data_8YLL
# 
_entry.id   8YLL 
# 
_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   8YLL         pdb_00008yll 10.2210/pdb8yll/pdb 
WWPDB D_1300045764 ?            ?                   
# 
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                        8YLL 
_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 non-polymer syn XANTHINE                                152.111   1  ? ? ? ? 
3 water       nat water                                   18.015    11 ? ? ? ? 
# 
_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         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 XANTHINE XAN 
3 water    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 
XAN non-polymer         . XANTHINE        ? 'C5 H4 N4 O2'    152.111 
# 
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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XAN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XAN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 XAN 1  201 1  XAN XAN A . 
C 3 HOH 1  301 17 HOH HOH A . 
C 3 HOH 2  302 30 HOH HOH A . 
C 3 HOH 3  303 13 HOH HOH A . 
C 3 HOH 4  304 8  HOH HOH A . 
C 3 HOH 5  305 3  HOH HOH A . 
C 3 HOH 6  306 7  HOH HOH A . 
C 3 HOH 7  307 2  HOH HOH A . 
C 3 HOH 8  308 9  HOH HOH A . 
C 3 HOH 9  309 10 HOH HOH A . 
C 3 HOH 10 310 16 HOH HOH A . 
C 3 HOH 11 311 32 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 GLN 51  ? CG  ? A GLN 56  CG  
2  1 Y 1 A GLN 51  ? CD  ? A GLN 56  CD  
3  1 Y 1 A GLN 51  ? OE1 ? A GLN 56  OE1 
4  1 Y 1 A GLN 51  ? NE2 ? A GLN 56  NE2 
5  1 Y 1 A ASN 88  ? CG  ? A ASN 93  CG  
6  1 Y 1 A ASN 88  ? OD1 ? A ASN 93  OD1 
7  1 Y 1 A ASN 88  ? ND2 ? A ASN 93  ND2 
8  1 Y 1 A LYS 95  ? CG  ? A LYS 100 CG  
9  1 Y 1 A LYS 95  ? CD  ? A LYS 100 CD  
10 1 Y 1 A LYS 95  ? CE  ? A LYS 100 CE  
11 1 Y 1 A LYS 95  ? NZ  ? A LYS 100 NZ  
12 1 Y 1 A ARG 136 ? CD  ? A ARG 141 CD  
13 1 Y 1 A ARG 136 ? NE  ? A ARG 141 NE  
14 1 Y 1 A ARG 136 ? CZ  ? A ARG 141 CZ  
15 1 Y 1 A ARG 136 ? NH1 ? A ARG 141 NH1 
16 1 Y 1 A ARG 136 ? NH2 ? A ARG 141 NH2 
17 1 Y 1 A ARG 147 ? CG  ? A ARG 152 CG  
18 1 Y 1 A ARG 147 ? CD  ? A ARG 152 CD  
19 1 Y 1 A ARG 147 ? NE  ? A ARG 152 NE  
20 1 Y 1 A ARG 147 ? CZ  ? A ARG 152 CZ  
21 1 Y 1 A ARG 147 ? NH1 ? A ARG 152 NH1 
22 1 Y 1 A ARG 147 ? NH2 ? A ARG 152 NH2 
23 1 Y 1 A LYS 151 ? CD  ? A LYS 156 CD  
24 1 Y 1 A LYS 151 ? CE  ? A LYS 156 CE  
25 1 Y 1 A LYS 151 ? NZ  ? A LYS 156 NZ  
26 1 Y 1 A LYS 155 ? NZ  ? A LYS 160 NZ  
# 
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                     8YLL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.462 
_cell.length_a_esd                 ? 
_cell.length_b                     62.462 
_cell.length_b_esd                 ? 
_cell.length_c                     77.060 
_cell.length_c_esd                 ? 
_cell.volume                       260370.279 
_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                         8YLL 
_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                   8YLL 
_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          48.02 
_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    'PEG 3350, ammonium formate' 
_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         2021-07-01 
_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                                       8YLL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               50.00 
_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                                     16422 
_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                                20.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          68.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             817 
_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                               20.2 
_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                                  0.717 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_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                               54.38 
_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                                 8YLL 
_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                            1.80 
_refine.ls_d_res_low                             28.94 
_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                     16366 
_refine.ls_number_reflns_R_free                  801 
_refine.ls_number_reflns_R_work                  15565 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.36 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2239 
_refine.ls_R_factor_R_free                       0.2459 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2227 
_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                          1.34 
_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                      8YLF 
_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                 33.2872 
_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                            0.2639 
_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                       1.80 
_refine_hist.d_res_low                        28.94 
_refine_hist.number_atoms_solvent             11 
_refine_hist.number_atoms_total               1177 
_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        1155 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_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' ? 0.0055  ? 1182 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7346  ? 1605 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0399  ? 188  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0047  ? 210  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.8084 ? 730  ? 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' 1.80 1.92  . . 113 2533 99.03 . . . . 0.3480 . . . . . . . . . . . 0.3914 
'X-RAY DIFFRACTION' 1.92 2.06  . . 118 2590 99.74 . . . . 0.2951 . . . . . . . . . . . 0.3336 
'X-RAY DIFFRACTION' 2.06 2.27  . . 131 2581 99.89 . . . . 0.2466 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 2.27 2.60  . . 153 2580 99.64 . . . . 0.2382 . . . . . . . . . . . 0.2703 
'X-RAY DIFFRACTION' 2.60 3.28  . . 159 2582 99.78 . . . . 0.2459 . . . . . . . . . . . 0.2514 
'X-RAY DIFFRACTION' 3.28 28.94 . . 127 2699 98.16 . . . . 0.1954 . . . . . . . . . . . 0.2245 
# 
_struct.entry_id                     8YLL 
_struct.title                        'Crystal structure of Burkholderia thailandensis MftR in complex with xanthine' 
_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        8YLL 
_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 ? 
C N N 3 ? 
# 
_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              8YLL 
_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 8YLL SER A 1 ? UNP A0A2N8QSC4 ? ? 'expression tag' -4 1 
1 8YLL ALA A 2 ? UNP A0A2N8QSC4 ? ? 'expression tag' -3 2 
1 8YLL LYS A 3 ? UNP A0A2N8QSC4 ? ? 'expression tag' -2 3 
1 8YLL ASP A 4 ? UNP A0A2N8QSC4 ? ? 'expression tag' -1 4 
1 8YLL 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)' 7760  ? 
1 MORE         -42   ? 
1 'SSA (A^2)'  12600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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' 4_556 y,x,-z+1 -0.5000000000 0.8660254038 0.0000000000 0.0000000000 0.8660254038 0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 77.0600000000 
# 
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 GLY A 58  ? SER A 69  ? GLY A 53  SER A 64  1 ? 12 
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 ? LEU A 143 ? THR A 116 LEU A 138 1 ? 23 
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       5.38 
# 
_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 VAL A 118 ? LEU A 120 ? VAL A 113 LEU A 115 
AA1 3 VAL A 104 ? ARG A 106 ? VAL A 99  ARG A 101 
# 
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 ALA A 119 ? O ALA A 114 N GLU A 105 ? N GLU A 100 
# 
_pdbx_entry_details.entry_id                   8YLL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 82  ? ? -83.05  48.62   
2 1 ARG A 102 ? ? -106.41 -139.76 
# 
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 7.83950476942 52.5636949537 39.9959139132 0.728296942444 ? 0.113974837516   ? 0.012076813682   ? 
0.371698763889 ? -0.0718250751302 ? 0.548624466855 ? 4.55137307817 ? -4.68929541822 ? -4.08803781467   ? 5.83485014766 ? 
3.03990316896 ? 5.82669429913 ? 0.227613302963  ? 0.0117529082356 ? 1.22579553062   ? 0.135638381158  ? 0.0543372928169  ? 
-0.601860040277  ? -1.55015830454  ? -0.886122054341 ? -0.314473423821  ? 
2 'X-RAY DIFFRACTION' ? refined 15.479276659  45.8585350394 40.551045856  0.404299293875 ? -0.0199862190129 ? 0.0116871173536  ? 
0.307289935717 ? -0.0118840328384 ? 0.29064986818  ? 8.62141101181 ? -4.51920220908 ? -4.83849636462   ? 3.78062711254 ? 
1.73062898077 ? 5.40417753742 ? 0.185455202944  ? -0.32337297759  ? 0.329645659737  ? 0.397336789885  ? -0.288369719659  ? 
0.39809346473    ? -0.476884367889 ? -0.402637995448 ? -0.0409478194844 ? 
3 'X-RAY DIFFRACTION' ? refined 25.3861770006 28.1602584621 25.6923972117 0.488702921589 ? 0.12778191218    ? -0.0450566945009 ? 
0.583550480687 ? -0.0770549184478 ? 0.314152551548 ? 8.28066309251 ? -5.75255968786 ? -0.544042830328  ? 6.71381507645 ? 
3.67864184848 ? 5.48079848748 ? 0.672583327761  ? 1.58359499586   ? -0.256134141084 ? 0.0174854004256 ? -0.828306163329  ? 
0.0654814828753  ? 0.244572006054  ? 0.297956697135  ? -0.0642620352734 ? 
4 'X-RAY DIFFRACTION' ? refined 35.3505581336 23.5049157867 38.0140733239 0.406128997461 ? 0.0174197097648  ? 0.061120044439   ? 
0.489924456666 ? 0.0506285054585  ? 0.295622360953 ? 8.41325958144 ? -3.67668592607 ? -0.0555577362986 ? 5.67903064904 ? 
1.6909603428  ? 5.38074846144 ? -0.118467600031 ? -0.198699434431 ? 0.136783336344  ? 0.324772051759  ? -0.0393106540293 ? 
-0.0655940282462 ? 0.334857518451  ? 0.422508468161  ? 0.0813470672407  ? 
5 'X-RAY DIFFRACTION' ? refined 31.9038107082 14.0607705868 35.3182562246 0.823728996717 ? 0.0675888354322  ? 0.206315225228   ? 
0.445201348096 ? 0.0824501834796  ? 0.433956821412 ? 5.34231047699 ? 2.34385258456  ? -2.15055267722   ? 4.84515642523 ? 
2.71017163848 ? 5.98233175342 ? -0.471589722491 ? -0.376206066783 ? -1.20541008621  ? 0.432634137062  ? -0.208418852447  ? 
0.191266536621   ? 1.46218853108   ? 0.0847933867442 ? 0.663923699382   ? 
6 'X-RAY DIFFRACTION' ? refined 33.1658190671 38.2848724921 31.6067797415 0.394496798946 ? -0.0906815933247 ? 0.107729226076   ? 
0.492325198788 ? 0.0434110838006  ? 0.401536838173 ? 2.85045593572 ? -2.16603946476 ? -0.889495624084  ? 4.99758690064 ? 
1.0494152803  ? 2.2626870425  ? 0.377321251514  ? 0.22224131715   ? 0.626696035742  ? -0.79659894314  ? 0.0136551391327  ? 
-0.712450068432  ? -0.410937058161 ? 0.505153417434  ? -0.39108877146   ? 
# 
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 14 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 15 through 39 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 40 through 53 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 54 through 85 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 86 through 116 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 117 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 
XAN N9   N Y N 377 
XAN C4   C Y N 378 
XAN N3   N Y N 379 
XAN C2   C Y N 380 
XAN O2   O N N 381 
XAN N1   N Y N 382 
XAN C6   C Y N 383 
XAN O6   O N N 384 
XAN C5   C Y N 385 
XAN N7   N Y N 386 
XAN C8   C Y N 387 
XAN HN9  H N N 388 
XAN HN3  H N N 389 
XAN HN1  H N N 390 
XAN H8   H N N 391 
# 
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 
XAN N9  C4   sing Y N 363 
XAN N9  C8   sing Y N 364 
XAN N9  HN9  sing N N 365 
XAN C4  N3   sing Y N 366 
XAN C4  C5   doub Y N 367 
XAN N3  C2   sing Y N 368 
XAN N3  HN3  sing N N 369 
XAN C2  O2   doub N N 370 
XAN C2  N1   sing Y N 371 
XAN N1  C6   sing Y N 372 
XAN N1  HN1  sing N N 373 
XAN C6  O6   doub N N 374 
XAN C6  C5   sing Y N 375 
XAN C5  N7   sing Y N 376 
XAN N7  C8   doub Y N 377 
XAN C8  H8   sing N N 378 
# 
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      PDB 
_pdbx_initial_refinement_model.accession_code   8YLF 
_pdbx_initial_refinement_model.details          ? 
# 
_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                    8YLL 
_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]   0.016010 
_atom_sites.fract_transf_matrix[1][2]   0.009243 
_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]   0.018486 
_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]   0.012977 
_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   ? 12.31581 54.96077 30.83876 1.000 78.81449  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 6   ? 12.21073 54.26114 32.12680 1.000 75.82402  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 6   ? 12.11097 52.74527 31.98056 1.000 68.49867  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 6   ? 11.27288 52.24338 31.23450 1.000 74.08843  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 6   ? 10.99739 54.75850 32.91537 1.000 78.45630  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 6   ? 11.31771 55.81078 33.96156 1.000 87.15038  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 6   ? 10.04549 55.93766 35.24062 1.000 87.76940  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 6   ? 10.69969 57.27617 36.23688 1.000 90.18885  ? 1   MET A CE  1 
ATOM   9    N N   . ASP A 1 7   ? 12.95273 52.01888 32.71639 1.000 58.97137  ? 2   ASP A N   1 
ATOM   10   C CA  . ASP A 1 7   ? 12.94536 50.56450 32.68620 1.000 55.16042  ? 2   ASP A CA  1 
ATOM   11   C C   . ASP A 1 7   ? 11.97965 50.02008 33.74080 1.000 50.70754  ? 2   ASP A C   1 
ATOM   12   O O   . ASP A 1 7   ? 11.30690 50.77254 34.45562 1.000 52.02023  ? 2   ASP A O   1 
ATOM   13   C CB  . ASP A 1 7   ? 14.36297 50.01482 32.88050 1.000 53.61287  ? 2   ASP A CB  1 
ATOM   14   C CG  . ASP A 1 7   ? 14.97450 50.39498 34.23096 1.000 52.57439  ? 2   ASP A CG  1 
ATOM   15   O OD1 . ASP A 1 7   ? 14.55339 51.39874 34.84304 1.000 55.21446  ? 2   ASP A OD1 1 
ATOM   16   O OD2 . ASP A 1 7   ? 15.90306 49.69027 34.67839 1.000 54.25712  ? 2   ASP A OD2 1 
ATOM   17   N N   . ARG A 1 8   ? 11.91515 48.68694 33.83025 1.000 42.35861  ? 3   ARG A N   1 
ATOM   18   C CA  . ARG A 1 8   ? 11.05263 48.02111 34.80322 1.000 43.45659  ? 3   ARG A CA  1 
ATOM   19   C C   . ARG A 1 8   ? 11.26932 48.57224 36.20248 1.000 39.65517  ? 3   ARG A C   1 
ATOM   20   O O   . ARG A 1 8   ? 10.31113 48.82597 36.93808 1.000 41.56132  ? 3   ARG A O   1 
ATOM   21   C CB  . ARG A 1 8   ? 11.32110 46.51215 34.81561 1.000 42.21003  ? 3   ARG A CB  1 
ATOM   22   C CG  . ARG A 1 8   ? 10.83077 45.75195 33.59421 1.000 41.70715  ? 3   ARG A CG  1 
ATOM   23   C CD  . ARG A 1 8   ? 11.29720 44.30272 33.60323 1.000 43.49169  ? 3   ARG A CD  1 
ATOM   24   N NE  . ARG A 1 8   ? 10.75948 43.59551 32.44043 1.000 45.31243  ? 3   ARG A NE  1 
ATOM   25   C CZ  . ARG A 1 8   ? 9.54620  43.05897 32.40316 1.000 47.91214  ? 3   ARG A CZ  1 
ATOM   26   N NH1 . ARG A 1 8   ? 8.76549  43.13492 33.46918 1.000 49.43057  ? 3   ARG A NH1 1 
ATOM   27   N NH2 . ARG A 1 8   ? 9.11266  42.45010 31.30343 1.000 53.43928  ? 3   ARG A NH2 1 
ATOM   28   N N   . ALA A 1 9   ? 12.53408 48.72979 36.59374 1.000 41.09794  ? 4   ALA A N   1 
ATOM   29   C CA  . ALA A 1 9   ? 12.84095 49.09336 37.97365 1.000 46.70675  ? 4   ALA A CA  1 
ATOM   30   C C   . ALA A 1 9   ? 12.42321 50.53135 38.27217 1.000 48.91534  ? 4   ALA A C   1 
ATOM   31   O O   . ALA A 1 9   ? 11.73465 50.79378 39.26695 1.000 45.60477  ? 4   ALA A O   1 
ATOM   32   C CB  . ALA A 1 9   ? 14.32708 48.87904 38.24851 1.000 48.22832  ? 4   ALA A CB  1 
ATOM   33   N N   . ALA A 1 10  ? 12.82842 51.48033 37.42031 1.000 45.31756  ? 5   ALA A N   1 
ATOM   34   C CA  . ALA A 1 10  ? 12.44945 52.87227 37.63933 1.000 52.56490  ? 5   ALA A CA  1 
ATOM   35   C C   . ALA A 1 10  ? 10.93562 53.04745 37.63394 1.000 50.80165  ? 5   ALA A C   1 
ATOM   36   O O   . ALA A 1 10  ? 10.38496 53.79269 38.45423 1.000 51.94579  ? 5   ALA A O   1 
ATOM   37   C CB  . ALA A 1 10  ? 13.09721 53.75904 36.57887 1.000 62.71141  ? 5   ALA A CB  1 
ATOM   38   N N   . HIS A 1 11  ? 10.24703 52.37954 36.70736 1.000 50.93156  ? 6   HIS A N   1 
ATOM   39   C CA  . HIS A 1 11  ? 8.79120  52.44169 36.68058 1.000 52.44823  ? 6   HIS A CA  1 
ATOM   40   C C   . HIS A 1 11  ? 8.19801  51.90767 37.97955 1.000 47.35146  ? 6   HIS A C   1 
ATOM   41   O O   . HIS A 1 11  ? 7.27051  52.50331 38.53791 1.000 47.70730  ? 6   HIS A O   1 
ATOM   42   C CB  . HIS A 1 11  ? 8.26595  51.65661 35.47899 1.000 54.91877  ? 6   HIS A CB  1 
ATOM   43   C CG  . HIS A 1 11  ? 6.77532  51.52625 35.43884 1.000 60.37698  ? 6   HIS A CG  1 
ATOM   44   N ND1 . HIS A 1 11  ? 5.93550  52.60626 35.26867 1.000 67.50282  ? 6   HIS A ND1 1 
ATOM   45   C CD2 . HIS A 1 11  ? 5.97343  50.43938 35.54242 1.000 61.47172  ? 6   HIS A CD2 1 
ATOM   46   C CE1 . HIS A 1 11  ? 4.68072  52.19080 35.27004 1.000 68.48784  ? 6   HIS A CE1 1 
ATOM   47   N NE2 . HIS A 1 11  ? 4.67614  50.87974 35.43495 1.000 64.60417  ? 6   HIS A NE2 1 
ATOM   48   N N   . ALA A 1 12  ? 8.72051  50.78317 38.47683 1.000 41.61918  ? 7   ALA A N   1 
ATOM   49   C CA  . ALA A 1 12  ? 8.18767  50.21980 39.71301 1.000 42.17789  ? 7   ALA A CA  1 
ATOM   50   C C   . ALA A 1 12  ? 8.42467  51.15530 40.89313 1.000 47.99935  ? 7   ALA A C   1 
ATOM   51   O O   . ALA A 1 12  ? 7.53280  51.33789 41.72722 1.000 47.44283  ? 7   ALA A O   1 
ATOM   52   C CB  . ALA A 1 12  ? 8.80585  48.84748 39.98247 1.000 40.62224  ? 7   ALA A CB  1 
ATOM   53   N N   . VAL A 1 13  ? 9.61227  51.76659 40.97394 1.000 47.00172  ? 8   VAL A N   1 
ATOM   54   C CA  . VAL A 1 13  ? 9.88550  52.71260 42.05573 1.000 49.83411  ? 8   VAL A CA  1 
ATOM   55   C C   . VAL A 1 13  ? 8.92416  53.88741 41.98487 1.000 53.67843  ? 8   VAL A C   1 
ATOM   56   O O   . VAL A 1 13  ? 8.43723  54.37695 43.01386 1.000 56.90563  ? 8   VAL A O   1 
ATOM   57   C CB  . VAL A 1 13  ? 11.35561 53.17324 42.01491 1.000 53.64171  ? 8   VAL A CB  1 
ATOM   58   C CG1 . VAL A 1 13  ? 11.55919 54.42292 42.86959 1.000 61.85335  ? 8   VAL A CG1 1 
ATOM   59   C CG2 . VAL A 1 13  ? 12.26092 52.05408 42.49787 1.000 52.45241  ? 8   VAL A CG2 1 
ATOM   60   N N   . GLU A 1 14  ? 8.61842  54.34580 40.77187 1.000 53.78392  ? 9   GLU A N   1 
ATOM   61   C CA  . GLU A 1 14  ? 7.67809  55.44720 40.61452 1.000 59.77789  ? 9   GLU A CA  1 
ATOM   62   C C   . GLU A 1 14  ? 6.30905  55.07445 41.16905 1.000 58.55308  ? 9   GLU A C   1 
ATOM   63   O O   . GLU A 1 14  ? 5.68741  55.85200 41.90554 1.000 59.81259  ? 9   GLU A O   1 
ATOM   64   C CB  . GLU A 1 14  ? 7.57911  55.84135 39.13850 1.000 60.41575  ? 9   GLU A CB  1 
ATOM   65   C CG  . GLU A 1 14  ? 6.65580  57.00573 38.87042 1.000 69.79330  ? 9   GLU A CG  1 
ATOM   66   C CD  . GLU A 1 14  ? 7.27779  58.34371 39.22890 1.000 79.97384  ? 9   GLU A CD  1 
ATOM   67   O OE1 . GLU A 1 14  ? 8.51519  58.48155 39.10432 1.000 81.48693  ? 9   GLU A OE1 1 
ATOM   68   O OE2 . GLU A 1 14  ? 6.52767  59.25760 39.63768 1.000 84.22180  ? 9   GLU A OE2 1 
ATOM   69   N N   . GLN A 1 15  ? 5.82374  53.87868 40.82631 1.000 52.84150  ? 10  GLN A N   1 
ATOM   70   C CA  . GLN A 1 15  ? 4.53616  53.43512 41.34404 1.000 48.82488  ? 10  GLN A CA  1 
ATOM   71   C C   . GLN A 1 15  ? 4.55966  53.32217 42.86317 1.000 48.45876  ? 10  GLN A C   1 
ATOM   72   O O   . GLN A 1 15  ? 3.57226  53.65530 43.52617 1.000 55.06246  ? 10  GLN A O   1 
ATOM   73   C CB  . GLN A 1 15  ? 4.14755  52.10406 40.70354 1.000 49.10382  ? 10  GLN A CB  1 
ATOM   74   C CG  . GLN A 1 15  ? 3.84219  52.21739 39.22831 1.000 49.22037  ? 10  GLN A CG  1 
ATOM   75   C CD  . GLN A 1 15  ? 3.29334  50.93478 38.64072 1.000 54.12391  ? 10  GLN A CD  1 
ATOM   76   O OE1 . GLN A 1 15  ? 3.81384  49.84750 38.89305 1.000 53.06183  ? 10  GLN A OE1 1 
ATOM   77   N NE2 . GLN A 1 15  ? 2.22886  51.05507 37.85530 1.000 53.12787  ? 10  GLN A NE2 1 
ATOM   78   N N   . TRP A 1 16  ? 5.67314  52.85503 43.43381 1.000 49.25074  ? 11  TRP A N   1 
ATOM   79   C CA  . TRP A 1 16  ? 5.74678  52.70663 44.88848 1.000 52.15568  ? 11  TRP A CA  1 
ATOM   80   C C   . TRP A 1 16  ? 5.70483  54.05574 45.58819 1.000 57.03970  ? 11  TRP A C   1 
ATOM   81   O O   . TRP A 1 16  ? 4.95886  54.23654 46.55831 1.000 64.50928  ? 11  TRP A O   1 
ATOM   82   C CB  . TRP A 1 16  ? 7.00645  51.93670 45.28304 1.000 52.51188  ? 11  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 16  ? 6.83603  50.44679 45.25781 1.000 45.94989  ? 11  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 16  ? 7.56911  49.54804 44.53882 1.000 46.35090  ? 11  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 16  ? 5.86751  49.68375 45.98736 1.000 48.13819  ? 11  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 16  ? 7.11875  48.26910 44.77912 1.000 47.24329  ? 11  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 16  ? 6.07819  48.32774 45.67131 1.000 44.33395  ? 11  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 16  ? 4.85287  50.01751 46.89845 1.000 58.29498  ? 11  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 16  ? 5.30034  47.30186 46.21911 1.000 45.86697  ? 11  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 16  ? 4.08198  48.99967 47.43960 1.000 60.34511  ? 11  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 16  ? 4.30884  47.66016 47.09707 1.000 50.62191  ? 11  TRP A CH2 1 
ATOM   92   N N   . ARG A 1 17  ? 6.50092  55.01781 45.11523 1.000 60.02829  ? 12  ARG A N   1 
ATOM   93   C CA  . ARG A 1 17  ? 6.45762  56.35802 45.69546 1.000 70.07487  ? 12  ARG A CA  1 
ATOM   94   C C   . ARG A 1 17  ? 5.04104  56.91569 45.70294 1.000 73.83664  ? 12  ARG A C   1 
ATOM   95   O O   . ARG A 1 17  ? 4.63146  57.58567 46.65836 1.000 75.75984  ? 12  ARG A O   1 
ATOM   96   C CB  . ARG A 1 17  ? 7.38392  57.29905 44.92717 1.000 75.11779  ? 12  ARG A CB  1 
ATOM   97   C CG  . ARG A 1 17  ? 8.83885  56.90230 44.94302 1.000 77.66627  ? 12  ARG A CG  1 
ATOM   98   C CD  . ARG A 1 17  ? 9.66348  57.93018 44.19469 1.000 84.29872  ? 12  ARG A CD  1 
ATOM   99   N NE  . ARG A 1 17  ? 11.04504 57.50079 44.01072 1.000 87.22531  ? 12  ARG A NE  1 
ATOM   100  C CZ  . ARG A 1 17  ? 11.99179 57.62051 44.93442 1.000 90.44411  ? 12  ARG A CZ  1 
ATOM   101  N NH1 . ARG A 1 17  ? 11.70569 58.15792 46.11478 1.000 92.47354  ? 12  ARG A NH1 1 
ATOM   102  N NH2 . ARG A 1 17  ? 13.22260 57.19857 44.67747 1.000 89.41385  ? 12  ARG A NH2 1 
ATOM   103  N N   . SER A 1 18  ? 4.27502  56.64983 44.64764 1.000 70.93733  ? 13  SER A N   1 
ATOM   104  C CA  . SER A 1 18  ? 2.90905  57.15279 44.59004 1.000 70.11177  ? 13  SER A CA  1 
ATOM   105  C C   . SER A 1 18  ? 1.95595  56.36931 45.48570 1.000 68.83714  ? 13  SER A C   1 
ATOM   106  O O   . SER A 1 18  ? 0.99234  56.94486 46.00083 1.000 74.21458  ? 13  SER A O   1 
ATOM   107  C CB  . SER A 1 18  ? 2.40258  57.12138 43.15179 1.000 73.81128  ? 13  SER A CB  1 
ATOM   108  O OG  . SER A 1 18  ? 0.99169  57.00393 43.14046 1.000 75.67563  ? 13  SER A OG  1 
ATOM   109  N N   . GLU A 1 19  ? 2.19566  55.07171 45.68001 1.000 68.02848  ? 14  GLU A N   1 
ATOM   110  C CA  . GLU A 1 19  ? 1.27422  54.20931 46.41349 1.000 61.29431  ? 14  GLU A CA  1 
ATOM   111  C C   . GLU A 1 19  ? 1.61191  54.07067 47.89279 1.000 65.81025  ? 14  GLU A C   1 
ATOM   112  O O   . GLU A 1 19  ? 0.70026  53.99676 48.71995 1.000 67.84545  ? 14  GLU A O   1 
ATOM   113  C CB  . GLU A 1 19  ? 1.22393  52.81802 45.77281 1.000 58.65689  ? 14  GLU A CB  1 
ATOM   114  C CG  . GLU A 1 19  ? 0.39908  52.76487 44.48799 1.000 56.99453  ? 14  GLU A CG  1 
ATOM   115  C CD  . GLU A 1 19  ? -1.08259 52.97071 44.75173 1.000 66.41010  ? 14  GLU A CD  1 
ATOM   116  O OE1 . GLU A 1 19  ? -1.56857 52.52324 45.81753 1.000 64.93749  ? 14  GLU A OE1 1 
ATOM   117  O OE2 . GLU A 1 19  ? -1.76341 53.58587 43.90477 1.000 68.08401  ? 14  GLU A OE2 1 
ATOM   118  N N   . ARG A 1 20  ? 2.89230  54.01768 48.24882 1.000 65.74169  ? 15  ARG A N   1 
ATOM   119  C CA  . ARG A 1 20  ? 3.32405  53.92637 49.64308 1.000 68.44694  ? 15  ARG A CA  1 
ATOM   120  C C   . ARG A 1 20  ? 4.30507  55.05410 49.93152 1.000 67.39282  ? 15  ARG A C   1 
ATOM   121  O O   . ARG A 1 20  ? 5.51148  54.82718 50.08448 1.000 64.86381  ? 15  ARG A O   1 
ATOM   122  C CB  . ARG A 1 20  ? 3.94978  52.56228 49.93706 1.000 68.17429  ? 15  ARG A CB  1 
ATOM   123  C CG  . ARG A 1 20  ? 2.98532  51.39271 49.83143 1.000 63.03094  ? 15  ARG A CG  1 
ATOM   124  C CD  . ARG A 1 20  ? 1.96482  51.43416 50.92999 1.000 68.78815  ? 15  ARG A CD  1 
ATOM   125  N NE  . ARG A 1 20  ? 2.59543  51.52809 52.24225 1.000 70.51467  ? 15  ARG A NE  1 
ATOM   126  C CZ  . ARG A 1 20  ? 2.96140  50.48330 52.97731 1.000 67.07401  ? 15  ARG A CZ  1 
ATOM   127  N NH1 . ARG A 1 20  ? 2.76536  49.24821 52.53713 1.000 65.24769  ? 15  ARG A NH1 1 
ATOM   128  N NH2 . ARG A 1 20  ? 3.52911  50.67578 54.15793 1.000 64.08694  ? 15  ARG A NH2 1 
ATOM   129  N N   . PRO A 1 21  ? 3.81472  56.29069 50.02622 1.000 71.43929  ? 16  PRO A N   1 
ATOM   130  C CA  . PRO A 1 21  ? 4.72395  57.41822 50.27976 1.000 73.66396  ? 16  PRO A CA  1 
ATOM   131  C C   . PRO A 1 21  ? 5.46892  57.30605 51.59795 1.000 75.28105  ? 16  PRO A C   1 
ATOM   132  O O   . PRO A 1 21  ? 6.48671  57.98461 51.77924 1.000 82.14069  ? 16  PRO A O   1 
ATOM   133  C CB  . PRO A 1 21  ? 3.78558  58.62994 50.26413 1.000 76.14936  ? 16  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 21  ? 2.45645  58.06992 50.65523 1.000 76.97643  ? 16  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 21  ? 2.39987  56.69943 50.06069 1.000 72.37222  ? 16  PRO A CD  1 
ATOM   136  N N   . ASP A 1 22  ? 4.99929  56.46655 52.52037 1.000 70.67032  ? 17  ASP A N   1 
ATOM   137  C CA  . ASP A 1 22  ? 5.70488  56.21233 53.77217 1.000 77.18337  ? 17  ASP A CA  1 
ATOM   138  C C   . ASP A 1 22  ? 6.99552  55.42432 53.57721 1.000 79.52624  ? 17  ASP A C   1 
ATOM   139  O O   . ASP A 1 22  ? 7.77176  55.29808 54.53405 1.000 81.60812  ? 17  ASP A O   1 
ATOM   140  C CB  . ASP A 1 22  ? 4.78743  55.45255 54.72730 1.000 77.65125  ? 17  ASP A CB  1 
ATOM   141  C CG  . ASP A 1 22  ? 4.17922  54.21923 54.07951 1.000 75.98150  ? 17  ASP A CG  1 
ATOM   142  O OD1 . ASP A 1 22  ? 3.73353  54.31862 52.91871 1.000 73.36048  ? 17  ASP A OD1 1 
ATOM   143  O OD2 . ASP A 1 22  ? 4.15525  53.14964 54.72128 1.000 77.51660  ? 17  ASP A OD2 1 
ATOM   144  N N   . LEU A 1 23  ? 7.23908  54.90592 52.37486 1.000 72.52734  ? 18  LEU A N   1 
ATOM   145  C CA  . LEU A 1 23  ? 8.35020  54.01397 52.08615 1.000 71.56958  ? 18  LEU A CA  1 
ATOM   146  C C   . LEU A 1 23  ? 9.43445  54.72290 51.29124 1.000 68.92800  ? 18  LEU A C   1 
ATOM   147  O O   . LEU A 1 23  ? 9.15497  55.57645 50.44662 1.000 70.97850  ? 18  LEU A O   1 
ATOM   148  C CB  . LEU A 1 23  ? 7.88523  52.79367 51.29063 1.000 74.00475  ? 18  LEU A CB  1 
ATOM   149  C CG  . LEU A 1 23  ? 7.41310  51.60455 52.11529 1.000 77.23000  ? 18  LEU A CG  1 
ATOM   150  C CD1 . LEU A 1 23  ? 7.20536  50.40441 51.22281 1.000 67.62786  ? 18  LEU A CD1 1 
ATOM   151  C CD2 . LEU A 1 23  ? 8.42718  51.30026 53.20725 1.000 82.05653  ? 18  LEU A CD2 1 
ATOM   152  N N   . ASP A 1 24  ? 10.67486 54.34699 51.56132 1.000 65.77660  ? 19  ASP A N   1 
ATOM   153  C CA  . ASP A 1 24  ? 11.79292 54.80974 50.75670 1.000 67.97671  ? 19  ASP A CA  1 
ATOM   154  C C   . ASP A 1 24  ? 12.19998 53.65073 49.86380 1.000 62.97421  ? 19  ASP A C   1 
ATOM   155  O O   . ASP A 1 24  ? 12.92146 52.74888 50.31270 1.000 64.00315  ? 19  ASP A O   1 
ATOM   156  C CB  . ASP A 1 24  ? 12.96111 55.26488 51.63215 1.000 84.05580  ? 19  ASP A CB  1 
ATOM   157  C CG  . ASP A 1 24  ? 14.07830 55.89770 50.82811 1.000 90.45633  ? 19  ASP A CG  1 
ATOM   158  O OD1 . ASP A 1 24  ? 13.81732 56.33690 49.68735 1.000 92.22523  ? 19  ASP A OD1 1 
ATOM   159  O OD2 . ASP A 1 24  ? 15.22370 55.94596 51.32876 1.000 93.23472  ? 19  ASP A OD2 1 
ATOM   160  N N   . PRO A 1 25  ? 11.73518 53.62219 48.60113 1.000 52.87968  ? 20  PRO A N   1 
ATOM   161  C CA  . PRO A 1 25  ? 11.97379 52.44959 47.74726 1.000 52.07454  ? 20  PRO A CA  1 
ATOM   162  C C   . PRO A 1 25  ? 13.18189 52.61648 46.84765 1.000 60.44386  ? 20  PRO A C   1 
ATOM   163  O O   . PRO A 1 25  ? 13.29766 51.93033 45.82440 1.000 58.35853  ? 20  PRO A O   1 
ATOM   164  C CB  . PRO A 1 25  ? 10.68716 52.36986 46.92074 1.000 50.40723  ? 20  PRO A CB  1 
ATOM   165  C CG  . PRO A 1 25  ? 10.36633 53.82502 46.68059 1.000 51.07109  ? 20  PRO A CG  1 
ATOM   166  C CD  . PRO A 1 25  ? 10.80734 54.57251 47.96311 1.000 51.25984  ? 20  PRO A CD  1 
ATOM   167  N N   . SER A 1 26  ? 14.07337 53.54266 47.21069 1.000 62.36220  ? 21  SER A N   1 
