data_8WTS
# 
_entry.id   8WTS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8WTS         pdb_00008wts 10.2210/pdb8wts/pdb 
WWPDB D_1300041776 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-23 ? 
2 'Structure model' 1 1 2025-05-14 ? 
3 'Structure model' 1 2 2025-05-28 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Derived calculations' 
2 3 'Structure model' 'Database references'  
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' pdbx_struct_assembly      
2 2 'Structure model' pdbx_struct_assembly_gen  
3 2 'Structure model' pdbx_struct_assembly_prop 
4 2 'Structure model' pdbx_struct_oper_list     
5 3 'Structure model' citation                  
6 3 'Structure model' citation_author           
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_pdbx_struct_assembly.details'             
2  2 'Structure model' '_pdbx_struct_assembly.method_details'      
3  2 'Structure model' '_pdbx_struct_assembly.oligomeric_count'    
4  2 'Structure model' '_pdbx_struct_assembly.oligomeric_details'  
5  2 'Structure model' '_pdbx_struct_assembly_gen.oper_expression' 
6  3 'Structure model' '_citation.country'                         
7  3 'Structure model' '_citation.journal_abbrev'                  
8  3 'Structure model' '_citation.journal_id_CSD'                  
9  3 'Structure model' '_citation.journal_id_ISSN'                 
10 3 'Structure model' '_citation.journal_volume'                  
11 3 'Structure model' '_citation.page_first'                      
12 3 'Structure model' '_citation.page_last'                       
13 3 'Structure model' '_citation.pdbx_database_id_DOI'            
14 3 'Structure model' '_citation.pdbx_database_id_PubMed'         
15 3 'Structure model' '_citation.title'                           
16 3 'Structure model' '_citation.year'                            
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8WTS 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              xiao.ding@insilico.ai 
_pdbx_contact_author.name_first         Xiao 
_pdbx_contact_author.name_last          Ding 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3482-1870 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Peng, J.' 1 0000-0001-9737-089X 
'Sun, D.'  2 0009-0004-0082-6918 
'Ding, X.' 3 0000-0003-3482-1870 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4546 
_citation.page_last                 4546 
_citation.title                     'A novel, covalent broad-spectrum inhibitor targeting human coronavirus M pro.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59870-4 
_citation.pdbx_database_id_PubMed   40374668 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sun, J.'           1  ?                   
primary 'Sun, D.'           2  ?                   
primary 'Yang, Q.'          3  0009-0009-1648-4189 
primary 'Wang, D.'          4  ?                   
primary 'Peng, J.'          5  ?                   
primary 'Guo, H.'           6  ?                   
primary 'Ding, X.'          7  ?                   
primary 'Chen, Z.'          8  ?                   
primary 'Yuan, B.'          9  ?                   
primary 'Ivanenkov, Y.A.'   10 ?                   
primary 'Yuan, J.'          11 ?                   
primary 'Zagribelnyy, B.A.' 12 ?                   
primary 'He, Y.'            13 ?                   
primary 'Su, J.'            14 ?                   
primary 'Wang, L.'          15 ?                   
primary 'Tang, J.'          16 ?                   
primary 'Li, Z.'            17 ?                   
primary 'Li, R.'            18 ?                   
primary 'Li, T.'            19 ?                   
primary 'Hu, X.'            20 ?                   
primary 'Liang, X.'         21 ?                   
primary 'Zhu, A.'           22 ?                   
primary 'Wei, P.'           23 ?                   
primary 'Fan, Y.'           24 ?                   
primary 'Liu, S.'           25 ?                   
primary 'Zheng, J.'         26 ?                   
primary 'Guan, X.'          27 ?                   
primary 'Aliper, A.'        28 ?                   
primary 'Yang, M.'          29 ?                   
primary 'Bezrukov, D.S.'    30 ?                   
primary 'Xie, Z.'           31 ?                   
primary 'Terentiev, V.A.'   32 ?                   
primary 'Peng, G.'          33 ?                   
primary 'Polykovskiy, D.A.' 34 0000-0002-0899-8368 
primary 'Malyshev, A.S.'    35 0000-0002-5308-1698 
primary 'Malkov, M.N.'      36 ?                   
primary 'Zhu, Q.'           37 ?                   
