32170 -0.07817 -0.00369 -0.11653 125 ASP A O   
898  C CB  . ASP A 130 ? 0.65804 0.75811 0.45381 -0.08876 -0.02830 -0.08535 125 ASP A CB  
899  C CG  . ASP A 130 ? 0.86227 0.99087 0.63456 -0.09590 -0.02698 -0.09075 125 ASP A CG  
900  O OD1 . ASP A 130 ? 1.08221 1.21103 0.84815 -0.09627 -0.01757 -0.10965 125 ASP A OD1 
901  O OD2 . ASP A 130 ? 0.84655 1.00168 0.60771 -0.10047 -0.03594 -0.07512 125 ASP A OD2 
902  N N   . ALA A 131 ? 0.45550 0.49634 0.27893 -0.07046 -0.01231 -0.08198 126 ALA A N   
903  C CA  . ALA A 131 ? 0.54449 0.57000 0.37070 -0.06313 -0.00582 -0.07508 126 ALA A CA  
904  C C   . ALA A 131 ? 0.52370 0.52798 0.36303 -0.06106 0.00215  -0.08876 126 ALA A C   
905  O O   . ALA A 131 ? 0.51829 0.51916 0.35753 -0.05780 0.00940  -0.09121 126 ALA A O   
906  C CB  . ALA A 131 ? 0.46975 0.48451 0.30351 -0.05395 -0.01162 -0.05637 126 ALA A CB  
907  N N   . VAL A 132 ? 0.52859 0.52066 0.38203 -0.06363 -0.00038 -0.09505 127 VAL A N   
908  C CA  . VAL A 132 ? 0.54189 0.51061 0.41212 -0.06153 0.00385  -0.10254 127 VAL A CA  
909  C C   . VAL A 132 ? 0.49251 0.45985 0.36178 -0.06183 0.00825  -0.12583 127 VAL A C   
910  O O   . VAL A 132 ? 0.54578 0.49904 0.42672 -0.05546 0.01369  -0.13151 127 VAL A O   
911  C CB  . VAL A 132 ? 0.51616 0.47483 0.40420 -0.06738 -0.00244 -0.09868 127 VAL A CB  
912  C CG1 . VAL A 132 ? 0.49137 0.45508 0.38075 -0.07890 -0.01010 -0.11214 127 VAL A CG1 
913  C CG2 . VAL A 132 ? 0.60994 0.54442 0.51722 -0.06508 -0.00044 -0.09850 127 VAL A CG2 
914  N N   . VAL A 133 ? 0.51981 0.50480 0.37599 -0.06780 0.00549  -0.14148 128 VAL A N   
915  C CA  . VAL A 133 ? 0.51268 0.50396 0.36526 -0.06510 0.01004  -0.16918 128 VAL A CA  
916  C C   . VAL A 133 ? 0.59173 0.60440 0.43338 -0.05794 0.02139  -0.16491 128 VAL A C   
917  O O   . VAL A 133 ? 0.55785 0.56772 0.40941 -0.04945 0.02871  -0.17911 128 VAL A O   
918  C CB  . VAL A 133 ? 0.55127 0.56318 0.38815 -0.07374 0.00359  -0.18806 128 VAL A CB  
919  C CG1 . VAL A 133 ? 0.58476 0.61523 0.41213 -0.06809 0.00989  -0.22009 128 VAL A CG1 
920  C CG2 . VAL A 133 ? 0.62784 0.61630 0.48149 -0.08271 -0.00924 -0.19470 128 VAL A CG2 
921  N N   . ALA A 134 ? 0.57698 0.61282 0.40114 -0.06168 0.02144  -0.14339 129 ALA A N   
922  C CA  . ALA A 134 ? 0.61522 0.67384 0.43125 -0.05918 0.02964  -0.13288 129 ALA A CA  
923  C C   . ALA A 134 ? 0.55335 0.58740 0.38826 -0.05172 0.03359  -0.12148 129 ALA A C   
924  O O   . ALA A 134 ? 0.55527 0.60326 0.39366 -0.04747 0.04225  -0.12365 129 ALA A O   
925  C CB  . ALA A 134 ? 0.64107 0.72260 0.43958 -0.06689 0.02372  -0.10670 129 ALA A CB  
926  N N   . HIS A 135 ? 0.49281 0.49606 0.34012 -0.05028 0.02730  -0.10945 130 HIS A N   
927  C CA  . HIS A 135 ? 0.52193 0.50339 0.38560 -0.04414 0.02931  -0.09884 130 HIS A CA  
928  C C   . HIS A 135 ? 0.49671 0.46869 0.37809 -0.03768 0.03561  -0.11711 130 HIS A C   
