data_9DDL
# 
_entry.id   9DDL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9DDL         pdb_00009ddl 10.2210/pdb9ddl/pdb 
WWPDB D_1000287904 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DDL 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        'Same protein with aditional loop' 
_pdbx_database_related.db_id          9C0A 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mirandab@uaem.mx 
_pdbx_contact_author.name_first         Ricardo 
_pdbx_contact_author.name_last          Miranda-Blancas 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6246-1935 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Miranda-Blancas, R.'      1  ? 
'Cardona-Echavarria, M.C.' 2  ? 
'Sanchez, C.'              3  ? 
'Sanchez-Perez, L.C.'      4  ? 
'Flores-Lopez, R.'         5  ? 
'Rodriguez-Lima, O.'       6  ? 
'Garcia-Gutierrez, P.'     7  ? 
'Zubillaga, R.'            8  ? 
'Landa, A.'                9  ? 
'Rudino-Pinera, E.'        10 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Plos Negl Trop Dis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1935-2735 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            19 
_citation.language                  ? 
_citation.page_first                e0013024 
_citation.page_last                 e0013024 
_citation.title                     
'Structural insights into sigma class glutathione transferase from Taenia solium: Analysis and functional implications.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1371/journal.pntd.0013024 
_citation.pdbx_database_id_PubMed   40445974 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Miranda-Blancas, R.'      1  ?                   
primary 'Garcia-Gutierrez, P.'     2  ?                   
primary 'Sanchez-Juarez, C.'       3  ?                   
primary 'Cardona-Echavarria, M.C.' 4  ?                   
primary 'Flores-Lopez, R.'         5  ?                   
primary 'Zubillaga, R.A.'          6  ?                   
primary 'Rodriguez-Lima, O.'       7  ?                   
primary 'Sanchez-Perez, L.C.'      8  ?                   
primary 'Rudino-Pinera, E.'        9  ?                   
primary 'Landa, A.'                10 0000-0003-2573-1806 
# 
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 'Sigma-type glutathione S-transferase' 24326.418 1   ? ? ? ? 
2 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                106.120   1   ? ? ? ? 
3 water       nat water                                  18.015    188 ? ? ? ? 
# 
_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       
;MDLQLKQAKLRLLYFNIRGRAELIRLVLNAAEKDFEDVRVSETEWPSLKSKMPFNQLPVLEVTTPNGQKVMLTESMAIAR
LLARTFGLYGDNAAEVYLIERMNSLTSSLLEEIYALGLKKVDSFKKLFEAEHLHEYMNAIEMALKERKSTFIAGPRVTLA
DLQVIVLIDTMNKFLPNTKHECKDKLDEIKEGVIRTKPGVARYLRSRPATDF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDLQLKQAKLRLLYFNIRGRAELIRLVLNAAEKDFEDVRVSETEWPSLKSKMPFNQLPVLEVTTPNGQKVMLTESMAIAR
LLARTFGLYGDNAAEVYLIERMNSLTSSLLEEIYALGLKKVDSFKKLFEAEHLHEYMNAIEMALKERKSTFIAGPRVTLA
DLQVIVLIDTMNKFLPNTKHECKDKLDEIKEGVIRTKPGVARYLRSRPATDF
;
_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 'DI(HYDROXYETHYL)ETHER' PEG 
3 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   LEU n 
1 4   GLN n 
1 5   LEU n 
1 6   LYS n 
1 7   GLN n 
1 8   ALA n 
1 9   LYS n 
1 10  LEU n 
1 11  ARG n 
1 12  LEU n 
1 13  LEU n 
1 14  TYR n 
1 15  PHE n 
1 16  ASN n 
1 17  ILE n 
1 18  ARG n 
1 19  GLY n 
1 20  ARG n 
1 21  ALA n 
1 22  GLU n 
1 23  LEU n 
1 24  ILE n 
1 25  ARG n 
1 26  LEU n 
1 27  VAL n 
1 28  LEU n 
1 29  ASN n 
1 30  ALA n 
1 31  ALA n 
1 32  GLU n 
1 33  LYS n 
1 34  ASP n 
1 35  PHE n 
1 36  GLU n 
1 37  ASP n 
1 38  VAL n 
1 39  ARG n 
1 40  VAL n 
1 41  SER n 
1 42  GLU n 
1 43  THR n 
1 44  GLU n 
1 45  TRP n 
1 46  PRO n 
1 47  SER n 
1 48  LEU n 
1 49  LYS n 
1 50  SER n 
1 51  LYS n 
1 52  MET n 
1 53  PRO n 
1 54  PHE n 
1 55  ASN n 
1 56  GLN n 
1 57  LEU n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  GLU n 
1 62  VAL n 
1 63  THR n 
1 64  THR n 
1 65  PRO n 
1 66  ASN n 
1 67  GLY n 
1 68  GLN n 
1 69  LYS n 
1 70  VAL n 
1 71  MET n 
1 72  LEU n 
1 73  THR n 
1 74  GLU n 
1 75  SER n 
1 76  MET n 
1 77  ALA n 
1 78  ILE n 
1 79  ALA n 
1 80  ARG n 
1 81  LEU n 
1 82  LEU n 
1 83  ALA n 
1 84  ARG n 
1 85  THR n 
1 86  PHE n 
1 87  GLY n 
1 88  LEU n 
1 89  TYR n 
1 90  GLY n 
1 91  ASP n 
1 92  ASN n 
1 93  ALA n 
1 94  ALA n 
1 95  GLU n 
1 96  VAL n 
1 97  TYR n 
1 98  LEU n 
1 99  ILE n 
1 100 GLU n 
1 101 ARG n 
1 102 MET n 
1 103 ASN n 
1 104 SER n 
1 105 LEU n 
1 106 THR n 
1 107 SER n 
1 108 SER n 
1 109 LEU n 
1 110 LEU n 
1 111 GLU n 
1 112 GLU n 
1 113 ILE n 
1 114 TYR n 
1 115 ALA n 
1 116 LEU n 
1 117 GLY n 
1 118 LEU n 
1 119 LYS n 
1 120 LYS n 
1 121 VAL n 
1 122 ASP n 
1 123 SER n 
1 124 PHE n 
1 125 LYS n 
1 126 LYS n 
1 127 LEU n 
1 128 PHE n 
1 129 GLU n 
1 130 ALA n 
1 131 GLU n 
1 132 HIS n 
1 133 LEU n 
1 134 HIS n 
1 135 GLU n 
1 136 TYR n 
1 137 MET n 
1 138 ASN n 
1 139 ALA n 
1 140 ILE n 
1 141 GLU n 
1 142 MET n 
1 143 ALA n 
1 144 LEU n 
1 145 LYS n 
1 146 GLU n 
1 147 ARG n 
1 148 LYS n 
1 149 SER n 
1 150 THR n 
1 151 PHE n 
1 152 ILE n 
1 153 ALA n 
1 154 GLY n 
1 155 PRO n 
1 156 ARG n 
1 157 VAL n 
1 158 THR n 
1 159 LEU n 
1 160 ALA n 
1 161 ASP n 
1 162 LEU n 
1 163 GLN n 
1 164 VAL n 
1 165 ILE n 
1 166 VAL n 
1 167 LEU n 
1 168 ILE n 
1 169 ASP n 
1 170 THR n 
1 171 MET n 
1 172 ASN n 
1 173 LYS n 
1 174 PHE n 
1 175 LEU n 
1 176 PRO n 
1 177 ASN n 
1 178 THR n 
1 179 LYS n 
1 180 HIS n 
1 181 GLU n 
1 182 CYS n 
1 183 LYS n 
1 184 ASP n 
1 185 LYS n 
1 186 LEU n 
1 187 ASP n 
1 188 GLU n 
1 189 ILE n 
1 190 LYS n 
1 191 GLU n 
1 192 GLY n 
1 193 VAL n 
1 194 ILE n 
1 195 ARG n 
1 196 THR n 
1 197 LYS n 
1 198 PRO n 
1 199 GLY n 
1 200 VAL n 
1 201 ALA n 
1 202 ARG n 
1 203 TYR n 
1 204 LEU n 
1 205 ARG n 
1 206 SER n 
1 207 ARG n 
1 208 PRO n 
1 209 ALA n 
1 210 THR n 
1 211 ASP n 
1 212 PHE 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                   212 
_entity_src_gen.gene_src_common_name               'pork tapeworm' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GST-28 
_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      'Taenia solium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6204 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE               ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE               ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ? 'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  TRP 45  45  45  TRP TRP A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  MET 52  52  52  MET MET A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  MET 71  71  71  MET MET A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 VAL 121 121 ?   ?   ?   A . n 
A 1 122 ASP 122 122 ?   ?   ?   A . n 
A 1 123 SER 123 123 ?   ?   ?   A . n 
A 1 124 PHE 124 124 ?   ?   ?   A . n 
A 1 125 LYS 125 125 ?   ?   ?   A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 LEU 127 127 ?   ?   ?   A . n 
A 1 128 PHE 128 128 ?   ?   ?   A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 MET 142 142 142 MET MET A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 ILE 168 168 168 ILE ILE A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 MET 171 171 171 MET MET A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 PRO 176 176 176 PRO PRO A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 CYS 182 182 182 CYS CYS A . n 
A 1 183 LYS 183 183 183 LYS LYS A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 LYS 185 185 185 LYS LYS A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 ILE 194 194 194 ILE ILE A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 LYS 197 197 197 LYS LYS A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PEG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PEG 
_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 PEG 1   301 301 PEG PEG A . 
C 3 HOH 1   401 197 HOH HOH A . 
C 3 HOH 2   402 198 HOH HOH A . 
C 3 HOH 3   403 177 HOH HOH A . 
C 3 HOH 4   404 43  HOH HOH A . 
C 3 HOH 5   405 147 HOH HOH A . 
C 3 HOH 6   406 75  HOH HOH A . 
C 3 HOH 7   407 102 HOH HOH A . 
C 3 HOH 8   408 164 HOH HOH A . 
C 3 HOH 9   409 155 HOH HOH A . 
C 3 HOH 10  410 137 HOH HOH A . 
C 3 HOH 11  411 175 HOH HOH A . 
C 3 HOH 12  412 59  HOH HOH A . 
C 3 HOH 13  413 15  HOH HOH A . 
C 3 HOH 14  414 41  HOH HOH A . 
C 3 HOH 15  415 97  HOH HOH A . 
C 3 HOH 16  416 80  HOH HOH A . 
C 3 HOH 17  417 71  HOH HOH A . 
C 3 HOH 18  418 148 HOH HOH A . 
C 3 HOH 19  419 170 HOH HOH A . 
C 3 HOH 20  420 193 HOH HOH A . 
C 3 HOH 21  421 104 HOH HOH A . 
C 3 HOH 22  422 23  HOH HOH A . 
C 3 HOH 23  423 119 HOH HOH A . 
C 3 HOH 24  424 161 HOH HOH A . 
C 3 HOH 25  425 109 HOH HOH A . 
C 3 HOH 26  426 3   HOH HOH A . 
C 3 HOH 27  427 120 HOH HOH A . 
C 3 HOH 28  428 132 HOH HOH A . 
C 3 HOH 29  429 93  HOH HOH A . 
C 3 HOH 30  430 35  HOH HOH A . 
C 3 HOH 31  431 125 HOH HOH A . 
C 3 HOH 32  432 39  HOH HOH A . 
C 3 HOH 33  433 73  HOH HOH A . 
C 3 HOH 34  434 63  HOH HOH A . 
C 3 HOH 35  435 173 HOH HOH A . 
C 3 HOH 36  436 68  HOH HOH A . 
C 3 HOH 37  437 27  HOH HOH A . 
C 3 HOH 38  438 88  HOH HOH A . 
C 3 HOH 39  439 13  HOH HOH A . 
C 3 HOH 40  440 28  HOH HOH A . 
C 3 HOH 41  441 1   HOH HOH A . 
C 3 HOH 42  442 6   HOH HOH A . 
C 3 HOH 43  443 36  HOH HOH A . 
C 3 HOH 44  444 130 HOH HOH A . 
C 3 HOH 45  445 42  HOH HOH A . 
C 3 HOH 46  446 55  HOH HOH A . 
C 3 HOH 47  447 191 HOH HOH A . 
C 3 HOH 48  448 18  HOH HOH A . 
C 3 HOH 49  449 53  HOH HOH A . 
C 3 HOH 50  450 99  HOH HOH A . 
C 3 HOH 51  451 34  HOH HOH A . 
C 3 HOH 52  452 117 HOH HOH A . 
C 3 HOH 53  453 47  HOH HOH A . 
C 3 HOH 54  454 183 HOH HOH A . 
C 3 HOH 55  455 44  HOH HOH A . 
C 3 HOH 56  456 48  HOH HOH A . 
C 3 HOH 57  457 162 HOH HOH A . 
C 3 HOH 58  458 2   HOH HOH A . 
C 3 HOH 59  459 37  HOH HOH A . 
C 3 HOH 60  460 40  HOH HOH A . 
C 3 HOH 61  461 12  HOH HOH A . 
C 3 HOH 62  462 64  HOH HOH A . 
C 3 HOH 63  463 30  HOH HOH A . 
C 3 HOH 64  464 172 HOH HOH A . 
C 3 HOH 65  465 169 HOH HOH A . 
C 3 HOH 66  466 14  HOH HOH A . 
C 3 HOH 67  467 151 HOH HOH A . 
C 3 HOH 68  468 112 HOH HOH A . 
C 3 HOH 69  469 54  HOH HOH A . 
C 3 HOH 70  470 52  HOH HOH A . 
C 3 HOH 71  471 89  HOH HOH A . 
C 3 HOH 72  472 51  HOH HOH A . 
C 3 HOH 73  473 122 HOH HOH A . 
C 3 HOH 74  474 46  HOH HOH A . 
C 3 HOH 75  475 22  HOH HOH A . 
C 3 HOH 76  476 8   HOH HOH A . 
C 3 HOH 77  477 9   HOH HOH A . 
C 3 HOH 78  478 20  HOH HOH A . 
C 3 HOH 79  479 21  HOH HOH A . 
C 3 HOH 80  480 5   HOH HOH A . 
C 3 HOH 81  481 94  HOH HOH A . 
C 3 HOH 82  482 98  HOH HOH A . 
C 3 HOH 83  483 33  HOH HOH A . 
C 3 HOH 84  484 87  HOH HOH A . 
C 3 HOH 85  485 127 HOH HOH A . 
C 3 HOH 86  486 81  HOH HOH A . 
C 3 HOH 87  487 82  HOH HOH A . 
C 3 HOH 88  488 32  HOH HOH A . 
C 3 HOH 89  489 24  HOH HOH A . 
C 3 HOH 90  490 179 HOH HOH A . 
C 3 HOH 91  491 7   HOH HOH A . 
C 3 HOH 92  492 101 HOH HOH A . 
C 3 HOH 93  493 38  HOH HOH A . 
C 3 HOH 94  494 107 HOH HOH A . 
C 3 HOH 95  495 79  HOH HOH A . 
C 3 HOH 96  496 65  HOH HOH A . 
C 3 HOH 97  497 200 HOH HOH A . 
C 3 HOH 98  498 95  HOH HOH A . 
C 3 HOH 99  499 11  HOH HOH A . 
C 3 HOH 100 500 50  HOH HOH A . 
C 3 HOH 101 501 189 HOH HOH A . 
C 3 HOH 102 502 57  HOH HOH A . 
C 3 HOH 103 503 61  HOH HOH A . 
C 3 HOH 104 504 90  HOH HOH A . 
C 3 HOH 105 505 67  HOH HOH A . 
C 3 HOH 106 506 49  HOH HOH A . 
C 3 HOH 107 507 84  HOH HOH A . 
C 3 HOH 108 508 77  HOH HOH A . 
C 3 HOH 109 509 190 HOH HOH A . 
C 3 HOH 110 510 153 HOH HOH A . 
C 3 HOH 111 511 113 HOH HOH A . 
C 3 HOH 112 512 60  HOH HOH A . 
C 3 HOH 113 513 85  HOH HOH A . 
C 3 HOH 114 514 26  HOH HOH A . 
C 3 HOH 115 515 78  HOH HOH A . 
C 3 HOH 116 516 196 HOH HOH A . 
C 3 HOH 117 517 103 HOH HOH A . 
C 3 HOH 118 518 17  HOH HOH A . 
C 3 HOH 119 519 74  HOH HOH A . 
C 3 HOH 120 520 56  HOH HOH A . 
C 3 HOH 121 521 150 HOH HOH A . 
C 3 HOH 122 522 145 HOH HOH A . 
C 3 HOH 123 523 182 HOH HOH A . 
C 3 HOH 124 524 66  HOH HOH A . 
C 3 HOH 125 525 128 HOH HOH A . 
C 3 HOH 126 526 174 HOH HOH A . 
C 3 HOH 127 527 178 HOH HOH A . 
C 3 HOH 128 528 83  HOH HOH A . 
C 3 HOH 129 529 118 HOH HOH A . 
C 3 HOH 130 530 16  HOH HOH A . 
C 3 HOH 131 531 10  HOH HOH A . 
C 3 HOH 132 532 25  HOH HOH A . 
C 3 HOH 133 533 91  HOH HOH A . 
C 3 HOH 134 534 160 HOH HOH A . 
C 3 HOH 135 535 96  HOH HOH A . 
C 3 HOH 136 536 29  HOH HOH A . 
C 3 HOH 137 537 76  HOH HOH A . 
C 3 HOH 138 538 31  HOH HOH A . 
C 3 HOH 139 539 139 HOH HOH A . 
C 3 HOH 140 540 72  HOH HOH A . 
C 3 HOH 141 541 4   HOH HOH A . 
C 3 HOH 142 542 131 HOH HOH A . 
C 3 HOH 143 543 156 HOH HOH A . 
C 3 HOH 144 544 144 HOH HOH A . 
C 3 HOH 145 545 163 HOH HOH A . 
C 3 HOH 146 546 176 HOH HOH A . 
C 3 HOH 147 547 121 HOH HOH A . 
C 3 HOH 148 548 180 HOH HOH A . 
C 3 HOH 149 549 165 HOH HOH A . 
C 3 HOH 150 550 143 HOH HOH A . 
C 3 HOH 151 551 140 HOH HOH A . 
C 3 HOH 152 552 152 HOH HOH A . 
C 3 HOH 153 553 105 HOH HOH A . 
C 3 HOH 154 554 136 HOH HOH A . 
C 3 HOH 155 555 142 HOH HOH A . 
C 3 HOH 156 556 195 HOH HOH A . 
C 3 HOH 157 557 146 HOH HOH A . 
C 3 HOH 158 558 45  HOH HOH A . 
C 3 HOH 159 559 126 HOH HOH A . 
C 3 HOH 160 560 154 HOH HOH A . 
C 3 HOH 161 561 186 HOH HOH A . 
C 3 HOH 162 562 58  HOH HOH A . 
C 3 HOH 163 563 69  HOH HOH A . 
C 3 HOH 164 564 194 HOH HOH A . 
C 3 HOH 165 565 166 HOH HOH A . 
C 3 HOH 166 566 171 HOH HOH A . 
C 3 HOH 167 567 159 HOH HOH A . 
C 3 HOH 168 568 192 HOH HOH A . 
C 3 HOH 169 569 116 HOH HOH A . 
C 3 HOH 170 570 114 HOH HOH A . 
C 3 HOH 171 571 124 HOH HOH A . 
C 3 HOH 172 572 157 HOH HOH A . 
C 3 HOH 173 573 92  HOH HOH A . 
C 3 HOH 174 574 134 HOH HOH A . 
C 3 HOH 175 575 70  HOH HOH A . 
C 3 HOH 176 576 149 HOH HOH A . 
C 3 HOH 177 577 138 HOH HOH A . 
C 3 HOH 178 578 141 HOH HOH A . 
C 3 HOH 179 579 100 HOH HOH A . 
C 3 HOH 180 580 167 HOH HOH A . 
C 3 HOH 181 581 129 HOH HOH A . 
C 3 HOH 182 582 123 HOH HOH A . 
C 3 HOH 183 583 133 HOH HOH A . 
C 3 HOH 184 584 158 HOH HOH A . 
C 3 HOH 185 585 108 HOH HOH A . 
C 3 HOH 186 586 106 HOH HOH A . 
C 3 HOH 187 587 115 HOH HOH A . 
C 3 HOH 188 588 188 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 0 A VAL 38  ? N   A A VAL 38  N   
2  1 Y 0 A VAL 38  ? CA  A A VAL 38  CA  
3  1 Y 0 A VAL 38  ? C   A A VAL 38  C   
4  1 Y 0 A VAL 38  ? O   A A VAL 38  O   
5  1 Y 0 A VAL 38  ? CB  A A VAL 38  CB  
6  1 Y 0 A VAL 38  ? CG1 A A VAL 38  CG1 
7  1 Y 0 A VAL 38  ? CG2 A A VAL 38  CG2 
8  1 Y 0 A MET 102 ? CA  A A MET 102 CA  
9  1 Y 0 A MET 102 ? CB  A A MET 102 CB  
10 1 Y 0 A MET 102 ? CG  A A MET 102 CG  
11 1 Y 0 A MET 102 ? SD  A A MET 102 SD  
12 1 Y 0 A MET 102 ? CE  A A MET 102 CE  
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20_4459: ???)' ? 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                  ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DDL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.020 
_cell.length_a_esd                 ? 
_cell.length_b                     111.300 
_cell.length_b_esd                 ? 
_cell.length_c                     65.310 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DDL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DDL 
_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             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.02 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_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    
;Tris 50 mM
Sodium citrate 100 mM
;
_exptl_crystal_grow.pdbx_pH_range   5.8-74 
_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                      'Si 111 double crystal monochromator' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-05 
_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   0.97 
_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                        'NSLS BEAMLINE X17B1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X17B1 
_diffrn_source.pdbx_synchrotron_site       NSLS 
# 
_reflns.B_iso_Wilson_estimate                          15.90 
_reflns.entry_id                                       9DDL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.30 
_reflns.d_resolution_low                               31.1 
_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                                     50886 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.97 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.96 
_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                                0.055 
_reflns.pdbx_Rpim_I_all                                0.014 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0530 
_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                                    1.3 
_reflns_shell.d_res_low                                     1.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.64 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4964 
_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                               13.1 
_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                               0.95 
_reflns_shell.pdbx_Rpim_I_all                               0.26 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.88 
_reflns_shell.pdbx_CC_star                                  0.97 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.85 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.91 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DDL 
_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                            1.30 
_refine.ls_d_res_low                             31.10 
_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                     50885 
_refine.ls_number_reflns_R_free                  2588 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.97 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1902 
_refine.ls_R_factor_R_free                       0.2226 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1885 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.95 
_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                            0.20 
_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                       1.30 
_refine_hist.d_res_low                        31.10 
_refine_hist.number_atoms_solvent             188 
_refine_hist.number_atoms_total               1832 
_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        1637 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         7 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? ?   ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.946 ? ?   ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 5.962 ? 270 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.078 ? 287 ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 336 ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.30 1.33 . . 140 2619 98.00  . . . . 0.3776 . . . . . . . . . . . . . . . 0.4280 
'X-RAY DIFFRACTION' 1.33 1.35 . . 136 2617 98.00  . . . . 0.3511 . . . . . . . . . . . . . . . 0.3784 
'X-RAY DIFFRACTION' 1.35 1.38 . . 142 2636 98.00  . . . . .      . . . . . . . . . . . . . . . 0.3244 
'X-RAY DIFFRACTION' 1.38 1.41 . . 131 2630 98.00  . . . . 0.3056 . . . . . . . . . . . . . . . 0.3431 
'X-RAY DIFFRACTION' 1.41 1.45 . . 154 2648 98.00  . . . . 0.2972 . . . . . . . . . . . . . . . 0.3209 
'X-RAY DIFFRACTION' 1.45 1.49 . . 146 2629 99.00  . . . . 0.2671 . . . . . . . . . . . . . . . 0.3218 
'X-RAY DIFFRACTION' 1.49 1.53 . . 152 2640 99.00  . . . . 0.2472 . . . . . . . . . . . . . . . 0.2821 
'X-RAY DIFFRACTION' 1.53 1.58 . . 139 2652 99.00  . . . . 0.2231 . . . . . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 1.58 1.64 . . 138 2686 99.00  . . . . 0.1997 . . . . . . . . . . . . . . . 0.2005 
'X-RAY DIFFRACTION' 1.64 1.70 . . 137 2674 99.00  . . . . 0.2139 . . . . . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 1.70 1.78 . . 158 2660 99.00  . . . . 0.1978 . . . . . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 1.78 1.87 . . 136 2676 100.00 . . . . 0.1848 . . . . . . . . . . . . . . . 0.2163 
'X-RAY DIFFRACTION' 1.87 1.99 . . 130 2720 100.00 . . . . 0.1761 . . . . . . . . . . . . . . . 0.2116 
'X-RAY DIFFRACTION' 1.99 2.15 . . 148 2700 100.00 . . . . 0.1687 . . . . . . . . . . . . . . . 0.2140 
'X-RAY DIFFRACTION' 2.15 2.36 . . 137 2730 100.00 . . . . 0.1605 . . . . . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 2.36 2.70 . . 147 2737 100.00 . . . . 0.1719 . . . . . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 2.70 3.41 . . 167 2750 100.00 . . . . 0.1680 . . . . . . . . . . . . . . . 0.1930 
'X-RAY DIFFRACTION' 3.41 10   . . 150 2893 100.00 . . . . 0.1647 . . . . . . . . . . . . . . . 0.2146 
# 
_struct.entry_id                     9DDL 
_struct.title                        'Glutathione transferase sigma class from Taenia solium 1.3' 
_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        9DDL 
_struct_keywords.text            
'Glutathione transferase, Prostaglandine D2 syntase, Glutathione transferase sigma class, Taenia solium, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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                    C0M0N5_TAESO 
_struct_ref.pdbx_db_accession          C0M0N5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDLQLKQAKLRLLYFNIRGRAELIRLVLNAAEKDFEDVRVSETEWPSLKSKMPFNQLPVLEVTTPNGQKVMLTESMAIAR
LLARTFGLYGDNAAEVYLIERMNSLTSSLLEEIYALGLKKVDSFKKLFEAEHLHEYMNAIEMALKERKSTFIAGPRVTLA
DLQVIVLIDTMNKFLPNTKHECKDKLDEIKEGVIRTKPGVARYLRSRPATDF
;
_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              9DDL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 212 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             C0M0N5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  212 
_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       212 
# 
_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)' 2380  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  20220 ? 
# 
_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                
'Superdex 75 column eluted with 1 volume of Tris 20 mM pH 7.4 and 150 mM NaCl' 
# 
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' 3_655 -x+1,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 57.0200000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 32.6550000000 
# 
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 ALA A 21  ? GLU A 32  ? ALA A 21  GLU A 32  1 ? 12 
HELX_P HELX_P2 AA2 GLU A 44  ? MET A 52  ? GLU A 44  MET A 52  1 ? 9  
HELX_P HELX_P3 AA3 GLU A 74  ? PHE A 86  ? GLU A 74  PHE A 86  1 ? 13 
HELX_P HELX_P4 AA4 ASN A 92  ? LYS A 120 ? ASN A 92  LYS A 120 1 ? 29 
HELX_P HELX_P5 AA5 ALA A 130 ? ARG A 147 ? ALA A 130 ARG A 147 1 ? 18 
HELX_P HELX_P6 AA6 THR A 158 ? LEU A 175 ? THR A 158 LEU A 175 1 ? 18 
HELX_P HELX_P7 AA7 HIS A 180 ? LYS A 197 ? HIS A 180 LYS A 197 1 ? 18 
HELX_P HELX_P8 AA8 LYS A 197 ? ARG A 207 ? LYS A 197 ARG A 207 1 ? 11 
# 
_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          LEU 
_struct_mon_prot_cis.label_seq_id           57 
_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           LEU 
_struct_mon_prot_cis.auth_seq_id            57 
_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    58 
_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     58 
_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       1.36 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_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 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 36 ? VAL A 40 ? GLU A 36 VAL A 40 
AA1 2 LYS A 9  ? PHE A 15 ? LYS A 9  PHE A 15 
AA1 3 VAL A 59 ? THR A 63 ? VAL A 59 THR A 63 
AA1 4 LYS A 69 ? LEU A 72 ? LYS A 69 LEU A 72 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 40 ? O VAL A 40 N TYR A 14 ? N TYR A 14 
AA1 2 3 N ARG A 11 ? N ARG A 11 O GLU A 61 ? O GLU A 61 
AA1 3 4 N VAL A 62 ? N VAL A 62 O VAL A 70 ? O VAL A 70 
# 
_pdbx_entry_details.entry_id                   9DDL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 A GLN 7   ? B O A HOH 401 ? ? 1.94 
2  1 O   A HOH 420 ? ? O A HOH 568 ? ? 1.98 
3  1 O   A HOH 401 ? ? O A HOH 561 ? ? 2.07 
4  1 O   A HOH 435 ? ? O A HOH 540 ? ? 2.11 
5  1 O   A HOH 492 ? ? O A HOH 556 ? ? 2.13 
6  1 O   A HOH 411 ? ? O A HOH 483 ? ? 2.14 
7  1 O   A HOH 548 ? ? O A HOH 577 ? ? 2.14 
8  1 O   A HOH 462 ? ? O A HOH 467 ? ? 2.15 
9  1 O1  A PEG 301 ? ? O A HOH 402 ? ? 2.17 
10 1 O   A HOH 411 ? ? O A HOH 527 ? ? 2.17 
11 1 O   A HOH 422 ? ? O A HOH 550 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 496 ? ? 1_555 O A HOH 496 ? ? 3_555 1.98 
2 1 O A HOH 548 ? ? 1_555 O A HOH 556 ? ? 3_655 2.06 
3 1 O A HOH 402 ? ? 1_555 O A HOH 467 ? ? 8_555 2.08 
4 1 O A HOH 428 ? ? 1_555 O A HOH 497 ? ? 8_555 2.09 
5 1 O A HOH 577 ? ? 1_555 O A HOH 583 ? ? 3_655 2.10 
6 1 O A HOH 515 ? ? 1_555 O A HOH 526 ? ? 3_655 2.10 
# 
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 GLU A 74 ? ? 79.32 100.25 
2 1 GLU A 74 ? ? 79.32 99.42  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     586 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 VAL 121 ? A VAL 121 
2 1 Y 1 A ASP 122 ? A ASP 122 
3 1 Y 1 A SER 123 ? A SER 123 
4 1 Y 1 A PHE 124 ? A PHE 124 
5 1 Y 1 A LYS 125 ? A LYS 125 
6 1 Y 1 A LYS 126 ? A LYS 126 
7 1 Y 1 A LEU 127 ? A LEU 127 
8 1 Y 1 A PHE 128 ? A PHE 128 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PEG C1   C N N 250 
PEG O1   O N N 251 
PEG C2   C N N 252 
PEG O2   O N N 253 
PEG C3   C N N 254 
PEG C4   C N N 255 
PEG O4   O N N 256 
PEG H11  H N N 257 
PEG H12  H N N 258 
PEG HO1  H N N 259 
PEG H21  H N N 260 
PEG H22  H N N 261 
PEG H31  H N N 262 
PEG H32  H N N 263 
PEG H41  H N N 264 
PEG H42  H N N 265 
PEG HO4  H N N 266 
PHE N    N N N 267 
PHE CA   C N S 268 
PHE C    C N N 269 
PHE O    O N N 270 
PHE CB   C N N 271 
PHE CG   C Y N 272 
PHE CD1  C Y N 273 
PHE CD2  C Y N 274 
PHE CE1  C Y N 275 
PHE CE2  C Y N 276 
PHE CZ   C Y N 277 
PHE OXT  O N N 278 
PHE H    H N N 279 
PHE H2   H N N 280 
PHE HA   H N N 281 
PHE HB2  H N N 282 
PHE HB3  H N N 283 
PHE HD1  H N N 284 
PHE HD2  H N N 285 
PHE HE1  H N N 286 
PHE HE2  H N N 287 
PHE HZ   H N N 288 
PHE HXT  H N N 289 
PRO N    N N N 290 