primary 'Aspuru-Guzik, A.'  38 0000-0002-8277-4434 
primary 'Ding, X.'          39 0000-0003-3482-1870 
primary 'Cai, X.'           40 0009-0008-5044-6568 
primary 'Zhang, M.'         41 ?                   
primary 'Zhao, J.'          42 0000-0002-2615-3182 
primary 'Zhong, N.'         43 ?                   
primary 'Ren, F.'           44 0000-0001-9157-9182 
primary 'Chen, X.'          45 0000-0002-4052-8155 
primary 'Zhavoronkov, A.'   46 0000-0001-7067-8966 
primary 'Zhao, J.'          47 0000-0003-2515-5589 
# 
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 '3C-like proteinase' 33697.418 1   3.4.22.69 ? ? ? 
2 non-polymer syn 
;(2~{R})-2-[[4-[chloranyl-bis(fluoranyl)methoxy]phenyl]-(2-chloranyl-2-fluoranyl-ethanoyl)amino]-~{N}-(oxan-4-yl)-2-pyrimidin-5-yl-propanamide
;
521.317   1   ?         ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?         ? ? ? 
4 non-polymer syn 'CHLORIDE ION' 35.453    4   ?         ? ? ? 
5 water       nat water 18.015    251 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO, 3CLp, Main protease, Mpro, Non-structural protein 5, nsp5, SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF
;
_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 
;(2~{R})-2-[[4-[chloranyl-bis(fluoranyl)methoxy]phenyl]-(2-chloranyl-2-fluoranyl-ethanoyl)amino]-~{N}-(oxan-4-yl)-2-pyrimidin-5-yl-propanamide
;
XDQ 
3 1,2-ETHANEDIOL EDO 
4 'CHLORIDE ION' CL  
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 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                   305 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 phage EcSzw-2' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     2419741 
_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 
CL  non-polymer         . 'CHLORIDE ION' ?                 'Cl -1'                35.453  
CYS 'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'         121.158 
EDO non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'             62.068  
GLN 'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'         146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'           147.129 
GLY 'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'           75.067  
HIS 'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'       156.162 
HOH non-polymer         . WATER ?                 'H2 O'                 18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'          131.173 
LEU 'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'          131.173 
LYS 'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1'       147.195 
MET 'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'        149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'          165.189 
PRO 'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'           115.130 
SER 'L-peptide linking' y SERINE ?                 'C3 H7 N O3'           105.093 
THR 'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'           119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'        204.225 
TYR 'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'          181.189 
VAL 'L-peptide linking' y VALINE ?                 'C5 H11 N O2'          117.146 
XDQ non-polymer         . 
;(2~{R})-2-[[4-[chloranyl-bis(fluoranyl)methoxy]phenyl]-(2-chloranyl-2-fluoranyl-ethanoyl)amino]-~{N}-(oxan-4-yl)-2-pyrimidin-5-yl-propanamide
;
?                 'C21 H21 Cl2 F3 N4 O4' 521.317 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XDQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XDQ 
_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 XDQ 1   401 1   XDQ LIG A . 
C 3 EDO 1   402 1   EDO EDO A . 
D 3 EDO 1   403 2   EDO EDO A . 
E 4 CL  1   404 1   CL  CL  A . 
F 4 CL  1   405 2   CL  CL  A . 
G 4 CL  1   406 3   CL  CL  A . 
H 4 CL  1   407 4   CL  CL  A . 
I 5 HOH 1   501 206 HOH HOH A . 
I 5 HOH 2   502 224 HOH HOH A . 
I 5 HOH 3   503 220 HOH HOH A . 
I 5 HOH 4   504 69  HOH HOH A . 
I 5 HOH 5   505 134 HOH HOH A . 
I 5 HOH 6   506 157 HOH HOH A . 
I 5 HOH 7   507 110 HOH HOH A . 
I 5 HOH 8   508 182 HOH HOH A . 
I 5 HOH 9   509 11  HOH HOH A . 
I 5 HOH 10  510 14  HOH HOH A . 
I 5 HOH 11  511 154 HOH HOH A . 
I 5 HOH 12  512 52  HOH HOH A . 
I 5 HOH 13  513 39  HOH HOH A . 
I 5 HOH 14  514 90  HOH HOH A . 
I 5 HOH 15  515 140 HOH HOH A . 