929  O O   . HIS A 135 ? 0.49209 0.46831 0.38149 -0.03258 0.04169  -0.11335 130 HIS A O   
930  C CB  . HIS A 135 ? 0.46548 0.42458 0.33704 -0.04369 0.02159  -0.08677 130 HIS A CB  
931  C CG  . HIS A 135 ? 0.49832 0.43832 0.38462 -0.03832 0.02240  -0.07742 130 HIS A CG  
932  N ND1 . HIS A 135 ? 0.51570 0.45649 0.40100 -0.03576 0.02350  -0.06494 130 HIS A ND1 
933  C CD2 . HIS A 135 ? 0.54016 0.46236 0.44264 -0.03692 0.02056  -0.07659 130 HIS A CD2 
934  C CE1 . HIS A 135 ? 0.53106 0.45515 0.42976 -0.03187 0.02268  -0.05943 130 HIS A CE1 
935  N NE2 . HIS A 135 ? 0.51438 0.42869 0.42313 -0.03242 0.02131  -0.06536 130 HIS A NE2 
936  N N   . VAL A 136 ? 0.44502 0.40343 0.33591 -0.03784 0.03218  -0.13650 131 VAL A N   
937  C CA  . VAL A 136 ? 0.51202 0.45388 0.42601 -0.02974 0.03407  -0.15327 131 VAL A CA  
938  C C   . VAL A 136 ? 0.52503 0.49550 0.43503 -0.02167 0.04406  -0.17419 131 VAL A C   
939  O O   . VAL A 136 ? 0.57247 0.54230 0.50021 -0.01160 0.04950  -0.17898 131 VAL A O   
940  C CB  . VAL A 136 ? 0.58344 0.49866 0.51308 -0.03342 0.02352  -0.16730 131 VAL A CB  
941  C CG1 . VAL A 136 ? 0.58492 0.47984 0.52458 -0.04083 0.01545  -0.14273 131 VAL A CG1 
942  C CG2 . VAL A 136 ? 0.69220 0.62189 0.60513 -0.04007 0.01965  -0.18596 131 VAL A CG2 
943  N N   . ASP A 137 ? 0.57320 0.57541 0.46030 -0.02569 0.04666  -0.18657 132 ASP A N   
944  C CA  . ASP A 137 ? 0.59884 0.64379 0.47756 -0.01908 0.05808  -0.20331 132 ASP A CA  
945  C C   . ASP A 137 ? 0.58467 0.64971 0.46435 -0.01873 0.06602  -0.17775 132 ASP A C   
946  O O   . ASP A 137 ? 0.61457 0.70040 0.50651 -0.00885 0.07527  -0.18762 132 ASP A O   
947  C CB  . ASP A 137 ? 0.67831 0.76209 0.52732 -0.02724 0.05859  -0.21255 132 ASP A CB  
948  C CG  . ASP A 137 ? 0.89084 0.96527 0.73999 -0.02527 0.05202  -0.24879 132 ASP A CG  
949  O OD1 . ASP A 137 ? 0.91287 0.94581 0.78806 -0.01839 0.04526  -0.26388 132 ASP A OD1 
950  O OD2 . ASP A 137 ? 1.03875 1.14312 0.86786 -0.03061 0.04988  -0.25292 132 ASP A OD2 
951  N N   . ASN A 138 ? 0.55227 0.61160 0.42166 -0.02905 0.06090  -0.14545 133 ASN A N   
952  C CA  . ASN A 138 ? 0.55964 0.63110 0.43213 -0.03144 0.06392  -0.11942 133 ASN A CA  
953  C C   . ASN A 138 ? 0.57059 0.61792 0.47005 -0.02194 0.06574  -0.11941 133 ASN A C   
954  O O   . ASN A 138 ? 0.55931 0.63056 0.46822 -0.01876 0.07298  -0.11453 133 ASN A O   
955  C CB  . ASN A 138 ? 0.55440 0.61131 0.41583 -0.04174 0.05320  -0.08935 133 ASN A CB  
956  C CG  . ASN A 138 ? 0.55456 0.62672 0.41643 -0.04826 0.05212  -0.06162 133 ASN A CG  
957  O OD1 . ASN A 138 ? 0.48372 0.59776 0.34329 -0.05135 0.06023  -0.05930 133 ASN A OD1 
958  N ND2 . ASN A 138 ? 0.49654 0.53749 0.36237 -0.05075 0.04099  -0.04098 133 ASN A ND2 
959  N N   . GLN A 139 ? 0.52131 0.52626 0.43459 -0.01855 0.05855  -0.12263 134 GLN A N   