PRO CA   C N S 291 
PRO C    C N N 292 
PRO O    O N N 293 
PRO CB   C N N 294 
PRO CG   C N N 295 
PRO CD   C N N 296 
PRO OXT  O N N 297 
PRO H    H N N 298 
PRO HA   H N N 299 
PRO HB2  H N N 300 
PRO HB3  H N N 301 
PRO HG2  H N N 302 
PRO HG3  H N N 303 
PRO HD2  H N N 304 
PRO HD3  H N N 305 
PRO HXT  H N N 306 
SER N    N N N 307 
SER CA   C N S 308 
SER C    C N N 309 
SER O    O N N 310 
SER CB   C N N 311 
SER OG   O N N 312 
SER OXT  O N N 313 
SER H    H N N 314 
SER H2   H N N 315 
SER HA   H N N 316 
SER HB2  H N N 317 
SER HB3  H N N 318 
SER HG   H N N 319 
SER HXT  H N N 320 
THR N    N N N 321 
THR CA   C N S 322 
THR C    C N N 323 
THR O    O N N 324 
THR CB   C N R 325 
THR OG1  O N N 326 
THR CG2  C N N 327 
THR OXT  O N N 328 
THR H    H N N 329 
THR H2   H N N 330 
THR HA   H N N 331 
THR HB   H N N 332 
THR HG1  H N N 333 
THR HG21 H N N 334 
THR HG22 H N N 335 
THR HG23 H N N 336 
THR HXT  H N N 337 
TRP N    N N N 338 
TRP CA   C N S 339 
TRP C    C N N 340 
TRP O    O N N 341 
TRP CB   C N N 342 
TRP CG   C Y N 343 
TRP CD1  C Y N 344 
TRP CD2  C Y N 345 
TRP NE1  N Y N 346 
TRP CE2  C Y N 347 
TRP CE3  C Y N 348 
TRP CZ2  C Y N 349 
TRP CZ3  C Y N 350 
TRP CH2  C Y N 351 
TRP OXT  O N N 352 
TRP H    H N N 353 
TRP H2   H N N 354 
TRP HA   H N N 355 
TRP HB2  H N N 356 
TRP HB3  H N N 357 
TRP HD1  H N N 358 
TRP HE1  H N N 359 
TRP HE3  H N N 360 
TRP HZ2  H N N 361 
TRP HZ3  H N N 362 
TRP HH2  H N N 363 
TRP HXT  H N N 364 
TYR N    N N N 365 
TYR CA   C N S 366 
TYR C    C N N 367 
TYR O    O N N 368 
TYR CB   C N N 369 
TYR CG   C Y N 370 
TYR CD1  C Y N 371 
TYR CD2  C Y N 372 
TYR CE1  C Y N 373 
TYR CE2  C Y N 374 
TYR CZ   C Y N 375 
TYR OH   O N N 376 
TYR OXT  O N N 377 
TYR H    H N N 378 
TYR H2   H N N 379 
TYR HA   H N N 380 
TYR HB2  H N N 381 
TYR HB3  H N N 382 
TYR HD1  H N N 383 
TYR HD2  H N N 384 
TYR HE1  H N N 385 
TYR HE2  H N N 386 
TYR HH   H N N 387 
TYR HXT  H N N 388 
VAL N    N N N 389 
VAL CA   C N S 390 
VAL C    C N N 391 
VAL O    O N N 392 
VAL CB   C N N 393 
VAL CG1  C N N 394 
VAL CG2  C N N 395 
VAL OXT  O N N 396 
VAL H    H N N 397 
VAL H2   H N N 398 
VAL HA   H N N 399 
VAL HB   H N N 400 
VAL HG11 H N N 401 
VAL HG12 H N N 402 
VAL HG13 H N N 403 
VAL HG21 H N N 404 
VAL HG22 H N N 405 
VAL HG23 H N N 406 
VAL HXT  H N N 407 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PEG C1  O1   sing N N 237 
PEG C1  C2   sing N N 238 
PEG C1  H11  sing N N 239 
PEG C1  H12  sing N N 240 
PEG O1  HO1  sing N N 241 
PEG C2  O2   sing N N 242 
PEG C2  H21  sing N N 243 
PEG C2  H22  sing N N 244 
PEG O2  C3   sing N N 245 
PEG C3  C4   sing N N 246 
PEG C3  H31  sing N N 247 
PEG C3  H32  sing N N 248 
PEG C4  O4   sing N N 249 
PEG C4  H41  sing N N 250 
PEG C4  H42  sing N N 251 
PEG O4  HO4  sing N N 252 
PHE N   CA   sing N N 253 
PHE N   H    sing N N 254 
PHE N   H2   sing N N 255 
PHE CA  C    sing N N 256 
PHE CA  CB   sing N N 257 
PHE CA  HA   sing N N 258 
PHE C   O    doub N N 259 
PHE C   OXT  sing N N 260 
PHE CB  CG   sing N N 261 
PHE CB  HB2  sing N N 262 
PHE CB  HB3  sing N N 263 
PHE CG  CD1  doub Y N 264 
PHE CG  CD2  sing Y N 265 
PHE CD1 CE1  sing Y N 266 
PHE CD1 HD1  sing N N 267 
PHE CD2 CE2  doub Y N 268 
PHE CD2 HD2  sing N N 269 
PHE CE1 CZ   doub Y N 270 
PHE CE1 HE1  sing N N 271 
PHE CE2 CZ   sing Y N 272 
PHE CE2 HE2  sing N N 273 
PHE CZ  HZ   sing N N 274 
PHE OXT HXT  sing N N 275 
PRO N   CA   sing N N 276 
PRO N   CD   sing N N 277 
PRO N   H    sing N N 278 
PRO CA  C    sing N N 279 
PRO CA  CB   sing N N 280 
PRO CA  HA   sing N N 281 
PRO C   O    doub N N 282 
PRO C   OXT  sing N N 283 
PRO CB  CG   sing N N 284 
PRO CB  HB2  sing N N 285 
PRO CB  HB3  sing N N 286 
PRO CG  CD   sing N N 287 
PRO CG  HG2  sing N N 288 
PRO CG  HG3  sing N N 289 
PRO CD  HD2  sing N N 290 
PRO CD  HD3  sing N N 291 
PRO OXT HXT  sing N N 292 
SER N   CA   sing N N 293 
SER N   H    sing N N 294 
SER N   H2   sing N N 295 
SER CA  C    sing N N 296 
SER CA  CB   sing N N 297 
SER CA  HA   sing N N 298 
SER C   O    doub N N 299 
SER C   OXT  sing N N 300 
SER CB  OG   sing N N 301 
SER CB  HB2  sing N N 302 
SER CB  HB3  sing N N 303 
SER OG  HG   sing N N 304 
SER OXT HXT  sing N N 305 
THR N   CA   sing N N 306 
THR N   H    sing N N 307 
THR N   H2   sing N N 308 
THR CA  C    sing N N 309 
THR CA  CB   sing N N 310 
THR CA  HA   sing N N 311 
THR C   O    doub N N 312 
THR C   OXT  sing N N 313 
THR CB  OG1  sing N N 314 
THR CB  CG2  sing N N 315 
THR CB  HB   sing N N 316 
THR OG1 HG1  sing N N 317 
THR CG2 HG21 sing N N 318 
THR CG2 HG22 sing N N 319 
THR CG2 HG23 sing N N 320 
THR OXT HXT  sing N N 321 
TRP N   CA   sing N N 322 
TRP N   H    sing N N 323 
TRP N   H2   sing N N 324 
TRP CA  C    sing N N 325 
TRP CA  CB   sing N N 326 
TRP CA  HA   sing N N 327 
TRP C   O    doub N N 328 
TRP C   OXT  sing N N 329 
TRP CB  CG   sing N N 330 
TRP CB  HB2  sing N N 331 
TRP CB  HB3  sing N N 332 
TRP CG  CD1  doub Y N 333 
TRP CG  CD2  sing Y N 334 
TRP CD1 NE1  sing Y N 335 
TRP CD1 HD1  sing N N 336 
TRP CD2 CE2  doub Y N 337 
TRP CD2 CE3  sing Y N 338 
TRP NE1 CE2  sing Y N 339 
TRP NE1 HE1  sing N N 340 
TRP CE2 CZ2  sing Y N 341 
TRP CE3 CZ3  doub Y N 342 
TRP CE3 HE3  sing N N 343 
TRP CZ2 CH2  doub Y N 344 
TRP CZ2 HZ2  sing N N 345 
TRP CZ3 CH2  sing Y N 346 
TRP CZ3 HZ3  sing N N 347 
TRP CH2 HH2  sing N N 348 
TRP OXT HXT  sing N N 349 
TYR N   CA   sing N N 350 
TYR N   H    sing N N 351 
TYR N   H2   sing N N 352 
TYR CA  C    sing N N 353 
TYR CA  CB   sing N N 354 
TYR CA  HA   sing N N 355 
TYR C   O    doub N N 356 
TYR C   OXT  sing N N 357 
TYR CB  CG   sing N N 358 
TYR CB  HB2  sing N N 359 
TYR CB  HB3  sing N N 360 
TYR CG  CD1  doub Y N 361 
TYR CG  CD2  sing Y N 362 
TYR CD1 CE1  sing Y N 363 
TYR CD1 HD1  sing N N 364 
TYR CD2 CE2  doub Y N 365 
TYR CD2 HD2  sing N N 366 
TYR CE1 CZ   doub Y N 367 
TYR CE1 HE1  sing N N 368 
TYR CE2 CZ   sing Y N 369 
TYR CE2 HE2  sing N N 370 
TYR CZ  OH   sing N N 371 
TYR OH  HH   sing N N 372 
TYR OXT HXT  sing N N 373 
VAL N   CA   sing N N 374 
VAL N   H    sing N N 375 
VAL N   H2   sing N N 376 
VAL CA  C    sing N N 377 
VAL CA  CB   sing N N 378 
VAL CA  HA   sing N N 379 
VAL C   O    doub N N 380 
VAL C   OXT  sing N N 381 
VAL CB  CG1  sing N N 382 
VAL CB  CG2  sing N N 383 
VAL CB  HB   sing N N 384 
VAL CG1 HG11 sing N N 385 
VAL CG1 HG12 sing N N 386 
VAL CG1 HG13 sing N N 387 
VAL CG2 HG21 sing N N 388 
VAL CG2 HG22 sing N N 389 
VAL CG2 HG23 sing N N 390 
VAL OXT HXT  sing N N 391 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Mexico 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DDL 
_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]   0.017538 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008985 
_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]   0.015312 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   A MET A 1 1   ? 34.297 29.577  -0.251  0.48 45.63  ? 1   MET A N   1 
ATOM   2    N N   B MET A 1 1   ? 34.262 29.430  -0.151  0.52 45.45  ? 1   MET A N   1 
ATOM   3    C CA  A MET A 1 1   ? 34.104 28.772  0.946   0.48 41.38  ? 1   MET A CA  1 
ATOM   4    C CA  B MET A 1 1   ? 34.178 28.817  1.169   0.52 41.24  ? 1   MET A CA  1 
ATOM   5    C C   A MET A 1 1   ? 32.665 28.806  1.459   0.48 35.11  ? 1   MET A C   1 
ATOM   6    C C   B MET A 1 1   ? 32.750 28.881  1.721   0.52 33.89  ? 1   MET A C   1 
ATOM   7    O O   A MET A 1 1   ? 32.121 27.774  1.844   0.48 34.77  ? 1   MET A O   1 
ATOM   8    O O   B MET A 1 1   ? 32.283 27.930  2.338   0.52 34.37  ? 1   MET A O   1 
ATOM   9    C CB  A MET A 1 1   ? 35.069 29.193  2.052   0.48 44.40  ? 1   MET A CB  1 
ATOM   10   C CB  B MET A 1 1   ? 35.198 29.445  2.129   0.52 45.08  ? 1   MET A CB  1 
ATOM   11   C CG  A MET A 1 1   ? 35.105 28.188  3.175   0.48 45.18  ? 1   MET A CG  1 
ATOM   12   C CG  B MET A 1 1   ? 35.196 28.865  3.540   0.52 45.80  ? 1   MET A CG  1 
ATOM   13   S SD  A MET A 1 1   ? 35.454 28.818  4.819   0.48 48.95  ? 1   MET A SD  1 
ATOM   14   S SD  B MET A 1 1   ? 35.844 30.003  4.790   0.52 58.65  ? 1   MET A SD  1 
ATOM   15   C CE  A MET A 1 1   ? 36.209 27.360  5.526   0.48 22.31  ? 1   MET A CE  1 
ATOM   16   C CE  B MET A 1 1   ? 34.696 31.366  4.659   0.52 44.43  ? 1   MET A CE  1 
ATOM   17   N N   . ASP A 1 2   ? 32.052 29.988  1.476   1.00 35.13  ? 2   ASP A N   1 
ATOM   18   C CA  . ASP A 1 2   ? 30.631 30.104  1.806   1.00 30.70  ? 2   ASP A CA  1 
ATOM   19   C C   . ASP A 1 2   ? 29.812 29.644  0.604   1.00 25.64  ? 2   ASP A C   1 
ATOM   20   O O   . ASP A 1 2   ? 29.890 30.238  -0.471  1.00 27.88  ? 2   ASP A O   1 
ATOM   21   C CB  . ASP A 1 2   ? 30.277 31.546  2.177   1.00 35.77  ? 2   ASP A CB  1 
ATOM   22   C CG  . ASP A 1 2   ? 28.767 31.793  2.268   1.00 42.03  ? 2   ASP A CG  1 
ATOM   23   O OD1 . ASP A 1 2   ? 27.997 30.906  2.708   1.00 27.92  ? 2   ASP A OD1 1 
ATOM   24   O OD2 . ASP A 1 2   ? 28.349 32.904  1.879   1.00 54.46  ? 2   ASP A OD2 1 
ATOM   25   N N   . LEU A 1 3   ? 29.020 28.592  0.789   1.00 19.62  ? 3   LEU A N   1 
ATOM   26   C CA  . LEU A 1 3   ? 28.221 28.027  -0.297  1.00 19.41  ? 3   LEU A CA  1 
ATOM   27   C C   . LEU A 1 3   ? 26.929 28.784  -0.582  1.00 17.00  ? 3   LEU A C   1 
ATOM   28   O O   . LEU A 1 3   ? 26.229 28.433  -1.546  1.00 16.91  ? 3   LEU A O   1 
ATOM   29   C CB  . LEU A 1 3   ? 27.904 26.564  0.028   1.00 19.87  ? 3   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 3   ? 29.163 25.671  0.059   1.00 21.15  ? 3   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 3   ? 28.811 24.217  0.220   1.00 27.40  ? 3   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 3   ? 30.016 25.886  -1.192  1.00 25.29  ? 3   LEU A CD2 1 
ATOM   33   N N   . GLN A 1 4   ? 26.585 29.794  0.217   1.00 16.02  ? 4   GLN A N   1 
ATOM   34   C CA  . GLN A 1 4   ? 25.373 30.581  0.004   1.00 14.36  ? 4   GLN A CA  1 
ATOM   35   C C   . GLN A 1 4   ? 24.146 29.678  -0.047  1.00 15.73  ? 4   GLN A C   1 
ATOM   36   O O   . GLN A 1 4   ? 23.345 29.727  -0.986  1.00 14.78  ? 4   GLN A O   1 
ATOM   37   C CB  . GLN A 1 4   ? 25.459 31.453  -1.249  1.00 18.50  ? 4   GLN A CB  1 
ATOM   38   C CG  . GLN A 1 4   ? 26.650 32.389  -1.299  1.00 21.70  ? 4   GLN A CG  1 
ATOM   39   C CD  . GLN A 1 4   ? 26.840 32.947  -2.694  1.00 21.97  ? 4   GLN A CD  1 
ATOM   40   O OE1 . GLN A 1 4   ? 26.074 33.794  -3.134  1.00 28.41  ? 4   GLN A OE1 1 
ATOM   41   N NE2 . GLN A 1 4   ? 27.844 32.440  -3.412  1.00 25.69  ? 4   GLN A NE2 1 
ATOM   42   N N   . LEU A 1 5   ? 24.009 28.854  0.990   1.00 14.46  ? 5   LEU A N   1 
ATOM   43   C CA  . LEU A 1 5   ? 23.035 27.764  0.984   1.00 14.37  ? 5   LEU A CA  1 
ATOM   44   C C   . LEU A 1 5   ? 21.591 28.244  0.958   1.00 16.16  ? 5   LEU A C   1 
ATOM   45   O O   . LEU A 1 5   ? 20.727 27.517  0.459   1.00 16.08  ? 5   LEU A O   1 
ATOM   46   C CB  . LEU A 1 5   ? 23.277 26.831  2.175   1.00 15.01  ? 5   LEU A CB  1 
ATOM   47   C CG  . LEU A 1 5   ? 24.601 26.050  2.141   1.00 14.21  ? 5   LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 5   ? 24.897 25.406  3.488   1.00 16.62  ? 5   LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 5   ? 24.612 25.018  1.016   1.00 17.21  ? 5   LEU A CD2 1 
ATOM   50   N N   . LYS A 1 6   ? 21.307 29.433  1.498   1.00 15.01  ? 6   LYS A N   1 
ATOM   51   C CA  . LYS A 1 6   ? 19.958 29.983  1.396   1.00 14.90  ? 6   LYS A CA  1 
ATOM   52   C C   . LYS A 1 6   ? 19.488 30.053  -0.048  1.00 13.06  ? 6   LYS A C   1 
ATOM   53   O O   . LYS A 1 6   ? 18.330 29.743  -0.338  1.00 14.20  ? 6   LYS A O   1 
ATOM   54   C CB  . LYS A 1 6   ? 19.872 31.377  2.021   1.00 17.24  ? 6   LYS A CB  1 
ATOM   55   C CG  . LYS A 1 6   ? 18.460 31.989  2.017   1.00 21.70  ? 6   LYS A CG  1 
ATOM   56   C CD  . LYS A 1 6   ? 18.369 33.203  2.932   1.00 33.96  ? 6   LYS A CD  1 
ATOM   57   C CE  . LYS A 1 6   ? 17.421 34.260  2.384   1.00 33.55  ? 6   LYS A CE  1 
ATOM   58   N NZ  . LYS A 1 6   ? 17.392 35.481  3.256   1.00 41.47  ? 6   LYS A NZ  1 
ATOM   59   N N   A GLN A 1 7   ? 20.362 30.483  -0.956  0.67 14.46  ? 7   GLN A N   1 
ATOM   60   N N   B GLN A 1 7   ? 20.362 30.474  -0.966  0.33 14.48  ? 7   GLN A N   1 
ATOM   61   C CA  A GLN A 1 7   ? 20.021 30.609  -2.371  0.67 13.82  ? 7   GLN A CA  1 
ATOM   62   C CA  B GLN A 1 7   ? 19.997 30.615  -2.374  0.33 13.87  ? 7   GLN A CA  1 
ATOM   63   C C   A GLN A 1 7   ? 20.407 29.391  -3.204  0.67 13.16  ? 7   GLN A C   1 
ATOM   64   C C   B GLN A 1 7   ? 20.619 29.573  -3.300  0.33 14.07  ? 7   GLN A C   1 
ATOM   65   O O   A GLN A 1 7   ? 19.768 29.118  -4.225  0.67 13.88  ? 7   GLN A O   1 
ATOM   66   O O   B GLN A 1 7   ? 20.368 29.623  -4.511  0.33 16.54  ? 7   GLN A O   1 
ATOM   67   C CB  A GLN A 1 7   ? 20.676 31.864  -2.957  0.67 14.77  ? 7   GLN A CB  1 
ATOM   68   C CB  B GLN A 1 7   ? 20.286 32.029  -2.902  0.33 17.26  ? 7   GLN A CB  1 
ATOM   69   C CG  A GLN A 1 7   ? 20.137 33.153  -2.368  0.67 17.22  ? 7   GLN A CG  1 
ATOM   70   C CG  B GLN A 1 7   ? 19.678 33.161  -2.086  0.33 17.75  ? 7   GLN A CG  1 
ATOM   71   C CD  A GLN A 1 7   ? 20.708 34.381  -3.029  0.67 23.30  ? 7   GLN A CD  1 
ATOM   72   C CD  B GLN A 1 7   ? 20.654 33.733  -1.090  0.33 21.56  ? 7   GLN A CD  1 
ATOM   73   O OE1 A GLN A 1 7   ? 21.566 34.291  -3.915  0.67 31.71  ? 7   GLN A OE1 1 
ATOM   74   O OE1 B GLN A 1 7   ? 21.814 33.336  -1.059  0.33 24.39  ? 7   GLN A OE1 1 
ATOM   75   N NE2 A GLN A 1 7   ? 20.226 35.540  -2.616  0.67 24.92  ? 7   GLN A NE2 1 
ATOM   76   N NE2 B GLN A 1 7   ? 20.196 34.669  -0.268  0.33 31.35  ? 7   GLN A NE2 1 
ATOM   77   N N   . ALA A 1 8   ? 21.417 28.639  -2.783  1.00 14.85  ? 8   ALA A N   1 
ATOM   78   C CA  . ALA A 1 8   ? 21.980 27.595  -3.630  1.00 13.44  ? 8   ALA A CA  1 
ATOM   79   C C   . ALA A 1 8   ? 20.939 26.545  -4.021  1.00 13.07  ? 8   ALA A C   1 
ATOM   80   O O   . ALA A 1 8   ? 19.989 26.266  -3.289  1.00 15.43  ? 8   ALA A O   1 
ATOM   81   C CB  . ALA A 1 8   ? 23.125 26.895  -2.897  1.00 13.23  ? 8   ALA A CB  1 
ATOM   82   N N   . LYS A 1 9   ? 21.135 25.939  -5.186  1.00 12.68  ? 9   LYS A N   1 
ATOM   83   C CA  . LYS A 1 9   ? 20.328 24.788  -5.548  1.00 14.19  ? 9   LYS A CA  1 
ATOM   84   C C   . LYS A 1 9   ? 20.833 23.581  -4.765  1.00 14.10  ? 9   LYS A C   1 
ATOM   85   O O   . LYS A 1 9   ? 22.043 23.377  -4.618  1.00 14.17  ? 9   LYS A O   1 
ATOM   86   C CB  . LYS A 1 9   ? 20.416 24.522  -7.049  1.00 15.90  ? 9   LYS A CB  1 
ATOM   87   C CG  . LYS A 1 9   ? 19.649 23.269  -7.469  1.00 21.30  ? 9   LYS A CG  1 
ATOM   88   C CD  . LYS A 1 9   ? 19.641 23.104  -8.977  1.00 30.25  ? 9   LYS A CD  1 
ATOM   89   C CE  . LYS A 1 9   ? 20.811 22.271  -9.438  1.00 38.65  ? 9   LYS A CE  1 
ATOM   90   N NZ  . LYS A 1 9   ? 20.495 21.569  -10.720 1.00 40.09  ? 9   LYS A NZ  1 
ATOM   91   N N   . LEU A 1 10  ? 19.905 22.799  -4.227  1.00 13.74  ? 10  LEU A N   1 
ATOM   92   C CA  . LEU A 1 10  ? 20.273 21.678  -3.370  1.00 13.80  ? 10  LEU A CA  1 
ATOM   93   C C   . LEU A 1 10  ? 19.611 20.419  -3.889  1.00 15.07  ? 10  LEU A C   1 
ATOM   94   O O   . LEU A 1 10  ? 18.404 20.421  -4.160  1.00 16.68  ? 10  LEU A O   1 
ATOM   95   C CB  . LEU A 1 10  ? 19.783 21.896  -1.930  1.00 13.67  ? 10  LEU A CB  1 
ATOM   96   C CG  . LEU A 1 10  ? 20.267 23.156  -1.221  1.00 12.94  ? 10  LEU A CG  1 
ATOM   97   C CD1 . LEU A 1 10  ? 19.659 23.204  0.162   1.00 15.62  ? 10  LEU A CD1 1 
ATOM   98   C CD2 . LEU A 1 10  ? 21.792 23.161  -1.115  1.00 14.74  ? 10  LEU A CD2 1 
ATOM   99   N N   A ARG A 1 11  ? 20.408 19.365  -4.055  0.56 13.47  ? 11  ARG A N   1 
ATOM   100  N N   B ARG A 1 11  ? 20.380 19.338  -3.974  0.44 13.54  ? 11  ARG A N   1 
ATOM   101  C CA  A ARG A 1 11  ? 19.931 18.027  -4.388  0.56 15.02  ? 11  ARG A CA  1 
ATOM   102  C CA  B ARG A 1 11  ? 19.873 18.037  -4.405  0.44 15.05  ? 11  ARG A CA  1 
ATOM   103  C C   A ARG A 1 11  ? 20.416 17.083  -3.302  0.56 16.03  ? 11  ARG A C   1 
ATOM   104  C C   B ARG A 1 11  ? 20.398 16.988  -3.435  0.44 15.79  ? 11  ARG A C   1 
ATOM   105  O O   A ARG A 1 11  ? 21.618 17.019  -3.024  0.56 15.18  ? 11  ARG A O   1 
ATOM   106  O O   B ARG A 1 11  ? 21.610 16.754  -3.368  0.44 15.26  ? 11  ARG A O   1 
ATOM   107  C CB  A ARG A 1 11  ? 20.476 17.567  -5.742  0.56 18.54  ? 11  ARG A CB  1 
ATOM   108  C CB  B ARG A 1 11  ? 20.332 17.742  -5.832  0.44 19.43  ? 11  ARG A CB  1 
ATOM   109  C CG  A ARG A 1 11  ? 19.929 18.351  -6.921  0.56 21.03  ? 11  ARG A CG  1 
ATOM   110  C CG  B ARG A 1 11  ? 20.208 16.306  -6.266  0.44 19.73  ? 11  ARG A CG  1 
ATOM   111  C CD  A ARG A 1 11  ? 20.499 17.857  -8.247  0.56 31.64  ? 11  ARG A CD  1 
ATOM   112  C CD  B ARG A 1 11  ? 20.996 16.079  -7.542  0.44 27.03  ? 11  ARG A CD  1 
ATOM   113  N NE  A ARG A 1 11  ? 20.078 16.502  -8.574  0.56 31.97  ? 11  ARG A NE  1 
ATOM   114  N NE  B ARG A 1 11  ? 20.444 16.814  -8.670  0.44 30.34  ? 11  ARG A NE  1 
ATOM   115  C CZ  A ARG A 1 11  ? 20.899 15.516  -8.915  0.56 31.24  ? 11  ARG A CZ  1 
ATOM   116  C CZ  B ARG A 1 11  ? 19.749 16.259  -9.653  0.44 33.51  ? 11  ARG A CZ  1 
ATOM   117  N NH1 A ARG A 1 11  ? 22.207 15.694  -8.982  0.56 31.76  ? 11  ARG A NH1 1 
ATOM   118  N NH1 B ARG A 1 11  ? 19.502 14.959  -9.676  0.44 35.66  ? 11  ARG A NH1 1 
ATOM   119  N NH2 A ARG A 1 11  ? 20.392 14.322  -9.202  0.56 30.49  ? 11  ARG A NH2 1 
ATOM   120  N NH2 B ARG A 1 11  ? 19.290 17.026  -10.638 0.44 42.08  ? 11  ARG A NH2 1 
ATOM   121  N N   . LEU A 1 12  ? 19.490 16.366  -2.679  1.00 13.78  ? 12  LEU A N   1 
ATOM   122  C CA  . LEU A 1 12  ? 19.837 15.367  -1.675  1.00 14.29  ? 12  LEU A CA  1 
ATOM   123  C C   . LEU A 1 12  ? 19.753 14.001  -2.341  1.00 15.44  ? 12  LEU A C   1 
ATOM   124  O O   . LEU A 1 12  ? 18.714 13.654  -2.913  1.00 16.98  ? 12  LEU A O   1 
ATOM   125  C CB  . LEU A 1 12  ? 18.865 15.432  -0.495  1.00 13.59  ? 12  LEU A CB  1 
ATOM   126  C CG  . LEU A 1 12  ? 19.105 14.385  0.590   1.00 14.90  ? 12  LEU A CG  1 
ATOM   127  C CD1 . LEU A 1 12  ? 20.450 14.648  1.281   1.00 16.30  ? 12  LEU A CD1 1 
ATOM   128  C CD2 . LEU A 1 12  ? 17.943 14.403  1.588   1.00 17.90  ? 12  LEU A CD2 1 
ATOM   129  N N   . LEU A 1 13  ? 20.843 13.231  -2.276  1.00 15.28  ? 13  LEU A N   1 
ATOM   130  C CA  . LEU A 1 13  ? 20.891 11.875  -2.815  1.00 16.68  ? 13  LEU A CA  1 
ATOM   131  C C   . LEU A 1 13  ? 20.918 10.910  -1.635  1.00 15.80  ? 13  LEU A C   1 
ATOM   132  O O   . LEU A 1 13  ? 21.846 10.944  -0.821  1.00 16.03  ? 13  LEU A O   1 
ATOM   133  C CB  . LEU A 1 13  ? 22.146 11.650  -3.657  1.00 18.07  ? 13  LEU A CB  1 
ATOM   134  C CG  . LEU A 1 13  ? 22.486 12.551  -4.838  1.00 26.41  ? 13  LEU A CG  1 
ATOM   135  C CD1 . LEU A 1 13  ? 23.257 11.758  -5.892  1.00 33.32  ? 13  LEU A CD1 1 
ATOM   136  C CD2 . LEU A 1 13  ? 21.273 13.141  -5.439  1.00 32.74  ? 13  LEU A CD2 1 
ATOM   137  N N   . TYR A 1 14  ? 19.909 10.047  -1.553  1.00 16.10  ? 14  TYR A N   1 
ATOM   138  C CA  . TYR A 1 14  ? 19.866 9.010   -0.532  1.00 19.06  ? 14  TYR A CA  1 
ATOM   139  C C   . TYR A 1 14  ? 18.943 7.906   -1.030  1.00 22.48  ? 14  TYR A C   1 
ATOM   140  O O   . TYR A 1 14  ? 18.332 8.016   -2.091  1.00 23.07  ? 14  TYR A O   1 
ATOM   141  C CB  . TYR A 1 14  ? 19.378 9.594   0.801   1.00 17.18  ? 14  TYR A CB  1 
ATOM   142  C CG  . TYR A 1 14  ? 19.543 8.662   1.989   1.00 17.61  ? 14  TYR A CG  1 
ATOM   143  C CD1 . TYR A 1 14  ? 20.810 8.255   2.404   1.00 18.75  ? 14  TYR A CD1 1 
ATOM   144  C CD2 . TYR A 1 14  ? 18.435 8.209   2.722   1.00 19.80  ? 14  TYR A CD2 1 
ATOM   145  C CE1 . TYR A 1 14  ? 20.979 7.412   3.498   1.00 19.28  ? 14  TYR A CE1 1 
ATOM   146  C CE2 . TYR A 1 14  ? 18.598 7.361   3.819   1.00 21.22  ? 14  TYR A CE2 1 
ATOM   147  C CZ  . TYR A 1 14  ? 19.867 6.968   4.196   1.00 19.84  ? 14  TYR A CZ  1 
ATOM   148  O OH  . TYR A 1 14  ? 20.035 6.136   5.291   1.00 21.60  ? 14  TYR A OH  1 
ATOM   149  N N   . PHE A 1 15  ? 18.817 6.852   -0.234  1.00 27.60  ? 15  PHE A N   1 
ATOM   150  C CA  . PHE A 1 15  ? 17.909 5.759   -0.548  1.00 24.08  ? 15  PHE A CA  1 
ATOM   151  C C   . PHE A 1 15  ? 16.460 6.157   -0.268  1.00 28.21  ? 15  PHE A C   1 
ATOM   152  O O   . PHE A 1 15  ? 16.177 7.181   0.359   1.00 24.50  ? 15  PHE A O   1 
ATOM   153  C CB  . PHE A 1 15  ? 18.326 4.529   0.255   1.00 26.03  ? 15  PHE A CB  1 
ATOM   154  C CG  . PHE A 1 15  ? 19.769 4.158   0.054   1.00 30.40  ? 15  PHE A CG  1 
ATOM   155  C CD1 . PHE A 1 15  ? 20.191 3.586   -1.138  1.00 31.02  ? 15  PHE A CD1 1 
ATOM   156  C CD2 . PHE A 1 15  ? 20.714 4.422   1.031   1.00 27.47  ? 15  PHE A CD2 1 
ATOM   157  C CE1 . PHE A 1 15  ? 21.519 3.263   -1.333  1.00 31.27  ? 15  PHE A CE1 1 
ATOM   158  C CE2 . PHE A 1 15  ? 22.039 4.104   0.838   1.00 30.55  ? 15  PHE A CE2 1 
ATOM   159  C CZ  . PHE A 1 15  ? 22.442 3.524   -0.346  1.00 36.17  ? 15  PHE A CZ  1 
ATOM   160  N N   . ASN A 1 16  ? 15.517 5.341   -0.751  1.00 25.60  ? 16  ASN A N   1 
ATOM   161  C CA  . ASN A 1 16  ? 14.099 5.657   -0.576  1.00 25.16  ? 16  ASN A CA  1 
ATOM   162  C C   . ASN A 1 16  ? 13.590 5.117   0.763   1.00 30.54  ? 16  ASN A C   1 
ATOM   163  O O   . ASN A 1 16  ? 12.682 4.282   0.868   1.00 27.65  ? 16  ASN A O   1 
ATOM   164  C CB  . ASN A 1 16  ? 13.265 5.188   -1.763  1.00 33.55  ? 16  ASN A CB  1 
ATOM   165  C CG  . ASN A 1 16  ? 11.775 5.373   -1.535  1.00 42.35  ? 16  ASN A CG  1 
ATOM   166  O OD1 . ASN A 1 16  ? 11.329 6.437   -1.090  1.00 37.01  ? 16  ASN A OD1 1 
ATOM   167  N ND2 . ASN A 1 16  ? 10.995 4.339   -1.830  1.00 48.57  ? 16  ASN A ND2 1 
ATOM   168  N N   . ILE A 1 17  ? 14.227 5.618   1.817   1.00 23.38  ? 17  ILE A N   1 
ATOM   169  C CA  . ILE A 1 17  ? 13.857 5.324   3.192   1.00 21.29  ? 17  ILE A CA  1 
ATOM   170  C C   . ILE A 1 17  ? 14.080 6.599   3.993   1.00 23.35  ? 17  ILE A C   1 
ATOM   171  O O   . ILE A 1 17  ? 14.719 7.545   3.527   1.00 24.06  ? 17  ILE A O   1 
ATOM   172  C CB  . ILE A 1 17  ? 14.689 4.170   3.803   1.00 26.07  ? 17  ILE A CB  1 
ATOM   173  C CG1 . ILE A 1 17  ? 16.184 4.489   3.754   1.00 28.21  ? 17  ILE A CG1 1 
ATOM   174  C CG2 . ILE A 1 17  ? 14.416 2.856   3.084   1.00 32.19  ? 17  ILE A CG2 1 
ATOM   175  C CD1 . ILE A 1 17  ? 17.040 3.646   4.697   1.00 30.94  ? 17  ILE A CD1 1 
ATOM   176  N N   A ARG A 1 18  ? 13.532 6.624   5.205   0.64 22.33  ? 18  ARG A N   1 
ATOM   177  N N   C ARG A 1 18  ? 13.548 6.615   5.214   0.36 22.36  ? 18  ARG A N   1 
ATOM   178  C CA  A ARG A 1 18  ? 13.865 7.697   6.139   0.64 20.75  ? 18  ARG A CA  1 
ATOM   179  C CA  C ARG A 1 18  ? 13.867 7.690   6.145   0.36 20.82  ? 18  ARG A CA  1 
ATOM   180  C C   A ARG A 1 18  ? 15.338 7.622   6.519   0.64 20.32  ? 18  ARG A C   1 
ATOM   181  C C   C ARG A 1 18  ? 15.347 7.605   6.489   0.36 20.35  ? 18  ARG A C   1 
ATOM   182  O O   A ARG A 1 18  ? 16.125 8.520   6.195   0.64 20.62  ? 18  ARG A O   1 
ATOM   183  O O   C ARG A 1 18  ? 16.129 8.489   6.127   0.36 20.62  ? 18  ARG A O   1 
ATOM   184  C CB  A ARG A 1 18  ? 12.963 7.616   7.370   0.64 20.00  ? 18  ARG A CB  1 
ATOM   185  C CB  C ARG A 1 18  ? 13.000 7.594   7.402   0.36 20.11  ? 18  ARG A CB  1 
ATOM   186  C CG  A ARG A 1 18  ? 11.473 7.765   7.077   0.64 24.56  ? 18  ARG A CG  1 
ATOM   187  C CG  C ARG A 1 18  ? 11.677 8.327   7.289   0.36 26.44  ? 18  ARG A CG  1 
ATOM   188  C CD  A ARG A 1 18  ? 10.661 7.723   8.372   0.64 25.61  ? 18  ARG A CD  1 
ATOM   189  C CD  C ARG A 1 18  ? 10.537 7.510   7.854   0.36 28.26  ? 18  ARG A CD  1 
ATOM   190  N NE  A ARG A 1 18  ? 10.993 6.541   9.153   0.64 29.70  ? 18  ARG A NE  1 
ATOM   191  N NE  C ARG A 1 18  ? 9.385  7.533   6.963   0.36 28.16  ? 18  ARG A NE  1 
ATOM   192  C CZ  A ARG A 1 18  ? 10.395 5.366   9.018   0.64 37.17  ? 18  ARG A CZ  1 
ATOM   193  C CZ  C ARG A 1 18  ? 8.151  7.217   7.327   0.36 32.17  ? 18  ARG A CZ  1 
ATOM   194  N NH1 A ARG A 1 18  ? 9.395  5.193   8.170   0.64 34.76  ? 18  ARG A NH1 1 
ATOM   195  N NH1 C ARG A 1 18  ? 7.869  6.844   8.565   0.36 38.12  ? 18  ARG A NH1 1 
ATOM   196  N NH2 A ARG A 1 18  ? 10.813 4.340   9.751   0.64 31.02  ? 18  ARG A NH2 1 
ATOM   197  N NH2 C ARG A 1 18  ? 7.176  7.273   6.425   0.36 31.07  ? 18  ARG A NH2 1 
ATOM   198  N N   . GLY A 1 19  ? 15.737 6.526   7.162   1.00 20.55  ? 19  GLY A N   1 
ATOM   199  C CA  . GLY A 1 19  ? 17.128 6.260   7.463   1.00 19.69  ? 19  GLY A CA  1 
ATOM   200  C C   . GLY A 1 19  ? 17.878 7.452   8.020   1.00 18.29  ? 19  GLY A C   1 
ATOM   201  O O   . GLY A 1 19  ? 17.372 8.210   8.858   1.00 20.85  ? 19  GLY A O   1 
ATOM   202  N N   . ARG A 1 20  ? 19.091 7.635   7.528   1.00 19.12  ? 20  ARG A N   1 
ATOM   203  C CA  . ARG A 1 20  ? 20.009 8.628   8.067   1.00 19.44  ? 20  ARG A CA  1 
ATOM   204  C C   . ARG A 1 20  ? 19.937 9.957   7.328   1.00 20.16  ? 20  ARG A C   1 
ATOM   205  O O   . ARG A 1 20  ? 20.654 10.893  7.705   1.00 23.60  ? 20  ARG A O   1 
ATOM   206  C CB  . ARG A 1 20  ? 21.435 8.059   8.046   1.00 22.35  ? 20  ARG A CB  1 
ATOM   207  C CG  . ARG A 1 20  ? 21.551 6.761   8.866   1.00 21.82  ? 20  ARG A CG  1 
ATOM   208  C CD  . ARG A 1 20  ? 23.000 6.276   8.972   1.00 24.67  ? 20  ARG A CD  1 
ATOM   209  N NE  . ARG A 1 20  ? 23.104 5.094   9.827   1.00 27.29  ? 20  ARG A NE  1 
ATOM   210  C CZ  . ARG A 1 20  ? 22.794 3.860   9.443   1.00 31.18  ? 20  ARG A CZ  1 
ATOM   211  N NH1 . ARG A 1 20  ? 22.387 3.599   8.209   1.00 28.51  ? 20  ARG A NH1 1 
ATOM   212  N NH2 . ARG A 1 20  ? 22.899 2.860   10.318  1.00 27.92  ? 20  ARG A NH2 1 
ATOM   213  N N   . ALA A 1 21  ? 19.091 10.069  6.294   1.00 18.65  ? 21  ALA A N   1 
ATOM   214  C CA  . ALA A 1 21  ? 18.882 11.349  5.620   1.00 19.77  ? 21  ALA A CA  1 
ATOM   215  C C   . ALA A 1 21  ? 17.613 12.056  6.055   1.00 18.06  ? 21  ALA A C   1 
ATOM   216  O O   . ALA A 1 21  ? 17.427 13.232  5.702   1.00 15.75  ? 21  ALA A O   1 
ATOM   217  C CB  . ALA A 1 21  ? 18.834 11.181  4.096   1.00 19.42  ? 21  ALA A CB  1 
ATOM   218  N N   A GLU A 1 22  ? 16.734 11.388  6.807   0.97 15.66  ? 22  GLU A N   1 