ATOM   168  C CA  . SER A 1 26  ? 15.19805 53.86827 46.33983 1.000 60.74151  ? 21  SER A CA  1 
ATOM   169  C C   . SER A 1 26  ? 16.04699 52.63810 46.03140 1.000 58.04432  ? 21  SER A C   1 
ATOM   170  O O   . SER A 1 26  ? 16.45981 52.43523 44.88293 1.000 62.53849  ? 21  SER A O   1 
ATOM   171  C CB  . SER A 1 26  ? 16.04350 54.96239 46.98216 1.000 66.87039  ? 21  SER A CB  1 
ATOM   172  O OG  . SER A 1 26  ? 16.17977 54.73170 48.37425 1.000 77.51328  ? 21  SER A OG  1 
ATOM   173  N N   . SER A 1 27  ? 16.28451 51.78629 47.03756 1.000 53.79065  ? 22  SER A N   1 
ATOM   174  C CA  . SER A 1 27  ? 17.14630 50.61514 46.87776 1.000 52.99438  ? 22  SER A CA  1 
ATOM   175  C C   . SER A 1 27  ? 16.66377 49.66864 45.78665 1.000 49.08237  ? 22  SER A C   1 
ATOM   176  O O   . SER A 1 27  ? 17.45728 48.86283 45.27681 1.000 45.67278  ? 22  SER A O   1 
ATOM   177  C CB  . SER A 1 27  ? 17.24336 49.86565 48.21021 1.000 60.99999  ? 22  SER A CB  1 
ATOM   178  O OG  . SER A 1 27  ? 15.96025 49.47534 48.67868 1.000 54.25030  ? 22  SER A OG  1 
ATOM   179  N N   . MET A 1 28  ? 15.39099 49.75989 45.40134 1.000 43.72287  ? 23  MET A N   1 
ATOM   180  C CA  . MET A 1 28  ? 14.83284 48.84521 44.41127 1.000 43.86813  ? 23  MET A CA  1 
ATOM   181  C C   . MET A 1 28  ? 15.43497 49.01960 43.01841 1.000 48.01527  ? 23  MET A C   1 
ATOM   182  O O   . MET A 1 28  ? 15.42004 48.06878 42.22486 1.000 44.81260  ? 23  MET A O   1 
ATOM   183  C CB  . MET A 1 28  ? 13.32040 49.02870 44.33385 1.000 39.82934  ? 23  MET A CB  1 
ATOM   184  C CG  . MET A 1 28  ? 12.56536 48.52519 45.54796 1.000 44.20212  ? 23  MET A CG  1 
ATOM   185  S SD  . MET A 1 28  ? 10.81845 48.86462 45.30434 1.000 49.98514  ? 23  MET A SD  1 
ATOM   186  C CE  . MET A 1 28  ? 10.10923 48.16108 46.77669 1.000 51.10730  ? 23  MET A CE  1 
ATOM   187  N N   . ILE A 1 29  ? 15.94935 50.20268 42.68998 1.000 43.96715  ? 24  ILE A N   1 
ATOM   188  C CA  . ILE A 1 29  ? 16.47224 50.41469 41.34437 1.000 46.86457  ? 24  ILE A CA  1 
ATOM   189  C C   . ILE A 1 29  ? 17.74497 49.60371 41.13013 1.000 45.88845  ? 24  ILE A C   1 
ATOM   190  O O   . ILE A 1 29  ? 17.82246 48.77998 40.21347 1.000 47.38371  ? 24  ILE A O   1 
ATOM   191  C CB  . ILE A 1 29  ? 16.68634 51.91120 41.06948 1.000 50.37141  ? 24  ILE A CB  1 
ATOM   192  C CG1 . ILE A 1 29  ? 15.32938 52.58236 40.88205 1.000 53.81715  ? 24  ILE A CG1 1 
ATOM   193  C CG2 . ILE A 1 29  ? 17.54454 52.11328 39.82622 1.000 51.57837  ? 24  ILE A CG2 1 
ATOM   194  C CD1 . ILE A 1 29  ? 15.40204 54.04985 40.60276 1.000 60.49187  ? 24  ILE A CD1 1 
ATOM   195  N N   . VAL A 1 30  ? 18.75244 49.80233 41.98050 1.000 47.52715  ? 25  VAL A N   1 
ATOM   196  C CA  . VAL A 1 30  ? 20.02890 49.11772 41.76667 1.000 49.60621  ? 25  VAL A CA  1 
ATOM   197  C C   . VAL A 1 30  ? 19.85910 47.59971 41.86107 1.000 47.34828  ? 25  VAL A C   1 
ATOM   198  O O   . VAL A 1 30  ? 20.41053 46.85009 41.04321 1.000 46.01782  ? 25  VAL A O   1 
ATOM   199  C CB  . VAL A 1 30  ? 21.09502 49.65096 42.74782 1.000 55.66490  ? 25  VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 30  ? 20.69194 49.38926 44.15357 1.000 54.12722  ? 25  VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 30  ? 22.44323 49.02261 42.46885 1.000 57.82183  ? 25  VAL A CG2 1 
ATOM   202  N N   . LEU A 1 31  ? 19.06911 47.11930 42.82522 1.000 39.49672  ? 26  LEU A N   1 
ATOM   203  C CA  . LEU A 1 31  ? 18.93784 45.67233 42.98812 1.000 44.02089  ? 26  LEU A CA  1 
ATOM   204  C C   . LEU A 1 31  ? 18.03192 45.06812 41.92352 1.000 44.60384  ? 26  LEU A C   1 
ATOM   205  O O   . LEU A 1 31  ? 18.26418 43.93635 41.47346 1.000 38.81385  ? 26  LEU A O   1 
ATOM   206  C CB  . LEU A 1 31  ? 18.41347 45.33412 44.38902 1.000 39.20980  ? 26  LEU A CB  1 
ATOM   207  C CG  . LEU A 1 31  ? 19.47274 45.52424 45.48361 1.000 42.51167  ? 26  LEU A CG  1 
ATOM   208  C CD1 . LEU A 1 31  ? 18.89788 45.29612 46.87615 1.000 40.55591  ? 26  LEU A CD1 1 
ATOM   209  C CD2 . LEU A 1 31  ? 20.65199 44.59492 45.25550 1.000 43.64996  ? 26  LEU A CD2 1 
ATOM   210  N N   . GLY A 1 32  ? 16.98461 45.79115 41.53535 1.000 39.48592  ? 27  GLY A N   1 
ATOM   211  C CA  . GLY A 1 32  ? 16.15181 45.32519 40.43830 1.000 37.93438  ? 27  GLY A CA  1 
ATOM   212  C C   . GLY A 1 32  ? 16.91527 45.25904 39.12774 1.000 41.53754  ? 27  GLY A C   1 
ATOM   213  O O   . GLY A 1 32  ? 16.79848 44.28423 38.37504 1.000 38.10689  ? 27  GLY A O   1 
ATOM   214  N N   . ARG A 1 33  ? 17.74162 46.27336 38.85684 1.000 38.80807  ? 28  ARG A N   1 
ATOM   215  C CA  . ARG A 1 33  ? 18.53809 46.24324 37.63438 1.000 43.77591  ? 28  ARG A CA  1 
ATOM   216  C C   . ARG A 1 33  ? 19.61407 45.17564 37.68953 1.000 46.56439  ? 28  ARG A C   1 
ATOM   217  O O   . ARG A 1 33  ? 19.93271 44.56796 36.65901 1.000 41.88372  ? 28  ARG A O   1 
ATOM   218  C CB  . ARG A 1 33  ? 19.16824 47.60637 37.37562 1.000 41.08388  ? 28  ARG A CB  1 
ATOM   219  C CG  . ARG A 1 33  ? 18.19343 48.57229 36.75284 1.000 46.51566  ? 28  ARG A CG  1 
ATOM   220  C CD  . ARG A 1 33  ? 18.80126 49.91839 36.52995 1.000 43.39888  ? 28  ARG A CD  1 
ATOM   221  N NE  . ARG A 1 33  ? 17.75142 50.86172 36.20348 1.000 43.74629  ? 28  ARG A NE  1 
ATOM   222  C CZ  . ARG A 1 33  ? 17.87722 52.17728 36.28891 1.000 44.78847  ? 28  ARG A CZ  1 
ATOM   223  N NH1 . ARG A 1 33  ? 19.02515 52.72073 36.68305 1.000 47.09777  ? 28  ARG A NH1 1 
ATOM   224  N NH2 . ARG A 1 33  ? 16.85085 52.94531 35.98076 1.000 47.12208  ? 28  ARG A NH2 1 
ATOM   225  N N   . LEU A 1 34  ? 20.18644 44.94614 38.86887 1.000 39.07395  ? 29  LEU A N   1 
ATOM   226  C CA  . LEU A 1 34  ? 21.19145 43.89838 39.02764 1.000 43.31310  ? 29  LEU A CA  1 
ATOM   227  C C   . LEU A 1 34  ? 20.62170 42.52817 38.67676 1.000 41.54327  ? 29  LEU A C   1 
ATOM   228  O O   . LEU A 1 34  ? 21.23066 41.75296 37.92300 1.000 37.33101  ? 29  LEU A O   1 
ATOM   229  C CB  . LEU A 1 34  ? 21.72497 43.90457 40.45859 1.000 40.98555  ? 29  LEU A CB  1 
ATOM   230  C CG  . LEU A 1 34  ? 22.69632 42.76580 40.77522 1.000 48.56614  ? 29  LEU A CG  1 
ATOM   231  C CD1 . LEU A 1 34  ? 24.04554 43.05487 40.15766 1.000 48.77666  ? 29  LEU A CD1 1 
ATOM   232  C CD2 . LEU A 1 34  ? 22.84778 42.54422 42.26680 1.000 54.97752  ? 29  LEU A CD2 1 
ATOM   233  N N   . GLN A 1 35  ? 19.45933 42.20308 39.23545 1.000 33.98521  ? 30  GLN A N   1 
ATOM   234  C CA  . GLN A 1 35  ? 18.86238 40.89036 39.00054 1.000 34.05197  ? 30  GLN A CA  1 
ATOM   235  C C   . GLN A 1 35  ? 18.34610 40.76202 37.56809 1.000 35.08883  ? 30  GLN A C   1 
ATOM   236  O O   . GLN A 1 35  ? 18.45475 39.69563 36.95736 1.000 35.80706  ? 30  GLN A O   1 
ATOM   237  C CB  . GLN A 1 35  ? 17.73891 40.64404 40.00497 1.000 37.39462  ? 30  GLN A CB  1 
ATOM   238  C CG  . GLN A 1 35  ? 18.24060 40.54461 41.45465 1.000 46.27964  ? 30  GLN A CG  1 
ATOM   239  C CD  . GLN A 1 35  ? 17.11949 40.44383 42.46925 1.000 54.38169  ? 30  GLN A CD  1 
ATOM   240  O OE1 . GLN A 1 35  ? 16.50767 39.39055 42.62478 1.000 60.80858  ? 30  GLN A OE1 1 
ATOM   241  N NE2 . GLN A 1 35  ? 16.83999 41.54670 43.16203 1.000 54.86107  ? 30  GLN A NE2 1 
ATOM   242  N N   . GLU A 1 36  ? 17.76609 41.82444 37.02048 1.000 33.97459  ? 31  GLU A N   1 
ATOM   243  C CA  . GLU A 1 36  ? 17.28052 41.73403 35.64049 1.000 38.18211  ? 31  GLU A CA  1 
ATOM   244  C C   . GLU A 1 36  ? 18.42796 41.61045 34.64784 1.000 41.50453  ? 31  GLU A C   1 
ATOM   245  O O   . GLU A 1 36  ? 18.29453 40.91158 33.62767 1.000 40.26044  ? 31  GLU A O   1 
ATOM   246  C CB  . GLU A 1 36  ? 16.41538 42.94323 35.29427 1.000 41.02609  ? 31  GLU A CB  1 
ATOM   247  C CG  . GLU A 1 36  ? 15.85245 42.94021 33.84900 1.000 44.77454  ? 31  GLU A CG  1 
ATOM   248  C CD  . GLU A 1 36  ? 14.72835 41.93334 33.66924 1.000 53.85240  ? 31  GLU A CD  1 
ATOM   249  O OE1 . GLU A 1 36  ? 14.46382 41.15741 34.62137 1.000 58.31428  ? 31  GLU A OE1 1 
ATOM   250  O OE2 . GLU A 1 36  ? 14.09725 41.91715 32.58941 1.000 53.85789  ? 31  GLU A OE2 1 
ATOM   251  N N   . ALA A 1 37  ? 19.54418 42.29695 34.90394 1.000 36.13270  ? 32  ALA A N   1 
ATOM   252  C CA  . ALA A 1 37  ? 20.67692 42.19838 33.99177 1.000 41.76672  ? 32  ALA A CA  1 
ATOM   253  C C   . ALA A 1 37  ? 21.26471 40.79532 34.01858 1.000 42.66100  ? 32  ALA A C   1 
ATOM   254  O O   . ALA A 1 37  ? 21.55206 40.21925 32.96209 1.000 38.20052  ? 32  ALA A O   1 
ATOM   255  C CB  . ALA A 1 37  ? 21.73848 43.24340 34.33711 1.000 41.44412  ? 32  ALA A CB  1 
ATOM   256  N N   . ALA A 1 38  ? 21.43791 40.22176 35.21876 1.000 38.04078  ? 33  ALA A N   1 
ATOM   257  C CA  . ALA A 1 38  ? 21.94235 38.85541 35.31392 1.000 35.92811  ? 33  ALA A CA  1 
ATOM   258  C C   . ALA A 1 38  ? 21.01959 37.88325 34.58803 1.000 37.40558  ? 33  ALA A C   1 
ATOM   259  O O   . ALA A 1 38  ? 21.48499 36.98008 33.88485 1.000 38.94489  ? 33  ALA A O   1 
ATOM   260  C CB  . ALA A 1 38  ? 22.10508 38.43838 36.78356 1.000 37.86746  ? 33  ALA A CB  1 
ATOM   261  N N   . LEU A 1 39  ? 19.70584 38.06282 34.73858 1.000 30.58661  ? 34  LEU A N   1 
ATOM   262  C CA  . LEU A 1 39  ? 18.74797 37.13079 34.15986 1.000 32.65747  ? 34  LEU A CA  1 
ATOM   263  C C   . LEU A 1 39  ? 18.71298 37.25543 32.63458 1.000 35.78921  ? 34  LEU A C   1 
ATOM   264  O O   . LEU A 1 39  ? 18.80426 36.25329 31.91068 1.000 35.47019  ? 34  LEU A O   1 
ATOM   265  C CB  . LEU A 1 39  ? 17.36088 37.39458 34.75391 1.000 35.45271  ? 34  LEU A CB  1 
ATOM   266  C CG  . LEU A 1 39  ? 16.20482 36.64410 34.08943 1.000 38.97820  ? 34  LEU A CG  1 
ATOM   267  C CD1 . LEU A 1 39  ? 16.46294 35.15709 34.10836 1.000 40.68247  ? 34  LEU A CD1 1 
ATOM   268  C CD2 . LEU A 1 39  ? 14.85596 36.96514 34.72490 1.000 39.98019  ? 34  LEU A CD2 1 
ATOM   269  N N   . VAL A 1 40  ? 18.59301 38.48309 32.13559 1.000 33.61629  ? 35  VAL A N   1 
ATOM   270  C CA  . VAL A 1 40  ? 18.46488 38.69454 30.69196 1.000 37.34408  ? 35  VAL A CA  1 
ATOM   271  C C   . VAL A 1 40  ? 19.72887 38.23774 29.97363 1.000 40.00585  ? 35  VAL A C   1 
ATOM   272  O O   . VAL A 1 40  ? 19.66388 37.62377 28.89812 1.000 42.82029  ? 35  VAL A O   1 
ATOM   273  C CB  . VAL A 1 40  ? 18.15020 40.17193 30.39857 1.000 40.77247  ? 35  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 40  ? 18.28931 40.44594 28.90259 1.000 43.91667  ? 35  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 40  ? 16.75071 40.50408 30.84820 1.000 40.91916  ? 35  VAL A CG2 1 
ATOM   276  N N   . ILE A 1 41  ? 20.89513 38.50267 30.56922 1.000 36.56398  ? 36  ILE A N   1 
ATOM   277  C CA  . ILE A 1 41  ? 22.15561 38.13020 29.93298 1.000 40.39176  ? 36  ILE A CA  1 
ATOM   278  C C   . ILE A 1 41  ? 22.31807 36.61495 29.91154 1.000 37.79123  ? 36  ILE A C   1 
ATOM   279  O O   . ILE A 1 41  ? 22.69222 36.03948 28.88125 1.000 41.37411  ? 36  ILE A O   1 
ATOM   280  C CB  . ILE A 1 41  ? 23.33283 38.84239 30.62511 1.000 39.74701  ? 36  ILE A CB  1 
ATOM   281  C CG1 . ILE A 1 41  ? 23.31754 40.33046 30.27399 1.000 40.12127  ? 36  ILE A CG1 1 
ATOM   282  C CG2 . ILE A 1 41  ? 24.66826 38.21001 30.26199 1.000 38.86246  ? 36  ILE A CG2 1 
ATOM   283  C CD1 . ILE A 1 41  ? 24.27737 41.15143 31.11617 1.000 47.40199  ? 36  ILE A CD1 1 
ATOM   284  N N   . ALA A 1 42  ? 22.00673 35.93456 31.02415 1.000 36.03856  ? 37  ALA A N   1 
ATOM   285  C CA  . ALA A 1 42  ? 22.03676 34.47290 31.01266 1.000 35.81927  ? 37  ALA A CA  1 
ATOM   286  C C   . ALA A 1 42  ? 21.05899 33.90902 29.98120 1.000 40.60960  ? 37  ALA A C   1 
ATOM   287  O O   . ALA A 1 42  ? 21.43203 33.08025 29.13929 1.000 38.81749  ? 37  ALA A O   1 
ATOM   288  C CB  . ALA A 1 42  ? 21.72372 33.91575 32.40700 1.000 38.21241  ? 37  ALA A CB  1 
ATOM   289  N N   . ARG A 1 43  ? 19.80258 34.36112 30.02411 1.000 33.27263  ? 38  ARG A N   1 
ATOM   290  C CA  . ARG A 1 43  ? 18.74647 33.72858 29.24410 1.000 38.78162  ? 38  ARG A CA  1 
ATOM   291  C C   . ARG A 1 43  ? 18.90967 34.00531 27.75290 1.000 42.20593  ? 38  ARG A C   1 
ATOM   292  O O   . ARG A 1 43  ? 18.75090 33.10139 26.92407 1.000 42.17792  ? 38  ARG A O   1 
ATOM   293  C CB  . ARG A 1 43  ? 17.38566 34.22550 29.71578 1.000 36.35577  ? 38  ARG A CB  1 
ATOM   294  C CG  . ARG A 1 43  ? 16.20636 33.60953 28.98464 1.000 45.03825  ? 38  ARG A CG  1 
ATOM   295  C CD  . ARG A 1 43  ? 14.92337 34.33105 29.37515 1.000 50.15076  ? 38  ARG A CD  1 
ATOM   296  N NE  . ARG A 1 43  ? 14.95505 35.73356 28.97074 1.000 55.85528  ? 38  ARG A NE  1 
ATOM   297  C CZ  . ARG A 1 43  ? 14.45789 36.73810 29.69135 1.000 64.73299  ? 38  ARG A CZ  1 
ATOM   298  N NH1 . ARG A 1 43  ? 13.90089 36.50155 30.87472 1.000 59.77910  ? 38  ARG A NH1 1 
ATOM   299  N NH2 . ARG A 1 43  ? 14.53716 37.98394 29.23827 1.000 66.16843  ? 38  ARG A NH2 1 
ATOM   300  N N   . ASP A 1 44  ? 19.23081 35.24721 27.39864 1.000 43.51182  ? 39  ASP A N   1 
ATOM   301  C CA  . ASP A 1 44  ? 19.19544 35.68596 26.01057 1.000 49.75412  ? 39  ASP A CA  1 
ATOM   302  C C   . ASP A 1 44  ? 20.55592 35.68906 25.31489 1.000 42.06689  ? 39  ASP A C   1 
ATOM   303  O O   . ASP A 1 44  ? 20.59399 35.67176 24.07661 1.000 44.87774  ? 39  ASP A O   1 
ATOM   304  C CB  . ASP A 1 44  ? 18.57453 37.08676 25.94061 1.000 47.84470  ? 39  ASP A CB  1 
ATOM   305  C CG  . ASP A 1 44  ? 17.08562 37.07842 26.25530 1.000 58.74589  ? 39  ASP A CG  1 
ATOM   306  O OD1 . ASP A 1 44  ? 16.49191 35.97646 26.34862 1.000 61.15538  ? 39  ASP A OD1 1 
ATOM   307  O OD2 . ASP A 1 44  ? 16.50151 38.17381 26.39589 1.000 62.36543  ? 39  ASP A OD2 1 
ATOM   308  N N   . ARG A 1 45  ? 21.66382 35.68531 26.05571 1.000 39.15138  ? 40  ARG A N   1 
ATOM   309  C CA  . ARG A 1 45  ? 22.99777 35.78777 25.46565 1.000 42.91602  ? 40  ARG A CA  1 
ATOM   310  C C   . ARG A 1 45  ? 23.86589 34.57167 25.76091 1.000 45.52037  ? 40  ARG A C   1 
ATOM   311  O O   . ARG A 1 45  ? 24.31218 33.90016 24.81866 1.000 40.84570  ? 40  ARG A O   1 
ATOM   312  C CB  . ARG A 1 45  ? 23.70704 37.06319 25.94769 1.000 46.08671  ? 40  ARG A CB  1 
ATOM   313  C CG  . ARG A 1 45  ? 22.90643 38.35159 25.80682 1.000 46.83766  ? 40  ARG A CG  1 
ATOM   314  C CD  . ARG A 1 45  ? 22.55437 38.64098 24.35785 1.000 44.58585  ? 40  ARG A CD  1 
ATOM   315  N NE  . ARG A 1 45  ? 23.71971 38.95751 23.52468 1.000 47.73600  ? 40  ARG A NE  1 
ATOM   316  C CZ  . ARG A 1 45  ? 24.19216 40.18653 23.31729 1.000 58.52961  ? 40  ARG A CZ  1 
ATOM   317  N NH1 . ARG A 1 45  ? 23.61772 41.22938 23.89598 1.000 58.30102  ? 40  ARG A NH1 1 
ATOM   318  N NH2 . ARG A 1 45  ? 25.23818 40.37972 22.51589 1.000 61.69420  ? 40  ARG A NH2 1 
ATOM   319  N N   . LEU A 1 46  ? 24.14971 34.27342 27.03574 1.000 38.47107  ? 41  LEU A N   1 
ATOM   320  C CA  . LEU A 1 46  ? 25.17375 33.28548 27.35346 1.000 34.32446  ? 41  LEU A CA  1 
ATOM   321  C C   . LEU A 1 46  ? 24.65838 31.86695 27.15654 1.000 37.22976  ? 41  LEU A C   1 
ATOM   322  O O   . LEU A 1 46  ? 25.33723 31.03030 26.55028 1.000 36.50796  ? 41  LEU A O   1 
ATOM   323  C CB  . LEU A 1 46  ? 25.66327 33.46147 28.80673 1.000 36.79101  ? 41  LEU A CB  1 
ATOM   324  C CG  . LEU A 1 46  ? 26.13723 34.86008 29.21508 1.000 38.11184  ? 41  LEU A CG  1 
ATOM   325  C CD1 . LEU A 1 46  ? 26.61586 34.84663 30.66833 1.000 40.41723  ? 41  LEU A CD1 1 
ATOM   326  C CD2 . LEU A 1 46  ? 27.24627 35.34348 28.28504 1.000 45.34018  ? 41  LEU A CD2 1 
ATOM   327  N N   . ASN A 1 47  ? 23.48952 31.56017 27.72158 1.000 35.54481  ? 42  ASN A N   1 
ATOM   328  C CA  . ASN A 1 47  ? 23.00131 30.18711 27.66871 1.000 35.90182  ? 42  ASN A CA  1 
ATOM   329  C C   . ASN A 1 47  ? 22.70947 29.71258 26.24918 1.000 39.72167  ? 42  ASN A C   1 
ATOM   330  O O   . ASN A 1 47  ? 23.02145 28.54807 25.95561 1.000 42.83624  ? 42  ASN A O   1 
ATOM   331  C CB  . ASN A 1 47  ? 21.77390 30.02660 28.56503 1.000 40.58324  ? 42  ASN A CB  1 
ATOM   332  C CG  . ASN A 1 47  ? 22.14679 30.09410 30.03303 1.000 42.20808  ? 42  ASN A CG  1 
ATOM   333  O OD1 . ASN A 1 47  ? 23.33374 30.05803 30.36386 1.000 38.55385  ? 42  ASN A OD1 1 
ATOM   334  N ND2 . ASN A 1 47  ? 21.15561 30.18439 30.91068 1.000 44.90182  ? 42  ASN A ND2 1 
ATOM   335  N N   . PRO A 1 48  ? 22.14914 30.51960 25.34050 1.000 39.29590  ? 43  PRO A N   1 
ATOM   336  C CA  . PRO A 1 48  ? 21.99205 30.02790 23.96036 1.000 42.59485  ? 43  PRO A CA  1 
ATOM   337  C C   . PRO A 1 48  ? 23.31297 29.64978 23.32357 1.000 49.71554  ? 43  PRO A C   1 
ATOM   338  O O   . PRO A 1 48  ? 23.35637 28.71315 22.50849 1.000 51.40622  ? 43  PRO A O   1 
ATOM   339  C CB  . PRO A 1 48  ? 21.31752 31.20691 23.23759 1.000 43.40259  ? 43  PRO A CB  1 
ATOM   340  C CG  . PRO A 1 48  ? 20.56365 31.91195 24.35149 1.000 40.20543  ? 43  PRO A CG  1 
ATOM   341  C CD  . PRO A 1 48  ? 21.51358 31.83543 25.52079 1.000 38.86539  ? 43  PRO A CD  1 
ATOM   342  N N   . LEU A 1 49  ? 24.40410 30.34046 23.67793 1.000 45.68566  ? 44  LEU A N   1 
ATOM   343  C CA  . LEU A 1 49  ? 25.70004 29.95232 23.13338 1.000 45.08972  ? 44  LEU A CA  1 
ATOM   344  C C   . LEU A 1 49  ? 26.15333 28.62357 23.72089 1.000 44.16309  ? 44  LEU A C   1 
ATOM   345  O O   . LEU A 1 49  ? 26.61313 27.74174 22.98633 1.000 46.50662  ? 44  LEU A O   1 
ATOM   346  C CB  . LEU A 1 49  ? 26.75244 31.04212 23.37082 1.000 44.34036  ? 44  LEU A CB  1 
ATOM   347  C CG  . LEU A 1 49  ? 28.17021 30.73421 22.85085 1.000 49.75293  ? 44  LEU A CG  1 
ATOM   348  C CD1 . LEU A 1 49  ? 28.81576 31.99133 22.32457 1.000 61.79049  ? 44  LEU A CD1 1 
ATOM   349  C CD2 . LEU A 1 49  ? 29.10136 30.07708 23.87096 1.000 43.29626  ? 44  LEU A CD2 1 
ATOM   350  N N   . PHE A 1 50  ? 26.02684 28.45415 25.03948 1.000 41.74126  ? 45  PHE A N   1 
ATOM   351  C CA  . PHE A 1 50  ? 26.35088 27.16384 25.63559 1.000 42.43309  ? 45  PHE A CA  1 
ATOM   352  C C   . PHE A 1 50  ? 25.54971 26.03981 24.98920 1.000 45.09989  ? 45  PHE A C   1 
ATOM   353  O O   . PHE A 1 50  ? 26.06556 24.93381 24.79189 1.000 44.30551  ? 45  PHE A O   1 
ATOM   354  C CB  . PHE A 1 50  ? 26.09247 27.19543 27.14356 1.000 39.11124  ? 45  PHE A CB  1 
ATOM   355  C CG  . PHE A 1 50  ? 26.90984 28.21719 27.88545 1.000 38.53202  ? 45  PHE A CG  1 
ATOM   356  C CD1 . PHE A 1 50  ? 28.20200 28.52439 27.47566 1.000 40.32434  ? 45  PHE A CD1 1 
ATOM   357  C CD2 . PHE A 1 50  ? 26.39628 28.84433 29.02548 1.000 33.43933  ? 45  PHE A CD2 1 
ATOM   358  C CE1 . PHE A 1 50  ? 28.96570 29.45746 28.17132 1.000 38.19711  ? 45  PHE A CE1 1 
ATOM   359  C CE2 . PHE A 1 50  ? 27.14753 29.77955 29.71670 1.000 37.31886  ? 45  PHE A CE2 1 
ATOM   360  C CZ  . PHE A 1 50  ? 28.43675 30.07811 29.30180 1.000 41.37526  ? 45  PHE A CZ  1 
ATOM   361  N N   . ALA A 1 51  ? 24.27577 26.29009 24.68000 1.000 49.59015  ? 46  ALA A N   1 
ATOM   362  C CA  . ALA A 1 51  ? 23.45121 25.22073 24.12461 1.000 53.23210  ? 46  ALA A CA  1 
ATOM   363  C C   . ALA A 1 51  ? 23.85841 24.87876 22.70090 1.000 52.90249  ? 46  ALA A C   1 
ATOM   364  O O   . ALA A 1 51  ? 23.68659 23.73238 22.26843 1.000 56.18629  ? 46  ALA A O   1 
ATOM   365  C CB  . ALA A 1 51  ? 21.97258 25.60220 24.18390 1.000 52.79379  ? 46  ALA A CB  1 
ATOM   366  N N   . ARG A 1 52  ? 24.41062 25.84316 21.95904 1.000 55.04356  ? 47  ARG A N   1 
ATOM   367  C CA  . ARG A 1 52  ? 24.99191 25.51849 20.66017 1.000 62.00230  ? 47  ARG A CA  1 
ATOM   368  C C   . ARG A 1 52  ? 26.05068 24.43076 20.79033 1.000 61.66980  ? 47  ARG A C   1 
ATOM   369  O O   . ARG A 1 52  ? 26.26566 23.64625 19.85388 1.000 56.85001  ? 47  ARG A O   1 
ATOM   370  C CB  . ARG A 1 52  ? 25.62307 26.75780 20.01796 1.000 63.94759  ? 47  ARG A CB  1 
ATOM   371  C CG  . ARG A 1 52  ? 24.66622 27.81995 19.49784 1.000 69.11975  ? 47  ARG A CG  1 
ATOM   372  C CD  . ARG A 1 52  ? 25.37738 28.61102 18.38905 1.000 83.97539  ? 47  ARG A CD  1 
ATOM   373  N NE  . ARG A 1 52  ? 26.40737 29.52342 18.90153 1.000 86.64228  ? 47  ARG A NE  1 
ATOM   374  C CZ  . ARG A 1 52  ? 27.55988 29.79258 18.28427 1.000 92.80415  ? 47  ARG A CZ  1 
ATOM   375  N NH1 . ARG A 1 52  ? 28.41802 30.64950 18.82659 1.000 92.15677  ? 47  ARG A NH1 1 
ATOM   376  N NH2 . ARG A 1 52  ? 27.86726 29.19832 17.13503 1.000 93.52777  ? 47  ARG A NH2 1 
ATOM   377  N N   . TYR A 1 53  ? 26.72584 24.38030 21.94062 1.000 56.45837  ? 48  TYR A N   1 
ATOM   378  C CA  . TYR A 1 53  ? 27.75981 23.40033 22.22795 1.000 56.10604  ? 48  TYR A CA  1 
ATOM   379  C C   . TYR A 1 53  ? 27.22887 22.19377 22.98760 1.000 56.16375  ? 48  TYR A C   1 
ATOM   380  O O   . TYR A 1 53  ? 28.02526 21.36790 23.44738 1.000 55.91613  ? 48  TYR A O   1 
ATOM   381  C CB  . TYR A 1 53  ? 28.89999 24.04987 23.01595 1.000 57.87539  ? 48  TYR A CB  1 
ATOM   382  C CG  . TYR A 1 53  ? 29.79759 24.90768 22.15846 1.000 56.99004  ? 48  TYR A CG  1 
ATOM   383  C CD1 . TYR A 1 53  ? 30.94632 24.37909 21.57697 1.000 60.21445  ? 48  TYR A CD1 1 
ATOM   384  C CD2 . TYR A 1 53  ? 29.49677 26.24061 21.92095 1.000 56.11984  ? 48  TYR A CD2 1 
ATOM   385  C CE1 . TYR A 1 53  ? 31.77071 25.15050 20.78137 1.000 59.63216  ? 48  TYR A CE1 1 
ATOM   386  C CE2 . TYR A 1 53  ? 30.31778 27.02397 21.10235 1.000 66.19416  ? 48  TYR A CE2 1 
ATOM   387  C CZ  . TYR A 1 53  ? 31.45435 26.47055 20.54736 1.000 65.33461  ? 48  TYR A CZ  1 
ATOM   388  O OH  . TYR A 1 53  ? 32.28282 27.23423 19.75476 1.000 75.32997  ? 48  TYR A OH  1 
ATOM   389  N N   . GLY A 1 54  ? 25.90937 22.06767 23.11410 1.000 55.43056  ? 49  GLY A N   1 
ATOM   390  C CA  . GLY A 1 54  ? 25.31724 20.95742 23.82473 1.000 54.95495  ? 49  GLY A CA  1 
ATOM   391  C C   . GLY A 1 54  ? 25.42053 21.05203 25.32841 1.000 51.55706  ? 49  GLY A C   1 
ATOM   392  O O   . GLY A 1 54  ? 25.24780 20.03572 26.01035 1.000 55.35135  ? 49  GLY A O   1 
ATOM   393  N N   . LEU A 1 55  ? 25.69351 22.23741 25.86459 1.000 46.18764  ? 50  LEU A N   1 
ATOM   394  C CA  . LEU A 1 55  ? 25.89635 22.43213 27.29287 1.000 47.74001  ? 50  LEU A CA  1 
ATOM   395  C C   . LEU A 1 55  ? 24.70290 23.15877 27.90139 1.000 54.70664  ? 50  LEU A C   1 
ATOM   396  O O   . LEU A 1 55  ? 24.31284 24.23096 27.42505 1.000 51.58796  ? 50  LEU A O   1 
ATOM   397  C CB  . LEU A 1 55  ? 27.17731 23.22828 27.55594 1.000 43.55420  ? 50  LEU A CB  1 
ATOM   398  C CG  . LEU A 1 55  ? 28.49486 22.54531 27.18607 1.000 41.45892  ? 50  LEU A CG  1 
ATOM   399  C CD1 . LEU A 1 55  ? 29.66212 23.46699 27.45956 1.000 48.75965  ? 50  LEU A CD1 1 
ATOM   400  C CD2 . LEU A 1 55  ? 28.66519 21.25681 27.98193 1.000 50.00424  ? 50  LEU A CD2 1 
ATOM   401  N N   . GLN A 1 56  ? 24.13320 22.57067 28.95334 1.000 56.64784  ? 51  GLN A N   1 
ATOM   402  C CA  . GLN A 1 56  ? 23.06904 23.18954 29.72087 1.000 61.78236  ? 51  GLN A CA  1 
ATOM   403  C C   . GLN A 1 56  ? 23.66178 24.23774 30.65421 1.000 60.09556  ? 51  GLN A C   1 
ATOM   404  O O   . GLN A 1 56  ? 24.87253 24.25777 30.89489 1.000 55.46376  ? 51  GLN A O   1 
ATOM   405  C CB  . GLN A 1 56  ? 22.30359 22.13165 30.51787 1.000 64.14258  ? 51  GLN A CB  1 
ATOM   406  N N   . PRO A 1 57  ? 22.84135 25.15507 31.15695 1.000 70.04286  ? 52  PRO A N   1 
ATOM   407  C CA  . PRO A 1 57  ? 23.35937 26.14516 32.11172 1.000 67.48754  ? 52  PRO A CA  1 
ATOM   408  C C   . PRO A 1 57  ? 23.96861 25.46468 33.33389 1.000 65.39876  ? 52  PRO A C   1 
ATOM   409  O O   . PRO A 1 57  ? 23.34483 24.60565 33.96822 1.000 66.15579  ? 52  PRO A O   1 
ATOM   410  C CB  . PRO A 1 57  ? 22.11856 26.97052 32.46873 1.000 71.55287  ? 52  PRO A CB  1 
ATOM   411  C CG  . PRO A 1 57  ? 21.23427 26.83973 31.25638 1.000 74.72404  ? 52  PRO A CG  1 
ATOM   412  C CD  . PRO A 1 57  ? 21.45051 25.43975 30.75604 1.000 73.40391  ? 52  PRO A CD  1 
ATOM   413  N N   . GLY A 1 58  ? 25.21359 25.84218 33.64890 1.000 45.51701  ? 53  GLY A N   1 
ATOM   414  C CA  . GLY A 1 58  ? 25.95661 25.27004 34.74415 1.000 42.08341  ? 53  GLY A CA  1 
ATOM   415  C C   . GLY A 1 58  ? 26.99497 24.26000 34.31950 1.000 46.75753  ? 53  GLY A C   1 
ATOM   416  O O   . GLY A 1 58  ? 27.99663 24.08262 35.01777 1.000 44.95443  ? 53  GLY A O   1 
ATOM   417  N N   . GLU A 1 59  ? 26.78064 23.59367 33.17995 1.000 39.87172  ? 54  GLU A N   1 
ATOM   418  C CA  . GLU A 1 59  ? 27.71166 22.56052 32.73927 1.000 38.57754  ? 54  GLU A CA  1 
ATOM   419  C C   . GLU A 1 59  ? 28.98167 23.16685 32.14972 1.000 36.32882  ? 54  GLU A C   1 
ATOM   420  O O   . GLU A 1 59  ? 30.07957 22.62513 32.33812 1.000 36.13853  ? 54  GLU A O   1 
ATOM   421  C CB  . GLU A 1 59  ? 27.02762 21.64576 31.71565 1.000 36.58867  ? 54  GLU A CB  1 
ATOM   422  C CG  . GLU A 1 59  ? 25.83450 20.89430 32.27623 1.000 43.93145  ? 54  GLU A CG  1 
ATOM   423  C CD  . GLU A 1 59  ? 25.18919 19.96433 31.26044 1.000 55.14510  ? 54  GLU A CD  1 
ATOM   424  O OE1 . GLU A 1 59  ? 25.37195 20.18304 30.03628 1.000 56.02771  ? 54  GLU A OE1 1 
ATOM   425  O OE2 . GLU A 1 59  ? 24.49988 19.01144 31.69012 1.000 60.78607  ? 54  GLU A OE2 1 
ATOM   426  N N   . PHE A 1 60  ? 28.84415 24.27208 31.41094 1.000 36.06077  ? 55  PHE A N   1 
ATOM   427  C CA  . PHE A 1 60  ? 30.01469 25.01299 30.96415 1.000 38.01003  ? 55  PHE A CA  1 
ATOM   428  C C   . PHE A 1 60  ? 30.93918 25.32435 32.13532 1.000 32.06343  ? 55  PHE A C   1 
ATOM   429  O O   . PHE A 1 60  ? 32.15001 25.08831 32.05927 1.000 36.85093  ? 55  PHE A O   1 
ATOM   430  C CB  . PHE A 1 60  ? 29.59568 26.30335 30.26617 1.000 37.57624  ? 55  PHE A CB  1 
ATOM   431  C CG  . PHE A 1 60  ? 30.75778 27.14618 29.81965 1.000 35.56821  ? 55  PHE A CG  1 
ATOM   432  C CD1 . PHE A 1 60  ? 31.32176 26.98285 28.54894 1.000 37.41027  ? 55  PHE A CD1 1 
ATOM   433  C CD2 . PHE A 1 60  ? 31.27485 28.11881 30.64971 1.000 34.94878  ? 55  PHE A CD2 1 
ATOM   434  C CE1 . PHE A 1 60  ? 32.39843 27.76074 28.14935 1.000 40.49041  ? 55  PHE A CE1 1 
ATOM   435  C CE2 . PHE A 1 60  ? 32.33777 28.90196 30.25600 1.000 39.03061  ? 55  PHE A CE2 1 
ATOM   436  C CZ  . PHE A 1 60  ? 32.90457 28.72765 28.98460 1.000 41.84813  ? 55  PHE A CZ  1 
ATOM   437  N N   . ASP A 1 61  ? 30.37644 25.85945 33.22950 1.000 33.69293  ? 56  ASP A N   1 
ATOM   438  C CA  . ASP A 1 61  ? 31.19654 26.20048 34.39294 1.000 33.80017  ? 56  ASP A CA  1 
ATOM   439  C C   . ASP A 1 61  ? 31.99880 24.99626 34.88163 1.000 34.90464  ? 56  ASP A C   1 
ATOM   440  O O   . ASP A 1 61  ? 33.18279 25.12578 35.20987 1.000 35.49553  ? 56  ASP A O   1 
ATOM   441  C CB  . ASP A 1 61  ? 30.31785 26.76505 35.52270 1.000 31.79079  ? 56  ASP A CB  1 
ATOM   442  C CG  . ASP A 1 61  ? 31.14496 27.48782 36.61429 1.000 51.53486  ? 56  ASP A CG  1 
ATOM   443  O OD1 . ASP A 1 61  ? 32.37279 27.69111 36.40580 1.000 49.37874  ? 56  ASP A OD1 1 
ATOM   444  O OD2 . ASP A 1 61  ? 30.56542 27.86747 37.67286 1.000 50.85823  ? 56  ASP A OD2 1 
ATOM   445  N N   . VAL A 1 62  ? 31.38057 23.81379 34.93732 1.000 33.47552  ? 57  VAL A N   1 
ATOM   446  C CA  . VAL A 1 62  ? 32.12091 22.64184 35.40187 1.000 34.49053  ? 57  VAL A CA  1 
ATOM   447  C C   . VAL A 1 62  ? 33.31773 22.37919 34.50234 1.000 36.73435  ? 57  VAL A C   1 
ATOM   448  O O   . VAL A 1 62  ? 34.45746 22.25894 34.96897 1.000 34.90954  ? 57  VAL A O   1 
ATOM   449  C CB  . VAL A 1 62  ? 31.21448 21.40121 35.48870 1.000 36.18740  ? 57  VAL A CB  1 
ATOM   450  C CG1 . VAL A 1 62  ? 32.07754 20.17734 35.81778 1.000 40.68054  ? 57  VAL A CG1 1 
ATOM   451  C CG2 . VAL A 1 62  ? 30.13332 21.57514 36.54405 1.000 35.07296  ? 57  VAL A CG2 1 
ATOM   452  N N   . LEU A 1 63  ? 33.07745 22.28701 33.19109 1.000 35.74613  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 63  ? 34.17395 22.02819 32.26934 1.000 32.31305  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 63  ? 35.21196 23.14362 32.31597 1.000 36.49862  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 63  ? 36.42132 22.89187 32.20535 1.000 36.65331  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 63  ? 33.61770 21.87667 30.84755 1.000 33.65954  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 63  ? 32.55002 20.79847 30.62482 1.000 34.84093  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 63  ? 32.18937 20.67513 29.11536 1.000 37.32314  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 63  ? 33.06999 19.47552 31.14932 1.000 39.99838  ? 58  LEU A CD2 1 
ATOM   460  N N   . ALA A 1 64  ? 34.75416 24.39271 32.42126 1.000 33.98519  ? 59  ALA A N   1 
ATOM   461  C CA  . ALA A 1 64  ? 35.68813 25.51220 32.44845 1.000 34.60660  ? 59  ALA A CA  1 
ATOM   462  C C   . ALA A 1 64  ? 36.58210 25.44066 33.68752 1.000 35.92057  ? 59  ALA A C   1 
ATOM   463  O O   . ALA A 1 64  ? 37.79901 25.65928 33.60654 1.000 38.95182  ? 59  ALA A O   1 
ATOM   464  C CB  . ALA A 1 64  ? 34.91416 26.82941 32.42562 1.000 35.17513  ? 59  ALA A CB  1 
ATOM   465  N N   . THR A 1 65  ? 35.99482 25.11034 34.83277 1.000 33.59666  ? 60  THR A N   1 
ATOM   466  C CA  . THR A 1 65  ? 36.77262 24.98327 36.06731 1.000 38.22041  ? 60  THR A CA  1 
ATOM   467  C C   . THR A 1 65  ? 37.82620 23.88049 35.93983 1.000 39.64803  ? 60  THR A C   1 