960  C CA  . GLN A 139 ? 0.46666 0.44897 0.40580 -0.01105 0.05782  -0.11882 134 GLN A CA  
961  C C   . GLN A 139 ? 0.54326 0.54008 0.50228 0.00220  0.06556  -0.14292 134 GLN A C   
962  O O   . GLN A 139 ? 0.50877 0.51183 0.48639 0.00866  0.06916  -0.13645 134 GLN A O   
963  C CB  . GLN A 139 ? 0.43153 0.37374 0.38080 -0.01247 0.04774  -0.11573 134 GLN A CB  
964  C CG  . GLN A 139 ? 0.43213 0.36298 0.36782 -0.02086 0.04054  -0.09330 134 GLN A CG  
965  C CD  . GLN A 139 ? 0.53937 0.44288 0.48956 -0.02147 0.03290  -0.08491 134 GLN A CD  
966  O OE1 . GLN A 139 ? 0.53344 0.43123 0.48218 -0.02275 0.02918  -0.06749 134 GLN A OE1 
967  N NE2 . GLN A 139 ? 0.50454 0.39318 0.46908 -0.02155 0.02897  -0.09704 134 GLN A NE2 
968  N N   . ARG A 140 ? 0.51703 0.52005 0.47424 0.00765  0.06690  -0.17291 135 ARG A N   
969  C CA  . ARG A 140 ? 0.53360 0.54953 0.51233 0.02450  0.07269  -0.20234 135 ARG A CA  
970  C C   . ARG A 140 ? 0.51908 0.59192 0.49346 0.02895  0.08694  -0.20128 135 ARG A C   
971  O O   . ARG A 140 ? 0.60055 0.68639 0.60017 0.04310  0.09241  -0.21026 135 ARG A O   
972  C CB  . ARG A 140 ? 0.67374 0.68598 0.64866 0.02939  0.06916  -0.23901 135 ARG A CB  
973  C CG  . ARG A 140 ? 0.72756 0.68377 0.71959 0.02661  0.05309  -0.24294 135 ARG A CG  
974  N N   . ARG A 141 ? 0.50405 0.61523 0.44891 0.01634  0.09207  -0.18816 136 ARG A N   
975  C CA  . ARG A 141 ? 0.52006 0.69195 0.46113 0.01561  0.10433  -0.17943 136 ARG A CA  
976  C C   . ARG A 141 ? 0.54404 0.70760 0.50170 0.01118  0.10251  -0.14693 136 ARG A C   
977  O O   . ARG A 141 ? 0.54036 0.74332 0.51380 0.01739  0.11156  -0.14568 136 ARG A O   
978  C CB  . ARG A 141 ? 0.57449 0.78766 0.48140 -0.00071 0.10639  -0.16613 136 ARG A CB  
979  C CG  . ARG A 141 ? 0.62560 0.85690 0.51250 0.00215  0.10801  -0.19907 136 ARG A CG  
980  C CD  . ARG A 141 ? 0.62728 0.90535 0.48062 -0.01558 0.10880  -0.18075 136 ARG A CD  
981  N N   . VAL A 142 ? 0.49863 0.61458 0.45383 0.00116  0.09043  -0.12237 137 VAL A N   
982  C CA  . VAL A 142 ? 0.42449 0.52703 0.39468 -0.00287 0.08581  -0.09528 137 VAL A CA  
983  C C   . VAL A 142 ? 0.44498 0.54013 0.44832 0.01316  0.08850  -0.10781 137 VAL A C   
984  O O   . VAL A 142 ? 0.52061 0.63583 0.54058 0.01371  0.09099  -0.09353 137 VAL A O   
985  C CB  . VAL A 142 ? 0.49283 0.54626 0.45393 -0.01235 0.07193  -0.07560 137 VAL A CB  
986  C CG1 . VAL A 142 ? 0.41488 0.45152 0.39239 -0.01417 0.06567  -0.05452 137 VAL A CG1 
987  C CG2 . VAL A 142 ? 0.55208 0.61383 0.48630 -0.02661 0.06682  -0.05929 137 VAL A CG2 
988  N N   . LEU A 143 ? 0.42927 0.49501 0.44547 0.02555  0.08576  -0.13279 138 LEU A N   
989  C CA  . LEU A 143 ? 0.46968 0.51660 0.52142 0.04070  0.08305  -0.14163 138 LEU A CA  
990  C C   . LEU A 143 ? 0.53127 0.61515 0.60328 0.06071  0.09335  -0.17312 138 LEU A C   
991  O O   . LEU A 143 ? 0.59607 0.66702 0.70268 0.07655  0.09017  -0.18250 138 LEU A O   