ATOM   219  N N   B GLU A 1 22  ? 16.741 11.381  6.810   0.03 15.81  ? 22  GLU A N   1 
ATOM   220  C CA  A GLU A 1 22  ? 15.477 12.017  7.186   0.97 15.69  ? 22  GLU A CA  1 
ATOM   221  C CA  B GLU A 1 22  ? 15.474 11.984  7.212   0.03 15.79  ? 22  GLU A CA  1 
ATOM   222  C C   A GLU A 1 22  ? 15.718 13.311  7.953   0.97 14.73  ? 22  GLU A C   1 
ATOM   223  C C   B GLU A 1 22  ? 15.681 13.266  8.007   0.03 14.79  ? 22  GLU A C   1 
ATOM   224  O O   A GLU A 1 22  ? 14.993 14.292  7.763   0.97 13.81  ? 22  GLU A O   1 
ATOM   225  O O   B GLU A 1 22  ? 14.875 14.197  7.902   0.03 14.26  ? 22  GLU A O   1 
ATOM   226  C CB  A GLU A 1 22  ? 14.596 11.035  7.979   0.97 15.69  ? 22  GLU A CB  1 
ATOM   227  C CB  B GLU A 1 22  ? 14.650 10.983  8.022   0.03 15.90  ? 22  GLU A CB  1 
ATOM   228  C CG  A GLU A 1 22  ? 13.133 11.481  8.055   0.97 16.94  ? 22  GLU A CG  1 
ATOM   229  C CG  B GLU A 1 22  ? 13.161 11.296  8.085   0.03 17.44  ? 22  GLU A CG  1 
ATOM   230  C CD  A GLU A 1 22  ? 12.419 11.507  6.683   0.97 22.51  ? 22  GLU A CD  1 
ATOM   231  C CD  B GLU A 1 22  ? 12.652 11.988  6.835   0.03 20.03  ? 22  GLU A CD  1 
ATOM   232  O OE1 A GLU A 1 22  ? 12.915 10.938  5.691   0.97 21.90  ? 22  GLU A OE1 1 
ATOM   233  O OE1 B GLU A 1 22  ? 12.490 11.308  5.800   0.03 19.64  ? 22  GLU A OE1 1 
ATOM   234  O OE2 A GLU A 1 22  ? 11.322 12.086  6.597   0.97 23.74  ? 22  GLU A OE2 1 
ATOM   235  O OE2 B GLU A 1 22  ? 12.408 13.211  6.889   0.03 18.53  ? 22  GLU A OE2 1 
ATOM   236  N N   . LEU A 1 23  ? 16.751 13.339  8.799   1.00 13.93  ? 23  LEU A N   1 
ATOM   237  C CA  . LEU A 1 23  ? 17.029 14.560  9.542   1.00 14.33  ? 23  LEU A CA  1 
ATOM   238  C C   . LEU A 1 23  ? 17.321 15.727  8.604   1.00 12.29  ? 23  LEU A C   1 
ATOM   239  O O   . LEU A 1 23  ? 16.867 16.847  8.854   1.00 13.32  ? 23  LEU A O   1 
ATOM   240  C CB  . LEU A 1 23  ? 18.189 14.327  10.503  1.00 12.84  ? 23  LEU A CB  1 
ATOM   241  C CG  . LEU A 1 23  ? 18.508 15.515  11.410  1.00 12.21  ? 23  LEU A CG  1 
ATOM   242  C CD1 . LEU A 1 23  ? 17.338 15.929  12.276  1.00 15.11  ? 23  LEU A CD1 1 
ATOM   243  C CD2 . LEU A 1 23  ? 19.740 15.176  12.254  1.00 14.14  ? 23  LEU A CD2 1 
ATOM   244  N N   . ILE A 1 24  ? 18.054 15.482  7.516   1.00 13.51  ? 24  ILE A N   1 
ATOM   245  C CA  . ILE A 1 24  ? 18.314 16.538  6.536   1.00 12.32  ? 24  ILE A CA  1 
ATOM   246  C C   . ILE A 1 24  ? 17.018 16.998  5.879   1.00 12.22  ? 24  ILE A C   1 
ATOM   247  O O   . ILE A 1 24  ? 16.779 18.208  5.704   1.00 12.91  ? 24  ILE A O   1 
ATOM   248  C CB  . ILE A 1 24  ? 19.346 16.069  5.495   1.00 12.14  ? 24  ILE A CB  1 
ATOM   249  C CG1 . ILE A 1 24  ? 20.691 15.792  6.178   1.00 14.27  ? 24  ILE A CG1 1 
ATOM   250  C CG2 . ILE A 1 24  ? 19.500 17.123  4.387   1.00 12.93  ? 24  ILE A CG2 1 
ATOM   251  C CD1 . ILE A 1 24  ? 21.627 14.927  5.328   1.00 15.30  ? 24  ILE A CD1 1 
ATOM   252  N N   . ARG A 1 25  ? 16.168 16.048  5.477   1.00 13.72  ? 25  ARG A N   1 
ATOM   253  C CA  . ARG A 1 25  ? 14.889 16.408  4.877   1.00 12.32  ? 25  ARG A CA  1 
ATOM   254  C C   . ARG A 1 25  ? 14.048 17.228  5.846   1.00 11.96  ? 25  ARG A C   1 
ATOM   255  O O   . ARG A 1 25  ? 13.391 18.199  5.446   1.00 13.31  ? 25  ARG A O   1 
ATOM   256  C CB  . ARG A 1 25  ? 14.131 15.144  4.455   1.00 14.39  ? 25  ARG A CB  1 
ATOM   257  C CG  . ARG A 1 25  ? 14.913 14.251  3.490   1.00 15.17  ? 25  ARG A CG  1 
ATOM   258  C CD  . ARG A 1 25  ? 14.047 13.083  3.022   1.00 16.65  ? 25  ARG A CD  1 
ATOM   259  N NE  . ARG A 1 25  ? 14.742 12.210  2.078   1.00 16.10  ? 25  ARG A NE  1 
ATOM   260  C CZ  . ARG A 1 25  ? 14.981 10.929  2.308   1.00 16.52  ? 25  ARG A CZ  1 
ATOM   261  N NH1 . ARG A 1 25  ? 14.651 10.364  3.457   1.00 19.36  ? 25  ARG A NH1 1 
ATOM   262  N NH2 . ARG A 1 25  ? 15.538 10.189  1.350   1.00 18.65  ? 25  ARG A NH2 1 
ATOM   263  N N   . LEU A 1 26  ? 14.104 16.890  7.141   1.00 13.14  ? 26  LEU A N   1 
ATOM   264  C CA  . LEU A 1 26  ? 13.327 17.636  8.127   1.00 12.89  ? 26  LEU A CA  1 
ATOM   265  C C   . LEU A 1 26  ? 13.849 19.062  8.308   1.00 12.19  ? 26  LEU A C   1 
ATOM   266  O O   . LEU A 1 26  ? 13.052 19.990  8.466   1.00 13.23  ? 26  LEU A O   1 
ATOM   267  C CB  . LEU A 1 26  ? 13.330 16.895  9.465   1.00 11.39  ? 26  LEU A CB  1 
ATOM   268  C CG  . LEU A 1 26  ? 12.480 15.620  9.464   1.00 12.12  ? 26  LEU A CG  1 
ATOM   269  C CD1 . LEU A 1 26  ? 12.786 14.754  10.689  1.00 14.88  ? 26  LEU A CD1 1 
ATOM   270  C CD2 . LEU A 1 26  ? 11.022 16.020  9.440   1.00 15.26  ? 26  LEU A CD2 1 
ATOM   271  N N   . VAL A 1 27  ? 15.176 19.251  8.332   1.00 12.48  ? 27  VAL A N   1 
ATOM   272  C CA  . VAL A 1 27  ? 15.732 20.606  8.439   1.00 12.36  ? 27  VAL A CA  1 
ATOM   273  C C   . VAL A 1 27  ? 15.274 21.456  7.266   1.00 11.90  ? 27  VAL A C   1 
ATOM   274  O O   . VAL A 1 27  ? 14.847 22.607  7.444   1.00 12.91  ? 27  VAL A O   1 
ATOM   275  C CB  . VAL A 1 27  ? 17.272 20.574  8.494   1.00 13.01  ? 27  VAL A CB  1 
ATOM   276  C CG1 . VAL A 1 27  ? 17.842 22.019  8.353   1.00 15.27  ? 27  VAL A CG1 1 
ATOM   277  C CG2 . VAL A 1 27  ? 17.737 19.941  9.762   1.00 14.12  ? 27  VAL A CG2 1 
ATOM   278  N N   . LEU A 1 28  ? 15.405 20.927  6.045   1.00 12.00  ? 28  LEU A N   1 
ATOM   279  C CA  . LEU A 1 28  ? 15.099 21.729  4.861   1.00 11.51  ? 28  LEU A CA  1 
ATOM   280  C C   . LEU A 1 28  ? 13.609 22.049  4.802   1.00 12.84  ? 28  LEU A C   1 
ATOM   281  O O   . LEU A 1 28  ? 13.213 23.171  4.456   1.00 14.18  ? 28  LEU A O   1 
ATOM   282  C CB  . LEU A 1 28  ? 15.550 20.973  3.609   1.00 12.11  ? 28  LEU A CB  1 
ATOM   283  C CG  . LEU A 1 28  ? 17.075 20.902  3.521   1.00 12.21  ? 28  LEU A CG  1 
ATOM   284  C CD1 . LEU A 1 28  ? 17.500 19.950  2.396   1.00 14.31  ? 28  LEU A CD1 1 
ATOM   285  C CD2 . LEU A 1 28  ? 17.653 22.301  3.299   1.00 15.36  ? 28  LEU A CD2 1 
ATOM   286  N N   . ASN A 1 29  ? 12.762 21.086  5.175   1.00 13.07  ? 29  ASN A N   1 
ATOM   287  C CA  . ASN A 1 29  ? 11.330 21.361  5.192   1.00 13.38  ? 29  ASN A CA  1 
ATOM   288  C C   . ASN A 1 29  ? 10.950 22.315  6.317   1.00 13.42  ? 29  ASN A C   1 
ATOM   289  O O   . ASN A 1 29  ? 10.091 23.201  6.128   1.00 13.55  ? 29  ASN A O   1 
ATOM   290  C CB  . ASN A 1 29  ? 10.542 20.063  5.252   1.00 13.15  ? 29  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 29  ? 10.370 19.438  3.879   1.00 15.25  ? 29  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 29  ? 9.475  19.823  3.126   1.00 17.85  ? 29  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 29  ? 11.221 18.481  3.546   1.00 13.51  ? 29  ASN A ND2 1 
ATOM   294  N N   . ALA A 1 30  ? 11.596 22.200  7.477   1.00 12.08  ? 30  ALA A N   1 
ATOM   295  C CA  . ALA A 1 30  ? 11.371 23.179  8.538   1.00 13.91  ? 30  ALA A CA  1 
ATOM   296  C C   . ALA A 1 30  ? 11.731 24.589  8.080   1.00 14.69  ? 30  ALA A C   1 
ATOM   297  O O   . ALA A 1 30  ? 11.040 25.564  8.428   1.00 14.46  ? 30  ALA A O   1 
ATOM   298  C CB  . ALA A 1 30  ? 12.203 22.805  9.761   1.00 14.95  ? 30  ALA A CB  1 
ATOM   299  N N   . ALA A 1 31  ? 12.833 24.735  7.343   1.00 12.72  ? 31  ALA A N   1 
ATOM   300  C CA  . ALA A 1 31  ? 13.254 26.034  6.825   1.00 12.70  ? 31  ALA A CA  1 
ATOM   301  C C   . ALA A 1 31  ? 12.471 26.462  5.590   1.00 14.29  ? 31  ALA A C   1 
ATOM   302  O O   . ALA A 1 31  ? 12.657 27.592  5.122   1.00 16.30  ? 31  ALA A O   1 
ATOM   303  C CB  . ALA A 1 31  ? 14.735 25.957  6.444   1.00 15.53  ? 31  ALA A CB  1 
ATOM   304  N N   . GLU A 1 32  ? 11.634 25.581  5.037   1.00 12.77  ? 32  GLU A N   1 
ATOM   305  C CA  . GLU A 1 32  ? 10.941 25.826  3.776   1.00 12.97  ? 32  GLU A CA  1 
ATOM   306  C C   . GLU A 1 32  ? 11.926 26.222  2.686   1.00 14.34  ? 32  GLU A C   1 
ATOM   307  O O   . GLU A 1 32  ? 11.708 27.158  1.905   1.00 17.17  ? 32  GLU A O   1 
ATOM   308  C CB  . GLU A 1 32  ? 9.806  26.842  3.949   1.00 14.49  ? 32  GLU A CB  1 
ATOM   309  C CG  . GLU A 1 32  ? 8.718  26.216  4.856   1.00 15.29  ? 32  GLU A CG  1 
ATOM   310  C CD  . GLU A 1 32  ? 7.530  27.105  5.115   1.00 19.86  ? 32  GLU A CD  1 
ATOM   311  O OE1 . GLU A 1 32  ? 7.562  28.301  4.762   1.00 20.39  ? 32  GLU A OE1 1 
ATOM   312  O OE2 . GLU A 1 32  ? 6.548  26.583  5.691   1.00 17.74  ? 32  GLU A OE2 1 
ATOM   313  N N   . LYS A 1 33  ? 13.032 25.491  2.645   1.00 14.79  ? 33  LYS A N   1 
ATOM   314  C CA  . LYS A 1 33  ? 14.012 25.601  1.575   1.00 12.76  ? 33  LYS A CA  1 
ATOM   315  C C   . LYS A 1 33  ? 13.785 24.449  0.601   1.00 12.22  ? 33  LYS A C   1 
ATOM   316  O O   . LYS A 1 33  ? 13.840 23.265  0.974   1.00 15.16  ? 33  LYS A O   1 
ATOM   317  C CB  . LYS A 1 33  ? 15.416 25.562  2.175   1.00 13.17  ? 33  LYS A CB  1 
ATOM   318  C CG  . LYS A 1 33  ? 16.533 25.308  1.159   1.00 14.35  ? 33  LYS A CG  1 
ATOM   319  C CD  . LYS A 1 33  ? 16.679 26.515  0.189   1.00 12.69  ? 33  LYS A CD  1 
ATOM   320  C CE  . LYS A 1 33  ? 17.823 26.206  -0.772  1.00 13.51  ? 33  LYS A CE  1 
ATOM   321  N NZ  . LYS A 1 33  ? 17.994 27.335  -1.755  1.00 14.64  ? 33  LYS A NZ  1 
ATOM   322  N N   . ASP A 1 34  ? 13.519 24.775  -0.656  1.00 14.14  ? 34  ASP A N   1 
ATOM   323  C CA  . ASP A 1 34  ? 13.276 23.725  -1.632  1.00 14.01  ? 34  ASP A CA  1 
ATOM   324  C C   . ASP A 1 34  ? 14.553 22.961  -1.952  1.00 15.55  ? 34  ASP A C   1 
ATOM   325  O O   . ASP A 1 34  ? 15.665 23.493  -1.909  1.00 14.36  ? 34  ASP A O   1 
ATOM   326  C CB  . ASP A 1 34  ? 12.719 24.318  -2.927  1.00 18.05  ? 34  ASP A CB  1 
ATOM   327  C CG  . ASP A 1 34  ? 11.297 24.817  -2.775  1.00 25.04  ? 34  ASP A CG  1 
ATOM   328  O OD1 . ASP A 1 34  ? 10.705 24.589  -1.704  1.00 31.07  ? 34  ASP A OD1 1 
ATOM   329  O OD2 . ASP A 1 34  ? 10.787 25.444  -3.722  1.00 30.63  ? 34  ASP A OD2 1 
ATOM   330  N N   . PHE A 1 35  ? 14.386 21.685  -2.280  1.00 14.94  ? 35  PHE A N   1 
ATOM   331  C CA  . PHE A 1 35  ? 15.499 20.835  -2.677  1.00 14.11  ? 35  PHE A CA  1 
ATOM   332  C C   . PHE A 1 35  ? 14.950 19.678  -3.483  1.00 16.51  ? 35  PHE A C   1 
ATOM   333  O O   . PHE A 1 35  ? 13.770 19.331  -3.361  1.00 17.36  ? 35  PHE A O   1 
ATOM   334  C CB  . PHE A 1 35  ? 16.308 20.340  -1.464  1.00 13.35  ? 35  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 35  ? 15.564 19.373  -0.568  1.00 13.58  ? 35  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 35  ? 14.590 19.838  0.315   1.00 13.38  ? 35  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 35  ? 15.840 18.005  -0.614  1.00 13.00  ? 35  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 35  ? 13.895 18.939  1.141   1.00 14.32  ? 35  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 35  ? 15.160 17.102  0.203   1.00 15.99  ? 35  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 35  ? 14.197 17.587  1.095   1.00 15.37  ? 35  PHE A CZ  1 
ATOM   341  N N   . GLU A 1 36  ? 15.794 19.118  -4.340  1.00 14.43  ? 36  GLU A N   1 
ATOM   342  C CA  . GLU A 1 36  ? 15.426 17.886  -5.029  1.00 16.24  ? 36  GLU A CA  1 
ATOM   343  C C   . GLU A 1 36  ? 15.715 16.704  -4.113  1.00 15.88  ? 36  GLU A C   1 
ATOM   344  O O   . GLU A 1 36  ? 16.868 16.472  -3.729  1.00 16.48  ? 36  GLU A O   1 
ATOM   345  C CB  . GLU A 1 36  ? 16.208 17.758  -6.326  1.00 18.02  ? 36  GLU A CB  1 
ATOM   346  C CG  . GLU A 1 36  ? 15.993 18.896  -7.295  1.00 24.05  ? 36  GLU A CG  1 
ATOM   347  C CD  . GLU A 1 36  ? 16.660 18.612  -8.624  1.00 37.87  ? 36  GLU A CD  1 
ATOM   348  O OE1 . GLU A 1 36  ? 16.889 17.417  -8.916  1.00 37.72  ? 36  GLU A OE1 1 
ATOM   349  O OE2 . GLU A 1 36  ? 16.948 19.572  -9.368  1.00 35.36  ? 36  GLU A OE2 1 
ATOM   350  N N   . ASP A 1 37  ? 14.661 15.997  -3.716  1.00 16.40  ? 37  ASP A N   1 
ATOM   351  C CA  . ASP A 1 37  ? 14.771 14.843  -2.827  1.00 16.85  ? 37  ASP A CA  1 
ATOM   352  C C   . ASP A 1 37  ? 14.897 13.604  -3.713  1.00 17.95  ? 37  ASP A C   1 
ATOM   353  O O   . ASP A 1 37  ? 13.911 12.932  -4.025  1.00 21.63  ? 37  ASP A O   1 
ATOM   354  C CB  . ASP A 1 37  ? 13.516 14.784  -1.965  1.00 17.05  ? 37  ASP A CB  1 
ATOM   355  C CG  . ASP A 1 37  ? 13.625 13.809  -0.807  1.00 19.50  ? 37  ASP A CG  1 
ATOM   356  O OD1 . ASP A 1 37  ? 14.735 13.322  -0.510  1.00 19.46  ? 37  ASP A OD1 1 
ATOM   357  O OD2 . ASP A 1 37  ? 12.577 13.544  -0.178  1.00 23.90  ? 37  ASP A OD2 1 
ATOM   358  N N   A VAL A 1 38  ? 16.094 13.345  -4.204  0.00 15.45  ? 38  VAL A N   1 
ATOM   359  N N   B VAL A 1 38  ? 16.148 13.271  -4.070  1.00 15.15  ? 38  VAL A N   1 
ATOM   360  C CA  A VAL A 1 38  ? 16.269 12.217  -5.108  0.00 16.54  ? 38  VAL A CA  1 
ATOM   361  C CA  B VAL A 1 38  ? 16.460 12.198  -5.025  1.00 15.40  ? 38  VAL A CA  1 
ATOM   362  C C   A VAL A 1 38  ? 16.515 10.956  -4.291  0.00 18.55  ? 38  VAL A C   1 
ATOM   363  C C   B VAL A 1 38  ? 16.610 10.880  -4.285  1.00 18.37  ? 38  VAL A C   1 
ATOM   364  O O   A VAL A 1 38  ? 17.384 10.922  -3.408  0.00 20.39  ? 38  VAL A O   1 
ATOM   365  O O   B VAL A 1 38  ? 17.556 10.691  -3.508  1.00 19.80  ? 38  VAL A O   1 
ATOM   366  C CB  A VAL A 1 38  ? 17.356 12.485  -6.165  0.00 19.61  ? 38  VAL A CB  1 
ATOM   367  C CB  B VAL A 1 38  ? 17.740 12.517  -5.811  1.00 18.20  ? 38  VAL A CB  1 
ATOM   368  C CG1 A VAL A 1 38  ? 17.959 13.874  -5.982  0.00 19.94  ? 38  VAL A CG1 1 
ATOM   369  C CG1 B VAL A 1 38  ? 18.068 11.398  -6.803  1.00 21.94  ? 38  VAL A CG1 1 
ATOM   370  C CG2 A VAL A 1 38  ? 18.404 11.371  -6.208  0.00 20.73  ? 38  VAL A CG2 1 
ATOM   371  C CG2 B VAL A 1 38  ? 17.590 13.851  -6.521  1.00 20.39  ? 38  VAL A CG2 1 
ATOM   372  N N   . ARG A 1 39  ? 15.696 9.944   -4.545  1.00 22.01  ? 39  ARG A N   1 
ATOM   373  C CA  . ARG A 1 39  ? 15.680 8.688   -3.805  1.00 22.58  ? 39  ARG A CA  1 
ATOM   374  C C   . ARG A 1 39  ? 16.200 7.596   -4.728  1.00 24.16  ? 39  ARG A C   1 
ATOM   375  O O   . ARG A 1 39  ? 15.613 7.348   -5.788  1.00 30.39  ? 39  ARG A O   1 
ATOM   376  C CB  . ARG A 1 39  ? 14.273 8.390   -3.282  1.00 22.52  ? 39  ARG A CB  1 
ATOM   377  C CG  . ARG A 1 39  ? 13.897 9.301   -2.109  1.00 24.51  ? 39  ARG A CG  1 
ATOM   378  C CD  . ARG A 1 39  ? 12.390 9.387   -1.846  1.00 26.92  ? 39  ARG A CD  1 
ATOM   379  N NE  . ARG A 1 39  ? 12.108 10.417  -0.855  1.00 27.02  ? 39  ARG A NE  1 
ATOM   380  C CZ  . ARG A 1 39  ? 11.839 10.169  0.420   1.00 25.99  ? 39  ARG A CZ  1 
ATOM   381  N NH1 . ARG A 1 39  ? 11.750 8.929   0.876   1.00 27.81  ? 39  ARG A NH1 1 
ATOM   382  N NH2 . ARG A 1 39  ? 11.664 11.190  1.259   1.00 23.81  ? 39  ARG A NH2 1 
ATOM   383  N N   . VAL A 1 40  ? 17.311 6.978   -4.331  1.00 23.89  ? 40  VAL A N   1 
ATOM   384  C CA  . VAL A 1 40  ? 18.102 6.072   -5.163  1.00 26.67  ? 40  VAL A CA  1 
ATOM   385  C C   . VAL A 1 40  ? 17.823 4.639   -4.732  1.00 30.71  ? 40  VAL A C   1 
ATOM   386  O O   . VAL A 1 40  ? 17.936 4.311   -3.547  1.00 29.70  ? 40  VAL A O   1 
ATOM   387  C CB  . VAL A 1 40  ? 19.603 6.372   -4.991  1.00 28.76  ? 40  VAL A CB  1 
ATOM   388  C CG1 . VAL A 1 40  ? 20.439 5.560   -5.969  1.00 31.87  ? 40  VAL A CG1 1 
ATOM   389  C CG2 . VAL A 1 40  ? 19.866 7.862   -5.170  1.00 29.40  ? 40  VAL A CG2 1 
ATOM   390  N N   . SER A 1 41  ? 17.506 3.777   -5.692  1.00 27.33  ? 41  SER A N   1 
ATOM   391  C CA  . SER A 1 41  ? 17.409 2.361   -5.376  1.00 29.87  ? 41  SER A CA  1 
ATOM   392  C C   . SER A 1 41  ? 18.792 1.718   -5.353  1.00 26.23  ? 41  SER A C   1 
ATOM   393  O O   . SER A 1 41  ? 19.743 2.195   -5.972  1.00 26.38  ? 41  SER A O   1 
ATOM   394  C CB  . SER A 1 41  ? 16.548 1.628   -6.403  1.00 36.54  ? 41  SER A CB  1 
ATOM   395  O OG  . SER A 1 41  ? 16.355 0.276   -6.005  1.00 35.18  ? 41  SER A OG  1 
ATOM   396  N N   . GLU A 1 42  ? 18.889 0.608   -4.616  0.79 22.69  ? 42  GLU A N   1 
ATOM   397  C CA  . GLU A 1 42  ? 20.092 -0.212  -4.671  0.79 25.00  ? 42  GLU A CA  1 
ATOM   398  C C   . GLU A 1 42  ? 20.354 -0.777  -6.063  0.79 24.32  ? 42  GLU A C   1 
ATOM   399  O O   . GLU A 1 42  ? 21.501 -1.115  -6.369  0.79 29.02  ? 42  GLU A O   1 
ATOM   400  C CB  . GLU A 1 42  ? 20.023 -1.342  -3.646  0.79 28.34  ? 42  GLU A CB  1 
ATOM   401  C CG  . GLU A 1 42  ? 19.863 -0.837  -2.236  0.79 33.18  ? 42  GLU A CG  1 
ATOM   402  C CD  . GLU A 1 42  ? 21.206 -0.571  -1.604  0.79 33.91  ? 42  GLU A CD  1 
ATOM   403  O OE1 . GLU A 1 42  ? 22.233 -0.920  -2.233  0.79 38.34  ? 42  GLU A OE1 1 
ATOM   404  O OE2 . GLU A 1 42  ? 21.240 -0.006  -0.493  0.79 44.55  ? 42  GLU A OE2 1 
ATOM   405  N N   . THR A 1 43  ? 19.328 -0.889  -6.913  1.00 29.67  ? 43  THR A N   1 
ATOM   406  C CA  . THR A 1 43  ? 19.582 -1.249  -8.307  1.00 29.25  ? 43  THR A CA  1 
ATOM   407  C C   . THR A 1 43  ? 20.384 -0.164  -9.015  1.00 35.52  ? 43  THR A C   1 
ATOM   408  O O   . THR A 1 43  ? 21.222 -0.458  -9.877  1.00 29.49  ? 43  THR A O   1 
ATOM   409  C CB  . THR A 1 43  ? 18.267 -1.487  -9.053  1.00 28.72  ? 43  THR A CB  1 
ATOM   410  O OG1 . THR A 1 43  ? 17.383 -0.375  -8.851  1.00 34.68  ? 43  THR A OG1 1 
ATOM   411  C CG2 . THR A 1 43  ? 17.591 -2.765  -8.559  1.00 30.83  ? 43  THR A CG2 1 
ATOM   412  N N   . GLU A 1 44  ? 20.143 1.099   -8.663  1.00 35.96  ? 44  GLU A N   1 
ATOM   413  C CA  . GLU A 1 44  ? 20.798 2.215   -9.331  1.00 37.87  ? 44  GLU A CA  1 
ATOM   414  C C   . GLU A 1 44  ? 22.118 2.603   -8.683  1.00 35.83  ? 44  GLU A C   1 
ATOM   415  O O   . GLU A 1 44  ? 22.948 3.249   -9.336  1.00 36.38  ? 44  GLU A O   1 
ATOM   416  C CB  . GLU A 1 44  ? 19.839 3.412   -9.371  1.00 39.77  ? 44  GLU A CB  1 
ATOM   417  C CG  . GLU A 1 44  ? 18.446 3.016   -9.868  1.00 44.77  ? 44  GLU A CG  1 
ATOM   418  C CD  . GLU A 1 44  ? 17.376 4.049   -9.574  1.00 56.08  ? 44  GLU A CD  1 
ATOM   419  O OE1 . GLU A 1 44  ? 17.208 4.431   -8.393  1.00 40.38  ? 44  GLU A OE1 1 
ATOM   420  O OE2 . GLU A 1 44  ? 16.689 4.466   -10.529 1.00 56.16  ? 44  GLU A OE2 1 
ATOM   421  N N   . TRP A 1 45  ? 22.334 2.190   -7.433  1.00 31.40  ? 45  TRP A N   1 
ATOM   422  C CA  . TRP A 1 45  ? 23.500 2.627   -6.665  1.00 36.37  ? 45  TRP A CA  1 
ATOM   423  C C   . TRP A 1 45  ? 24.836 2.255   -7.299  1.00 41.22  ? 45  TRP A C   1 
ATOM   424  O O   . TRP A 1 45  ? 25.729 3.118   -7.344  1.00 34.43  ? 45  TRP A O   1 
ATOM   425  C CB  . TRP A 1 45  ? 23.367 2.147   -5.212  1.00 37.27  ? 45  TRP A CB  1 
ATOM   426  C CG  . TRP A 1 45  ? 24.492 2.529   -4.267  1.00 38.19  ? 45  TRP A CG  1 
ATOM   427  C CD1 . TRP A 1 45  ? 25.046 1.730   -3.308  1.00 46.99  ? 45  TRP A CD1 1 
ATOM   428  C CD2 . TRP A 1 45  ? 25.152 3.803   -4.153  1.00 42.33  ? 45  TRP A CD2 1 
ATOM   429  N NE1 . TRP A 1 45  ? 26.025 2.408   -2.629  1.00 42.76  ? 45  TRP A NE1 1 
ATOM   430  C CE2 . TRP A 1 45  ? 26.106 3.684   -3.122  1.00 41.19  ? 45  TRP A CE2 1 
ATOM   431  C CE3 . TRP A 1 45  ? 25.036 5.023   -4.824  1.00 40.74  ? 45  TRP A CE3 1 
ATOM   432  C CZ2 . TRP A 1 45  ? 26.941 4.738   -2.750  1.00 39.32  ? 45  TRP A CZ2 1 
ATOM   433  C CZ3 . TRP A 1 45  ? 25.869 6.069   -4.452  1.00 34.57  ? 45  TRP A CZ3 1 
ATOM   434  C CH2 . TRP A 1 45  ? 26.806 5.918   -3.425  1.00 29.58  ? 45  TRP A CH2 1 
ATOM   435  N N   . PRO A 1 46  ? 25.059 1.018   -7.770  1.00 42.16  ? 46  PRO A N   1 
ATOM   436  C CA  . PRO A 1 46  ? 26.363 0.696   -8.378  1.00 43.54  ? 46  PRO A CA  1 
ATOM   437  C C   . PRO A 1 46  ? 26.798 1.653   -9.476  1.00 44.73  ? 46  PRO A C   1 
ATOM   438  O O   . PRO A 1 46  ? 27.958 2.094   -9.496  1.00 53.07  ? 46  PRO A O   1 
ATOM   439  C CB  . PRO A 1 46  ? 26.126 -0.707  -8.922  1.00 36.12  ? 46  PRO A CB  1 
ATOM   440  C CG  . PRO A 1 46  ? 25.282 -1.343  -7.879  1.00 37.65  ? 46  PRO A CG  1 
ATOM   441  C CD  . PRO A 1 46  ? 24.376 -0.221  -7.343  1.00 39.28  ? 46  PRO A CD  1 
ATOM   442  N N   . SER A 1 47  ? 25.899 1.979   -10.409 1.00 40.40  ? 47  SER A N   1 
ATOM   443  C CA  . SER A 1 47  ? 26.263 2.878   -11.501 1.00 48.64  ? 47  SER A CA  1 
ATOM   444  C C   . SER A 1 47  ? 26.481 4.297   -10.996 1.00 60.73  ? 47  SER A C   1 
ATOM   445  O O   . SER A 1 47  ? 27.387 4.994   -11.465 1.00 57.82  ? 47  SER A O   1 
ATOM   446  C CB  . SER A 1 47  ? 25.189 2.851   -12.587 1.00 49.21  ? 47  SER A CB  1 
ATOM   447  O OG  . SER A 1 47  ? 23.900 3.082   -12.042 1.00 53.22  ? 47  SER A OG  1 
ATOM   448  N N   . LEU A 1 48  ? 25.655 4.745   -10.045 1.00 50.22  ? 48  LEU A N   1 
ATOM   449  C CA  . LEU A 1 48  ? 25.822 6.087   -9.495  1.00 51.27  ? 48  LEU A CA  1 
ATOM   450  C C   . LEU A 1 48  ? 27.133 6.201   -8.726  1.00 53.09  ? 48  LEU A C   1 
ATOM   451  O O   . LEU A 1 48  ? 27.844 7.206   -8.839  1.00 59.33  ? 48  LEU A O   1 
ATOM   452  C CB  . LEU A 1 48  ? 24.640 6.423   -8.584  1.00 45.07  ? 48  LEU A CB  1 
ATOM   453  C CG  . LEU A 1 48  ? 24.700 7.767   -7.858  1.00 51.45  ? 48  LEU A CG  1 
ATOM   454  C CD1 . LEU A 1 48  ? 24.532 8.898   -8.860  1.00 46.22  ? 48  LEU A CD1 1 
ATOM   455  C CD2 . LEU A 1 48  ? 23.649 7.850   -6.756  1.00 44.35  ? 48  LEU A CD2 1 
ATOM   456  N N   . LYS A 1 49  ? 27.469 5.173   -7.945  1.00 45.78  ? 49  LYS A N   1 
ATOM   457  C CA  . LYS A 1 49  ? 28.706 5.174   -7.175  1.00 48.45  ? 49  LYS A CA  1 
ATOM   458  C C   . LYS A 1 49  ? 29.940 5.202   -8.070  1.00 62.05  ? 49  LYS A C   1 
ATOM   459  O O   . LYS A 1 49  ? 31.003 5.657   -7.634  1.00 66.22  ? 49  LYS A O   1 
ATOM   460  C CB  . LYS A 1 49  ? 28.715 3.940   -6.268  1.00 45.83  ? 49  LYS A CB  1 
ATOM   461  C CG  . LYS A 1 49  ? 29.973 3.730   -5.439  1.00 61.30  ? 49  LYS A CG  1 
ATOM   462  C CD  . LYS A 1 49  ? 29.986 2.346   -4.792  1.00 57.57  ? 49  LYS A CD  1 
ATOM   463  C CE  . LYS A 1 49  ? 28.578 1.798   -4.593  1.00 59.66  ? 49  LYS A CE  1 
ATOM   464  N NZ  . LYS A 1 49  ? 28.530 0.308   -4.579  1.00 60.20  ? 49  LYS A NZ  1 
ATOM   465  N N   . SER A 1 50  ? 29.817 4.753   -9.320  1.00 61.92  ? 50  SER A N   1 
ATOM   466  C CA  . SER A 1 50  ? 30.977 4.673   -10.200 1.00 74.32  ? 50  SER A CA  1 
ATOM   467  C C   . SER A 1 50  ? 31.294 6.013   -10.857 1.00 81.40  ? 50  SER A C   1 
ATOM   468  O O   . SER A 1 50  ? 32.468 6.350   -11.044 1.00 91.57  ? 50  SER A O   1 
ATOM   469  C CB  . SER A 1 50  ? 30.763 3.590   -11.259 1.00 77.48  ? 50  SER A CB  1 
ATOM   470  O OG  . SER A 1 50  ? 29.972 4.074   -12.332 1.00 74.46  ? 50  SER A OG  1 
ATOM   471  N N   . LYS A 1 51  ? 30.273 6.787   -11.219 1.00 78.29  ? 51  LYS A N   1 
ATOM   472  C CA  . LYS A 1 51  ? 30.510 8.049   -11.910 1.00 80.67  ? 51  LYS A CA  1 
ATOM   473  C C   . LYS A 1 51  ? 30.713 9.232   -10.973 1.00 87.41  ? 51  LYS A C   1 
ATOM   474  O O   . LYS A 1 51  ? 31.288 10.242  -11.395 1.00 99.14  ? 51  LYS A O   1 
ATOM   475  C CB  . LYS A 1 51  ? 29.379 8.353   -12.900 1.00 80.22  ? 51  LYS A CB  1 
ATOM   476  C CG  . LYS A 1 51  ? 28.756 7.124   -13.534 1.00 75.81  ? 51  LYS A CG  1 
ATOM   477  C CD  . LYS A 1 51  ? 27.374 7.426   -14.090 1.00 74.00  ? 51  LYS A CD  1 
ATOM   478  C CE  . LYS A 1 51  ? 26.855 6.261   -14.916 1.00 78.01  ? 51  LYS A CE  1 
ATOM   479  N NZ  . LYS A 1 51  ? 25.934 6.706   -15.997 1.00 80.76  ? 51  LYS A NZ  1 
ATOM   480  N N   . MET A 1 52  ? 30.265 9.140   -9.731  1.00 84.26  ? 52  MET A N   1 
ATOM   481  C CA  . MET A 1 52  ? 30.344 10.259  -8.808  1.00 84.48  ? 52  MET A CA  1 
ATOM   482  C C   . MET A 1 52  ? 31.509 10.098  -7.842  1.00 83.95  ? 52  MET A C   1 
ATOM   483  O O   . MET A 1 52  ? 31.969 8.983   -7.582  1.00 79.45  ? 52  MET A O   1 
ATOM   484  C CB  . MET A 1 52  ? 29.038 10.384  -8.023  1.00 82.71  ? 52  MET A CB  1 
ATOM   485  C CG  . MET A 1 52  ? 27.741 10.340  -8.840  1.00 88.52  ? 52  MET A CG  1 
ATOM   486  S SD  . MET A 1 52  ? 27.325 11.784  -9.863  1.00 104.50 ? 52  MET A SD  1 
ATOM   487  C CE  . MET A 1 52  ? 28.396 11.635  -11.292 1.00 89.69  ? 52  MET A CE  1 
ATOM   488  N N   . PRO A 1 53  ? 32.014 11.211  -7.287  1.00 86.41  ? 53  PRO A N   1 
ATOM   489  C CA  . PRO A 1 53  ? 33.234 11.150  -6.466  1.00 81.64  ? 53  PRO A CA  1 
ATOM   490  C C   . PRO A 1 53  ? 33.032 10.700  -5.025  1.00 83.66  ? 53  PRO A C   1 
ATOM   491  O O   . PRO A 1 53  ? 33.870 11.010  -4.172  1.00 88.14  ? 53  PRO A O   1 
ATOM   492  C CB  . PRO A 1 53  ? 33.740 12.599  -6.499  1.00 79.61  ? 53  PRO A CB  1 
ATOM   493  C CG  . PRO A 1 53  ? 32.498 13.403  -6.713  1.00 81.14  ? 53  PRO A CG  1 
ATOM   494  C CD  . PRO A 1 53  ? 31.707 12.594  -7.691  1.00 86.75  ? 53  PRO A CD  1 
ATOM   495  N N   . PHE A 1 54  ? 31.956 9.976   -4.723  1.00 76.60  ? 54  PHE A N   1 
ATOM   496  C CA  . PHE A 1 54  ? 31.693 9.545   -3.357  1.00 68.62  ? 54  PHE A CA  1 
ATOM   497  C C   . PHE A 1 54  ? 31.415 8.048   -3.321  1.00 67.18  ? 54  PHE A C   1 
ATOM   498  O O   . PHE A 1 54  ? 31.148 7.419   -4.347  1.00 73.62  ? 54  PHE A O   1 
ATOM   499  C CB  . PHE A 1 54  ? 30.533 10.327  -2.720  1.00 67.17  ? 54  PHE A CB  1 
ATOM   500  C CG  . PHE A 1 54  ? 29.362 10.549  -3.642  1.00 68.39  ? 54  PHE A CG  1 
ATOM   501  C CD1 . PHE A 1 54  ? 28.467 9.523   -3.909  1.00 53.31  ? 54  PHE A CD1 1 
ATOM   502  C CD2 . PHE A 1 54  ? 29.150 11.786  -4.233  1.00 65.07  ? 54  PHE A CD2 1 
ATOM   503  C CE1 . PHE A 1 54  ? 27.385 9.725   -4.747  1.00 45.50  ? 54  PHE A CE1 1 
ATOM   504  C CE2 . PHE A 1 54  ? 28.069 11.993  -5.075  1.00 59.11  ? 54  PHE A CE2 1 
ATOM   505  C CZ  . PHE A 1 54  ? 27.183 10.959  -5.328  1.00 48.11  ? 54  PHE A CZ  1 
ATOM   506  N N   . ASN A 1 55  ? 31.477 7.482   -2.115  1.00 64.19  ? 55  ASN A N   1 
ATOM   507  C CA  . ASN A 1 55  ? 31.300 6.049   -1.921  1.00 62.78  ? 55  ASN A CA  1 
ATOM   508  C C   . ASN A 1 55  ? 30.161 5.696   -0.971  1.00 61.82  ? 55  ASN A C   1 
ATOM   509  O O   . ASN A 1 55  ? 29.879 4.506   -0.783  1.00 51.39  ? 55  ASN A O   1 
ATOM   510  C CB  . ASN A 1 55  ? 32.611 5.411   -1.434  1.00 77.77  ? 55  ASN A CB  1 
ATOM   511  C CG  . ASN A 1 55  ? 32.686 3.924   -1.733  1.00 86.96  ? 55  ASN A CG  1 
ATOM   512  O OD1 . ASN A 1 55  ? 33.130 3.519   -2.809  1.00 90.75  ? 55  ASN A OD1 1 
ATOM   513  N ND2 . ASN A 1 55  ? 32.257 3.104   -0.780  1.00 88.06  ? 55  ASN A ND2 1 
ATOM   514  N N   . GLN A 1 56  ? 29.501 6.686   -0.368  1.00 49.20  ? 56  GLN A N   1 