ATOM   468  O O   . THR A 1 65  ? 39.00161 24.08729 36.26448 1.000 38.41998  ? 60  THR A O   1 
ATOM   469  C CB  . THR A 1 65  ? 35.83624 24.71526 37.25268 1.000 35.56799  ? 60  THR A CB  1 
ATOM   470  O OG1 . THR A 1 65  ? 34.85476 25.75682 37.33490 1.000 35.26057  ? 60  THR A OG1 1 
ATOM   471  C CG2 . THR A 1 65  ? 36.61970 24.68693 38.56382 1.000 37.22773  ? 60  THR A CG2 1 
ATOM   472  N N   . LEU A 1 66  ? 37.42069 22.70219 35.45303 1.000 37.71155  ? 61  LEU A N   1 
ATOM   473  C CA  . LEU A 1 66  ? 38.37293 21.61684 35.22933 1.000 35.80291  ? 61  LEU A CA  1 
ATOM   474  C C   . LEU A 1 66  ? 39.48432 22.03807 34.27337 1.000 42.80411  ? 61  LEU A C   1 
ATOM   475  O O   . LEU A 1 66  ? 40.67343 21.83752 34.55820 1.000 41.36685  ? 61  LEU A O   1 
ATOM   476  C CB  . LEU A 1 66  ? 37.64605 20.38351 34.69527 1.000 36.57679  ? 61  LEU A CB  1 
ATOM   477  C CG  . LEU A 1 66  ? 36.73084 19.71959 35.72973 1.000 38.84814  ? 61  LEU A CG  1 
ATOM   478  C CD1 . LEU A 1 66  ? 35.90318 18.61698 35.10830 1.000 42.01879  ? 61  LEU A CD1 1 
ATOM   479  C CD2 . LEU A 1 66  ? 37.59144 19.17796 36.86385 1.000 37.43332  ? 61  LEU A CD2 1 
ATOM   480  N N   . ARG A 1 67  ? 39.11306 22.61886 33.12692 1.000 39.09873  ? 62  ARG A N   1 
ATOM   481  C CA  . ARG A 1 67  ? 40.11954 22.97871 32.13294 1.000 45.26657  ? 62  ARG A CA  1 
ATOM   482  C C   . ARG A 1 67  ? 41.12738 23.96109 32.71080 1.000 48.02744  ? 62  ARG A C   1 
ATOM   483  O O   . ARG A 1 67  ? 42.34211 23.77426 32.57275 1.000 46.62540  ? 62  ARG A O   1 
ATOM   484  C CB  . ARG A 1 67  ? 39.45508 23.56148 30.88227 1.000 37.00341  ? 62  ARG A CB  1 
ATOM   485  C CG  . ARG A 1 67  ? 40.44826 24.10182 29.85028 1.000 41.55335  ? 62  ARG A CG  1 
ATOM   486  C CD  . ARG A 1 67  ? 41.26334 22.97889 29.20927 1.000 46.14672  ? 62  ARG A CD  1 
ATOM   487  N NE  . ARG A 1 67  ? 42.24889 23.48736 28.25946 1.000 51.37789  ? 62  ARG A NE  1 
ATOM   488  C CZ  . ARG A 1 67  ? 43.43009 23.97392 28.62122 1.000 52.04370  ? 62  ARG A CZ  1 
ATOM   489  N NH1 . ARG A 1 67  ? 43.75597 24.03160 29.91052 1.000 47.65412  ? 62  ARG A NH1 1 
ATOM   490  N NH2 . ARG A 1 67  ? 44.27898 24.41393 27.71341 1.000 53.88774  ? 62  ARG A NH2 1 
ATOM   491  N N   . ARG A 1 68  ? 40.65007 25.00961 33.38164 1.000 39.38879  ? 63  ARG A N   1 
ATOM   492  C CA  . ARG A 1 68  ? 41.60936 26.02850 33.79151 1.000 48.01661  ? 63  ARG A CA  1 
ATOM   493  C C   . ARG A 1 68  ? 42.40112 25.62977 35.02856 1.000 43.37649  ? 63  ARG A C   1 
ATOM   494  O O   . ARG A 1 68  ? 43.31309 26.36648 35.41196 1.000 45.55188  ? 63  ARG A O   1 
ATOM   495  C CB  . ARG A 1 68  ? 40.92225 27.37681 34.02212 1.000 48.21896  ? 63  ARG A CB  1 
ATOM   496  C CG  . ARG A 1 68  ? 39.98768 27.43362 35.18492 1.000 44.84087  ? 63  ARG A CG  1 
ATOM   497  C CD  . ARG A 1 68  ? 39.37040 28.81166 35.21910 1.000 45.62486  ? 63  ARG A CD  1 
ATOM   498  N NE  . ARG A 1 68  ? 37.96340 28.76446 35.59117 1.000 41.33805  ? 63  ARG A NE  1 
ATOM   499  C CZ  . ARG A 1 68  ? 37.52119 28.70755 36.84644 1.000 43.09967  ? 63  ARG A CZ  1 
ATOM   500  N NH1 . ARG A 1 68  ? 38.37531 28.69604 37.86793 1.000 41.01268  ? 63  ARG A NH1 1 
ATOM   501  N NH2 . ARG A 1 68  ? 36.21714 28.66871 37.07475 1.000 40.55342  ? 63  ARG A NH2 1 
ATOM   502  N N   . SER A 1 69  ? 42.11577 24.47233 35.62576 1.000 40.73681  ? 64  SER A N   1 
ATOM   503  C CA  . SER A 1 69  ? 42.95097 23.99024 36.71717 1.000 45.46127  ? 64  SER A CA  1 
ATOM   504  C C   . SER A 1 69  ? 44.25798 23.38103 36.22777 1.000 49.82993  ? 64  SER A C   1 
ATOM   505  O O   . SER A 1 69  ? 45.15359 23.14130 37.04403 1.000 48.99123  ? 64  SER A O   1 
ATOM   506  C CB  . SER A 1 69  ? 42.18566 22.97036 37.56174 1.000 46.33252  ? 64  SER A CB  1 
ATOM   507  O OG  . SER A 1 69  ? 41.98154 21.75079 36.86691 1.000 45.41473  ? 64  SER A OG  1 
ATOM   508  N N   . GLY A 1 70  ? 44.38913 23.12759 34.92924 1.000 50.76458  ? 65  GLY A N   1 
ATOM   509  C CA  . GLY A 1 70  ? 45.60594 22.58321 34.36455 1.000 53.22549  ? 65  GLY A CA  1 
ATOM   510  C C   . GLY A 1 70  ? 45.62424 21.06288 34.35613 1.000 49.85212  ? 65  GLY A C   1 
ATOM   511  O O   . GLY A 1 70  ? 44.90657 20.39230 35.10239 1.000 48.02279  ? 65  GLY A O   1 
ATOM   512  N N   . ALA A 1 71  ? 46.47468 20.52177 33.48241 1.000 51.53895  ? 66  ALA A N   1 
ATOM   513  C CA  . ALA A 1 71  ? 46.61146 19.07913 33.35711 1.000 52.21768  ? 66  ALA A CA  1 
ATOM   514  C C   . ALA A 1 71  ? 46.90331 18.45975 34.72340 1.000 54.86661  ? 66  ALA A C   1 
ATOM   515  O O   . ALA A 1 71  ? 47.70060 19.01020 35.49341 1.000 56.60204  ? 66  ALA A O   1 
ATOM   516  C CB  . ALA A 1 71  ? 47.73278 18.73583 32.37366 1.000 61.72830  ? 66  ALA A CB  1 
ATOM   517  N N   . PRO A 1 72  ? 46.30067 17.30721 35.05322 1.000 58.67232  ? 67  PRO A N   1 
ATOM   518  C CA  . PRO A 1 72  ? 45.44799 16.49131 34.18385 1.000 57.32858  ? 67  PRO A CA  1 
ATOM   519  C C   . PRO A 1 72  ? 43.96178 16.85069 34.19896 1.000 51.96301  ? 67  PRO A C   1 
ATOM   520  O O   . PRO A 1 72  ? 43.14846 15.98434 33.85705 1.000 51.93658  ? 67  PRO A O   1 
ATOM   521  C CB  . PRO A 1 72  ? 45.64108 15.09416 34.75432 1.000 59.35656  ? 67  PRO A CB  1 
ATOM   522  C CG  . PRO A 1 72  ? 45.75571 15.35283 36.22905 1.000 62.40267  ? 67  PRO A CG  1 
ATOM   523  C CD  . PRO A 1 72  ? 46.47172 16.68096 36.37718 1.000 64.01903  ? 67  PRO A CD  1 
ATOM   524  N N   . TYR A 1 73  ? 43.61872 18.08263 34.58971 1.000 46.99489  ? 68  TYR A N   1 
ATOM   525  C CA  . TYR A 1 73  ? 42.24054 18.58134 34.51974 1.000 46.49682  ? 68  TYR A CA  1 
ATOM   526  C C   . TYR A 1 73  ? 41.31343 17.73832 35.38097 1.000 49.12339  ? 68  TYR A C   1 
ATOM   527  O O   . TYR A 1 73  ? 40.23177 17.32426 34.94884 1.000 45.11695  ? 68  TYR A O   1 
ATOM   528  C CB  . TYR A 1 73  ? 41.72010 18.62387 33.07905 1.000 47.90596  ? 68  TYR A CB  1 
ATOM   529  C CG  . TYR A 1 73  ? 42.73082 19.11728 32.08955 1.000 50.91549  ? 68  TYR A CG  1 
ATOM   530  C CD1 . TYR A 1 73  ? 43.20364 20.41863 32.14510 1.000 52.19205  ? 68  TYR A CD1 1 
ATOM   531  C CD2 . TYR A 1 73  ? 43.21534 18.28152 31.09526 1.000 53.30278  ? 68  TYR A CD2 1 
ATOM   532  C CE1 . TYR A 1 73  ? 44.15176 20.87369 31.23127 1.000 50.55239  ? 68  TYR A CE1 1 
ATOM   533  C CE2 . TYR A 1 73  ? 44.15261 18.72545 30.18535 1.000 55.21514  ? 68  TYR A CE2 1 
ATOM   534  C CZ  . TYR A 1 73  ? 44.61666 20.01973 30.25843 1.000 51.54351  ? 68  TYR A CZ  1 
ATOM   535  O OH  . TYR A 1 73  ? 45.55294 20.44881 29.35105 1.000 57.09901  ? 68  TYR A OH  1 
ATOM   536  N N   . ALA A 1 74  ? 41.74466 17.49225 36.61443 1.000 45.56622  ? 69  ALA A N   1 
ATOM   537  C CA  . ALA A 1 74  ? 41.00339 16.66042 37.54029 1.000 49.29095  ? 69  ALA A CA  1 
ATOM   538  C C   . ALA A 1 74  ? 40.96580 17.34250 38.90499 1.000 47.17438  ? 69  ALA A C   1 
ATOM   539  O O   . ALA A 1 74  ? 42.01281 17.72452 39.44362 1.000 49.06365  ? 69  ALA A O   1 
ATOM   540  C CB  . ALA A 1 74  ? 41.64030 15.26998 37.65035 1.000 56.13396  ? 69  ALA A CB  1 
ATOM   541  N N   . LEU A 1 75  ? 39.76283 17.49418 39.45476 1.000 44.91358  ? 70  LEU A N   1 
ATOM   542  C CA  . LEU A 1 75  ? 39.57201 18.10283 40.76708 1.000 44.22486  ? 70  LEU A CA  1 
ATOM   543  C C   . LEU A 1 75  ? 38.62722 17.26727 41.61520 1.000 49.18481  ? 70  LEU A C   1 
ATOM   544  O O   . LEU A 1 75  ? 37.71142 16.61329 41.10306 1.000 47.63036  ? 70  LEU A O   1 
ATOM   545  C CB  . LEU A 1 75  ? 38.99691 19.51951 40.66242 1.000 46.96874  ? 70  LEU A CB  1 
ATOM   546  C CG  . LEU A 1 75  ? 39.82103 20.56534 39.92471 1.000 47.49780  ? 70  LEU A CG  1 
ATOM   547  C CD1 . LEU A 1 75  ? 39.00375 21.83314 39.72737 1.000 41.35038  ? 70  LEU A CD1 1 
ATOM   548  C CD2 . LEU A 1 75  ? 41.09438 20.85144 40.70724 1.000 46.20763  ? 70  LEU A CD2 1 
ATOM   549  N N   . THR A 1 76  ? 38.82659 17.34647 42.93062 1.000 53.21386  ? 71  THR A N   1 
ATOM   550  C CA  . THR A 1 76  ? 37.81795 16.85908 43.85444 1.000 56.60094  ? 71  THR A CA  1 
ATOM   551  C C   . THR A 1 76  ? 36.52848 17.65372 43.64906 1.000 56.98795  ? 71  THR A C   1 
ATOM   552  O O   . THR A 1 76  ? 36.56860 18.81974 43.24541 1.000 53.99467  ? 71  THR A O   1 
ATOM   553  C CB  . THR A 1 76  ? 38.29148 17.00492 45.30503 1.000 56.72275  ? 71  THR A CB  1 
ATOM   554  O OG1 . THR A 1 76  ? 38.32856 18.39214 45.66169 1.000 54.78909  ? 71  THR A OG1 1 
ATOM   555  C CG2 . THR A 1 76  ? 39.68377 16.42749 45.49174 1.000 55.21550  ? 71  THR A CG2 1 
ATOM   556  N N   . PRO A 1 77  ? 35.36790 17.05243 43.91360 1.000 65.60797  ? 72  PRO A N   1 
ATOM   557  C CA  . PRO A 1 77  ? 34.11458 17.82808 43.83073 1.000 63.78909  ? 72  PRO A CA  1 
ATOM   558  C C   . PRO A 1 77  ? 34.11337 19.06501 44.72770 1.000 54.90532  ? 72  PRO A C   1 
ATOM   559  O O   . PRO A 1 77  ? 33.47876 20.07731 44.39661 1.000 55.33512  ? 72  PRO A O   1 
ATOM   560  C CB  . PRO A 1 77  ? 33.04652 16.81163 44.26503 1.000 71.82460  ? 72  PRO A CB  1 
ATOM   561  C CG  . PRO A 1 77  ? 33.69230 15.45986 44.08784 1.000 74.06861  ? 72  PRO A CG  1 
ATOM   562  C CD  . PRO A 1 77  ? 35.14256 15.67134 44.37614 1.000 72.32280  ? 72  PRO A CD  1 
ATOM   563  N N   . THR A 1 78  ? 34.82803 19.02185 45.84514 1.000 57.92074  ? 73  THR A N   1 
ATOM   564  C CA  . THR A 1 78  ? 34.90128 20.19899 46.70369 1.000 61.85191  ? 73  THR A CA  1 
ATOM   565  C C   . THR A 1 78  ? 35.70873 21.30797 46.04270 1.000 51.98758  ? 73  THR A C   1 
ATOM   566  O O   . THR A 1 78  ? 35.26814 22.45952 45.98823 1.000 49.86772  ? 73  THR A O   1 
ATOM   567  C CB  . THR A 1 78  ? 35.49967 19.81972 48.04704 1.000 62.08591  ? 73  THR A CB  1 
ATOM   568  O OG1 . THR A 1 78  ? 34.67694 18.81789 48.65271 1.000 72.50330  ? 73  THR A OG1 1 
ATOM   569  C CG2 . THR A 1 78  ? 35.58381 21.03533 48.97046 1.000 57.71731  ? 73  THR A CG2 1 
ATOM   570  N N   . ALA A 1 79  ? 36.90233 20.97589 45.54630 1.000 47.35915  ? 74  ALA A N   1 
ATOM   571  C CA  . ALA A 1 79  ? 37.69697 21.94526 44.79632 1.000 48.43900  ? 74  ALA A CA  1 
ATOM   572  C C   . ALA A 1 79  ? 36.92851 22.47968 43.59814 1.000 47.97845  ? 74  ALA A C   1 
ATOM   573  O O   . ALA A 1 79  ? 37.05061 23.66075 43.24584 1.000 41.12622  ? 74  ALA A O   1 
ATOM   574  C CB  . ALA A 1 79  ? 39.01081 21.30629 44.33954 1.000 52.84514  ? 74  ALA A CB  1 
ATOM   575  N N   . LEU A 1 80  ? 36.13913 21.62067 42.95085 1.000 48.20003  ? 75  LEU A N   1 
ATOM   576  C CA  . LEU A 1 80  ? 35.32517 22.06035 41.82210 1.000 47.19923  ? 75  LEU A CA  1 
ATOM   577  C C   . LEU A 1 80  ? 34.33063 23.14163 42.24499 1.000 43.99244  ? 75  LEU A C   1 
ATOM   578  O O   . LEU A 1 80  ? 34.13568 24.14006 41.53249 1.000 41.58276  ? 75  LEU A O   1 
ATOM   579  C CB  . LEU A 1 80  ? 34.61287 20.84442 41.23229 1.000 57.14741  ? 75  LEU A CB  1 
ATOM   580  C CG  . LEU A 1 80  ? 33.99775 20.81289 39.83868 1.000 53.01749  ? 75  LEU A CG  1 
ATOM   581  C CD1 . LEU A 1 80  ? 34.97511 21.28667 38.77510 1.000 38.47495  ? 75  LEU A CD1 1 
ATOM   582  C CD2 . LEU A 1 80  ? 33.52758 19.38482 39.57487 1.000 52.98663  ? 75  LEU A CD2 1 
ATOM   583  N N   . TYR A 1 81  ? 33.71419 22.97524 43.41651 1.000 48.06165  ? 76  TYR A N   1 
ATOM   584  C CA  . TYR A 1 81  ? 32.81183 24.00039 43.92760 1.000 47.86165  ? 76  TYR A CA  1 
ATOM   585  C C   . TYR A 1 81  ? 33.56026 25.26561 44.32501 1.000 46.60124  ? 76  TYR A C   1 
ATOM   586  O O   . TYR A 1 81  ? 33.09287 26.37755 44.05154 1.000 43.59965  ? 76  TYR A O   1 
ATOM   587  C CB  . TYR A 1 81  ? 32.02803 23.48201 45.12942 1.000 42.35305  ? 76  TYR A CB  1 
ATOM   588  C CG  . TYR A 1 81  ? 31.16042 24.57018 45.70868 1.000 53.00995  ? 76  TYR A CG  1 
ATOM   589  C CD1 . TYR A 1 81  ? 29.90352 24.83665 45.18203 1.000 54.59162  ? 76  TYR A CD1 1 
ATOM   590  C CD2 . TYR A 1 81  ? 31.60518 25.35558 46.77141 1.000 54.74194  ? 76  TYR A CD2 1 
ATOM   591  C CE1 . TYR A 1 81  ? 29.10840 25.84411 45.70467 1.000 54.98008  ? 76  TYR A CE1 1 
ATOM   592  C CE2 . TYR A 1 81  ? 30.82514 26.36247 47.28867 1.000 55.87361  ? 76  TYR A CE2 1 
ATOM   593  C CZ  . TYR A 1 81  ? 29.57510 26.59915 46.76261 1.000 58.62404  ? 76  TYR A CZ  1 
ATOM   594  O OH  . TYR A 1 81  ? 28.79499 27.60348 47.29158 1.000 67.39623  ? 76  TYR A OH  1 
ATOM   595  N N   . ASP A 1 82  ? 34.69259 25.12141 45.02550 1.000 43.59424  ? 77  ASP A N   1 
ATOM   596  C CA  . ASP A 1 82  ? 35.43241 26.30061 45.46350 1.000 45.63670  ? 77  ASP A CA  1 
ATOM   597  C C   . ASP A 1 82  ? 36.00689 27.09581 44.29086 1.000 43.37433  ? 77  ASP A C   1 
ATOM   598  O O   . ASP A 1 82  ? 36.08818 28.32735 44.36889 1.000 44.37253  ? 77  ASP A O   1 
ATOM   599  C CB  . ASP A 1 82  ? 36.55075 25.89608 46.42206 1.000 47.39939  ? 77  ASP A CB  1 
ATOM   600  C CG  . ASP A 1 82  ? 36.02893 25.52528 47.78661 1.000 53.35216  ? 77  ASP A CG  1 
ATOM   601  O OD1 . ASP A 1 82  ? 34.97046 26.06617 48.18510 1.000 50.37207  ? 77  ASP A OD1 1 
ATOM   602  O OD2 . ASP A 1 82  ? 36.68218 24.69813 48.45920 1.000 57.57333  ? 77  ASP A OD2 1 
ATOM   603  N N   . ALA A 1 83  ? 36.40623 26.42954 43.21034 1.000 41.15015  ? 78  ALA A N   1 
ATOM   604  C CA  . ALA A 1 83  ? 37.02234 27.12009 42.08251 1.000 38.65627  ? 78  ALA A CA  1 
ATOM   605  C C   . ALA A 1 83  ? 36.01853 27.54798 41.02070 1.000 40.36334  ? 78  ALA A C   1 
ATOM   606  O O   . ALA A 1 83  ? 36.41569 28.17850 40.03101 1.000 41.55841  ? 78  ALA A O   1 
ATOM   607  C CB  . ALA A 1 83  ? 38.10269 26.23985 41.44810 1.000 41.36175  ? 78  ALA A CB  1 
ATOM   608  N N   . ALA A 1 84  ? 34.73773 27.23375 41.20096 1.000 35.74271  ? 79  ALA A N   1 
ATOM   609  C CA  . ALA A 1 84  ? 33.73057 27.59355 40.21017 1.000 39.19254  ? 79  ALA A CA  1 
ATOM   610  C C   . ALA A 1 84  ? 33.63181 29.10985 40.06706 1.000 35.87405  ? 79  ALA A C   1 
ATOM   611  O O   . ALA A 1 84  ? 33.87371 29.86477 41.00824 1.000 40.03804  ? 79  ALA A O   1 
ATOM   612  C CB  . ALA A 1 84  ? 32.37032 27.01557 40.61190 1.000 42.45724  ? 79  ALA A CB  1 
ATOM   613  N N   . MET A 1 85  ? 33.28896 29.56546 38.85821 1.000 33.38486  ? 80  MET A N   1 
ATOM   614  C CA  . MET A 1 85  ? 33.01711 30.98949 38.67754 1.000 37.03815  ? 80  MET A CA  1 
ATOM   615  C C   . MET A 1 85  ? 31.79050 31.43515 39.47402 1.000 35.82466  ? 80  MET A C   1 
ATOM   616  O O   . MET A 1 85  ? 31.75496 32.56092 39.99202 1.000 38.83159  ? 80  MET A O   1 
ATOM   617  C CB  . MET A 1 85  ? 32.80142 31.28801 37.19353 1.000 38.52825  ? 80  MET A CB  1 
ATOM   618  C CG  . MET A 1 85  ? 32.39896 32.71030 36.89674 1.000 39.27715  ? 80  MET A CG  1 
ATOM   619  S SD  . MET A 1 85  ? 33.76665 33.87012 37.09080 1.000 47.96332  ? 80  MET A SD  1 
ATOM   620  C CE  . MET A 1 85  ? 34.81230 33.45437 35.67952 1.000 44.50078  ? 80  MET A CE  1 
ATOM   621  N N   . ILE A 1 86  ? 30.78461 30.57002 39.56843 1.000 40.15992  ? 81  ILE A N   1 
ATOM   622  C CA  . ILE A 1 86  ? 29.48969 30.88061 40.15960 1.000 43.94302  ? 81  ILE A CA  1 
ATOM   623  C C   . ILE A 1 86  ? 29.17381 29.80716 41.19414 1.000 42.91451  ? 81  ILE A C   1 
ATOM   624  O O   . ILE A 1 86  ? 29.30433 28.61063 40.90859 1.000 42.62205  ? 81  ILE A O   1 
ATOM   625  C CB  . ILE A 1 86  ? 28.38369 30.94210 39.08817 1.000 45.30538  ? 81  ILE A CB  1 
ATOM   626  C CG1 . ILE A 1 86  ? 28.68230 32.05083 38.06993 1.000 43.18807  ? 81  ILE A CG1 1 
ATOM   627  C CG2 . ILE A 1 86  ? 27.01942 31.14546 39.74035 1.000 50.91682  ? 81  ILE A CG2 1 
ATOM   628  C CD1 . ILE A 1 86  ? 28.86038 33.41990 38.69783 1.000 47.12926  ? 81  ILE A CD1 1 
ATOM   629  N N   . SER A 1 87  ? 28.74808 30.22893 42.37946 1.000 44.04504  ? 82  SER A N   1 
ATOM   630  C CA  . SER A 1 87  ? 28.48124 29.28279 43.46039 1.000 42.87245  ? 82  SER A CA  1 
ATOM   631  C C   . SER A 1 87  ? 27.08894 28.66653 43.33789 1.000 44.18444  ? 82  SER A C   1 
ATOM   632  O O   . SER A 1 87  ? 26.33743 28.61127 44.31421 1.000 45.12592  ? 82  SER A O   1 
ATOM   633  C CB  . SER A 1 87  ? 28.65253 29.96323 44.82009 1.000 44.59463  ? 82  SER A CB  1 
ATOM   634  O OG  . SER A 1 87  ? 27.68494 30.98155 45.05416 1.000 46.18147  ? 82  SER A OG  1 
ATOM   635  N N   . SER A 1 88  ? 26.74134 28.18350 42.14911 1.000 42.08380  ? 83  SER A N   1 
ATOM   636  C CA  . SER A 1 88  ? 25.44020 27.57146 41.92899 1.000 47.68823  ? 83  SER A CA  1 
ATOM   637  C C   . SER A 1 88  ? 25.44883 26.11475 42.38991 1.000 50.47648  ? 83  SER A C   1 
ATOM   638  O O   . SER A 1 88  ? 26.50069 25.48323 42.52246 1.000 49.75379  ? 83  SER A O   1 
ATOM   639  C CB  . SER A 1 88  ? 25.05908 27.64657 40.45219 1.000 49.81058  ? 83  SER A CB  1 
ATOM   640  O OG  . SER A 1 88  ? 26.01209 26.96266 39.66189 1.000 46.77260  ? 83  SER A OG  1 
ATOM   641  N N   . GLY A 1 89  ? 24.25218 25.57427 42.59999 1.000 49.97858  ? 84  GLY A N   1 
ATOM   642  C CA  . GLY A 1 89  ? 24.07178 24.26770 43.20031 1.000 56.86805  ? 84  GLY A CA  1 
ATOM   643  C C   . GLY A 1 89  ? 23.88588 23.15023 42.19021 1.000 55.82476  ? 84  GLY A C   1 
ATOM   644  O O   . GLY A 1 89  ? 24.24914 23.26376 41.01391 1.000 48.64646  ? 84  GLY A O   1 
ATOM   645  N N   . SER A 1 90  ? 23.32186 22.03892 42.67374 1.000 56.57673  ? 85  SER A N   1 
ATOM   646  C CA  . SER A 1 90  ? 23.06803 20.84468 41.86252 1.000 57.56306  ? 85  SER A CA  1 
ATOM   647  C C   . SER A 1 90  ? 24.33827 20.32258 41.20277 1.000 58.82851  ? 85  SER A C   1 
ATOM   648  O O   . SER A 1 90  ? 24.29992 19.79629 40.08845 1.000 66.68808  ? 85  SER A O   1 
ATOM   649  C CB  . SER A 1 90  ? 21.99409 21.10860 40.80568 1.000 58.42832  ? 85  SER A CB  1 
ATOM   650  O OG  . SER A 1 90  ? 20.73057 21.28687 41.41359 1.000 64.64511  ? 85  SER A OG  1 
ATOM   651  N N   . MET A 1 91  ? 25.47395 20.46292 41.88509 1.000 53.94071  ? 86  MET A N   1 
ATOM   652  C CA  . MET A 1 91  ? 26.74682 20.07076 41.28560 1.000 59.67090  ? 86  MET A CA  1 
ATOM   653  C C   . MET A 1 91  ? 26.81234 18.56837 41.02927 1.000 58.22342  ? 86  MET A C   1 
ATOM   654  O O   . MET A 1 91  ? 27.42141 18.13403 40.04583 1.000 56.26592  ? 86  MET A O   1 
ATOM   655  C CB  . MET A 1 91  ? 27.89460 20.52217 42.18891 1.000 66.54090  ? 86  MET A CB  1 
ATOM   656  C CG  . MET A 1 91  ? 29.26065 20.02111 41.79101 1.000 59.24865  ? 86  MET A CG  1 
ATOM   657  S SD  . MET A 1 91  ? 29.88661 20.92008 40.37035 1.000 58.76079  ? 86  MET A SD  1 
ATOM   658  C CE  . MET A 1 91  ? 30.30617 22.50159 41.08996 1.000 65.11924  ? 86  MET A CE  1 
ATOM   659  N N   . THR A 1 92  ? 26.19303 17.75895 41.89071 1.000 59.85660  ? 87  THR A N   1 
ATOM   660  C CA  . THR A 1 92  ? 26.21132 16.32113 41.65680 1.000 63.21999  ? 87  THR A CA  1 
ATOM   661  C C   . THR A 1 92  ? 25.41602 15.96584 40.40949 1.000 65.32219  ? 87  THR A C   1 
ATOM   662  O O   . THR A 1 92  ? 25.84940 15.12680 39.61015 1.000 67.70884  ? 87  THR A O   1 
ATOM   663  C CB  . THR A 1 92  ? 25.67505 15.56853 42.87365 1.000 71.56033  ? 87  THR A CB  1 
ATOM   664  O OG1 . THR A 1 92  ? 26.42789 15.93388 44.04055 1.000 72.46422  ? 87  THR A OG1 1 
ATOM   665  C CG2 . THR A 1 92  ? 25.79059 14.06313 42.64969 1.000 73.66721  ? 87  THR A CG2 1 
ATOM   666  N N   . ASN A 1 93  ? 24.26201 16.60976 40.21047 1.000 58.60509  ? 88  ASN A N   1 
ATOM   667  C CA  . ASN A 1 93  ? 23.47779 16.35282 39.00552 1.000 57.77878  ? 88  ASN A CA  1 
ATOM   668  C C   . ASN A 1 93  ? 24.24383 16.74852 37.74945 1.000 58.68606  ? 88  ASN A C   1 
ATOM   669  O O   . ASN A 1 93  ? 24.22617 16.02117 36.74572 1.000 60.01983  ? 88  ASN A O   1 
ATOM   670  C CB  . ASN A 1 93  ? 22.15054 17.10487 39.07272 1.000 57.12159  ? 88  ASN A CB  1 
ATOM   671  N N   . ARG A 1 94  ? 24.91629 17.90337 37.77836 1.000 52.23156  ? 89  ARG A N   1 
ATOM   672  C CA  . ARG A 1 94  ? 25.67402 18.33485 36.60585 1.000 49.06079  ? 89  ARG A CA  1 
ATOM   673  C C   . ARG A 1 94  ? 26.79511 17.36007 36.26929 1.000 52.57316  ? 89  ARG A C   1 
ATOM   674  O O   . ARG A 1 94  ? 27.00866 17.03671 35.09145 1.000 51.05657  ? 89  ARG A O   1 
ATOM   675  C CB  . ARG A 1 94  ? 26.22564 19.74204 36.82176 1.000 51.99254  ? 89  ARG A CB  1 
ATOM   676  C CG  . ARG A 1 94  ? 25.15414 20.81932 36.76280 1.000 53.12438  ? 89  ARG A CG  1 
ATOM   677  C CD  . ARG A 1 94  ? 25.73557 22.19917 36.98384 1.000 44.52376  ? 89  ARG A CD  1 
ATOM   678  N NE  . ARG A 1 94  ? 25.95523 22.49909 38.40326 1.000 45.08855  ? 89  ARG A NE  1 
ATOM   679  C CZ  . ARG A 1 94  ? 26.86891 23.37077 38.82167 1.000 49.56813  ? 89  ARG A CZ  1 
ATOM   680  N NH1 . ARG A 1 94  ? 27.63356 24.00154 37.92909 1.000 49.02645  ? 89  ARG A NH1 1 
ATOM   681  N NH2 . ARG A 1 94  ? 27.03050 23.60484 40.12112 1.000 52.69615  ? 89  ARG A NH2 1 
ATOM   682  N N   . ILE A 1 95  ? 27.52646 16.87938 37.27709 1.000 50.81291  ? 90  ILE A N   1 
ATOM   683  C CA  . ILE A 1 95  ? 28.59922 15.92377 37.00204 1.000 55.69193  ? 90  ILE A CA  1 
ATOM   684  C C   . ILE A 1 95  ? 28.03177 14.64560 36.39590 1.000 60.57254  ? 90  ILE A C   1 
ATOM   685  O O   . ILE A 1 95  ? 28.58038 14.10242 35.42397 1.000 57.20028  ? 90  ILE A O   1 
ATOM   686  C CB  . ILE A 1 95  ? 29.41110 15.64388 38.27843 1.000 56.78217  ? 90  ILE A CB  1 
ATOM   687  C CG1 . ILE A 1 95  ? 30.27488 16.85568 38.63809 1.000 55.75456  ? 90  ILE A CG1 1 
ATOM   688  C CG2 . ILE A 1 95  ? 30.28317 14.40384 38.11403 1.000 57.94348  ? 90  ILE A CG2 1 
ATOM   689  C CD1 . ILE A 1 95  ? 30.74701 16.85057 40.07703 1.000 62.22989  ? 90  ILE A CD1 1 
ATOM   690  N N   . ASP A 1 96  ? 26.91089 14.16076 36.94115 1.000 55.12065  ? 91  ASP A N   1 
ATOM   691  C CA  . ASP A 1 96  ? 26.24913 12.98516 36.37806 1.000 62.97122  ? 91  ASP A CA  1 
ATOM   692  C C   . ASP A 1 96  ? 25.92157 13.17764 34.90274 1.000 62.79431  ? 91  ASP A C   1 
ATOM   693  O O   . ASP A 1 96  ? 26.25974 12.33343 34.06280 1.000 62.55720  ? 91  ASP A O   1 
ATOM   694  C CB  . ASP A 1 96  ? 24.98017 12.67805 37.17271 1.000 69.94685  ? 91  ASP A CB  1 
ATOM   695  C CG  . ASP A 1 96  ? 25.27853 12.01200 38.47896 1.000 77.94951  ? 91  ASP A CG  1 
ATOM   696  O OD1 . ASP A 1 96  ? 26.35400 11.38434 38.56884 1.000 80.27524  ? 91  ASP A OD1 1 
ATOM   697  O OD2 . ASP A 1 96  ? 24.44990 12.10856 39.41064 1.000 87.32847  ? 91  ASP A OD2 1 
ATOM   698  N N   . ARG A 1 97  ? 25.25644 14.28653 34.57274 1.000 60.17617  ? 92  ARG A N   1 
ATOM   699  C CA  . ARG A 1 97  ? 24.90468 14.58539 33.18841 1.000 61.04724  ? 92  ARG A CA  1 
ATOM   700  C C   . ARG A 1 97  ? 26.14040 14.61399 32.29696 1.000 60.88780  ? 92  ARG A C   1 
ATOM   701  O O   . ARG A 1 97  ? 26.16834 13.98831 31.22512 1.000 61.28094  ? 92  ARG A O   1 
ATOM   702  C CB  . ARG A 1 97  ? 24.17168 15.92625 33.13661 1.000 64.08396  ? 92  ARG A CB  1 
ATOM   703  C CG  . ARG A 1 97  ? 22.83362 15.89530 32.42458 1.000 70.23222  ? 92  ARG A CG  1 
ATOM   704  C CD  . ARG A 1 97  ? 23.00884 15.76984 30.92388 1.000 74.61605  ? 92  ARG A CD  1 
ATOM   705  N NE  . ARG A 1 97  ? 23.79040 16.86590 30.35331 1.000 72.34766  ? 92  ARG A NE  1 
ATOM   706  C CZ  . ARG A 1 97  ? 24.07905 16.97696 29.05943 1.000 69.55716  ? 92  ARG A CZ  1 
ATOM   707  N NH1 . ARG A 1 97  ? 24.79940 17.99843 28.62026 1.000 66.36137  ? 92  ARG A NH1 1 
ATOM   708  N NH2 . ARG A 1 97  ? 23.64860 16.06012 28.20136 1.000 73.57074  ? 92  ARG A NH2 1 
ATOM   709  N N   . LEU A 1 98  ? 27.17415 15.34602 32.72847 1.000 57.65421  ? 93  LEU A N   1 
ATOM   710  C CA  . LEU A 1 98  ? 28.40523 15.45597 31.95400 1.000 55.19636  ? 93  LEU A CA  1 
ATOM   711  C C   . LEU A 1 98  ? 29.07841 14.10287 31.76734 1.000 58.85362  ? 93  LEU A C   1 
ATOM   712  O O   . LEU A 1 98  ? 29.77048 13.88476 30.76359 1.000 57.13826  ? 93  LEU A O   1 
ATOM   713  C CB  . LEU A 1 98  ? 29.35663 16.42960 32.64318 1.000 55.53068  ? 93  LEU A CB  1 
ATOM   714  C CG  . LEU A 1 98  ? 28.88888 17.88272 32.63295 1.000 54.55823  ? 93  LEU A CG  1 
ATOM   715  C CD1 . LEU A 1 98  ? 29.77207 18.73816 33.50727 1.000 48.92103  ? 93  LEU A CD1 1 
ATOM   716  C CD2 . LEU A 1 98  ? 28.89590 18.39981 31.22596 1.000 57.33473  ? 93  LEU A CD2 1 
ATOM   717  N N   . GLU A 1 99  ? 28.88799 13.18637 32.71532 1.000 66.00669  ? 94  GLU A N   1 
ATOM   718  C CA  . GLU A 1 99  ? 29.49504 11.86698 32.60626 1.000 63.31994  ? 94  GLU A CA  1 
ATOM   719  C C   . GLU A 1 99  ? 28.78247 11.02645 31.55673 1.000 67.97216  ? 94  GLU A C   1 
ATOM   720  O O   . GLU A 1 99  ? 29.42691 10.39742 30.70920 1.000 68.97953  ? 94  GLU A O   1 
ATOM   721  C CB  . GLU A 1 99  ? 29.47193 11.17099 33.96432 1.000 66.67195  ? 94  GLU A CB  1 
ATOM   722  C CG  . GLU A 1 99  ? 30.78841 10.51598 34.32287 1.000 77.04958  ? 94  GLU A CG  1 
ATOM   723  C CD  . GLU A 1 99  ? 30.63878 9.40239  35.33884 1.000 85.81262  ? 94  GLU A CD  1 
ATOM   724  O OE1 . GLU A 1 99  ? 29.66039 9.42615  36.12465 1.000 85.96103  ? 94  GLU A OE1 1 
ATOM   725  O OE2 . GLU A 1 99  ? 31.50397 8.49568  35.34296 1.000 90.92626  ? 94  GLU A OE2 1 
ATOM   726  N N   . LYS A 1 100 ? 27.44536 11.00683 31.59386 1.000 68.26018  ? 95  LYS A N   1 
ATOM   727  C CA  . LYS A 1 100 ? 26.69762 10.28021 30.57179 1.000 69.64364  ? 95  LYS A CA  1 
ATOM   728  C C   . LYS A 1 100 ? 26.92904 10.86877 29.18563 1.000 65.96859  ? 95  LYS A C   1 
ATOM   729  O O   . LYS A 1 100 ? 26.85282 10.14882 28.18641 1.000 68.58746  ? 95  LYS A O   1 
ATOM   730  C CB  . LYS A 1 100 ? 25.20534 10.28278 30.90250 1.000 70.49951  ? 95  LYS A CB  1 
ATOM   731  N N   . ALA A 1 101 ? 27.20672 12.16895 29.10265 1.000 59.43065  ? 96  ALA A N   1 
ATOM   732  C CA  . ALA A 1 101 ? 27.49286 12.81070 27.82674 1.000 60.23558  ? 96  ALA A CA  1 
ATOM   733  C C   . ALA A 1 101 ? 28.90668 12.53759 27.32663 1.000 61.68031  ? 96  ALA A C   1 
ATOM   734  O O   . ALA A 1 101 ? 29.19997 12.80748 26.15220 1.000 61.34455  ? 96  ALA A O   1 
ATOM   735  C CB  . ALA A 1 101 ? 27.26291 14.31793 27.93872 1.000 58.59445  ? 96  ALA A CB  1 
ATOM   736  N N   . GLY A 1 102 ? 29.78212 12.01070 28.17610 1.000 58.53811  ? 97  GLY A N   1 
ATOM   737  C CA  . GLY A 1 102 ? 31.11693 11.63338 27.76513 1.000 56.50227  ? 97  GLY A CA  1 
ATOM   738  C C   . GLY A 1 102 ? 32.17626 12.69664 27.93471 1.000 50.47233  ? 97  GLY A C   1 
ATOM   739  O O   . GLY A 1 102 ? 33.28128 12.52531 27.40957 1.000 52.68391  ? 97  GLY A O   1 
ATOM   740  N N   . TRP A 1 103 ? 31.88662 13.77165 28.67361 1.000 45.30057  ? 98  TRP A N   1 
ATOM   741  C CA  . TRP A 1 103 ? 32.78332 14.91513 28.78630 1.000 41.71585  ? 98  TRP A CA  1 
ATOM   742  C C   . TRP A 1 103 ? 33.61040 14.93898 30.06366 1.000 46.81229  ? 98  TRP A C   1 
ATOM   743  O O   . TRP A 1 103 ? 34.66115 15.58872 30.08793 1.000 47.18152  ? 98  TRP A O   1 
ATOM   744  C CB  . TRP A 1 103 ? 31.97871 16.20827 28.68519 1.000 44.30989  ? 98  TRP A CB  1 
ATOM   745  C CG  . TRP A 1 103 ? 31.33786 16.32152 27.35759 1.000 51.09962  ? 98  TRP A CG  1 
ATOM   746  C CD1 . TRP A 1 103 ? 31.84280 15.86634 26.16512 1.000 54.72404  ? 98  TRP A CD1 1 
ATOM   747  C CD2 . TRP A 1 103 ? 30.06348 16.89251 27.06010 1.000 53.98257  ? 98  TRP A CD2 1 
ATOM   748  N NE1 . TRP A 1 103 ? 30.96371 16.13112 25.15324 1.000 55.39622  ? 98  TRP A NE1 1 
ATOM   749  C CE2 . TRP A 1 103 ? 29.86642 16.76639 25.67046 1.000 55.34199  ? 98  TRP A CE2 1 
ATOM   750  C CE3 . TRP A 1 103 ? 29.07623 17.51345 27.82694 1.000 56.68631  ? 98  TRP A CE3 1 
ATOM   751  C CZ2 . TRP A 1 103 ? 28.71827 17.22760 25.03603 1.000 66.87763  ? 98  TRP A CZ2 1 
ATOM   752  C CZ3 . TRP A 1 103 ? 27.93552 17.97054 27.19654 1.000 62.37821  ? 98  TRP A CZ3 1 
ATOM   753  C CH2 . TRP A 1 103 ? 27.76632 17.82670 25.81319 1.000 64.57550  ? 98  TRP A CH2 1 
ATOM   754  N N   . VAL A 1 104 ? 33.15375 14.28475 31.12826 1.000 48.60394  ? 99  VAL A N   1 
ATOM   755  C CA  . VAL A 1 104 ? 33.96257 14.08690 32.32223 1.000 49.35095  ? 99  VAL A CA  1 
ATOM   756  C C   . VAL A 1 104 ? 33.92524 12.61447 32.67423 1.000 54.69609  ? 99  VAL A C   1 
ATOM   757  O O   . VAL A 1 104 ? 33.08292 11.85835 32.18926 1.000 55.16557  ? 99  VAL A O   1 
ATOM   758  C CB  . VAL A 1 104 ? 33.48896 14.92003 33.53076 1.000 50.23187  ? 99  VAL A CB  1 
ATOM   759  C CG1 . VAL A 1 104 ? 33.41527 16.38881 33.16331 1.000 46.56544  ? 99  VAL A CG1 1 
ATOM   760  C CG2 . VAL A 1 104 ? 32.14944 14.40689 34.04605 1.000 49.20775  ? 99  VAL A CG2 1 
ATOM   761  N N   . GLU A 1 105 ? 34.85622 12.21619 33.53714 1.000 58.07389  ? 100 GLU A N   1 
ATOM   762  C CA  . GLU A 1 105 ? 34.83374 10.89495 34.13807 1.000 66.31426  ? 100 GLU A CA  1 
ATOM   763  C C   . GLU A 1 105 ? 35.18942 11.01843 35.61280 1.000 61.99113  ? 100 GLU A C   1 
ATOM   764  O O   . GLU A 1 105 ? 35.86525 11.96445 36.02624 1.000 56.42622  ? 100 GLU A O   1 
ATOM   765  C CB  . GLU A 1 105 ? 35.79775 9.94393  33.43979 1.000 67.81975  ? 100 GLU A CB  1 
ATOM   766  C CG  . GLU A 1 105 ? 37.24536 10.37849 33.48825 1.000 70.51788  ? 100 GLU A CG  1 
ATOM   767  C CD  . GLU A 1 105 ? 38.13100 9.47606  32.65417 1.000 82.21265  ? 100 GLU A CD  1 
ATOM   768  O OE1 . GLU A 1 105 ? 37.62580 8.43827  32.16705 1.000 85.59642  ? 100 GLU A OE1 1 