992  C CB  . LEU A 143 ? 0.50710 0.49848 0.56723 0.04162  0.07020  -0.14747 138 LEU A CB  
993  C CG  . LEU A 143 ? 0.54277 0.50264 0.59090 0.02634  0.06018  -0.11738 138 LEU A CG  
994  C CD1 . LEU A 143 ? 0.56819 0.48997 0.61531 0.02256  0.04994  -0.12334 138 LEU A CD1 
995  C CD2 . LEU A 143 ? 0.54050 0.49176 0.61101 0.02811  0.05540  -0.09697 138 LEU A CD2 
996  N N   . SER A 144 ? 0.54959 0.68274 0.60179 0.06124  0.10486  -0.18977 139 SER A N   
997  C CA  . SER A 144 ? 0.56897 0.73755 0.63626 0.08328  0.11408  -0.23037 139 SER A CA  
998  C C   . SER A 144 ? 0.58709 0.79635 0.68624 0.09865  0.12273  -0.23081 139 SER A C   
999  O O   . SER A 144 ? 0.58273 0.81182 0.70590 0.12334  0.12759  -0.26748 139 SER A O   
1000 C CB  . SER A 144 ? 0.56544 0.78823 0.59914 0.07802  0.12494  -0.24584 139 SER A CB  
1001 O OG  . SER A 144 ? 0.58748 0.86305 0.60411 0.06171  0.13355  -0.21387 139 SER A OG  
1002 N N   . ALA A 145 ? 0.56200 0.78515 0.66400 0.08560  0.12345  -0.19277 140 ALA A N   
1003 C CA  . ALA A 145 ? 0.60471 0.86722 0.74050 0.09877  0.13005  -0.18980 140 ALA A CA  
1004 C C   . ALA A 145 ? 0.59706 0.80997 0.77315 0.11610  0.11844  -0.19632 140 ALA A C   
1005 O O   . ALA A 145 ? 0.61830 0.86195 0.82974 0.13485  0.12292  -0.20481 140 ALA A O   
1006 C CB  . ALA A 145 ? 0.60433 0.89353 0.73272 0.07660  0.13074  -0.14555 140 ALA A CB  
1007 N N   . LEU A 146 ? 0.52649 0.66832 0.70000 0.10977  0.10295  -0.19019 141 LEU A N   
1008 C CA  . LEU A 146 ? 0.49473 0.58811 0.70616 0.12309  0.08892  -0.19249 141 LEU A CA  
1009 C C   . LEU A 146 ? 0.57817 0.64181 0.80411 0.14139  0.08256  -0.23302 141 LEU A C   
1010 O O   . LEU A 146 ? 0.58845 0.63559 0.78682 0.13302  0.08118  -0.24656 141 LEU A O   
1011 C CB  . LEU A 146 ? 0.45556 0.49489 0.65763 0.10300  0.07407  -0.15761 141 LEU A CB  
1012 C CG  . LEU A 146 ? 0.44964 0.50658 0.63463 0.08349  0.07565  -0.12026 141 LEU A CG  
1013 C CD1 . LEU A 146 ? 0.47413 0.48034 0.65363 0.06926  0.06022  -0.09385 141 LEU A CD1 
1014 C CD2 . LEU A 146 ? 0.41501 0.51536 0.62921 0.09294  0.08120  -0.11270 141 LEU A CD2 
1015 N N   . SER A 147 ? 0.61521 0.66934 0.88706 0.16624  0.07606  -0.25200 142 SER A N   
1016 C CA  . SER A 147 ? 0.67834 0.69128 0.96505 0.18029  0.06288  -0.28446 142 SER A CA  
1017 C C   . SER A 147 ? 0.69015 0.63087 0.97581 0.16280  0.04281  -0.26507 142 SER A C   
1018 O O   . SER A 147 ? 0.65176 0.57667 0.92726 0.14314  0.03941  -0.22710 142 SER A O   
1019 C CB  . SER A 147 ? 0.68028 0.69371 1.00807 0.20422  0.05509  -0.29520 142 SER A CB  
1020 O OG  . SER A 147 ? 0.71340 0.68264 1.07467 0.20202  0.03819  -0.26647 142 SER A OG  
1021 N N   . ALA A 148 ? 0.73014 0.63313 1.01559 0.16315  0.02751  -0.28058 143 ALA A N   
1022 C CA  . ALA A 148 ? 0.69864 0.54210 0.98450 0.14427  0.00770  -0.25911 143 ALA A CA  
1023 C C   . ALA A 148 ? 0.68735 0.50231 1.00679 0.14153  -0.00614 -0.22450 143 ALA A C   