I 5 HOH 16  516 118 HOH HOH A . 
I 5 HOH 17  517 225 HOH HOH A . 
I 5 HOH 18  518 63  HOH HOH A . 
I 5 HOH 19  519 44  HOH HOH A . 
I 5 HOH 20  520 145 HOH HOH A . 
I 5 HOH 21  521 161 HOH HOH A . 
I 5 HOH 22  522 120 HOH HOH A . 
I 5 HOH 23  523 103 HOH HOH A . 
I 5 HOH 24  524 95  HOH HOH A . 
I 5 HOH 25  525 162 HOH HOH A . 
I 5 HOH 26  526 130 HOH HOH A . 
I 5 HOH 27  527 250 HOH HOH A . 
I 5 HOH 28  528 122 HOH HOH A . 
I 5 HOH 29  529 117 HOH HOH A . 
I 5 HOH 30  530 217 HOH HOH A . 
I 5 HOH 31  531 99  HOH HOH A . 
I 5 HOH 32  532 180 HOH HOH A . 
I 5 HOH 33  533 128 HOH HOH A . 
I 5 HOH 34  534 74  HOH HOH A . 
I 5 HOH 35  535 37  HOH HOH A . 
I 5 HOH 36  536 77  HOH HOH A . 
I 5 HOH 37  537 68  HOH HOH A . 
I 5 HOH 38  538 246 HOH HOH A . 
I 5 HOH 39  539 126 HOH HOH A . 
I 5 HOH 40  540 53  HOH HOH A . 
I 5 HOH 41  541 15  HOH HOH A . 
I 5 HOH 42  542 50  HOH HOH A . 
I 5 HOH 43  543 171 HOH HOH A . 
I 5 HOH 44  544 96  HOH HOH A . 
I 5 HOH 45  545 119 HOH HOH A . 
I 5 HOH 46  546 61  HOH HOH A . 
I 5 HOH 47  547 218 HOH HOH A . 
I 5 HOH 48  548 10  HOH HOH A . 
I 5 HOH 49  549 179 HOH HOH A . 
I 5 HOH 50  550 167 HOH HOH A . 
I 5 HOH 51  551 4   HOH HOH A . 
I 5 HOH 52  552 78  HOH HOH A . 
I 5 HOH 53  553 48  HOH HOH A . 
I 5 HOH 54  554 144 HOH HOH A . 
I 5 HOH 55  555 23  HOH HOH A . 
I 5 HOH 56  556 143 HOH HOH A . 
I 5 HOH 57  557 60  HOH HOH A . 
I 5 HOH 58  558 168 HOH HOH A . 
I 5 HOH 59  559 247 HOH HOH A . 
I 5 HOH 60  560 42  HOH HOH A . 
I 5 HOH 61  561 141 HOH HOH A . 
I 5 HOH 62  562 105 HOH HOH A . 
I 5 HOH 63  563 177 HOH HOH A . 
I 5 HOH 64  564 8   HOH HOH A . 
I 5 HOH 65  565 132 HOH HOH A . 
I 5 HOH 66  566 45  HOH HOH A . 
I 5 HOH 67  567 244 HOH HOH A . 
I 5 HOH 68  568 29  HOH HOH A . 
I 5 HOH 69  569 22  HOH HOH A . 
I 5 HOH 70  570 33  HOH HOH A . 
I 5 HOH 71  571 158 HOH HOH A . 
I 5 HOH 72  572 133 HOH HOH A . 
I 5 HOH 73  573 248 HOH HOH A . 
I 5 HOH 74  574 85  HOH HOH A . 
I 5 HOH 75  575 239 HOH HOH A . 
I 5 HOH 76  576 46  HOH HOH A . 
I 5 HOH 77  577 35  HOH HOH A . 
I 5 HOH 78  578 174 HOH HOH A . 
I 5 HOH 79  579 210 HOH HOH A . 
I 5 HOH 80  580 86  HOH HOH A . 
I 5 HOH 81  581 27  HOH HOH A . 
I 5 HOH 82  582 163 HOH HOH A . 
I 5 HOH 83  583 232 HOH HOH A . 
I 5 HOH 84  584 26  HOH HOH A . 
I 5 HOH 85  585 101 HOH HOH A . 
I 5 HOH 86  586 129 HOH HOH A . 