ATOM   769  O OE2 . GLU A 1 105 ? 39.32573 9.80452  32.48359 1.000 83.75511  ? 100 GLU A OE2 1 
ATOM   770  N N   . ARG A 1 106 ? 34.71787 10.06077 36.40528 1.000 71.18046  ? 101 ARG A N   1 
ATOM   771  C CA  . ARG A 1 106 ? 34.99405 10.03090 37.83766 1.000 74.39780  ? 101 ARG A CA  1 
ATOM   772  C C   . ARG A 1 106 ? 36.12867 9.05026  38.09712 1.000 74.58144  ? 101 ARG A C   1 
ATOM   773  O O   . ARG A 1 106 ? 35.98699 7.84814  37.85775 1.000 79.75733  ? 101 ARG A O   1 
ATOM   774  C CB  . ARG A 1 106 ? 33.74794 9.65664  38.63239 1.000 77.06399  ? 101 ARG A CB  1 
ATOM   775  C CG  . ARG A 1 106 ? 32.76363 10.80489 38.82301 1.000 74.31998  ? 101 ARG A CG  1 
ATOM   776  C CD  . ARG A 1 106 ? 31.88194 10.52932 40.03919 1.000 77.73643  ? 101 ARG A CD  1 
ATOM   777  N NE  . ARG A 1 106 ? 30.67138 11.34592 40.06802 1.000 74.74410  ? 101 ARG A NE  1 
ATOM   778  C CZ  . ARG A 1 106 ? 29.59602 11.11457 39.32011 1.000 75.18882  ? 101 ARG A CZ  1 
ATOM   779  N NH1 . ARG A 1 106 ? 29.57919 10.10010 38.46560 1.000 78.50816  ? 101 ARG A NH1 1 
ATOM   780  N NH2 . ARG A 1 106 ? 28.53478 11.90063 39.42435 1.000 74.27787  ? 101 ARG A NH2 1 
ATOM   781  N N   . ARG A 1 107 ? 37.25497 9.57134  38.57712 1.000 76.88336  ? 102 ARG A N   1 
ATOM   782  C CA  . ARG A 1 107 ? 38.41454 8.75287  38.90284 1.000 85.89724  ? 102 ARG A CA  1 
ATOM   783  C C   . ARG A 1 107 ? 38.56638 8.62691  40.41552 1.000 94.09471  ? 102 ARG A C   1 
ATOM   784  O O   . ARG A 1 107 ? 37.56910 8.47569  41.12956 1.000 98.15991  ? 102 ARG A O   1 
ATOM   785  C CB  . ARG A 1 107 ? 39.67293 9.34236  38.26271 1.000 87.53441  ? 102 ARG A CB  1 
ATOM   786  C CG  . ARG A 1 107 ? 39.85546 8.95368  36.80572 1.000 89.80281  ? 102 ARG A CG  1 
ATOM   787  C CD  . ARG A 1 107 ? 40.56748 10.04141 36.00984 1.000 88.42571  ? 102 ARG A CD  1 
ATOM   788  N NE  . ARG A 1 107 ? 41.77233 10.52140 36.67950 1.000 91.31133  ? 102 ARG A NE  1 
ATOM   789  C CZ  . ARG A 1 107 ? 42.61986 11.39666 36.14902 1.000 88.39674  ? 102 ARG A CZ  1 
ATOM   790  N NH1 . ARG A 1 107 ? 42.39718 11.88416 34.93390 1.000 79.69520  ? 102 ARG A NH1 1 
ATOM   791  N NH2 . ARG A 1 107 ? 43.69144 11.77869 36.83358 1.000 92.49546  ? 102 ARG A NH2 1 
ATOM   792  N N   . ALA A 1 108 ? 39.79522 8.68721  40.91925 1.000 94.85801  ? 103 ALA A N   1 
ATOM   793  C CA  . ALA A 1 108 ? 40.03667 8.39681  42.33220 1.000 93.80014  ? 103 ALA A CA  1 
ATOM   794  C C   . ALA A 1 108 ? 41.08523 9.31740  42.95763 1.000 90.01414  ? 103 ALA A C   1 
ATOM   795  O O   . ALA A 1 108 ? 42.28891 9.08549  42.84766 1.000 88.32830  ? 103 ALA A O   1 
ATOM   796  C CB  . ALA A 1 108 ? 40.44730 6.94776  42.49290 1.000 101.10937 ? 103 ALA A CB  1 
ATOM   797  N N   . THR A 1 116 ? 38.63641 10.37784 45.14759 1.000 78.33396  ? 111 THR A N   1 
ATOM   798  C CA  . THR A 1 116 ? 37.56960 10.62008 44.16895 1.000 81.80518  ? 111 THR A CA  1 
ATOM   799  C C   . THR A 1 116 ? 37.74361 11.92726 43.40759 1.000 81.51445  ? 111 THR A C   1 
ATOM   800  O O   . THR A 1 116 ? 37.57864 13.01145 43.96513 1.000 76.51918  ? 111 THR A O   1 
ATOM   801  C CB  . THR A 1 116 ? 36.18223 10.65212 44.83450 1.000 83.11511  ? 111 THR A CB  1 
ATOM   802  O OG1 . THR A 1 116 ? 35.91974 9.39371  45.47328 1.000 87.52178  ? 111 THR A OG1 1 
ATOM   803  C CG2 . THR A 1 116 ? 35.10689 10.93505 43.79652 1.000 76.01049  ? 111 THR A CG2 1 
ATOM   804  N N   . LEU A 1 117 ? 38.04262 11.82795 42.11745 1.000 76.35417  ? 112 LEU A N   1 
ATOM   805  C CA  . LEU A 1 117 ? 38.25427 12.99780 41.28592 1.000 73.42536  ? 112 LEU A CA  1 
ATOM   806  C C   . LEU A 1 117 ? 37.20953 13.05337 40.17845 1.000 64.41310  ? 112 LEU A C   1 
ATOM   807  O O   . LEU A 1 117 ? 36.59110 12.04879 39.82142 1.000 69.22364  ? 112 LEU A O   1 
ATOM   808  C CB  . LEU A 1 117 ? 39.66282 12.99355 40.67691 1.000 76.85858  ? 112 LEU A CB  1 
ATOM   809  C CG  . LEU A 1 117 ? 40.80445 12.99875 41.69325 1.000 82.17839  ? 112 LEU A CG  1 
ATOM   810  C CD1 . LEU A 1 117 ? 42.14117 12.74452 41.00555 1.000 84.87729  ? 112 LEU A CD1 1 
ATOM   811  C CD2 . LEU A 1 117 ? 40.82949 14.32036 42.44303 1.000 77.42038  ? 112 LEU A CD2 1 
ATOM   812  N N   . VAL A 1 118 ? 37.00528 14.25540 39.65436 1.000 58.99910  ? 113 VAL A N   1 
ATOM   813  C CA  . VAL A 1 118 ? 36.23492 14.48501 38.43678 1.000 55.90758  ? 113 VAL A CA  1 
ATOM   814  C C   . VAL A 1 118 ? 37.19319 15.07247 37.41065 1.000 55.84378  ? 113 VAL A C   1 
ATOM   815  O O   . VAL A 1 118 ? 37.84956 16.08106 37.68784 1.000 54.09452  ? 113 VAL A O   1 
ATOM   816  C CB  . VAL A 1 118 ? 35.04536 15.43156 38.68634 1.000 54.76213  ? 113 VAL A CB  1 
ATOM   817  C CG1 . VAL A 1 118 ? 34.24576 15.64768 37.41315 1.000 52.78636  ? 113 VAL A CG1 1 
ATOM   818  C CG2 . VAL A 1 118 ? 34.15986 14.89997 39.82440 1.000 56.87219  ? 113 VAL A CG2 1 
ATOM   819  N N   . ALA A 1 119 ? 37.29328 14.43589 36.23849 1.000 55.27945  ? 114 ALA A N   1 
ATOM   820  C CA  . ALA A 1 119 ? 38.31546 14.78417 35.25977 1.000 52.03718  ? 114 ALA A CA  1 
ATOM   821  C C   . ALA A 1 119 ? 37.71445 14.92281 33.86694 1.000 53.96721  ? 114 ALA A C   1 
ATOM   822  O O   . ALA A 1 119 ? 36.82241 14.15486 33.49052 1.000 49.39630  ? 114 ALA A O   1 
ATOM   823  C CB  . ALA A 1 119 ? 39.43486 13.72592 35.20752 1.000 56.98560  ? 114 ALA A CB  1 
ATOM   824  N N   . LEU A 1 120 ? 38.21822 15.89740 33.10212 1.000 45.92903  ? 115 LEU A N   1 
ATOM   825  C CA  . LEU A 1 120 ? 37.82116 16.01351 31.70559 1.000 47.90967  ? 115 LEU A CA  1 
ATOM   826  C C   . LEU A 1 120 ? 38.20415 14.74549 30.97086 1.000 50.72938  ? 115 LEU A C   1 
ATOM   827  O O   . LEU A 1 120 ? 39.22746 14.11614 31.26248 1.000 52.33643  ? 115 LEU A O   1 
ATOM   828  C CB  . LEU A 1 120 ? 38.49101 17.21194 31.02018 1.000 51.37060  ? 115 LEU A CB  1 
ATOM   829  C CG  . LEU A 1 120 ? 38.17331 18.63205 31.48381 1.000 51.24410  ? 115 LEU A CG  1 
ATOM   830  C CD1 . LEU A 1 120 ? 39.06446 19.59649 30.72991 1.000 47.64731  ? 115 LEU A CD1 1 
ATOM   831  C CD2 . LEU A 1 120 ? 36.70242 18.98495 31.28062 1.000 46.24429  ? 115 LEU A CD2 1 
ATOM   832  N N   . THR A 1 121 ? 37.35681 14.35142 30.03988 1.000 50.71790  ? 116 THR A N   1 
ATOM   833  C CA  . THR A 1 121 ? 37.79685 13.39975 29.04416 1.000 52.29769  ? 116 THR A CA  1 
ATOM   834  C C   . THR A 1 121 ? 38.50594 14.14809 27.91479 1.000 49.67079  ? 116 THR A C   1 
ATOM   835  O O   . THR A 1 121 ? 38.53445 15.38830 27.87532 1.000 43.94955  ? 116 THR A O   1 
ATOM   836  C CB  . THR A 1 121 ? 36.61187 12.60082 28.51361 1.000 53.63632  ? 116 THR A CB  1 
ATOM   837  O OG1 . THR A 1 121 ? 35.68948 13.50144 27.88402 1.000 50.89405  ? 116 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 121 ? 35.90373 11.89007 29.66391 1.000 55.75140  ? 116 THR A CG2 1 
ATOM   839  N N   . SER A 1 122 ? 39.11632 13.37963 27.01368 1.000 46.35911  ? 117 SER A N   1 
ATOM   840  C CA  . SER A 1 122 ? 39.65921 13.97619 25.79574 1.000 45.85002  ? 117 SER A CA  1 
ATOM   841  C C   . SER A 1 122 ? 38.57963 14.77297 25.07791 1.000 45.90450  ? 117 SER A C   1 
ATOM   842  O O   . SER A 1 122 ? 38.80524 15.91971 24.67123 1.000 53.98371  ? 117 SER A O   1 
ATOM   843  C CB  . SER A 1 122 ? 40.24111 12.89340 24.88591 1.000 57.07662  ? 117 SER A CB  1 
ATOM   844  O OG  . SER A 1 122 ? 39.21454 12.05484 24.39750 1.000 63.47770  ? 117 SER A OG  1 
ATOM   845  N N   . ALA A 1 123 ? 37.38079 14.19176 24.95458 1.000 47.13149  ? 118 ALA A N   1 
ATOM   846  C CA  . ALA A 1 123 ? 36.27907 14.86637 24.27698 1.000 42.60759  ? 118 ALA A CA  1 
ATOM   847  C C   . ALA A 1 123 ? 35.83717 16.10746 25.03108 1.000 48.26639  ? 118 ALA A C   1 
ATOM   848  O O   . ALA A 1 123 ? 35.44725 17.11029 24.42019 1.000 43.81612  ? 118 ALA A O   1 
ATOM   849  C CB  . ALA A 1 123 ? 35.09769 13.91226 24.11116 1.000 45.68605  ? 118 ALA A CB  1 
ATOM   850  N N   . GLY A 1 124 ? 35.88166 16.05845 26.36287 1.000 45.63235  ? 119 GLY A N   1 
ATOM   851  C CA  . GLY A 1 124 ? 35.44676 17.19049 27.14679 1.000 42.22606  ? 119 GLY A CA  1 
ATOM   852  C C   . GLY A 1 124 ? 36.45497 18.31542 27.11205 1.000 39.72704  ? 119 GLY A C   1 
ATOM   853  O O   . GLY A 1 124 ? 36.07786 19.48823 27.06741 1.000 39.68043  ? 119 GLY A O   1 
ATOM   854  N N   . ARG A 1 125 ? 37.74346 17.96732 27.14408 1.000 41.17358  ? 120 ARG A N   1 
ATOM   855  C CA  . ARG A 1 125 ? 38.78391 18.96915 26.95296 1.000 40.09907  ? 120 ARG A CA  1 
ATOM   856  C C   . ARG A 1 125 ? 38.64072 19.65271 25.59262 1.000 45.37657  ? 120 ARG A C   1 
ATOM   857  O O   . ARG A 1 125 ? 38.72601 20.88224 25.48679 1.000 48.32047  ? 120 ARG A O   1 
ATOM   858  C CB  . ARG A 1 125 ? 40.15676 18.31625 27.07327 1.000 44.01401  ? 120 ARG A CB  1 
ATOM   859  C CG  . ARG A 1 125 ? 41.29065 19.29798 27.11593 1.000 47.09380  ? 120 ARG A CG  1 
ATOM   860  C CD  . ARG A 1 125 ? 42.10391 19.22910 25.85763 1.000 62.12797  ? 120 ARG A CD  1 
ATOM   861  N NE  . ARG A 1 125 ? 43.33404 19.99704 25.98219 1.000 71.23446  ? 120 ARG A NE  1 
ATOM   862  C CZ  . ARG A 1 125 ? 44.53554 19.46206 26.16381 1.000 75.26444  ? 120 ARG A CZ  1 
ATOM   863  N NH1 . ARG A 1 125 ? 44.67955 18.14298 26.23812 1.000 73.94957  ? 120 ARG A NH1 1 
ATOM   864  N NH2 . ARG A 1 125 ? 45.59399 20.25151 26.26559 1.000 76.57561  ? 120 ARG A NH2 1 
ATOM   865  N N   . ALA A 1 126 ? 38.44975 18.86901 24.53407 1.000 42.27139  ? 121 ALA A N   1 
ATOM   866  C CA  . ALA A 1 126 ? 38.31151 19.47767 23.20978 1.000 43.43818  ? 121 ALA A CA  1 
ATOM   867  C C   . ALA A 1 126 ? 37.11268 20.42100 23.16270 1.000 45.31908  ? 121 ALA A C   1 
ATOM   868  O O   . ALA A 1 126 ? 37.19043 21.50935 22.57600 1.000 43.70111  ? 121 ALA A O   1 
ATOM   869  C CB  . ALA A 1 126 ? 38.19417 18.39492 22.14051 1.000 45.43958  ? 121 ALA A CB  1 
ATOM   870  N N   . LEU A 1 127 ? 36.00138 20.02634 23.78982 1.000 43.14116  ? 122 LEU A N   1 
ATOM   871  C CA  . LEU A 1 127 ? 34.78531 20.83056 23.73996 1.000 44.59576  ? 122 LEU A CA  1 
ATOM   872  C C   . LEU A 1 127 ? 34.99025 22.17724 24.41795 1.000 40.51304  ? 122 LEU A C   1 
ATOM   873  O O   . LEU A 1 127 ? 34.65109 23.22468 23.85285 1.000 44.64634  ? 122 LEU A O   1 
ATOM   874  C CB  . LEU A 1 127 ? 33.62666 20.06969 24.39186 1.000 47.27514  ? 122 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 127 ? 32.33172 20.88318 24.49687 1.000 46.13107  ? 122 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 127 ? 31.83862 21.27839 23.11627 1.000 52.34158  ? 122 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 127 ? 31.25649 20.11973 25.24926 1.000 43.62467  ? 122 LEU A CD2 1 
ATOM   878  N N   . ILE A 1 128 ? 35.54170 22.16631 25.63891 1.000 37.56244  ? 123 ILE A N   1 
ATOM   879  C CA  . ILE A 1 128 ? 35.71559 23.40247 26.40049 1.000 37.02277  ? 123 ILE A CA  1 
ATOM   880  C C   . ILE A 1 128 ? 36.77864 24.29675 25.76067 1.000 41.29567  ? 123 ILE A C   1 
ATOM   881  O O   . ILE A 1 128 ? 36.65369 25.52834 25.78875 1.000 40.10665  ? 123 ILE A O   1 
ATOM   882  C CB  . ILE A 1 128 ? 36.01772 23.08327 27.88688 1.000 38.99600  ? 123 ILE A CB  1 
ATOM   883  C CG1 . ILE A 1 128 ? 35.82674 24.33011 28.76038 1.000 36.28299  ? 123 ILE A CG1 1 
ATOM   884  C CG2 . ILE A 1 128 ? 37.41820 22.51072 28.07049 1.000 42.95866  ? 123 ILE A CG2 1 
ATOM   885  C CD1 . ILE A 1 128 ? 34.42004 24.91783 28.67659 1.000 37.67636  ? 123 ILE A CD1 1 
ATOM   886  N N   . ASP A 1 129 ? 37.81523 23.70989 25.15173 1.000 42.91252  ? 124 ASP A N   1 
ATOM   887  C CA  . ASP A 1 129 ? 38.80269 24.51650 24.43660 1.000 47.40248  ? 124 ASP A CA  1 
ATOM   888  C C   . ASP A 1 129 ? 38.15227 25.28658 23.29012 1.000 49.39086  ? 124 ASP A C   1 
ATOM   889  O O   . ASP A 1 129 ? 38.49373 26.44799 23.03624 1.000 50.91160  ? 124 ASP A O   1 
ATOM   890  C CB  . ASP A 1 129 ? 39.93229 23.63027 23.90532 1.000 47.80302  ? 124 ASP A CB  1 
ATOM   891  C CG  . ASP A 1 129 ? 41.01430 23.34835 24.94649 1.000 54.38337  ? 124 ASP A CG  1 
ATOM   892  O OD1 . ASP A 1 129 ? 41.17924 24.14849 25.89182 1.000 49.24934  ? 124 ASP A OD1 1 
ATOM   893  O OD2 . ASP A 1 129 ? 41.72353 22.32675 24.79335 1.000 57.35735  ? 124 ASP A OD2 1 
ATOM   894  N N   . ASP A 1 130 ? 37.21746 24.64285 22.58547 1.000 47.62536  ? 125 ASP A N   1 
ATOM   895  C CA  . ASP A 1 130 ? 36.42751 25.30340 21.54692 1.000 53.08691  ? 125 ASP A CA  1 
ATOM   896  C C   . ASP A 1 130 ? 35.44938 26.31417 22.15157 1.000 52.23897  ? 125 ASP A C   1 
ATOM   897  O O   . ASP A 1 130 ? 35.38614 27.47429 21.72027 1.000 47.78200  ? 125 ASP A O   1 
ATOM   898  C CB  . ASP A 1 130 ? 35.67638 24.23277 20.75254 1.000 56.39882  ? 125 ASP A CB  1 
ATOM   899  C CG  . ASP A 1 130 ? 35.21634 24.70339 19.38583 1.000 69.18260  ? 125 ASP A CG  1 
ATOM   900  O OD1 . ASP A 1 130 ? 35.26654 25.91810 19.08520 1.000 73.99352  ? 125 ASP A OD1 1 
ATOM   901  O OD2 . ASP A 1 130 ? 34.79878 23.82272 18.60751 1.000 69.67190  ? 125 ASP A OD2 1 
ATOM   902  N N   . ALA A 1 131 ? 34.67366 25.88854 23.15091 1.000 42.32264  ? 126 ALA A N   1 
ATOM   903  C CA  . ALA A 1 131 ? 33.58067 26.72449 23.63732 1.000 44.53279  ? 126 ALA A CA  1 
ATOM   904  C C   . ALA A 1 131 ? 34.07901 27.98028 24.34350 1.000 44.49805  ? 126 ALA A C   1 
ATOM   905  O O   . ALA A 1 131 ? 33.42143 29.02681 24.26732 1.000 44.77827  ? 126 ALA A O   1 
ATOM   906  C CB  . ALA A 1 131 ? 32.67446 25.93135 24.58123 1.000 45.00706  ? 126 ALA A CB  1 
ATOM   907  N N   . VAL A 1 132 ? 35.22336 27.91259 25.03163 1.000 40.47675  ? 127 VAL A N   1 
ATOM   908  C CA  . VAL A 1 132 ? 35.64262 29.08512 25.79705 1.000 40.23275  ? 127 VAL A CA  1 
ATOM   909  C C   . VAL A 1 132 ? 36.00353 30.24123 24.85935 1.000 41.00148  ? 127 VAL A C   1 
ATOM   910  O O   . VAL A 1 132 ? 35.80643 31.41544 25.20332 1.000 43.75374  ? 127 VAL A O   1 
ATOM   911  C CB  . VAL A 1 132 ? 36.80214 28.74065 26.75121 1.000 39.03955  ? 127 VAL A CB  1 
ATOM   912  C CG1 . VAL A 1 132 ? 38.07954 28.45041 25.98930 1.000 42.49573  ? 127 VAL A CG1 1 
ATOM   913  C CG2 . VAL A 1 132 ? 37.01700 29.87896 27.73580 1.000 44.70946  ? 127 VAL A CG2 1 
ATOM   914  N N   . VAL A 1 133 ? 36.52893 29.94065 23.67682 1.000 45.30508  ? 128 VAL A N   1 
ATOM   915  C CA  . VAL A 1 133 ? 36.84276 31.00050 22.72180 1.000 47.87972  ? 128 VAL A CA  1 
ATOM   916  C C   . VAL A 1 133 ? 35.55985 31.66762 22.23832 1.000 48.79354  ? 128 VAL A C   1 
ATOM   917  O O   . VAL A 1 133 ? 35.46311 32.90202 22.19678 1.000 52.19400  ? 128 VAL A O   1 
ATOM   918  C CB  . VAL A 1 133 ? 37.68522 30.43398 21.56353 1.000 53.08768  ? 128 VAL A CB  1 
ATOM   919  C CG1 . VAL A 1 133 ? 37.79262 31.43241 20.40611 1.000 56.70022  ? 128 VAL A CG1 1 
ATOM   920  C CG2 . VAL A 1 133 ? 39.07553 30.03987 22.06999 1.000 52.65593  ? 128 VAL A CG2 1 
ATOM   921  N N   . ALA A 1 134 ? 34.53852 30.86571 21.91579 1.000 46.74041  ? 129 ALA A N   1 
ATOM   922  C CA  . ALA A 1 134 ? 33.25402 31.42967 21.51054 1.000 51.86661  ? 129 ALA A CA  1 
ATOM   923  C C   . ALA A 1 134 ? 32.62760 32.22307 22.64787 1.000 47.78275  ? 129 ALA A C   1 
ATOM   924  O O   . ALA A 1 134 ? 32.02815 33.28916 22.42134 1.000 42.90868  ? 129 ALA A O   1 
ATOM   925  C CB  . ALA A 1 134 ? 32.31117 30.31584 21.04666 1.000 50.98703  ? 129 ALA A CB  1 
ATOM   926  N N   . HIS A 1 135 ? 32.77334 31.71017 23.87975 1.000 42.74887  ? 130 HIS A N   1 
ATOM   927  C CA  . HIS A 1 135 ? 32.20384 32.33664 25.06965 1.000 39.54469  ? 130 HIS A CA  1 
ATOM   928  C C   . HIS A 1 135 ? 32.76531 33.73515 25.29510 1.000 42.25651  ? 130 HIS A C   1 
ATOM   929  O O   . HIS A 1 135 ? 32.01136 34.67728 25.55888 1.000 42.49474  ? 130 HIS A O   1 
ATOM   930  C CB  . HIS A 1 135 ? 32.45618 31.43884 26.28608 1.000 36.07497  ? 130 HIS A CB  1 
ATOM   931  C CG  . HIS A 1 135 ? 32.02310 32.03580 27.58393 1.000 37.57767  ? 130 HIS A CG  1 
ATOM   932  N ND1 . HIS A 1 135 ? 30.71932 32.40831 27.83553 1.000 38.35715  ? 130 HIS A ND1 1 
ATOM   933  C CD2 . HIS A 1 135 ? 32.71610 32.29134 28.71983 1.000 41.42163  ? 130 HIS A CD2 1 
ATOM   934  C CE1 . HIS A 1 135 ? 30.63034 32.87068 29.07195 1.000 41.85236  ? 130 HIS A CE1 1 
ATOM   935  N NE2 . HIS A 1 135 ? 31.83177 32.82908 29.62021 1.000 36.71386  ? 130 HIS A NE2 1 
ATOM   936  N N   . VAL A 1 136 ? 34.08528 33.90499 25.18483 1.000 41.67895  ? 131 VAL A N   1 
ATOM   937  C CA  . VAL A 1 136 ? 34.64080 35.22286 25.48019 1.000 46.76621  ? 131 VAL A CA  1 
ATOM   938  C C   . VAL A 1 136 ? 34.28656 36.22260 24.38088 1.000 48.36958  ? 131 VAL A C   1 
ATOM   939  O O   . VAL A 1 136 ? 34.04503 37.40196 24.66504 1.000 51.75664  ? 131 VAL A O   1 
ATOM   940  C CB  . VAL A 1 136 ? 36.15892 35.15099 25.73185 1.000 48.01329  ? 131 VAL A CB  1 
ATOM   941  C CG1 . VAL A 1 136 ? 36.43087 34.47784 27.07624 1.000 44.13790  ? 131 VAL A CG1 1 
ATOM   942  C CG2 . VAL A 1 136 ? 36.86140 34.42286 24.62581 1.000 54.86488  ? 131 VAL A CG2 1 
ATOM   943  N N   . ASP A 1 137 ? 34.22595 35.78105 23.11819 1.000 54.57346  ? 132 ASP A N   1 
ATOM   944  C CA  . ASP A 1 137 ? 33.73698 36.68387 22.07282 1.000 54.69926  ? 132 ASP A CA  1 
ATOM   945  C C   . ASP A 1 137 ? 32.30019 37.10762 22.34729 1.000 51.84683  ? 132 ASP A C   1 
ATOM   946  O O   . ASP A 1 137 ? 31.94580 38.27914 22.17129 1.000 53.82490  ? 132 ASP A O   1 
ATOM   947  C CB  . ASP A 1 137 ? 33.81539 36.04955 20.68572 1.000 58.15636  ? 132 ASP A CB  1 
ATOM   948  C CG  . ASP A 1 137 ? 33.12372 36.91225 19.62244 1.000 71.66194  ? 132 ASP A CG  1 
ATOM   949  O OD1 . ASP A 1 137 ? 33.73957 37.90306 19.16730 1.000 77.87079  ? 132 ASP A OD1 1 
ATOM   950  O OD2 . ASP A 1 137 ? 31.95534 36.62702 19.26320 1.000 70.74811  ? 132 ASP A OD2 1 
ATOM   951  N N   . ASN A 1 138 ? 31.45759 36.16004 22.77095 1.000 46.78670  ? 133 ASN A N   1 
ATOM   952  C CA  . ASN A 1 138 ? 30.08058 36.48507 23.13899 1.000 45.20938  ? 133 ASN A CA  1 
ATOM   953  C C   . ASN A 1 138 ? 30.02912 37.48525 24.28882 1.000 48.26780  ? 133 ASN A C   1 
ATOM   954  O O   . ASN A 1 138 ? 29.22335 38.42691 24.27068 1.000 46.93189  ? 133 ASN A O   1 
ATOM   955  C CB  . ASN A 1 138 ? 29.34069 35.20395 23.51028 1.000 41.88437  ? 133 ASN A CB  1 
ATOM   956  C CG  . ASN A 1 138 ? 27.82666 35.36649 23.54199 1.000 43.82038  ? 133 ASN A CG  1 
ATOM   957  O OD1 . ASN A 1 138 ? 27.23212 36.14490 22.77433 1.000 45.71983  ? 133 ASN A OD1 1 
ATOM   958  N ND2 . ASN A 1 138 ? 27.18846 34.58993 24.41236 1.000 42.47747  ? 133 ASN A ND2 1 
ATOM   959  N N   . GLN A 1 139 ? 30.88342 37.29975 25.29638 1.000 48.54945  ? 134 GLN A N   1 
ATOM   960  C CA  . GLN A 1 139 ? 30.88777 38.21273 26.43513 1.000 48.20323  ? 134 GLN A CA  1 
ATOM   961  C C   . GLN A 1 139 ? 31.29683 39.61889 26.01441 1.000 45.72950  ? 134 GLN A C   1 
ATOM   962  O O   . GLN A 1 139 ? 30.75610 40.60776 26.52099 1.000 47.36147  ? 134 GLN A O   1 
ATOM   963  C CB  . GLN A 1 139 ? 31.81912 37.69468 27.53172 1.000 42.79709  ? 134 GLN A CB  1 
ATOM   964  C CG  . GLN A 1 139 ? 31.32694 36.46148 28.24099 1.000 40.12622  ? 134 GLN A CG  1 
ATOM   965  C CD  . GLN A 1 139 ? 32.02967 36.25315 29.56424 1.000 46.45026  ? 134 GLN A CD  1 
ATOM   966  O OE1 . GLN A 1 139 ? 31.41655 35.81523 30.54952 1.000 47.82871  ? 134 GLN A OE1 1 
ATOM   967  N NE2 . GLN A 1 139 ? 33.32047 36.56729 29.60243 1.000 46.24741  ? 134 GLN A NE2 1 
ATOM   968  N N   . ARG A 1 140 ? 32.25508 39.73949 25.09959 1.000 49.29957  ? 135 ARG A N   1 
ATOM   969  C CA  . ARG A 1 140 ? 32.64943 41.07838 24.68917 1.000 52.75575  ? 135 ARG A CA  1 
ATOM   970  C C   . ARG A 1 140 ? 31.50669 41.77595 23.96677 1.000 57.20228  ? 135 ARG A C   1 
ATOM   971  O O   . ARG A 1 140 ? 31.30015 42.98327 24.13614 1.000 61.77428  ? 135 ARG A O   1 
ATOM   972  C CB  . ARG A 1 140 ? 33.90442 41.02357 23.81578 1.000 62.88435  ? 135 ARG A CB  1 
ATOM   973  C CG  . ARG A 1 140 ? 35.14574 40.57561 24.57686 1.000 66.93163  ? 135 ARG A CG  1 
ATOM   974  C CD  . ARG A 1 140 ? 36.39995 40.70188 23.72079 1.000 72.00079  ? 135 ARG A CD  1 
ATOM   975  N NE  . ARG A 1 140 ? 36.39630 39.78840 22.58172 1.000 75.33498  ? 135 ARG A NE  1 
ATOM   976  C CZ  . ARG A 1 140 ? 37.08306 38.65131 22.53249 1.000 79.05268  ? 135 ARG A CZ  1 
ATOM   977  N NH1 . ARG A 1 140 ? 37.83416 38.28494 23.56444 1.000 83.69651  ? 135 ARG A NH1 1 
ATOM   978  N NH2 . ARG A 1 140 ? 37.01773 37.87860 21.45445 1.000 75.75518  ? 135 ARG A NH2 1 
ATOM   979  N N   . ARG A 1 141 ? 30.74026 41.02634 23.16904 1.000 50.60973  ? 136 ARG A N   1 
ATOM   980  C CA  . ARG A 1 141 ? 29.58069 41.60636 22.50269 1.000 52.55946  ? 136 ARG A CA  1 
ATOM   981  C C   . ARG A 1 141 ? 28.48330 41.96366 23.50300 1.000 54.80104  ? 136 ARG A C   1 
ATOM   982  O O   . ARG A 1 141 ? 27.72555 42.91584 23.27732 1.000 56.10241  ? 136 ARG A O   1 
ATOM   983  C CB  . ARG A 1 141 ? 29.06453 40.63622 21.43610 1.000 57.05385  ? 136 ARG A CB  1 
ATOM   984  C CG  . ARG A 1 141 ? 30.08200 40.35330 20.32044 1.000 61.02454  ? 136 ARG A CG  1 
ATOM   985  N N   . VAL A 1 142 ? 28.39659 41.22668 24.61121 1.000 50.79721  ? 137 VAL A N   1 
ATOM   986  C CA  . VAL A 1 142 ? 27.44288 41.55809 25.67114 1.000 44.62699  ? 137 VAL A CA  1 
ATOM   987  C C   . VAL A 1 142 ? 27.82188 42.87128 26.34171 1.000 47.34583  ? 137 VAL A C   1 
ATOM   988  O O   . VAL A 1 142 ? 26.95620 43.69688 26.65612 1.000 54.10286  ? 137 VAL A O   1 
ATOM   989  C CB  . VAL A 1 142 ? 27.36536 40.39942 26.67966 1.000 47.27042  ? 137 VAL A CB  1 
ATOM   990  C CG1 . VAL A 1 142 ? 26.72377 40.84804 28.01270 1.000 44.14452  ? 137 VAL A CG1 1 
ATOM   991  C CG2 . VAL A 1 142 ? 26.60802 39.22664 26.08132 1.000 47.90802  ? 137 VAL A CG2 1 
ATOM   992  N N   . LEU A 1 143 ? 29.11480 43.09889 26.54998 1.000 48.52029  ? 138 LEU A N   1 
ATOM   993  C CA  . LEU A 1 143 ? 29.59414 44.26317 27.28313 1.000 55.03672  ? 138 LEU A CA  1 
ATOM   994  C C   . LEU A 1 143 ? 29.91638 45.45945 26.39550 1.000 57.66395  ? 138 LEU A C   1 
ATOM   995  O O   . LEU A 1 143 ? 30.39817 46.47800 26.90408 1.000 60.01448  ? 138 LEU A O   1 
ATOM   996  C CB  . LEU A 1 143 ? 30.83493 43.88781 28.08632 1.000 56.13230  ? 138 LEU A CB  1 
ATOM   997  C CG  . LEU A 1 143 ? 30.57320 42.85810 29.18716 1.000 49.08030  ? 138 LEU A CG  1 
ATOM   998  C CD1 . LEU A 1 143 ? 31.87884 42.24229 29.61651 1.000 47.32687  ? 138 LEU A CD1 1 
ATOM   999  C CD2 . LEU A 1 143 ? 29.88223 43.51451 30.36237 1.000 47.13525  ? 138 LEU A CD2 1 
ATOM   1000 N N   . SER A 1 144 ? 29.66932 45.36904 25.09118 1.000 60.13999  ? 139 SER A N   1 
ATOM   1001 C CA  . SER A 1 144 ? 30.16302 46.39334 24.17385 1.000 65.47021  ? 139 SER A CA  1 
ATOM   1002 C C   . SER A 1 144 ? 29.51832 47.75954 24.38979 1.000 66.93226  ? 139 SER A C   1 
ATOM   1003 O O   . SER A 1 144 ? 30.09607 48.76638 23.96980 1.000 72.69608  ? 139 SER A O   1 
ATOM   1004 C CB  . SER A 1 144 ? 29.96409 45.94275 22.72612 1.000 64.42455  ? 139 SER A CB  1 
ATOM   1005 O OG  . SER A 1 144 ? 28.64718 45.47767 22.51251 1.000 66.23148  ? 139 SER A OG  1 
ATOM   1006 N N   . ALA A 1 145 ? 28.35009 47.82764 25.03391 1.000 68.81041  ? 140 ALA A N   1 
ATOM   1007 C CA  . ALA A 1 145 ? 27.74033 49.12861 25.30042 1.000 72.74099  ? 140 ALA A CA  1 
ATOM   1008 C C   . ALA A 1 145 ? 28.55960 49.94436 26.29501 1.000 77.98654  ? 140 ALA A C   1 
ATOM   1009 O O   . ALA A 1 145 ? 28.51422 51.18106 26.26626 1.000 82.37859  ? 140 ALA A O   1 
ATOM   1010 C CB  . ALA A 1 145 ? 26.31180 48.95207 25.81615 1.000 64.45607  ? 140 ALA A CB  1 
ATOM   1011 N N   . LEU A 1 146 ? 29.30984 49.27743 27.17004 1.000 69.18993  ? 141 LEU A N   1 
ATOM   1012 C CA  . LEU A 1 146 ? 30.13914 49.93546 28.16902 1.000 65.00322  ? 141 LEU A CA  1 
ATOM   1013 C C   . LEU A 1 146 ? 31.56912 50.06964 27.65950 1.000 69.79478  ? 141 LEU A C   1 
ATOM   1014 O O   . LEU A 1 146 ? 32.11656 49.13750 27.06082 1.000 64.26189  ? 141 LEU A O   1 
ATOM   1015 C CB  . LEU A 1 146 ? 30.13379 49.15367 29.48491 1.000 60.66602  ? 141 LEU A CB  1 
ATOM   1016 C CG  . LEU A 1 146 ? 28.79053 48.73184 30.07504 1.000 55.96909  ? 141 LEU A CG  1 
ATOM   1017 C CD1 . LEU A 1 146 ? 29.02328 47.87147 31.29235 1.000 55.71609  ? 141 LEU A CD1 1 
ATOM   1018 C CD2 . LEU A 1 146 ? 27.95431 49.93906 30.43250 1.000 59.38961  ? 141 LEU A CD2 1 
ATOM   1019 N N   . SER A 1 147 ? 32.17129 51.23418 27.90270 1.000 70.35163  ? 142 SER A N   1 
ATOM   1020 C CA  . SER A 1 147 ? 33.57271 51.43948 27.57411 1.000 71.57586  ? 142 SER A CA  1 
ATOM   1021 C C   . SER A 1 147 ? 34.45811 50.61939 28.51048 1.000 70.72498  ? 142 SER A C   1 
ATOM   1022 O O   . SER A 1 147 ? 33.99617 50.02615 29.48826 1.000 64.52199  ? 142 SER A O   1 
ATOM   1023 C CB  . SER A 1 147 ? 33.93705 52.91658 27.67379 1.000 74.40900  ? 142 SER A CB  1 
ATOM   1024 O OG  . SER A 1 147 ? 33.94600 53.32513 29.02680 1.000 74.93611  ? 142 SER A OG  1 
ATOM   1025 N N   . ALA A 1 148 ? 35.75781 50.59528 28.20507 1.000 71.30657  ? 143 ALA A N   1 
ATOM   1026 C CA  . ALA A 1 148 ? 36.68346 49.82738 29.03283 1.000 73.03511  ? 143 ALA A CA  1 
ATOM   1027 C C   . ALA A 1 148 ? 36.71062 50.35645 30.46155 1.000 75.00904  ? 143 ALA A C   1 
ATOM   1028 O O   . ALA A 1 148 ? 36.70812 49.57526 31.42233 1.000 65.51599  ? 143 ALA A O   1 
ATOM   1029 C CB  . ALA A 1 148 ? 38.08270 49.84736 28.42222 1.000 68.96494  ? 143 ALA A CB  1 
ATOM   1030 N N   . ALA A 1 149 ? 36.71663 51.68441 30.61790 1.000 75.75735  ? 144 ALA A N   1 
ATOM   1031 C CA  . ALA A 1 149 ? 36.68307 52.28158 31.94973 1.000 76.74767  ? 144 ALA A CA  1 
ATOM   1032 C C   . ALA A 1 149 ? 35.37395 51.97432 32.67178 1.000 72.22610  ? 144 ALA A C   1 
ATOM   1033 O O   . ALA A 1 149 ? 35.37959 51.70133 33.87822 1.000 68.73467  ? 144 ALA A O   1 
ATOM   1034 C CB  . ALA A 1 149 ? 36.90316 53.79169 31.85337 1.000 80.77649  ? 144 ALA A CB  1 
ATOM   1035 N N   . GLU A 1 150 ? 34.24084 52.02403 31.95823 1.000 70.94358  ? 145 GLU A N   1 
ATOM   1036 C CA  . GLU A 1 150 ? 32.95746 51.69388 32.58046 1.000 64.33611  ? 145 GLU A CA  1 
ATOM   1037 C C   . GLU A 1 150 ? 32.90570 50.23313 32.99514 1.000 60.26479  ? 145 GLU A C   1 
ATOM   1038 O O   . GLU A 1 150 ? 32.27654 49.88393 34.00306 1.000 54.25193  ? 145 GLU A O   1 
ATOM   1039 C CB  . GLU A 1 150 ? 31.79987 51.98138 31.62829 1.000 69.26889  ? 145 GLU A CB  1 
ATOM   1040 C CG  . GLU A 1 150 ? 31.57154 53.43400 31.27683 1.000 76.93634  ? 145 GLU A CG  1 
ATOM   1041 C CD  . GLU A 1 150 ? 30.54157 53.58245 30.17341 1.000 79.79516  ? 145 GLU A CD  1 
ATOM   1042 O OE1 . GLU A 1 150 ? 30.69120 52.91165 29.12992 1.000 78.07143  ? 145 GLU A OE1 1 
ATOM   1043 O OE2 . GLU A 1 150 ? 29.57265 54.35189 30.35233 1.000 82.89064  ? 145 GLU A OE2 1 
ATOM   1044 N N   . GLN A 1 151 ? 33.52924 49.35763 32.21139 1.000 60.14839  ? 146 GLN A N   1 
ATOM   1045 C CA  . GLN A 1 151 ? 33.53983 47.94782 32.57390 1.000 56.29337  ? 146 GLN A CA  1 
ATOM   1046 C C   . GLN A 1 151 ? 34.36047 47.72262 33.83713 1.000 56.13567  ? 146 GLN A C   1 
ATOM   1047 O O   . GLN A 1 151 ? 33.89463 47.07312 34.77966 1.000 57.24142  ? 146 GLN A O   1 
ATOM   1048 C CB  . GLN A 1 151 ? 34.05718 47.12000 31.39997 1.000 60.88557  ? 146 GLN A CB  1 
ATOM   1049 C CG  . GLN A 1 151 ? 33.10177 47.14819 30.22040 1.000 63.53199  ? 146 GLN A CG  1 
ATOM   1050 C CD  . GLN A 1 151 ? 33.55799 46.29408 29.06306 1.000 61.58918  ? 146 GLN A CD  1 
ATOM   1051 O OE1 . GLN A 1 151 ? 34.13819 45.22737 29.25667 1.000 61.05118  ? 146 GLN A OE1 1 
ATOM   1052 N NE2 . GLN A 1 151 ? 33.28957 46.75549 27.84556 1.000 58.91641  ? 146 GLN A NE2 1 
ATOM   1053 N N   . ARG A 1 152 ? 35.56956 48.29180 33.89587 1.000 57.92577  ? 147 ARG A N   1 
ATOM   1054 C CA  . ARG A 1 152 ? 36.35606 48.21511 35.12495 1.000 61.78267  ? 147 ARG A CA  1 
ATOM   1055 C C   . ARG A 1 152 ? 35.60985 48.85336 36.29051 1.000 62.59051  ? 147 ARG A C   1 
ATOM   1056 O O   . ARG A 1 152 ? 35.61142 48.32434 37.40812 1.000 61.13426  ? 147 ARG A O   1 
ATOM   1057 C CB  . ARG A 1 152 ? 37.71600 48.88878 34.92775 1.000 62.74274  ? 147 ARG A CB  1 
ATOM   1058 N N   . GLN A 1 153 ? 34.96769 49.99427 36.03901 1.000 64.48734  ? 148 GLN A N   1 
ATOM   1059 C CA  . GLN A 1 153 ? 34.16786 50.66852 37.05406 1.000 66.31792  ? 148 GLN A CA  1 
ATOM   1060 C C   . GLN A 1 153 ? 33.05026 49.76550 37.56005 1.000 60.40576  ? 148 GLN A C   1 
ATOM   1061 O O   . GLN A 1 153 ? 32.78360 49.69601 38.76403 1.000 59.41978  ? 148 GLN A O   1 
ATOM   1062 C CB  . GLN A 1 153 ? 33.60415 51.95172 36.45165 1.000 73.44919  ? 148 GLN A CB  1 
ATOM   1063 C CG  . GLN A 1 153 ? 33.04931 52.96897 37.40489 1.000 79.22802  ? 148 GLN A CG  1 
ATOM   1064 C CD  . GLN A 1 153 ? 32.75794 54.27029 36.68161 1.000 89.06564  ? 148 GLN A CD  1 
ATOM   1065 O OE1 . GLN A 1 153 ? 33.45547 54.63012 35.72579 1.000 91.50529  ? 148 GLN A OE1 1 
ATOM   1066 N NE2 . GLN A 1 153 ? 31.71693 54.97419 37.11481 1.000 89.14108  ? 148 GLN A NE2 1 
ATOM   1067 N N   . LEU A 1 154 ? 32.38275 49.06316 36.64575 1.000 57.92687  ? 149 LEU A N   1 
ATOM   1068 C CA  . LEU A 1 154 ? 31.30817 48.16587 37.04427 1.000 51.50786  ? 149 LEU A CA  1 
ATOM   1069 C C   . LEU A 1 154 ? 31.85148 46.95567 37.79625 1.000 51.60597  ? 149 LEU A C   1 