1024 O O   . ALA A 148 ? 0.60092 0.39488 0.91248 0.12198  -0.01147 -0.19268 143 ALA A O   
1025 C CB  . ALA A 148 ? 0.72519 0.53860 1.01502 0.14658  -0.00788 -0.28121 143 ALA A CB  
1026 N N   . ALA A 149 ? 0.71588 0.53403 1.07203 0.16074  -0.01234 -0.22920 144 ALA A N   
1027 C CA  . ALA A 149 ? 0.70207 0.49943 1.09038 0.15799  -0.02648 -0.19433 144 ALA A CA  
1028 C C   . ALA A 149 ? 0.69031 0.51322 1.07408 0.15123  -0.01442 -0.16765 144 ALA A C   
1029 O O   . ALA A 149 ? 0.71040 0.51217 1.10244 0.13681  -0.02625 -0.13022 144 ALA A O   
1030 C CB  . ALA A 149 ? 0.71106 0.51286 1.14000 0.18209  -0.03425 -0.20746 144 ALA A CB  
1031 N N   . GLU A 150 ? 0.65201 0.52674 1.01813 0.15783  0.00838  -0.18217 145 GLU A N   
1032 C CA  . GLU A 150 ? 0.60226 0.50901 0.94331 0.14027  0.01821  -0.14692 145 GLU A CA  
1033 C C   . GLU A 150 ? 0.63172 0.51773 0.92924 0.11145  0.01596  -0.12219 145 GLU A C   
1034 O O   . GLU A 150 ? 0.61449 0.49797 0.90275 0.09568  0.01123  -0.08775 145 GLU A O   
1035 C CB  . GLU A 150 ? 0.57947 0.55155 0.90508 0.14725  0.04068  -0.16142 145 GLU A CB  
1036 C CG  . GLU A 150 ? 0.61398 0.62426 0.98318 0.17268  0.04497  -0.17264 145 GLU A CG  
1037 C CD  . GLU A 150 ? 0.60353 0.68747 0.95921 0.18020  0.06791  -0.19120 145 GLU A CD  
1038 O OE1 . GLU A 150 ? 0.62480 0.72377 0.94745 0.17613  0.07845  -0.21238 145 GLU A OE1 
1039 O OE2 . GLU A 150 ? 0.63732 0.76894 1.01617 0.18892  0.07480  -0.18250 145 GLU A OE2 
1040 N N   . GLN A 151 ? 0.65268 0.52663 0.92390 0.10536  0.01859  -0.14107 146 GLN A N   
1041 C CA  . GLN A 151 ? 0.56236 0.41923 0.79662 0.08094  0.01581  -0.11996 146 GLN A CA  
1042 C C   . GLN A 151 ? 0.59070 0.40548 0.84229 0.07037  -0.00394 -0.09458 146 GLN A C   
1043 O O   . GLN A 151 ? 0.58853 0.40383 0.82158 0.05337  -0.00668 -0.06409 146 GLN A O   
1044 C CB  . GLN A 151 ? 0.59253 0.44951 0.79925 0.07781  0.02171  -0.14607 146 GLN A CB  
1045 C CG  . GLN A 151 ? 0.56562 0.47312 0.75074 0.08412  0.04105  -0.16486 146 GLN A CG  
1046 C CD  . GLN A 151 ? 0.60570 0.51858 0.76167 0.07993  0.04599  -0.18890 146 GLN A CD  
1047 O OE1 . GLN A 151 ? 0.63867 0.52477 0.77618 0.06476  0.03838  -0.18041 146 GLN A OE1 
1048 N NE2 . GLN A 151 ? 0.56621 0.52017 0.71798 0.09330  0.05885  -0.21907 146 GLN A NE2 
1049 N N   . ARG A 152 ? 0.59752 0.37777 0.88627 0.08007  -0.01943 -0.10624 147 ARG A N   
1050 C CA  . ARG A 152 ? 0.58062 0.32552 0.89086 0.06763  -0.04058 -0.07564 147 ARG A CA  
1051 C C   . ARG A 152 ? 0.60158 0.36123 0.92366 0.06517  -0.04370 -0.04216 147 ARG A C   
1052 O O   . ARG A 152 ? 0.59097 0.34640 0.90340 0.04637  -0.05236 -0.00828 147 ARG A O   
1053 C CB  . ARG A 152 ? 0.62874 0.34685 0.96967 0.07590  -0.05794 -0.08802 147 ARG A CB  
1054 N N   . GLN A 153 ? 0.58720 0.37027 0.92982 0.08393  -0.03661 -0.05193 148 GLN A N   