ATOM   515  C CA  . GLN A 1 56  ? 28.366 6.431   0.509   1.00 39.11  ? 56  GLN A CA  1 
ATOM   516  C C   . GLN A 1 56  ? 27.355 7.560   0.371   1.00 30.11  ? 56  GLN A C   1 
ATOM   517  O O   . GLN A 1 56  ? 27.689 8.676   -0.027  1.00 33.04  ? 56  GLN A O   1 
ATOM   518  C CB  . GLN A 1 56  ? 28.787 6.280   1.978   1.00 37.22  ? 56  GLN A CB  1 
ATOM   519  C CG  . GLN A 1 56  ? 27.810 5.456   2.829   1.00 53.82  ? 56  GLN A CG  1 
ATOM   520  C CD  . GLN A 1 56  ? 27.078 4.382   2.031   1.00 60.95  ? 56  GLN A CD  1 
ATOM   521  O OE1 . GLN A 1 56  ? 25.862 4.464   1.812   1.00 39.63  ? 56  GLN A OE1 1 
ATOM   522  N NE2 . GLN A 1 56  ? 27.813 3.357   1.609   1.00 75.70  ? 56  GLN A NE2 1 
ATOM   523  N N   . LEU A 1 57  ? 26.109 7.248   0.693   1.00 22.74  ? 57  LEU A N   1 
ATOM   524  C CA  . LEU A 1 57  ? 25.054 8.244   0.786   1.00 19.64  ? 57  LEU A CA  1 
ATOM   525  C C   . LEU A 1 57  ? 24.702 8.471   2.255   1.00 19.94  ? 57  LEU A C   1 
ATOM   526  O O   . LEU A 1 57  ? 24.982 7.624   3.110   1.00 22.81  ? 57  LEU A O   1 
ATOM   527  C CB  . LEU A 1 57  ? 23.813 7.749   0.030   1.00 19.14  ? 57  LEU A CB  1 
ATOM   528  C CG  . LEU A 1 57  ? 24.034 7.430   -1.457  1.00 20.15  ? 57  LEU A CG  1 
ATOM   529  C CD1 . LEU A 1 57  ? 22.743 6.966   -2.094  1.00 21.33  ? 57  LEU A CD1 1 
ATOM   530  C CD2 . LEU A 1 57  ? 24.563 8.658   -2.182  1.00 21.69  ? 57  LEU A CD2 1 
ATOM   531  N N   . PRO A 1 58  ? 24.075 9.599   2.598   1.00 19.10  ? 58  PRO A N   1 
ATOM   532  C CA  . PRO A 1 58  ? 23.619 10.709  1.748   1.00 16.55  ? 58  PRO A CA  1 
ATOM   533  C C   . PRO A 1 58  ? 24.735 11.625  1.271   1.00 17.81  ? 58  PRO A C   1 
ATOM   534  O O   . PRO A 1 58  ? 25.782 11.781  1.912   1.00 18.96  ? 58  PRO A O   1 
ATOM   535  C CB  . PRO A 1 58  ? 22.683 11.475  2.684   1.00 19.28  ? 58  PRO A CB  1 
ATOM   536  C CG  . PRO A 1 58  ? 23.315 11.287  4.028   1.00 19.60  ? 58  PRO A CG  1 
ATOM   537  C CD  . PRO A 1 58  ? 23.781 9.854   4.017   1.00 21.03  ? 58  PRO A CD  1 
ATOM   538  N N   . VAL A 1 59  ? 24.513 12.251  0.122   1.00 17.02  ? 59  VAL A N   1 
ATOM   539  C CA  . VAL A 1 59  ? 25.336 13.354  -0.346  1.00 19.41  ? 59  VAL A CA  1 
ATOM   540  C C   . VAL A 1 59  ? 24.388 14.514  -0.597  1.00 16.62  ? 59  VAL A C   1 
ATOM   541  O O   . VAL A 1 59  ? 23.258 14.308  -1.055  1.00 17.25  ? 59  VAL A O   1 
ATOM   542  C CB  . VAL A 1 59  ? 26.083 12.952  -1.635  1.00 19.82  ? 59  VAL A CB  1 
ATOM   543  C CG1 . VAL A 1 59  ? 26.616 14.175  -2.410  1.00 22.84  ? 59  VAL A CG1 1 
ATOM   544  C CG2 . VAL A 1 59  ? 27.197 11.958  -1.317  1.00 25.63  ? 59  VAL A CG2 1 
ATOM   545  N N   . LEU A 1 60  ? 24.810 15.717  -0.235  1.00 13.41  ? 60  LEU A N   1 
ATOM   546  C CA  . LEU A 1 60  ? 24.087 16.928  -0.622  1.00 14.02  ? 60  LEU A CA  1 
ATOM   547  C C   . LEU A 1 60  ? 24.872 17.596  -1.737  1.00 14.70  ? 60  LEU A C   1 
ATOM   548  O O   . LEU A 1 60  ? 25.971 18.119  -1.507  1.00 15.25  ? 60  LEU A O   1 
ATOM   549  C CB  . LEU A 1 60  ? 23.892 17.870  0.562   1.00 13.17  ? 60  LEU A CB  1 
ATOM   550  C CG  . LEU A 1 60  ? 22.959 19.062  0.275   1.00 15.33  ? 60  LEU A CG  1 
ATOM   551  C CD1 . LEU A 1 60  ? 21.532 18.562  0.178   1.00 18.11  ? 60  LEU A CD1 1 
ATOM   552  C CD2 . LEU A 1 60  ? 23.105 20.175  1.325   1.00 18.86  ? 60  LEU A CD2 1 
ATOM   553  N N   A GLU A 1 61  ? 24.329 17.576  -2.950  0.59 14.34  ? 61  GLU A N   1 
ATOM   554  N N   B GLU A 1 61  ? 24.326 17.541  -2.946  0.41 14.35  ? 61  GLU A N   1 
ATOM   555  C CA  A GLU A 1 61  ? 24.956 18.261  -4.076  0.59 14.26  ? 61  GLU A CA  1 
ATOM   556  C CA  B GLU A 1 61  ? 24.881 18.275  -4.072  0.41 14.34  ? 61  GLU A CA  1 
ATOM   557  C C   A GLU A 1 61  ? 24.473 19.705  -4.109  0.59 13.42  ? 61  GLU A C   1 
ATOM   558  C C   B GLU A 1 61  ? 24.432 19.724  -3.960  0.41 13.84  ? 61  GLU A C   1 
ATOM   559  O O   A GLU A 1 61  ? 23.295 19.969  -4.378  0.59 15.64  ? 61  GLU A O   1 
ATOM   560  O O   B GLU A 1 61  ? 23.230 20.012  -3.931  0.41 14.37  ? 61  GLU A O   1 
ATOM   561  C CB  A GLU A 1 61  ? 24.620 17.581  -5.397  0.59 16.42  ? 61  GLU A CB  1 
ATOM   562  C CB  B GLU A 1 61  ? 24.377 17.670  -5.379  0.41 16.39  ? 61  GLU A CB  1 
ATOM   563  C CG  A GLU A 1 61  ? 25.130 18.378  -6.578  0.59 18.67  ? 61  GLU A CG  1 
ATOM   564  C CG  B GLU A 1 61  ? 24.574 16.165  -5.487  0.41 22.06  ? 61  GLU A CG  1 
ATOM   565  C CD  A GLU A 1 61  ? 24.440 18.010  -7.877  0.59 26.18  ? 61  GLU A CD  1 
ATOM   566  C CD  B GLU A 1 61  ? 24.492 15.663  -6.919  0.41 24.68  ? 61  GLU A CD  1 
ATOM   567  O OE1 A GLU A 1 61  ? 24.856 17.028  -8.522  0.59 31.01  ? 61  GLU A OE1 1 
ATOM   568  O OE1 B GLU A 1 61  ? 24.263 16.490  -7.825  0.41 27.34  ? 61  GLU A OE1 1 
ATOM   569  O OE2 A GLU A 1 61  ? 23.451 18.685  -8.229  0.59 25.89  ? 61  GLU A OE2 1 
ATOM   570  O OE2 B GLU A 1 61  ? 24.679 14.449  -7.131  0.41 32.03  ? 61  GLU A OE2 1 
ATOM   571  N N   . VAL A 1 62  ? 25.389 20.637  -3.866  1.00 15.58  ? 62  VAL A N   1 
ATOM   572  C CA  . VAL A 1 62  ? 25.104 22.060  -3.798  1.00 15.96  ? 62  VAL A CA  1 
ATOM   573  C C   . VAL A 1 62  ? 25.566 22.681  -5.104  1.00 15.41  ? 62  VAL A C   1 
ATOM   574  O O   . VAL A 1 62  ? 26.707 22.452  -5.534  1.00 16.89  ? 62  VAL A O   1 
ATOM   575  C CB  . VAL A 1 62  ? 25.882 22.683  -2.626  1.00 12.93  ? 62  VAL A CB  1 
ATOM   576  C CG1 . VAL A 1 62  ? 25.610 24.152  -2.557  1.00 15.85  ? 62  VAL A CG1 1 
ATOM   577  C CG2 . VAL A 1 62  ? 25.542 21.987  -1.293  1.00 15.13  ? 62  VAL A CG2 1 
ATOM   578  N N   . THR A 1 63  ? 24.709 23.499  -5.727  1.00 14.10  ? 63  THR A N   1 
ATOM   579  C CA  . THR A 1 63  ? 25.138 24.363  -6.823  1.00 13.43  ? 63  THR A CA  1 
ATOM   580  C C   . THR A 1 63  ? 24.995 25.786  -6.309  1.00 13.87  ? 63  THR A C   1 
ATOM   581  O O   . THR A 1 63  ? 23.879 26.278  -6.109  1.00 14.79  ? 63  THR A O   1 
ATOM   582  C CB  . THR A 1 63  ? 24.340 24.144  -8.104  1.00 14.72  ? 63  THR A CB  1 
ATOM   583  O OG1 . THR A 1 63  ? 24.394 22.762  -8.473  1.00 16.28  ? 63  THR A OG1 1 
ATOM   584  C CG2 . THR A 1 63  ? 24.947 24.979  -9.222  1.00 19.88  ? 63  THR A CG2 1 
ATOM   585  N N   . THR A 1 64  ? 26.121 26.449  -6.056  1.00 13.85  ? 64  THR A N   1 
ATOM   586  C CA  . THR A 1 64  ? 26.049 27.781  -5.473  1.00 14.76  ? 64  THR A CA  1 
ATOM   587  C C   . THR A 1 64  ? 25.386 28.743  -6.459  1.00 13.15  ? 64  THR A C   1 
ATOM   588  O O   . THR A 1 64  ? 25.269 28.425  -7.648  1.00 13.79  ? 64  THR A O   1 
ATOM   589  C CB  . THR A 1 64  ? 27.439 28.332  -5.124  1.00 13.80  ? 64  THR A CB  1 
ATOM   590  O OG1 . THR A 1 64  ? 28.128 28.653  -6.337  1.00 15.24  ? 64  THR A OG1 1 
ATOM   591  C CG2 . THR A 1 64  ? 28.263 27.358  -4.303  1.00 16.89  ? 64  THR A CG2 1 
ATOM   592  N N   . PRO A 1 65  ? 24.980 29.941  -6.011  1.00 13.96  ? 65  PRO A N   1 
ATOM   593  C CA  . PRO A 1 65  ? 24.389 30.922  -6.939  1.00 14.04  ? 65  PRO A CA  1 
ATOM   594  C C   . PRO A 1 65  ? 25.335 31.340  -8.037  1.00 15.66  ? 65  PRO A C   1 
ATOM   595  O O   . PRO A 1 65  ? 24.868 31.868  -9.060  1.00 16.96  ? 65  PRO A O   1 
ATOM   596  C CB  . PRO A 1 65  ? 24.024 32.093  -6.029  1.00 16.48  ? 65  PRO A CB  1 
ATOM   597  C CG  . PRO A 1 65  ? 23.768 31.428  -4.695  1.00 17.49  ? 65  PRO A CG  1 
ATOM   598  C CD  . PRO A 1 65  ? 24.837 30.361  -4.610  1.00 14.37  ? 65  PRO A CD  1 
ATOM   599  N N   . ASN A 1 66  ? 26.645 31.127  -7.867  1.00 15.05  ? 66  ASN A N   1 
ATOM   600  C CA  . ASN A 1 66  ? 27.608 31.435  -8.920  1.00 15.59  ? 66  ASN A CA  1 
ATOM   601  C C   . ASN A 1 66  ? 27.889 30.240  -9.825  1.00 13.31  ? 66  ASN A C   1 
ATOM   602  O O   . ASN A 1 66  ? 28.740 30.334  -10.718 1.00 15.10  ? 66  ASN A O   1 
ATOM   603  C CB  . ASN A 1 66  ? 28.919 31.948  -8.306  1.00 15.46  ? 66  ASN A CB  1 
ATOM   604  C CG  . ASN A 1 66  ? 28.702 33.027  -7.256  1.00 19.64  ? 66  ASN A CG  1 
ATOM   605  O OD1 . ASN A 1 66  ? 28.889 32.791  -6.056  1.00 21.97  ? 66  ASN A OD1 1 
ATOM   606  N ND2 . ASN A 1 66  ? 28.306 34.214  -7.698  1.00 20.51  ? 66  ASN A ND2 1 
ATOM   607  N N   . GLY A 1 67  ? 27.181 29.127  -9.635  1.00 13.25  ? 67  GLY A N   1 
ATOM   608  C CA  . GLY A 1 67  ? 27.287 27.983  -10.504 1.00 14.94  ? 67  GLY A CA  1 
ATOM   609  C C   . GLY A 1 67  ? 28.251 26.905  -10.085 1.00 14.84  ? 67  GLY A C   1 
ATOM   610  O O   . GLY A 1 67  ? 28.441 25.953  -10.846 1.00 16.19  ? 67  GLY A O   1 
ATOM   611  N N   . GLN A 1 68  ? 28.854 27.005  -8.909  1.00 14.16  ? 68  GLN A N   1 
ATOM   612  C CA  . GLN A 1 68  ? 29.852 26.025  -8.505  1.00 13.25  ? 68  GLN A CA  1 
ATOM   613  C C   . GLN A 1 68  ? 29.180 24.809  -7.875  1.00 13.33  ? 68  GLN A C   1 
ATOM   614  O O   . GLN A 1 68  ? 28.366 24.949  -6.957  1.00 14.86  ? 68  GLN A O   1 
ATOM   615  C CB  . GLN A 1 68  ? 30.825 26.649  -7.511  1.00 14.58  ? 68  GLN A CB  1 
ATOM   616  C CG  . GLN A 1 68  ? 31.986 25.699  -7.201  1.00 14.71  ? 68  GLN A CG  1 
ATOM   617  C CD  . GLN A 1 68  ? 33.060 26.370  -6.398  1.00 17.87  ? 68  GLN A CD  1 
ATOM   618  O OE1 . GLN A 1 68  ? 33.020 27.582  -6.209  1.00 17.69  ? 68  GLN A OE1 1 
ATOM   619  N NE2 . GLN A 1 68  ? 34.018 25.602  -5.903  1.00 18.77  ? 68  GLN A NE2 1 
ATOM   620  N N   A LYS A 1 69  ? 29.531 23.623  -8.358  0.52 16.17  ? 69  LYS A N   1 
ATOM   621  N N   B LYS A 1 69  ? 29.527 23.632  -8.369  0.48 16.17  ? 69  LYS A N   1 
ATOM   622  C CA  A LYS A 1 69  ? 28.978 22.371  -7.852  0.52 16.28  ? 69  LYS A CA  1 
ATOM   623  C CA  B LYS A 1 69  ? 29.001 22.384  -7.838  0.48 16.31  ? 69  LYS A CA  1 
ATOM   624  C C   A LYS A 1 69  ? 29.909 21.790  -6.788  0.52 16.87  ? 69  LYS A C   1 
ATOM   625  C C   B LYS A 1 69  ? 29.936 21.857  -6.757  0.48 16.85  ? 69  LYS A C   1 
ATOM   626  O O   A LYS A 1 69  ? 31.083 21.510  -7.062  0.52 17.90  ? 69  LYS A O   1 
ATOM   627  O O   B LYS A 1 69  ? 31.145 21.711  -6.980  0.48 18.06  ? 69  LYS A O   1 
ATOM   628  C CB  A LYS A 1 69  ? 28.764 21.366  -8.988  0.52 20.04  ? 69  LYS A CB  1 
ATOM   629  C CB  B LYS A 1 69  ? 28.851 21.362  -8.966  0.48 19.99  ? 69  LYS A CB  1 
ATOM   630  C CG  A LYS A 1 69  ? 28.146 20.059  -8.522  0.52 22.29  ? 69  LYS A CG  1 
ATOM   631  C CG  B LYS A 1 69  ? 27.795 21.770  -9.975  0.48 22.86  ? 69  LYS A CG  1 
ATOM   632  C CD  A LYS A 1 69  ? 27.109 19.494  -9.488  0.52 31.49  ? 69  LYS A CD  1 
ATOM   633  C CD  B LYS A 1 69  ? 27.709 20.786  -11.127 0.48 30.03  ? 69  LYS A CD  1 
ATOM   634  C CE  A LYS A 1 69  ? 27.302 19.991  -10.905 0.52 32.11  ? 69  LYS A CE  1 
ATOM   635  C CE  B LYS A 1 69  ? 26.645 21.207  -12.127 0.48 41.29  ? 69  LYS A CE  1 
ATOM   636  N NZ  A LYS A 1 69  ? 26.898 18.949  -11.894 0.52 36.87  ? 69  LYS A NZ  1 
ATOM   637  N NZ  B LYS A 1 69  ? 26.578 20.280  -13.295 0.48 43.38  ? 69  LYS A NZ  1 
ATOM   638  N N   . VAL A 1 70  ? 29.378 21.585  -5.583  1.00 14.69  ? 70  VAL A N   1 
ATOM   639  C CA  . VAL A 1 70  ? 30.130 21.034  -4.459  1.00 16.30  ? 70  VAL A CA  1 
ATOM   640  C C   . VAL A 1 70  ? 29.320 19.875  -3.890  1.00 17.50  ? 70  VAL A C   1 
ATOM   641  O O   . VAL A 1 70  ? 28.119 20.019  -3.653  1.00 19.32  ? 70  VAL A O   1 
ATOM   642  C CB  . VAL A 1 70  ? 30.335 22.101  -3.366  1.00 18.15  ? 70  VAL A CB  1 
ATOM   643  C CG1 . VAL A 1 70  ? 31.093 21.511  -2.175  1.00 21.81  ? 70  VAL A CG1 1 
ATOM   644  C CG2 . VAL A 1 70  ? 31.048 23.358  -3.917  1.00 18.66  ? 70  VAL A CG2 1 
ATOM   645  N N   . MET A 1 71  ? 29.974 18.739  -3.636  1.00 16.67  ? 71  MET A N   1 
ATOM   646  C CA  . MET A 1 71  ? 29.328 17.556  -3.063  1.00 16.63  ? 71  MET A CA  1 
ATOM   647  C C   . MET A 1 71  ? 29.678 17.506  -1.585  1.00 18.54  ? 71  MET A C   1 
ATOM   648  O O   . MET A 1 71  ? 30.848 17.333  -1.220  1.00 21.96  ? 71  MET A O   1 
ATOM   649  C CB  . MET A 1 71  ? 29.842 16.267  -3.709  1.00 21.80  ? 71  MET A CB  1 
ATOM   650  C CG  . MET A 1 71  ? 29.701 16.106  -5.199  1.00 36.26  ? 71  MET A CG  1 
ATOM   651  S SD  . MET A 1 71  ? 28.007 16.350  -5.736  1.00 40.88  ? 71  MET A SD  1 
ATOM   652  C CE  . MET A 1 71  ? 28.266 16.738  -7.468  1.00 42.93  ? 71  MET A CE  1 
ATOM   653  N N   . LEU A 1 72  ? 28.677 17.636  -0.732  1.00 14.16  ? 72  LEU A N   1 
ATOM   654  C CA  . LEU A 1 72  ? 28.899 17.536  0.704   1.00 13.43  ? 72  LEU A CA  1 
ATOM   655  C C   . LEU A 1 72  ? 28.569 16.136  1.197   1.00 14.16  ? 72  LEU A C   1 
ATOM   656  O O   . LEU A 1 72  ? 27.569 15.532  0.781   1.00 15.11  ? 72  LEU A O   1 
ATOM   657  C CB  . LEU A 1 72  ? 28.050 18.551  1.465   1.00 13.96  ? 72  LEU A CB  1 
ATOM   658  C CG  . LEU A 1 72  ? 28.181 20.012  1.036   1.00 15.09  ? 72  LEU A CG  1 
ATOM   659  C CD1 . LEU A 1 72  ? 27.257 20.848  1.896   1.00 18.85  ? 72  LEU A CD1 1 
ATOM   660  C CD2 . LEU A 1 72  ? 29.635 20.507  1.143   1.00 18.35  ? 72  LEU A CD2 1 
ATOM   661  N N   . THR A 1 73  ? 29.389 15.646  2.115   1.00 13.90  ? 73  THR A N   1 
ATOM   662  C CA  . THR A 1 73  ? 29.199 14.330  2.701   1.00 13.21  ? 73  THR A CA  1 
ATOM   663  C C   . THR A 1 73  ? 29.136 14.430  4.218   1.00 14.22  ? 73  THR A C   1 
ATOM   664  O O   . THR A 1 73  ? 29.406 15.484  4.810   1.00 15.26  ? 73  THR A O   1 
ATOM   665  C CB  . THR A 1 73  ? 30.340 13.381  2.308   1.00 16.92  ? 73  THR A CB  1 
ATOM   666  O OG1 . THR A 1 73  ? 31.576 13.929  2.774   1.00 20.44  ? 73  THR A OG1 1 
ATOM   667  C CG2 . THR A 1 73  ? 30.414 13.205  0.793   1.00 20.70  ? 73  THR A CG2 1 
ATOM   668  N N   . GLU A 1 74  ? 28.801 13.284  4.831   1.00 13.82  ? 74  GLU A N   1 
ATOM   669  C CA  . GLU A 1 74  ? 28.700 13.075  6.274   1.00 14.27  ? 74  GLU A CA  1 
ATOM   670  C C   . GLU A 1 74  ? 27.380 13.625  6.797   1.00 13.46  ? 74  GLU A C   1 
ATOM   671  O O   . GLU A 1 74  ? 27.249 14.835  7.035   1.00 13.72  ? 74  GLU A O   1 
ATOM   672  C CB  . GLU A 1 74  ? 29.928 13.586  7.043   1.00 16.85  ? 74  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 74  ? 31.277 13.011  6.594   1.00 17.32  ? 74  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 74  ? 31.297 11.502  6.555   1.00 22.04  ? 74  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 74  ? 31.624 10.942  5.482   1.00 26.30  ? 74  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 74  ? 30.989 10.891  7.596   1.00 22.71  ? 74  GLU A OE2 1 
ATOM   677  N N   A SER A 1 75  ? 26.414 12.725  7.008   0.62 15.03  ? 75  SER A N   1 
ATOM   678  N N   B SER A 1 75  ? 26.405 12.736  6.994   0.38 15.05  ? 75  SER A N   1 
ATOM   679  C CA  A SER A 1 75  ? 25.019 13.102  7.219   0.62 16.20  ? 75  SER A CA  1 
ATOM   680  C CA  B SER A 1 75  ? 25.023 13.154  7.213   0.38 16.27  ? 75  SER A CA  1 
ATOM   681  C C   A SER A 1 75  ? 24.835 14.128  8.334   0.62 15.24  ? 75  SER A C   1 
ATOM   682  C C   B SER A 1 75  ? 24.887 14.180  8.334   0.38 15.24  ? 75  SER A C   1 
ATOM   683  O O   A SER A 1 75  ? 24.105 15.115  8.166   0.62 14.45  ? 75  SER A O   1 
ATOM   684  O O   B SER A 1 75  ? 24.253 15.227  8.151   0.38 14.66  ? 75  SER A O   1 
ATOM   685  C CB  A SER A 1 75  ? 24.168 11.855  7.483   0.62 17.03  ? 75  SER A CB  1 
ATOM   686  C CB  B SER A 1 75  ? 24.135 11.943  7.485   0.38 17.02  ? 75  SER A CB  1 
ATOM   687  O OG  A SER A 1 75  ? 24.665 11.123  8.591   0.62 18.81  ? 75  SER A OG  1 
ATOM   688  O OG  B SER A 1 75  ? 22.784 12.350  7.556   0.38 22.40  ? 75  SER A OG  1 
ATOM   689  N N   A MET A 1 76  ? 25.451 13.900  9.499   0.62 15.06  ? 76  MET A N   1 
ATOM   690  N N   B MET A 1 76  ? 25.452 13.893  9.512   0.38 15.08  ? 76  MET A N   1 
ATOM   691  C CA  A MET A 1 76  ? 25.237 14.834  10.601  0.62 14.20  ? 76  MET A CA  1 
ATOM   692  C CA  B MET A 1 76  ? 25.282 14.817  10.630  0.38 14.30  ? 76  MET A CA  1 
ATOM   693  C C   A MET A 1 76  ? 25.954 16.160  10.388  0.62 13.30  ? 76  MET A C   1 
ATOM   694  C C   B MET A 1 76  ? 25.937 16.161  10.354  0.38 13.34  ? 76  MET A C   1 
ATOM   695  O O   A MET A 1 76  ? 25.436 17.206  10.803  0.62 15.43  ? 76  MET A O   1 
ATOM   696  O O   B MET A 1 76  ? 25.380 17.210  10.704  0.38 15.40  ? 76  MET A O   1 
ATOM   697  C CB  A MET A 1 76  ? 25.637 14.195  11.937  0.62 18.25  ? 76  MET A CB  1 
ATOM   698  C CB  B MET A 1 76  ? 25.829 14.227  11.931  0.38 18.85  ? 76  MET A CB  1 
ATOM   699  C CG  A MET A 1 76  ? 24.944 14.775  13.161  0.62 21.20  ? 76  MET A CG  1 
ATOM   700  C CG  B MET A 1 76  ? 24.889 13.297  12.670  0.38 18.82  ? 76  MET A CG  1 
ATOM   701  S SD  A MET A 1 76  ? 23.141 14.777  13.065  0.62 23.24  ? 76  MET A SD  1 
ATOM   702  S SD  B MET A 1 76  ? 23.192 13.868  12.882  0.38 17.07  ? 76  MET A SD  1 
ATOM   703  C CE  A MET A 1 76  ? 22.724 15.210  14.746  0.62 20.24  ? 76  MET A CE  1 
ATOM   704  C CE  B MET A 1 76  ? 23.437 15.562  13.464  0.38 11.17  ? 76  MET A CE  1 
ATOM   705  N N   . ALA A 1 77  ? 27.125 16.154  9.742   1.00 13.45  ? 77  ALA A N   1 
ATOM   706  C CA  . ALA A 1 77  ? 27.779 17.413  9.399   1.00 13.78  ? 77  ALA A CA  1 
ATOM   707  C C   . ALA A 1 77  ? 26.910 18.238  8.455   1.00 11.69  ? 77  ALA A C   1 
ATOM   708  O O   . ALA A 1 77  ? 26.791 19.463  8.618   1.00 13.62  ? 77  ALA A O   1 
ATOM   709  C CB  . ALA A 1 77  ? 29.149 17.147  8.757   1.00 13.98  ? 77  ALA A CB  1 
ATOM   710  N N   . ILE A 1 78  ? 26.279 17.581  7.480   1.00 12.78  ? 78  ILE A N   1 
ATOM   711  C CA  . ILE A 1 78  ? 25.361 18.255  6.571   1.00 12.74  ? 78  ILE A CA  1 
ATOM   712  C C   . ILE A 1 78  ? 24.176 18.816  7.342   1.00 12.26  ? 78  ILE A C   1 
ATOM   713  O O   . ILE A 1 78  ? 23.810 19.980  7.174   1.00 13.12  ? 78  ILE A O   1 
ATOM   714  C CB  . ILE A 1 78  ? 24.895 17.280  5.482   1.00 12.71  ? 78  ILE A CB  1 
ATOM   715  C CG1 . ILE A 1 78  ? 26.065 16.839  4.617   1.00 12.11  ? 78  ILE A CG1 1 
ATOM   716  C CG2 . ILE A 1 78  ? 23.803 17.944  4.634   1.00 12.58  ? 78  ILE A CG2 1 
ATOM   717  C CD1 . ILE A 1 78  ? 25.706 15.624  3.770   1.00 14.00  ? 78  ILE A CD1 1 
ATOM   718  N N   . ALA A 1 79  ? 23.569 18.007  8.208   1.00 11.46  ? 79  ALA A N   1 
ATOM   719  C CA  . ALA A 1 79  ? 22.404 18.464  8.956   1.00 12.07  ? 79  ALA A CA  1 
ATOM   720  C C   . ALA A 1 79  ? 22.726 19.677  9.824   1.00 13.03  ? 79  ALA A C   1 
ATOM   721  O O   . ALA A 1 79  ? 21.919 20.603  9.905   1.00 13.00  ? 79  ALA A O   1 
ATOM   722  C CB  . ALA A 1 79  ? 21.833 17.323  9.806   1.00 13.15  ? 79  ALA A CB  1 
ATOM   723  N N   . ARG A 1 80  ? 23.868 19.664  10.524  1.00 12.91  ? 80  ARG A N   1 
ATOM   724  C CA  . ARG A 1 80  ? 24.226 20.785  11.386  1.00 14.22  ? 80  ARG A CA  1 
ATOM   725  C C   . ARG A 1 80  ? 24.526 22.034  10.569  1.00 13.91  ? 80  ARG A C   1 
ATOM   726  O O   . ARG A 1 80  ? 24.137 23.141  10.950  1.00 12.23  ? 80  ARG A O   1 
ATOM   727  C CB  . ARG A 1 80  ? 25.425 20.410  12.265  1.00 12.51  ? 80  ARG A CB  1 
ATOM   728  C CG  . ARG A 1 80  ? 25.169 19.313  13.272  1.00 13.23  ? 80  ARG A CG  1 
ATOM   729  C CD  . ARG A 1 80  ? 26.319 19.275  14.269  1.00 13.68  ? 80  ARG A CD  1 
ATOM   730  N NE  . ARG A 1 80  ? 26.533 17.946  14.834  1.00 17.14  ? 80  ARG A NE  1 
ATOM   731  C CZ  . ARG A 1 80  ? 27.414 17.069  14.370  1.00 19.22  ? 80  ARG A CZ  1 
ATOM   732  N NH1 . ARG A 1 80  ? 28.149 17.325  13.294  1.00 18.65  ? 80  ARG A NH1 1 
ATOM   733  N NH2 . ARG A 1 80  ? 27.540 15.889  14.978  1.00 19.67  ? 80  ARG A NH2 1 
ATOM   734  N N   . LEU A 1 81  ? 25.210 21.884  9.438   1.00 12.31  ? 81  LEU A N   1 
ATOM   735  C CA  . LEU A 1 81  ? 25.469 23.029  8.570   1.00 10.35  ? 81  LEU A CA  1 
ATOM   736  C C   . LEU A 1 81  ? 24.163 23.662  8.108   1.00 12.27  ? 81  LEU A C   1 
ATOM   737  O O   . LEU A 1 81  ? 24.012 24.892  8.115   1.00 13.73  ? 81  LEU A O   1 
ATOM   738  C CB  . LEU A 1 81  ? 26.288 22.543  7.378   1.00 12.76  ? 81  LEU A CB  1 
ATOM   739  C CG  . LEU A 1 81  ? 26.456 23.556  6.256   1.00 11.79  ? 81  LEU A CG  1 
ATOM   740  C CD1 . LEU A 1 81  ? 27.176 24.836  6.719   1.00 15.34  ? 81  LEU A CD1 1 
ATOM   741  C CD2 . LEU A 1 81  ? 27.214 22.906  5.103   1.00 15.72  ? 81  LEU A CD2 1 
ATOM   742  N N   . LEU A 1 82  ? 23.208 22.833  7.676   1.00 11.36  ? 82  LEU A N   1 
ATOM   743  C CA  . LEU A 1 82  ? 21.924 23.367  7.235   1.00 12.27  ? 82  LEU A CA  1 
ATOM   744  C C   . LEU A 1 82  ? 21.171 23.974  8.404   1.00 13.35  ? 82  LEU A C   1 
ATOM   745  O O   . LEU A 1 82  ? 20.561 25.037  8.263   1.00 13.05  ? 82  LEU A O   1 
ATOM   746  C CB  . LEU A 1 82  ? 21.109 22.263  6.573   1.00 11.84  ? 82  LEU A CB  1 
ATOM   747  C CG  . LEU A 1 82  ? 21.710 21.761  5.264   1.00 12.59  ? 82  LEU A CG  1 
ATOM   748  C CD1 . LEU A 1 82  ? 20.922 20.522  4.859   1.00 13.59  ? 82  LEU A CD1 1 
ATOM   749  C CD2 . LEU A 1 82  ? 21.645 22.822  4.169   1.00 14.55  ? 82  LEU A CD2 1 
ATOM   750  N N   . ALA A 1 83  ? 21.232 23.347  9.582   1.00 12.12  ? 83  ALA A N   1 
ATOM   751  C CA  . ALA A 1 83  ? 20.540 23.923  10.730  1.00 12.31  ? 83  ALA A CA  1 
ATOM   752  C C   . ALA A 1 83  ? 21.113 25.292  11.083  1.00 12.66  ? 83  ALA A C   1 
ATOM   753  O O   . ALA A 1 83  ? 20.363 26.238  11.372  1.00 14.42  ? 83  ALA A O   1 
ATOM   754  C CB  . ALA A 1 83  ? 20.604 22.985  11.931  1.00 11.43  ? 83  ALA A CB  1 
ATOM   755  N N   . ARG A 1 84  ? 22.445 25.426  11.065  1.00 13.04  ? 84  ARG A N   1 
ATOM   756  C CA  . ARG A 1 84  ? 23.046 26.722  11.353  1.00 12.71  ? 84  ARG A CA  1 
ATOM   757  C C   . ARG A 1 84  ? 22.614 27.758  10.330  1.00 13.76  ? 84  ARG A C   1 
ATOM   758  O O   . ARG A 1 84  ? 22.329 28.909  10.684  1.00 16.20  ? 84  ARG A O   1 
ATOM   759  C CB  . ARG A 1 84  ? 24.564 26.610  11.333  1.00 14.15  ? 84  ARG A CB  1 
ATOM   760  C CG  . ARG A 1 84  ? 25.123 25.824  12.501  1.00 12.96  ? 84  ARG A CG  1 
ATOM   761  C CD  . ARG A 1 84  ? 26.643 25.682  12.393  1.00 14.74  ? 84  ARG A CD  1 
ATOM   762  N NE  . ARG A 1 84  ? 27.148 24.943  13.548  1.00 17.49  ? 84  ARG A NE  1 
ATOM   763  C CZ  . ARG A 1 84  ? 27.536 23.668  13.533  1.00 13.44  ? 84  ARG A CZ  1 
ATOM   764  N NH1 . ARG A 1 84  ? 27.640 22.983  12.392  1.00 14.47  ? 84  ARG A NH1 1 
ATOM   765  N NH2 . ARG A 1 84  ? 27.851 23.066  14.689  1.00 15.11  ? 84  ARG A NH2 1 
ATOM   766  N N   . THR A 1 85  ? 22.550 27.364  9.068   1.00 13.15  ? 85  THR A N   1 
ATOM   767  C CA  . THR A 1 85  ? 22.211 28.305  8.005   1.00 12.64  ? 85  THR A CA  1 
ATOM   768  C C   . THR A 1 85  ? 20.811 28.855  8.196   1.00 15.70  ? 85  THR A C   1 
ATOM   769  O O   . THR A 1 85  ? 20.556 30.044  7.954   1.00 17.53  ? 85  THR A O   1 
ATOM   770  C CB  . THR A 1 85  ? 22.256 27.572  6.671   1.00 13.78  ? 85  THR A CB  1 
ATOM   771  O OG1 . THR A 1 85  ? 23.586 27.083  6.438   1.00 17.00  ? 85  THR A OG1 1 
ATOM   772  C CG2 . THR A 1 85  ? 21.876 28.496  5.536   1.00 17.11  ? 85  THR A CG2 1 
ATOM   773  N N   . PHE A 1 86  ? 19.887 28.014  8.654   1.00 13.13  ? 86  PHE A N   1 
ATOM   774  C CA  . PHE A 1 86  ? 18.481 28.394  8.712   1.00 14.26  ? 86  PHE A CA  1 
ATOM   775  C C   . PHE A 1 86  ? 17.986 28.657  10.134  1.00 14.81  ? 86  PHE A C   1 
ATOM   776  O O   . PHE A 1 86  ? 16.777 28.625  10.385  1.00 17.04  ? 86  PHE A O   1 
ATOM   777  C CB  . PHE A 1 86  ? 17.637 27.344  7.992   1.00 12.98  ? 86  PHE A CB  1 
ATOM   778  C CG  . PHE A 1 86  ? 17.935 27.256  6.521   1.00 15.23  ? 86  PHE A CG  1 
ATOM   779  C CD1 . PHE A 1 86  ? 17.586 28.310  5.674   1.00 16.46  ? 86  PHE A CD1 1 
ATOM   780  C CD2 . PHE A 1 86  ? 18.542 26.132  5.980   1.00 13.35  ? 86  PHE A CD2 1 
ATOM   781  C CE1 . PHE A 1 86  ? 17.852 28.244  4.300   1.00 18.13  ? 86  PHE A CE1 1 
ATOM   782  C CE2 . PHE A 1 86  ? 18.815 26.059  4.608   1.00 16.17  ? 86  PHE A CE2 1 
ATOM   783  C CZ  . PHE A 1 86  ? 18.472 27.126  3.767   1.00 17.15  ? 86  PHE A CZ  1 
ATOM   784  N N   . GLY A 1 87  ? 18.889 28.953  11.054  1.00 13.79  ? 87  GLY A N   1 
ATOM   785  C CA  . GLY A 1 87  ? 18.482 29.406  12.374  1.00 15.69  ? 87  GLY A CA  1 
ATOM   786  C C   . GLY A 1 87  ? 17.917 28.319  13.266  1.00 17.54  ? 87  GLY A C   1 
ATOM   787  O O   . GLY A 1 87  ? 17.117 28.611  14.171  1.00 17.61  ? 87  GLY A O   1 
ATOM   788  N N   A LEU A 1 88  ? 18.296 27.062  13.022  0.54 14.53  ? 88  LEU A N   1 
ATOM   789  N N   B LEU A 1 88  ? 18.320 27.071  13.048  0.46 14.51  ? 88  LEU A N   1 
ATOM   790  C CA  A LEU A 1 88  ? 17.786 25.900  13.740  0.54 14.53  ? 88  LEU A CA  1 
ATOM   791  C CA  B LEU A 1 88  ? 17.782 25.926  13.770  0.46 14.65  ? 88  LEU A CA  1 
ATOM   792  C C   A LEU A 1 88  ? 18.853 25.282  14.632  0.54 14.27  ? 88  LEU A C   1 
ATOM   793  C C   B LEU A 1 88  ? 18.863 25.278  14.621  0.46 14.27  ? 88  LEU A C   1 
ATOM   794  O O   A LEU A 1 88  ? 18.780 24.096  14.948  0.54 13.95  ? 88  LEU A O   1 
ATOM   795  O O   B LEU A 1 88  ? 18.811 24.084  14.904  0.46 13.98  ? 88  LEU A O   1 
ATOM   796  C CB  A LEU A 1 88  ? 17.214 24.867  12.765  0.54 13.14  ? 88  LEU A CB  1 
ATOM   797  C CB  B LEU A 1 88  ? 17.131 24.935  12.809  0.46 13.21  ? 88  LEU A CB  1 
ATOM   798  C CG  A LEU A 1 88  ? 15.926 25.239  12.023  0.54 13.96  ? 88  LEU A CG  1 
ATOM   799  C CG  B LEU A 1 88  ? 16.017 25.616  12.005  0.46 11.74  ? 88  LEU A CG  1 
ATOM   800  C CD1 A LEU A 1 88  ? 15.824 24.440  10.726  0.54 12.49  ? 88  LEU A CD1 1 
ATOM   801  C CD1 B LEU A 1 88  ? 15.434 24.665  10.970  0.46 14.09  ? 88  LEU A CD1 1 
ATOM   802  C CD2 A LEU A 1 88  ? 14.696 24.999  12.904  0.54 12.29  ? 88  LEU A CD2 1 
ATOM   803  C CD2 B LEU A 1 88  ? 14.936 26.152  12.938  0.46 15.86  ? 88  LEU A CD2 1 
ATOM   804  N N   . TYR A 1 89  ? 19.856 26.064  15.039  1.00 13.66  ? 89  TYR A N   1 
ATOM   805  C CA  . TYR A 1 89  ? 20.967 25.527  15.817  1.00 12.69  ? 89  TYR A CA  1 
ATOM   806  C C   . TYR A 1 89  ? 21.311 26.394  17.020  1.00 14.22  ? 89  TYR A C   1 
ATOM   807  O O   . TYR A 1 89  ? 22.473 26.440  17.443  1.00 15.85  ? 89  TYR A O   1 
ATOM   808  C CB  . TYR A 1 89  ? 22.196 25.258  14.943  1.00 13.54  ? 89  TYR A CB  1 
ATOM   809  C CG  . TYR A 1 89  ? 22.986 24.064  15.436  1.00 11.95  ? 89  TYR A CG  1 
ATOM   810  C CD1 . TYR A 1 89  ? 22.488 22.760  15.302  1.00 13.21  ? 89  TYR A CD1 1 