I 5 HOH 87  587 201 HOH HOH A . 
I 5 HOH 88  588 147 HOH HOH A . 
I 5 HOH 89  589 2   HOH HOH A . 
I 5 HOH 90  590 113 HOH HOH A . 
I 5 HOH 91  591 38  HOH HOH A . 
I 5 HOH 92  592 40  HOH HOH A . 
I 5 HOH 93  593 3   HOH HOH A . 
I 5 HOH 94  594 202 HOH HOH A . 
I 5 HOH 95  595 47  HOH HOH A . 
I 5 HOH 96  596 159 HOH HOH A . 
I 5 HOH 97  597 116 HOH HOH A . 
I 5 HOH 98  598 136 HOH HOH A . 
I 5 HOH 99  599 156 HOH HOH A . 
I 5 HOH 100 600 30  HOH HOH A . 
I 5 HOH 101 601 97  HOH HOH A . 
I 5 HOH 102 602 18  HOH HOH A . 
I 5 HOH 103 603 71  HOH HOH A . 
I 5 HOH 104 604 139 HOH HOH A . 
I 5 HOH 105 605 57  HOH HOH A . 
I 5 HOH 106 606 151 HOH HOH A . 
I 5 HOH 107 607 219 HOH HOH A . 
I 5 HOH 108 608 64  HOH HOH A . 
I 5 HOH 109 609 150 HOH HOH A . 
I 5 HOH 110 610 186 HOH HOH A . 
I 5 HOH 111 611 226 HOH HOH A . 
I 5 HOH 112 612 215 HOH HOH A . 
I 5 HOH 113 613 65  HOH HOH A . 
I 5 HOH 114 614 31  HOH HOH A . 
I 5 HOH 115 615 56  HOH HOH A . 
I 5 HOH 116 616 6   HOH HOH A . 
I 5 HOH 117 617 34  HOH HOH A . 
I 5 HOH 118 618 94  HOH HOH A . 
I 5 HOH 119 619 1   HOH HOH A . 
I 5 HOH 120 620 7   HOH HOH A . 
I 5 HOH 121 621 127 HOH HOH A . 
I 5 HOH 122 622 203 HOH HOH A . 
I 5 HOH 123 623 58  HOH HOH A . 
I 5 HOH 124 624 178 HOH HOH A . 
I 5 HOH 125 625 41  HOH HOH A . 
I 5 HOH 126 626 72  HOH HOH A . 
I 5 HOH 127 627 87  HOH HOH A . 
I 5 HOH 128 628 16  HOH HOH A . 
I 5 HOH 129 629 115 HOH HOH A . 
I 5 HOH 130 630 70  HOH HOH A . 
I 5 HOH 131 631 243 HOH HOH A . 
I 5 HOH 132 632 75  HOH HOH A . 
I 5 HOH 133 633 36  HOH HOH A . 
I 5 HOH 134 634 43  HOH HOH A . 
I 5 HOH 135 635 185 HOH HOH A . 
I 5 HOH 136 636 184 HOH HOH A . 
I 5 HOH 137 637 28  HOH HOH A . 
I 5 HOH 138 638 123 HOH HOH A . 
I 5 HOH 139 639 207 HOH HOH A . 
I 5 HOH 140 640 245 HOH HOH A . 
I 5 HOH 141 641 80  HOH HOH A . 
I 5 HOH 142 642 12  HOH HOH A . 
I 5 HOH 143 643 5   HOH HOH A . 
I 5 HOH 144 644 241 HOH HOH A . 
I 5 HOH 145 645 112 HOH HOH A . 
I 5 HOH 146 646 25  HOH HOH A . 
I 5 HOH 147 647 109 HOH HOH A . 
I 5 HOH 148 648 73  HOH HOH A . 
I 5 HOH 149 649 49  HOH HOH A . 
I 5 HOH 150 650 83  HOH HOH A . 
I 5 HOH 151 651 9   HOH HOH A . 
I 5 HOH 152 652 13  HOH HOH A . 
I 5 HOH 153 653 137 HOH HOH A . 
I 5 HOH 154 654 121 HOH HOH A . 
I 5 HOH 155 655 108 HOH HOH A . 
I 5 HOH 156 656 24  HOH HOH A . 