1055 C CA  . GLN A 153 ? 0.62591 0.42669 0.98257 0.08272  -0.04026 -0.02240 148 GLN A CA  
1056 C C   . GLN A 153 ? 0.63049 0.45754 0.94200 0.06321  -0.03031 -0.00112 148 GLN A C   
1057 O O   . GLN A 153 ? 0.61683 0.44538 0.92582 0.05021  -0.03971 0.03051  148 GLN A O   
1058 C CB  . GLN A 153 ? 0.66036 0.48879 1.04745 0.10774  -0.03227 -0.04205 148 GLN A CB  
1059 C CG  . GLN A 153 ? 0.75487 0.59859 1.17262 0.11252  -0.04003 -0.01681 148 GLN A CG  
1060 C CD  . GLN A 153 ? 0.90577 0.77984 1.35867 0.14088  -0.03161 -0.04268 148 GLN A CD  
1061 O OE1 . GLN A 153 ? 0.96882 0.86596 1.40974 0.15241  -0.01492 -0.07646 148 GLN A OE1 
1062 N NE2 . GLN A 153 ? 0.94623 0.82556 1.44358 0.15286  -0.04332 -0.02720 148 GLN A NE2 
1063 N N   . LEU A 154 ? 0.55623 0.40523 0.83256 0.06129  -0.01289 -0.01874 149 LEU A N   
1064 C CA  . LEU A 154 ? 0.54280 0.41067 0.77918 0.04451  -0.00644 -0.00198 149 LEU A CA  
1065 C C   . LEU A 154 ? 0.56939 0.41770 0.78200 0.02677  -0.01477 0.01458  149 LEU A C   
1066 O O   . LEU A 154 ? 0.52467 0.38253 0.71924 0.01478  -0.01837 0.03605  149 LEU A O   
1067 C CB  . LEU A 154 ? 0.53697 0.42956 0.74534 0.04554  0.01060  -0.02188 149 LEU A CB  
1068 C CG  . LEU A 154 ? 0.51923 0.42794 0.69037 0.03021  0.01516  -0.00803 149 LEU A CG  
1069 C CD1 . LEU A 154 ? 0.49240 0.41530 0.67366 0.02627  0.00922  0.01440  149 LEU A CD1 
1070 C CD2 . LEU A 154 ? 0.49074 0.42649 0.64410 0.03171  0.02942  -0.02403 149 LEU A CD2 
1071 N N   . ALA A 155 ? 0.57974 0.40434 0.79308 0.02497  -0.01868 0.00388  150 ALA A N   
1072 C CA  . ALA A 155 ? 0.55471 0.36929 0.74814 0.00761  -0.02589 0.02065  150 ALA A CA  
1073 C C   . ALA A 155 ? 0.59259 0.40183 0.80674 -0.00094 -0.04218 0.05271  150 ALA A C   
1074 O O   . ALA A 155 ? 0.51469 0.33615 0.70696 -0.01573 -0.04554 0.07324  150 ALA A O   
1075 C CB  . ALA A 155 ? 0.54384 0.33679 0.73758 0.00583  -0.02812 0.00331  150 ALA A CB  
1076 N N   . LYS A 156 ? 0.58037 0.37507 0.83758 0.00881  -0.05327 0.05749  151 LYS A N   
1077 C CA  . LYS A 156 ? 0.56048 0.35295 0.83977 -0.00054 -0.07092 0.09267  151 LYS A CA  
1078 C C   . LYS A 156 ? 0.56999 0.39423 0.83258 -0.00498 -0.06802 0.11109  151 LYS A C   
1079 O O   . LYS A 156 ? 0.55645 0.39515 0.80610 -0.02051 -0.07614 0.13835  151 LYS A O   
1080 C CB  . LYS A 156 ? 0.52860 0.29757 0.86048 0.01290  -0.08563 0.09228  151 LYS A CB  
1081 N N   . LEU A 157 ? 0.56858 0.40825 0.83084 0.00736  -0.05722 0.09648  152 LEU A N   
1082 C CA  . LEU A 157 ? 0.55416 0.42168 0.80189 0.00176  -0.05690 0.11229  152 LEU A CA  
1083 C C   . LEU A 157 ? 0.54134 0.42279 0.74011 -0.01204 -0.05091 0.11269  152 LEU A C   
1084 O O   . LEU A 157 ? 0.47927 0.37814 0.66343 -0.02284 -0.05836 0.13223  152 LEU A O   
1085 C CB  . LEU A 157 ? 0.48337 0.36706 0.74377 0.01568  -0.04731 0.09754  152 LEU A CB  
1086 C CG  . LEU A 157 ? 0.50421 0.38321 0.81679 0.03353  -0.05350 0.09576  152 LEU A CG  