ATOM   811  C CD2 . TYR A 1 89  ? 24.227 24.229  16.036  1.00 14.88  ? 89  TYR A CD2 1 
ATOM   812  C CE1 . TYR A 1 89  ? 23.182 21.652  15.776  1.00 12.42  ? 89  TYR A CE1 1 
ATOM   813  C CE2 . TYR A 1 89  ? 24.937 23.101  16.507  1.00 14.18  ? 89  TYR A CE2 1 
ATOM   814  C CZ  . TYR A 1 89  ? 24.400 21.824  16.374  1.00 12.88  ? 89  TYR A CZ  1 
ATOM   815  O OH  . TYR A 1 89  ? 25.084 20.729  16.844  1.00 15.33  ? 89  TYR A OH  1 
ATOM   816  N N   . GLY A 1 90  ? 20.318 27.072  17.586  1.00 16.07  ? 90  GLY A N   1 
ATOM   817  C CA  . GLY A 1 90  ? 20.529 27.871  18.787  1.00 17.53  ? 90  GLY A CA  1 
ATOM   818  C C   . GLY A 1 90  ? 21.322 29.139  18.540  1.00 16.98  ? 90  GLY A C   1 
ATOM   819  O O   . GLY A 1 90  ? 21.725 29.459  17.427  1.00 19.65  ? 90  GLY A O   1 
ATOM   820  N N   . ASP A 1 91  ? 21.564 29.862  19.644  1.00 17.77  ? 91  ASP A N   1 
ATOM   821  C CA  . ASP A 1 91  ? 22.130 31.204  19.600  1.00 23.12  ? 91  ASP A CA  1 
ATOM   822  C C   . ASP A 1 91  ? 23.442 31.345  20.351  1.00 22.59  ? 91  ASP A C   1 
ATOM   823  O O   . ASP A 1 91  ? 24.117 32.367  20.186  1.00 24.51  ? 91  ASP A O   1 
ATOM   824  C CB  . ASP A 1 91  ? 21.148 32.225  20.197  1.00 27.77  ? 91  ASP A CB  1 
ATOM   825  C CG  . ASP A 1 91  ? 19.831 32.246  19.473  1.00 37.94  ? 91  ASP A CG  1 
ATOM   826  O OD1 . ASP A 1 91  ? 19.852 32.218  18.224  1.00 33.65  ? 91  ASP A OD1 1 
ATOM   827  O OD2 . ASP A 1 91  ? 18.781 32.287  20.151  1.00 40.97  ? 91  ASP A OD2 1 
ATOM   828  N N   . ASN A 1 92  ? 23.822 30.365  21.164  1.00 18.68  ? 92  ASN A N   1 
ATOM   829  C CA  . ASN A 1 92  ? 25.060 30.447  21.923  1.00 18.24  ? 92  ASN A CA  1 
ATOM   830  C C   . ASN A 1 92  ? 25.513 29.039  22.261  1.00 17.54  ? 92  ASN A C   1 
ATOM   831  O O   . ASN A 1 92  ? 24.788 28.061  22.048  1.00 15.93  ? 92  ASN A O   1 
ATOM   832  C CB  . ASN A 1 92  ? 24.887 31.307  23.176  1.00 19.49  ? 92  ASN A CB  1 
ATOM   833  C CG  . ASN A 1 92  ? 23.752 30.845  24.038  1.00 22.31  ? 92  ASN A CG  1 
ATOM   834  O OD1 . ASN A 1 92  ? 23.717 29.705  24.478  1.00 21.74  ? 92  ASN A OD1 1 
ATOM   835  N ND2 . ASN A 1 92  ? 22.818 31.748  24.321  1.00 28.81  ? 92  ASN A ND2 1 
ATOM   836  N N   . ALA A 1 93  ? 26.737 28.948  22.785  1.00 17.38  ? 93  ALA A N   1 
ATOM   837  C CA  . ALA A 1 93  ? 27.349 27.637  22.996  1.00 16.78  ? 93  ALA A CA  1 
ATOM   838  C C   . ALA A 1 93  ? 26.623 26.838  24.067  1.00 15.16  ? 93  ALA A C   1 
ATOM   839  O O   . ALA A 1 93  ? 26.623 25.602  24.023  1.00 15.90  ? 93  ALA A O   1 
ATOM   840  C CB  . ALA A 1 93  ? 28.828 27.788  23.361  1.00 18.82  ? 93  ALA A CB  1 
ATOM   841  N N   . ALA A 1 94  ? 26.010 27.516  25.039  1.00 15.57  ? 94  ALA A N   1 
ATOM   842  C CA  . ALA A 1 94  ? 25.276 26.800  26.078  1.00 15.16  ? 94  ALA A CA  1 
ATOM   843  C C   . ALA A 1 94  ? 24.041 26.125  25.507  1.00 16.25  ? 94  ALA A C   1 
ATOM   844  O O   . ALA A 1 94  ? 23.759 24.954  25.810  1.00 16.12  ? 94  ALA A O   1 
ATOM   845  C CB  . ALA A 1 94  ? 24.885 27.762  27.196  1.00 18.59  ? 94  ALA A CB  1 
ATOM   846  N N   A GLU A 1 95  ? 23.297 26.841  24.678  0.15 16.66  ? 95  GLU A N   1 
ATOM   847  N N   B GLU A 1 95  ? 23.283 26.842  24.666  0.85 16.57  ? 95  GLU A N   1 
ATOM   848  C CA  A GLU A 1 95  ? 22.177 26.212  24.008  0.15 16.13  ? 95  GLU A CA  1 
ATOM   849  C CA  B GLU A 1 95  ? 22.159 26.213  23.973  0.85 16.02  ? 95  GLU A CA  1 
ATOM   850  C C   A GLU A 1 95  ? 22.654 25.061  23.132  0.15 13.65  ? 95  GLU A C   1 
ATOM   851  C C   B GLU A 1 95  ? 22.629 25.076  23.084  0.85 13.52  ? 95  GLU A C   1 
ATOM   852  O O   A GLU A 1 95  ? 22.024 23.996  23.094  0.15 13.67  ? 95  GLU A O   1 
ATOM   853  O O   B GLU A 1 95  ? 21.980 24.021  23.011  0.85 13.59  ? 95  GLU A O   1 
ATOM   854  C CB  A GLU A 1 95  ? 21.446 27.254  23.180  0.15 16.99  ? 95  GLU A CB  1 
ATOM   855  C CB  B GLU A 1 95  ? 21.410 27.247  23.134  0.85 16.96  ? 95  GLU A CB  1 
ATOM   856  C CG  A GLU A 1 95  ? 20.160 26.740  22.680  0.15 13.64  ? 95  GLU A CG  1 
ATOM   857  C CG  B GLU A 1 95  ? 20.756 28.306  23.986  0.85 19.65  ? 95  GLU A CG  1 
ATOM   858  C CD  A GLU A 1 95  ? 20.284 26.107  21.332  0.15 19.28  ? 95  GLU A CD  1 
ATOM   859  C CD  B GLU A 1 95  ? 19.961 29.307  23.179  0.85 28.89  ? 95  GLU A CD  1 
ATOM   860  O OE1 A GLU A 1 95  ? 21.425 25.952  20.856  0.15 19.38  ? 95  GLU A OE1 1 
ATOM   861  O OE1 B GLU A 1 95  ? 19.901 29.185  21.936  0.85 20.94  ? 95  GLU A OE1 1 
ATOM   862  O OE2 A GLU A 1 95  ? 19.242 25.782  20.736  0.15 25.33  ? 95  GLU A OE2 1 
ATOM   863  O OE2 B GLU A 1 95  ? 19.399 30.228  23.805  0.85 27.94  ? 95  GLU A OE2 1 
ATOM   864  N N   . VAL A 1 96  ? 23.762 25.261  22.410  1.00 13.67  ? 96  VAL A N   1 
ATOM   865  C CA  . VAL A 1 96  ? 24.268 24.225  21.522  1.00 13.77  ? 96  VAL A CA  1 
ATOM   866  C C   . VAL A 1 96  ? 24.665 22.994  22.320  1.00 13.05  ? 96  VAL A C   1 
ATOM   867  O O   . VAL A 1 96  ? 24.493 21.868  21.851  1.00 13.05  ? 96  VAL A O   1 
ATOM   868  C CB  . VAL A 1 96  ? 25.416 24.753  20.643  1.00 13.30  ? 96  VAL A CB  1 
ATOM   869  C CG1 . VAL A 1 96  ? 26.044 23.622  19.851  1.00 14.17  ? 96  VAL A CG1 1 
ATOM   870  C CG2 . VAL A 1 96  ? 24.877 25.808  19.696  1.00 14.20  ? 96  VAL A CG2 1 
ATOM   871  N N   . TYR A 1 97  ? 25.196 23.174  23.535  1.00 12.71  ? 97  TYR A N   1 
ATOM   872  C CA  . TYR A 1 97  ? 25.467 21.998  24.361  1.00 13.54  ? 97  TYR A CA  1 
ATOM   873  C C   . TYR A 1 97  ? 24.193 21.185  24.592  1.00 14.05  ? 97  TYR A C   1 
ATOM   874  O O   . TYR A 1 97  ? 24.206 19.940  24.521  1.00 12.94  ? 97  TYR A O   1 
ATOM   875  C CB  . TYR A 1 97  ? 26.131 22.391  25.700  1.00 12.64  ? 97  TYR A CB  1 
ATOM   876  C CG  . TYR A 1 97  ? 26.252 21.168  26.565  1.00 13.00  ? 97  TYR A CG  1 
ATOM   877  C CD1 . TYR A 1 97  ? 27.236 20.196  26.318  1.00 14.44  ? 97  TYR A CD1 1 
ATOM   878  C CD2 . TYR A 1 97  ? 25.313 20.913  27.550  1.00 14.64  ? 97  TYR A CD2 1 
ATOM   879  C CE1 . TYR A 1 97  ? 27.289 19.011  27.061  1.00 13.76  ? 97  TYR A CE1 1 
ATOM   880  C CE2 . TYR A 1 97  ? 25.357 19.745  28.297  1.00 14.28  ? 97  TYR A CE2 1 
ATOM   881  C CZ  . TYR A 1 97  ? 26.328 18.803  28.051  1.00 14.40  ? 97  TYR A CZ  1 
ATOM   882  O OH  . TYR A 1 97  ? 26.313 17.646  28.826  1.00 16.92  ? 97  TYR A OH  1 
ATOM   883  N N   . LEU A 1 98  ? 23.076 21.858  24.887  1.00 12.17  ? 98  LEU A N   1 
ATOM   884  C CA  . LEU A 1 98  ? 21.821 21.136  25.060  1.00 11.79  ? 98  LEU A CA  1 
ATOM   885  C C   . LEU A 1 98  ? 21.433 20.394  23.787  1.00 11.80  ? 98  LEU A C   1 
ATOM   886  O O   . LEU A 1 98  ? 20.978 19.237  23.851  1.00 13.09  ? 98  LEU A O   1 
ATOM   887  C CB  . LEU A 1 98  ? 20.703 22.093  25.489  1.00 14.27  ? 98  LEU A CB  1 
ATOM   888  C CG  . LEU A 1 98  ? 20.940 22.704  26.865  1.00 15.71  ? 98  LEU A CG  1 
ATOM   889  C CD1 . LEU A 1 98  ? 19.793 23.665  27.220  1.00 21.61  ? 98  LEU A CD1 1 
ATOM   890  C CD2 . LEU A 1 98  ? 21.085 21.623  27.936  1.00 18.60  ? 98  LEU A CD2 1 
ATOM   891  N N   . ILE A 1 99  ? 21.583 21.038  22.622  1.00 12.17  ? 99  ILE A N   1 
ATOM   892  C CA  . ILE A 1 99  ? 21.288 20.358  21.357  1.00 14.46  ? 99  ILE A CA  1 
ATOM   893  C C   . ILE A 1 99  ? 22.143 19.114  21.218  1.00 13.17  ? 99  ILE A C   1 
ATOM   894  O O   . ILE A 1 99  ? 21.653 18.034  20.859  1.00 12.54  ? 99  ILE A O   1 
ATOM   895  C CB  . ILE A 1 99  ? 21.537 21.305  20.168  1.00 11.55  ? 99  ILE A CB  1 
ATOM   896  C CG1 . ILE A 1 99  ? 20.611 22.516  20.198  1.00 13.12  ? 99  ILE A CG1 1 
ATOM   897  C CG2 . ILE A 1 99  ? 21.443 20.556  18.853  1.00 13.84  ? 99  ILE A CG2 1 
ATOM   898  C CD1 . ILE A 1 99  ? 20.939 23.559  19.092  1.00 14.49  ? 99  ILE A CD1 1 
ATOM   899  N N   . GLU A 1 100 ? 23.453 19.269  21.432  1.00 11.50  ? 100 GLU A N   1 
ATOM   900  C CA  . GLU A 1 100 ? 24.406 18.218  21.107  1.00 13.29  ? 100 GLU A CA  1 
ATOM   901  C C   . GLU A 1 100 ? 24.406 17.116  22.148  1.00 12.32  ? 100 GLU A C   1 
ATOM   902  O O   . GLU A 1 100 ? 24.656 15.957  21.807  1.00 14.11  ? 100 GLU A O   1 
ATOM   903  C CB  . GLU A 1 100 ? 25.801 18.818  20.925  1.00 13.81  ? 100 GLU A CB  1 
ATOM   904  C CG  . GLU A 1 100 ? 25.854 19.637  19.641  1.00 13.21  ? 100 GLU A CG  1 
ATOM   905  C CD  . GLU A 1 100 ? 27.151 20.353  19.385  1.00 14.65  ? 100 GLU A CD  1 
ATOM   906  O OE1 . GLU A 1 100 ? 28.072 20.334  20.239  1.00 14.26  ? 100 GLU A OE1 1 
ATOM   907  O OE2 . GLU A 1 100 ? 27.237 20.948  18.281  1.00 14.66  ? 100 GLU A OE2 1 
ATOM   908  N N   A ARG A 1 101 ? 24.118 17.435  23.408  0.53 12.06  ? 101 ARG A N   1 
ATOM   909  N N   B ARG A 1 101 ? 24.102 17.441  23.407  0.47 12.08  ? 101 ARG A N   1 
ATOM   910  C CA  A ARG A 1 101 ? 23.935 16.371  24.389  0.53 13.54  ? 101 ARG A CA  1 
ATOM   911  C CA  B ARG A 1 101 ? 23.925 16.397  24.413  0.47 13.54  ? 101 ARG A CA  1 
ATOM   912  C C   A ARG A 1 101 ? 22.764 15.489  23.991  0.53 13.40  ? 101 ARG A C   1 
ATOM   913  C C   B ARG A 1 101 ? 22.754 15.504  24.044  0.47 13.34  ? 101 ARG A C   1 
ATOM   914  O O   A ARG A 1 101 ? 22.878 14.255  23.947  0.53 13.72  ? 101 ARG A O   1 
ATOM   915  O O   B ARG A 1 101 ? 22.852 14.268  24.089  0.47 14.13  ? 101 ARG A O   1 
ATOM   916  C CB  A ARG A 1 101 ? 23.701 16.973  25.771  0.53 12.60  ? 101 ARG A CB  1 
ATOM   917  C CB  B ARG A 1 101 ? 23.687 17.027  25.784  0.47 12.57  ? 101 ARG A CB  1 
ATOM   918  C CG  A ARG A 1 101 ? 23.598 15.911  26.875  0.53 14.40  ? 101 ARG A CG  1 
ATOM   919  C CG  B ARG A 1 101 ? 23.459 16.006  26.912  0.47 14.88  ? 101 ARG A CG  1 
ATOM   920  C CD  A ARG A 1 101 ? 23.361 16.574  28.222  0.53 19.85  ? 101 ARG A CD  1 
ATOM   921  C CD  B ARG A 1 101 ? 22.967 16.719  28.168  0.47 18.24  ? 101 ARG A CD  1 
ATOM   922  N NE  A ARG A 1 101 ? 22.039 17.186  28.282  0.53 20.03  ? 101 ARG A NE  1 
ATOM   923  N NE  B ARG A 1 101 ? 23.190 15.941  29.381  0.47 17.85  ? 101 ARG A NE  1 
ATOM   924  C CZ  A ARG A 1 101 ? 21.581 17.883  29.312  0.53 24.19  ? 101 ARG A CZ  1 
ATOM   925  C CZ  B ARG A 1 101 ? 22.339 15.047  29.867  0.47 23.85  ? 101 ARG A CZ  1 
ATOM   926  N NH1 A ARG A 1 101 ? 22.321 18.091  30.391  0.53 27.56  ? 101 ARG A NH1 1 
ATOM   927  N NH1 B ARG A 1 101 ? 21.207 14.760  29.244  0.47 21.23  ? 101 ARG A NH1 1 
ATOM   928  N NH2 A ARG A 1 101 ? 20.351 18.386  29.256  0.53 25.03  ? 101 ARG A NH2 1 
ATOM   929  N NH2 B ARG A 1 101 ? 22.634 14.423  31.006  0.47 25.63  ? 101 ARG A NH2 1 
ATOM   930  N N   . MET A 1 102 ? 21.632 16.113  23.653  1.00 13.05  ? 102 MET A N   1 
ATOM   931  C CA  A MET A 1 102 ? 20.461 15.342  23.252  0.00 13.67  ? 102 MET A CA  1 
ATOM   932  C CA  B MET A 1 102 ? 20.480 15.311  23.269  1.00 13.53  ? 102 MET A CA  1 
ATOM   933  C C   . MET A 1 102 ? 20.729 14.568  21.970  1.00 15.25  ? 102 MET A C   1 
ATOM   934  O O   . MET A 1 102 ? 20.367 13.397  21.855  1.00 14.75  ? 102 MET A O   1 
ATOM   935  C CB  A MET A 1 102 ? 19.258 16.269  23.081  0.00 14.01  ? 102 MET A CB  1 
ATOM   936  C CB  B MET A 1 102 ? 19.230 16.174  23.153  1.00 13.90  ? 102 MET A CB  1 
ATOM   937  C CG  A MET A 1 102 ? 17.944 15.545  22.831  0.00 15.24  ? 102 MET A CG  1 
ATOM   938  C CG  B MET A 1 102 ? 17.972 15.319  22.995  1.00 15.19  ? 102 MET A CG  1 
ATOM   939  S SD  A MET A 1 102 ? 17.430 14.526  24.226  0.00 17.10  ? 102 MET A SD  1 
ATOM   940  S SD  B MET A 1 102 ? 17.585 14.283  24.430  1.00 17.88  ? 102 MET A SD  1 
ATOM   941  C CE  A MET A 1 102 ? 16.837 15.781  25.357  0.00 19.82  ? 102 MET A CE  1 
ATOM   942  C CE  B MET A 1 102 ? 16.619 15.441  25.360  1.00 21.23  ? 102 MET A CE  1 
ATOM   943  N N   . ASN A 1 103 ? 21.354 15.205  20.991  1.00 14.00  ? 103 ASN A N   1 
ATOM   944  C CA  . ASN A 1 103 ? 21.615 14.492  19.745  1.00 15.37  ? 103 ASN A CA  1 
ATOM   945  C C   . ASN A 1 103 ? 22.587 13.345  19.939  1.00 17.19  ? 103 ASN A C   1 
ATOM   946  O O   . ASN A 1 103 ? 22.481 12.334  19.239  1.00 16.36  ? 103 ASN A O   1 
ATOM   947  C CB  . ASN A 1 103 ? 22.100 15.450  18.660  1.00 17.79  ? 103 ASN A CB  1 
ATOM   948  C CG  . ASN A 1 103 ? 20.956 16.197  18.017  1.00 17.87  ? 103 ASN A CG  1 
ATOM   949  O OD1 . ASN A 1 103 ? 19.791 15.820  18.167  1.00 19.94  ? 103 ASN A OD1 1 
ATOM   950  N ND2 . ASN A 1 103 ? 21.276 17.257  17.294  1.00 20.66  ? 103 ASN A ND2 1 
ATOM   951  N N   . SER A 1 104 ? 23.516 13.454  20.887  1.00 15.79  ? 104 SER A N   1 
ATOM   952  C CA  . SER A 1 104 ? 24.391 12.325  21.167  1.00 17.17  ? 104 SER A CA  1 
ATOM   953  C C   . SER A 1 104 ? 23.582 11.143  21.667  1.00 18.09  ? 104 SER A C   1 
ATOM   954  O O   . SER A 1 104 ? 23.789 10.007  21.220  1.00 19.32  ? 104 SER A O   1 
ATOM   955  C CB  . SER A 1 104 ? 25.413 12.721  22.224  1.00 16.19  ? 104 SER A CB  1 
ATOM   956  O OG  . SER A 1 104 ? 26.237 11.607  22.548  1.00 23.01  ? 104 SER A OG  1 
ATOM   957  N N   . LEU A 1 105 ? 22.639 11.392  22.578  1.00 15.16  ? 105 LEU A N   1 
ATOM   958  C CA  . LEU A 1 105 ? 21.813 10.323  23.122  1.00 16.69  ? 105 LEU A CA  1 
ATOM   959  C C   . LEU A 1 105 ? 20.913 9.726   22.051  1.00 20.15  ? 105 LEU A C   1 
ATOM   960  O O   . LEU A 1 105 ? 20.833 8.501   21.908  1.00 20.10  ? 105 LEU A O   1 
ATOM   961  C CB  . LEU A 1 105 ? 20.964 10.860  24.273  1.00 16.41  ? 105 LEU A CB  1 
ATOM   962  C CG  . LEU A 1 105 ? 21.721 11.207  25.553  1.00 19.09  ? 105 LEU A CG  1 
ATOM   963  C CD1 . LEU A 1 105 ? 20.791 11.923  26.516  1.00 19.75  ? 105 LEU A CD1 1 
ATOM   964  C CD2 . LEU A 1 105 ? 22.265 9.946   26.204  1.00 20.54  ? 105 LEU A CD2 1 
ATOM   965  N N   . THR A 1 106 ? 20.224 10.574  21.287  1.00 17.06  ? 106 THR A N   1 
ATOM   966  C CA  . THR A 1 106 ? 19.272 10.060  20.306  1.00 16.62  ? 106 THR A CA  1 
ATOM   967  C C   . THR A 1 106 ? 19.972 9.429   19.108  1.00 18.74  ? 106 THR A C   1 
ATOM   968  O O   . THR A 1 106 ? 19.489 8.420   18.580  1.00 20.01  ? 106 THR A O   1 
ATOM   969  C CB  . THR A 1 106 ? 18.266 11.146  19.890  1.00 16.29  ? 106 THR A CB  1 
ATOM   970  O OG1 . THR A 1 106 ? 18.942 12.249  19.295  1.00 18.35  ? 106 THR A OG1 1 
ATOM   971  C CG2 . THR A 1 106 ? 17.470 11.649  21.090  1.00 16.95  ? 106 THR A CG2 1 
ATOM   972  N N   . SER A 1 107 ? 21.121 9.966   18.679  1.00 17.22  ? 107 SER A N   1 
ATOM   973  C CA  . SER A 1 107 ? 21.879 9.313   17.609  1.00 19.43  ? 107 SER A CA  1 
ATOM   974  C C   . SER A 1 107 ? 22.362 7.936   18.040  1.00 21.69  ? 107 SER A C   1 
ATOM   975  O O   . SER A 1 107 ? 22.309 6.971   17.256  1.00 22.33  ? 107 SER A O   1 
ATOM   976  C CB  . SER A 1 107 ? 23.093 10.150  17.220  1.00 20.34  ? 107 SER A CB  1 
ATOM   977  O OG  . SER A 1 107 ? 22.720 11.350  16.552  1.00 23.03  ? 107 SER A OG  1 
ATOM   978  N N   . SER A 1 108 ? 22.877 7.832   19.266  1.00 20.65  ? 108 SER A N   1 
ATOM   979  C CA  . SER A 1 108 ? 23.347 6.543   19.760  1.00 22.79  ? 108 SER A CA  1 
ATOM   980  C C   . SER A 1 108 ? 22.198 5.559   19.870  1.00 25.34  ? 108 SER A C   1 
ATOM   981  O O   . SER A 1 108 ? 22.326 4.403   19.453  1.00 23.57  ? 108 SER A O   1 
ATOM   982  C CB  . SER A 1 108 ? 24.042 6.723   21.108  1.00 22.63  ? 108 SER A CB  1 
ATOM   983  O OG  . SER A 1 108 ? 25.306 7.326   20.907  1.00 25.86  ? 108 SER A OG  1 
ATOM   984  N N   . LEU A 1 109 ? 21.052 6.004   20.394  1.00 21.24  ? 109 LEU A N   1 
ATOM   985  C CA  . LEU A 1 109 ? 19.903 5.112   20.496  1.00 20.56  ? 109 LEU A CA  1 
ATOM   986  C C   . LEU A 1 109 ? 19.430 4.672   19.117  1.00 21.93  ? 109 LEU A C   1 
ATOM   987  O O   . LEU A 1 109 ? 19.137 3.490   18.905  1.00 23.83  ? 109 LEU A O   1 
ATOM   988  C CB  . LEU A 1 109 ? 18.784 5.797   21.280  1.00 20.82  ? 109 LEU A CB  1 
ATOM   989  C CG  . LEU A 1 109 ? 17.480 5.018   21.441  1.00 21.42  ? 109 LEU A CG  1 
ATOM   990  C CD1 . LEU A 1 109 ? 17.718 3.601   21.979  1.00 23.15  ? 109 LEU A CD1 1 
ATOM   991  C CD2 . LEU A 1 109 ? 16.487 5.763   22.334  1.00 22.13  ? 109 LEU A CD2 1 
ATOM   992  N N   . LEU A 1 110 ? 19.393 5.597   18.151  1.00 18.70  ? 110 LEU A N   1 
ATOM   993  C CA  . LEU A 1 110 ? 19.018 5.237   16.782  1.00 19.05  ? 110 LEU A CA  1 
ATOM   994  C C   . LEU A 1 110 ? 19.919 4.144   16.232  1.00 23.38  ? 110 LEU A C   1 
ATOM   995  O O   . LEU A 1 110 ? 19.434 3.153   15.671  1.00 24.28  ? 110 LEU A O   1 
ATOM   996  C CB  . LEU A 1 110 ? 19.094 6.462   15.878  1.00 21.40  ? 110 LEU A CB  1 
ATOM   997  C CG  . LEU A 1 110 ? 17.884 7.378   15.963  1.00 17.74  ? 110 LEU A CG  1 
ATOM   998  C CD1 . LEU A 1 110 ? 18.221 8.700   15.279  1.00 20.63  ? 110 LEU A CD1 1 
ATOM   999  C CD2 . LEU A 1 110 ? 16.674 6.745   15.301  1.00 21.18  ? 110 LEU A CD2 1 
ATOM   1000 N N   . GLU A 1 111 ? 21.235 4.325   16.344  1.00 20.33  ? 111 GLU A N   1 
ATOM   1001 C CA  . GLU A 1 111 ? 22.164 3.334   15.798  1.00 25.11  ? 111 GLU A CA  1 
ATOM   1002 C C   . GLU A 1 111 ? 22.032 1.984   16.508  1.00 25.72  ? 111 GLU A C   1 
ATOM   1003 O O   . GLU A 1 111 ? 22.173 0.930   15.868  1.00 28.80  ? 111 GLU A O   1 
ATOM   1004 C CB  . GLU A 1 111 ? 23.601 3.858   15.856  1.00 25.57  ? 111 GLU A CB  1 
ATOM   1005 C CG  . GLU A 1 111 ? 23.919 5.004   14.878  1.00 26.37  ? 111 GLU A CG  1 
ATOM   1006 C CD  . GLU A 1 111 ? 23.681 4.646   13.416  1.00 30.18  ? 111 GLU A CD  1 
ATOM   1007 O OE1 . GLU A 1 111 ? 23.888 3.472   13.042  1.00 31.57  ? 111 GLU A OE1 1 
ATOM   1008 O OE2 . GLU A 1 111 ? 23.315 5.546   12.629  1.00 27.50  ? 111 GLU A OE2 1 
ATOM   1009 N N   . GLU A 1 112 ? 21.749 1.988   17.815  1.00 24.88  ? 112 GLU A N   1 
ATOM   1010 C CA  . GLU A 1 112 ? 21.514 0.734   18.536  1.00 25.91  ? 112 GLU A CA  1 
ATOM   1011 C C   . GLU A 1 112 ? 20.244 0.043   18.055  1.00 32.79  ? 112 GLU A C   1 
ATOM   1012 O O   . GLU A 1 112 ? 20.211 -1.187  17.916  1.00 37.70  ? 112 GLU A O   1 
ATOM   1013 C CB  . GLU A 1 112 ? 21.410 0.991   20.039  1.00 28.45  ? 112 GLU A CB  1 
ATOM   1014 C CG  . GLU A 1 112 ? 22.694 1.436   20.706  1.00 45.29  ? 112 GLU A CG  1 
ATOM   1015 C CD  . GLU A 1 112 ? 23.230 0.392   21.664  1.00 57.99  ? 112 GLU A CD  1 
ATOM   1016 O OE1 . GLU A 1 112 ? 22.466 -0.528  22.028  1.00 67.31  ? 112 GLU A OE1 1 
ATOM   1017 O OE2 . GLU A 1 112 ? 24.410 0.498   22.060  1.00 63.85  ? 112 GLU A OE2 1 
ATOM   1018 N N   . ILE A 1 113 ? 19.182 0.813   17.820  1.00 22.83  ? 113 ILE A N   1 
ATOM   1019 C CA  . ILE A 1 113 ? 17.940 0.235   17.318  1.00 24.85  ? 113 ILE A CA  1 
ATOM   1020 C C   . ILE A 1 113 ? 18.150 -0.335  15.923  1.00 33.63  ? 113 ILE A C   1 
ATOM   1021 O O   . ILE A 1 113 ? 17.700 -1.447  15.617  1.00 33.06  ? 113 ILE A O   1 
ATOM   1022 C CB  . ILE A 1 113 ? 16.819 1.287   17.343  1.00 27.19  ? 113 ILE A CB  1 
ATOM   1023 C CG1 . ILE A 1 113 ? 16.476 1.677   18.774  1.00 26.53  ? 113 ILE A CG1 1 
ATOM   1024 C CG2 . ILE A 1 113 ? 15.575 0.758   16.665  1.00 29.34  ? 113 ILE A CG2 1 
ATOM   1025 C CD1 . ILE A 1 113 ? 15.576 2.891   18.855  1.00 26.07  ? 113 ILE A CD1 1 
ATOM   1026 N N   . TYR A 1 114 ? 18.842 0.414   15.057  1.00 28.73  ? 114 TYR A N   1 
ATOM   1027 C CA  . TYR A 1 114 ? 19.111 -0.072  13.706  1.00 33.58  ? 114 TYR A CA  1 
ATOM   1028 C C   . TYR A 1 114 ? 19.855 -1.400  13.736  1.00 41.05  ? 114 TYR A C   1 
ATOM   1029 O O   . TYR A 1 114 ? 19.561 -2.304  12.944  1.00 48.51  ? 114 TYR A O   1 
ATOM   1030 C CB  . TYR A 1 114 ? 19.948 0.942   12.928  1.00 27.53  ? 114 TYR A CB  1 
ATOM   1031 C CG  . TYR A 1 114 ? 19.327 2.302   12.656  1.00 30.34  ? 114 TYR A CG  1 
ATOM   1032 C CD1 . TYR A 1 114 ? 17.951 2.489   12.636  1.00 30.51  ? 114 TYR A CD1 1 
ATOM   1033 C CD2 . TYR A 1 114 ? 20.139 3.397   12.389  1.00 25.46  ? 114 TYR A CD2 1 
ATOM   1034 C CE1 . TYR A 1 114 ? 17.403 3.749   12.363  1.00 31.39  ? 114 TYR A CE1 1 
ATOM   1035 C CE2 . TYR A 1 114 ? 19.609 4.652   12.117  1.00 29.18  ? 114 TYR A CE2 1 
ATOM   1036 C CZ  . TYR A 1 114 ? 18.246 4.827   12.106  1.00 30.20  ? 114 TYR A CZ  1 
ATOM   1037 O OH  . TYR A 1 114 ? 17.734 6.083   11.835  1.00 27.90  ? 114 TYR A OH  1 
ATOM   1038 N N   . ALA A 1 115 ? 20.826 -1.534  14.644  1.00 36.18  ? 115 ALA A N   1 
ATOM   1039 C CA  . ALA A 1 115 ? 21.674 -2.719  14.680  1.00 45.82  ? 115 ALA A CA  1 
ATOM   1040 C C   . ALA A 1 115 ? 20.955 -3.951  15.215  1.00 60.29  ? 115 ALA A C   1 
ATOM   1041 O O   . ALA A 1 115 ? 21.417 -5.072  14.976  1.00 70.11  ? 115 ALA A O   1 
ATOM   1042 C CB  . ALA A 1 115 ? 22.929 -2.438  15.510  1.00 41.84  ? 115 ALA A CB  1 
ATOM   1043 N N   . LEU A 1 116 ? 19.843 -3.777  15.923  1.00 47.55  ? 116 LEU A N   1 
ATOM   1044 C CA  . LEU A 1 116 ? 19.124 -4.893  16.524  1.00 65.13  ? 116 LEU A CA  1 
ATOM   1045 C C   . LEU A 1 116 ? 17.987 -5.411  15.656  1.00 69.19  ? 116 LEU A C   1 
ATOM   1046 O O   . LEU A 1 116 ? 17.339 -6.393  16.034  1.00 74.04  ? 116 LEU A O   1 
ATOM   1047 C CB  . LEU A 1 116 ? 18.574 -4.491  17.896  1.00 60.59  ? 116 LEU A CB  1 
ATOM   1048 C CG  . LEU A 1 116 ? 19.320 -4.972  19.141  1.00 74.33  ? 116 LEU A CG  1 
ATOM   1049 C CD1 . LEU A 1 116 ? 20.617 -5.694  18.789  1.00 78.63  ? 116 LEU A CD1 1 
ATOM   1050 C CD2 . LEU A 1 116 ? 19.599 -3.778  20.035  1.00 74.28  ? 116 LEU A CD2 1 
ATOM   1051 N N   . GLY A 1 117 ? 17.730 -4.779  14.510  1.00 60.46  ? 117 GLY A N   1 
ATOM   1052 C CA  . GLY A 1 117 ? 16.616 -5.205  13.679  1.00 65.15  ? 117 GLY A CA  1 
ATOM   1053 C C   . GLY A 1 117 ? 16.763 -6.633  13.191  1.00 80.33  ? 117 GLY A C   1 
ATOM   1054 O O   . GLY A 1 117 ? 15.833 -7.436  13.293  1.00 87.67  ? 117 GLY A O   1 
ATOM   1055 N N   . LEU A 1 118 ? 17.939 -6.972  12.657  1.00 83.37  ? 118 LEU A N   1 
ATOM   1056 C CA  . LEU A 1 118 ? 18.179 -8.295  12.098  1.00 93.15  ? 118 LEU A CA  1 
ATOM   1057 C C   . LEU A 1 118 ? 19.296 -9.081  12.771  1.00 101.95 ? 118 LEU A C   1 
ATOM   1058 O O   . LEU A 1 118 ? 19.489 -10.252 12.423  1.00 105.35 ? 118 LEU A O   1 
ATOM   1059 C CB  . LEU A 1 118 ? 18.464 -8.216  10.588  1.00 81.75  ? 118 LEU A CB  1 
ATOM   1060 C CG  . LEU A 1 118 ? 17.285 -8.446  9.636   1.00 79.98  ? 118 LEU A CG  1 
ATOM   1061 C CD1 . LEU A 1 118 ? 16.806 -9.887  9.738   1.00 84.11  ? 118 LEU A CD1 1 
ATOM   1062 C CD2 . LEU A 1 118 ? 16.138 -7.483  9.882   1.00 82.54  ? 118 LEU A CD2 1 
ATOM   1063 N N   . LYS A 1 119 ? 20.038 -8.481  13.709  1.00 100.04 ? 119 LYS A N   1 
ATOM   1064 C CA  . LYS A 1 119 ? 21.115 -9.204  14.383  1.00 107.96 ? 119 LYS A CA  1 
ATOM   1065 C C   . LYS A 1 119 ? 20.606 -10.486 15.032  1.00 120.11 ? 119 LYS A C   1 
ATOM   1066 O O   . LYS A 1 119 ? 21.250 -11.538 14.941  1.00 118.42 ? 119 LYS A O   1 
ATOM   1067 C CB  . LYS A 1 119 ? 21.785 -8.305  15.426  1.00 100.50 ? 119 LYS A CB  1 
ATOM   1068 C CG  . LYS A 1 119 ? 22.277 -9.050  16.664  1.00 108.31 ? 119 LYS A CG  1 
ATOM   1069 C CD  . LYS A 1 119 ? 23.255 -8.225  17.484  1.00 97.68  ? 119 LYS A CD  1 
ATOM   1070 C CE  . LYS A 1 119 ? 24.525 -9.011  17.780  1.00 82.33  ? 119 LYS A CE  1 
ATOM   1071 N NZ  . LYS A 1 119 ? 24.743 -10.118 16.809  1.00 78.82  ? 119 LYS A NZ  1 
ATOM   1072 N N   . LYS A 1 120 ? 19.446 -10.419 15.682  1.00 119.35 ? 120 LYS A N   1 
ATOM   1073 C CA  . LYS A 1 120 ? 18.852 -11.594 16.308  1.00 118.58 ? 120 LYS A CA  1 
ATOM   1074 C C   . LYS A 1 120 ? 17.407 -11.784 15.862  1.00 116.86 ? 120 LYS A C   1 
ATOM   1075 O O   . LYS A 1 120 ? 16.939 -12.921 15.746  1.00 118.52 ? 120 LYS A O   1 
ATOM   1076 C CB  . LYS A 1 120 ? 18.983 -11.542 17.838  1.00 112.65 ? 120 LYS A CB  1 
ATOM   1077 C CG  . LYS A 1 120 ? 18.045 -10.578 18.570  1.00 115.84 ? 120 LYS A CG  1 
ATOM   1078 C CD  . LYS A 1 120 ? 18.353 -9.114  18.273  1.00 108.94 ? 120 LYS A CD  1 
ATOM   1079 C CE  . LYS A 1 120 ? 17.366 -8.179  18.959  1.00 103.48 ? 120 LYS A CE  1 
ATOM   1080 N NZ  . LYS A 1 120 ? 16.307 -8.913  19.707  1.00 104.75 ? 120 LYS A NZ  1 
ATOM   1081 N N   . GLU A 1 129 ? 19.105 -6.783  24.960  1.00 102.16 ? 129 GLU A N   1 
ATOM   1082 C CA  . GLU A 1 129 ? 19.547 -5.400  24.748  1.00 96.74  ? 129 GLU A CA  1 
ATOM   1083 C C   . GLU A 1 129 ? 18.611 -4.312  25.265  1.00 82.90  ? 129 GLU A C   1 
ATOM   1084 O O   . GLU A 1 129 ? 18.971 -3.130  25.243  1.00 77.18  ? 129 GLU A O   1 
ATOM   1085 C CB  . GLU A 1 129 ? 19.849 -5.127  23.274  1.00 98.65  ? 129 GLU A CB  1 
ATOM   1086 C CG  . GLU A 1 129 ? 20.836 -6.068  22.632  1.00 103.01 ? 129 GLU A CG  1 
ATOM   1087 C CD  . GLU A 1 129 ? 22.152 -6.135  23.372  1.00 101.52 ? 129 GLU A CD  1 
ATOM   1088 O OE1 . GLU A 1 129 ? 22.779 -5.071  23.576  1.00 97.61  ? 129 GLU A OE1 1 
ATOM   1089 O OE2 . GLU A 1 129 ? 22.578 -7.256  23.714  1.00 98.98  ? 129 GLU A OE2 1 
ATOM   1090 N N   . ALA A 1 130 ? 17.416 -4.692  25.724  1.00 80.07  ? 130 ALA A N   1 
ATOM   1091 C CA  . ALA A 1 130 ? 16.537 -3.747  26.399  1.00 79.52  ? 130 ALA A CA  1 
ATOM   1092 C C   . ALA A 1 130 ? 17.259 -2.978  27.498  1.00 76.24  ? 130 ALA A C   1 
ATOM   1093 O O   . ALA A 1 130 ? 16.861 -1.859  27.822  1.00 72.92  ? 130 ALA A O   1 
ATOM   1094 C CB  . ALA A 1 130 ? 15.319 -4.478  26.968  1.00 78.26  ? 130 ALA A CB  1 
ATOM   1095 N N   . GLU A 1 131 ? 18.323 -3.547  28.076  1.00 76.76  ? 131 GLU A N   1 
ATOM   1096 C CA  . GLU A 1 131 ? 19.106 -2.829  29.085  1.00 77.21  ? 131 GLU A CA  1 
ATOM   1097 C C   . GLU A 1 131 ? 19.846 -1.637  28.491  1.00 70.09  ? 131 GLU A C   1 
ATOM   1098 O O   . GLU A 1 131 ? 19.719 -0.506  28.977  1.00 55.95  ? 131 GLU A O   1 
ATOM   1099 C CB  . GLU A 1 131 ? 20.086 -3.775  29.782  1.00 78.92  ? 131 GLU A CB  1 
ATOM   1100 C CG  . GLU A 1 131 ? 20.392 -3.409  31.230  1.00 71.81  ? 131 GLU A CG  1 
ATOM   1101 C CD  . GLU A 1 131 ? 19.155 -3.238  32.085  1.00 65.92  ? 131 GLU A CD  1 
ATOM   1102 O OE1 . GLU A 1 131 ? 18.555 -2.139  32.087  1.00 69.52  ? 131 GLU A OE1 1 
ATOM   1103 O OE2 . GLU A 1 131 ? 18.795 -4.207  32.776  1.00 66.55  ? 131 GLU A OE2 1 
ATOM   1104 N N   . HIS A 1 132 ? 20.665 -1.877  27.464  1.00 74.62  ? 132 HIS A N   1 
ATOM   1105 C CA  . HIS A 1 132 ? 21.366 -0.771  26.821  1.00 70.59  ? 132 HIS A CA  1 
ATOM   1106 C C   . HIS A 1 132 ? 20.375 0.209   26.205  1.00 59.45  ? 132 HIS A C   1 
ATOM   1107 O O   . HIS A 1 132 ? 20.565 1.431   26.279  1.00 49.49  ? 132 HIS A O   1 
ATOM   1108 C CB  . HIS A 1 132 ? 22.333 -1.309  25.765  1.00 74.65  ? 132 HIS A CB  1 