ATOM   1070 O O   . LEU A 1 154 ? 31.23323 46.49541 38.76426 1.000 53.68030  ? 149 LEU A O   1 
ATOM   1071 C CB  . LEU A 1 154 ? 30.50849 47.74117 35.81285 1.000 50.93543  ? 149 LEU A CB  1 
ATOM   1072 C CG  . LEU A 1 154 ? 29.41014 46.70721 36.04081 1.000 44.66976  ? 149 LEU A CG  1 
ATOM   1073 C CD1 . LEU A 1 154 ? 28.46126 47.17282 37.13425 1.000 48.18522  ? 149 LEU A CD1 1 
ATOM   1074 C CD2 . LEU A 1 154 ? 28.66548 46.47033 34.74215 1.000 46.83416  ? 149 LEU A CD2 1 
ATOM   1075 N N   . ALA A 1 155 ? 33.01620 46.44015 37.38013 1.000 52.29554  ? 150 ALA A N   1 
ATOM   1076 C CA  . ALA A 1 155 ? 33.62439 45.31718 38.08852 1.000 51.84725  ? 150 ALA A CA  1 
ATOM   1077 C C   . ALA A 1 155 ? 34.00982 45.70470 39.51443 1.000 55.02749  ? 150 ALA A C   1 
ATOM   1078 O O   . ALA A 1 155 ? 33.86949 44.89840 40.44256 1.000 54.44320  ? 150 ALA A O   1 
ATOM   1079 C CB  . ALA A 1 155 ? 34.84407 44.80531 37.32427 1.000 49.63952  ? 150 ALA A CB  1 
ATOM   1080 N N   . LYS A 1 156 ? 34.48711 46.93744 39.71028 1.000 54.35544  ? 151 LYS A N   1 
ATOM   1081 C CA  . LYS A 1 156 ? 34.87960 47.37153 41.04808 1.000 57.49839  ? 151 LYS A CA  1 
ATOM   1082 C C   . LYS A 1 156 ? 33.67084 47.51006 41.97001 1.000 55.37642  ? 151 LYS A C   1 
ATOM   1083 O O   . LYS A 1 156 ? 33.70161 47.05321 43.11859 1.000 57.88593  ? 151 LYS A O   1 
ATOM   1084 C CB  . LYS A 1 156 ? 35.65557 48.68670 40.97711 1.000 58.00221  ? 151 LYS A CB  1 
ATOM   1085 C CG  . LYS A 1 156 ? 37.17215 48.52874 41.07028 1.000 65.32720  ? 151 LYS A CG  1 
ATOM   1086 N N   . LEU A 1 157 ? 32.59998 48.14996 41.49573 1.000 53.72998  ? 152 LEU A N   1 
ATOM   1087 C CA  . LEU A 1 157 ? 31.40983 48.28574 42.33441 1.000 54.29403  ? 152 LEU A CA  1 
ATOM   1088 C C   . LEU A 1 157 ? 30.80784 46.92413 42.66302 1.000 52.82406  ? 152 LEU A C   1 
ATOM   1089 O O   . LEU A 1 157 ? 30.35613 46.68905 43.79157 1.000 50.30024  ? 152 LEU A O   1 
ATOM   1090 C CB  . LEU A 1 157 ? 30.37724 49.17960 41.64587 1.000 51.02101  ? 152 LEU A CB  1 
ATOM   1091 C CG  . LEU A 1 157 ? 30.79278 50.64043 41.46505 1.000 57.58233  ? 152 LEU A CG  1 
ATOM   1092 C CD1 . LEU A 1 157 ? 29.94945 51.30209 40.39637 1.000 60.28325  ? 152 LEU A CD1 1 
ATOM   1093 C CD2 . LEU A 1 157 ? 30.67678 51.40186 42.78045 1.000 57.83119  ? 152 LEU A CD2 1 
ATOM   1094 N N   . LEU A 1 158 ? 30.79150 46.00822 41.69105 1.000 50.08246  ? 153 LEU A N   1 
ATOM   1095 C CA  . LEU A 1 158 ? 30.24535 44.68468 41.96610 1.000 47.70730  ? 153 LEU A CA  1 
ATOM   1096 C C   . LEU A 1 158 ? 31.10764 43.93576 42.97621 1.000 44.68163  ? 153 LEU A C   1 
ATOM   1097 O O   . LEU A 1 158 ? 30.57945 43.21094 43.83010 1.000 47.87799  ? 153 LEU A O   1 
ATOM   1098 C CB  . LEU A 1 158 ? 30.09471 43.88956 40.66669 1.000 42.93040  ? 153 LEU A CB  1 
ATOM   1099 C CG  . LEU A 1 158 ? 28.94410 44.33101 39.75515 1.000 45.74512  ? 153 LEU A CG  1 
ATOM   1100 C CD1 . LEU A 1 158 ? 29.03724 43.61618 38.42148 1.000 46.57837  ? 153 LEU A CD1 1 
ATOM   1101 C CD2 . LEU A 1 158 ? 27.57985 44.09608 40.39392 1.000 49.79359  ? 153 LEU A CD2 1 
ATOM   1102 N N   . ASP A 1 159 ? 32.43221 44.11758 42.91964 1.000 43.06403  ? 154 ASP A N   1 
ATOM   1103 C CA  . ASP A 1 159 ? 33.29284 43.46894 43.90542 1.000 49.22580  ? 154 ASP A CA  1 
ATOM   1104 C C   . ASP A 1 159 ? 33.02391 44.01180 45.30506 1.000 54.42783  ? 154 ASP A C   1 
ATOM   1105 O O   . ASP A 1 159 ? 32.98465 43.24791 46.27596 1.000 55.60098  ? 154 ASP A O   1 
ATOM   1106 C CB  . ASP A 1 159 ? 34.76508 43.64001 43.53019 1.000 55.60739  ? 154 ASP A CB  1 
ATOM   1107 C CG  . ASP A 1 159 ? 35.71362 43.05631 44.58034 1.000 62.55551  ? 154 ASP A CG  1 
ATOM   1108 O OD1 . ASP A 1 159 ? 35.46113 41.93345 45.07261 1.000 63.69463  ? 154 ASP A OD1 1 
ATOM   1109 O OD2 . ASP A 1 159 ? 36.72476 43.71487 44.90339 1.000 70.07111  ? 154 ASP A OD2 1 
ATOM   1110 N N   . LYS A 1 160 ? 32.81299 45.32513 45.42663 1.000 52.26930  ? 155 LYS A N   1 
ATOM   1111 C CA  . LYS A 1 160 ? 32.53232 45.90162 46.74042 1.000 56.63711  ? 155 LYS A CA  1 
ATOM   1112 C C   . LYS A 1 160 ? 31.20100 45.39704 47.28971 1.000 53.58338  ? 155 LYS A C   1 
ATOM   1113 O O   . LYS A 1 160 ? 31.10410 45.04959 48.47504 1.000 52.53860  ? 155 LYS A O   1 
ATOM   1114 C CB  . LYS A 1 160 ? 32.54838 47.42891 46.65479 1.000 57.49644  ? 155 LYS A CB  1 
ATOM   1115 C CG  . LYS A 1 160 ? 32.75807 48.13656 47.98210 1.000 64.53118  ? 155 LYS A CG  1 
ATOM   1116 C CD  . LYS A 1 160 ? 33.08706 49.61855 47.76696 1.000 63.66186  ? 155 LYS A CD  1 
ATOM   1117 C CE  . LYS A 1 160 ? 33.61933 50.26007 49.03429 1.000 63.91949  ? 155 LYS A CE  1 
ATOM   1118 N N   . LEU A 1 161 ? 30.17309 45.33778 46.43756 1.000 47.70420  ? 156 LEU A N   1 
ATOM   1119 C CA  . LEU A 1 161 ? 28.87461 44.79799 46.83871 1.000 45.56788  ? 156 LEU A CA  1 
ATOM   1120 C C   . LEU A 1 161 ? 28.99532 43.34807 47.30061 1.000 48.51790  ? 156 LEU A C   1 
ATOM   1121 O O   . LEU A 1 161 ? 28.42754 42.96007 48.33229 1.000 45.16507  ? 156 LEU A O   1 
ATOM   1122 C CB  . LEU A 1 161 ? 27.88571 44.90827 45.67413 1.000 46.36981  ? 156 LEU A CB  1 
ATOM   1123 C CG  . LEU A 1 161 ? 26.42338 44.53230 45.93089 1.000 47.56637  ? 156 LEU A CG  1 
ATOM   1124 C CD1 . LEU A 1 161 ? 25.81431 45.44976 46.97305 1.000 48.59489  ? 156 LEU A CD1 1 
ATOM   1125 C CD2 . LEU A 1 161 ? 25.62072 44.58159 44.63253 1.000 47.72283  ? 156 LEU A CD2 1 
ATOM   1126 N N   . LEU A 1 162 ? 29.71888 42.52654 46.53485 1.000 46.55022  ? 157 LEU A N   1 
ATOM   1127 C CA  . LEU A 1 162 ? 29.88969 41.12027 46.89028 1.000 49.32899  ? 157 LEU A CA  1 
ATOM   1128 C C   . LEU A 1 162 ? 30.59274 40.96530 48.23419 1.000 56.14260  ? 157 LEU A C   1 
ATOM   1129 O O   . LEU A 1 162 ? 30.16774 40.16775 49.07905 1.000 57.29145  ? 157 LEU A O   1 
ATOM   1130 C CB  . LEU A 1 162 ? 30.67403 40.39406 45.79630 1.000 52.09258  ? 157 LEU A CB  1 
ATOM   1131 C CG  . LEU A 1 162 ? 29.83235 39.68160 44.74651 1.000 56.31538  ? 157 LEU A CG  1 
ATOM   1132 C CD1 . LEU A 1 162 ? 30.69340 39.25562 43.55703 1.000 57.24574  ? 157 LEU A CD1 1 
ATOM   1133 C CD2 . LEU A 1 162 ? 29.12950 38.48392 45.38493 1.000 50.41753  ? 157 LEU A CD2 1 
ATOM   1134 N N   . GLN A 1 163 ? 31.68650 41.70615 48.43975 1.000 59.15196  ? 158 GLN A N   1 
ATOM   1135 C CA  . GLN A 1 163 ? 32.40460 41.62783 49.70954 1.000 63.01740  ? 158 GLN A CA  1 
ATOM   1136 C C   . GLN A 1 163 ? 31.52781 42.08533 50.86330 1.000 66.65808  ? 158 GLN A C   1 
ATOM   1137 O O   . GLN A 1 163 ? 31.60796 41.53784 51.96731 1.000 70.69200  ? 158 GLN A O   1 
ATOM   1138 C CB  . GLN A 1 163 ? 33.68443 42.45731 49.64666 1.000 69.09770  ? 158 GLN A CB  1 
ATOM   1139 C CG  . GLN A 1 163 ? 34.67353 41.94977 48.62099 1.000 76.55288  ? 158 GLN A CG  1 
ATOM   1140 C CD  . GLN A 1 163 ? 34.80044 40.43677 48.63853 1.000 82.72338  ? 158 GLN A CD  1 
ATOM   1141 O OE1 . GLN A 1 163 ? 35.00368 39.83052 49.69363 1.000 88.34174  ? 158 GLN A OE1 1 
ATOM   1142 N NE2 . GLN A 1 163 ? 34.66831 39.81585 47.46559 1.000 79.09799  ? 158 GLN A NE2 1 
ATOM   1143 N N   . GLY A 1 164 ? 30.67527 43.08278 50.62359 1.000 66.06741  ? 159 GLY A N   1 
ATOM   1144 C CA  . GLY A 1 164 ? 29.71689 43.53881 51.61856 1.000 62.02909  ? 159 GLY A CA  1 
ATOM   1145 C C   . GLY A 1 164 ? 28.71881 42.48509 52.05465 1.000 61.39614  ? 159 GLY A C   1 
ATOM   1146 O O   . GLY A 1 164 ? 27.96072 42.73203 52.99869 1.000 64.63341  ? 159 GLY A O   1 
ATOM   1147 N N   . GLN A 1 165 ? 28.70169 41.32747 51.40281 1.000 62.60981  ? 160 GLN A N   1 
ATOM   1148 C CA  . GLN A 1 165 ? 27.83679 40.22410 51.80027 1.000 63.62802  ? 160 GLN A CA  1 
ATOM   1149 C C   . GLN A 1 165 ? 28.63808 39.20370 52.60233 1.000 68.23061  ? 160 GLN A C   1 
ATOM   1150 O O   . GLN A 1 165 ? 28.14997 38.65882 53.59010 1.000 72.09355  ? 160 GLN A O   1 
ATOM   1151 C CB  . GLN A 1 165 ? 27.20129 39.54506 50.57924 1.000 61.23199  ? 160 GLN A CB  1 
ATOM   1152 C CG  . GLN A 1 165 ? 26.71194 40.49608 49.48329 1.000 52.54022  ? 160 GLN A CG  1 
ATOM   1153 C CD  . GLN A 1 165 ? 25.58660 41.41617 49.92724 1.000 46.99355  ? 160 GLN A CD  1 
ATOM   1154 O OE1 . GLN A 1 165 ? 24.57897 40.96702 50.46765 1.000 47.34050  ? 160 GLN A OE1 1 
ATOM   1155 N NE2 . GLN A 1 165 ? 25.74887 42.71423 49.68079 1.000 44.61171  ? 160 GLN A NE2 1 
HETATM 1156 N N9  . XAN B 2 .   ? 31.38778 29.51853 34.43918 1.000 53.64912  ? 201 XAN A N9  1 
HETATM 1157 C C4  . XAN B 2 .   ? 32.57341 30.07826 34.03408 1.000 53.38749  ? 201 XAN A C4  1 
HETATM 1158 N N3  . XAN B 2 .   ? 33.87415 29.72016 34.20137 1.000 51.67103  ? 201 XAN A N3  1 
HETATM 1159 C C2  . XAN B 2 .   ? 34.88119 30.48448 33.66849 1.000 53.06716  ? 201 XAN A C2  1 
HETATM 1160 O O2  . XAN B 2 .   ? 36.04608 30.15648 33.82927 1.000 46.05462  ? 201 XAN A O2  1 
HETATM 1161 N N1  . XAN B 2 .   ? 34.54092 31.61797 32.96190 1.000 54.79599  ? 201 XAN A N1  1 
HETATM 1162 C C6  . XAN B 2 .   ? 33.22932 32.06093 32.74461 1.000 52.84201  ? 201 XAN A C6  1 
HETATM 1163 O O6  . XAN B 2 .   ? 33.03350 33.09856 32.10078 1.000 43.17006  ? 201 XAN A O6  1 
HETATM 1164 C C5  . XAN B 2 .   ? 32.23141 31.22719 33.32137 1.000 53.01398  ? 201 XAN A C5  1 
HETATM 1165 N N7  . XAN B 2 .   ? 30.84468 31.35068 33.30567 1.000 60.17712  ? 201 XAN A N7  1 
HETATM 1166 C C8  . XAN B 2 .   ? 30.40518 30.31115 33.97833 1.000 52.61939  ? 201 XAN A C8  1 
HETATM 1167 O O   . HOH C 3 .   ? 29.33015 32.59646 32.19674 1.000 42.27132  ? 301 HOH A O   1 
HETATM 1168 O O   . HOH C 3 .   ? 18.14040 30.67040 27.19821 1.000 45.01933  ? 302 HOH A O   1 
HETATM 1169 O O   . HOH C 3 .   ? 18.56903 37.51973 38.35717 1.000 43.21094  ? 303 HOH A O   1 
HETATM 1170 O O   . HOH C 3 .   ? 24.26783 31.79545 32.21971 1.000 43.27169  ? 304 HOH A O   1 
HETATM 1171 O O   . HOH C 3 .   ? 32.312   35.332   33.491   1.000 36.40736  ? 305 HOH A O   1 
HETATM 1172 O O   . HOH C 3 .   ? 32.02791 35.29276 40.15939 1.000 40.90047  ? 306 HOH A O   1 
HETATM 1173 O O   . HOH C 3 .   ? 28.45133 32.63216 26.29193 1.000 38.18843  ? 307 HOH A O   1 
HETATM 1174 O O   . HOH C 3 .   ? 22.67185 26.47643 27.89553 1.000 39.89832  ? 308 HOH A O   1 
HETATM 1175 O O   . HOH C 3 .   ? 14.10441 39.37655 44.15891 1.000 44.55208  ? 309 HOH A O   1 
HETATM 1176 O O   . HOH C 3 .   ? 40.13184 25.55701 38.50394 1.000 42.20978  ? 310 HOH A O   1 
HETATM 1177 O O   . HOH C 3 .   ? 0.585    48.590   36.617   1.000 47.20412  ? 311 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   ? 1.27049 0.62861 1.09549 0.13127  0.21639  0.13696  1   MET A N   
2    C CA  . MET A 6   ? 1.21310 0.59783 1.07004 0.10041  0.18076  0.10612  1   MET A CA  
3    C C   . MET A 6   ? 1.09233 0.55427 0.95604 0.08596  0.15147  0.10769  1   MET A C   
4    O O   . MET A 6   ? 1.15677 0.67739 0.98087 0.12288  0.14170  0.12493  1   MET A O   
5    C CB  . MET A 6   ? 1.26633 0.63512 1.07953 0.14178  0.17277  0.09714  1   MET A CB  
6    C CG  . MET A 6   ? 1.38340 0.70364 1.22428 0.12011  0.17720  0.06654  1   MET A CG  
7    S SD  . MET A 6   ? 1.39582 0.73663 1.20239 0.15021  0.14944  0.04111  1   MET A SD  
8    C CE  . MET A 6   ? 1.44105 0.70424 1.28148 0.12357  0.16227  0.00766  1   MET A CE  
9    N N   . ASP A 7   ? 0.94291 0.43489 0.86285 0.03046  0.12988  0.08072  2   ASP A N   
10   C CA  . ASP A 7   ? 0.85988 0.44353 0.79244 0.00870  0.09998  0.07580  2   ASP A CA  
11   C C   . ASP A 7   ? 0.78312 0.43689 0.70664 0.01233  0.06697  0.04935  2   ASP A C   
12   O O   . ASP A 7   ? 0.81163 0.44738 0.71752 0.03394  0.06435  0.03627  2   ASP A O   
13   C CB  . ASP A 7   ? 0.82319 0.40153 0.81233 -0.04416 0.09800  0.06405  2   ASP A CB  
14   C CG  . ASP A 7   ? 0.79935 0.36950 0.82873 -0.07226 0.07925  0.02250  2   ASP A CG  
15   O OD1 . ASP A 7   ? 0.85150 0.37519 0.87121 -0.05710 0.08512  0.00789  2   ASP A OD1 
16   O OD2 . ASP A 7   ? 0.79409 0.41179 0.85565 -0.10216 0.05469  0.00414  2   ASP A OD2 
17   N N   . ARG A 8   ? 0.64890 0.37736 0.58318 -0.00829 0.04732  0.04242  3   ARG A N   
18   C CA  . ARG A 8   ? 0.64436 0.43418 0.57261 -0.00791 0.02676  0.01922  3   ARG A CA  
19   C C   . ARG A 8   ? 0.60589 0.36132 0.53950 -0.01513 0.01697  -0.00787 3   ARG A C   
20   O O   . ARG A 8   ? 0.63228 0.40195 0.54492 0.00707  0.01105  -0.02088 3   ARG A O   
21   C CB  . ARG A 8   ? 0.60360 0.45258 0.54761 -0.03816 0.01780  0.01464  3   ARG A CB  
22   C CG  . ARG A 8   ? 0.58117 0.48415 0.51936 -0.03027 0.02232  0.03016  3   ARG A CG  
23   C CD  . ARG A 8   ? 0.58473 0.52795 0.53981 -0.06516 0.01996  0.02581  3   ARG A CD  
24   N NE  . ARG A 8   ? 0.59057 0.58841 0.54268 -0.05766 0.02310  0.03313  3   ARG A NE  
25   C CZ  . ARG A 8   ? 0.59937 0.66702 0.55405 -0.04696 0.02069  0.01461  3   ARG A CZ  
26   N NH1 . ARG A 8   ? 0.61195 0.69649 0.56970 -0.04305 0.02005  -0.00617 3   ARG A NH1 
27   N NH2 . ARG A 8   ? 0.64993 0.77297 0.60755 -0.03953 0.01997  0.01305  3   ARG A NH2 
28   N N   . ALA A 9   ? 0.62713 0.34317 0.59123 -0.04460 0.01400  -0.02064 4   ALA A N   
29   C CA  . ALA A 9   ? 0.70278 0.39889 0.67297 -0.05035 -0.00251 -0.05546 4   ALA A CA  
30   C C   . ALA A 9   ? 0.75479 0.39086 0.71292 -0.02716 0.00681  -0.06369 4   ALA A C   
31   O O   . ALA A 9   ? 0.72023 0.35915 0.65339 -0.00782 -0.00451 -0.08265 4   ALA A O   
32   C CB  . ALA A 9   ? 0.71130 0.39550 0.72565 -0.08498 -0.01197 -0.07521 4   ALA A CB  
33   N N   . ALA A 10  ? 0.72564 0.29926 0.69696 -0.02627 0.03300  -0.04806 5   ALA A N   
34   C CA  . ALA A 10  ? 0.84620 0.34941 0.80162 -0.00260 0.05045  -0.05333 5   ALA A CA  
35   C C   . ALA A 10  ? 0.83409 0.36178 0.73436 0.04479  0.05017  -0.03808 5   ALA A C   
36   O O   . ALA A 10  ? 0.86456 0.36526 0.74388 0.06534  0.04763  -0.05519 5   ALA A O   
37   C CB  . ALA A 10  ? 0.99593 0.41925 0.96757 -0.00548 0.09152  -0.03143 5   ALA A CB  
38   N N   . HIS A 11  ? 0.82415 0.40737 0.70364 0.06408  0.05212  -0.00998 6   HIS A N   
39   C CA  . HIS A 11  ? 0.84170 0.46950 0.68159 0.10885  0.04851  -0.00326 6   HIS A CA  
40   C C   . HIS A 11  ? 0.76099 0.43770 0.60044 0.10414  0.02629  -0.03155 6   HIS A C   
41   O O   . HIS A 11  ? 0.77530 0.44904 0.58832 0.13648  0.02664  -0.03895 6   HIS A O   
42   C CB  . HIS A 11  ? 0.85310 0.54931 0.68426 0.12501  0.04869  0.01951  6   HIS A CB  
43   C CG  . HIS A 11  ? 0.90582 0.67453 0.71370 0.16681  0.04023  0.01580  6   HIS A CG  
44   N ND1 . HIS A 11  ? 1.01747 0.76152 0.78581 0.22109  0.05084  0.02466  6   HIS A ND1 
45   C CD2 . HIS A 11  ? 0.88124 0.74886 0.70554 0.16229  0.02539  0.00082  6   HIS A CD2 
46   C CE1 . HIS A 11  ? 1.00076 0.83553 0.76593 0.24940  0.03809  0.01327  6   HIS A CE1 
47   N NE2 . HIS A 11  ? 0.91346 0.82405 0.71715 0.21137  0.02435  -0.00318 6   HIS A NE2 
48   N N   . ALA A 12  ? 0.66725 0.38408 0.53001 0.06867  0.01112  -0.04547 7   ALA A N   
49   C CA  . ALA A 12  ? 0.66596 0.41829 0.51832 0.06981  -0.00131 -0.06817 7   ALA A CA  
50   C C   . ALA A 12  ? 0.76436 0.45700 0.60240 0.07832  -0.00868 -0.09303 7   ALA A C   
51   O O   . ALA A 12  ? 0.76342 0.46481 0.57439 0.10384  -0.01009 -0.10417 7   ALA A O   
52   C CB  . ALA A 12  ? 0.62756 0.41944 0.49646 0.03670  -0.00930 -0.07441 7   ALA A CB  
53   N N   . VAL A 13  ? 0.76404 0.39765 0.62416 0.05718  -0.01197 -0.10586 8   VAL A N   
54   C CA  . VAL A 13  ? 0.82067 0.39893 0.67387 0.06373  -0.02070 -0.13857 8   VAL A CA  
55   C C   . VAL A 13  ? 0.89393 0.42960 0.71600 0.10091  -0.00369 -0.13008 8   VAL A C   
56   O O   . VAL A 13  ? 0.95018 0.46732 0.74465 0.12266  -0.01084 -0.15137 8   VAL A O   
57   C CB  . VAL A 13  ? 0.86883 0.39975 0.76955 0.02923  -0.02396 -0.16150 8   VAL A CB  
58   C CG1 . VAL A 13  ? 0.99448 0.45915 0.89652 0.03617  -0.02630 -0.19886 8   VAL A CG1 
59   C CG2 . VAL A 13  ? 0.83092 0.40925 0.75278 0.00368  -0.04881 -0.18074 8   VAL A CG2 
60   N N   . GLU A 14  ? 0.90242 0.42057 0.72056 0.11535  0.02012  -0.09770 9   GLU A N   
61   C CA  . GLU A 14  ? 1.00481 0.48219 0.78428 0.16013  0.03916  -0.08530 9   GLU A CA  
62   C C   . GLU A 14  ? 0.97818 0.52044 0.72612 0.19412  0.02898  -0.08633 9   GLU A C   
63   O O   . GLU A 14  ? 1.01453 0.52574 0.73233 0.22343  0.03160  -0.09769 9   GLU A O   
64   C CB  . GLU A 14  ? 1.02403 0.47866 0.79283 0.18058  0.06706  -0.04670 9   GLU A CB  
65   C CG  . GLU A 14  ? 1.17552 0.58200 0.89431 0.23670  0.09068  -0.02961 9   GLU A CG  
66   C CD  . GLU A 14  ? 1.34567 0.63153 1.06144 0.23341  0.11703  -0.04165 9   GLU A CD  
67   O OE1 . GLU A 14  ? 1.36450 0.60514 1.12649 0.18835  0.12703  -0.05244 9   GLU A OE1 
68   O OE2 . GLU A 14  ? 1.42337 0.67506 1.10161 0.27043  0.12734  -0.04271 9   GLU A OE2 
69   N N   . GLN A 15  ? 0.87225 0.50430 0.63118 0.18912  0.02094  -0.07707 10  GLN A N   
70   C CA  . GLN A 15  ? 0.80358 0.50346 0.54808 0.21487  0.01800  -0.08289 10  GLN A CA  
71   C C   . GLN A 15  ? 0.80874 0.49326 0.53921 0.21051  0.00849  -0.11021 10  GLN A C   
72   O O   . GLN A 15  ? 0.89794 0.59106 0.60313 0.24295  0.01324  -0.11697 10  GLN A O   
73   C CB  . GLN A 15  ? 0.76609 0.56143 0.53820 0.20030  0.01624  -0.07594 10  GLN A CB  
74   C CG  . GLN A 15  ? 0.75624 0.58202 0.53189 0.21998  0.02212  -0.05328 10  GLN A CG  
75   C CD  . GLN A 15  ? 0.77309 0.70292 0.58045 0.20831  0.01865  -0.05670 10  GLN A CD  
76   O OE1 . GLN A 15  ? 0.74382 0.69619 0.57611 0.16693  0.01618  -0.06428 10  GLN A OE1 
77   N NE2 . GLN A 15  ? 0.73878 0.73431 0.54553 0.24754  0.01914  -0.05473 10  GLN A NE2 
78   N N   . TRP A 16  ? 0.82163 0.48545 0.56422 0.17655  -0.00499 -0.12691 11  TRP A N   
79   C CA  . TRP A 16  ? 0.87168 0.52108 0.58893 0.18238  -0.01614 -0.15421 11  TRP A CA  
80   C C   . TRP A 16  ? 0.96653 0.54408 0.65664 0.20677  -0.01922 -0.17340 11  TRP A C   
81   O O   . TRP A 16  ? 1.07439 0.64879 0.72787 0.23683  -0.01822 -0.18487 11  TRP A O   
82   C CB  . TRP A 16  ? 0.87173 0.52012 0.60337 0.14988  -0.03353 -0.17058 11  TRP A CB  
83   C CG  . TRP A 16  ? 0.76672 0.47787 0.50130 0.13723  -0.02680 -0.15954 11  TRP A CG  
84   C CD1 . TRP A 16  ? 0.75264 0.49170 0.51679 0.10487  -0.02799 -0.14838 11  TRP A CD1 
85   C CD2 . TRP A 16  ? 0.79186 0.53803 0.49915 0.15641  -0.01057 -0.15890 11  TRP A CD2 
86   N NE1 . TRP A 16  ? 0.75130 0.53738 0.50635 0.10217  -0.01335 -0.14174 11  TRP A NE1 
87   C CE2 . TRP A 16  ? 0.72415 0.51369 0.44665 0.13240  0.00032  -0.14833 11  TRP A CE2 
88   C CE3 . TRP A 16  ? 0.93451 0.67436 0.60607 0.19188  0.00086  -0.16641 11  TRP A CE3 
89   C CZ2 . TRP A 16  ? 0.73815 0.55995 0.44463 0.14023  0.02763  -0.14578 11  TRP A CZ2 
90   C CZ3 . TRP A 16  ? 0.95310 0.72934 0.61040 0.20052  0.02691  -0.16277 11  TRP A CZ3 
91   C CH2 . TRP A 16  ? 0.81099 0.62520 0.48720 0.17363  0.04251  -0.15304 11  TRP A CH2 
92   N N   . ARG A 17  ? 1.01945 0.53357 0.72778 0.19394  -0.01801 -0.17819 12  ARG A N   
93   C CA  . ARG A 17  ? 1.17965 0.61673 0.86614 0.21429  -0.01460 -0.19884 12  ARG A CA  
94   C C   . ARG A 17  ? 1.24049 0.67937 0.88560 0.26216  0.00267  -0.18031 12  ARG A C   
95   O O   . ARG A 17  ? 1.28182 0.69616 0.90055 0.28259  0.00112  -0.19567 12  ARG A O   
96   C CB  . ARG A 17  ? 1.25674 0.62134 0.97605 0.19203  0.00003  -0.20035 12  ARG A CB  
97   C CG  . ARG A 17  ? 1.27020 0.63676 1.04401 0.14328  -0.01523 -0.22484 12  ARG A CG  
98   C CD  . ARG A 17  ? 1.35825 0.66321 1.18151 0.11759  0.01206  -0.22432 12  ARG A CD  
99   N NE  . ARG A 17  ? 1.36759 0.69060 1.25597 0.06852  0.00588  -0.24315 12  ARG A NE  
100  C CZ  . ARG A 17  ? 1.39899 0.73340 1.30408 0.04049  -0.00790 -0.28069 12  ARG A CZ  
101  N NH1 . ARG A 17  ? 1.43235 0.76456 1.31667 0.05614  -0.01918 -0.30965 12  ARG A NH1 
102  N NH2 . ARG A 17  ? 1.36614 0.72430 1.30688 0.00329  -0.01918 -0.28634 12  ARG A NH2 
103  N N   . SER A 18  ? 1.18664 0.67363 0.83502 0.27728  0.01762  -0.14588 13  SER A N   
104  C CA  . SER A 18  ? 1.18163 0.68573 0.79658 0.32753  0.03172  -0.13144 13  SER A CA  
105  C C   . SER A 18  ? 1.14579 0.71921 0.75049 0.34228  0.02705  -0.14096 13  SER A C   
106  O O   . SER A 18  ? 1.22599 0.79459 0.79923 0.38274  0.03580  -0.14301 13  SER A O   
107  C CB  . SER A 18  ? 1.21267 0.75699 0.83484 0.34643  0.04520  -0.09844 13  SER A CB  
108  O OG  . SER A 18  ? 1.21718 0.83256 0.82559 0.38917  0.04947  -0.09215 13  SER A OG  
109  N N   . GLU A 19  ? 1.10778 0.74005 0.73694 0.31209  0.01942  -0.14560 14  GLU A N   
110  C CA  . GLU A 19  ? 1.00328 0.69791 0.62771 0.32348  0.02801  -0.15117 14  GLU A CA  
111  C C   . GLU A 19  ? 1.08639 0.74023 0.67387 0.32727  0.02182  -0.17439 14  GLU A C   
112  O O   . GLU A 19  ? 1.10895 0.78630 0.68256 0.34578  0.03386  -0.17229 14  GLU A O   
113  C CB  . GLU A 19  ? 0.92821 0.70481 0.59568 0.29286  0.03367  -0.14241 14  GLU A CB  
114  C CG  . GLU A 19  ? 0.87229 0.72057 0.57267 0.30421  0.04107  -0.12713 14  GLU A CG  
115  C CD  . GLU A 19  ? 0.97338 0.87632 0.67357 0.34433  0.05636  -0.13239 14  GLU A CD  
116  O OE1 . GLU A 19  ? 0.95346 0.86711 0.64676 0.34759  0.07088  -0.14504 14  GLU A OE1 
117  O OE2 . GLU A 19  ? 0.98264 0.91741 0.68684 0.37729  0.05606  -0.12397 14  GLU A OE2 
118  N N   . ARG A 20  ? 0.89300 0.83641 0.76848 0.18544  0.23332  -0.15190 15  ARG A N   
119  C CA  . ARG A 20  ? 0.94710 0.87269 0.78088 0.17155  0.24131  -0.16659 15  ARG A CA  
120  C C   . ARG A 20  ? 0.96739 0.82821 0.76502 0.16796  0.24003  -0.19068 15  ARG A C   
121  O O   . ARG A 20  ? 0.94700 0.79138 0.72615 0.14333  0.22313  -0.19977 15  ARG A O   
122  C CB  . ARG A 20  ? 0.93595 0.88726 0.76710 0.14419  0.23001  -0.15489 15  ARG A CB  
123  C CG  . ARG A 20  ? 0.83643 0.84484 0.71362 0.14171  0.24230  -0.13748 15  ARG A CG  
124  C CD  . ARG A 20  ? 0.90420 0.93340 0.77604 0.15895  0.27352  -0.13947 15  ARG A CD  
125  N NE  . ARG A 20  ? 0.95461 0.96189 0.76274 0.16172  0.28152  -0.14570 15  ARG A NE  
126  C CZ  . ARG A 20  ? 0.91239 0.93475 0.70137 0.15510  0.29253  -0.12904 15  ARG A CZ  
127  N NH1 . ARG A 20  ? 0.86555 0.91251 0.70105 0.13903  0.30180  -0.10541 15  ARG A NH1 
128  N NH2 . ARG A 20  ? 0.89872 0.91404 0.62225 0.16812  0.29692  -0.13770 15  ARG A NH2 
129  N N   . PRO A 21  ? 1.03246 0.85690 0.82501 0.19201  0.26090  -0.20476 16  PRO A N   
130  C CA  . PRO A 21  ? 1.08974 0.84650 0.86265 0.18436  0.26762  -0.23559 16  PRO A CA  
131  C C   . PRO A 21  ? 1.12156 0.88270 0.85608 0.16438  0.26035  -0.27222 16  PRO A C   
132  O O   . PRO A 21  ? 1.22364 0.94506 0.95227 0.14638  0.25762  -0.30682 16  PRO A O   
133  C CB  . PRO A 21  ? 1.13173 0.85309 0.90851 0.21978  0.30037  -0.24110 16  PRO A CB  
134  C CG  . PRO A 21  ? 1.12036 0.90349 0.90090 0.24177  0.30742  -0.22579 16  PRO A CG  
135  C CD  . PRO A 21  ? 1.03254 0.87789 0.83938 0.22681  0.28387  -0.19782 16  PRO A CD  
136  N N   . ASP A 22  ? 1.05347 0.86719 0.76449 0.16977  0.25973  -0.26701 17  ASP A N   
137  C CA  . ASP A 22  ? 1.14391 0.97974 0.80897 0.16214  0.25128  -0.29595 17  ASP A CA  
138  C C   . ASP A 22  ? 1.16970 1.02273 0.82920 0.13539  0.22263  -0.29220 17  ASP A C   
139  O O   . ASP A 22  ? 1.20045 1.07943 0.82086 0.13244  0.21128  -0.32061 17  ASP A O   
140  C CB  . ASP A 22  ? 1.14115 1.02771 0.78154 0.18435  0.26706  -0.27822 17  ASP A CB  
141  C CG  . ASP A 22  ? 1.09630 1.01764 0.77300 0.18112  0.26966  -0.22874 17  ASP A CG  
142  O OD1 . ASP A 22  ? 1.05032 0.96257 0.77447 0.17830  0.26762  -0.21208 17  ASP A OD1 
143  O OD2 . ASP A 22  ? 1.10855 1.06834 0.76839 0.18379  0.27657  -0.20824 17  ASP A OD2 
144  N N   . LEU A 23  ? 1.07132 0.91776 0.76663 0.12055  0.21030  -0.25998 18  LEU A N   
145  C CA  . LEU A 23  ? 1.05380 0.91861 0.74690 0.09815  0.18560  -0.24792 18  LEU A CA  
146  C C   . LEU A 23  ? 1.02716 0.84971 0.74208 0.07626  0.17227  -0.26593 18  LEU A C   
147  O O   . LEU A 23  ? 1.05852 0.83476 0.80358 0.08036  0.18478  -0.26375 18  LEU A O   
148  C CB  . LEU A 23  ? 1.06660 0.95711 0.78813 0.09585  0.18348  -0.20078 18  LEU A CB  
149  C CG  . LEU A 23  ? 1.09808 1.03398 0.80232 0.10518  0.19643  -0.17802 18  LEU A CG  
150  C CD1 . LEU A 23  ? 0.95685 0.91038 0.70232 0.09322  0.19530  -0.14195 18  LEU A CD1 
151  C CD2 . LEU A 23  ? 1.17016 1.12784 0.81978 0.10741  0.18776  -0.19123 18  LEU A CD2 
152  N N   . ASP A 24  ? 0.98568 0.82722 0.68631 0.05698  0.15069  -0.28064 19  ASP A N   
153  C CA  . ASP A 24  ? 1.01472 0.82364 0.74444 0.03243  0.13932  -0.29295 19  ASP A CA  
154  C C   . ASP A 24  ? 0.94147 0.76892 0.68234 0.02345  0.12165  -0.24838 19  ASP A C   
155  O O   . ASP A 24  ? 0.94818 0.81766 0.66599 0.01689  0.10402  -0.24415 19  ASP A O   
156  C CB  . ASP A 24  ? 1.21682 1.04350 0.93341 0.01513  0.12626  -0.34968 19  ASP A CB  
157  C CG  . ASP A 24  ? 1.29579 1.08422 1.05692 -0.01387 0.12295  -0.36868 19  ASP A CG  
158  O OD1 . ASP A 24  ? 1.32541 1.05681 1.12193 -0.01360 0.14013  -0.34124 19  ASP A OD1 
159  O OD2 . ASP A 24  ? 1.31930 1.14098 1.08222 -0.03305 0.10404  -0.40765 19  ASP A OD2 
160  N N   . PRO A 25  ? 0.81129 0.61334 0.58456 0.02822  0.12696  -0.21478 20  PRO A N   
161  C CA  . PRO A 25  ? 0.78968 0.61437 0.57454 0.02212  0.11110  -0.17669 20  PRO A CA  
162  C C   . PRO A 25  ? 0.89745 0.69818 0.70096 0.00435  0.09831  -0.17368 20  PRO A C   
163  O O   . PRO A 25  ? 0.86373 0.67070 0.68293 0.00406  0.08873  -0.14263 20  PRO A O   
164  C CB  . PRO A 25  ? 0.75931 0.58640 0.56953 0.04298  0.12265  -0.15103 20  PRO A CB  
165  C CG  . PRO A 25  ? 0.78039 0.55987 0.60021 0.05815  0.14215  -0.16587 20  PRO A CG  
166  C CD  . PRO A 25  ? 0.79641 0.55884 0.59239 0.04804  0.14956  -0.20907 20  PRO A CD  
167  N N   . SER A 26  ? 0.92891 0.70436 0.73621 -0.01088 0.10045  -0.20979 21  SER A N   
168  C CA  . SER A 26  ? 0.90845 0.65513 0.74431 -0.02859 0.09681  -0.20857 21  SER A CA  
169  C C   . SER A 26  ? 0.86390 0.64941 0.69211 -0.04050 0.07064  -0.18550 21  SER A C   
170  O O   . SER A 26  ? 0.91950 0.68866 0.76802 -0.04229 0.06750  -0.15791 21  SER A O   
171  C CB  . SER A 26  ? 0.98800 0.71241 0.84036 -0.04979 0.10566  -0.26291 21  SER A CB  
172  O OG  . SER A 26  ? 1.11636 0.89239 0.93641 -0.05356 0.09142  -0.30146 21  SER A OG  
173  N N   . SER A 27  ? 0.80374 0.64119 0.59887 -0.04253 0.05507  -0.19271 22  SER A N   
174  C CA  . SER A 27  ? 0.78550 0.65872 0.56933 -0.04950 0.03489  -0.17045 22  SER A CA  
175  C C   . SER A 27  ? 0.73398 0.60153 0.52940 -0.04219 0.03451  -0.12374 22  SER A C   
176  O O   . SER A 27  ? 0.68617 0.56618 0.48301 -0.04945 0.02126  -0.10350 22  SER A O   
177  C CB  . SER A 27  ? 0.88334 0.81244 0.62194 -0.03884 0.02802  -0.17778 22  SER A CB  
178  O OG  . SER A 27  ? 0.80210 0.73591 0.52325 -0.01898 0.04526  -0.16104 22  SER A OG  
179  N N   . MET A 28  ? 0.66636 0.52146 0.47345 -0.02711 0.04832  -0.11101 23  MET A N   
180  C CA  . MET A 28  ? 0.65876 0.52393 0.48410 -0.02016 0.04643  -0.07958 23  MET A CA  
181  C C   . MET A 28  ? 0.71073 0.55578 0.55785 -0.02075 0.03773  -0.06435 23  MET A C   
182  O O   . MET A 28  ? 0.66085 0.52327 0.51856 -0.01924 0.02906  -0.04378 23  MET A O   
183  C CB  . MET A 28  ? 0.60054 0.47213 0.44067 -0.00204 0.06161  -0.07891 23  MET A CB  
184  C CG  . MET A 28  ? 0.65271 0.54958 0.47719 0.00153  0.07526  -0.08356 23  MET A CG  
185  S SD  . MET A 28  ? 0.71166 0.62180 0.56574 0.02205  0.09314  -0.08586 23  MET A SD  
186  C CE  . MET A 28  ? 0.72256 0.65909 0.56019 0.02436  0.11556  -0.08597 23  MET A CE  
187  N N   . ILE A 29  ? 0.66883 0.47618 0.52555 -0.02129 0.04449  -0.07441 24  ILE A N   
188  C CA  . ILE A 29  ? 0.70661 0.49226 0.58176 -0.01429 0.04397  -0.05315 24  ILE A CA  
189  C C   . ILE A 29  ? 0.69058 0.48989 0.56308 -0.03333 0.02604  -0.04359 24  ILE A C   
190  O O   . ILE A 29  ? 0.70349 0.51757 0.57931 -0.02624 0.01576  -0.01973 24  ILE A O   
191  C CB  . ILE A 29  ? 0.76345 0.49502 0.65542 -0.00774 0.06844  -0.06142 24  ILE A CB  
192  C CG1 . ILE A 29  ? 0.81048 0.53077 0.70355 0.02428  0.08781  -0.05706 24  ILE A CG1 
193  C CG2 . ILE A 29  ? 0.78161 0.48753 0.69060 -0.00188 0.07378  -0.03623 24  ILE A CG2 
194  C CD1 . ILE A 29  ? 0.91059 0.56817 0.81966 0.03821  0.12236  -0.05912 24  ILE A CD1 
195  N N   . VAL A 30  ? 0.71197 0.51440 0.57945 -0.05562 0.02118  -0.06593 25  VAL A N   
196  C CA  . VAL A 30  ? 0.73228 0.55318 0.59935 -0.07030 0.00493  -0.05699 25  VAL A CA  
197  C C   . VAL A 30  ? 0.69889 0.55639 0.54374 -0.06557 -0.00833 -0.03458 25  VAL A C   
198  O O   . VAL A 30  ? 0.67918 0.54153 0.52775 -0.06529 -0.01710 -0.01128 25  VAL A O   
199  C CB  . VAL A 30  ? 0.80287 0.63864 0.67350 -0.09244 0.00022  -0.09445 25  VAL A CB  
200  C CG1 . VAL A 30  ? 0.78146 0.65522 0.61991 -0.08963 -0.00541 -0.11765 25  VAL A CG1 
201  C CG2 . VAL A 30  ? 0.81991 0.68194 0.69512 -0.10469 -0.01609 -0.08558 25  VAL A CG2 
202  N N   . LEU A 31  ? 0.59911 0.47810 0.42348 -0.06007 -0.00421 -0.03980 26  LEU A N   
203  C CA  . LEU A 31  ? 0.65283 0.55678 0.46299 -0.05589 -0.00500 -0.01700 26  LEU A CA  