1087 C CD1 . LEU A 157 ? 0.52226 0.42791 0.84369 0.04734  -0.03999 0.07743  152 LEU A CD1 
1088 C CD2 . LEU A 157 ? 0.56449 0.44713 0.90303 0.02867  -0.07194 0.12896  152 LEU A CD2 
1089 N N   . LEU A 158 ? 0.47970 0.35576 0.65340 -0.01075 -0.03864 0.09009  153 LEU A N   
1090 C CA  . LEU A 158 ? 0.45664 0.34325 0.58843 -0.02055 -0.03478 0.08817  153 LEU A CA  
1091 C C   . LEU A 158 ? 0.51095 0.40203 0.63350 -0.03242 -0.04307 0.10526  153 LEU A C   
1092 O O   . LEU A 158 ? 0.60680 0.51789 0.70152 -0.03968 -0.04462 0.11102  153 LEU A O   
1093 C CB  . LEU A 158 ? 0.36424 0.24391 0.47610 -0.01657 -0.02221 0.06353  153 LEU A CB  
1094 C CG  . LEU A 158 ? 0.45775 0.34561 0.57014 -0.00929 -0.01339 0.05064  153 LEU A CG  
1095 C CD1 . LEU A 158 ? 0.44281 0.32675 0.54024 -0.00603 -0.00230 0.02927  153 LEU A CD1 
1096 C CD2 . LEU A 158 ? 0.50267 0.40442 0.59554 -0.01582 -0.01692 0.05870  153 LEU A CD2 
1097 N N   . ASP A 159 ? 0.49844 0.37397 0.64547 -0.03482 -0.04981 0.11353  154 ASP A N   
1098 C CA  . ASP A 159 ? 0.45223 0.33909 0.59458 -0.04965 -0.05903 0.13610  154 ASP A CA  
1099 C C   . ASP A 159 ? 0.56311 0.47505 0.70865 -0.05770 -0.07014 0.16467  154 ASP A C   
1100 O O   . ASP A 159 ? 0.54579 0.48878 0.66568 -0.06841 -0.07183 0.17668  154 ASP A O   
1101 C CB  . ASP A 159 ? 0.53982 0.40013 0.71412 -0.05286 -0.06810 0.14185  154 ASP A CB  
1102 C CG  . ASP A 159 ? 0.62362 0.49965 0.79921 -0.07225 -0.08007 0.17240  154 ASP A CG  
1103 O OD1 . ASP A 159 ? 0.60825 0.51563 0.75030 -0.08075 -0.07399 0.17478  154 ASP A OD1 
1104 O OD2 . ASP A 159 ? 0.66355 0.52227 0.87601 -0.07881 -0.09654 0.19421  154 ASP A OD2 
1105 N N   . LYS A 160 ? 0.54400 0.44802 0.72076 -0.05162 -0.07780 0.17456  155 LYS A N   
1106 C CA  . LYS A 160 ? 0.59898 0.52849 0.78076 -0.05978 -0.09016 0.20347  155 LYS A CA  
1107 C C   . LYS A 160 ? 0.58164 0.53929 0.72633 -0.06055 -0.08445 0.19468  155 LYS A C   
1108 O O   . LYS A 160 ? 0.63205 0.62250 0.75787 -0.07154 -0.09142 0.21178  155 LYS A O   
1109 C CB  . LYS A 160 ? 0.59777 0.51147 0.82584 -0.05054 -0.10030 0.21421  155 LYS A CB  
1110 C CG  . LYS A 160 ? 0.58953 0.52771 0.83128 -0.06016 -0.11680 0.24891  155 LYS A CG  
1111 C CD  . LYS A 160 ? 0.65862 0.58323 0.94987 -0.04813 -0.12595 0.25122  155 LYS A CD  
1112 C CE  . LYS A 160 ? 0.67709 0.63286 0.98162 -0.05821 -0.14145 0.28083  155 LYS A CE  
1113 N NZ  . LYS A 160 ? 0.74268 0.68655 1.09688 -0.04527 -0.15046 0.28295  155 LYS A NZ  
1114 N N   . LEU A 161 ? 0.56339 0.51053 0.69804 -0.04979 -0.07353 0.16838  156 LEU A N   
1115 C CA  . LEU A 161 ? 0.49272 0.45824 0.59399 -0.05127 -0.07133 0.15757  156 LEU A CA  
1116 C C   . LEU A 161 ? 0.55547 0.53802 0.61888 -0.05719 -0.06857 0.15046  156 LEU A C   
1117 O O   . LEU A 161 ? 0.55543 0.56602 0.59516 -0.06248 -0.07447 0.15355  156 LEU A O   