ATOM   1109 C CG  . HIS A 1 132 ? 23.584 -0.499  25.624  1.00 76.60  ? 132 HIS A CG  1 
ATOM   1110 N ND1 . HIS A 1 132 ? 24.672 -0.933  24.897  1.00 82.96  ? 132 HIS A ND1 1 
ATOM   1111 C CD2 . HIS A 1 132 ? 23.922 0.715   26.119  1.00 73.63  ? 132 HIS A CD2 1 
ATOM   1112 C CE1 . HIS A 1 132 ? 25.626 -0.020  24.949  1.00 83.68  ? 132 HIS A CE1 1 
ATOM   1113 N NE2 . HIS A 1 132 ? 25.196 0.990   25.684  1.00 84.14  ? 132 HIS A NE2 1 
ATOM   1114 N N   . LEU A 1 133 ? 19.297 -0.312  25.617  1.00 54.55  ? 133 LEU A N   1 
ATOM   1115 C CA  . LEU A 1 133 ? 18.249 0.557   25.098  1.00 40.39  ? 133 LEU A CA  1 
ATOM   1116 C C   . LEU A 1 133 ? 17.607 1.356   26.225  1.00 37.44  ? 133 LEU A C   1 
ATOM   1117 O O   . LEU A 1 133 ? 17.385 2.565   26.088  1.00 33.88  ? 133 LEU A O   1 
ATOM   1118 C CB  . LEU A 1 133 ? 17.186 -0.278  24.386  1.00 48.54  ? 133 LEU A CB  1 
ATOM   1119 C CG  . LEU A 1 133 ? 17.404 -0.708  22.930  1.00 47.67  ? 133 LEU A CG  1 
ATOM   1120 C CD1 . LEU A 1 133 ? 16.062 -0.923  22.232  1.00 49.72  ? 133 LEU A CD1 1 
ATOM   1121 C CD2 . LEU A 1 133 ? 18.311 0.218   22.134  1.00 52.69  ? 133 LEU A CD2 1 
ATOM   1122 N N   . HIS A 1 134 ? 17.309 0.695   27.352  1.00 38.94  ? 134 HIS A N   1 
ATOM   1123 C CA  . HIS A 1 134 ? 16.654 1.362   28.479  1.00 40.26  ? 134 HIS A CA  1 
ATOM   1124 C C   . HIS A 1 134 ? 17.519 2.482   29.033  1.00 31.03  ? 134 HIS A C   1 
ATOM   1125 O O   . HIS A 1 134 ? 17.001 3.509   29.483  1.00 33.78  ? 134 HIS A O   1 
ATOM   1126 C CB  . HIS A 1 134 ? 16.361 0.348   29.591  1.00 41.67  ? 134 HIS A CB  1 
ATOM   1127 C CG  . HIS A 1 134 ? 15.214 0.722   30.478  1.00 54.81  ? 134 HIS A CG  1 
ATOM   1128 N ND1 . HIS A 1 134 ? 15.369 1.474   31.624  1.00 51.90  ? 134 HIS A ND1 1 
ATOM   1129 C CD2 . HIS A 1 134 ? 13.893 0.435   30.393  1.00 59.88  ? 134 HIS A CD2 1 
ATOM   1130 C CE1 . HIS A 1 134 ? 14.191 1.639   32.201  1.00 51.48  ? 134 HIS A CE1 1 
ATOM   1131 N NE2 . HIS A 1 134 ? 13.279 1.019   31.474  1.00 55.89  ? 134 HIS A NE2 1 
ATOM   1132 N N   . GLU A 1 135 ? 18.839 2.291   29.023  1.00 31.91  ? 135 GLU A N   1 
ATOM   1133 C CA  . GLU A 1 135 ? 19.748 3.315   29.521  1.00 32.43  ? 135 GLU A CA  1 
ATOM   1134 C C   . GLU A 1 135 ? 19.584 4.613   28.734  1.00 30.05  ? 135 GLU A C   1 
ATOM   1135 O O   . GLU A 1 135 ? 19.384 5.687   29.316  1.00 26.20  ? 135 GLU A O   1 
ATOM   1136 C CB  . GLU A 1 135 ? 21.180 2.785   29.445  1.00 40.25  ? 135 GLU A CB  1 
ATOM   1137 C CG  . GLU A 1 135 ? 22.265 3.725   29.935  1.00 60.22  ? 135 GLU A CG  1 
ATOM   1138 C CD  . GLU A 1 135 ? 23.656 3.205   29.605  1.00 77.33  ? 135 GLU A CD  1 
ATOM   1139 O OE1 . GLU A 1 135 ? 24.614 4.007   29.608  1.00 77.42  ? 135 GLU A OE1 1 
ATOM   1140 O OE2 . GLU A 1 135 ? 23.788 1.990   29.343  1.00 75.63  ? 135 GLU A OE2 1 
ATOM   1141 N N   . TYR A 1 136 ? 19.630 4.523   27.403  1.00 27.19  ? 136 TYR A N   1 
ATOM   1142 C CA  . TYR A 1 136 ? 19.428 5.712   26.574  1.00 22.70  ? 136 TYR A CA  1 
ATOM   1143 C C   . TYR A 1 136 ? 18.038 6.290   26.780  1.00 23.19  ? 136 TYR A C   1 
ATOM   1144 O O   . TYR A 1 136 ? 17.882 7.511   26.912  1.00 23.10  ? 136 TYR A O   1 
ATOM   1145 C CB  . TYR A 1 136 ? 19.620 5.364   25.098  1.00 25.41  ? 136 TYR A CB  1 
ATOM   1146 C CG  . TYR A 1 136 ? 21.053 5.096   24.704  1.00 27.36  ? 136 TYR A CG  1 
ATOM   1147 C CD1 . TYR A 1 136 ? 22.041 6.057   24.881  1.00 29.39  ? 136 TYR A CD1 1 
ATOM   1148 C CD2 . TYR A 1 136 ? 21.415 3.878   24.143  1.00 31.13  ? 136 TYR A CD2 1 
ATOM   1149 C CE1 . TYR A 1 136 ? 23.350 5.811   24.518  1.00 31.41  ? 136 TYR A CE1 1 
ATOM   1150 C CE2 . TYR A 1 136 ? 22.722 3.626   23.770  1.00 32.52  ? 136 TYR A CE2 1 
ATOM   1151 C CZ  . TYR A 1 136 ? 23.683 4.592   23.962  1.00 30.96  ? 136 TYR A CZ  1 
ATOM   1152 O OH  . TYR A 1 136 ? 24.983 4.332   23.595  1.00 42.54  ? 136 TYR A OH  1 
ATOM   1153 N N   . MET A 1 137 ? 17.015 5.435   26.797  1.00 27.40  ? 137 MET A N   1 
ATOM   1154 C CA  . MET A 1 137 ? 15.653 5.934   26.929  1.00 24.56  ? 137 MET A CA  1 
ATOM   1155 C C   . MET A 1 137 ? 15.463 6.651   28.255  1.00 31.58  ? 137 MET A C   1 
ATOM   1156 O O   . MET A 1 137 ? 14.802 7.695   28.313  1.00 24.41  ? 137 MET A O   1 
ATOM   1157 C CB  . MET A 1 137 ? 14.654 4.789   26.769  1.00 28.80  ? 137 MET A CB  1 
ATOM   1158 C CG  . MET A 1 137 ? 14.514 4.311   25.333  1.00 34.01  ? 137 MET A CG  1 
ATOM   1159 S SD  . MET A 1 137 ? 13.306 2.986   25.155  1.00 40.54  ? 137 MET A SD  1 
ATOM   1160 C CE  . MET A 1 137 ? 13.668 2.457   23.480  1.00 42.72  ? 137 MET A CE  1 
ATOM   1161 N N   . ASN A 1 138 ? 16.060 6.124   29.329  1.00 29.63  ? 138 ASN A N   1 
ATOM   1162 C CA  . ASN A 1 138 ? 15.943 6.798   30.614  1.00 27.61  ? 138 ASN A CA  1 
ATOM   1163 C C   . ASN A 1 138 ? 16.655 8.144   30.602  1.00 25.17  ? 138 ASN A C   1 
ATOM   1164 O O   . ASN A 1 138 ? 16.137 9.123   31.150  1.00 24.52  ? 138 ASN A O   1 
ATOM   1165 C CB  . ASN A 1 138 ? 16.486 5.927   31.747  1.00 31.49  ? 138 ASN A CB  1 
ATOM   1166 C CG  . ASN A 1 138 ? 15.430 5.020   32.342  1.00 52.23  ? 138 ASN A CG  1 
ATOM   1167 O OD1 . ASN A 1 138 ? 14.231 5.235   32.155  1.00 48.85  ? 138 ASN A OD1 1 
ATOM   1168 N ND2 . ASN A 1 138 ? 15.869 4.024   33.103  1.00 59.40  ? 138 ASN A ND2 1 
ATOM   1169 N N   . ALA A 1 139 ? 17.849 8.207   29.999  1.00 21.05  ? 139 ALA A N   1 
ATOM   1170 C CA  . ALA A 1 139 ? 18.579 9.474   29.930  1.00 22.91  ? 139 ALA A CA  1 
ATOM   1171 C C   . ALA A 1 139 ? 17.798 10.511  29.134  1.00 22.20  ? 139 ALA A C   1 
ATOM   1172 O O   . ALA A 1 139 ? 17.706 11.676  29.535  1.00 20.81  ? 139 ALA A O   1 
ATOM   1173 C CB  . ALA A 1 139 ? 19.958 9.260   29.300  1.00 24.34  ? 139 ALA A CB  1 
ATOM   1174 N N   . ILE A 1 140 ? 17.227 10.100  28.004  1.00 20.40  ? 140 ILE A N   1 
ATOM   1175 C CA  . ILE A 1 140 ? 16.438 11.012  27.185  1.00 18.66  ? 140 ILE A CA  1 
ATOM   1176 C C   . ILE A 1 140 ? 15.205 11.471  27.948  1.00 20.63  ? 140 ILE A C   1 
ATOM   1177 O O   . ILE A 1 140 ? 14.896 12.668  28.006  1.00 21.81  ? 140 ILE A O   1 
ATOM   1178 C CB  . ILE A 1 140 ? 16.065 10.314  25.870  1.00 18.33  ? 140 ILE A CB  1 
ATOM   1179 C CG1 . ILE A 1 140 ? 17.332 10.086  25.046  1.00 19.62  ? 140 ILE A CG1 1 
ATOM   1180 C CG2 . ILE A 1 140 ? 15.021 11.152  25.092  1.00 18.05  ? 140 ILE A CG2 1 
ATOM   1181 C CD1 . ILE A 1 140 ? 17.166 9.067   23.909  1.00 22.15  ? 140 ILE A CD1 1 
ATOM   1182 N N   . GLU A 1 141 ? 14.482 10.529  28.554  1.00 24.65  ? 141 GLU A N   1 
ATOM   1183 C CA  . GLU A 1 141 ? 13.288 10.899  29.304  1.00 22.85  ? 141 GLU A CA  1 
ATOM   1184 C C   . GLU A 1 141 ? 13.636 11.857  30.432  1.00 23.83  ? 141 GLU A C   1 
ATOM   1185 O O   . GLU A 1 141 ? 12.918 12.836  30.676  1.00 24.03  ? 141 GLU A O   1 
ATOM   1186 C CB  . GLU A 1 141 ? 12.591 9.633   29.813  1.00 27.79  ? 141 GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 141 ? 11.396 9.858   30.704  1.00 31.59  ? 141 GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 141 ? 11.028 8.598   31.468  1.00 40.93  ? 141 GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 141 ? 11.090 7.508   30.868  1.00 48.26  ? 141 GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 141 ? 10.674 8.688   32.658  1.00 51.50  ? 141 GLU A OE2 1 
ATOM   1191 N N   . MET A 1 142 ? 14.773 11.628  31.079  1.00 24.37  ? 142 MET A N   1 
ATOM   1192 C CA  . MET A 1 142 ? 15.192 12.463  32.194  1.00 28.10  ? 142 MET A CA  1 
ATOM   1193 C C   . MET A 1 142 ? 15.469 13.894  31.732  1.00 27.18  ? 142 MET A C   1 
ATOM   1194 O O   . MET A 1 142 ? 14.990 14.861  32.336  1.00 24.58  ? 142 MET A O   1 
ATOM   1195 C CB  . MET A 1 142 ? 16.437 11.824  32.815  1.00 32.75  ? 142 MET A CB  1 
ATOM   1196 C CG  . MET A 1 142 ? 16.836 12.287  34.198  1.00 56.79  ? 142 MET A CG  1 
ATOM   1197 S SD  . MET A 1 142 ? 15.561 12.392  35.494  1.00 72.48  ? 142 MET A SD  1 
ATOM   1198 C CE  . MET A 1 142 ? 14.400 11.072  35.092  1.00 45.87  ? 142 MET A CE  1 
ATOM   1199 N N   . ALA A 1 143 ? 16.231 14.048  30.646  1.00 22.80  ? 143 ALA A N   1 
ATOM   1200 C CA  . ALA A 1 143 ? 16.503 15.382  30.113  1.00 23.29  ? 143 ALA A CA  1 
ATOM   1201 C C   . ALA A 1 143 ? 15.225 16.079  29.675  1.00 20.71  ? 143 ALA A C   1 
ATOM   1202 O O   . ALA A 1 143 ? 15.083 17.299  29.838  1.00 21.44  ? 143 ALA A O   1 
ATOM   1203 C CB  . ALA A 1 143 ? 17.482 15.292  28.942  1.00 21.01  ? 143 ALA A CB  1 
ATOM   1204 N N   . LEU A 1 144 ? 14.291 15.332  29.089  1.00 21.47  ? 144 LEU A N   1 
ATOM   1205 C CA  . LEU A 1 144 ? 13.049 15.957  28.658  1.00 18.56  ? 144 LEU A CA  1 
ATOM   1206 C C   . LEU A 1 144 ? 12.218 16.420  29.848  1.00 25.05  ? 144 LEU A C   1 
ATOM   1207 O O   . LEU A 1 144 ? 11.594 17.484  29.789  1.00 21.04  ? 144 LEU A O   1 
ATOM   1208 C CB  . LEU A 1 144 ? 12.255 15.004  27.770  1.00 21.97  ? 144 LEU A CB  1 
ATOM   1209 C CG  . LEU A 1 144 ? 12.892 14.733  26.412  1.00 20.81  ? 144 LEU A CG  1 
ATOM   1210 C CD1 . LEU A 1 144 ? 12.134 13.646  25.690  1.00 23.49  ? 144 LEU A CD1 1 
ATOM   1211 C CD2 . LEU A 1 144 ? 12.920 16.004  25.576  1.00 26.27  ? 144 LEU A CD2 1 
ATOM   1212 N N   . LYS A 1 145 ? 12.191 15.642  30.940  1.00 23.65  ? 145 LYS A N   1 
ATOM   1213 C CA  . LYS A 1 145 ? 11.438 16.093  32.109  1.00 26.48  ? 145 LYS A CA  1 
ATOM   1214 C C   . LYS A 1 145 ? 12.103 17.254  32.841  1.00 25.32  ? 145 LYS A C   1 
ATOM   1215 O O   . LYS A 1 145 ? 11.400 18.099  33.409  1.00 29.38  ? 145 LYS A O   1 
ATOM   1216 C CB  . LYS A 1 145 ? 11.113 14.957  33.081  1.00 29.22  ? 145 LYS A CB  1 
ATOM   1217 C CG  . LYS A 1 145 ? 10.477 13.753  32.458  1.00 31.07  ? 145 LYS A CG  1 
ATOM   1218 C CD  . LYS A 1 145 ? 9.804  12.936  33.551  1.00 44.15  ? 145 LYS A CD  1 
ATOM   1219 C CE  . LYS A 1 145 ? 10.107 11.474  33.445  1.00 53.91  ? 145 LYS A CE  1 
ATOM   1220 N NZ  . LYS A 1 145 ? 9.077  10.626  34.115  1.00 55.69  ? 145 LYS A NZ  1 
ATOM   1221 N N   . GLU A 1 146 ? 13.429 17.322  32.844  1.00 21.64  ? 146 GLU A N   1 
ATOM   1222 C CA  . GLU A 1 146 ? 14.132 18.373  33.575  1.00 23.37  ? 146 GLU A CA  1 
ATOM   1223 C C   . GLU A 1 146 ? 14.183 19.718  32.855  1.00 22.28  ? 146 GLU A C   1 
ATOM   1224 O O   . GLU A 1 146 ? 14.520 20.734  33.485  1.00 21.61  ? 146 GLU A O   1 
ATOM   1225 C CB  . GLU A 1 146 ? 15.572 17.967  33.866  1.00 29.58  ? 146 GLU A CB  1 
ATOM   1226 C CG  . GLU A 1 146 ? 15.737 16.884  34.895  1.00 47.45  ? 146 GLU A CG  1 
ATOM   1227 C CD  . GLU A 1 146 ? 17.089 16.225  34.792  1.00 59.17  ? 146 GLU A CD  1 
ATOM   1228 O OE1 . GLU A 1 146 ? 18.061 16.915  34.406  1.00 55.74  ? 146 GLU A OE1 1 
ATOM   1229 O OE2 . GLU A 1 146 ? 17.198 15.046  35.164  1.00 61.96  ? 146 GLU A OE2 1 
ATOM   1230 N N   . ARG A 1 147 ? 13.894 19.757  31.559  1.00 20.49  ? 147 ARG A N   1 
ATOM   1231 C CA  . ARG A 1 147 ? 14.116 20.988  30.812  1.00 16.21  ? 147 ARG A CA  1 
ATOM   1232 C C   . ARG A 1 147 ? 13.204 22.108  31.303  1.00 16.17  ? 147 ARG A C   1 
ATOM   1233 O O   . ARG A 1 147 ? 12.092 21.873  31.769  1.00 18.53  ? 147 ARG A O   1 
ATOM   1234 C CB  . ARG A 1 147 ? 13.909 20.741  29.315  1.00 17.41  ? 147 ARG A CB  1 
ATOM   1235 C CG  . ARG A 1 147 ? 12.458 20.541  28.928  1.00 19.55  ? 147 ARG A CG  1 
ATOM   1236 C CD  . ARG A 1 147 ? 12.386 20.240  27.421  1.00 16.24  ? 147 ARG A CD  1 
ATOM   1237 N NE  . ARG A 1 147 ? 11.045 20.388  26.880  1.00 19.38  ? 147 ARG A NE  1 
ATOM   1238 C CZ  . ARG A 1 147 ? 10.122 19.439  26.855  1.00 18.28  ? 147 ARG A CZ  1 
ATOM   1239 N NH1 . ARG A 1 147 ? 10.346 18.242  27.376  1.00 21.79  ? 147 ARG A NH1 1 
ATOM   1240 N NH2 . ARG A 1 147 ? 8.953  19.690  26.280  1.00 21.78  ? 147 ARG A NH2 1 
ATOM   1241 N N   . LYS A 1 148 ? 13.708 23.336  31.201  1.00 16.05  ? 148 LYS A N   1 
ATOM   1242 C CA  . LYS A 1 148 ? 12.951 24.522  31.587  1.00 16.69  ? 148 LYS A CA  1 
ATOM   1243 C C   . LYS A 1 148 ? 12.604 25.346  30.358  1.00 15.53  ? 148 LYS A C   1 
ATOM   1244 O O   . LYS A 1 148 ? 12.771 26.568  30.345  1.00 14.82  ? 148 LYS A O   1 
ATOM   1245 C CB  . LYS A 1 148 ? 13.708 25.337  32.635  1.00 17.08  ? 148 LYS A CB  1 
ATOM   1246 C CG  . LYS A 1 148 ? 13.903 24.572  33.938  1.00 21.49  ? 148 LYS A CG  1 
ATOM   1247 C CD  . LYS A 1 148 ? 14.544 25.501  34.967  1.00 26.29  ? 148 LYS A CD  1 
ATOM   1248 C CE  . LYS A 1 148 ? 16.043 25.384  34.920  1.00 30.35  ? 148 LYS A CE  1 
ATOM   1249 N NZ  . LYS A 1 148 ? 16.635 25.701  36.253  1.00 26.30  ? 148 LYS A NZ  1 
ATOM   1250 N N   . SER A 1 149 ? 12.126 24.676  29.315  1.00 14.56  ? 149 SER A N   1 
ATOM   1251 C CA  . SER A 1 149 ? 11.757 25.328  28.062  1.00 15.40  ? 149 SER A CA  1 
ATOM   1252 C C   . SER A 1 149 ? 10.831 24.398  27.300  1.00 12.28  ? 149 SER A C   1 
ATOM   1253 O O   . SER A 1 149 ? 10.716 23.209  27.612  1.00 15.78  ? 149 SER A O   1 
ATOM   1254 C CB  . SER A 1 149 ? 12.991 25.682  27.219  1.00 17.05  ? 149 SER A CB  1 
ATOM   1255 O OG  . SER A 1 149 ? 13.751 24.516  26.916  1.00 17.95  ? 149 SER A OG  1 
ATOM   1256 N N   . THR A 1 150 ? 10.185 24.958  26.272  1.00 13.82  ? 150 THR A N   1 
ATOM   1257 C CA  . THR A 1 150 ? 9.211  24.181  25.516  1.00 14.40  ? 150 THR A CA  1 
ATOM   1258 C C   . THR A 1 150 ? 9.902  23.129  24.661  1.00 11.83  ? 150 THR A C   1 
ATOM   1259 O O   . THR A 1 150 ? 9.412  21.993  24.538  1.00 15.55  ? 150 THR A O   1 
ATOM   1260 C CB  . THR A 1 150 ? 8.362  25.110  24.673  1.00 16.37  ? 150 THR A CB  1 
ATOM   1261 O OG1 . THR A 1 150 ? 7.592  25.902  25.585  1.00 17.42  ? 150 THR A OG1 1 
ATOM   1262 C CG2 . THR A 1 150 ? 7.409  24.330  23.767  1.00 18.76  ? 150 THR A CG2 1 
ATOM   1263 N N   . PHE A 1 151 ? 11.043 23.479  24.079  1.00 12.98  ? 151 PHE A N   1 
ATOM   1264 C CA  . PHE A 1 151 ? 11.820 22.567  23.249  1.00 13.38  ? 151 PHE A CA  1 
ATOM   1265 C C   . PHE A 1 151 ? 13.112 22.201  23.959  1.00 13.28  ? 151 PHE A C   1 
ATOM   1266 O O   . PHE A 1 151 ? 13.403 22.651  25.069  1.00 14.66  ? 151 PHE A O   1 
ATOM   1267 C CB  . PHE A 1 151 ? 11.976 23.167  21.852  1.00 12.13  ? 151 PHE A CB  1 
ATOM   1268 C CG  . PHE A 1 151 ? 10.657 23.266  21.142  1.00 11.49  ? 151 PHE A CG  1 
ATOM   1269 C CD1 . PHE A 1 151 ? 10.028 22.118  20.672  1.00 12.37  ? 151 PHE A CD1 1 
ATOM   1270 C CD2 . PHE A 1 151 ? 10.025 24.497  21.012  1.00 13.91  ? 151 PHE A CD2 1 
ATOM   1271 C CE1 . PHE A 1 151 ? 8.759  22.194  20.050  1.00 12.49  ? 151 PHE A CE1 1 
ATOM   1272 C CE2 . PHE A 1 151 ? 8.784  24.602  20.386  1.00 14.17  ? 151 PHE A CE2 1 
ATOM   1273 C CZ  . PHE A 1 151 ? 8.146  23.453  19.912  1.00 13.64  ? 151 PHE A CZ  1 
ATOM   1274 N N   . ILE A 1 152 ? 13.878 21.316  23.332  1.00 14.16  ? 152 ILE A N   1 
ATOM   1275 C CA  . ILE A 1 152 ? 15.007 20.698  24.024  1.00 14.70  ? 152 ILE A CA  1 
ATOM   1276 C C   . ILE A 1 152 ? 16.026 21.743  24.463  1.00 15.17  ? 152 ILE A C   1 
ATOM   1277 O O   . ILE A 1 152 ? 16.603 21.640  25.559  1.00 15.87  ? 152 ILE A O   1 
ATOM   1278 C CB  . ILE A 1 152 ? 15.625 19.620  23.121  1.00 13.91  ? 152 ILE A CB  1 
ATOM   1279 C CG1 . ILE A 1 152 ? 14.709 18.405  23.153  1.00 14.76  ? 152 ILE A CG1 1 
ATOM   1280 C CG2 . ILE A 1 152 ? 17.028 19.256  23.583  1.00 19.22  ? 152 ILE A CG2 1 
ATOM   1281 C CD1 . ILE A 1 152 ? 14.858 17.486  21.968  1.00 16.62  ? 152 ILE A CD1 1 
ATOM   1282 N N   . ALA A 1 153 ? 16.297 22.742  23.626  1.00 14.01  ? 153 ALA A N   1 
ATOM   1283 C CA  . ALA A 1 153 ? 17.400 23.656  23.885  1.00 17.19  ? 153 ALA A CA  1 
ATOM   1284 C C   . ALA A 1 153 ? 16.932 25.067  24.169  1.00 19.89  ? 153 ALA A C   1 
ATOM   1285 O O   . ALA A 1 153 ? 17.758 25.979  24.307  1.00 20.24  ? 153 ALA A O   1 
ATOM   1286 C CB  . ALA A 1 153 ? 18.440 23.606  22.766  1.00 16.47  ? 153 ALA A CB  1 
ATOM   1287 N N   . GLY A 1 154 ? 15.630 25.272  24.299  1.00 15.01  ? 154 GLY A N   1 
ATOM   1288 C CA  . GLY A 1 154 ? 15.127 26.600  24.489  1.00 15.89  ? 154 GLY A CA  1 
ATOM   1289 C C   . GLY A 1 154 ? 13.696 26.705  24.025  1.00 16.09  ? 154 GLY A C   1 
ATOM   1290 O O   . GLY A 1 154 ? 12.995 25.701  23.839  1.00 14.51  ? 154 GLY A O   1 
ATOM   1291 N N   . PRO A 1 155 ? 13.223 27.944  23.849  1.00 15.35  ? 155 PRO A N   1 
ATOM   1292 C CA  . PRO A 1 155 ? 11.815 28.157  23.499  1.00 15.26  ? 155 PRO A CA  1 
ATOM   1293 C C   . PRO A 1 155 ? 11.469 27.844  22.057  1.00 16.34  ? 155 PRO A C   1 
ATOM   1294 O O   . PRO A 1 155 ? 10.273 27.835  21.723  1.00 17.54  ? 155 PRO A O   1 
ATOM   1295 C CB  . PRO A 1 155 ? 11.607 29.651  23.805  1.00 19.79  ? 155 PRO A CB  1 
ATOM   1296 C CG  . PRO A 1 155 ? 12.958 30.242  23.601  1.00 26.29  ? 155 PRO A CG  1 
ATOM   1297 C CD  . PRO A 1 155 ? 13.937 29.207  24.088  1.00 20.41  ? 155 PRO A CD  1 
ATOM   1298 N N   . ARG A 1 156 ? 12.463 27.585  21.202  1.00 14.97  ? 156 ARG A N   1 
ATOM   1299 C CA  . ARG A 1 156 ? 12.215 27.380  19.784  1.00 17.58  ? 156 ARG A CA  1 
ATOM   1300 C C   . ARG A 1 156 ? 12.870 26.077  19.327  1.00 14.23  ? 156 ARG A C   1 
ATOM   1301 O O   . ARG A 1 156 ? 13.864 25.625  19.896  1.00 14.73  ? 156 ARG A O   1 
ATOM   1302 C CB  . ARG A 1 156 ? 12.765 28.562  18.981  1.00 20.78  ? 156 ARG A CB  1 
ATOM   1303 C CG  . ARG A 1 156 ? 11.795 29.748  18.950  1.00 23.38  ? 156 ARG A CG  1 
ATOM   1304 C CD  . ARG A 1 156 ? 12.498 31.044  18.573  1.00 30.33  ? 156 ARG A CD  1 
ATOM   1305 N NE  . ARG A 1 156 ? 13.539 31.409  19.526  1.00 49.00  ? 156 ARG A NE  1 
ATOM   1306 C CZ  . ARG A 1 156 ? 13.349 32.157  20.608  1.00 51.53  ? 156 ARG A CZ  1 
ATOM   1307 N NH1 . ARG A 1 156 ? 12.149 32.611  20.939  1.00 33.64  ? 156 ARG A NH1 1 
ATOM   1308 N NH2 . ARG A 1 156 ? 14.392 32.452  21.380  1.00 51.39  ? 156 ARG A NH2 1 
ATOM   1309 N N   . VAL A 1 157 ? 12.308 25.515  18.250  1.00 14.01  ? 157 VAL A N   1 
ATOM   1310 C CA  . VAL A 1 157 ? 12.767 24.241  17.693  1.00 12.96  ? 157 VAL A CA  1 
ATOM   1311 C C   . VAL A 1 157 ? 14.181 24.372  17.176  1.00 12.89  ? 157 VAL A C   1 
ATOM   1312 O O   . VAL A 1 157 ? 14.548 25.374  16.539  1.00 14.67  ? 157 VAL A O   1 
ATOM   1313 C CB  . VAL A 1 157 ? 11.826 23.867  16.537  1.00 13.40  ? 157 VAL A CB  1 
ATOM   1314 C CG1 . VAL A 1 157 ? 12.445 22.792  15.615  1.00 15.13  ? 157 VAL A CG1 1 
ATOM   1315 C CG2 . VAL A 1 157 ? 10.503 23.402  17.111  1.00 16.35  ? 157 VAL A CG2 1 
ATOM   1316 N N   . THR A 1 158 ? 14.984 23.356  17.462  1.00 12.34  ? 158 THR A N   1 
ATOM   1317 C CA  . THR A 1 158 ? 16.321 23.224  16.906  1.00 13.02  ? 158 THR A CA  1 
ATOM   1318 C C   . THR A 1 158 ? 16.474 21.826  16.315  1.00 11.87  ? 158 THR A C   1 
ATOM   1319 O O   . THR A 1 158 ? 15.561 20.988  16.352  1.00 13.66  ? 158 THR A O   1 
ATOM   1320 C CB  . THR A 1 158 ? 17.408 23.434  17.957  1.00 12.06  ? 158 THR A CB  1 
ATOM   1321 O OG1 . THR A 1 158 ? 17.307 22.379  18.933  1.00 13.53  ? 158 THR A OG1 1 
ATOM   1322 C CG2 . THR A 1 158 ? 17.300 24.833  18.576  1.00 13.63  ? 158 THR A CG2 1 
ATOM   1323 N N   . LEU A 1 159 ? 17.670 21.573  15.774  1.00 12.12  ? 159 LEU A N   1 
ATOM   1324 C CA  . LEU A 1 159 ? 17.992 20.250  15.232  1.00 11.54  ? 159 LEU A CA  1 
ATOM   1325 C C   . LEU A 1 159 ? 17.676 19.105  16.190  1.00 12.22  ? 159 LEU A C   1 
ATOM   1326 O O   . LEU A 1 159 ? 17.281 18.022  15.740  1.00 13.15  ? 159 LEU A O   1 
ATOM   1327 C CB  . LEU A 1 159 ? 19.468 20.209  14.814  1.00 12.52  ? 159 LEU A CB  1 
ATOM   1328 C CG  . LEU A 1 159 ? 19.842 18.979  13.989  1.00 11.70  ? 159 LEU A CG  1 
ATOM   1329 C CD1 . LEU A 1 159 ? 19.196 19.036  12.619  1.00 13.76  ? 159 LEU A CD1 1 
ATOM   1330 C CD2 . LEU A 1 159 ? 21.377 18.851  13.894  1.00 14.75  ? 159 LEU A CD2 1 
ATOM   1331 N N   . ALA A 1 160 ? 17.835 19.306  17.499  1.00 12.18  ? 160 ALA A N   1 
ATOM   1332 C CA  . ALA A 1 160 ? 17.574 18.202  18.421  1.00 11.53  ? 160 ALA A CA  1 
ATOM   1333 C C   . ALA A 1 160 ? 16.104 17.811  18.435  1.00 11.83  ? 160 ALA A C   1 
ATOM   1334 O O   . ALA A 1 160 ? 15.785 16.617  18.533  1.00 12.31  ? 160 ALA A O   1 
ATOM   1335 C CB  . ALA A 1 160 ? 18.058 18.560  19.822  1.00 14.27  ? 160 ALA A CB  1 
ATOM   1336 N N   . ASP A 1 161 ? 15.186 18.789  18.343  1.00 12.27  ? 161 ASP A N   1 
ATOM   1337 C CA  . ASP A 1 161 ? 13.768 18.446  18.278  1.00 12.71  ? 161 ASP A CA  1 
ATOM   1338 C C   . ASP A 1 161 ? 13.430 17.730  16.978  1.00 14.90  ? 161 ASP A C   1 
ATOM   1339 O O   . ASP A 1 161 ? 12.556 16.862  16.961  1.00 14.33  ? 161 ASP A O   1 
ATOM   1340 C CB  . ASP A 1 161 ? 12.918 19.709  18.465  1.00 11.63  ? 161 ASP A CB  1 
ATOM   1341 C CG  . ASP A 1 161 ? 13.366 20.514  19.656  1.00 12.99  ? 161 ASP A CG  1 
ATOM   1342 O OD1 . ASP A 1 161 ? 13.013 20.149  20.794  1.00 13.89  ? 161 ASP A OD1 1 
ATOM   1343 O OD2 . ASP A 1 161 ? 14.079 21.519  19.433  1.00 14.29  ? 161 ASP A OD2 1 
ATOM   1344 N N   . LEU A 1 162 ? 14.114 18.075  15.882  1.00 13.44  ? 162 LEU A N   1 
ATOM   1345 C CA  . LEU A 1 162 ? 13.889 17.376  14.624  1.00 13.18  ? 162 LEU A CA  1 
ATOM   1346 C C   . LEU A 1 162 ? 14.377 15.934  14.701  1.00 15.08  ? 162 LEU A C   1 
ATOM   1347 O O   . LEU A 1 162 ? 13.737 15.025  14.149  1.00 15.36  ? 162 LEU A O   1 
ATOM   1348 C CB  . LEU A 1 162 ? 14.560 18.146  13.476  1.00 12.27  ? 162 LEU A CB  1 
ATOM   1349 C CG  . LEU A 1 162 ? 14.049 19.571  13.306  1.00 11.49  ? 162 LEU A CG  1 
ATOM   1350 C CD1 . LEU A 1 162 ? 14.778 20.231  12.127  1.00 14.20  ? 162 LEU A CD1 1 
ATOM   1351 C CD2 . LEU A 1 162 ? 12.548 19.596  13.042  1.00 16.04  ? 162 LEU A CD2 1 
ATOM   1352 N N   A GLN A 1 163 ? 15.516 15.691  15.346  0.60 13.24  ? 163 GLN A N   1 
ATOM   1353 N N   B GLN A 1 163 ? 15.511 15.708  15.373  0.40 13.25  ? 163 GLN A N   1 
ATOM   1354 C CA  A GLN A 1 163 ? 15.975 14.310  15.419  0.60 14.38  ? 163 GLN A CA  1 
ATOM   1355 C CA  B GLN A 1 163 ? 16.051 14.359  15.516  0.40 14.53  ? 163 GLN A CA  1 
ATOM   1356 C C   A GLN A 1 163 ? 15.077 13.485  16.334  0.60 15.79  ? 163 GLN A C   1 
ATOM   1357 C C   B GLN A 1 163 ? 15.156 13.498  16.395  0.40 15.68  ? 163 GLN A C   1 
ATOM   1358 O O   A GLN A 1 163 ? 14.947 12.270  16.136  0.60 15.40  ? 163 GLN A O   1 
ATOM   1359 O O   B GLN A 1 163 ? 15.128 12.271  16.241  0.40 15.92  ? 163 GLN A O   1 
ATOM   1360 C CB  A GLN A 1 163 ? 17.461 14.226  15.794  0.60 15.29  ? 163 GLN A CB  1 
ATOM   1361 C CB  B GLN A 1 163 ? 17.479 14.430  16.068  0.40 14.51  ? 163 GLN A CB  1 
ATOM   1362 C CG  A GLN A 1 163 ? 17.947 12.782  15.899  0.60 17.44  ? 163 GLN A CG  1 
ATOM   1363 C CG  B GLN A 1 163 ? 18.120 13.078  16.309  0.40 18.96  ? 163 GLN A CG  1 
ATOM   1364 C CD  A GLN A 1 163 ? 19.433 12.577  15.662  0.60 19.75  ? 163 GLN A CD  1 
ATOM   1365 C CD  B GLN A 1 163 ? 18.776 12.512  15.072  0.40 18.40  ? 163 GLN A CD  1 
ATOM   1366 O OE1 A GLN A 1 163 ? 19.910 12.560  14.518  0.60 19.60  ? 163 GLN A OE1 1 
ATOM   1367 O OE1 B GLN A 1 163 ? 18.179 12.482  13.996  0.40 20.84  ? 163 GLN A OE1 1 
ATOM   1368 N NE2 A GLN A 1 163 ? 20.173 12.410  16.748  0.60 17.87  ? 163 GLN A NE2 1 
ATOM   1369 N NE2 B GLN A 1 163 ? 20.004 12.015  15.227  0.40 19.40  ? 163 GLN A NE2 1 
ATOM   1370 N N   . VAL A 1 164 ? 14.398 14.123  17.297  1.00 15.20  ? 164 VAL A N   1 
ATOM   1371 C CA  . VAL A 1 164 ? 13.407 13.391  18.085  1.00 17.47  ? 164 VAL A CA  1 
ATOM   1372 C C   . VAL A 1 164 ? 12.346 12.777  17.174  1.00 18.23  ? 164 VAL A C   1 
ATOM   1373 O O   . VAL A 1 164 ? 11.875 11.654  17.407  1.00 19.23  ? 164 VAL A O   1 
ATOM   1374 C CB  . VAL A 1 164 ? 12.793 14.334  19.139  1.00 17.15  ? 164 VAL A CB  1 
ATOM   1375 C CG1 . VAL A 1 164 ? 11.434 13.804  19.607  1.00 19.68  ? 164 VAL A CG1 1 
ATOM   1376 C CG2 . VAL A 1 164 ? 13.729 14.506  20.312  1.00 22.25  ? 164 VAL A CG2 1 
ATOM   1377 N N   . ILE A 1 165 ? 11.965 13.490  16.106  1.00 15.83  ? 165 ILE A N   1 
ATOM   1378 C CA  . ILE A 1 165 ? 10.996 12.940  15.157  1.00 17.02  ? 165 ILE A CA  1 
ATOM   1379 C C   . ILE A 1 165 ? 11.547 11.686  14.491  1.00 18.46  ? 165 ILE A C   1 
ATOM   1380 O O   . ILE A 1 165 ? 10.848 10.677  14.344  1.00 19.46  ? 165 ILE A O   1 
ATOM   1381 C CB  . ILE A 1 165 ? 10.590 14.002  14.115  1.00 16.81  ? 165 ILE A CB  1 
ATOM   1382 C CG1 . ILE A 1 165 ? 9.864  15.163  14.816  1.00 19.88  ? 165 ILE A CG1 1 
ATOM   1383 C CG2 . ILE A 1 165 ? 9.722  13.357  13.031  1.00 19.37  ? 165 ILE A CG2 1 
ATOM   1384 C CD1 . ILE A 1 165 ? 9.454  16.334  13.912  1.00 19.22  ? 165 ILE A CD1 1 
ATOM   1385 N N   . VAL A 1 166 ? 12.808 11.735  14.064  1.00 16.31  ? 166 VAL A N   1 
ATOM   1386 C CA  . VAL A 1 166 ? 13.443 10.557  13.485  1.00 15.53  ? 166 VAL A CA  1 
ATOM   1387 C C   . VAL A 1 166 ? 13.399 9.395   14.471  1.00 18.38  ? 166 VAL A C   1 
ATOM   1388 O O   . VAL A 1 166 ? 13.130 8.246   14.091  1.00 20.02  ? 166 VAL A O   1 
ATOM   1389 C CB  . VAL A 1 166 ? 14.888 10.890  13.084  1.00 17.50  ? 166 VAL A CB  1 
ATOM   1390 C CG1 . VAL A 1 166 ? 15.572 9.651   12.510  1.00 17.89  ? 166 VAL A CG1 1 
ATOM   1391 C CG2 . VAL A 1 166 ? 14.927 12.096  12.116  1.00 16.53  ? 166 VAL A CG2 1 
ATOM   1392 N N   . LEU A 1 167 ? 13.700 9.676   15.743  1.00 15.83  ? 167 LEU A N   1 
ATOM   1393 C CA  . LEU A 1 167 ? 13.717 8.629   16.761  1.00 17.39  ? 167 LEU A CA  1 
ATOM   1394 C C   . LEU A 1 167 ? 12.329 8.028   16.969  1.00 23.25  ? 167 LEU A C   1 
ATOM   1395 O O   . LEU A 1 167 ? 12.190 6.803   17.043  1.00 20.76  ? 167 LEU A O   1 
ATOM   1396 C CB  . LEU A 1 167 ? 14.275 9.189   18.071  1.00 15.59  ? 167 LEU A CB  1 
ATOM   1397 C CG  . LEU A 1 167 ? 14.251 8.220   19.263  1.00 17.36  ? 167 LEU A CG  1 
ATOM   1398 C CD1 . LEU A 1 167 ? 15.019 6.937   18.925  1.00 18.09  ? 167 LEU A CD1 1 
ATOM   1399 C CD2 . LEU A 1 167 ? 14.829 8.898   20.507  1.00 18.74  ? 167 LEU A CD2 1 
ATOM   1400 N N   . ILE A 1 168 ? 11.288 8.867   17.051  1.00 19.11  ? 168 ILE A N   1 
ATOM   1401 C CA  . ILE A 1 168 ? 9.919  8.356   17.227  1.00 23.01  ? 168 ILE A CA  1 
ATOM   1402 C C   . ILE A 1 168 ? 9.546  7.398   16.103  1.00 30.45  ? 168 ILE A C   1 
ATOM   1403 O O   . ILE A 1 168 ? 9.034  6.290   16.339  1.00 26.66  ? 168 ILE A O   1 
ATOM   1404 C CB  . ILE A 1 168 ? 8.918  9.519   17.286  1.00 26.21  ? 168 ILE A CB  1 