204  C C   . LEU A 31  ? 0.65373 0.55212 0.48889 -0.04878 -0.00030 -0.00032 26  LEU A C   
205  O O   . LEU A 31  ? 0.57598 0.48309 0.41568 -0.05035 -0.00188 0.01760  26  LEU A O   
206  C CB  . LEU A 31  ? 0.59360 0.52069 0.37550 -0.04812 0.00665  -0.02346 26  LEU A CB  
207  C CG  . LEU A 31  ? 0.63603 0.59399 0.38523 -0.04786 -0.00317 -0.04033 26  LEU A CG  
208  C CD1 . LEU A 31  ? 0.61420 0.59988 0.32686 -0.02982 0.01056  -0.04551 26  LEU A CD1 
209  C CD2 . LEU A 31  ? 0.64715 0.62585 0.38550 -0.04801 -0.01425 -0.01885 26  LEU A CD2 
210  N N   . GLY A 32  ? 0.58572 0.47558 0.43899 -0.03875 0.00633  -0.00980 27  GLY A N   
211  C CA  . GLY A 32  ? 0.55244 0.45528 0.43361 -0.02792 0.00571  -0.00340 27  GLY A CA  
212  C C   . GLY A 32  ? 0.59766 0.49478 0.48580 -0.02251 -0.00777 0.01025  27  GLY A C   
213  O O   . GLY A 32  ? 0.54251 0.45970 0.44568 -0.02066 -0.01370 0.01563  27  GLY A O   
214  N N   . ARG A 33  ? 0.57488 0.44388 0.45576 -0.02047 -0.00905 0.01401  28  ARG A N   
215  C CA  . ARG A 33  ? 0.63881 0.50016 0.52431 -0.01190 -0.01658 0.03218  28  ARG A CA  
216  C C   . ARG A 33  ? 0.67396 0.54422 0.55105 -0.02873 -0.02772 0.04298  28  ARG A C   
217  O O   . ARG A 33  ? 0.61048 0.48886 0.49206 -0.02016 -0.03563 0.05689  28  ARG A O   
218  C CB  . ARG A 33  ? 0.61660 0.43870 0.50570 -0.00688 -0.00441 0.03574  28  ARG A CB  
219  C CG  . ARG A 33  ? 0.68734 0.49684 0.58321 0.02540  0.01118  0.03971  28  ARG A CG  
220  C CD  . ARG A 33  ? 0.66211 0.41949 0.56736 0.03122  0.03582  0.04659  28  ARG A CD  
221  N NE  . ARG A 33  ? 0.67121 0.41331 0.57764 0.06637  0.05714  0.05166  28  ARG A NE  
222  C CZ  . ARG A 33  ? 0.69894 0.38605 0.61676 0.07408  0.09023  0.05279  28  ARG A CZ  
223  N NH1 . ARG A 33  ? 0.73530 0.38104 0.67316 0.04314  0.10468  0.04195  28  ARG A NH1 
224  N NH2 . ARG A 33  ? 0.73336 0.40950 0.64756 0.11338  0.11158  0.06215  28  ARG A NH2 
225  N N   . LEU A 34  ? 0.58296 0.45688 0.44479 -0.04714 -0.02799 0.03661  29  LEU A N   
226  C CA  . LEU A 34  ? 0.63632 0.52390 0.48549 -0.05607 -0.03566 0.05039  29  LEU A CA  
227  C C   . LEU A 34  ? 0.60804 0.50766 0.46275 -0.05194 -0.03197 0.06099  29  LEU A C   
228  O O   . LEU A 34  ? 0.55347 0.45447 0.41047 -0.05047 -0.03742 0.07552  29  LEU A O   
229  C CB  . LEU A 34  ? 0.60891 0.51332 0.43504 -0.06541 -0.03547 0.04007  29  LEU A CB  
230  C CG  . LEU A 34  ? 0.70425 0.63082 0.51022 -0.06495 -0.03984 0.05860  29  LEU A CG  
231  C CD1 . LEU A 34  ? 0.70315 0.63275 0.51740 -0.07139 -0.05320 0.06316  29  LEU A CD1 
232  C CD2 . LEU A 34  ? 0.78598 0.74306 0.55985 -0.05949 -0.03568 0.05217  29  LEU A CD2 
233  N N   . GLN A 35  ? 0.50709 0.41466 0.36953 -0.05144 -0.01889 0.05117  30  GLN A N   
234  C CA  . GLN A 35  ? 0.49814 0.41470 0.38097 -0.05338 -0.00675 0.05391  30  GLN A CA  
235  C C   . GLN A 35  ? 0.49624 0.42619 0.41079 -0.04561 -0.01676 0.04267  30  GLN A C   
236  O O   . GLN A 35  ? 0.49754 0.43350 0.42947 -0.04866 -0.01466 0.04281  30  GLN A O   
237  C CB  . GLN A 35  ? 0.53529 0.45818 0.42736 -0.05596 0.01608  0.04501  30  GLN A CB  
238  C CG  . GLN A 35  ? 0.66191 0.58178 0.51472 -0.05411 0.02878  0.05855  30  GLN A CG  
239  C CD  . GLN A 35  ? 0.76142 0.68645 0.61839 -0.05090 0.05505  0.05346  30  GLN A CD  
240  O OE1 . GLN A 35  ? 0.83563 0.75784 0.71698 -0.05338 0.08381  0.06125  30  GLN A OE1 
241  N NE2 . GLN A 35  ? 0.77220 0.70220 0.61007 -0.04570 0.04990  0.03907  30  GLN A NE2 
242  N N   . GLU A 36  ? 0.47695 0.41548 0.39845 -0.03107 -0.02570 0.03136  31  GLU A N   
243  C CA  . GLU A 36  ? 0.51313 0.48032 0.45730 -0.01244 -0.03740 0.02017  31  GLU A CA  
244  C C   . GLU A 36  ? 0.56325 0.52188 0.49185 -0.00311 -0.05038 0.03817  31  GLU A C   
245  O O   . GLU A 36  ? 0.53320 0.51895 0.47756 0.00723  -0.05904 0.02833  31  GLU A O   
246  C CB  . GLU A 36  ? 0.54321 0.52500 0.49060 0.01256  -0.03987 0.01129  31  GLU A CB  
247  C CG  . GLU A 36  ? 0.56946 0.59878 0.53298 0.04531  -0.05374 -0.00070 31  GLU A CG  
248  C CD  . GLU A 36  ? 0.65006 0.73582 0.66027 0.03885  -0.05545 -0.03796 31  GLU A CD  
249  O OE1 . GLU A 36  ? 0.70293 0.77806 0.73468 0.00710  -0.03946 -0.04725 31  GLU A OE1 
250  O OE2 . GLU A 36  ? 0.62416 0.76930 0.65290 0.06750  -0.06983 -0.05986 31  GLU A OE2 
251  N N   . ALA A 37  ? 0.51456 0.44117 0.41714 -0.00616 -0.05106 0.05987  32  ALA A N   
252  C CA  . ALA A 37  ? 0.59231 0.51079 0.48385 0.00246  -0.05928 0.07969  32  ALA A CA  
253  C C   . ALA A 37  ? 0.60249 0.52461 0.49382 -0.01140 -0.06078 0.08448  32  ALA A C   
254  O O   . ALA A 37  ? 0.54115 0.47481 0.43549 0.00089  -0.06830 0.08716  32  ALA A O   
255  C CB  . ALA A 37  ? 0.60301 0.49026 0.48142 -0.00343 -0.05479 0.09571  32  ALA A CB  
256  N N   . ALA A 38  ? 0.54915 0.46210 0.43413 -0.03171 -0.05047 0.08689  33  ALA A N   
257  C CA  . ALA A 38  ? 0.52389 0.43351 0.40770 -0.03932 -0.04269 0.09688  33  ALA A CA  
258  C C   . ALA A 38  ? 0.52622 0.45051 0.44450 -0.03865 -0.03662 0.07480  33  ALA A C   
259  O O   . ALA A 38  ? 0.54414 0.46725 0.46833 -0.03662 -0.03637 0.07685  33  ALA A O   
260  C CB  . ALA A 38  ? 0.55316 0.45928 0.42635 -0.04706 -0.02388 0.10232  33  ALA A CB  
261  N N   . LEU A 39  ? 0.42422 0.36713 0.37081 -0.04087 -0.03112 0.04838  34  LEU A N   
262  C CA  . LEU A 39  ? 0.42591 0.39440 0.42052 -0.04570 -0.02346 0.01515  34  LEU A CA  
263  C C   . LEU A 39  ? 0.45049 0.45581 0.45353 -0.02370 -0.04799 -0.00383 34  LEU A C   
264  O O   . LEU A 39  ? 0.43464 0.45232 0.46074 -0.02582 -0.04726 -0.02242 34  LEU A O   
265  C CB  . LEU A 39  ? 0.44334 0.43278 0.47092 -0.05277 -0.01163 -0.01015 34  LEU A CB  
266  C CG  . LEU A 39  ? 0.45105 0.48554 0.54440 -0.05909 -0.00646 -0.05808 34  LEU A CG  
267  C CD1 . LEU A 39  ? 0.46907 0.48130 0.59537 -0.08059 0.02031  -0.06504 34  LEU A CD1 
268  C CD2 . LEU A 39  ? 0.44270 0.50337 0.57299 -0.06597 0.00670  -0.08188 34  LEU A CD2 
269  N N   . VAL A 40  ? 0.42389 0.44666 0.40672 0.00186  -0.06620 0.00123  35  VAL A N   
270  C CA  . VAL A 40  ? 0.45644 0.52340 0.43907 0.03575  -0.08680 -0.01248 35  VAL A CA  
271  C C   . VAL A 40  ? 0.50439 0.55341 0.46225 0.04339  -0.09293 0.00940  35  VAL A C   
272  O O   . VAL A 40  ? 0.52403 0.61023 0.49272 0.06020  -0.10432 -0.01311 35  VAL A O   
273  C CB  . VAL A 40  ? 0.50396 0.58172 0.46349 0.06929  -0.09416 0.00120  35  VAL A CB  
274  C CG1 . VAL A 40  ? 0.53577 0.65428 0.47859 0.11657  -0.11047 0.00261  35  VAL A CG1 
275  C CG2 . VAL A 40  ? 0.48480 0.59680 0.47314 0.06978  -0.09090 -0.02743 35  VAL A CG2 
276  N N   . ILE A 41  ? 0.48761 0.48690 0.41475 0.03182  -0.08589 0.04889  36  ILE A N   
277  C CA  . ILE A 41  ? 0.54842 0.53264 0.45364 0.03975  -0.08984 0.07297  36  ILE A CA  
278  C C   . ILE A 41  ? 0.51065 0.49133 0.43392 0.02271  -0.08196 0.05860  36  ILE A C   
279  O O   . ILE A 41  ? 0.55152 0.54715 0.47335 0.03829  -0.08960 0.05184  36  ILE A O   
280  C CB  . ILE A 41  ? 0.54899 0.51117 0.45005 0.03382  -0.05919 0.08702  36  ILE A CB  
281  C CG1 . ILE A 41  ? 0.55114 0.51944 0.45384 0.05069  -0.04948 0.08891  36  ILE A CG1 
282  C CG2 . ILE A 41  ? 0.54091 0.49610 0.43958 0.03775  -0.04430 0.08561  36  ILE A CG2 
283  C CD1 . ILE A 41  ? 0.65588 0.59335 0.55182 0.03990  -0.03703 0.09292  36  ILE A CD1 
284  N N   . ALA A 42  ? 0.48962 0.44889 0.43080 -0.00582 -0.06160 0.05384  37  ALA A N   
285  C CA  . ALA A 42  ? 0.48252 0.42917 0.44928 -0.02058 -0.04223 0.04030  37  ALA A CA  
286  C C   . ALA A 42  ? 0.51280 0.50383 0.52636 -0.01668 -0.04831 -0.01418 37  ALA A C   
287  O O   . ALA A 42  ? 0.48519 0.48176 0.50794 -0.01120 -0.04924 -0.02947 37  ALA A O   
288  C CB  . ALA A 42  ? 0.51919 0.43408 0.49863 -0.04463 -0.00983 0.04896  37  ALA A CB  
289  N N   . ARG A 43  ? 0.39594 0.42675 0.44152 -0.01771 -0.05357 -0.04870 38  ARG A N   
290  C CA  . ARG A 43  ? 0.42696 0.51474 0.53183 -0.01930 -0.05730 -0.11261 38  ARG A CA  
291  C C   . ARG A 43  ? 0.45688 0.60215 0.54460 0.01969  -0.09073 -0.13216 38  ARG A C   
292  O O   . ARG A 43  ? 0.43360 0.61356 0.55541 0.02044  -0.09417 -0.17844 38  ARG A O   
293  C CB  . ARG A 43  ? 0.37061 0.49676 0.51398 -0.02654 -0.05554 -0.14269 38  ARG A CB  
294  C CG  . ARG A 43  ? 0.43030 0.63258 0.64837 -0.03089 -0.06027 -0.21889 38  ARG A CG  
295  C CD  . ARG A 43  ? 0.46844 0.72007 0.71699 -0.02916 -0.06399 -0.24282 38  ARG A CD  
296  N NE  . ARG A 43  ? 0.55054 0.83030 0.74141 0.01525  -0.09423 -0.21594 38  ARG A NE  
297  C CZ  . ARG A 43  ? 0.67051 0.94352 0.84553 0.02111  -0.09143 -0.19457 38  ARG A CZ  
298  N NH1 . ARG A 43  ? 0.60645 0.85089 0.81400 -0.01340 -0.06348 -0.19607 38  ARG A NH1 
299  N NH2 . ARG A 43  ? 0.69952 0.98948 0.82510 0.06436  -0.11133 -0.16882 38  ARG A NH2 
300  N N   . ASP A 44  ? 0.48724 0.64270 0.52331 0.05494  -0.11133 -0.09805 39  ASP A N   
301  C CA  . ASP A 44  ? 0.55253 0.77099 0.56690 0.10463  -0.13857 -0.11107 39  ASP A CA  
302  C C   . ASP A 44  ? 0.48478 0.66259 0.45098 0.12079  -0.13302 -0.06697 39  ASP A C   
303  O O   . ASP A 44  ? 0.51504 0.71992 0.47019 0.14758  -0.13141 -0.07822 39  ASP A O   
304  C CB  . ASP A 44  ? 0.53327 0.75958 0.52503 0.12920  -0.13357 -0.09076 39  ASP A CB  
305  C CG  . ASP A 44  ? 0.63597 0.92017 0.67594 0.12401  -0.13777 -0.14037 39  ASP A CG  
306  O OD1 . ASP A 44  ? 0.63481 0.95360 0.73521 0.09721  -0.13742 -0.19535 39  ASP A OD1 
307  O OD2 . ASP A 44  ? 0.68517 0.97558 0.70885 0.14307  -0.13448 -0.12594 39  ASP A OD2 
308  N N   . ARG A 45  ? 0.54605 0.58045 0.36107 0.10827  0.00035  0.05321  40  ARG A N   
309  C CA  . ARG A 45  ? 0.58422 0.64074 0.40565 0.11526  0.01537  0.09177  40  ARG A CA  
310  C C   . ARG A 45  ? 0.61018 0.67631 0.44308 0.10225  0.00866  0.07245  40  ARG A C   
311  O O   . ARG A 45  ? 0.53730 0.65517 0.35948 0.12975  0.01147  0.06997  40  ARG A O   
312  C CB  . ARG A 45  ? 0.62771 0.64419 0.47919 0.09184  0.02934  0.13565  40  ARG A CB  
313  C CG  . ARG A 45  ? 0.64948 0.63854 0.49160 0.10291  0.03520  0.15740  40  ARG A CG  
314  C CD  . ARG A 45  ? 0.62142 0.65163 0.42101 0.15537  0.05055  0.18261  40  ARG A CD  
315  N NE  . ARG A 45  ? 0.65190 0.70373 0.45811 0.16751  0.08316  0.23564  40  ARG A NE  
316  C CZ  . ARG A 45  ? 0.79344 0.81181 0.61861 0.16413  0.11321  0.29208  40  ARG A CZ  
317  N NH1 . ARG A 45  ? 0.80651 0.76498 0.64368 0.15102  0.10838  0.29974  40  ARG A NH1 
318  N NH2 . ARG A 45  ? 0.82133 0.86522 0.65755 0.17448  0.15136  0.34130  40  ARG A NH2 
319  N N   . LEU A 46  ? 0.53185 0.54982 0.38006 0.06808  -0.00127 0.05841  41  LEU A N   
320  C CA  . LEU A 46  ? 0.47638 0.49644 0.33135 0.06156  -0.00792 0.04765  41  LEU A CA  
321  C C   . LEU A 46  ? 0.51695 0.54482 0.35280 0.07321  -0.01780 0.00747  41  LEU A C   
322  O O   . LEU A 46  ? 0.49657 0.55957 0.33100 0.09124  -0.02119 -0.00085 41  LEU A O   
323  C CB  . LEU A 46  ? 0.52221 0.48626 0.38942 0.03259  -0.01815 0.04466  41  LEU A CB  
324  C CG  . LEU A 46  ? 0.53198 0.48065 0.43545 0.01627  -0.01451 0.07113  41  LEU A CG  
325  C CD1 . LEU A 46  ? 0.57396 0.47688 0.48483 -0.00108 -0.03362 0.05341  41  LEU A CD1 
326  C CD2 . LEU A 46  ? 0.59444 0.59123 0.53705 0.02224  0.00316  0.10350  41  LEU A CD2 
327  N N   . ASN A 47  ? 0.50937 0.50297 0.33820 0.06138  -0.02102 -0.02021 42  ASN A N   
328  C CA  . ASN A 47  ? 0.51574 0.50456 0.34381 0.06426  -0.02590 -0.06058 42  ASN A CA  
329  C C   . ASN A 47  ? 0.53884 0.59751 0.37289 0.09937  -0.03232 -0.08454 42  ASN A C   
330  O O   . ASN A 47  ? 0.57354 0.64153 0.41251 0.10971  -0.04044 -0.11105 42  ASN A O   
331  C CB  . ASN A 47  ? 0.58949 0.53064 0.42186 0.04061  -0.01899 -0.08351 42  ASN A CB  
332  C CG  . ASN A 47  ? 0.64061 0.51010 0.45301 0.01652  -0.01401 -0.06709 42  ASN A CG  
333  O OD1 . ASN A 47  ? 0.60277 0.45952 0.40257 0.01931  -0.02167 -0.04861 42  ASN A OD1 
334  N ND2 . ASN A 47  ? 0.68933 0.51821 0.49852 -0.00197 -0.00182 -0.07704 42  ASN A ND2 
335  N N   . PRO A 48  ? 0.51863 0.62640 0.34804 0.12530  -0.03170 -0.07939 43  PRO A N   
336  C CA  . PRO A 48  ? 0.53738 0.71921 0.36182 0.17192  -0.04203 -0.10547 43  PRO A CA  
337  C C   . PRO A 48  ? 0.61973 0.83799 0.43124 0.19432  -0.04065 -0.08609 43  PRO A C   
338  O O   . PRO A 48  ? 0.62517 0.89097 0.43706 0.22682  -0.05443 -0.12218 43  PRO A O   
339  C CB  . PRO A 48  ? 0.54251 0.75981 0.34677 0.20256  -0.03881 -0.08883 43  PRO A CB  
340  C CG  . PRO A 48  ? 0.51731 0.67602 0.33429 0.16425  -0.03362 -0.08389 43  PRO A CG  
341  C CD  . PRO A 48  ? 0.51870 0.61555 0.34246 0.12130  -0.02488 -0.05677 43  PRO A CD  
342  N N   . LEU A 49  ? 0.57506 0.77731 0.38348 0.17865  -0.02535 -0.03578 44  LEU A N   
343  C CA  . LEU A 49  ? 0.55419 0.79801 0.36100 0.19723  -0.02107 -0.02080 44  LEU A CA  
344  C C   . LEU A 49  ? 0.54792 0.76481 0.36527 0.18497  -0.03824 -0.05565 44  LEU A C   
345  O O   . LEU A 49  ? 0.56372 0.82615 0.37718 0.21586  -0.04804 -0.07829 44  LEU A O   
346  C CB  . LEU A 49  ? 0.54143 0.78061 0.36269 0.17987  0.00187  0.03537  44  LEU A CB  
347  C CG  . LEU A 49  ? 0.58853 0.87983 0.42202 0.19525  0.01219  0.05164  44  LEU A CG  
348  C CD1 . LEU A 49  ? 0.72663 1.04588 0.57525 0.19786  0.04799  0.11011  44  LEU A CD1 
349  C CD2 . LEU A 49  ? 0.50866 0.76873 0.36767 0.16831  -0.00243 0.03561  44  LEU A CD2 
350  N N   . PHE A 50  ? 0.54025 0.68094 0.36479 0.14609  -0.04193 -0.06012 45  PHE A N   
351  C CA  . PHE A 50  ? 0.56318 0.66273 0.38636 0.14011  -0.05530 -0.08921 45  PHE A CA  
352  C C   . PHE A 50  ? 0.58947 0.70329 0.42083 0.15900  -0.06706 -0.13953 45  PHE A C   
353  O O   . PHE A 50  ? 0.57863 0.69341 0.41137 0.17496  -0.07997 -0.16500 45  PHE A O   
354  C CB  . PHE A 50  ? 0.55346 0.56380 0.36878 0.10401  -0.05257 -0.08381 45  PHE A CB  
355  C CG  . PHE A 50  ? 0.55059 0.54676 0.36669 0.08855  -0.04946 -0.04830 45  PHE A CG  
356  C CD1 . PHE A 50  ? 0.55142 0.59665 0.38407 0.10057  -0.05083 -0.03015 45  PHE A CD1 
357  C CD2 . PHE A 50  ? 0.50835 0.44571 0.31648 0.06293  -0.04541 -0.03881 45  PHE A CD2 
358  C CE1 . PHE A 50  ? 0.52042 0.55669 0.37420 0.08381  -0.04991 -0.00743 45  PHE A CE1 
359  C CE2 . PHE A 50  ? 0.55734 0.48490 0.37571 0.05194  -0.04867 -0.01687 45  PHE A CE2 
360  C CZ  . PHE A 50  ? 0.58301 0.55901 0.43005 0.06053  -0.05205 -0.00367 45  PHE A CZ  
361  N N   . ALA A 51  ? 0.63822 0.76346 0.48251 0.15856  -0.06546 -0.16081 46  ALA A N   
362  C CA  . ALA A 51  ? 0.66957 0.81115 0.54185 0.17332  -0.07925 -0.22062 46  ALA A CA  
363  C C   . ALA A 51  ? 0.63697 0.86880 0.50428 0.22750  -0.09676 -0.24358 46  ALA A C   
364  O O   . ALA A 51  ? 0.66525 0.90886 0.56072 0.24331  -0.11476 -0.29319 46  ALA A O   
365  C CB  . ALA A 51  ? 0.65497 0.79676 0.55419 0.16057  -0.07524 -0.24639 46  ALA A CB  
366  N N   . ARG A 52  ? 0.65391 0.94736 0.49014 0.25676  -0.08911 -0.20419 47  ARG A N   
367  C CA  . ARG A 52  ? 0.71785 1.09653 0.54142 0.31218  -0.09921 -0.21379 47  ARG A CA  
368  C C   . ARG A 52  ? 0.71406 1.08477 0.54434 0.31554  -0.10980 -0.22758 47  ARG A C   
369  O O   . ARG A 52  ? 0.62832 1.05094 0.48078 0.35134  -0.12743 -0.25156 47  ARG A O   
370  C CB  . ARG A 52  ? 0.73782 1.16797 0.52393 0.33724  -0.07519 -0.15328 47  ARG A CB  
371  C CG  . ARG A 52  ? 0.80070 1.25009 0.57545 0.35467  -0.06678 -0.13569 47  ARG A CG  
372  C CD  . ARG A 52  ? 0.97727 1.48590 0.72751 0.39803  -0.04262 -0.08325 47  ARG A CD  
373  N NE  . ARG A 52  ? 1.02385 1.51323 0.75493 0.37150  -0.00849 -0.01772 47  ARG A NE  
374  C CZ  . ARG A 52  ? 1.08804 1.62175 0.81634 0.39037  0.01778  0.02474  47  ARG A CZ  
375  N NH1 . ARG A 52  ? 1.08345 1.59710 0.82098 0.35714  0.05063  0.08116  47  ARG A NH1 
376  N NH2 . ARG A 52  ? 1.07472 1.67319 0.80571 0.44000  0.01043  0.00988  47  ARG A NH2 
377  N N   . TYR A 53  ? 0.67189 0.97406 0.49920 0.27657  -0.10173 -0.20343 48  TYR A N   
378  C CA  . TYR A 53  ? 0.67333 0.95739 0.50105 0.28137  -0.11366 -0.21496 48  TYR A CA  
379  C C   . TYR A 53  ? 0.69673 0.89522 0.54201 0.26044  -0.12704 -0.25636 48  TYR A C   
380  O O   . TYR A 53  ? 0.70913 0.86813 0.54730 0.26277  -0.13675 -0.26242 48  TYR A O   
381  C CB  . TYR A 53  ? 0.70533 0.96858 0.52509 0.25857  -0.09970 -0.16499 48  TYR A CB  
382  C CG  . TYR A 53  ? 0.66531 1.01716 0.48290 0.28257  -0.08237 -0.12809 48  TYR A CG  
383  C CD1 . TYR A 53  ? 0.68520 1.09872 0.50395 0.31554  -0.08723 -0.13478 48  TYR A CD1 
384  C CD2 . TYR A 53  ? 0.64802 1.01995 0.46433 0.27363  -0.05715 -0.08510 48  TYR A CD2 
385  C CE1 . TYR A 53  ? 0.64864 1.14585 0.47126 0.33609  -0.06158 -0.09738 48  TYR A CE1 
386  C CE2 . TYR A 53  ? 0.75073 1.19639 0.56797 0.29502  -0.03097 -0.04410 48  TYR A CE2 
387  C CZ  . TYR A 53  ? 0.71677 1.22633 0.53932 0.32433  -0.03043 -0.04932 48  TYR A CZ  
388  O OH  . TYR A 53  ? 0.81620 1.40027 0.64573 0.34322  0.00480  -0.00510 48  TYR A OH  
389  N N   . GLY A 54  ? 0.68879 0.85758 0.55974 0.24209  -0.12531 -0.28503 49  GLY A N   
390  C CA  . GLY A 54  ? 0.70218 0.78454 0.60132 0.21670  -0.12669 -0.31916 49  GLY A CA  
391  C C   . GLY A 54  ? 0.70211 0.67848 0.57834 0.17463  -0.10601 -0.28102 49  GLY A C   
392  O O   . GLY A 54  ? 0.77654 0.66689 0.65967 0.15979  -0.10113 -0.29618 49  GLY A O   
393  N N   . LEU A 55  ? 0.64310 0.62029 0.49152 0.15870  -0.09293 -0.23203 50  LEU A N   
394  C CA  . LEU A 55  ? 0.70246 0.59087 0.52057 0.12962  -0.07850 -0.19757 50  LEU A CA  
395  C C   . LEU A 55  ? 0.79791 0.65558 0.62512 0.09599  -0.05702 -0.18773 50  LEU A C   
396  O O   . LEU A 55  ? 0.73592 0.65093 0.57326 0.09551  -0.05518 -0.17790 50  LEU A O   
397  C CB  . LEU A 55  ? 0.64996 0.56409 0.44081 0.13836  -0.08455 -0.15907 50  LEU A CB  
398  C CG  . LEU A 55  ? 0.61679 0.55986 0.39861 0.17077  -0.10408 -0.16710 50  LEU A CG  
399  C CD1 . LEU A 55  ? 0.69854 0.67819 0.47591 0.17297  -0.10644 -0.13492 50  LEU A CD1 
400  C CD2 . LEU A 55  ? 0.76447 0.61448 0.52098 0.17571  -0.11084 -0.18289 50  LEU A CD2 
401  N N   . GLN A 56  ? 0.85560 0.62078 0.67598 0.07146  -0.03805 -0.18827 51  GLN A N   
402  C CA  . GLN A 56  ? 0.93072 0.66137 0.75536 0.04028  -0.01340 -0.17729 51  GLN A CA  
403  C C   . GLN A 56  ? 0.93193 0.64262 0.70881 0.03633  -0.01251 -0.13327 51  GLN A C   
404  O O   . GLN A 56  ? 0.88522 0.59220 0.62995 0.05405  -0.02835 -0.11521 51  GLN A O   
405  C CB  . GLN A 56  ? 0.98820 0.62600 0.82292 0.01750  0.01526  -0.18933 51  GLN A CB  
406  N N   . PRO A 57  ? 1.05880 0.76469 0.83782 0.01610  0.00214  -0.12213 52  PRO A N   
407  C CA  . PRO A 57  ? 1.04670 0.73094 0.78658 0.01441  -0.00075 -0.08871 52  PRO A CA  
408  C C   . PRO A 57  ? 1.06742 0.66678 0.75065 0.02279  0.00353  -0.07369 52  PRO A C   
409  O O   . PRO A 57  ? 1.10687 0.63464 0.77210 0.01461  0.02928  -0.07543 52  PRO A O   
410  C CB  . PRO A 57  ? 1.09359 0.77755 0.84754 -0.00699 0.01696  -0.08924 52  PRO A CB  
411  C CG  . PRO A 57  ? 1.09499 0.84094 0.90324 -0.00840 0.01721  -0.12120 52  PRO A CG  
412  C CD  . PRO A 57  ? 1.07614 0.81209 0.90079 -0.00051 0.01551  -0.14667 52  PRO A CD  
413  N N   . GLY A 58  ? 0.82139 0.42949 0.47856 0.04246  -0.02036 -0.05969 53  GLY A N   
414  C CA  . GLY A 58  ? 0.82146 0.36046 0.41706 0.06458  -0.02614 -0.04982 53  GLY A CA  
415  C C   . GLY A 58  ? 0.88336 0.42312 0.47009 0.09097  -0.04481 -0.05996 53  GLY A C   
416  O O   . GLY A 58  ? 0.88364 0.39761 0.42681 0.11959  -0.06430 -0.05585 53  GLY A O   
417  N N   . GLU A 59  ? 0.46127 0.58178 0.47189 0.00877  0.04322  -0.05073 54  GLU A N   
418  C CA  . GLU A 59  ? 0.45581 0.56297 0.44699 0.01246  0.04346  -0.04785 54  GLU A CA  
419  C C   . GLU A 59  ? 0.43896 0.54893 0.39244 0.02878  0.03984  -0.02395 54  GLU A C   
420  O O   . GLU A 59  ? 0.44641 0.54442 0.38227 0.02907  0.04679  -0.01160 54  GLU A O   
421  C CB  . GLU A 59  ? 0.41869 0.54047 0.43104 0.01966  0.02870  -0.08118 54  GLU A CB  
422  C CG  . GLU A 59  ? 0.49407 0.61421 0.56092 -0.00285 0.03589  -0.10596 54  GLU A CG  
423  C CD  . GLU A 59  ? 0.61945 0.75535 0.72046 0.00187  0.01676  -0.14786 54  GLU A CD  
424  O OE1 . GLU A 59  ? 0.63049 0.79152 0.70678 0.03008  -0.00730 -0.16206 54  GLU A OE1 
425  O OE2 . GLU A 59  ? 0.67724 0.80111 0.83124 -0.02186 0.02645  -0.16717 54  GLU A OE2 
426  N N   . PHE A 60  ? 0.43309 0.55993 0.37713 0.04384  0.03065  -0.01551 55  PHE A N   
427  C CA  . PHE A 60  ? 0.46579 0.59420 0.38422 0.05378  0.03489  0.01446  55  PHE A CA  
428  C C   . PHE A 60  ? 0.39445 0.50544 0.31838 0.03550  0.04712  0.03166  55  PHE A C   
429  O O   . PHE A 60  ? 0.45745 0.57190 0.37082 0.03681  0.05347  0.04597  55  PHE A O   
430  C CB  . PHE A 60  ? 0.45963 0.59598 0.37212 0.06941  0.02810  0.02847  55  PHE A CB  
431  C CG  . PHE A 60  ? 0.44041 0.57440 0.33661 0.07491  0.03890  0.06550  55  PHE A CG  
432  C CD1 . PHE A 60  ? 0.46739 0.62284 0.33119 0.09865  0.04191  0.08084  55  PHE A CD1 
433  C CD2 . PHE A 60  ? 0.43243 0.54597 0.34949 0.05700  0.04721  0.08342  55  PHE A CD2 
434  C CE1 . PHE A 60  ? 0.50832 0.66512 0.36502 0.10045  0.05910  0.11997  55  PHE A CE1 
435  C CE2 . PHE A 60  ? 0.48438 0.59589 0.40271 0.05610  0.05964  0.11680  55  PHE A CE2 
436  C CZ  . PHE A 60  ? 0.52227 0.65595 0.41182 0.07656  0.06863  0.13892  55  PHE A CZ  
437  N N   . ASP A 61  ? 0.41328 0.51203 0.35487 0.02166  0.04895  0.02645  56  ASP A N   
438  C CA  . ASP A 61  ? 0.41746 0.50518 0.36161 0.00921  0.05508  0.03511  56  ASP A CA  
439  C C   . ASP A 61  ? 0.43726 0.52132 0.36764 0.00718  0.06105  0.03592  56  ASP A C   
440  O O   . ASP A 61  ? 0.44423 0.53281 0.37163 0.00670  0.06161  0.04672  56  ASP A O   
441  C CB  . ASP A 61  ? 0.39009 0.47006 0.34776 0.00096  0.05592  0.02196  56  ASP A CB  
442  C CG  . ASP A 61  ? 0.64154 0.71510 0.60144 -0.00569 0.05506  0.02456  56  ASP A CG  
443  O OD1 . ASP A 61  ? 0.61236 0.68943 0.57438 -0.00717 0.05279  0.03724  56  ASP A OD1 
444  O OD2 . ASP A 61  ? 0.63293 0.70360 0.59585 -0.00798 0.05601  0.01040  56  ASP A OD2 
445  N N   . VAL A 62  ? 0.42297 0.49836 0.35059 0.00661  0.06496  0.02390  57  VAL A N   
446  C CA  . VAL A 62  ? 0.44525 0.50699 0.35825 0.00868  0.07091  0.02810  57  VAL A CA  
447  C C   . VAL A 62  ? 0.47268 0.54807 0.37498 0.02266  0.06651  0.03563  57  VAL A C   
448  O O   . VAL A 62  ? 0.45061 0.53056 0.34524 0.02708  0.06732  0.04595  57  VAL A O   
449  C CB  . VAL A 62  ? 0.47069 0.51194 0.39233 0.00344  0.07814  0.01545  57  VAL A CB  
450  C CG1 . VAL A 62  ? 0.54124 0.55874 0.44570 0.01092  0.08341  0.02367  57  VAL A CG1 
451  C CG2 . VAL A 62  ? 0.45455 0.48881 0.38926 -0.01105 0.09048  0.01283  57  VAL A CG2 
452  N N   . LEU A 63  ? 0.45595 0.54505 0.35719 0.03351  0.06131  0.02851  58  LEU A N   
453  C CA  . LEU A 63  ? 0.41019 0.51980 0.29775 0.05095  0.06122  0.03536  58  LEU A CA  
454  C C   . LEU A 63  ? 0.45371 0.58532 0.34775 0.04806  0.06653  0.05884  58  LEU A C   
455  O O   . LEU A 63  ? 0.44933 0.60014 0.34319 0.05577  0.07110  0.06757  58  LEU A O   
456  C CB  . LEU A 63  ? 0.42509 0.55163 0.30219 0.06849  0.05394  0.02201  58  LEU A CB  
457  C CG  . LEU A 63  ? 0.44235 0.55335 0.32810 0.06985  0.04433  -0.01058 58  LEU A CG  
458  C CD1 . LEU A 63  ? 0.46951 0.60887 0.33973 0.09561  0.03075  -0.03053 58  LEU A CD1 
459  C CD2 . LEU A 63  ? 0.51633 0.59979 0.40364 0.06963  0.04828  -0.01811 58  LEU A CD2 
460  N N   . ALA A 64  ? 0.41796 0.54829 0.32504 0.03736  0.06615  0.06767  59  ALA A N   
461  C CA  . ALA A 64  ? 0.41453 0.55907 0.34128 0.02970  0.07208  0.08878  59  ALA A CA  
462  C C   . ALA A 64  ? 0.42481 0.57156 0.36845 0.01882  0.06965  0.08509  59  ALA A C   
463  O O   . ALA A 64  ? 0.44788 0.62061 0.41150 0.01747  0.07400  0.09535  59  ALA A O   
464  C CB  . ALA A 64  ? 0.42194 0.55191 0.36265 0.02156  0.06999  0.09575  59  ALA A CB  
465  N N   . THR A 65  ? 0.40493 0.53055 0.34104 0.01362  0.06321  0.07003  60  THR A N   
466  C CA  . THR A 65  ? 0.46063 0.59108 0.40049 0.01156  0.05729  0.06444  60  THR A CA  
467  C C   . THR A 65  ? 0.47692 0.62317 0.40635 0.02692  0.05789  0.06737  60  THR A C   
468  O O   . THR A 65  ? 0.44533 0.62006 0.39440 0.02872  0.05291  0.06821  60  THR A O   
469  C CB  . THR A 65  ? 0.44172 0.54769 0.36201 0.00979  0.05540  0.05256  60  THR A CB  
470  O OG1 . THR A 65  ? 0.43656 0.53326 0.36992 -0.00048 0.05449  0.04617  60  THR A OG1 
471  C CG2 . THR A 65  ? 0.46202 0.57723 0.37523 0.01511  0.04646  0.04628  60  THR A CG2 
472  N N   . LEU A 66  ? 0.46606 0.59564 0.37117 0.03920  0.06221  0.06514  61  LEU A N   
473  C CA  . LEU A 66  ? 0.44195 0.58123 0.33717 0.05877  0.06207  0.06556  61  LEU A CA  
474  C C   . LEU A 66  ? 0.50813 0.69347 0.42476 0.06478  0.06656  0.07342  61  LEU A C   
475  O O   . LEU A 66  ? 0.47540 0.69056 0.40579 0.07440  0.06379  0.07436  61  LEU A O   
476  C CB  . LEU A 66  ? 0.46902 0.57704 0.34369 0.06925  0.06501  0.05666  61  LEU A CB  
477  C CG  . LEU A 66  ? 0.51746 0.58020 0.37840 0.06288  0.06748  0.05443  61  LEU A CG  
478  C CD1 . LEU A 66  ? 0.56872 0.59927 0.42853 0.06550  0.07076  0.04170  61  LEU A CD1 
479  C CD2 . LEU A 66  ? 0.50792 0.56293 0.35145 0.07680  0.06480  0.06380  61  LEU A CD2 
480  N N   . ARG A 67  ? 0.45656 0.65264 0.37637 0.06186  0.07492  0.08057  62  ARG A N   
481  C CA  . ARG A 67  ? 0.51415 0.75588 0.44990 0.06940  0.08712  0.09471  62  ARG A CA  
482  C C   . ARG A 67  ? 0.52329 0.79521 0.50632 0.05193  0.08932  0.10486  62  ARG A C   
483  O O   . ARG A 67  ? 0.48265 0.79852 0.49039 0.05928  0.09485  0.10789  62  ARG A O   
484  C CB  . ARG A 67  ? 0.41303 0.65797 0.33496 0.07265  0.09696  0.10671  62  ARG A CB  
485  C CG  . ARG A 67  ? 0.45018 0.74315 0.38551 0.07983  0.11772  0.13124  62  ARG A CG  
486  C CD  . ARG A 67  ? 0.50224 0.83027 0.42086 0.10872  0.12350  0.12229  62  ARG A CD  
487  N NE  . ARG A 67  ? 0.54517 0.92858 0.47838 0.11649  0.14942  0.14812  62  ARG A NE  
488  C CZ  . ARG A 67  ? 0.52266 0.94545 0.50932 0.10179  0.16199  0.16181  62  ARG A CZ  
489  N NH1 . ARG A 67  ? 0.45802 0.87093 0.48169 0.08274  0.14511  0.14782  62  ARG A NH1 
490  N NH2 . ARG A 67  ? 0.52194 0.99829 0.52726 0.10698  0.19170  0.18858  62  ARG A NH2 
491  N N   . ARG A 68  ? 0.41378 0.66589 0.41693 0.02933  0.08355  0.10546  63  ARG A N   
492  C CA  . ARG A 68  ? 0.49435 0.77527 0.55479 0.01020  0.08421  0.10995  63  ARG A CA  
493  C C   . ARG A 68  ? 0.42396 0.72396 0.50019 0.01352  0.06564  0.08861  63  ARG A C   
494  O O   . ARG A 68  ? 0.42121 0.75511 0.55445 -0.00105 0.06123  0.08355  63  ARG A O   
495  C CB  . ARG A 68  ? 0.49892 0.75062 0.58256 -0.01279 0.08259  0.11406  63  ARG A CB  
496  C CG  . ARG A 68  ? 0.47488 0.69016 0.53871 -0.01582 0.06392  0.09150  63  ARG A CG  
497  C CD  . ARG A 68  ? 0.48475 0.67333 0.57546 -0.03383 0.06346  0.09464  63  ARG A CD  
498  N NE  . ARG A 68  ? 0.45480 0.60666 0.50919 -0.02844 0.05650  0.08316  63  ARG A NE  
499  C CZ  . ARG A 68  ? 0.48483 0.62474 0.52802 -0.02806 0.04253  0.05863  63  ARG A CZ  
500  N NH1 . ARG A 68  ? 0.44664 0.60641 0.50525 -0.02931 0.02927  0.04084  63  ARG A NH1 
501  N NH2 . ARG A 68  ? 0.46999 0.58429 0.48656 -0.02358 0.04198  0.05082  63  ARG A NH2 
502  N N   . SER A 69  ? 0.41223 0.69292 0.44266 0.03390  0.05477  0.07658  64  SER A N   
503  C CA  . SER A 69  ? 0.46363 0.76562 0.49807 0.04724  0.03684  0.06102  64  SER A CA  
504  C C   . SER A 69  ? 0.49392 0.84787 0.55153 0.06511  0.03998  0.06237  64  SER A C   
505  O O   . SER A 69  ? 0.46695 0.85347 0.54102 0.07805  0.02264  0.04823  64  SER A O   
506  C CB  . SER A 69  ? 0.50980 0.76656 0.48406 0.06530  0.02867  0.05591  64  SER A CB  
507  O OG  . SER A 69  ? 0.51601 0.75208 0.45746 0.08411  0.03827  0.06317  64  SER A OG  
508  N N   . GLY A 70  ? 0.50107 0.86918 0.55857 0.07063  0.06041  0.07661  65  GLY A N   
509  C CA  . GLY A 70  ? 0.50552 0.93014 0.58667 0.09019  0.06774  0.07710  65  GLY A CA  
510  C C   . GLY A 70  ? 0.48558 0.89075 0.51782 0.12702  0.06103  0.06842  65  GLY A C   
511  O O   . GLY A 70  ? 0.49538 0.84579 0.48348 0.13596  0.04812  0.06265  65  GLY A O   
512  N N   . ALA A 71  ? 0.48805 0.93855 0.53164 0.14937  0.07276  0.06869  66  ALA A N   
513  C CA  . ALA A 71  ? 0.51579 0.94769 0.52054 0.18805  0.06626  0.05727  66  ALA A CA  
514  C C   . ALA A 71  ? 0.56024 0.97180 0.55264 0.20539  0.04131  0.04799  66  ALA A C   
515  O O   . ALA A 71  ? 0.55404 1.01133 0.58525 0.20113  0.02859  0.04292  66  ALA A O   
516  C CB  . ALA A 71  ? 0.60471 1.10606 0.63462 0.21315  0.08104  0.05453  66  ALA A CB  
517  N N   . PRO A 72  ? 0.64800 0.99256 0.58873 0.22707  0.03355  0.04553  67  PRO A N   
518  C CA  . PRO A 72  ? 0.65984 0.95250 0.56589 0.23499  0.04326  0.04198  67  PRO A CA  
519  C C   . PRO A 72  ? 0.61790 0.85384 0.50262 0.20442  0.04839  0.04694  67  PRO A C   
520  O O   . PRO A 72  ? 0.64422 0.82587 0.50327 0.21096  0.04975  0.03931  67  PRO A O   
521  C CB  . PRO A 72  ? 0.71134 0.95652 0.58741 0.27110  0.03101  0.03720  67  PRO A CB  