I 5 HOH 157 657 55  HOH HOH A . 
I 5 HOH 158 658 32  HOH HOH A . 
I 5 HOH 159 659 20  HOH HOH A . 
I 5 HOH 160 660 152 HOH HOH A . 
I 5 HOH 161 661 17  HOH HOH A . 
I 5 HOH 162 662 66  HOH HOH A . 
I 5 HOH 163 663 153 HOH HOH A . 
I 5 HOH 164 664 81  HOH HOH A . 
I 5 HOH 165 665 176 HOH HOH A . 
I 5 HOH 166 666 170 HOH HOH A . 
I 5 HOH 167 667 183 HOH HOH A . 
I 5 HOH 168 668 166 HOH HOH A . 
I 5 HOH 169 669 242 HOH HOH A . 
I 5 HOH 170 670 257 HOH HOH A . 
I 5 HOH 171 671 82  HOH HOH A . 
I 5 HOH 172 672 254 HOH HOH A . 
I 5 HOH 173 673 54  HOH HOH A . 
I 5 HOH 174 674 172 HOH HOH A . 
I 5 HOH 175 675 84  HOH HOH A . 
I 5 HOH 176 676 138 HOH HOH A . 
I 5 HOH 177 677 187 HOH HOH A . 
I 5 HOH 178 678 238 HOH HOH A . 
I 5 HOH 179 679 255 HOH HOH A . 
I 5 HOH 180 680 240 HOH HOH A . 
I 5 HOH 181 681 227 HOH HOH A . 
I 5 HOH 182 682 211 HOH HOH A . 
I 5 HOH 183 683 76  HOH HOH A . 
I 5 HOH 184 684 62  HOH HOH A . 
I 5 HOH 185 685 234 HOH HOH A . 
I 5 HOH 186 686 256 HOH HOH A . 
I 5 HOH 187 687 124 HOH HOH A . 
I 5 HOH 188 688 230 HOH HOH A . 
I 5 HOH 189 689 142 HOH HOH A . 
I 5 HOH 190 690 155 HOH HOH A . 
I 5 HOH 191 691 93  HOH HOH A . 
I 5 HOH 192 692 114 HOH HOH A . 
I 5 HOH 193 693 229 HOH HOH A . 
I 5 HOH 194 694 231 HOH HOH A . 
I 5 HOH 195 695 160 HOH HOH A . 
I 5 HOH 196 696 135 HOH HOH A . 
I 5 HOH 197 697 252 HOH HOH A . 
I 5 HOH 198 698 131 HOH HOH A . 
I 5 HOH 199 699 198 HOH HOH A . 
I 5 HOH 200 700 190 HOH HOH A . 
I 5 HOH 201 701 237 HOH HOH A . 
I 5 HOH 202 702 208 HOH HOH A . 
I 5 HOH 203 703 98  HOH HOH A . 
I 5 HOH 204 704 21  HOH HOH A . 
I 5 HOH 205 705 233 HOH HOH A . 
I 5 HOH 206 706 125 HOH HOH A . 
I 5 HOH 207 707 189 HOH HOH A . 
I 5 HOH 208 708 107 HOH HOH A . 
I 5 HOH 209 709 100 HOH HOH A . 
I 5 HOH 210 710 91  HOH HOH A . 
I 5 HOH 211 711 19  HOH HOH A . 
I 5 HOH 212 712 204 HOH HOH A . 
I 5 HOH 213 713 253 HOH HOH A . 
I 5 HOH 214 714 79  HOH HOH A . 
I 5 HOH 215 715 148 HOH HOH A . 
I 5 HOH 216 716 89  HOH HOH A . 
I 5 HOH 217 717 195 HOH HOH A . 
I 5 HOH 218 718 223 HOH HOH A . 
I 5 HOH 219 719 236 HOH HOH A . 
I 5 HOH 220 720 216 HOH HOH A . 
I 5 HOH 221 721 165 HOH HOH A . 
I 5 HOH 222 722 51  HOH HOH A . 
I 5 HOH 223 723 191 HOH HOH A . 
I 5 HOH 224 724 197 HOH HOH A . 
I 5 HOH 225 725 104 HOH HOH A . 
I 5 HOH 226 726 106 HOH HOH A . 
I 5 HOH 227 727 221 HOH HOH A . 