ATOM   1405 C CG1 . ILE A 1 168 ? 9.004  10.217  18.624  1.00 23.42  ? 168 ILE A CG1 1 
ATOM   1406 C CG2 . ILE A 1 168 ? 7.486  9.014   17.009  1.00 26.77  ? 168 ILE A CG2 1 
ATOM   1407 C CD1 . ILE A 1 168 ? 8.392  11.595  18.577  1.00 26.50  ? 168 ILE A CD1 1 
ATOM   1408 N N   A ASP A 1 169 ? 9.764  7.824   14.855  0.01 24.75  ? 169 ASP A N   1 
ATOM   1409 N N   B ASP A 1 169 ? 9.780  7.814   14.860  0.99 24.35  ? 169 ASP A N   1 
ATOM   1410 C CA  A ASP A 1 169 ? 9.391  6.997   13.711  0.01 28.71  ? 169 ASP A CA  1 
ATOM   1411 C CA  B ASP A 1 169 ? 9.389  6.987   13.726  0.99 28.63  ? 169 ASP A CA  1 
ATOM   1412 C C   A ASP A 1 169 ? 10.173 5.693   13.685  0.01 30.63  ? 169 ASP A C   1 
ATOM   1413 C C   B ASP A 1 169 ? 10.167 5.683   13.705  0.99 30.76  ? 169 ASP A C   1 
ATOM   1414 O O   A ASP A 1 169 ? 9.655  4.666   13.231  0.01 31.83  ? 169 ASP A O   1 
ATOM   1415 O O   B ASP A 1 169 ? 9.638  4.642   13.293  0.99 31.93  ? 169 ASP A O   1 
ATOM   1416 C CB  A ASP A 1 169 ? 9.601  7.775   12.411  0.01 30.97  ? 169 ASP A CB  1 
ATOM   1417 C CB  B ASP A 1 169 ? 9.586  7.767   12.427  0.99 31.09  ? 169 ASP A CB  1 
ATOM   1418 C CG  A ASP A 1 169 ? 8.857  9.096   12.394  0.01 35.89  ? 169 ASP A CG  1 
ATOM   1419 C CG  B ASP A 1 169 ? 8.748  9.030   12.377  0.99 36.41  ? 169 ASP A CG  1 
ATOM   1420 O OD1 A ASP A 1 169 ? 8.274  9.466   13.436  0.01 38.36  ? 169 ASP A OD1 1 
ATOM   1421 O OD1 B ASP A 1 169 ? 7.974  9.283   13.330  0.99 46.34  ? 169 ASP A OD1 1 
ATOM   1422 O OD2 A ASP A 1 169 ? 8.856  9.767   11.341  0.01 38.04  ? 169 ASP A OD2 1 
ATOM   1423 O OD2 B ASP A 1 169 ? 8.874  9.784   11.397  0.99 38.68  ? 169 ASP A OD2 1 
ATOM   1424 N N   . THR A 1 170 ? 11.415 5.712   14.168  1.00 23.26  ? 170 THR A N   1 
ATOM   1425 C CA  . THR A 1 170 ? 12.197 4.491   14.243  1.00 22.05  ? 170 THR A CA  1 
ATOM   1426 C C   . THR A 1 170 ? 11.681 3.568   15.343  1.00 29.68  ? 170 THR A C   1 
ATOM   1427 O O   . THR A 1 170 ? 11.528 2.360   15.118  1.00 29.38  ? 170 THR A O   1 
ATOM   1428 C CB  . THR A 1 170 ? 13.671 4.836   14.438  1.00 24.11  ? 170 THR A CB  1 
ATOM   1429 O OG1 . THR A 1 170 ? 14.138 5.588   13.309  1.00 26.69  ? 170 THR A OG1 1 
ATOM   1430 C CG2 . THR A 1 170 ? 14.508 3.585   14.592  1.00 29.07  ? 170 THR A CG2 1 
ATOM   1431 N N   . MET A 1 171 ? 11.391 4.108   16.535  1.00 24.65  ? 171 MET A N   1 
ATOM   1432 C CA  . MET A 1 171 ? 10.795 3.258   17.570  1.00 25.56  ? 171 MET A CA  1 
ATOM   1433 C C   . MET A 1 171 ? 9.442  2.690   17.145  1.00 33.30  ? 171 MET A C   1 
ATOM   1434 O O   . MET A 1 171 ? 9.122  1.546   17.474  1.00 36.41  ? 171 MET A O   1 
ATOM   1435 C CB  . MET A 1 171 ? 10.769 3.882   18.978  1.00 29.14  ? 171 MET A CB  1 
ATOM   1436 C CG  . MET A 1 171 ? 12.033 4.607   19.457  1.00 22.80  ? 171 MET A CG  1 
ATOM   1437 S SD  . MET A 1 171 ? 11.776 5.699   20.886  1.00 28.66  ? 171 MET A SD  1 
ATOM   1438 C CE  . MET A 1 171 ? 11.081 4.556   22.087  1.00 39.62  ? 171 MET A CE  1 
ATOM   1439 N N   . ASN A 1 172 ? 8.638  3.456   16.405  1.00 32.58  ? 172 ASN A N   1 
ATOM   1440 C CA  . ASN A 1 172 ? 7.353  2.914   15.948  1.00 34.34  ? 172 ASN A CA  1 
ATOM   1441 C C   . ASN A 1 172 ? 7.538  1.726   15.006  1.00 42.61  ? 172 ASN A C   1 
ATOM   1442 O O   . ASN A 1 172 ? 6.750  0.771   15.039  1.00 41.01  ? 172 ASN A O   1 
ATOM   1443 C CB  . ASN A 1 172 ? 6.507  4.011   15.301  1.00 29.06  ? 172 ASN A CB  1 
ATOM   1444 C CG  . ASN A 1 172 ? 5.947  4.983   16.315  1.00 33.21  ? 172 ASN A CG  1 
ATOM   1445 O OD1 . ASN A 1 172 ? 6.028  4.756   17.523  1.00 45.43  ? 172 ASN A OD1 1 
ATOM   1446 N ND2 . ASN A 1 172 ? 5.410  6.100   15.829  1.00 46.57  ? 172 ASN A ND2 1 
ATOM   1447 N N   . LYS A 1 173 ? 8.572  1.753   14.169  1.00 37.64  ? 173 LYS A N   1 
ATOM   1448 C CA  . LYS A 1 173 ? 8.770  0.654   13.228  1.00 36.63  ? 173 LYS A CA  1 
ATOM   1449 C C   . LYS A 1 173 ? 9.496  -0.521  13.874  1.00 35.70  ? 173 LYS A C   1 
ATOM   1450 O O   . LYS A 1 173 ? 9.090  -1.676  13.709  1.00 46.67  ? 173 LYS A O   1 
ATOM   1451 C CB  . LYS A 1 173 ? 9.515  1.136   11.984  1.00 39.33  ? 173 LYS A CB  1 
ATOM   1452 C CG  . LYS A 1 173 ? 8.749  2.170   11.165  1.00 56.03  ? 173 LYS A CG  1 
ATOM   1453 C CD  . LYS A 1 173 ? 7.843  1.516   10.123  1.00 58.26  ? 173 LYS A CD  1 
ATOM   1454 C CE  . LYS A 1 173 ? 6.825  2.508   9.577   1.00 54.21  ? 173 LYS A CE  1 
ATOM   1455 N NZ  . LYS A 1 173 ? 6.415  2.177   8.184   1.00 60.20  ? 173 LYS A NZ  1 
ATOM   1456 N N   . PHE A 1 174 ? 10.566 -0.247  14.621  1.00 34.54  ? 174 PHE A N   1 
ATOM   1457 C CA  . PHE A 1 174 ? 11.390 -1.305  15.195  1.00 33.51  ? 174 PHE A CA  1 
ATOM   1458 C C   . PHE A 1 174 ? 10.902 -1.790  16.559  1.00 43.54  ? 174 PHE A C   1 
ATOM   1459 O O   . PHE A 1 174 ? 11.190 -2.934  16.933  1.00 41.52  ? 174 PHE A O   1 
ATOM   1460 C CB  . PHE A 1 174 ? 12.831 -0.818  15.356  1.00 39.17  ? 174 PHE A CB  1 
ATOM   1461 C CG  . PHE A 1 174 ? 13.619 -0.754  14.072  1.00 43.32  ? 174 PHE A CG  1 
ATOM   1462 C CD1 . PHE A 1 174 ? 13.498 0.332   13.216  1.00 41.51  ? 174 PHE A CD1 1 
ATOM   1463 C CD2 . PHE A 1 174 ? 14.528 -1.751  13.754  1.00 45.86  ? 174 PHE A CD2 1 
ATOM   1464 C CE1 . PHE A 1 174 ? 14.243 0.402   12.045  1.00 39.81  ? 174 PHE A CE1 1 
ATOM   1465 C CE2 . PHE A 1 174 ? 15.278 -1.686  12.590  1.00 49.86  ? 174 PHE A CE2 1 
ATOM   1466 C CZ  . PHE A 1 174 ? 15.135 -0.608  11.734  1.00 46.95  ? 174 PHE A CZ  1 
ATOM   1467 N N   . LEU A 1 175 ? 10.197 -0.956  17.326  1.00 39.91  ? 175 LEU A N   1 
ATOM   1468 C CA  . LEU A 1 175 ? 9.770  -1.307  18.685  1.00 42.11  ? 175 LEU A CA  1 
ATOM   1469 C C   . LEU A 1 175 ? 8.321  -0.880  18.907  1.00 47.14  ? 175 LEU A C   1 
ATOM   1470 O O   . LEU A 1 175 ? 8.023  -0.089  19.808  1.00 48.22  ? 175 LEU A O   1 
ATOM   1471 C CB  . LEU A 1 175 ? 10.689 -0.650  19.716  1.00 45.20  ? 175 LEU A CB  1 
ATOM   1472 C CG  . LEU A 1 175 ? 12.199 -0.853  19.582  1.00 47.94  ? 175 LEU A CG  1 
ATOM   1473 C CD1 . LEU A 1 175 ? 12.951 0.117   20.482  1.00 42.01  ? 175 LEU A CD1 1 
ATOM   1474 C CD2 . LEU A 1 175 ? 12.567 -2.285  19.925  1.00 50.24  ? 175 LEU A CD2 1 
ATOM   1475 N N   . PRO A 1 176 ? 7.384  -1.409  18.111  1.00 46.22  ? 176 PRO A N   1 
ATOM   1476 C CA  . PRO A 1 176 ? 6.008  -0.877  18.162  1.00 57.50  ? 176 PRO A CA  1 
ATOM   1477 C C   . PRO A 1 176 ? 5.338  -1.017  19.518  1.00 58.79  ? 176 PRO A C   1 
ATOM   1478 O O   . PRO A 1 176 ? 4.632  -0.100  19.955  1.00 59.51  ? 176 PRO A O   1 
ATOM   1479 C CB  . PRO A 1 176 ? 5.275  -1.693  17.086  1.00 50.62  ? 176 PRO A CB  1 
ATOM   1480 C CG  . PRO A 1 176 ? 6.107  -2.921  16.913  1.00 59.69  ? 176 PRO A CG  1 
ATOM   1481 C CD  . PRO A 1 176 ? 7.518  -2.477  17.107  1.00 51.15  ? 176 PRO A CD  1 
ATOM   1482 N N   . ASN A 1 177 ? 5.541  -2.142  20.199  1.00 62.76  ? 177 ASN A N   1 
ATOM   1483 C CA  . ASN A 1 177 ? 4.836  -2.425  21.441  1.00 69.75  ? 177 ASN A CA  1 
ATOM   1484 C C   . ASN A 1 177 ? 5.608  -2.015  22.687  1.00 69.04  ? 177 ASN A C   1 
ATOM   1485 O O   . ASN A 1 177 ? 5.040  -2.061  23.784  1.00 75.60  ? 177 ASN A O   1 
ATOM   1486 C CB  . ASN A 1 177 ? 4.466  -3.911  21.514  1.00 73.28  ? 177 ASN A CB  1 
ATOM   1487 C CG  . ASN A 1 177 ? 4.263  -4.525  20.141  1.00 74.26  ? 177 ASN A CG  1 
ATOM   1488 O OD1 . ASN A 1 177 ? 5.120  -5.253  19.638  1.00 76.54  ? 177 ASN A OD1 1 
ATOM   1489 N ND2 . ASN A 1 177 ? 3.125  -4.226  19.525  1.00 72.30  ? 177 ASN A ND2 1 
ATOM   1490 N N   . THR A 1 178 ? 6.877  -1.629  22.550  1.00 68.09  ? 178 THR A N   1 
ATOM   1491 C CA  . THR A 1 178 ? 7.642  -1.131  23.687  1.00 66.95  ? 178 THR A CA  1 
ATOM   1492 C C   . THR A 1 178 ? 6.884  0.007   24.357  1.00 67.77  ? 178 THR A C   1 
ATOM   1493 O O   . THR A 1 178 ? 6.424  0.940   23.694  1.00 69.63  ? 178 THR A O   1 
ATOM   1494 C CB  . THR A 1 178 ? 9.014  -0.643  23.207  1.00 68.63  ? 178 THR A CB  1 
ATOM   1495 O OG1 . THR A 1 178 ? 9.900  -1.761  23.065  1.00 71.12  ? 178 THR A OG1 1 
ATOM   1496 C CG2 . THR A 1 178 ? 9.619  0.347   24.200  1.00 62.82  ? 178 THR A CG2 1 
ATOM   1497 N N   . LYS A 1 179 ? 6.730  -0.087  25.675  1.00 64.41  ? 179 LYS A N   1 
ATOM   1498 C CA  . LYS A 1 179 ? 5.929  0.863   26.444  1.00 69.51  ? 179 LYS A CA  1 
ATOM   1499 C C   . LYS A 1 179 ? 6.818  1.509   27.503  1.00 67.69  ? 179 LYS A C   1 
ATOM   1500 O O   . LYS A 1 179 ? 6.808  1.122   28.674  1.00 80.40  ? 179 LYS A O   1 
ATOM   1501 C CB  . LYS A 1 179 ? 4.692  0.171   27.049  1.00 73.33  ? 179 LYS A CB  1 
ATOM   1502 C CG  . LYS A 1 179 ? 3.710  1.120   27.718  1.00 77.98  ? 179 LYS A CG  1 
ATOM   1503 C CD  . LYS A 1 179 ? 2.300  0.546   27.720  1.00 81.25  ? 179 LYS A CD  1 
ATOM   1504 C CE  . LYS A 1 179 ? 2.283  -0.916  28.136  1.00 76.25  ? 179 LYS A CE  1 
ATOM   1505 N NZ  . LYS A 1 179 ? 2.172  -1.071  29.611  1.00 80.78  ? 179 LYS A NZ  1 
ATOM   1506 N N   . HIS A 1 180 ? 7.592  2.502   27.076  1.00 59.06  ? 180 HIS A N   1 
ATOM   1507 C CA  . HIS A 1 180 ? 8.465  3.277   27.942  1.00 48.90  ? 180 HIS A CA  1 
ATOM   1508 C C   . HIS A 1 180 ? 7.911  4.693   28.028  1.00 44.89  ? 180 HIS A C   1 
ATOM   1509 O O   . HIS A 1 180 ? 7.362  5.216   27.053  1.00 47.66  ? 180 HIS A O   1 
ATOM   1510 C CB  . HIS A 1 180 ? 9.882  3.313   27.352  1.00 48.14  ? 180 HIS A CB  1 
ATOM   1511 C CG  . HIS A 1 180 ? 10.942 3.741   28.321  1.00 43.52  ? 180 HIS A CG  1 
ATOM   1512 N ND1 . HIS A 1 180 ? 11.183 5.062   28.631  1.00 41.07  ? 180 HIS A ND1 1 
ATOM   1513 C CD2 . HIS A 1 180 ? 11.840 3.020   29.034  1.00 56.04  ? 180 HIS A CD2 1 
ATOM   1514 C CE1 . HIS A 1 180 ? 12.177 5.137   29.498  1.00 44.03  ? 180 HIS A CE1 1 
ATOM   1515 N NE2 . HIS A 1 180 ? 12.592 3.911   29.762  1.00 40.71  ? 180 HIS A NE2 1 
ATOM   1516 N N   . GLU A 1 181 ? 8.048  5.312   29.206  1.00 46.92  ? 181 GLU A N   1 
ATOM   1517 C CA  . GLU A 1 181 ? 7.531  6.666   29.387  1.00 45.21  ? 181 GLU A CA  1 
ATOM   1518 C C   . GLU A 1 181 ? 8.244  7.679   28.502  1.00 37.06  ? 181 GLU A C   1 
ATOM   1519 O O   . GLU A 1 181 ? 7.715  8.775   28.277  1.00 37.72  ? 181 GLU A O   1 
ATOM   1520 C CB  . GLU A 1 181 ? 7.620  7.100   30.854  1.00 42.94  ? 181 GLU A CB  1 
ATOM   1521 C CG  . GLU A 1 181 ? 7.243  6.020   31.853  1.00 61.82  ? 181 GLU A CG  1 
ATOM   1522 C CD  . GLU A 1 181 ? 7.847  6.258   33.224  1.00 75.45  ? 181 GLU A CD  1 
ATOM   1523 O OE1 . GLU A 1 181 ? 8.339  7.379   33.473  1.00 67.43  ? 181 GLU A OE1 1 
ATOM   1524 O OE2 . GLU A 1 181 ? 7.828  5.324   34.054  1.00 84.93  ? 181 GLU A OE2 1 
ATOM   1525 N N   A CYS A 1 182 ? 9.434  7.349   27.992  0.51 36.32  ? 182 CYS A N   1 
ATOM   1526 N N   B CYS A 1 182 ? 9.431  7.334   28.008  0.49 36.32  ? 182 CYS A N   1 
ATOM   1527 C CA  A CYS A 1 182 ? 10.129 8.287   27.117  0.51 33.15  ? 182 CYS A CA  1 
ATOM   1528 C CA  B CYS A 1 182 ? 10.156 8.217   27.107  0.49 33.16  ? 182 CYS A CA  1 
ATOM   1529 C C   A CYS A 1 182 ? 9.371  8.506   25.814  0.51 32.45  ? 182 CYS A C   1 
ATOM   1530 C C   B CYS A 1 182 ? 9.348  8.505   25.849  0.49 32.47  ? 182 CYS A C   1 
ATOM   1531 O O   A CYS A 1 182 ? 9.454  9.594   25.236  0.51 26.64  ? 182 CYS A O   1 
ATOM   1532 O O   B CYS A 1 182 ? 9.375  9.627   25.331  0.49 26.52  ? 182 CYS A O   1 
ATOM   1533 C CB  A CYS A 1 182 ? 11.567 7.834   26.846  0.51 33.35  ? 182 CYS A CB  1 
ATOM   1534 C CB  B CYS A 1 182 ? 11.484 7.564   26.740  0.49 33.95  ? 182 CYS A CB  1 
ATOM   1535 S SG  A CYS A 1 182 ? 11.795 6.745   25.409  0.51 31.94  ? 182 CYS A SG  1 
ATOM   1536 S SG  B CYS A 1 182 ? 12.646 8.654   25.972  0.49 34.25  ? 182 CYS A SG  1 
ATOM   1537 N N   . LYS A 1 183 ? 8.618  7.502   25.350  1.00 29.77  ? 183 LYS A N   1 
ATOM   1538 C CA  . LYS A 1 183 ? 7.854  7.665   24.113  1.00 25.43  ? 183 LYS A CA  1 
ATOM   1539 C C   . LYS A 1 183 ? 6.883  8.839   24.196  1.00 25.76  ? 183 LYS A C   1 
ATOM   1540 O O   . LYS A 1 183 ? 6.736  9.602   23.233  1.00 25.86  ? 183 LYS A O   1 
ATOM   1541 C CB  . LYS A 1 183 ? 7.095  6.380   23.784  1.00 34.43  ? 183 LYS A CB  1 
ATOM   1542 C CG  . LYS A 1 183 ? 6.478  6.382   22.394  1.00 41.19  ? 183 LYS A CG  1 
ATOM   1543 C CD  . LYS A 1 183 ? 5.849  5.038   22.051  1.00 56.26  ? 183 LYS A CD  1 
ATOM   1544 C CE  . LYS A 1 183 ? 4.734  5.201   21.024  1.00 58.75  ? 183 LYS A CE  1 
ATOM   1545 N NZ  . LYS A 1 183 ? 3.677  6.144   21.490  1.00 57.82  ? 183 LYS A NZ  1 
ATOM   1546 N N   . ASP A 1 184 ? 6.209  9.000   25.338  1.00 28.34  ? 184 ASP A N   1 
ATOM   1547 C CA  A ASP A 1 184 ? 5.251  10.093  25.473  0.50 27.19  ? 184 ASP A CA  1 
ATOM   1548 C CA  B ASP A 1 184 ? 5.252  10.095  25.483  0.50 27.20  ? 184 ASP A CA  1 
ATOM   1549 C C   . ASP A 1 184 ? 5.954  11.445  25.497  1.00 27.26  ? 184 ASP A C   1 
ATOM   1550 O O   . ASP A 1 184 ? 5.460  12.420  24.913  1.00 22.99  ? 184 ASP A O   1 
ATOM   1551 C CB  A ASP A 1 184 ? 4.418  9.894   26.737  0.50 26.77  ? 184 ASP A CB  1 
ATOM   1552 C CB  B ASP A 1 184 ? 4.430  9.909   26.759  0.50 26.76  ? 184 ASP A CB  1 
ATOM   1553 C CG  A ASP A 1 184 ? 2.989  9.500   26.430  0.50 34.18  ? 184 ASP A CG  1 
ATOM   1554 C CG  B ASP A 1 184 ? 3.274  10.889  26.858  0.50 27.94  ? 184 ASP A CG  1 
ATOM   1555 O OD1 A ASP A 1 184 ? 2.182  10.390  26.083  0.50 40.27  ? 184 ASP A OD1 1 
ATOM   1556 O OD1 B ASP A 1 184 ? 2.455  10.944  25.915  0.50 30.04  ? 184 ASP A OD1 1 
ATOM   1557 O OD2 A ASP A 1 184 ? 2.677  8.296   26.526  0.50 37.33  ? 184 ASP A OD2 1 
ATOM   1558 O OD2 B ASP A 1 184 ? 3.175  11.598  27.883  0.50 37.00  ? 184 ASP A OD2 1 
ATOM   1559 N N   . LYS A 1 185 ? 7.104  11.525  26.169  1.00 23.95  ? 185 LYS A N   1 
ATOM   1560 C CA  . LYS A 1 185 ? 7.841  12.781  26.221  1.00 21.88  ? 185 LYS A CA  1 
ATOM   1561 C C   . LYS A 1 185 ? 8.392  13.143  24.848  1.00 17.35  ? 185 LYS A C   1 
ATOM   1562 O O   . LYS A 1 185 ? 8.423  14.324  24.481  1.00 19.37  ? 185 LYS A O   1 
ATOM   1563 C CB  . LYS A 1 185 ? 8.980  12.683  27.237  1.00 24.30  ? 185 LYS A CB  1 
ATOM   1564 C CG  . LYS A 1 185 ? 8.533  12.340  28.656  1.00 31.13  ? 185 LYS A CG  1 
ATOM   1565 C CD  . LYS A 1 185 ? 7.396  13.240  29.135  1.00 32.46  ? 185 LYS A CD  1 
ATOM   1566 C CE  . LYS A 1 185 ? 7.910  14.589  29.609  1.00 42.25  ? 185 LYS A CE  1 
ATOM   1567 N NZ  . LYS A 1 185 ? 6.806  15.594  29.693  1.00 41.07  ? 185 LYS A NZ  1 
ATOM   1568 N N   . LEU A 1 186 ? 8.831  12.144  24.078  1.00 17.05  ? 186 LEU A N   1 
ATOM   1569 C CA  . LEU A 1 186 ? 9.270  12.401  22.705  1.00 18.02  ? 186 LEU A CA  1 
ATOM   1570 C C   . LEU A 1 186 ? 8.106  12.880  21.848  1.00 19.72  ? 186 LEU A C   1 
ATOM   1571 O O   . LEU A 1 186 ? 8.249  13.837  21.067  1.00 16.54  ? 186 LEU A O   1 
ATOM   1572 C CB  . LEU A 1 186 ? 9.855  11.124  22.100  1.00 19.86  ? 186 LEU A CB  1 
ATOM   1573 C CG  . LEU A 1 186 ? 11.183 10.649  22.677  1.00 21.55  ? 186 LEU A CG  1 
ATOM   1574 C CD1 . LEU A 1 186 ? 11.439 9.217   22.217  1.00 26.98  ? 186 LEU A CD1 1 
ATOM   1575 C CD2 . LEU A 1 186 ? 12.344 11.575  22.262  1.00 20.96  ? 186 LEU A CD2 1 
ATOM   1576 N N   A ASP A 1 187 ? 6.941  12.237  21.985  0.64 19.08  ? 187 ASP A N   1 
ATOM   1577 N N   B ASP A 1 187 ? 6.940  12.234  21.986  0.36 19.13  ? 187 ASP A N   1 
ATOM   1578 C CA  A ASP A 1 187 ? 5.788  12.622  21.177  0.64 19.20  ? 187 ASP A CA  1 
ATOM   1579 C CA  B ASP A 1 187 ? 5.771  12.612  21.195  0.36 19.28  ? 187 ASP A CA  1 
ATOM   1580 C C   A ASP A 1 187 ? 5.349  14.046  21.468  0.64 16.96  ? 187 ASP A C   1 
ATOM   1581 C C   B ASP A 1 187 ? 5.362  14.051  21.466  0.36 17.04  ? 187 ASP A C   1 
ATOM   1582 O O   A ASP A 1 187 ? 4.862  14.736  20.566  0.64 17.09  ? 187 ASP A O   1 
ATOM   1583 O O   B ASP A 1 187 ? 4.896  14.751  20.560  0.36 17.10  ? 187 ASP A O   1 
ATOM   1584 C CB  A ASP A 1 187 ? 4.625  11.654  21.404  0.64 23.76  ? 187 ASP A CB  1 
ATOM   1585 C CB  B ASP A 1 187 ? 4.601  11.676  21.502  0.36 23.73  ? 187 ASP A CB  1 
ATOM   1586 C CG  A ASP A 1 187 ? 3.530  11.824  20.379  0.64 23.79  ? 187 ASP A CG  1 
ATOM   1587 C CG  B ASP A 1 187 ? 4.823  10.273  20.986  0.36 23.56  ? 187 ASP A CG  1 
ATOM   1588 O OD1 A ASP A 1 187 ? 3.836  11.719  19.174  0.64 27.11  ? 187 ASP A OD1 1 
ATOM   1589 O OD1 B ASP A 1 187 ? 5.640  10.099  20.061  0.36 29.43  ? 187 ASP A OD1 1 
ATOM   1590 O OD2 A ASP A 1 187 ? 2.373  12.070  20.771  0.64 25.15  ? 187 ASP A OD2 1 
ATOM   1591 O OD2 B ASP A 1 187 ? 4.178  9.340   21.507  0.36 33.89  ? 187 ASP A OD2 1 
ATOM   1592 N N   . GLU A 1 188 ? 5.509  14.502  22.716  1.00 17.77  ? 188 GLU A N   1 
ATOM   1593 C CA  . GLU A 1 188 ? 5.220  15.896  23.049  1.00 15.27  ? 188 GLU A CA  1 
ATOM   1594 C C   . GLU A 1 188 ? 6.081  16.852  22.226  1.00 14.58  ? 188 GLU A C   1 
ATOM   1595 O O   . GLU A 1 188 ? 5.593  17.865  21.713  1.00 15.78  ? 188 GLU A O   1 
ATOM   1596 C CB  . GLU A 1 188 ? 5.476  16.147  24.539  1.00 20.28  ? 188 GLU A CB  1 
ATOM   1597 C CG  . GLU A 1 188 ? 4.418  15.525  25.469  1.00 23.43  ? 188 GLU A CG  1 
ATOM   1598 C CD  . GLU A 1 188 ? 4.736  15.666  26.956  1.00 29.09  ? 188 GLU A CD  1 
ATOM   1599 O OE1 . GLU A 1 188 ? 5.868  16.048  27.315  1.00 32.19  ? 188 GLU A OE1 1 
ATOM   1600 O OE2 . GLU A 1 188 ? 3.830  15.406  27.778  1.00 32.40  ? 188 GLU A OE2 1 
ATOM   1601 N N   . ILE A 1 189 ? 7.386  16.566  22.137  1.00 13.87  ? 189 ILE A N   1 
ATOM   1602 C CA  . ILE A 1 189 ? 8.279  17.388  21.327  1.00 14.51  ? 189 ILE A CA  1 
ATOM   1603 C C   . ILE A 1 189 ? 7.811  17.391  19.878  1.00 15.06  ? 189 ILE A C   1 
ATOM   1604 O O   . ILE A 1 189 ? 7.735  18.446  19.239  1.00 16.11  ? 189 ILE A O   1 
ATOM   1605 C CB  . ILE A 1 189 ? 9.728  16.871  21.456  1.00 15.31  ? 189 ILE A CB  1 
ATOM   1606 C CG1 . ILE A 1 189 ? 10.257 17.097  22.868  1.00 16.83  ? 189 ILE A CG1 1 
ATOM   1607 C CG2 . ILE A 1 189 ? 10.646 17.531  20.417  1.00 13.53  ? 189 ILE A CG2 1 
ATOM   1608 C CD1 . ILE A 1 189 ? 10.523 18.552  23.194  1.00 16.45  ? 189 ILE A CD1 1 
ATOM   1609 N N   . LYS A 1 190 ? 7.502  16.210  19.341  1.00 15.68  ? 190 LYS A N   1 
ATOM   1610 C CA  . LYS A 1 190 ? 7.039  16.127  17.957  1.00 15.44  ? 190 LYS A CA  1 
ATOM   1611 C C   . LYS A 1 190 ? 5.785  16.962  17.748  1.00 16.74  ? 190 LYS A C   1 
ATOM   1612 O O   . LYS A 1 190 ? 5.666  17.683  16.751  1.00 15.02  ? 190 LYS A O   1 
ATOM   1613 C CB  . LYS A 1 190 ? 6.784  14.667  17.589  1.00 15.70  ? 190 LYS A CB  1 
ATOM   1614 C CG  . LYS A 1 190 ? 6.093  14.510  16.241  1.00 18.45  ? 190 LYS A CG  1 
ATOM   1615 C CD  . LYS A 1 190 ? 6.070  13.057  15.816  1.00 21.21  ? 190 LYS A CD  1 
ATOM   1616 C CE  . LYS A 1 190 ? 5.607  12.913  14.370  1.00 32.47  ? 190 LYS A CE  1 
ATOM   1617 N NZ  . LYS A 1 190 ? 5.323  11.482  14.013  1.00 33.40  ? 190 LYS A NZ  1 
ATOM   1618 N N   . GLU A 1 191 ? 4.839  16.892  18.686  1.00 17.15  ? 191 GLU A N   1 
ATOM   1619 C CA  . GLU A 1 191 ? 3.637  17.722  18.580  1.00 16.44  ? 191 GLU A CA  1 
ATOM   1620 C C   . GLU A 1 191 ? 3.983  19.206  18.475  1.00 16.64  ? 191 GLU A C   1 
ATOM   1621 O O   . GLU A 1 191 ? 3.369  19.948  17.695  1.00 16.57  ? 191 GLU A O   1 
ATOM   1622 C CB  . GLU A 1 191 ? 2.748  17.437  19.797  1.00 16.93  ? 191 GLU A CB  1 
ATOM   1623 C CG  . GLU A 1 191 ? 1.452  18.229  19.867  1.00 15.70  ? 191 GLU A CG  1 
ATOM   1624 C CD  . GLU A 1 191 ? 0.587  17.729  21.002  1.00 15.96  ? 191 GLU A CD  1 
ATOM   1625 O OE1 . GLU A 1 191 ? 0.213  16.529  20.985  1.00 19.12  ? 191 GLU A OE1 1 
ATOM   1626 O OE2 . GLU A 1 191 ? 0.322  18.535  21.918  1.00 21.02  ? 191 GLU A OE2 1 
ATOM   1627 N N   . GLY A 1 192 ? 4.980  19.661  19.239  1.00 14.81  ? 192 GLY A N   1 
ATOM   1628 C CA  . GLY A 1 192 ? 5.343  21.058  19.200  1.00 13.56  ? 192 GLY A CA  1 
ATOM   1629 C C   . GLY A 1 192 ? 6.062  21.441  17.923  1.00 14.23  ? 192 GLY A C   1 
ATOM   1630 O O   . GLY A 1 192 ? 5.899  22.564  17.438  1.00 14.66  ? 192 GLY A O   1 
ATOM   1631 N N   . VAL A 1 193 ? 6.860  20.526  17.363  1.00 14.07  ? 193 VAL A N   1 
ATOM   1632 C CA  . VAL A 1 193 ? 7.496  20.801  16.078  1.00 13.83  ? 193 VAL A CA  1 
ATOM   1633 C C   . VAL A 1 193 ? 6.423  20.981  15.009  1.00 16.23  ? 193 VAL A C   1 
ATOM   1634 O O   . VAL A 1 193 ? 6.466  21.916  14.200  1.00 16.41  ? 193 VAL A O   1 
ATOM   1635 C CB  . VAL A 1 193 ? 8.466  19.665  15.694  1.00 13.55  ? 193 VAL A CB  1 
ATOM   1636 C CG1 . VAL A 1 193 ? 8.978  19.878  14.262  1.00 14.86  ? 193 VAL A CG1 1 
ATOM   1637 C CG2 . VAL A 1 193 ? 9.673  19.574  16.631  1.00 13.64  ? 193 VAL A CG2 1 
ATOM   1638 N N   . ILE A 1 194 ? 5.431  20.088  15.008  1.00 15.04  ? 194 ILE A N   1 
ATOM   1639 C CA  . ILE A 1 194 ? 4.363  20.162  14.012  1.00 17.60  ? 194 ILE A CA  1 
ATOM   1640 C C   . ILE A 1 194 ? 3.603  21.468  14.154  1.00 19.28  ? 194 ILE A C   1 
ATOM   1641 O O   . ILE A 1 194 ? 3.277  22.137  13.156  1.00 19.39  ? 194 ILE A O   1 
ATOM   1642 C CB  . ILE A 1 194 ? 3.465  18.906  14.132  1.00 15.71  ? 194 ILE A CB  1 
ATOM   1643 C CG1 . ILE A 1 194 ? 4.184  17.676  13.587  1.00 19.62  ? 194 ILE A CG1 1 
ATOM   1644 C CG2 . ILE A 1 194 ? 2.092  19.135  13.466  1.00 21.14  ? 194 ILE A CG2 1 
ATOM   1645 C CD1 . ILE A 1 194 ? 3.532  16.348  13.927  1.00 22.55  ? 194 ILE A CD1 1 
ATOM   1646 N N   A ARG A 1 195 ? 3.324  21.868  15.392  0.81 18.30  ? 195 ARG A N   1 
ATOM   1647 N N   B ARG A 1 195 ? 3.341  21.886  15.393  0.19 18.32  ? 195 ARG A N   1 
ATOM   1648 C CA  A ARG A 1 195 ? 2.607  23.112  15.621  0.81 17.44  ? 195 ARG A CA  1 
ATOM   1649 C CA  B ARG A 1 195 ? 2.596  23.122  15.614  0.19 17.62  ? 195 ARG A CA  1 
ATOM   1650 C C   A ARG A 1 195 ? 3.395  24.321  15.135  0.81 19.81  ? 195 ARG A C   1 
ATOM   1651 C C   B ARG A 1 195 ? 3.388  24.348  15.173  0.19 19.75  ? 195 ARG A C   1 
ATOM   1652 O O   A ARG A 1 195 ? 2.837  25.214  14.490  0.81 22.88  ? 195 ARG A O   1 
ATOM   1653 O O   B ARG A 1 195 ? 2.823  25.274  14.581  0.19 22.77  ? 195 ARG A O   1 
ATOM   1654 C CB  A ARG A 1 195 ? 2.310  23.264  17.111  0.81 22.54  ? 195 ARG A CB  1 
ATOM   1655 C CB  B ARG A 1 195 ? 2.199  23.234  17.086  0.19 22.31  ? 195 ARG A CB  1 
ATOM   1656 C CG  A ARG A 1 195 ? 1.577  24.527  17.452  0.81 25.96  ? 195 ARG A CG  1 
ATOM   1657 C CG  B ARG A 1 195 ? 1.346  24.444  17.458  0.19 23.88  ? 195 ARG A CG  1 
ATOM   1658 C CD  A ARG A 1 195 ? 1.103  24.468  18.899  0.81 19.31  ? 195 ARG A CD  1 
ATOM   1659 C CD  B ARG A 1 195 ? 2.177  25.592  18.025  0.19 21.57  ? 195 ARG A CD  1 
ATOM   1660 N NE  A ARG A 1 195 ? 2.234  24.314  19.804  0.81 20.38  ? 195 ARG A NE  1 
ATOM   1661 N NE  B ARG A 1 195 ? 2.319  25.536  19.479  0.19 15.49  ? 195 ARG A NE  1 
ATOM   1662 C CZ  A ARG A 1 195 ? 3.039  25.313  20.109  0.81 16.55  ? 195 ARG A CZ  1 
ATOM   1663 C CZ  B ARG A 1 195 ? 3.177  24.753  20.123  0.19 17.85  ? 195 ARG A CZ  1 
ATOM   1664 N NH1 A ARG A 1 195 ? 2.867  26.512  19.580  0.81 20.93  ? 195 ARG A NH1 1 
ATOM   1665 N NH1 B ARG A 1 195 ? 4.011  23.954  19.476  0.19 18.74  ? 195 ARG A NH1 1 
ATOM   1666 N NH2 A ARG A 1 195 ? 4.071  25.099  20.928  0.81 18.26  ? 195 ARG A NH2 1 
ATOM   1667 N NH2 B ARG A 1 195 ? 3.213  24.781  21.449  0.19 22.78  ? 195 ARG A NH2 1 
ATOM   1668 N N   . THR A 1 196 ? 4.694  24.380  15.449  1.00 16.32  ? 196 THR A N   1 
ATOM   1669 C CA  . THR A 1 196 ? 5.483  25.584  15.220  1.00 14.87  ? 196 THR A CA  1 
ATOM   1670 C C   . THR A 1 196 ? 6.236  25.626  13.889  1.00 14.59  ? 196 THR A C   1 
ATOM   1671 O O   . THR A 1 196 ? 6.716  26.703  13.505  1.00 18.89  ? 196 THR A O   1 
ATOM   1672 C CB  . THR A 1 196 ? 6.469  25.852  16.374  1.00 20.39  ? 196 THR A CB  1 
ATOM   1673 O OG1 . THR A 1 196 ? 7.485  24.839  16.402  1.00 18.10  ? 196 THR A OG1 1 
ATOM   1674 C CG2 . THR A 1 196 ? 5.745  25.887  17.706  1.00 17.97  ? 196 THR A CG2 1 
ATOM   1675 N N   . LYS A 1 197 ? 6.331  24.504  13.185  1.00 15.72  ? 197 LYS A N   1 
ATOM   1676 C CA  . LYS A 1 197 ? 7.082  24.407  11.933  1.00 15.80  ? 197 LYS A CA  1 
ATOM   1677 C C   . LYS A 1 197 ? 6.122  23.850  10.901  1.00 14.15  ? 197 LYS A C   1 
ATOM   1678 O O   . LYS A 1 197 ? 6.092  22.640  10.636  1.00 15.02  ? 197 LYS A O   1 
ATOM   1679 C CB  . LYS A 1 197 ? 8.328  23.524  12.094  1.00 13.98  ? 197 LYS A CB  1 
ATOM   1680 C CG  . LYS A 1 197 ? 9.358  24.092  13.067  1.00 15.36  ? 197 LYS A CG  1 
ATOM   1681 C CD  . LYS A 1 197 ? 9.892  25.446  12.551  1.00 16.61  ? 197 LYS A CD  1 
ATOM   1682 C CE  . LYS A 1 197 ? 10.951 25.989  13.495  1.00 18.12  ? 197 LYS A CE  1 
ATOM   1683 N NZ  . LYS A 1 197 ? 11.394 27.351  13.106  1.00 20.38  ? 197 LYS A NZ  1 
ATOM   1684 N N   . PRO A 1 198 ? 5.291  24.713  10.314  1.00 14.87  ? 198 PRO A N   1 
ATOM   1685 C CA  . PRO A 1 198 ? 4.302  24.230  9.343   1.00 15.09  ? 198 PRO A CA  1 
ATOM   1686 C C   . PRO A 1 198 ? 4.932  23.509  8.164   1.00 14.96  ? 198 PRO A C   1 
ATOM   1687 O O   . PRO A 1 198 ? 4.321  22.596  7.598   1.00 15.05  ? 198 PRO A O   1 
ATOM   1688 C CB  . PRO A 1 198 ? 3.530  25.502  8.956   1.00 17.54  ? 198 PRO A CB  1 
ATOM   1689 C CG  . PRO A 1 198 ? 4.397  26.637  9.372   1.00 20.98  ? 198 PRO A CG  1 
ATOM   1690 C CD  . PRO A 1 198 ? 5.151  26.139  10.600  1.00 17.04  ? 198 PRO A CD  1 
ATOM   1691 N N   . GLY A 1 199 ? 6.171  23.847  7.805   1.00 13.31  ? 199 GLY A N   1 
ATOM   1692 C CA  . GLY A 1 199 ? 6.852  23.082  6.769   1.00 15.04  ? 199 GLY A CA  1 
ATOM   1693 C C   . GLY A 1 199 ? 7.109  21.634  7.152   1.00 14.72  ? 199 GLY A C   1 
ATOM   1694 O O   . GLY A 1 199 ? 7.061  20.743  6.308   1.00 15.85  ? 199 GLY A O   1 
ATOM   1695 N N   . VAL A 1 200 ? 7.400  21.379  8.430   1.00 13.74  ? 200 VAL A N   1 
ATOM   1696 C CA  . VAL A 1 200 ? 7.523  19.991  8.875   1.00 14.32  ? 200 VAL A CA  1 
ATOM   1697 C C   . VAL A 1 200 ? 6.172  19.306  8.879   1.00 16.14  ? 200 VAL A C   1 
ATOM   1698 O O   . VAL A 1 200 ? 6.055  18.160  8.448   1.00 14.79  ? 200 VAL A O   1 
ATOM   1699 C CB  . VAL A 1 200 ? 8.168  19.934  10.267  1.00 13.26  ? 200 VAL A CB  1 
ATOM   1700 C CG1 . VAL A 1 200 ? 8.113  18.497  10.809  1.00 14.80  ? 200 VAL A CG1 1 
ATOM   1701 C CG2 . VAL A 1 200 ? 9.608  20.419  10.190  1.00 13.98  ? 200 VAL A CG2 1 
ATOM   1702 N N   . ALA A 1 201 ? 5.142  19.971  9.417   1.00 13.92  ? 201 ALA A N   1 