522  C CG  . PRO A 72  ? 0.75605 0.99142 0.62355 0.26867  0.01675  0.04813  67  PRO A CG  
523  C CD  . PRO A 72  ? 0.73421 1.04898 0.64924 0.24830  0.01354  0.04580  67  PRO A CD  
524  N N   . TYR A 73  ? 0.54485 0.79407 0.44667 0.17271  0.04991  0.05572  68  TYR A N   
525  C CA  . TYR A 73  ? 0.55644 0.76483 0.44539 0.14575  0.05512  0.05874  68  TYR A CA  
526  C C   . TYR A 73  ? 0.62299 0.76357 0.47990 0.14694  0.05114  0.05836  68  TYR A C   
527  O O   . TYR A 73  ? 0.58936 0.68967 0.43521 0.13923  0.05653  0.05261  68  TYR A O   
528  C CB  . TYR A 73  ? 0.57381 0.78769 0.45871 0.14546  0.06599  0.05435  68  TYR A CB  
529  C CG  . TYR A 73  ? 0.58267 0.86236 0.48953 0.15415  0.07740  0.06022  68  TYR A CG  
530  C CD1 . TYR A 73  ? 0.57299 0.89362 0.51646 0.13222  0.08533  0.07620  68  TYR A CD1 
531  C CD2 . TYR A 73  ? 0.60987 0.91097 0.50442 0.18465  0.08260  0.04947  68  TYR A CD2 
532  C CE1 . TYR A 73  ? 0.52241 0.90540 0.49295 0.13732  0.10315  0.08783  68  TYR A CE1 
533  C CE2 . TYR A 73  ? 0.60526 0.97427 0.51839 0.19476  0.09925  0.05826  68  TYR A CE2 
534  C CZ  . TYR A 73  ? 0.53192 0.94211 0.48439 0.16938  0.11190  0.08064  68  TYR A CZ  
535  O OH  . TYR A 73  ? 0.57123 1.04999 0.54828 0.17680  0.13529  0.09505  68  TYR A OH  
536  N N   . ALA A 74  ? 0.58509 0.71682 0.42939 0.15765  0.04233  0.06486  69  ALA A N   
537  C CA  . ALA A 74  ? 0.66486 0.73314 0.47483 0.16251  0.04448  0.07382  69  ALA A CA  
538  C C   . ALA A 74  ? 0.64042 0.71569 0.43630 0.15719  0.03830  0.08200  69  ALA A C   
539  O O   . ALA A 74  ? 0.64726 0.76695 0.44998 0.17141  0.02310  0.07848  69  ALA A O   
540  C CB  . ALA A 74  ? 0.76792 0.80663 0.55828 0.19822  0.04066  0.07708  69  ALA A CB  
541  N N   . LEU A 75  ? 0.62969 0.66768 0.40914 0.13874  0.04909  0.08871  70  LEU A N   
542  C CA  . LEU A 75  ? 0.62650 0.67006 0.38378 0.13784  0.04538  0.09362  70  LEU A CA  
543  C C   . LEU A 75  ? 0.72230 0.70755 0.43894 0.14202  0.06337  0.11410  70  LEU A C   
544  O O   . LEU A 75  ? 0.71422 0.65624 0.43928 0.12778  0.08108  0.11907  70  LEU A O   
545  C CB  . LEU A 75  ? 0.64330 0.71368 0.42762 0.10861  0.04453  0.08030  70  LEU A CB  
546  C CG  . LEU A 75  ? 0.61697 0.74007 0.44766 0.09799  0.03266  0.06640  70  LEU A CG  
547  C CD1 . LEU A 75  ? 0.52955 0.65715 0.38443 0.07004  0.03579  0.05846  70  LEU A CD1 
548  C CD2 . LEU A 75  ? 0.58345 0.75083 0.42140 0.11547  0.01178  0.05741  70  LEU A CD2 
549  N N   . THR A 76  ? 0.78599 0.77459 0.46130 0.16142  0.05944  0.12480  71  THR A N   
550  C CA  . THR A 76  ? 0.85738 0.80068 0.49251 0.16208  0.08333  0.14870  71  THR A CA  
551  C C   . THR A 76  ? 0.85226 0.79910 0.51393 0.12607  0.09868  0.13799  71  THR A C   
552  O O   . THR A 76  ? 0.79002 0.77820 0.48333 0.11002  0.08468  0.11359  71  THR A O   
553  C CB  . THR A 76  ? 0.87268 0.83289 0.44963 0.19533  0.07429  0.15919  71  THR A CB  
554  O OG1 . THR A 76  ? 0.82573 0.84092 0.41509 0.18594  0.05713  0.13074  71  THR A OG1 
555  C CG2 . THR A 76  ? 0.85570 0.82960 0.41264 0.23574  0.05039  0.16242  71  THR A CG2 
556  N N   . PRO A 77  ? 0.97780 0.88200 0.63301 0.11311  0.12848  0.15643  72  PRO A N   
557  C CA  . PRO A 77  ? 0.94121 0.85843 0.62406 0.08334  0.14242  0.14395  72  PRO A CA  
558  C C   . PRO A 77  ? 0.82112 0.78198 0.48306 0.08991  0.13277  0.13056  72  PRO A C   
559  O O   . PRO A 77  ? 0.80742 0.79294 0.50212 0.06990  0.12962  0.10837  72  PRO A O   
560  C CB  . PRO A 77  ? 1.06105 0.92934 0.73862 0.07372  0.17977  0.17135  72  PRO A CB  
561  C CG  . PRO A 77  ? 1.11086 0.92790 0.77552 0.09053  0.18247  0.19319  72  PRO A CG  
562  C CD  . PRO A 77  ? 1.09266 0.93564 0.71963 0.12558  0.15277  0.19105  72  PRO A CD  
563  N N   . THR A 78  ? 0.87383 0.84533 0.48157 0.12157  0.12468  0.14006  73  THR A N   
564  C CA  . THR A 78  ? 0.91505 0.93092 0.50413 0.13179  0.10954  0.11767  73  THR A CA  
565  C C   . THR A 78  ? 0.76098 0.81696 0.39735 0.12207  0.07495  0.08224  73  THR A C   
566  O O   . THR A 78  ? 0.71753 0.79537 0.38185 0.10654  0.06803  0.05703  73  THR A O   
567  C CB  . THR A 78  ? 0.94070 0.96304 0.45525 0.17436  0.10532  0.13305  73  THR A CB  
568  O OG1 . THR A 78  ? 1.09849 1.07845 0.57785 0.17878  0.14337  0.17201  73  THR A OG1 
569  C CG2 . THR A 78  ? 0.87550 0.94794 0.36956 0.18929  0.08485  0.10030  73  THR A CG2 
570  N N   . ALA A 79  ? 0.69481 0.76027 0.34434 0.13186  0.05510  0.08131  74  ALA A N   
571  C CA  . ALA A 79  ? 0.67725 0.78056 0.38265 0.11790  0.03005  0.05443  74  ALA A CA  
572  C C   . ALA A 79  ? 0.65833 0.75157 0.41307 0.08413  0.04108  0.04983  74  ALA A C   
573  O O   . ALA A 79  ? 0.55019 0.66649 0.34593 0.06822  0.02858  0.02990  74  ALA A O   
574  C CB  . ALA A 79  ? 0.72459 0.84265 0.44063 0.13393  0.01519  0.05869  74  ALA A CB  
575  N N   . LEU A 80  ? 0.67335 0.73108 0.42695 0.07464  0.06306  0.06727  75  LEU A N   
576  C CA  . LEU A 80  ? 0.64895 0.70172 0.44269 0.04941  0.07025  0.06067  75  LEU A CA  
577  C C   . LEU A 80  ? 0.60251 0.66307 0.40593 0.03723  0.07319  0.04651  75  LEU A C   
578  O O   . LEU A 80  ? 0.55618 0.62823 0.39555 0.02339  0.06542  0.03416  75  LEU A O   
579  C CB  . LEU A 80  ? 0.78734 0.80401 0.58000 0.04448  0.08927  0.07392  75  LEU A CB  
580  C CG  . LEU A 80  ? 0.72425 0.73734 0.55283 0.02846  0.09145  0.06530  75  LEU A CG  
581  C CD1 . LEU A 80  ? 0.52486 0.56474 0.37226 0.03180  0.07597  0.05977  75  LEU A CD1 
582  C CD2 . LEU A 80  ? 0.73708 0.71189 0.56429 0.02836  0.10581  0.07275  75  LEU A CD2 
583  N N   . TYR A 81  ? 0.66742 0.72211 0.43660 0.04599  0.08571  0.04978  76  TYR A N   
584  C CA  . TYR A 81  ? 0.65824 0.72616 0.43412 0.04054  0.08840  0.03207  76  TYR A CA  
585  C C   . TYR A 81  ? 0.62976 0.72437 0.41650 0.04646  0.06108  0.00588  76  TYR A C   
586  O O   . TYR A 81  ? 0.57886 0.67896 0.39876 0.03552  0.05411  -0.01321 76  TYR A O   
587  C CB  . TYR A 81  ? 0.60479 0.66729 0.33715 0.05240  0.11304  0.04350  76  TYR A CB  
588  C CG  . TYR A 81  ? 0.73077 0.81494 0.46842 0.05259  0.11524  0.02029  76  TYR A CG  
589  C CD1 . TYR A 81  ? 0.73812 0.82264 0.51348 0.03483  0.13051  0.01427  76  TYR A CD1 
590  C CD2 . TYR A 81  ? 0.75447 0.86296 0.46251 0.07407  0.09848  -0.00149 76  TYR A CD2 
591  C CE1 . TYR A 81  ? 0.73340 0.83970 0.51589 0.03946  0.13189  -0.00948 76  TYR A CE1 
592  C CE2 . TYR A 81  ? 0.76069 0.88803 0.47422 0.07818  0.09878  -0.02823 76  TYR A CE2 
593  C CZ  . TYR A 81  ? 0.78407 0.90926 0.53411 0.06146  0.11697  -0.03052 76  TYR A CZ  
594  O OH  . TYR A 81  ? 0.88604 1.03194 0.64277 0.07017  0.11697  -0.05930 76  TYR A OH  
595  N N   . ASP A 82  ? 0.59428 0.70530 0.35680 0.06557  0.04381  0.00194  77  ASP A N   
596  C CA  . ASP A 82  ? 0.60325 0.74304 0.38770 0.06931  0.01452  -0.03063 77  ASP A CA  
597  C C   . ASP A 82  ? 0.55083 0.69440 0.40279 0.04545  0.00196  -0.03719 77  ASP A C   
598  O O   . ASP A 82  ? 0.54803 0.69925 0.43867 0.03624  -0.01379 -0.06286 77  ASP A O   
599  C CB  . ASP A 82  ? 0.62890 0.79426 0.37780 0.09775  -0.00524 -0.03723 77  ASP A CB  
600  C CG  . ASP A 82  ? 0.72742 0.89601 0.40371 0.12778  0.00354  -0.03566 77  ASP A CG  
601  O OD1 . ASP A 82  ? 0.69357 0.85929 0.36106 0.12539  0.01640  -0.04633 77  ASP A OD1 
602  O OD2 . ASP A 82  ? 0.79518 0.97135 0.42100 0.15737  -0.00132 -0.02232 77  ASP A OD2 
603  N N   . ALA A 83  ? 0.51995 0.65677 0.38679 0.03695  0.01031  -0.01401 78  ALA A N   
604  C CA  . ALA A 83  ? 0.46665 0.61178 0.39033 0.01804  0.00465  -0.01272 78  ALA A CA  
605  C C   . ALA A 83  ? 0.48986 0.61159 0.43217 0.00219  0.01898  -0.00195 78  ALA A C   
606  O O   . ALA A 83  ? 0.49086 0.61534 0.47283 -0.01069 0.01890  0.00604  78  ALA A O   
607  C CB  . ALA A 83  ? 0.49410 0.65531 0.42214 0.02366  0.00554  0.00373  78  ALA A CB  
608  N N   . ALA A 84  ? 0.44629 0.54907 0.36269 0.00466  0.03209  -0.00044 79  ALA A N   
609  C CA  . ALA A 84  ? 0.48894 0.57701 0.42319 -0.00489 0.04104  0.00537  79  ALA A CA  
610  C C   . ALA A 84  ? 0.43595 0.51947 0.40763 -0.01262 0.03027  -0.00652 79  ALA A C   
611  O O   . ALA A 84  ? 0.48426 0.57165 0.46534 -0.01114 0.01757  -0.02847 79  ALA A O   
612  C CB  . ALA A 84  ? 0.54086 0.61941 0.45291 -0.00173 0.05611  0.00290  79  ALA A CB  
613  N N   . MET A 85  ? 0.40103 0.47411 0.39334 -0.01786 0.03409  0.00736  80  MET A N   
614  C CA  . MET A 85  ? 0.44152 0.49800 0.46777 -0.02226 0.02657  0.00156  80  MET A CA  
615  C C   . MET A 85  ? 0.43067 0.47946 0.45104 -0.01406 0.02394  -0.02251 80  MET A C   
616  O O   . MET A 85  ? 0.46482 0.50098 0.50962 -0.01386 0.01243  -0.04192 80  MET A O   
617  C CB  . MET A 85  ? 0.46053 0.50673 0.49664 -0.02155 0.03332  0.02784  80  MET A CB  
618  C CG  . MET A 85  ? 0.46898 0.48770 0.53567 -0.02145 0.02800  0.02986  80  MET A CG  
619  S SD  . MET A 85  ? 0.56512 0.56969 0.68758 -0.04077 0.02273  0.03331  80  MET A SD  
620  C CE  . MET A 85  ? 0.51480 0.53610 0.63992 -0.04640 0.04163  0.07791  80  MET A CE  
621  N N   . ILE A 86  ? 0.49116 0.54880 0.48594 -0.00748 0.03536  -0.02368 81  ILE A N   
622  C CA  . ILE A 86  ? 0.53810 0.59907 0.53246 0.00101  0.03901  -0.04367 81  ILE A CA  
623  C C   . ILE A 86  ? 0.53022 0.60842 0.49192 0.00391  0.05426  -0.04842 81  ILE A C   
624  O O   . ILE A 86  ? 0.53109 0.61146 0.47689 -0.00085 0.06573  -0.03137 81  ILE A O   
625  C CB  . ILE A 86  ? 0.55043 0.61151 0.55946 0.00557  0.04177  -0.03791 81  ILE A CB  
626  C CG1 . ILE A 86  ? 0.52356 0.56231 0.55507 0.00871  0.02964  -0.02483 81  ILE A CG1 
627  C CG2 . ILE A 86  ? 0.61394 0.69024 0.63043 0.01481  0.04784  -0.06102 81  ILE A CG2 
628  C CD1 . ILE A 86  ? 0.57292 0.58902 0.62875 0.01092  0.01792  -0.04073 81  ILE A CD1 
629  N N   . SER A 87  ? 0.54488 0.63316 0.49547 0.01405  0.05601  -0.07047 82  SER A N   
630  C CA  . SER A 87  ? 0.53754 0.64207 0.44935 0.02066  0.07556  -0.06842 82  SER A CA  
631  C C   . SER A 87  ? 0.54656 0.66405 0.46820 0.01695  0.10077  -0.06400 82  SER A C   
632  O O   . SER A 87  ? 0.55652 0.69404 0.46402 0.02589  0.11931  -0.07304 82  SER A O   
633  C CB  . SER A 87  ? 0.56288 0.68092 0.45060 0.03861  0.06821  -0.09503 82  SER A CB  
634  O OG  . SER A 87  ? 0.57352 0.69904 0.48213 0.04797  0.06630  -0.12223 82  SER A OG  
635  N N   . SER A 88  ? 0.51287 0.62476 0.46137 0.00482  0.10217  -0.05229 83  SER A N   
636  C CA  . SER A 88  ? 0.56937 0.69904 0.54353 -0.00211 0.12202  -0.05417 83  SER A CA  
637  C C   . SER A 88  ? 0.61208 0.73688 0.56892 -0.01236 0.14862  -0.03374 83  SER A C   
638  O O   . SER A 88  ? 0.62084 0.72413 0.54545 -0.01190 0.14667  -0.01566 83  SER A O   
639  C CB  . SER A 88  ? 0.58423 0.71392 0.59442 -0.00648 0.10713  -0.05657 83  SER A CB  
640  O OG  . SER A 88  ? 0.55662 0.66680 0.55372 -0.01244 0.09930  -0.03916 83  SER A OG  
641  N N   . GLY A 89  ? 0.58975 0.73431 0.57490 -0.02155 0.17446  -0.03605 84  GLY A N   
642  C CA  . GLY A 89  ? 0.68294 0.81854 0.65925 -0.03293 0.20778  -0.01320 84  GLY A CA  
643  C C   . GLY A 89  ? 0.66244 0.78124 0.67741 -0.05297 0.20962  -0.00790 84  GLY A C   
644  O O   . GLY A 89  ? 0.56924 0.68082 0.59828 -0.05299 0.18158  -0.01826 84  GLY A O   
645  N N   . SER A 90  ? 0.66865 0.78018 0.70083 -0.06897 0.24477  0.00867  85  SER A N   
646  C CA  . SER A 90  ? 0.67272 0.76320 0.75121 -0.09057 0.24935  0.00933  85  SER A CA  
647  C C   . SER A 90  ? 0.71358 0.76273 0.75891 -0.08304 0.22557  0.01845  85  SER A C   
648  O O   . SER A 90  ? 0.80433 0.84517 0.88434 -0.09098 0.20888  0.00232  85  SER A O   
649  C CB  . SER A 90  ? 0.64637 0.77422 0.79942 -0.10194 0.23376  -0.02720 85  SER A CB  
650  O OG  . SER A 90  ? 0.69544 0.86519 0.89559 -0.11265 0.26200  -0.03574 85  SER A OG  
651  N N   . MET A 91  ? 0.79434 0.73188 0.52328 -0.09399 0.23331  -0.02686 86  MET A N   
652  C CA  . MET A 91  ? 0.88918 0.79732 0.58072 -0.06335 0.21348  0.00658  86  MET A CA  
653  C C   . MET A 91  ? 0.90254 0.74732 0.56236 -0.06512 0.22889  0.02503  86  MET A C   
654  O O   . MET A 91  ? 0.88690 0.70748 0.54347 -0.04391 0.21489  0.03457  86  MET A O   
655  C CB  . MET A 91  ? 0.98582 0.90925 0.63318 -0.05105 0.20797  0.03419  86  MET A CB  
656  C CG  . MET A 91  ? 0.91305 0.81379 0.52434 -0.01956 0.19115  0.06806  86  MET A CG  
657  S SD  . MET A 91  ? 0.88752 0.81258 0.53254 0.00504  0.15973  0.05446  86  MET A SD  
658  C CE  . MET A 91  ? 0.94668 0.93109 0.59647 0.00210  0.15193  0.04454  86  MET A CE  
659  N N   . THR A 92  ? 0.94255 0.75493 0.57680 -0.09270 0.26132  0.02845  87  THR A N   
660  C CA  . THR A 92  ? 1.02001 0.75972 0.62234 -0.09633 0.28123  0.04529  87  THR A CA  
661  C C   . THR A 92  ? 1.03172 0.76795 0.68228 -0.10702 0.28186  0.01043  87  THR A C   
662  O O   . THR A 92  ? 1.08108 0.77161 0.71993 -0.09462 0.28197  0.01983  87  THR A O   
663  C CB  . THR A 92  ? 1.15516 0.85263 0.71118 -0.12885 0.31959  0.05690  87  THR A CB  
664  O OG1 . THR A 92  ? 1.16990 0.88939 0.69403 -0.11592 0.30282  0.08659  87  THR A OG1 
665  C CG2 . THR A 92  ? 1.22429 0.83224 0.74248 -0.12955 0.34162  0.07855  87  THR A CG2 
666  N N   . ASN A 93  ? 0.90979 0.69892 0.61801 -0.12936 0.28137  -0.03229 88  ASN A N   
667  C CA  . ASN A 93  ? 0.87913 0.68050 0.63570 -0.13960 0.27557  -0.06758 88  ASN A CA  
668  C C   . ASN A 93  ? 0.88405 0.69629 0.64946 -0.10706 0.23814  -0.06171 88  ASN A C   
669  O O   . ASN A 93  ? 0.90888 0.69586 0.67574 -0.10960 0.23792  -0.07062 88  ASN A O   
670  C CB  . ASN A 93  ? 0.82510 0.69517 0.65009 -0.16225 0.27508  -0.11361 88  ASN A CB  
671  N N   . ARG A 94  ? 0.78935 0.63749 0.55772 -0.08090 0.20968  -0.04975 89  ARG A N   
672  C CA  . ARG A 94  ? 0.74670 0.60161 0.51577 -0.05470 0.17750  -0.04440 89  ARG A CA  
673  C C   . ARG A 94  ? 0.82471 0.62426 0.54857 -0.03930 0.18438  -0.01750 89  ARG A C   
674  O O   . ARG A 94  ? 0.80882 0.59602 0.53508 -0.03491 0.17436  -0.02611 89  ARG A O   
675  C CB  . ARG A 94  ? 0.76871 0.66358 0.54319 -0.03429 0.15323  -0.03675 89  ARG A CB  
676  C CG  . ARG A 94  ? 0.74696 0.69400 0.57753 -0.04083 0.13989  -0.06677 89  ARG A CG  
677  C CD  . ARG A 94  ? 0.62866 0.60196 0.46108 -0.02208 0.12166  -0.05951 89  ARG A CD  
678  N NE  . ARG A 94  ? 0.63721 0.62079 0.45516 -0.03006 0.14281  -0.05209 89  ARG A NE  
679  C CZ  . ARG A 94  ? 0.69670 0.69240 0.49427 -0.01786 0.13631  -0.03894 89  ARG A CZ  
680  N NH1 . ARG A 94  ? 0.69327 0.68677 0.48274 0.00218  0.11215  -0.03155 89  ARG A NH1 
681  N NH2 . ARG A 94  ? 0.73686 0.74737 0.51798 -0.02991 0.15587  -0.03518 89  ARG A NH2 
682  N N   . ILE A 95  ? 0.82677 0.59419 0.50970 -0.03025 0.20087  0.01444  90  ILE A N   
683  C CA  . ILE A 95  ? 0.91730 0.63265 0.56609 -0.00922 0.20709  0.04034  90  ILE A CA  
684  C C   . ILE A 95  ? 0.99721 0.65739 0.64688 -0.02770 0.23236  0.02634  90  ILE A C   
685  O O   . ILE A 95  ? 0.96415 0.59737 0.61183 -0.01685 0.23133  0.02358  90  ILE A O   
686  C CB  . ILE A 95  ? 0.95226 0.64747 0.55773 0.00700  0.21582  0.08024  90  ILE A CB  
687  C CG1 . ILE A 95  ? 0.92039 0.67366 0.52436 0.02702  0.18949  0.09052  90  ILE A CG1 
688  C CG2 . ILE A 95  ? 0.99830 0.62838 0.57490 0.02963  0.22798  0.10729  90  ILE A CG2 
689  C CD1 . ILE A 95  ? 1.01411 0.77157 0.57877 0.03227  0.19490  0.12179  90  ILE A CD1 
690  N N   . ASP A 96  ? 0.93215 0.57621 0.58598 -0.06029 0.25909  0.01221  91  ASP A N   
691  C CA  . ASP A 96  ? 1.04707 0.64141 0.70414 -0.08635 0.28798  -0.00868 91  ASP A CA  
692  C C   . ASP A 96  ? 1.02157 0.64876 0.71557 -0.09362 0.26932  -0.04508 91  ASP A C   
693  O O   . ASP A 96  ? 1.03565 0.62044 0.72080 -0.09412 0.28055  -0.05129 91  ASP A O   
694  C CB  . ASP A 96  ? 1.13471 0.72480 0.79816 -0.12736 0.31885  -0.02765 91  ASP A CB  
695  C CG  . ASP A 96  ? 1.27581 0.80260 0.88332 -0.12885 0.34831  0.01012  91  ASP A CG  
696  O OD1 . ASP A 96  ? 1.33810 0.80681 0.90519 -0.09896 0.35024  0.04847  91  ASP A OD1 
697  O OD2 . ASP A 96  ? 1.39314 0.92853 0.99641 -0.15937 0.36933  0.00161  91  ASP A OD2 
698  N N   . ARG A 97  ? 0.95025 0.65177 0.68440 -0.09927 0.24084  -0.06947 92  ARG A N   
699  C CA  . ARG A 97  ? 0.93929 0.67816 0.70207 -0.10510 0.21586  -0.09991 92  ARG A CA  
700  C C   . ARG A 97  ? 0.95229 0.67230 0.68887 -0.07943 0.19930  -0.08429 92  ARG A C   
701  O O   . ARG A 97  ? 0.96414 0.66672 0.69754 -0.09101 0.20333  -0.10327 92  ARG A O   
702  C CB  . ARG A 97  ? 0.93739 0.75419 0.74332 -0.10304 0.18249  -0.11683 92  ARG A CB  
703  C CG  . ARG A 97  ? 0.98318 0.84782 0.83751 -0.13040 0.17421  -0.16076 92  ARG A CG  
704  C CD  . ARG A 97  ? 1.03838 0.91001 0.88669 -0.13102 0.15077  -0.17438 92  ARG A CD  
705  N NE  . ARG A 97  ? 1.00869 0.89824 0.84195 -0.10017 0.11159  -0.15424 92  ARG A NE  
706  C CZ  . ARG A 97  ? 0.97696 0.87248 0.79342 -0.09916 0.08731  -0.16063 92  ARG A CZ  
707  N NH1 . ARG A 97  ? 0.94058 0.84451 0.73634 -0.07480 0.05646  -0.14093 92  ARG A NH1 
708  N NH2 . ARG A 97  ? 1.02944 0.92060 0.84531 -0.12699 0.09683  -0.18876 92  ARG A NH2 
709  N N   . LEU A 98  ? 0.91490 0.64239 0.63331 -0.04833 0.18316  -0.05414 93  LEU A N   
710  C CA  . LEU A 98  ? 0.89434 0.61144 0.59144 -0.02561 0.16998  -0.04260 93  LEU A CA  
711  C C   . LEU A 98  ? 0.96946 0.62106 0.64565 -0.02129 0.19994  -0.03545 93  LEU A C   
712  O O   . LEU A 98  ? 0.95395 0.59453 0.62251 -0.01551 0.19732  -0.04367 93  LEU A O   
713  C CB  . LEU A 98  ? 0.89457 0.63583 0.57951 0.00245  0.15312  -0.01511 93  LEU A CB  
714  C CG  . LEU A 98  ? 0.85692 0.65453 0.56152 0.00191  0.12408  -0.02336 93  LEU A CG  
715  C CD1 . LEU A 98  ? 0.78325 0.60069 0.47484 0.02251  0.11671  -0.00010 93  LEU A CD1 
716  C CD2 . LEU A 98  ? 0.88652 0.70014 0.59180 -0.00077 0.09887  -0.04001 93  LEU A CD2 
717  N N   . GLU A 99  ? 1.07985 0.68315 0.74495 -0.02469 0.23069  -0.02067 94  GLU A N   
718  C CA  . GLU A 99  ? 1.07674 0.60575 0.72339 -0.01648 0.26167  -0.01082 94  GLU A CA  
719  C C   . GLU A 99  ? 1.14094 0.64306 0.79864 -0.05000 0.28299  -0.04960 94  GLU A C   
720  O O   . GLU A 99  ? 1.16612 0.63514 0.81966 -0.04471 0.29475  -0.05921 94  GLU A O   
721  C CB  . GLU A 99  ? 1.14511 0.62117 0.76694 -0.01038 0.28745  0.02173  94  GLU A CB  
722  C CG  . GLU A 99  ? 1.30083 0.72683 0.89987 0.03049  0.29504  0.05892  94  GLU A CG  
723  C CD  . GLU A 99  ? 1.45041 0.79351 1.01657 0.03160  0.32862  0.08881  94  GLU A CD  
724  O OE1 . GLU A 99  ? 1.45837 0.79664 1.01112 0.00244  0.34176  0.08888  94  GLU A OE1 
725  O OE2 . GLU A 99  ? 1.54051 0.82032 1.09395 0.06176  0.34331  0.11194  94  GLU A OE2 
726  N N   . LYS A 100 ? 1.13224 0.65384 0.80749 -0.08724 0.28989  -0.07697 95  LYS A N   
727  C CA  . LYS A 100 ? 1.14889 0.66010 0.83716 -0.12479 0.30772  -0.12014 95  LYS A CA  
728  C C   . LYS A 100 ? 1.08332 0.64375 0.77944 -0.12624 0.27630  -0.14366 95  LYS A C   
729  O O   . LYS A 100 ? 1.12383 0.66431 0.81787 -0.14914 0.29236  -0.17392 95  LYS A O   
730  C CB  . LYS A 100 ? 1.14076 0.68329 0.85461 -0.16460 0.31659  -0.14916 95  LYS A CB  
731  N N   . ALA A 101 ? 0.97919 0.59964 0.67926 -0.10541 0.23404  -0.13105 96  ALA A N   
732  C CA  . ALA A 101 ? 0.97822 0.63746 0.67300 -0.10651 0.20323  -0.14667 96  ALA A CA  
733  C C   . ALA A 101 ? 1.01676 0.64065 0.68616 -0.08547 0.21151  -0.13527 96  ALA A C   
734  O O   . ALA A 101 ? 1.01085 0.65303 0.66693 -0.09489 0.19677  -0.15334 96  ALA A O   
735  C CB  . ALA A 101 ? 0.93229 0.65680 0.63723 -0.09231 0.15871  -0.13591 96  ALA A CB  
736  N N   . GLY A 102 ? 0.99496 0.57188 0.65734 -0.05776 0.23413  -0.10682 97  GLY A N   
737  C CA  . GLY A 102 ? 0.98290 0.53012 0.63380 -0.03491 0.24559  -0.10007 97  GLY A CA  
738  C C   . GLY A 102 ? 0.89580 0.48199 0.53993 -0.00386 0.21810  -0.07735 97  GLY A C   
739  O O   . GLY A 102 ? 0.92826 0.50543 0.56806 0.01094  0.22492  -0.08022 97  GLY A O   
740  N N   . TRP A 103 ? 0.81517 0.44478 0.46126 0.00436  0.19134  -0.05876 98  TRP A N   
741  C CA  . TRP A 103 ? 0.75876 0.42910 0.39715 0.02585  0.16629  -0.04309 98  TRP A CA  
742  C C   . TRP A 103 ? 0.82285 0.49326 0.46254 0.05888  0.16992  -0.00968 98  TRP A C   
743  O O   . TRP A 103 ? 0.81914 0.51872 0.45482 0.07779  0.15791  -0.00119 98  TRP A O   
744  C CB  . TRP A 103 ? 0.77518 0.49365 0.41475 0.01307  0.13416  -0.04732 98  TRP A CB  
745  C CG  . TRP A 103 ? 0.86036 0.58828 0.49291 -0.01417 0.12137  -0.07557 98  TRP A CG  
746  C CD1 . TRP A 103 ? 0.91798 0.62966 0.53162 -0.02701 0.12935  -0.09556 98  TRP A CD1 
747  C CD2 . TRP A 103 ? 0.88229 0.64230 0.52651 -0.03283 0.09755  -0.08889 98  TRP A CD2 
748  N NE1 . TRP A 103 ? 0.92288 0.65448 0.52745 -0.05471 0.10994  -0.11796 98  TRP A NE1 
749  C CE2 . TRP A 103 ? 0.90445 0.66797 0.53032 -0.05581 0.08771  -0.11318 98  TRP A CE2 
750  C CE3 . TRP A 103 ? 0.89743 0.68790 0.56849 -0.03194 0.08328  -0.08466 98  TRP A CE3 
751  C CZ2 . TRP A 103 ? 1.03632 0.83563 0.66910 -0.07435 0.05904  -0.12945 98  TRP A CZ2 
752  C CZ3 . TRP A 103 ? 0.95238 0.77828 0.63943 -0.04819 0.05755  -0.10377 98  TRP A CZ3 
753  C CH2 . TRP A 103 ? 0.98483 0.81645 0.65229 -0.06743 0.04296  -0.12400 98  TRP A CH2 
754  N N   . VAL A 104 ? 0.85442 0.49628 0.49602 0.06316  0.18571  0.00852  99  VAL A N   
755  C CA  . VAL A 104 ? 0.86823 0.50390 0.50299 0.09478  0.18934  0.04336  99  VAL A CA  
756  C C   . VAL A 104 ? 0.96195 0.52480 0.59145 0.10259  0.22087  0.05617  99  VAL A C   
757  O O   . VAL A 104 ? 0.98133 0.50177 0.61294 0.07675  0.24263  0.03607  99  VAL A O   
758  C CB  . VAL A 104 ? 0.86962 0.54063 0.49833 0.09246  0.17580  0.06129  99  VAL A CB  
759  C CG1 . VAL A 104 ? 0.80071 0.53216 0.43641 0.08369  0.14860  0.04691  99  VAL A CG1 
760  C CG2 . VAL A 104 ? 0.86686 0.50823 0.49459 0.06622  0.19355  0.05761  99  VAL A CG2 
761  N N   . GLU A 105 ? 1.01222 0.56049 0.63383 0.13865  0.22299  0.09014  100 GLU A N   
762  C CA  . GLU A 105 ? 1.14711 0.61723 0.75530 0.15223  0.25056  0.11428  100 GLU A CA  
763  C C   . GLU A 105 ? 1.09802 0.57597 0.68139 0.17683  0.23938  0.15935  100 GLU A C   
764  O O   . GLU A 105 ? 1.00399 0.55069 0.58926 0.19310  0.21172  0.16944  100 GLU A O   
765  C CB  . GLU A 105 ? 1.17486 0.60190 0.80008 0.18002  0.26757  0.11052  100 GLU A CB  
766  C CG  . GLU A 105 ? 1.18579 0.66485 0.82872 0.22192  0.24577  0.12234  100 GLU A CG  
767  C CD  . GLU A 105 ? 1.33644 0.77945 1.00782 0.24632  0.26596  0.10803  100 GLU A CD  
768  O OE1 . GLU A 105 ? 1.40451 0.77134 1.07642 0.23251  0.29901  0.09414  100 GLU A OE1 
769  O OE2 . GLU A 105 ? 1.33110 0.82383 1.02738 0.27683  0.25181  0.10641  100 GLU A OE2 
770  N N   . ARG A 106 ? 1.24795 0.65374 0.80284 0.17536  0.26266  0.18531  101 ARG A N   
771  C CA  . ARG A 106 ? 1.30220 0.70438 0.82020 0.19523  0.25401  0.23219  101 ARG A CA  
772  C C   . ARG A 106 ? 1.31721 0.68029 0.83625 0.24456  0.25356  0.26451  101 ARG A C   
773  O O   . ARG A 106 ? 1.40848 0.69304 0.92890 0.24667  0.28051  0.26515  101 ARG A O   
774  C CB  . ARG A 106 ? 1.36335 0.71825 0.84648 0.15752  0.27757  0.23889  101 ARG A CB  
775  C CG  . ARG A 106 ? 1.30515 0.72508 0.79358 0.11674  0.26900  0.21284  101 ARG A CG  
776  C CD  . ARG A 106 ? 1.36672 0.76395 0.82295 0.08786  0.28422  0.22529  101 ARG A CD  
777  N NE  . ARG A 106 ? 1.31410 0.74785 0.77799 0.04338  0.29304  0.19443  101 ARG A NE  
778  C CZ  . ARG A 106 ? 1.31452 0.73565 0.80667 0.00771  0.31283  0.15395  101 ARG A CZ  
779  N NH1 . ARG A 106 ? 1.37495 0.73378 0.87423 0.00686  0.33376  0.14320  101 ARG A NH1 
780  N NH2 . ARG A 106 ? 1.27661 0.75173 0.79388 -0.02724 0.31203  0.12120  101 ARG A NH2 
781  N N   . ARG A 107 ? 1.31922 0.75297 0.84903 0.27963  0.22037  0.28249  102 ARG A N   
782  C CA  . ARG A 107 ? 1.43083 0.85659 0.97629 0.32673  0.21010  0.30795  102 ARG A CA  
783  C C   . ARG A 107 ? 1.53796 0.98300 1.05421 0.33151  0.18847  0.34438  102 ARG A C   
784  O O   . ARG A 107 ? 1.61252 1.02480 1.09231 0.29700  0.19955  0.35182  102 ARG A O   
785  C CB  . ARG A 107 ? 1.41509 0.91008 1.00074 0.36344  0.18942  0.29697  102 ARG A CB  
786  C CG  . ARG A 107 ? 1.44590 0.90010 1.06610 0.37103  0.21422  0.26489  102 ARG A CG  
787  C CD  . ARG A 107 ? 1.38351 0.93479 1.04148 0.36769  0.19500  0.22738  102 ARG A CD  
788  N NE  . ARG A 107 ? 1.38832 1.02024 1.06086 0.40750  0.16359  0.24726  102 ARG A NE  
789  C CZ  . ARG A 107 ? 1.31073 1.03075 1.01719 0.40915  0.14808  0.21744  102 ARG A CZ  
790  N NH1 . ARG A 107 ? 1.19196 0.92230 0.91379 0.37447  0.16034  0.17118  102 ARG A NH1 
791  N NH2 . ARG A 107 ? 1.33139 1.13005 1.05296 0.44314  0.12061  0.23339  102 ARG A NH2 
792  N N   . ALA A 108 ? 1.52436 1.02376 1.05605 0.37128  0.15803  0.36509  103 ALA A N   
793  C CA  . ALA A 108 ? 1.51878 1.02591 1.01929 0.37808  0.13611  0.40289  103 ALA A CA  
794  C C   . ALA A 108 ? 1.43010 1.04662 0.94341 0.39628  0.09581  0.40871  103 ALA A C   
795  O O   . ALA A 108 ? 1.38623 1.03744 0.93240 0.44069  0.07679  0.41733  103 ALA A O   
796  C CB  . ALA A 108 ? 1.63850 1.06560 1.13760 0.41165  0.14361  0.43271  103 ALA A CB  
797  N N   . THR A 116 ? 1.31622 0.93343 0.72668 0.28103  0.10292  0.41302  111 THR A N   
798  C CA  . THR A 116 ? 1.36555 0.95310 0.78958 0.25192  0.13354  0.37857  111 THR A CA  
799  C C   . THR A 116 ? 1.32335 0.98947 0.78436 0.24506  0.12412  0.34175  111 THR A C   
800  O O   . THR A 116 ? 1.23835 0.97115 0.69787 0.21834  0.11043  0.32778  111 THR A O   
801  C CB  . THR A 116 ? 1.40480 0.96078 0.79242 0.20035  0.15423  0.37442  111 THR A CB  
802  O OG1 . THR A 116 ? 1.50178 0.97425 0.84940 0.20121  0.16847  0.40725  111 THR A OG1 
803  C CG2 . THR A 116 ? 1.31555 0.84968 0.72281 0.17211  0.18299  0.33627  111 THR A CG2 
804  N N   . LEU A 117 ? 1.25215 0.90495 0.74401 0.26564  0.13386  0.32443  112 LEU A N   
805  C CA  . LEU A 117 ? 1.18386 0.90160 0.70436 0.26004  0.12570  0.29199  112 LEU A CA  
806  C C   . LEU A 117 ? 1.08438 0.75577 0.60726 0.23476  0.15177  0.26526  112 LEU A C   
807  O O   . LEU A 117 ? 1.17699 0.76461 0.68858 0.23017  0.17867  0.26921  112 LEU A O   
808  C CB  . LEU A 117 ? 1.20442 0.96066 0.75519 0.30535  0.11109  0.29298  112 LEU A CB  
809  C CG  . LEU A 117 ? 1.25031 1.06671 0.80539 0.33256  0.08220  0.31561  112 LEU A CG  
810  C CD1 . LEU A 117 ? 1.26142 1.10870 0.85483 0.38179  0.07268  0.31490  112 LEU A CD1 
811  C CD2 . LEU A 117 ? 1.16208 1.06520 0.71434 0.30198  0.06291  0.30028  112 LEU A CD2 
812  N N   . VAL A 118 ? 0.99238 0.71914 0.53017 0.21477  0.14375  0.23565  113 VAL A N   
813  C CA  . VAL A 118 ? 0.95611 0.66113 0.50699 0.19181  0.15814  0.20323  113 VAL A CA  
814  C C   . VAL A 118 ? 0.92884 0.68126 0.51171 0.20556  0.14329  0.17970  113 VAL A C   
815  O O   . VAL A 118 ? 0.88231 0.70403 0.46901 0.20981  0.12394  0.17645  113 VAL A O   
816  C CB  . VAL A 118 ? 0.93308 0.66495 0.48269 0.15097  0.15875  0.18209  113 VAL A CB  
817  C CG1 . VAL A 118 ? 0.90130 0.62456 0.47979 0.12660  0.16358  0.14355  113 VAL A CG1 
818  C CG2 . VAL A 118 ? 0.97990 0.67736 0.50362 0.13085  0.17446  0.19877  113 VAL A CG2 
819  N N   . ALA A 119 ? 0.92758 0.64221 0.53057 0.20838  0.15584  0.16059  114 ALA A N   
820  C CA  . ALA A 119 ? 0.86588 0.61676 0.49454 0.22114  0.14786  0.13871  114 ALA A CA  
821  C C   . ALA A 119 ? 0.89305 0.62596 0.53149 0.19116  0.15644  0.10122  114 ALA A C   
822  O O   . ALA A 119 ? 0.85474 0.53169 0.49040 0.17404  0.17472  0.09323  114 ALA A O   
823  C CB  . ALA A 119 ? 0.93008 0.65909 0.57603 0.26364  0.15506  0.15327  114 ALA A CB  
824  N N   . LEU A 120 ? 0.77299 0.55346 0.41865 0.18231  0.14385  0.07780  115 LEU A N   
825  C CA  . LEU A 120 ? 0.80303 0.56798 0.44934 0.15571  0.14888  0.04512  115 LEU A CA  
826  C C   . LEU A 120 ? 0.85028 0.56745 0.50976 0.16537  0.17264  0.03388  115 LEU A C   
827  O O   . LEU A 120 ? 0.86554 0.58045 0.54255 0.19892  0.18038  0.04493  115 LEU A O   
828  C CB  . LEU A 120 ? 0.83167 0.64626 0.47391 0.14577  0.13465  0.02588  115 LEU A CB  
829  C CG  . LEU A 120 ? 0.82039 0.67663 0.45002 0.13212  0.11461  0.02912  115 LEU A CG  
830  C CD1 . LEU A 120 ? 0.76631 0.65635 0.38772 0.12331  0.10882  0.01018  115 LEU A CD1 
831  C CD2 . LEU A 120 ? 0.76605 0.60304 0.38798 0.10655  0.10742  0.02361  115 LEU A CD2 
832  N N   . THR A 121 ? 0.86404 0.54489 0.51813 0.13654  0.18443  0.01041  116 THR A N   
833  C CA  . THR A 121 ? 0.89250 0.53689 0.55769 0.13589  0.20876  -0.01309 116 THR A CA  
834  C C   . THR A 121 ? 0.84811 0.53077 0.50839 0.12183  0.20215  -0.04172 116 THR A C   
835  O O   . THR A 121 ? 0.76596 0.49380 0.41012 0.11079  0.17893  -0.04126 116 THR A O   
836  C CB  . THR A 121 ? 0.92901 0.52126 0.58766 0.10515  0.22749  -0.03096 116 THR A CB  
837  O OG1 . THR A 121 ? 0.88981 0.51249 0.53143 0.06932  0.20712  -0.04889 116 THR A OG1 
838  C CG2 . THR A 121 ? 0.97032 0.52002 0.62795 0.11319  0.23893  -0.00388 116 THR A CG2 