1118 C CB  . LEU A 161 ? 0.43918 0.38843 0.53898 -0.04162 -0.06136 0.13388  156 LEU A CB  
1119 C CG  . LEU A 161 ? 0.50160 0.45976 0.57423 -0.04357 -0.06259 0.12225  156 LEU A CG  
1120 C CD1 . LEU A 161 ? 0.50029 0.47925 0.57809 -0.04963 -0.07570 0.13872  156 LEU A CD1 
1121 C CD2 . LEU A 161 ? 0.49928 0.44317 0.57662 -0.03734 -0.05376 0.10583  156 LEU A CD2 
1122 N N   . LEU A 162 ? 0.55243 0.52212 0.61090 -0.05553 -0.06021 0.13961  157 LEU A N   
1123 C CA  . LEU A 162 ? 0.60945 0.59793 0.63524 -0.05815 -0.05600 0.12983  157 LEU A CA  
1124 C C   . LEU A 162 ? 0.63399 0.66232 0.65245 -0.06996 -0.06390 0.15319  157 LEU A C   
1125 O O   . LEU A 162 ? 0.58924 0.65017 0.57736 -0.07036 -0.06414 0.14561  157 LEU A O   
1126 C CB  . LEU A 162 ? 0.63120 0.60043 0.65931 -0.05568 -0.04712 0.11799  157 LEU A CB  
1127 C CG  . LEU A 162 ? 0.65595 0.61159 0.66323 -0.04668 -0.03742 0.09002  157 LEU A CG  
1128 C CD1 . LEU A 162 ? 0.67291 0.61641 0.68531 -0.04749 -0.03129 0.08429  157 LEU A CD1 
1129 C CD2 . LEU A 162 ? 0.61283 0.59251 0.58731 -0.04443 -0.03851 0.07887  157 LEU A CD2 
1130 N N   . GLN A 163 ? 0.66067 0.68919 0.70777 -0.07965 -0.07160 0.18165  158 GLN A N   
1131 C CA  . GLN A 163 ? 0.71557 0.78813 0.75848 -0.09482 -0.08057 0.21133  158 GLN A CA  
1132 C C   . GLN A 163 ? 0.84750 0.95181 0.87838 -0.09762 -0.08894 0.22117  158 GLN A C   
1133 O O   . GLN A 163 ? 0.92768 1.08311 0.93681 -0.10705 -0.09263 0.23365  158 GLN A O   
1134 C CB  . GLN A 163 ? 0.68469 0.74331 0.76714 -0.10640 -0.09148 0.24360  158 GLN A CB  
1135 C CG  . GLN A 163 ? 0.70083 0.74271 0.79034 -0.11014 -0.08699 0.23910  158 GLN A CG  
1136 N N   . GLY A 164 ? 0.83495 0.91549 0.87929 -0.09004 -0.09215 0.21546  159 GLY A N   
1137 C CA  . GLY A 164 ? 0.76667 0.87432 0.79734 -0.09217 -0.10064 0.21920  159 GLY A CA  
1138 C C   . GLY A 164 ? 0.75753 0.88609 0.74493 -0.08677 -0.09635 0.18932  159 GLY A C   
1139 O O   . GLY A 164 ? 0.85919 1.01488 0.83057 -0.08963 -0.10531 0.18940  159 GLY A O   
1140 N N   . GLN A 165 ? 0.74324 0.85920 0.71313 -0.07840 -0.08497 0.16296  160 GLN A N   
1141 C CA  . GLN A 165 ? 0.71955 0.85112 0.65238 -0.07011 -0.08305 0.13177  160 GLN A CA  
1142 C C   . GLN A 165 ? 0.70822 0.89273 0.61768 -0.07362 -0.08022 0.13389  160 GLN A C   
1143 O O   . GLN A 165 ? 0.68479 0.91310 0.59515 -0.08634 -0.08623 0.16172  160 GLN A O   
1144 C CB  . GLN A 165 ? 0.66783 0.75647 0.59741 -0.05756 -0.07438 0.10229  160 GLN A CB  
1145 C CG  . GLN A 165 ? 0.58830 0.63300 0.54297 -0.05525 -0.07416 0.10254  160 GLN A CG  
1146 C CD  . GLN A 165 ? 0.63408 0.68314 0.59444 -0.05918 -0.08597 0.10964  160 GLN A CD  
1147 O OE1 . GLN A 165 ? 0.68562 0.74411 0.62341 -0.05772 -0.09423 0.09340  160 GLN A OE1 
1148 N NE2 . GLN A 165 ? 0.58121 0.62340 0.57393 -0.06348 -0.08855 0.13274  160 GLN A NE2 
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