ATOM   1703 C CA  . ALA A 1 201 ? 3.813  19.361  9.447   1.00 14.96  ? 201 ALA A CA  1 
ATOM   1704 C C   . ALA A 1 201 ? 3.383  18.910  8.060   1.00 16.31  ? 201 ALA A C   1 
ATOM   1705 O O   . ALA A 1 201 ? 2.907  17.784  7.879   1.00 16.76  ? 201 ALA A O   1 
ATOM   1706 C CB  . ALA A 1 201 ? 2.795  20.361  9.995   1.00 16.17  ? 201 ALA A CB  1 
ATOM   1707 N N   . ARG A 1 202 ? 3.559  19.779  7.062   1.00 14.67  ? 202 ARG A N   1 
ATOM   1708 C CA  . ARG A 1 202 ? 3.151  19.425  5.706   1.00 15.40  ? 202 ARG A CA  1 
ATOM   1709 C C   . ARG A 1 202 ? 4.004  18.295  5.153   1.00 16.21  ? 202 ARG A C   1 
ATOM   1710 O O   . ARG A 1 202 ? 3.493  17.398  4.470   1.00 18.34  ? 202 ARG A O   1 
ATOM   1711 C CB  . ARG A 1 202 ? 3.235  20.661  4.813   1.00 17.87  ? 202 ARG A CB  1 
ATOM   1712 C CG  . ARG A 1 202 ? 2.758  20.406  3.390   1.00 22.04  ? 202 ARG A CG  1 
ATOM   1713 C CD  . ARG A 1 202 ? 1.245  20.332  3.371   1.00 27.22  ? 202 ARG A CD  1 
ATOM   1714 N NE  . ARG A 1 202 ? 0.704  19.997  2.061   1.00 45.10  ? 202 ARG A NE  1 
ATOM   1715 C CZ  . ARG A 1 202 ? -0.228 19.074  1.860   1.00 44.62  ? 202 ARG A CZ  1 
ATOM   1716 N NH1 . ARG A 1 202 ? -0.727 18.366  2.862   1.00 44.26  ? 202 ARG A NH1 1 
ATOM   1717 N NH2 . ARG A 1 202 ? -0.666 18.853  0.624   1.00 55.59  ? 202 ARG A NH2 1 
ATOM   1718 N N   . TYR A 1 203 ? 5.310  18.345  5.403   1.00 14.55  ? 203 TYR A N   1 
ATOM   1719 C CA  . TYR A 1 203 ? 6.202  17.309  4.902   1.00 16.90  ? 203 TYR A CA  1 
ATOM   1720 C C   . TYR A 1 203 ? 5.853  15.936  5.476   1.00 16.24  ? 203 TYR A C   1 
ATOM   1721 O O   . TYR A 1 203 ? 5.820  14.936  4.752   1.00 18.89  ? 203 TYR A O   1 
ATOM   1722 C CB  . TYR A 1 203 ? 7.655  17.689  5.223   1.00 15.77  ? 203 TYR A CB  1 
ATOM   1723 C CG  . TYR A 1 203 ? 8.577  16.552  4.952   1.00 13.88  ? 203 TYR A CG  1 
ATOM   1724 C CD1 . TYR A 1 203 ? 8.832  16.141  3.647   1.00 16.71  ? 203 TYR A CD1 1 
ATOM   1725 C CD2 . TYR A 1 203 ? 9.154  15.855  5.997   1.00 17.22  ? 203 TYR A CD2 1 
ATOM   1726 C CE1 . TYR A 1 203 ? 9.660  15.075  3.395   1.00 16.81  ? 203 TYR A CE1 1 
ATOM   1727 C CE2 . TYR A 1 203 ? 9.978  14.783  5.754   1.00 18.78  ? 203 TYR A CE2 1 
ATOM   1728 C CZ  . TYR A 1 203 ? 10.224 14.403  4.457   1.00 18.02  ? 203 TYR A CZ  1 
ATOM   1729 O OH  . TYR A 1 203 ? 11.030 13.318  4.227   1.00 22.14  ? 203 TYR A OH  1 
ATOM   1730 N N   . LEU A 1 204 ? 5.624  15.857  6.792   1.00 16.28  ? 204 LEU A N   1 
ATOM   1731 C CA  . LEU A 1 204 ? 5.288  14.577  7.402   1.00 15.87  ? 204 LEU A CA  1 
ATOM   1732 C C   . LEU A 1 204 ? 3.998  14.018  6.832   1.00 20.90  ? 204 LEU A C   1 
ATOM   1733 O O   . LEU A 1 204 ? 3.866  12.800  6.681   1.00 19.87  ? 204 LEU A O   1 
ATOM   1734 C CB  . LEU A 1 204 ? 5.146  14.764  8.914   1.00 16.56  ? 204 LEU A CB  1 
ATOM   1735 C CG  . LEU A 1 204 ? 6.456  15.052  9.641   1.00 16.15  ? 204 LEU A CG  1 
ATOM   1736 C CD1 . LEU A 1 204 ? 6.185  15.256  11.119  1.00 18.04  ? 204 LEU A CD1 1 
ATOM   1737 C CD2 . LEU A 1 204 ? 7.414  13.907  9.428   1.00 19.22  ? 204 LEU A CD2 1 
ATOM   1738 N N   . ARG A 1 205 ? 3.057  14.894  6.488   1.00 18.18  ? 205 ARG A N   1 
ATOM   1739 C CA  . ARG A 1 205 ? 1.788  14.456  5.920   1.00 26.02  ? 205 ARG A CA  1 
ATOM   1740 C C   . ARG A 1 205 ? 1.952  13.958  4.488   1.00 26.00  ? 205 ARG A C   1 
ATOM   1741 O O   . ARG A 1 205 ? 1.239  13.035  4.070   1.00 32.26  ? 205 ARG A O   1 
ATOM   1742 C CB  . ARG A 1 205 ? 0.770  15.600  6.022   1.00 21.98  ? 205 ARG A CB  1 
ATOM   1743 C CG  . ARG A 1 205 ? -0.666 15.215  5.697   1.00 27.56  ? 205 ARG A CG  1 
ATOM   1744 C CD  . ARG A 1 205 ? -1.201 14.196  6.698   1.00 23.23  ? 205 ARG A CD  1 
ATOM   1745 N NE  . ARG A 1 205 ? -1.264 14.699  8.068   1.00 22.47  ? 205 ARG A NE  1 
ATOM   1746 C CZ  . ARG A 1 205 ? -1.591 13.949  9.113   1.00 26.93  ? 205 ARG A CZ  1 
ATOM   1747 N NH1 . ARG A 1 205 ? -1.850 12.661  8.977   1.00 25.81  ? 205 ARG A NH1 1 
ATOM   1748 N NH2 . ARG A 1 205 ? -1.668 14.504  10.319  1.00 24.04  ? 205 ARG A NH2 1 
ATOM   1749 N N   . SER A 1 206 ? 2.902  14.521  3.734   1.00 21.86  ? 206 SER A N   1 
ATOM   1750 C CA  . SER A 1 206 ? 3.033  14.261  2.305   1.00 24.45  ? 206 SER A CA  1 
ATOM   1751 C C   . SER A 1 206 ? 4.193  13.345  1.925   1.00 28.95  ? 206 SER A C   1 
ATOM   1752 O O   . SER A 1 206 ? 4.239  12.883  0.778   1.00 30.80  ? 206 SER A O   1 
ATOM   1753 C CB  . SER A 1 206 ? 3.164  15.588  1.547   1.00 32.03  ? 206 SER A CB  1 
ATOM   1754 O OG  . SER A 1 206 ? 4.451  16.147  1.723   1.00 41.34  ? 206 SER A OG  1 
ATOM   1755 N N   . ARG A 1 207 ? 5.121  13.059  2.835   1.00 24.20  ? 207 ARG A N   1 
ATOM   1756 C CA  . ARG A 1 207 ? 6.287  12.268  2.461   1.00 22.10  ? 207 ARG A CA  1 
ATOM   1757 C C   . ARG A 1 207 ? 5.886  10.822  2.153   1.00 26.57  ? 207 ARG A C   1 
ATOM   1758 O O   . ARG A 1 207 ? 4.854  10.337  2.622   1.00 25.77  ? 207 ARG A O   1 
ATOM   1759 C CB  . ARG A 1 207 ? 7.330  12.298  3.580   1.00 20.41  ? 207 ARG A CB  1 
ATOM   1760 C CG  . ARG A 1 207 ? 6.899  11.598  4.843   1.00 24.15  ? 207 ARG A CG  1 
ATOM   1761 C CD  . ARG A 1 207 ? 8.027  11.507  5.881   1.00 21.63  ? 207 ARG A CD  1 
ATOM   1762 N NE  . ARG A 1 207 ? 7.524  10.899  7.109   1.00 21.64  ? 207 ARG A NE  1 
ATOM   1763 C CZ  . ARG A 1 207 ? 8.220  10.748  8.229   1.00 22.68  ? 207 ARG A CZ  1 
ATOM   1764 N NH1 . ARG A 1 207 ? 9.494  11.106  8.312   1.00 22.76  ? 207 ARG A NH1 1 
ATOM   1765 N NH2 . ARG A 1 207 ? 7.629  10.217  9.291   1.00 25.37  ? 207 ARG A NH2 1 
ATOM   1766 N N   . PRO A 1 208 ? 6.692  10.111  1.362   1.00 27.38  ? 208 PRO A N   1 
ATOM   1767 C CA  . PRO A 1 208 ? 6.371  8.713   1.052   1.00 32.73  ? 208 PRO A CA  1 
ATOM   1768 C C   . PRO A 1 208 ? 6.334  7.865   2.314   1.00 35.25  ? 208 PRO A C   1 
ATOM   1769 O O   . PRO A 1 208 ? 7.211  7.959   3.175   1.00 39.13  ? 208 PRO A O   1 
ATOM   1770 C CB  . PRO A 1 208 ? 7.532  8.284   0.146   1.00 35.14  ? 208 PRO A CB  1 
ATOM   1771 C CG  . PRO A 1 208 ? 8.028  9.556   -0.451  1.00 34.73  ? 208 PRO A CG  1 
ATOM   1772 C CD  . PRO A 1 208 ? 7.918  10.547  0.671   1.00 32.31  ? 208 PRO A CD  1 
ATOM   1773 N N   . ALA A 1 209 ? 5.313  7.020   2.413   1.00 37.70  ? 209 ALA A N   1 
ATOM   1774 C CA  . ALA A 1 209 ? 5.231  6.066   3.511   1.00 39.14  ? 209 ALA A CA  1 
ATOM   1775 C C   . ALA A 1 209 ? 6.182  4.914   3.209   1.00 42.65  ? 209 ALA A C   1 
ATOM   1776 O O   . ALA A 1 209 ? 5.937  4.118   2.296   1.00 51.84  ? 209 ALA A O   1 
ATOM   1777 C CB  . ALA A 1 209 ? 3.797  5.573   3.682   1.00 48.35  ? 209 ALA A CB  1 
ATOM   1778 N N   . THR A 1 210 ? 7.277  4.835   3.957   1.00 39.99  ? 210 THR A N   1 
ATOM   1779 C CA  . THR A 1 210 ? 8.288  3.808   3.771   1.00 43.38  ? 210 THR A CA  1 
ATOM   1780 C C   . THR A 1 210 ? 8.415  2.971   5.036   1.00 38.96  ? 210 THR A C   1 
ATOM   1781 O O   . THR A 1 210 ? 8.026  3.391   6.130   1.00 40.18  ? 210 THR A O   1 
ATOM   1782 C CB  . THR A 1 210 ? 9.655  4.419   3.412   1.00 38.85  ? 210 THR A CB  1 
ATOM   1783 O OG1 . THR A 1 210 ? 10.162 5.144   4.540   1.00 35.41  ? 210 THR A OG1 1 
ATOM   1784 C CG2 . THR A 1 210 ? 9.535  5.359   2.223   1.00 40.00  ? 210 THR A CG2 1 
ATOM   1785 N N   . ASP A 1 211 ? 8.974  1.772   4.869   1.00 39.71  ? 211 ASP A N   1 
ATOM   1786 C CA  . ASP A 1 211 ? 9.169  0.882   6.008   1.00 48.93  ? 211 ASP A CA  1 
ATOM   1787 C C   . ASP A 1 211 ? 10.286 1.376   6.919   1.00 45.56  ? 211 ASP A C   1 
ATOM   1788 O O   . ASP A 1 211 ? 10.140 1.376   8.145   1.00 44.72  ? 211 ASP A O   1 
ATOM   1789 C CB  . ASP A 1 211 ? 9.461  -0.536  5.517   1.00 50.73  ? 211 ASP A CB  1 
ATOM   1790 C CG  . ASP A 1 211 ? 8.254  -1.445  5.619   1.00 66.64  ? 211 ASP A CG  1 
ATOM   1791 O OD1 . ASP A 1 211 ? 8.194  -2.442  4.868   1.00 73.14  ? 211 ASP A OD1 1 
ATOM   1792 O OD2 . ASP A 1 211 ? 7.364  -1.157  6.448   1.00 69.98  ? 211 ASP A OD2 1 
ATOM   1793 N N   . PHE A 1 212 ? 11.407 1.799   6.346   1.00 43.96  ? 212 PHE A N   1 
ATOM   1794 C CA  . PHE A 1 212 ? 12.544 2.220   7.158   1.00 35.25  ? 212 PHE A CA  1 
ATOM   1795 C C   . PHE A 1 212 ? 12.867 3.691   6.945   1.00 34.95  ? 212 PHE A C   1 
ATOM   1796 O O   . PHE A 1 212 ? 12.173 4.339   6.154   1.00 30.41  ? 212 PHE A O   1 
ATOM   1797 C CB  . PHE A 1 212 ? 13.761 1.344   6.868   1.00 36.13  ? 212 PHE A CB  1 
ATOM   1798 C CG  . PHE A 1 212 ? 13.549 -0.100  7.211   1.00 47.06  ? 212 PHE A CG  1 
ATOM   1799 C CD1 . PHE A 1 212 ? 12.895 -0.950  6.331   1.00 51.25  ? 212 PHE A CD1 1 
ATOM   1800 C CD2 . PHE A 1 212 ? 13.961 -0.598  8.436   1.00 47.71  ? 212 PHE A CD2 1 
ATOM   1801 C CE1 . PHE A 1 212 ? 12.684 -2.278  6.656   1.00 51.08  ? 212 PHE A CE1 1 
ATOM   1802 C CE2 . PHE A 1 212 ? 13.754 -1.927  8.765   1.00 49.33  ? 212 PHE A CE2 1 
ATOM   1803 C CZ  . PHE A 1 212 ? 13.114 -2.766  7.875   1.00 49.67  ? 212 PHE A CZ  1 
ATOM   1804 O OXT . PHE A 1 212 ? 13.800 4.232   7.559   1.00 30.20  ? 212 PHE A OXT 1 
HETATM 1805 C C1  . PEG B 2 .   ? 34.596 32.462  -1.675  1.00 56.13  ? 301 PEG A C1  1 
HETATM 1806 O O1  . PEG B 2 .   ? 35.552 31.658  -2.355  1.00 46.18  ? 301 PEG A O1  1 
HETATM 1807 C C2  . PEG B 2 .   ? 33.193 32.031  -1.962  1.00 52.58  ? 301 PEG A C2  1 
HETATM 1808 O O2  . PEG B 2 .   ? 33.198 30.926  -2.855  1.00 54.32  ? 301 PEG A O2  1 
HETATM 1809 C C3  . PEG B 2 .   ? 31.944 30.263  -2.905  1.00 54.28  ? 301 PEG A C3  1 
HETATM 1810 C C4  . PEG B 2 .   ? 30.854 31.269  -3.132  1.00 36.95  ? 301 PEG A C4  1 
HETATM 1811 O O4  . PEG B 2 .   ? 29.574 30.654  -3.093  1.00 39.11  ? 301 PEG A O4  1 
HETATM 1812 O O   . HOH C 3 .   ? 22.724 32.877  0.597   1.00 36.70  ? 401 HOH A O   1 
HETATM 1813 O O   . HOH C 3 .   ? 37.598 31.784  -1.644  1.00 46.29  ? 402 HOH A O   1 
HETATM 1814 O O   . HOH C 3 .   ? 26.136 9.284   21.454  1.00 31.55  ? 403 HOH A O   1 
HETATM 1815 O O   . HOH C 3 .   ? 18.277 35.757  -0.657  1.00 29.06  ? 404 HOH A O   1 
HETATM 1816 O O   . HOH C 3 .   ? 3.265  16.218  29.908  1.00 45.94  ? 405 HOH A O   1 
HETATM 1817 O O   . HOH C 3 .   ? 18.524 32.236  22.487  1.00 38.94  ? 406 HOH A O   1 
HETATM 1818 O O   . HOH C 3 .   ? 17.521 29.116  24.793  1.00 38.74  ? 407 HOH A O   1 
HETATM 1819 O O   . HOH C 3 .   ? 0.490  11.151  19.586  1.00 50.55  ? 408 HOH A O   1 
HETATM 1820 O O   . HOH C 3 .   ? 26.122 33.687  2.353   1.00 46.13  ? 409 HOH A O   1 
HETATM 1821 O O   . HOH C 3 .   ? 22.491 20.229  31.495  1.00 42.00  ? 410 HOH A O   1 
HETATM 1822 O O   . HOH C 3 .   ? 17.639 27.503  21.304  1.00 42.85  ? 411 HOH A O   1 
HETATM 1823 O O   . HOH C 3 .   ? 9.225  8.285   4.516   1.00 33.36  ? 412 HOH A O   1 
HETATM 1824 O O   . HOH C 3 .   ? 19.244 11.105  12.271  1.00 19.79  ? 413 HOH A O   1 
HETATM 1825 O O   . HOH C 3 .   ? 0.614  20.969  22.118  1.00 22.52  ? 414 HOH A O   1 
HETATM 1826 O O   . HOH C 3 .   ? 16.166 21.820  -8.725  1.00 37.25  ? 415 HOH A O   1 
HETATM 1827 O O   . HOH C 3 .   ? 11.043 10.698  10.653  1.00 29.03  ? 416 HOH A O   1 
HETATM 1828 O O   . HOH C 3 .   ? 10.426 14.766  -0.270  1.00 27.42  ? 417 HOH A O   1 
HETATM 1829 O O   . HOH C 3 .   ? 23.879 34.597  -1.620  1.00 40.92  ? 418 HOH A O   1 
HETATM 1830 O O   . HOH C 3 .   ? 13.180 4.173   10.590  1.00 43.23  ? 419 HOH A O   1 
HETATM 1831 O O   . HOH C 3 .   ? 4.974  27.209  21.963  1.00 35.99  ? 420 HOH A O   1 
HETATM 1832 O O   . HOH C 3 .   ? 33.312 12.253  3.505   1.00 30.45  ? 421 HOH A O   1 
HETATM 1833 O O   . HOH C 3 .   ? 1.498  22.936  11.545  1.00 22.46  ? 422 HOH A O   1 
HETATM 1834 O O   . HOH C 3 .   ? 5.256  6.636   27.098  1.00 43.05  ? 423 HOH A O   1 
HETATM 1835 O O   . HOH C 3 .   ? -0.281 10.697  26.661  1.00 44.68  ? 424 HOH A O   1 
HETATM 1836 O O   . HOH C 3 .   ? 31.287 25.616  2.954   1.00 35.65  ? 425 HOH A O   1 
HETATM 1837 O O   . HOH C 3 .   ? 15.366 23.198  20.909  1.00 15.90  ? 426 HOH A O   1 
HETATM 1838 O O   . HOH C 3 .   ? 23.081 15.494  33.316  1.00 59.00  ? 427 HOH A O   1 
HETATM 1839 O O   . HOH C 3 .   ? 30.375 29.789  -5.676  1.00 22.86  ? 428 HOH A O   1 
HETATM 1840 O O   . HOH C 3 .   ? 25.547 35.516  -5.034  1.00 37.94  ? 429 HOH A O   1 
HETATM 1841 O O   . HOH C 3 .   ? 22.374 4.991   5.629   1.00 23.37  ? 430 HOH A O   1 
HETATM 1842 O O   . HOH C 3 .   ? 14.952 21.139  36.055  1.00 39.79  ? 431 HOH A O   1 
HETATM 1843 O O   . HOH C 3 .   ? 1.217  17.689  24.252  1.00 26.13  ? 432 HOH A O   1 
HETATM 1844 O O   . HOH C 3 .   ? 12.105 25.494  -6.023  1.00 32.65  ? 433 HOH A O   1 
HETATM 1845 O O   . HOH C 3 .   ? 23.678 0.815   13.661  1.00 31.22  ? 434 HOH A O   1 
HETATM 1846 O O   . HOH C 3 .   ? 14.865 0.396   -3.788  1.00 43.59  ? 435 HOH A O   1 
HETATM 1847 O O   . HOH C 3 .   ? 31.645 8.549   8.734   1.00 34.04  ? 436 HOH A O   1 
HETATM 1848 O O   . HOH C 3 .   ? 25.614 28.788  5.986   1.00 22.20  ? 437 HOH A O   1 
HETATM 1849 O O   . HOH C 3 .   ? 1.981  26.703  12.422  1.00 29.77  ? 438 HOH A O   1 
HETATM 1850 O O   . HOH C 3 .   ? 16.259 23.745  27.508  1.00 18.65  ? 439 HOH A O   1 
HETATM 1851 O O   . HOH C 3 .   ? 27.804 10.963  3.495   1.00 20.19  ? 440 HOH A O   1 
HETATM 1852 O O   . HOH C 3 .   ? 28.272 21.070  22.825  1.00 13.28  ? 441 HOH A O   1 
HETATM 1853 O O   . HOH C 3 .   ? 17.746 14.795  19.595  1.00 17.60  ? 442 HOH A O   1 
HETATM 1854 O O   . HOH C 3 .   ? 7.192  21.195  3.571   1.00 23.72  ? 443 HOH A O   1 
HETATM 1855 O O   . HOH C 3 .   ? 3.436  10.394  4.922   1.00 36.47  ? 444 HOH A O   1 
HETATM 1856 O O   . HOH C 3 .   ? 33.644 22.681  -6.581  1.00 25.45  ? 445 HOH A O   1 
HETATM 1857 O O   . HOH C 3 .   ? 17.143 19.061  29.744  1.00 28.65  ? 446 HOH A O   1 
HETATM 1858 O O   . HOH C 3 .   ? 4.291  28.806  19.840  1.00 42.64  ? 447 HOH A O   1 
HETATM 1859 O O   . HOH C 3 .   ? 16.833 11.612  -0.792  1.00 19.52  ? 448 HOH A O   1 
HETATM 1860 O O   . HOH C 3 .   ? 0.147  15.121  18.655  1.00 25.76  ? 449 HOH A O   1 
HETATM 1861 O O   . HOH C 3 .   ? 23.664 21.983  -10.979 1.00 37.93  ? 450 HOH A O   1 
HETATM 1862 O O   . HOH C 3 .   ? 23.771 18.337  16.936  1.00 22.75  ? 451 HOH A O   1 
HETATM 1863 O O   . HOH C 3 .   ? 23.541 0.466   -11.338 1.00 35.18  ? 452 HOH A O   1 
HETATM 1864 O O   . HOH C 3 .   ? 22.346 29.981  13.200  1.00 27.41  ? 453 HOH A O   1 
HETATM 1865 O O   . HOH C 3 .   ? 24.544 16.464  31.699  1.00 26.16  ? 454 HOH A O   1 
HETATM 1866 O O   . HOH C 3 .   ? 14.302 28.622  9.207   1.00 22.59  ? 455 HOH A O   1 
HETATM 1867 O O   . HOH C 3 .   ? 11.198 9.892   3.826   1.00 26.71  ? 456 HOH A O   1 
HETATM 1868 O O   . HOH C 3 .   ? 15.921 2.953   -2.252  1.00 40.44  ? 457 HOH A O   1 
HETATM 1869 O O   . HOH C 3 .   ? 17.144 23.835  -4.210  1.00 14.82  ? 458 HOH A O   1 
HETATM 1870 O O   . HOH C 3 .   ? 19.470 8.225   11.724  1.00 24.55  ? 459 HOH A O   1 
HETATM 1871 O O   . HOH C 3 .   ? 8.486  16.296  26.413  1.00 24.76  ? 460 HOH A O   1 
HETATM 1872 O O   . HOH C 3 .   ? 22.756 21.032  -6.949  1.00 18.60  ? 461 HOH A O   1 
HETATM 1873 O O   . HOH C 3 .   ? 11.635 21.763  1.702   1.00 27.03  ? 462 HOH A O   1 
HETATM 1874 O O   . HOH C 3 .   ? -2.017 16.194  22.587  1.00 21.99  ? 463 HOH A O   1 
HETATM 1875 O O   . HOH C 3 .   ? 17.801 27.616  26.537  1.00 43.83  ? 464 HOH A O   1 
HETATM 1876 O O   . HOH C 3 .   ? 22.568 19.468  -10.732 1.00 40.12  ? 465 HOH A O   1 
HETATM 1877 O O   . HOH C 3 .   ? 14.948 28.180  30.930  1.00 19.93  ? 466 HOH A O   1 
HETATM 1878 O O   . HOH C 3 .   ? 10.304 22.780  0.359   1.00 48.29  ? 467 HOH A O   1 
HETATM 1879 O O   . HOH C 3 .   ? 19.726 12.965  30.936  1.00 31.13  ? 468 HOH A O   1 
HETATM 1880 O O   . HOH C 3 .   ? 15.422 6.783   10.445  1.00 29.28  ? 469 HOH A O   1 
HETATM 1881 O O   . HOH C 3 .   ? 24.703 28.026  16.910  1.00 23.20  ? 470 HOH A O   1 
HETATM 1882 O O   . HOH C 3 .   ? 30.262 15.573  12.778  1.00 28.16  ? 471 HOH A O   1 
HETATM 1883 O O   . HOH C 3 .   ? 12.413 26.981  10.416  1.00 21.30  ? 472 HOH A O   1 
HETATM 1884 O O   . HOH C 3 .   ? 26.839 24.888  -12.886 1.00 37.72  ? 473 HOH A O   1 
HETATM 1885 O O   . HOH C 3 .   ? 11.835 18.209  -1.670  1.00 22.80  ? 474 HOH A O   1 
HETATM 1886 O O   . HOH C 3 .   ? 17.592 19.489  27.063  1.00 20.53  ? 475 HOH A O   1 
HETATM 1887 O O   . HOH C 3 .   ? 18.465 27.772  -6.321  1.00 17.11  ? 476 HOH A O   1 
HETATM 1888 O O   . HOH C 3 .   ? 17.865 10.917  9.691   1.00 18.29  ? 477 HOH A O   1 
HETATM 1889 O O   . HOH C 3 .   ? 20.685 28.834  14.890  1.00 19.29  ? 478 HOH A O   1 
HETATM 1890 O O   . HOH C 3 .   ? 25.527 29.754  3.404   1.00 21.26  ? 479 HOH A O   1 
HETATM 1891 O O   . HOH C 3 .   ? 28.443 23.911  9.859   1.00 15.30  ? 480 HOH A O   1 
HETATM 1892 O O   . HOH C 3 .   ? 14.062 29.538  6.594   1.00 30.41  ? 481 HOH A O   1 
HETATM 1893 O O   . HOH C 3 .   ? 22.032 8.008   13.111  1.00 34.64  ? 482 HOH A O   1 
HETATM 1894 O O   . HOH C 3 .   ? 15.501 27.449  21.296  1.00 22.11  ? 483 HOH A O   1 
HETATM 1895 O O   . HOH C 3 .   ? 11.286 12.157  -3.334  1.00 34.50  ? 484 HOH A O   1 
HETATM 1896 O O   . HOH C 3 .   ? 8.641  28.458  23.941  1.00 28.22  ? 485 HOH A O   1 
HETATM 1897 O O   . HOH C 3 .   ? 20.066 15.415  26.733  1.00 25.52  ? 486 HOH A O   1 
HETATM 1898 O O   . HOH C 3 .   ? 4.744  10.617  8.266   1.00 37.21  ? 487 HOH A O   1 
HETATM 1899 O O   . HOH C 3 .   ? 31.367 23.541  -10.529 1.00 26.90  ? 488 HOH A O   1 
HETATM 1900 O O   . HOH C 3 .   ? 13.228 27.574  15.320  1.00 21.33  ? 489 HOH A O   1 
HETATM 1901 O O   . HOH C 3 .   ? 28.776 27.158  3.233   1.00 31.51  ? 490 HOH A O   1 
HETATM 1902 O O   . HOH C 3 .   ? 19.847 18.175  26.235  1.00 15.54  ? 491 HOH A O   1 
HETATM 1903 O O   . HOH C 3 .   ? 24.034 24.329  28.575  1.00 32.33  ? 492 HOH A O   1 
HETATM 1904 O O   . HOH C 3 .   ? 2.806  21.794  21.004  1.00 24.79  ? 493 HOH A O   1 
HETATM 1905 O O   . HOH C 3 .   ? 19.760 31.813  5.867   1.00 33.97  ? 494 HOH A O   1 
HETATM 1906 O O   . HOH C 3 .   ? 24.349 6.772   5.756   1.00 31.05  ? 495 HOH A O   1 
HETATM 1907 O O   . HOH C 3 .   ? 0.977  18.962  16.495  1.00 25.73  ? 496 HOH A O   1 
HETATM 1908 O O   . HOH C 3 .   ? 3.621  24.753  5.867   1.00 51.27  ? 497 HOH A O   1 
HETATM 1909 O O   . HOH C 3 .   ? 23.413 10.937  11.149  1.00 34.46  ? 498 HOH A O   1 
HETATM 1910 O O   . HOH C 3 .   ? 8.207  25.480  8.981   1.00 16.26  ? 499 HOH A O   1 
HETATM 1911 O O   . HOH C 3 .   ? 17.655 27.936  16.908  1.00 22.63  ? 500 HOH A O   1 
HETATM 1912 O O   . HOH C 3 .   ? 6.034  27.928  24.276  1.00 21.89  ? 501 HOH A O   1 
HETATM 1913 O O   . HOH C 3 .   ? 27.888 36.543  -6.035  1.00 28.06  ? 502 HOH A O   1 
HETATM 1914 O O   . HOH C 3 .   ? 8.356  18.698  0.706   1.00 30.64  ? 503 HOH A O   1 
HETATM 1915 O O   . HOH C 3 .   ? 18.822 31.038  15.788  1.00 36.56  ? 504 HOH A O   1 
HETATM 1916 O O   . HOH C 3 .   ? 13.811 10.346  -6.707  1.00 34.24  ? 505 HOH A O   1 
HETATM 1917 O O   . HOH C 3 .   ? 16.404 23.564  30.161  1.00 23.81  ? 506 HOH A O   1 
HETATM 1918 O O   . HOH C 3 .   ? 25.008 3.316   19.247  1.00 33.36  ? 507 HOH A O   1 
HETATM 1919 O O   . HOH C 3 .   ? 28.309 31.387  22.792  1.00 30.37  ? 508 HOH A O   1 
HETATM 1920 O O   . HOH C 3 .   ? 8.371  28.202  19.557  1.00 36.65  ? 509 HOH A O   1 
HETATM 1921 O O   . HOH C 3 .   ? 22.630 36.497  -5.482  1.00 44.08  ? 510 HOH A O   1 
HETATM 1922 O O   . HOH C 3 .   ? 21.351 11.870  10.355  1.00 33.47  ? 511 HOH A O   1 
HETATM 1923 O O   . HOH C 3 .   ? 12.072 16.395  -4.984  1.00 26.45  ? 512 HOH A O   1 
HETATM 1924 O O   . HOH C 3 .   ? 12.765 7.780   11.102  1.00 31.08  ? 513 HOH A O   1 
HETATM 1925 O O   . HOH C 3 .   ? 32.802 18.629  -4.324  1.00 26.29  ? 514 HOH A O   1 
HETATM 1926 O O   . HOH C 3 .   ? 28.588 13.327  22.492  1.00 28.55  ? 515 HOH A O   1 
HETATM 1927 O O   . HOH C 3 .   ? 1.907  22.330  0.786   1.00 42.95  ? 516 HOH A O   1 
HETATM 1928 O O   . HOH C 3 .   ? 2.577  13.927  17.736  1.00 38.80  ? 517 HOH A O   1 
HETATM 1929 O O   . HOH C 3 .   ? 9.700  26.596  17.181  1.00 22.55  ? 518 HOH A O   1 
HETATM 1930 O O   . HOH C 3 .   ? 0.555  20.788  17.647  1.00 27.48  ? 519 HOH A O   1 
HETATM 1931 O O   . HOH C 3 .   ? 26.936 9.986   6.083   1.00 26.76  ? 520 HOH A O   1 
HETATM 1932 O O   . HOH C 3 .   ? 11.424 1.630   0.611   1.00 39.71  ? 521 HOH A O   1 
HETATM 1933 O O   . HOH C 3 .   ? 8.961  29.012  13.019  1.00 47.40  ? 522 HOH A O   1 
HETATM 1934 O O   . HOH C 3 .   ? 8.908  30.028  2.778   1.00 33.22  ? 523 HOH A O   1 
HETATM 1935 O O   . HOH C 3 .   ? 25.063 13.142  16.908  1.00 29.71  ? 524 HOH A O   1 
HETATM 1936 O O   . HOH C 3 .   ? 4.234  11.640  11.241  1.00 33.43  ? 525 HOH A O   1 
HETATM 1937 O O   . HOH C 3 .   ? 27.253 11.593  10.239  1.00 36.53  ? 526 HOH A O   1 
HETATM 1938 O O   . HOH C 3 .   ? 17.540 29.285  20.063  1.00 39.65  ? 527 HOH A O   1 
HETATM 1939 O O   . HOH C 3 .   ? 14.502 29.859  15.086  1.00 40.63  ? 528 HOH A O   1 
HETATM 1940 O O   . HOH C 3 .   ? 25.683 8.432   7.609   1.00 34.69  ? 529 HOH A O   1 
HETATM 1941 O O   . HOH C 3 .   ? 16.719 26.650  -4.431  1.00 17.83  ? 530 HOH A O   1 
HETATM 1942 O O   . HOH C 3 .   ? 10.761 17.333  0.749   1.00 19.00  ? 531 HOH A O   1 
HETATM 1943 O O   . HOH C 3 .   ? 23.161 31.408  2.935   1.00 22.79  ? 532 HOH A O   1 
HETATM 1944 O O   . HOH C 3 .   ? 22.826 34.572  23.117  1.00 39.00  ? 533 HOH A O   1 
HETATM 1945 O O   . HOH C 3 .   ? 23.296 -2.839  -4.401  1.00 46.04  ? 534 HOH A O   1 
HETATM 1946 O O   . HOH C 3 .   ? 23.472 34.514  -9.811  1.00 39.32  ? 535 HOH A O   1 
HETATM 1947 O O   . HOH C 3 .   ? 27.359 26.083  16.436  1.00 22.35  ? 536 HOH A O   1 
HETATM 1948 O O   . HOH C 3 .   ? 11.323 21.213  -2.692  1.00 30.47  ? 537 HOH A O   1 
HETATM 1949 O O   . HOH C 3 .   ? 27.018 30.365  25.857  1.00 25.09  ? 538 HOH A O   1 
HETATM 1950 O O   . HOH C 3 .   ? 29.019 13.431  13.694  1.00 36.80  ? 539 HOH A O   1 
HETATM 1951 O O   . HOH C 3 .   ? 16.554 -0.156  -2.648  1.00 32.56  ? 540 HOH A O   1 
HETATM 1952 O O   . HOH C 3 .   ? 25.463 16.090  17.351  1.00 15.58  ? 541 HOH A O   1 
HETATM 1953 O O   . HOH C 3 .   ? 6.421  20.982  24.853  1.00 36.67  ? 542 HOH A O   1 
HETATM 1954 O O   . HOH C 3 .   ? 7.112  5.163   11.399  1.00 49.86  ? 543 HOH A O   1 
HETATM 1955 O O   . HOH C 3 .   ? 22.620 10.519  13.489  1.00 43.47  ? 544 HOH A O   1 
HETATM 1956 O O   . HOH C 3 .   ? 4.165  18.919  0.152   1.00 46.16  ? 545 HOH A O   1 
HETATM 1957 O O   . HOH C 3 .   ? 26.421 9.835   19.225  1.00 39.48  ? 546 HOH A O   1 
HETATM 1958 O O   . HOH C 3 .   ? 29.948 9.635   2.079   1.00 44.21  ? 547 HOH A O   1 
HETATM 1959 O O   . HOH C 3 .   ? 33.756 24.898  1.905   1.00 53.19  ? 548 HOH A O   1 
HETATM 1960 O O   . HOH C 3 .   ? 22.587 32.140  15.653  1.00 52.95  ? 549 HOH A O   1 
HETATM 1961 O O   . HOH C 3 .   ? -0.019 21.705  12.531  1.00 35.27  ? 550 HOH A O   1 
HETATM 1962 O O   . HOH C 3 .   ? 31.726 26.337  -11.889 1.00 35.10  ? 551 HOH A O   1 
HETATM 1963 O O   . HOH C 3 .   ? 11.615 21.367  -5.226  1.00 46.03  ? 552 HOH A O   1 
HETATM 1964 O O   . HOH C 3 .   ? 28.340 28.541  5.277   1.00 31.57  ? 553 HOH A O   1 
HETATM 1965 O O   . HOH C 3 .   ? 26.295 29.582  18.796  1.00 40.54  ? 554 HOH A O   1 
HETATM 1966 O O   . HOH C 3 .   ? 5.919  19.361  1.862   1.00 34.45  ? 555 HOH A O   1 
HETATM 1967 O O   . HOH C 3 .   ? 22.171 25.247  29.035  1.00 51.52  ? 556 HOH A O   1 
HETATM 1968 O O   . HOH C 3 .   ? 3.697  19.539  24.323  1.00 43.50  ? 557 HOH A O   1 
HETATM 1969 O O   . HOH C 3 .   ? 14.477 28.669  27.840  1.00 22.93  ? 558 HOH A O   1 
HETATM 1970 O O   . HOH C 3 .   ? -1.073 12.985  19.638  1.00 48.47  ? 559 HOH A O   1 
HETATM 1971 O O   . HOH C 3 .   ? 25.337 31.631  27.284  1.00 45.02  ? 560 HOH A O   1 
HETATM 1972 O O   . HOH C 3 .   ? 23.745 33.751  2.165   1.00 67.08  ? 561 HOH A O   1 
HETATM 1973 O O   . HOH C 3 .   ? 15.416 22.492  -6.082  1.00 27.17  ? 562 HOH A O   1 
HETATM 1974 O O   . HOH C 3 .   ? 1.983  13.356  10.125  1.00 35.19  ? 563 HOH A O   1 
HETATM 1975 O O   . HOH C 3 .   ? 9.559  28.866  16.139  1.00 50.57  ? 564 HOH A O   1 
HETATM 1976 O O   . HOH C 3 .   ? 2.005  13.212  15.233  1.00 43.76  ? 565 HOH A O   1 
HETATM 1977 O O   . HOH C 3 .   ? 10.669 29.342  -4.279  1.00 40.01  ? 566 HOH A O   1 
HETATM 1978 O O   . HOH C 3 .   ? 28.742 28.574  13.585  1.00 44.89  ? 567 HOH A O   1 
HETATM 1979 O O   . HOH C 3 .   ? 6.219  28.444  21.038  1.00 38.31  ? 568 HOH A O   1 
HETATM 1980 O O   . HOH C 3 .   ? 34.358 26.019  -9.847  1.00 37.27  ? 569 HOH A O   1 
HETATM 1981 O O   . HOH C 3 .   ? 25.959 30.602  10.571  1.00 42.29  ? 570 HOH A O   1 
HETATM 1982 O O   . HOH C 3 .   ? 21.856 32.574  5.020   1.00 37.44  ? 571 HOH A O   1 
HETATM 1983 O O   . HOH C 3 .   ? 20.236 34.759  23.275  1.00 50.20  ? 572 HOH A O   1 
HETATM 1984 O O   . HOH C 3 .   ? 24.349 29.071  14.297  1.00 33.03  ? 573 HOH A O   1 
HETATM 1985 O O   . HOH C 3 .   ? 11.280 29.100  -1.705  1.00 29.57  ? 574 HOH A O   1 
HETATM 1986 O O   . HOH C 3 .   ? 7.993  28.265  9.239   1.00 35.52  ? 575 HOH A O   1 
HETATM 1987 O O   . HOH C 3 .   ? 33.970 23.438  -9.505  1.00 42.62  ? 576 HOH A O   1 
HETATM 1988 O O   . HOH C 3 .   ? 32.165 23.638  1.211   1.00 52.25  ? 577 HOH A O   1 
HETATM 1989 O O   . HOH C 3 .   ? 12.910 23.269  -6.635  1.00 40.55  ? 578 HOH A O   1 
HETATM 1990 O O   . HOH C 3 .   ? 25.153 30.762  7.954   1.00 43.60  ? 579 HOH A O   1 
HETATM 1991 O O   . HOH C 3 .   ? 34.660 20.901  -4.338  1.00 46.53  ? 580 HOH A O   1 
HETATM 1992 O O   . HOH C 3 .   ? 26.809 29.346  12.797  1.00 39.48  ? 581 HOH A O   1 
HETATM 1993 O O   . HOH C 3 .   ? 18.002 22.001  30.905  1.00 44.73  ? 582 HOH A O   1 
HETATM 1994 O O   . HOH C 3 .   ? 23.185 22.371  31.534  1.00 45.65  ? 583 HOH A O   1 
HETATM 1995 O O   . HOH C 3 .   ? 26.760 4.915   6.266   1.00 45.84  ? 584 HOH A O   1 
HETATM 1996 O O   . HOH C 3 .   ? 10.103 16.639  -2.944  1.00 33.83  ? 585 HOH A O   1 
HETATM 1997 O O   . HOH C 3 .   ? 0.000  16.360  16.328  0.50 32.04  ? 586 HOH A O   1 
HETATM 1998 O O   . HOH C 3 .   ? 16.183 31.550  5.483   1.00 36.56  ? 587 HOH A O   1 
HETATM 1999 O O   . HOH C 3 .   ? 36.800 25.223  2.213   1.00 58.14  ? 588 HOH A O   1 
# 