839  N N   . SER A 122 ? 0.60065 0.70998 0.45080 0.19171  0.00043  -0.09743 117 SER A N   
840  C CA  . SER A 122 ? 0.60119 0.71526 0.42565 0.19469  0.01820  -0.10164 117 SER A CA  
841  C C   . SER A 122 ? 0.62076 0.71071 0.41269 0.18219  0.01052  -0.09946 117 SER A C   
842  O O   . SER A 122 ? 0.72165 0.82436 0.50512 0.17422  0.02488  -0.09218 117 SER A O   
843  C CB  . SER A 122 ? 0.75763 0.85361 0.55742 0.21729  0.02624  -0.11566 117 SER A CB  
844  O OG  . SER A 122 ? 0.86355 0.91403 0.63429 0.22142  0.00706  -0.12632 117 SER A OG  
845  N N   . ALA A 123 ? 0.65281 0.70767 0.43031 0.18053  -0.01227 -0.10587 118 ALA A N   
846  C CA  . ALA A 123 ? 0.61244 0.64505 0.36140 0.17188  -0.02510 -0.10657 118 ALA A CA  
847  C C   . ALA A 123 ? 0.66986 0.72243 0.44161 0.15166  -0.02590 -0.09082 118 ALA A C   
848  O O   . ALA A 123 ? 0.62345 0.67033 0.37103 0.14616  -0.02453 -0.08612 118 ALA A O   
849  C CB  . ALA A 123 ? 0.66501 0.66158 0.40928 0.17332  -0.05162 -0.12029 118 ALA A CB  
850  N N   . GLY A 124 ? 0.61566 0.68846 0.42970 0.14270  -0.02801 -0.08243 119 GLY A N   
851  C CA  . GLY A 124 ? 0.55994 0.64967 0.39478 0.12479  -0.02936 -0.06934 119 GLY A CA  
852  C C   . GLY A 124 ? 0.51575 0.63667 0.35703 0.11987  -0.00809 -0.06196 119 GLY A C   
853  O O   . GLY A 124 ? 0.51495 0.63898 0.35374 0.10695  -0.00533 -0.05366 119 GLY A O   
854  N N   . ARG A 125 ? 0.52187 0.66618 0.37637 0.13009  0.00781  -0.06566 120 ARG A N   
855  C CA  . ARG A 125 ? 0.49372 0.66812 0.36175 0.12523  0.03159  -0.06177 120 ARG A CA  
856  C C   . ARG A 125 ? 0.58204 0.73462 0.40743 0.12578  0.04643  -0.05926 120 ARG A C   
857  O O   . ARG A 125 ? 0.61556 0.77609 0.44431 0.11339  0.06043  -0.05011 120 ARG A O   
858  C CB  . ARG A 125 ? 0.52565 0.72841 0.41827 0.13913  0.04547  -0.06932 120 ARG A CB  
859  C CG  . ARG A 125 ? 0.54029 0.78227 0.46679 0.13182  0.06958  -0.06776 120 ARG A CG  
860  C CD  . ARG A 125 ? 0.73806 0.97693 0.64560 0.14280  0.09785  -0.07135 120 ARG A CD  
861  N NE  . ARG A 125 ? 0.82327 1.10478 0.77854 0.13622  0.12419  -0.07206 120 ARG A NE  
862  C CZ  . ARG A 125 ? 0.84938 1.16605 0.84428 0.14779  0.13528  -0.08182 120 ARG A CZ  
863  N NH1 . ARG A 125 ? 0.83767 1.14834 0.82374 0.16820  0.12302  -0.08995 120 ARG A NH1 
864  N NH2 . ARG A 125 ? 0.83472 1.19255 0.88226 0.13906  0.15909  -0.08437 120 ARG A NH2 
865  N N   . ALA A 126 ? 0.56745 0.68940 0.34926 0.14206  0.04442  -0.06756 121 ALA A N   
866  C CA  . ALA A 126 ? 0.60838 0.70426 0.33781 0.14815  0.05797  -0.06489 121 ALA A CA  
867  C C   . ALA A 126 ? 0.64449 0.72139 0.35604 0.13622  0.04320  -0.05626 121 ALA A C   
868  O O   . ALA A 126 ? 0.63424 0.70363 0.32257 0.13335  0.06107  -0.04575 121 ALA A O   
869  C CB  . ALA A 126 ? 0.66113 0.72387 0.34150 0.17053  0.05209  -0.07877 121 ALA A CB  
870  N N   . LEU A 127 ? 0.61553 0.68358 0.34005 0.12982  0.01287  -0.05978 122 LEU A N   
871  C CA  . LEU A 127 ? 0.64375 0.69502 0.35567 0.12056  -0.00368 -0.05368 122 LEU A CA  
872  C C   . LEU A 127 ? 0.57550 0.64901 0.31480 0.10266  0.01096  -0.03831 122 LEU A C   
873  O O   . LEU A 127 ? 0.64165 0.70053 0.35418 0.10043  0.01764  -0.02912 122 LEU A O   
874  C CB  . LEU A 127 ? 0.67330 0.71552 0.40742 0.11586  -0.03484 -0.06129 122 LEU A CB  
875  C CG  . LEU A 127 ? 0.66248 0.69369 0.39660 0.10557  -0.05278 -0.05593 122 LEU A CG  
876  C CD1 . LEU A 127 ? 0.77026 0.77155 0.44694 0.11915  -0.06004 -0.05980 122 LEU A CD1 
877  C CD2 . LEU A 127 ? 0.62085 0.64717 0.38952 0.09887  -0.07753 -0.06287 122 LEU A CD2 
878  N N   . ILE A 128 ? 0.50998 0.61660 0.30062 0.09157  0.01510  -0.03621 123 ILE A N   
879  C CA  . ILE A 128 ? 0.48567 0.61400 0.30702 0.07409  0.02532  -0.02569 123 ILE A CA  
880  C C   . ILE A 128 ? 0.53800 0.67560 0.35545 0.07231  0.05814  -0.01997 123 ILE A C   
881  O O   . ILE A 128 ? 0.52229 0.65850 0.34308 0.06010  0.06930  -0.00995 123 ILE A O   
882  C CB  . ILE A 128 ? 0.48357 0.64285 0.35525 0.06680  0.01739  -0.02796 123 ILE A CB  
883  C CG1 . ILE A 128 ? 0.43514 0.60964 0.33381 0.04909  0.01921  -0.02007 123 ILE A CG1 
884  C CG2 . ILE A 128 ? 0.51597 0.70445 0.41182 0.07490  0.03137  -0.03524 123 ILE A CG2 
885  C CD1 . ILE A 128 ? 0.46764 0.61594 0.34795 0.04221  0.00517  -0.01279 123 ILE A CD1 
886  N N   . ASP A 129 ? 0.55809 0.70267 0.36973 0.08456  0.07671  -0.02579 124 ASP A N   
887  C CA  . ASP A 129 ? 0.61413 0.76393 0.42303 0.08354  0.11358  -0.01956 124 ASP A CA  
888  C C   . ASP A 129 ? 0.67360 0.78115 0.42188 0.08871  0.12304  -0.00814 124 ASP A C   
889  O O   . ASP A 129 ? 0.69314 0.79794 0.44333 0.07971  0.15003  0.00367  124 ASP A O   
890  C CB  . ASP A 129 ? 0.61491 0.77652 0.42487 0.09912  0.13242  -0.02836 124 ASP A CB  
891  C CG  . ASP A 129 ? 0.65827 0.87016 0.53789 0.09339  0.13629  -0.03692 124 ASP A CG  
892  O OD1 . ASP A 129 ? 0.56833 0.80766 0.49526 0.07585  0.13499  -0.03527 124 ASP A OD1 
893  O OD2 . ASP A 129 ? 0.68995 0.91349 0.57588 0.10854  0.13981  -0.04674 124 ASP A OD2 
894  N N   . ASP A 130 ? 0.68080 0.75358 0.37517 0.10456  0.10050  -0.01246 125 ASP A N   
895  C CA  . ASP A 130 ? 0.78530 0.81587 0.41588 0.11431  0.10001  -0.00361 125 ASP A CA  
896  C C   . ASP A 130 ? 0.77101 0.79827 0.41556 0.09875  0.08481  0.00598  125 ASP A C   
897  O O   . ASP A 130 ? 0.72803 0.73722 0.35025 0.09652  0.10346  0.02054  125 ASP A O   
898  C CB  . ASP A 130 ? 0.85484 0.85483 0.43322 0.13611  0.07225  -0.01702 125 ASP A CB  
899  C CG  . ASP A 130 ? 1.05896 1.01336 0.55631 0.15668  0.07579  -0.01146 125 ASP A CG  
900  O OD1 . ASP A 130 ? 1.13076 1.07181 0.60885 0.15375  0.09781  0.00609  125 ASP A OD1 
901  O OD2 . ASP A 130 ? 1.08912 1.01842 0.53967 0.17767  0.05554  -0.02572 125 ASP A OD2 
902  N N   . ALA A 131 ? 0.62862 0.67031 0.30914 0.08905  0.05352  -0.00110 126 ALA A N   
903  C CA  . ALA A 131 ? 0.65617 0.69094 0.34493 0.07804  0.03650  0.00624  126 ALA A CA  
904  C C   . ALA A 131 ? 0.63729 0.69056 0.36287 0.05862  0.05904  0.01811  126 ALA A C   
905  O O   . ALA A 131 ? 0.65062 0.68678 0.36397 0.05386  0.05889  0.02883  126 ALA A O   
906  C CB  . ALA A 131 ? 0.64734 0.69291 0.36981 0.07232  0.00338  -0.00355 126 ALA A CB  
907  N N   . VAL A 132 ? 0.55917 0.64700 0.33176 0.04817  0.07693  0.01470  127 VAL A N   
908  C CA  . VAL A 132 ? 0.53549 0.64267 0.35050 0.02843  0.09333  0.02108  127 VAL A CA  
909  C C   . VAL A 132 ? 0.56196 0.64543 0.35048 0.02766  0.12680  0.03509  127 VAL A C   
910  O O   . VAL A 132 ? 0.59324 0.67221 0.39699 0.01382  0.13566  0.04381  127 VAL A O   
911  C CB  . VAL A 132 ? 0.48530 0.63777 0.36025 0.01948  0.10057  0.01041  127 VAL A CB  
912  C CG1 . VAL A 132 ? 0.52516 0.68778 0.40171 0.02677  0.13035  0.00763  127 VAL A CG1 
913  C CG2 . VAL A 132 ? 0.53441 0.70756 0.45678 -0.00100 0.10671  0.01156  127 VAL A CG2 
914  N N   . VAL A 133 ? 0.63682 0.70119 0.38338 0.04348  0.14804  0.03816  128 VAL A N   
915  C CA  . VAL A 133 ? 0.69097 0.72478 0.40347 0.04613  0.18450  0.05467  128 VAL A CA  
916  C C   . VAL A 133 ? 0.73501 0.72599 0.39293 0.05482  0.16881  0.06674  128 VAL A C   
917  O O   . VAL A 133 ? 0.78445 0.75777 0.44091 0.04634  0.18788  0.08118  128 VAL A O   
918  C CB  . VAL A 133 ? 0.77456 0.79477 0.44776 0.06500  0.21260  0.05546  128 VAL A CB  
919  C CG1 . VAL A 133 ? 0.85453 0.82900 0.47082 0.07491  0.25028  0.07597  128 VAL A CG1 
920  C CG2 . VAL A 133 ? 0.73151 0.79808 0.47109 0.05443  0.23468  0.04496  128 VAL A CG2 
921  N N   . ALA A 134 ? 0.72765 0.70251 0.34576 0.07165  0.13230  0.05944  129 ALA A N   
922  C CA  . ALA A 134 ? 0.81904 0.75905 0.39260 0.08184  0.11080  0.06728  129 ALA A CA  
923  C C   . ALA A 134 ? 0.74580 0.70118 0.36854 0.06102  0.09819  0.07038  129 ALA A C   
924  O O   . ALA A 134 ? 0.70034 0.62912 0.30088 0.06248  0.10153  0.08384  129 ALA A O   
925  C CB  . ALA A 134 ? 0.82393 0.75177 0.36157 0.10170  0.07042  0.05294  129 ALA A CB  
926  N N   . HIS A 135 ? 0.64757 0.64326 0.33344 0.04397  0.08459  0.05834  130 HIS A N   
927  C CA  . HIS A 135 ? 0.58639 0.59809 0.31803 0.02588  0.07207  0.05888  130 HIS A CA  
928  C C   . HIS A 135 ? 0.61506 0.62406 0.36643 0.01042  0.10303  0.07048  130 HIS A C   
929  O O   . HIS A 135 ? 0.62326 0.61698 0.37437 0.00538  0.09834  0.07862  130 HIS A O   
930  C CB  . HIS A 135 ? 0.51111 0.56282 0.29675 0.01521  0.05669  0.04447  130 HIS A CB  
931  C CG  . HIS A 135 ? 0.50987 0.57850 0.33941 -0.00144 0.04735  0.04403  130 HIS A CG  
932  N ND1 . HIS A 135 ? 0.52666 0.58022 0.35052 -0.00097 0.02709  0.04800  130 HIS A ND1 
933  C CD2 . HIS A 135 ? 0.53168 0.63137 0.41079 -0.01692 0.05421  0.03824  130 HIS A CD2 
934  C CE1 . HIS A 135 ? 0.55103 0.62327 0.41590 -0.01556 0.02489  0.04611  130 HIS A CE1 
935  N NE2 . HIS A 135 ? 0.46654 0.56577 0.36264 -0.02491 0.03993  0.03970  130 HIS A NE2 
936  N N   . VAL A 136 ? 0.59579 0.61908 0.36874 0.00258  0.13598  0.07047  131 VAL A N   
937  C CA  . VAL A 136 ? 0.65007 0.67258 0.45425 -0.01547 0.16583  0.07833  131 VAL A CA  
938  C C   . VAL A 136 ? 0.70616 0.67739 0.45428 -0.00526 0.18842  0.09916  131 VAL A C   
939  O O   . VAL A 136 ? 0.75017 0.70609 0.51026 -0.01642 0.19964  0.10837  131 VAL A O   
940  C CB  . VAL A 136 ? 0.63689 0.69374 0.49365 -0.02860 0.19466  0.06967  131 VAL A CB  
941  C CG1 . VAL A 136 ? 0.55171 0.65783 0.46750 -0.03907 0.16950  0.04988  131 VAL A CG1 
942  C CG2 . VAL A 136 ? 0.73742 0.78636 0.56083 -0.01239 0.21509  0.07180  131 VAL A CG2 
943  N N   . ASP A 137 ? 0.81717 0.75746 0.49891 0.01841  0.19497  0.10690  132 ASP A N   
944  C CA  . ASP A 137 ? 0.85919 0.74473 0.47440 0.03458  0.21137  0.12793  132 ASP A CA  
945  C C   . ASP A 137 ? 0.83433 0.70293 0.43268 0.04016  0.17635  0.13097  132 ASP A C   
946  O O   . ASP A 137 ? 0.87591 0.71221 0.45698 0.04041  0.19046  0.14709  132 ASP A O   
947  C CB  . ASP A 137 ? 0.94011 0.79311 0.47645 0.06450  0.21817  0.13335  132 ASP A CB  
948  C CG  . ASP A 137 ? 1.15614 0.95044 0.61624 0.08723  0.22438  0.15331  132 ASP A CG  
949  O OD1 . ASP A 137 ? 1.24024 1.01332 0.70518 0.08212  0.26083  0.16682  132 ASP A OD1 
950  O OD2 . ASP A 137 ? 1.16505 0.94186 0.58119 0.10767  0.18460  0.14976  132 ASP A OD2 
951  N N   . ASN A 138 ? 0.76086 0.64991 0.36691 0.04514  0.13237  0.11570  133 ASN A N   
952  C CA  . ASN A 138 ? 0.74422 0.62503 0.34850 0.04877  0.09882  0.11582  133 ASN A CA  
953  C C   . ASN A 138 ? 0.75968 0.65445 0.41982 0.02467  0.10656  0.11845  133 ASN A C   
954  O O   . ASN A 138 ? 0.75570 0.62540 0.40210 0.02833  0.10253  0.12905  133 ASN A O   
955  C CB  . ASN A 138 ? 0.68884 0.59449 0.30809 0.05358  0.05664  0.09707  133 ASN A CB  
956  C CG  . ASN A 138 ? 0.72065 0.61413 0.33020 0.06409  0.02085  0.09583  133 ASN A CG  
957  O OD1 . ASN A 138 ? 0.77250 0.62989 0.33476 0.08116  0.01941  0.10794  133 ASN A OD1 
958  N ND2 . ASN A 138 ? 0.67880 0.60166 0.33349 0.05590  -0.00771 0.08112  133 ASN A ND2 
959  N N   . GLN A 139 ? 0.72966 0.66352 0.45148 0.00207  0.11621  0.10756  134 GLN A N   
960  C CA  . GLN A 139 ? 0.70337 0.65108 0.47705 -0.01968 0.12127  0.10599  134 GLN A CA  
961  C C   . GLN A 139 ? 0.68574 0.60097 0.45080 -0.02583 0.15787  0.12209  134 GLN A C   
962  O O   . GLN A 139 ? 0.70611 0.60862 0.48479 -0.03356 0.15743  0.12690  134 GLN A O   
963  C CB  . GLN A 139 ? 0.59822 0.59373 0.43414 -0.03844 0.12217  0.08870  134 GLN A CB  
964  C CG  . GLN A 139 ? 0.54993 0.57392 0.40076 -0.03457 0.08807  0.07474  134 GLN A CG  
965  C CD  . GLN A 139 ? 0.59698 0.66220 0.50572 -0.05088 0.08567  0.05972  134 GLN A CD  
966  O OE1 . GLN A 139 ? 0.60309 0.68414 0.53004 -0.05201 0.06193  0.05211  134 GLN A OE1 
967  N NE2 . GLN A 139 ? 0.57876 0.66116 0.51728 -0.06212 0.11069  0.05486  134 GLN A NE2 
968  N N   . ARG A 140 ? 0.74345 0.64247 0.48724 -0.02236 0.19286  0.13106  135 ARG A N   
969  C CA  . ARG A 140 ? 0.80128 0.66433 0.53886 -0.02875 0.23299  0.14829  135 ARG A CA  
970  C C   . ARG A 140 ? 0.89684 0.70730 0.56929 -0.00728 0.22623  0.16772  135 ARG A C   
971  O O   . ARG A 140 ? 0.96167 0.74522 0.64025 -0.01447 0.24281  0.17907  135 ARG A O   
972  C CB  . ARG A 140 ? 0.93567 0.78978 0.66386 -0.02808 0.27712  0.15564  135 ARG A CB  
973  C CG  . ARG A 140 ? 0.94327 0.85114 0.74869 -0.05106 0.28807  0.13589  135 ARG A CG  
974  C CD  . ARG A 140 ? 1.01010 0.90868 0.81692 -0.05248 0.33865  0.14412  135 ARG A CD  
975  N NE  . ARG A 140 ? 1.08062 0.96181 0.81996 -0.02504 0.33842  0.15064  135 ARG A NE  
976  C CZ  . ARG A 140 ? 1.11200 1.02695 0.86469 -0.02153 0.33674  0.13747  135 ARG A CZ  
977  N NH1 . ARG A 140 ? 1.12486 1.09614 0.95908 -0.04244 0.32979  0.11622  135 ARG A NH1 
978  N NH2 . ARG A 140 ? 1.09988 0.99300 0.78547 0.00502  0.33641  0.14276  135 ARG A NH2 
979  N N   . ARG A 141 ? 0.83889 0.63407 0.44998 0.02047  0.19970  0.16997  136 ARG A N   
980  C CA  . ARG A 141 ? 0.89904 0.64888 0.44910 0.04506  0.18508  0.18503  136 ARG A CA  
981  C C   . ARG A 141 ? 0.91028 0.67464 0.49727 0.03732  0.15279  0.17789  136 ARG A C   
982  O O   . ARG A 141 ? 0.94755 0.67616 0.50793 0.04846  0.15199  0.19186  136 ARG A O   
983  C CB  . ARG A 141 ? 0.98381 0.71912 0.46486 0.07727  0.15940  0.18322  136 ARG A CB  
984  C CG  . ARG A 141 ? 1.05231 0.77083 0.49552 0.08853  0.18994  0.18826  136 ARG A CG  
985  N N   . VAL A 142 ? 0.82336 0.63727 0.46943 0.02019  0.12850  0.15741  137 VAL A N   
986  C CA  . VAL A 142 ? 0.72707 0.55616 0.41239 0.01146  0.10388  0.15051  137 VAL A CA  
987  C C   . VAL A 142 ? 0.75343 0.57254 0.47296 -0.00865 0.13136  0.15644  137 VAL A C   
988  O O   . VAL A 142 ? 0.84449 0.64582 0.56535 -0.00602 0.12360  0.16217  137 VAL A O   
989  C CB  . VAL A 142 ? 0.72755 0.60704 0.46147 -0.00002 0.07736  0.12923  137 VAL A CB  
990  C CG1 . VAL A 142 ? 0.66546 0.56316 0.44867 -0.01446 0.06456  0.12209  137 VAL A CG1 
991  C CG2 . VAL A 142 ? 0.74398 0.62725 0.44905 0.02051  0.04443  0.12235  137 VAL A CG2 
992  N N   . LEU A 143 ? 0.75420 0.58431 0.50504 -0.02852 0.16376  0.15366  138 LEU A N   
993  C CA  . LEU A 143 ? 0.82310 0.64928 0.61877 -0.05134 0.18840  0.15308  138 LEU A CA  
994  C C   . LEU A 143 ? 0.88463 0.65707 0.64926 -0.04802 0.22894  0.17542  138 LEU A C   
995  O O   . LEU A 143 ? 0.90383 0.66801 0.70844 -0.06840 0.25414  0.17474  138 LEU A O   
996  C CB  . LEU A 143 ? 0.80087 0.67248 0.65943 -0.07587 0.19908  0.13363  138 LEU A CB  
997  C CG  . LEU A 143 ? 0.68401 0.60473 0.57608 -0.08001 0.16272  0.11246  138 LEU A CG  
998  C CD1 . LEU A 143 ? 0.63287 0.59544 0.56990 -0.09463 0.17156  0.09562  138 LEU A CD1 
999  C CD2 . LEU A 143 ? 0.64768 0.57327 0.56998 -0.08941 0.14767  0.10466  138 LEU A CD2 
1000 N N   . SER A 144 ? 0.95306 0.68589 0.64609 -0.02183 0.23658  0.19470  139 SER A N   
1001 C CA  . SER A 144 ? 1.04452 0.73156 0.71149 -0.01646 0.27501  0.21276  139 SER A CA  
1002 C C   . SER A 144 ? 1.07308 0.72649 0.74355 -0.01646 0.27873  0.22149  139 SER A C   
1003 O O   . SER A 144 ? 1.15227 0.77971 0.83015 -0.02051 0.30956  0.22815  139 SER A O   
1004 C CB  . SER A 144 ? 1.06576 0.72522 0.65686 0.01662  0.27088  0.22408  139 SER A CB  
1005 O OG  . SER A 144 ? 1.10769 0.75830 0.65050 0.04220  0.23000  0.22625  139 SER A OG  
1006 N N   . ALA A 145 ? 1.09856 0.75053 0.76539 -0.01119 0.24957  0.22149  140 ALA A N   
1007 C CA  . ALA A 145 ? 1.15635 0.77762 0.82986 -0.01086 0.25347  0.22844  140 ALA A CA  
1008 C C   . ALA A 145 ? 1.19385 0.82871 0.94057 -0.04472 0.27732  0.21553  140 ALA A C   
1009 O O   . ALA A 145 ? 1.25714 0.86134 1.01153 -0.04675 0.29407  0.22087  140 ALA A O   
1010 C CB  . ALA A 145 ? 1.05546 0.67735 0.71623 0.00312  0.21528  0.22877  140 ALA A CB  
1011 N N   . LEU A 146 ? 1.04887 0.72995 0.85008 -0.06982 0.27710  0.19631  141 LEU A N   
1012 C CA  . LEU A 146 ? 0.96379 0.66645 0.83958 -0.10076 0.29178  0.17699  141 LEU A CA  
1013 C C   . LEU A 146 ? 1.01231 0.72372 0.91585 -0.11247 0.32265  0.17217  141 LEU A C   
1014 O O   . LEU A 146 ? 0.94172 0.66978 0.83017 -0.10670 0.32681  0.17368  141 LEU A O   
1015 C CB  . LEU A 146 ? 0.87462 0.63125 0.79917 -0.11730 0.26460  0.15196  141 LEU A CB  
1016 C CG  . LEU A 146 ? 0.81591 0.58586 0.72479 -0.10215 0.22135  0.14732  141 LEU A CG  
1017 C CD1 . LEU A 146 ? 0.77774 0.60590 0.73331 -0.11483 0.19481  0.12032  141 LEU A CD1 
1018 C CD2 . LEU A 146 ? 0.87178 0.60576 0.77900 -0.10016 0.22325  0.15388  141 LEU A CD2 
1019 N N   . SER A 147 ? 1.00941 0.70862 0.95501 -0.12811 0.34465  0.16561  142 SER A N   
1020 C CA  . SER A 147 ? 1.00793 0.71794 0.99369 -0.14193 0.37432  0.15794  142 SER A CA  
1021 C C   . SER A 147 ? 0.95441 0.72702 1.00580 -0.16375 0.36245  0.13021  142 SER A C   
1022 O O   . SER A 147 ? 0.85993 0.66448 0.92713 -0.16961 0.33336  0.11616  142 SER A O   
1023 C CB  . SER A 147 ? 1.04308 0.72320 1.06093 -0.15314 0.39933  0.15602  142 SER A CB  
1024 O OG  . SER A 147 ? 1.02161 0.72694 1.09868 -0.17444 0.38337  0.13147  142 SER A OG  
1025 N N   . ALA A 148 ? 0.94284 0.73275 1.03374 -0.17438 0.38564  0.12174  143 ALA A N   
1026 C CA  . ALA A 148 ? 0.92292 0.77420 1.07789 -0.19187 0.37314  0.09421  143 ALA A CA  
1027 C C   . ALA A 148 ? 0.91939 0.79611 1.13450 -0.21141 0.35289  0.06679  143 ALA A C   
1028 O O   . ALA A 148 ? 0.77516 0.69754 1.01661 -0.21742 0.32423  0.04643  143 ALA A O   
1029 C CB  . ALA A 148 ? 0.85576 0.71786 1.04673 -0.19867 0.40325  0.08997  143 ALA A CB  
1030 N N   . ALA A 149 ? 0.93296 0.77855 1.16692 -0.21946 0.36720  0.06523  144 ALA A N   
1031 C CA  . ALA A 149 ? 0.92284 0.78619 1.20703 -0.23547 0.34783  0.03836  144 ALA A CA  
1032 C C   . ALA A 149 ? 0.87683 0.73907 1.12836 -0.22798 0.31684  0.03953  144 ALA A C   
1033 O O   . ALA A 149 ? 0.80901 0.70756 1.09503 -0.23710 0.28986  0.01363  144 ALA A O   
1034 C CB  . ALA A 149 ? 0.97976 0.80373 1.28565 -0.24382 0.37299  0.03843  144 ALA A CB  
1035 N N   . GLU A 150 ? 0.89697 0.71706 1.08150 -0.20948 0.31962  0.06843  145 GLU A N   
1036 C CA  . GLU A 150 ? 0.82401 0.64154 0.97892 -0.20111 0.29216  0.07108  145 GLU A CA  
1037 C C   . GLU A 150 ? 0.75703 0.62076 0.91200 -0.19986 0.26824  0.06188  145 GLU A C   
1038 O O   . GLU A 150 ? 0.67241 0.55689 0.83203 -0.19909 0.23917  0.04829  145 GLU A O   
1039 C CB  . GLU A 150 ? 0.92788 0.69264 1.01139 -0.17792 0.29801  0.10380  145 GLU A CB  
1040 C CG  . GLU A 150 ? 1.04472 0.75918 1.11933 -0.17468 0.31843  0.11491  145 GLU A CG  
1041 C CD  . GLU A 150 ? 1.12201 0.78837 1.12146 -0.14645 0.32187  0.14711  145 GLU A CD  
1042 O OE1 . GLU A 150 ? 1.11546 0.77706 1.07384 -0.13159 0.32827  0.16298  145 GLU A OE1 
1043 O OE2 . GLU A 150 ? 1.17842 0.81245 1.15859 -0.13691 0.31610  0.15512  145 GLU A OE2 
1044 N N   . GLN A 151 ? 0.75362 0.63389 0.89786 -0.19479 0.27706  0.06877  146 GLN A N   
1045 C CA  . GLN A 151 ? 0.69004 0.61655 0.83230 -0.18899 0.25022  0.05830  146 GLN A CA  
1046 C C   . GLN A 151 ? 0.64823 0.62770 0.85696 -0.20596 0.23295  0.02364  146 GLN A C   
1047 O O   . GLN A 151 ? 0.65396 0.66182 0.85913 -0.19812 0.19731  0.01000  146 GLN A O   
1048 C CB  . GLN A 151 ? 0.75697 0.68509 0.87132 -0.17862 0.26632  0.07297  146 GLN A CB  
1049 C CG  . GLN A 151 ? 0.83306 0.71162 0.86925 -0.15455 0.27201  0.10417  146 GLN A CG  
1050 C CD  . GLN A 151 ? 0.82126 0.69821 0.82063 -0.14066 0.28556  0.11698  146 GLN A CD  
1051 O OE1 . GLN A 151 ? 0.79365 0.71407 0.81195 -0.14127 0.27303  0.10272  146 GLN A OE1 
1052 N NE2 . GLN A 151 ? 0.82361 0.64914 0.76580 -0.12429 0.30852  0.14307  146 GLN A NE2 
1053 N N   . ARG A 152 ? 0.64826 0.64053 0.91212 -0.22237 0.25119  0.00840  147 ARG A N   
1054 C CA  . ARG A 152 ? 0.66049 0.70086 0.98611 -0.23459 0.22963  -0.02736 147 ARG A CA  
1055 C C   . ARG A 152 ? 0.67117 0.70439 1.00259 -0.23874 0.20868  -0.04239 147 ARG A C   
1056 O O   . ARG A 152 ? 0.63416 0.70485 0.98381 -0.23906 0.17898  -0.06673 147 ARG A O   
1057 C CB  . ARG A 152 ? 0.65208 0.70055 1.03131 -0.24637 0.24903  -0.04045 147 ARG A CB  
1058 N N   . GLN A 153 ? 0.71802 0.70163 1.03057 -0.23945 0.22393  -0.02829 148 GLN A N   
1059 C CA  . GLN A 153 ? 0.74577 0.71524 1.05877 -0.24175 0.20797  -0.04011 148 GLN A CA  
1060 C C   . GLN A 153 ? 0.68253 0.66230 0.95031 -0.22330 0.17728  -0.03489 148 GLN A C   
1061 O O   . GLN A 153 ? 0.66157 0.66004 0.93607 -0.22017 0.15060  -0.05589 148 GLN A O   
1062 C CB  . GLN A 153 ? 0.86330 0.77357 1.15386 -0.24000 0.23186  -0.01937 148 GLN A CB  
1063 C CG  . GLN A 153 ? 0.93960 0.82951 1.24119 -0.24457 0.22341  -0.03382 148 GLN A CG  
1064 C CD  . GLN A 153 ? 1.08807 0.92185 1.37417 -0.24261 0.25094  -0.01401 148 GLN A CD  
1065 O OE1 . GLN A 153 ? 1.12224 0.94152 1.41302 -0.24448 0.27735  -0.00181 148 GLN A OE1 
1066 N NE2 . GLN A 153 ? 1.10681 0.90729 1.37286 -0.23710 0.24626  -0.01028 148 GLN A NE2 
1067 N N   . LEU A 154 ? 0.67289 0.63966 0.88841 -0.20548 0.17766  -0.00683 149 LEU A N   
1068 C CA  . LEU A 154 ? 0.60193 0.57890 0.77624 -0.18461 0.14730  -0.00073 149 LEU A CA  
1069 C C   . LEU A 154 ? 0.58113 0.60972 0.76994 -0.18100 0.12246  -0.02007 149 LEU A C   
1070 O O   . LEU A 154 ? 0.60707 0.64923 0.78331 -0.17025 0.09743  -0.02818 149 LEU A O   
1071 C CB  . LEU A 154 ? 0.62113 0.57182 0.74236 -0.16705 0.15225  0.03024  149 LEU A CB  
1072 C CG  . LEU A 154 ? 0.54933 0.51184 0.63608 -0.14681 0.12313  0.03673  149 LEU A CG  
1073 C CD1 . LEU A 154 ? 0.59541 0.55175 0.68365 -0.14303 0.10798  0.02941  149 LEU A CD1 
1074 C CD2 . LEU A 154 ? 0.60195 0.53598 0.64156 -0.13006 0.12686  0.06318  149 LEU A CD2 
1075 N N   . ALA A 155 ? 0.57202 0.62798 0.78699 -0.18835 0.13110  -0.02704 150 ALA A N   
1076 C CA  . ALA A 155 ? 0.54513 0.64945 0.77538 -0.18301 0.10764  -0.04593 150 ALA A CA  
1077 C C   . ALA A 155 ? 0.56596 0.69355 0.83128 -0.18917 0.08868  -0.07754 150 ALA A C   
1078 O O   . ALA A 155 ? 0.55431 0.70669 0.80759 -0.17566 0.06164  -0.08881 150 ALA A O   
1079 C CB  . ALA A 155 ? 0.50000 0.62881 0.75727 -0.18950 0.12321  -0.04825 150 ALA A CB  
1080 N N   . LYS A 156 ? 0.54737 0.66412 0.85377 -0.20801 0.10274  -0.09260 151 LYS A N   
1081 C CA  . LYS A 156 ? 0.56922 0.70665 0.90880 -0.21300 0.08212  -0.12704 151 LYS A CA  
1082 C C   . LYS A 156 ? 0.56333 0.68074 0.85998 -0.19800 0.06309  -0.12553 151 LYS A C   
1083 O O   . LYS A 156 ? 0.58967 0.73037 0.87936 -0.18608 0.03595  -0.14536 151 LYS A O   
1084 C CB  . LYS A 156 ? 0.55891 0.68652 0.95839 -0.23859 0.10308  -0.14534 151 LYS A CB  
1085 C CG  . LYS A 156 ? 0.62050 0.78810 1.07354 -0.24386 0.09948  -0.16809 151 LYS A CG  
1086 N N   . LEU A 157 ? 0.56736 0.64049 0.83365 -0.19622 0.07792  -0.10210 152 LEU A N   
1087 C CA  . LEU A 157 ? 0.59278 0.64756 0.82259 -0.18141 0.06340  -0.09969 152 LEU A CA  
1088 C C   . LEU A 157 ? 0.58096 0.65433 0.77178 -0.15963 0.04369  -0.08935 152 LEU A C   
1089 O O   . LEU A 157 ? 0.55345 0.63205 0.72568 -0.14642 0.02599  -0.09988 152 LEU A O   
1090 C CB  . LEU A 157 ? 0.57471 0.58075 0.78310 -0.18160 0.08312  -0.07519 152 LEU A CB  
1091 C CG  . LEU A 157 ? 0.65628 0.63297 0.89862 -0.20132 0.10507  -0.08392 152 LEU A CG  
1092 C CD1 . LEU A 157 ? 0.71546 0.64370 0.93133 -0.19838 0.12834  -0.05218 152 LEU A CD1 
1093 C CD2 . LEU A 157 ? 0.65648 0.62894 0.91190 -0.20312 0.09189  -0.11239 152 LEU A CD2 
1094 N N   . LEU A 158 ? 0.54862 0.62905 0.72523 -0.15477 0.04825  -0.06883 153 LEU A N   
1095 C CA  . LEU A 158 ? 0.52388 0.61956 0.66922 -0.13586 0.03156  -0.05972 153 LEU A CA  
1096 C C   . LEU A 158 ? 0.46962 0.60280 0.62528 -0.12949 0.01168  -0.08304 153 LEU A C   
1097 O O   . LEU A 158 ? 0.51751 0.65566 0.64597 -0.11220 -0.00327 -0.08302 153 LEU A O   
1098 C CB  . LEU A 158 ? 0.46937 0.56284 0.59895 -0.13220 0.03939  -0.03634 153 LEU A CB  
1099 C CG  . LEU A 158 ? 0.52566 0.58220 0.63024 -0.12837 0.05039  -0.01131 153 LEU A CG  
1100 C CD1 . LEU A 158 ? 0.54210 0.59704 0.63063 -0.12435 0.05660  0.00624  153 LEU A CD1 
1101 C CD2 . LEU A 158 ? 0.58799 0.63391 0.67003 -0.11383 0.03853  -0.00384 153 LEU A CD2 
1102 N N   . ASP A 159 ? 0.42713 0.58607 0.62304 -0.14179 0.01202  -0.10335 154 ASP A N   
1103 C CA  . ASP A 159 ? 0.48883 0.68527 0.69625 -0.13279 -0.01087 -0.12847 154 ASP A CA  
1104 C C   . ASP A 159 ? 0.55985 0.75144 0.75672 -0.12461 -0.02796 -0.14982 154 ASP A C   
1105 O O   . ASP A 159 ? 0.57920 0.78415 0.74924 -0.10422 -0.04825 -0.15774 154 ASP A O   
1106 C CB  . ASP A 159 ? 0.54033 0.76876 0.80374 -0.14835 -0.00714 -0.14869 154 ASP A CB  
1107 C CG  . ASP A 159 ? 0.60860 0.87920 0.88903 -0.13690 -0.03530 -0.17891 154 ASP A CG  
1108 O OD1 . ASP A 159 ? 0.63243 0.91239 0.87529 -0.11434 -0.05206 -0.17294 154 ASP A OD1 
1109 O OD2 . ASP A 159 ? 0.67843 0.97228 1.01168 -0.14958 -0.04083 -0.20930 154 ASP A OD2 
1110 N N   . LYS A 160 ? 0.53498 0.70323 0.74779 -0.13813 -0.01875 -0.15858 155 LYS A N   
1111 C CA  . LYS A 160 ? 0.59767 0.75748 0.79680 -0.12920 -0.03441 -0.18068 155 LYS A CA  
1112 C C   . LYS A 160 ? 0.58586 0.72299 0.72707 -0.10699 -0.03668 -0.16063 155 LYS A C   
1113 O O   . LYS A 160 ? 0.58080 0.72282 0.69261 -0.08728 -0.05438 -0.17401 155 LYS A O   
1114 C CB  . LYS A 160 ? 0.60644 0.74138 0.83678 -0.14934 -0.02115 -0.19329 155 LYS A CB  
1115 C CG  . LYS A 160 ? 0.69441 0.82939 0.92809 -0.14470 -0.04072 -0.22924 155 LYS A CG  
1116 C CD  . LYS A 160 ? 0.67426 0.78918 0.95542 -0.16972 -0.02672 -0.24678 155 LYS A CD  
1117 C CE  . LYS A 160 ? 0.66917 0.79298 0.96650 -0.16750 -0.05123 -0.29193 155 LYS A CE  
1118 N N   . LEU A 161 ? 0.52521 0.63728 0.65005 -0.10839 -0.01844 -0.12900 156 LEU A N   
1119 C CA  . LEU A 161 ? 0.51855 0.61238 0.60044 -0.08943 -0.01739 -0.10895 156 LEU A CA  
1120 C C   . LEU A 161 ? 0.55723 0.67210 0.61413 -0.07041 -0.03010 -0.10480 156 LEU A C   
1121 O O   . LEU A 161 ? 0.52885 0.63588 0.55133 -0.05075 -0.03554 -0.10472 156 LEU A O   
1122 C CB  . LEU A 161 ? 0.53733 0.60795 0.61656 -0.09481 0.00052  -0.07881 156 LEU A CB  
1123 C CG  . LEU A 161 ? 0.56850 0.62012 0.61869 -0.07903 0.00474  -0.05851 156 LEU A CG  
1124 C CD1 . LEU A 161 ? 0.59265 0.62275 0.63099 -0.07250 0.00692  -0.06902 156 LEU A CD1 
1125 C CD2 . LEU A 161 ? 0.57443 0.61016 0.62866 -0.08370 0.01635  -0.03305 156 LEU A CD2 
1126 N N   . LEU A 162 ? 0.51965 0.65778 0.59126 -0.07460 -0.03219 -0.09994 157 LEU A N   
1127 C CA  . LEU A 162 ? 0.55643 0.71189 0.60596 -0.05641 -0.04300 -0.09513 157 LEU A CA  
1128 C C   . LEU A 162 ? 0.64208 0.81354 0.67754 -0.03998 -0.06339 -0.12061 157 LEU A C   
1129 O O   . LEU A 162 ? 0.67206 0.83704 0.66772 -0.01702 -0.06877 -0.11457 157 LEU A O   
1130 C CB  . LEU A 162 ? 0.57674 0.75435 0.64819 -0.06441 -0.04147 -0.08923 157 LEU A CB  
1131 C CG  . LEU A 162 ? 0.63861 0.80245 0.69866 -0.06433 -0.02966 -0.06068 157 LEU A CG  
1132 C CD1 . LEU A 162 ? 0.63738 0.81884 0.71886 -0.07406 -0.02541 -0.05796 157 LEU A CD1 
1133 C CD2 . LEU A 162 ? 0.57639 0.73508 0.60417 -0.04365 -0.03444 -0.04869 157 LEU A CD2 
1134 N N   . GLN A 163 ? 0.66254 0.85413 0.73084 -0.05020 -0.07481 -0.14989 158 GLN A N   
1135 C CA  . GLN A 163 ? 0.70980 0.91878 0.76579 -0.03242 -0.09986 -0.17920 158 GLN A CA  
1136 C C   . GLN A 163 ? 0.78067 0.96023 0.79179 -0.01562 -0.10188 -0.18281 158 GLN A C   
1137 O O   . GLN A 163 ? 0.84552 1.02582 0.81463 0.01151  -0.11765 -0.19165 158 GLN A O   
1138 C CB  . GLN A 163 ? 0.75867 0.99600 0.87073 -0.04986 -0.11193 -0.21359 158 GLN A CB  
1139 C CG  . GLN A 163 ? 0.82713 1.09683 0.98470 -0.06330 -0.10852 -0.21241 158 GLN A CG  
1140 C CD  . GLN A 163 ? 0.90985 1.19455 1.03871 -0.04154 -0.11666 -0.19808 158 GLN A CD  
1141 O OE1 . GLN A 163 ? 0.98893 1.28222 1.08543 -0.01535 -0.13839 -0.20946 158 GLN A OE1 
1142 N NE2 . GLN A 163 ? 0.86157 1.14576 0.99803 -0.05022 -0.09897 -0.17287 158 GLN A NE2 
1143 N N   . GLY A 164 ? 0.78125 0.93215 0.79686 -0.02884 -0.08471 -0.17511 159 GLY A N   
1144 C CA  . GLY A 164 ? 0.75430 0.87422 0.72830 -0.01311 -0.08122 -0.17539 159 GLY A CA  
1145 C C   . GLY A 164 ? 0.76878 0.87154 0.69245 0.01081  -0.07147 -0.14839 159 GLY A C   
1146 O O   . GLY A 164 ? 0.83136 0.90872 0.71570 0.02819  -0.06631 -0.14809 159 GLY A O   
1147 N N   . GLN A 165 ? 0.77983 0.89384 0.70522 0.01222  -0.06674 -0.12647 160 GLN A N   
1148 C CA  . GLN A 165 ? 0.81151 0.90940 0.69666 0.03344  -0.05576 -0.10158 160 GLN A CA  
1149 C C   . GLN A 165 ? 0.87612 0.98791 0.72842 0.05854  -0.07308 -0.11015 160 GLN A C   
1150 O O   . GLN A 165 ? 0.94867 1.04009 0.75047 0.08515  -0.06847 -0.10209 160 GLN A O   
1151 C CB  . GLN A 165 ? 0.77401 0.87092 0.68160 0.02060  -0.03969 -0.07253 160 GLN A CB  
1152 C CG  . GLN A 165 ? 0.65400 0.74379 0.59850 -0.00425 -0.02832 -0.06561 160 GLN A CG  
1153 C CD  . GLN A 165 ? 0.59635 0.65766 0.53152 -0.00233 -0.01486 -0.06143 160 GLN A CD  
1154 O OE1 . GLN A 165 ? 0.61426 0.65811 0.52635 0.01266  -0.00246 -0.04624 160 GLN A OE1 
1155 N NE2 . GLN A 165 ? 0.56120 0.61634 0.51750 -0.01762 -0.01467 -0.07447 160 GLN A NE2 
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