I 5 HOH 228 728 251 HOH HOH A . 
I 5 HOH 229 729 205 HOH HOH A . 
I 5 HOH 230 730 200 HOH HOH A . 
I 5 HOH 231 731 88  HOH HOH A . 
I 5 HOH 232 732 194 HOH HOH A . 
I 5 HOH 233 733 164 HOH HOH A . 
I 5 HOH 234 734 111 HOH HOH A . 
I 5 HOH 235 735 146 HOH HOH A . 
I 5 HOH 236 736 222 HOH HOH A . 
I 5 HOH 237 737 59  HOH HOH A . 
I 5 HOH 238 738 181 HOH HOH A . 
I 5 HOH 239 739 199 HOH HOH A . 
I 5 HOH 240 740 188 HOH HOH A . 
I 5 HOH 241 741 235 HOH HOH A . 
I 5 HOH 242 742 175 HOH HOH A . 
I 5 HOH 243 743 92  HOH HOH A . 
I 5 HOH 244 744 192 HOH HOH A . 
I 5 HOH 245 745 196 HOH HOH A . 
I 5 HOH 246 746 169 HOH HOH A . 
I 5 HOH 247 747 67  HOH HOH A . 
I 5 HOH 248 748 173 HOH HOH A . 
I 5 HOH 249 749 214 HOH HOH A . 
I 5 HOH 250 750 193 HOH HOH A . 
I 5 HOH 251 751 149 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   115.69 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WTS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     98.460 
_cell.length_a_esd                 ? 
_cell.length_b                     80.980 
_cell.length_b_esd                 ? 
_cell.length_c                     51.340 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8WTS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8WTS 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.06 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Sodium acetate pH 4.6, 8 % w/v PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-23 
_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   0.96546 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID09' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID09 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8WTS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.56 
_reflns.d_resolution_low                               46.31 
_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                                     50168 
_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                           97.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.56 
_reflns_shell.d_res_low                                     1.59 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             327 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.818 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            0.70 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.33 
_refine.aniso_B[2][2]                            1.91 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.56 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.637 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8WTS 
_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                            1.56 
_refine.ls_d_res_low                             46.31 
_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                     47381 
_refine.ls_number_reflns_R_free                  2518 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.69 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18055 
_refine.ls_R_factor_R_free                       0.20713 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17915 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.078 
_refine.pdbx_overall_ESU_R_Free                  0.079 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             2.006 
_refine.overall_SU_ML                            0.067 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.56 
_refine_hist.d_res_low                        46.31 
_refine_hist.number_atoms_solvent             251 
_refine_hist.number_atoms_total               2654 
_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        2358 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.013  2504 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  2323 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.866  1.661  3417 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.502  1.587  5347 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.189  5.000  322  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.306 23.279 122  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.722 15.000 401  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.566 15.000 11   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.099  0.200  326  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  2891 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  597  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.790  2.653  1240 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.779  2.651  1239 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.964  3.971  1554 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.964  3.975  1555 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.762  3.028  1264 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.761  3.031  1265 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.694  4.384  1856 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.755  32.611 2824 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.732  32.159 2771 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.560 
_refine_ls_shell.d_res_low                        1.601 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             179 
_refine_ls_shell.number_reflns_R_work             3467 
_refine_ls_shell.percent_reflns_obs               95.60 
_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                  0.309 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_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                  0.297 
# 
_struct.entry_id                     8WTS 
_struct.title                        'SARS-CoV-2 3CLpro bound to covalent inhibitor' 
_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        8WTS 
_struct_keywords.text            'protease inhibitor, covalent, VIRUS, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8WTS 
_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                 305 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3568 
_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       305 
# 
_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)' 3990  ? 
1 MORE         -91   ? 
1 'SSA (A^2)'  26470 ? 
# 
_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,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'mass spectrometry' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_556 -x,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 -22.2559829447 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 46.2651793811 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 THR A 45  ? MET A 49  ? THR A 45  MET A 49  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           XDQ 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C15 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            XDQ 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.909 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      XDQ 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       XDQ 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C15 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        XDQ 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   8WTS 
_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   Y 
# 
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 O A HOH 567 ? ? O A HOH 711 ? ? 2.00 
2 1 O A HOH 583 ? ? O A HOH 711 ? ? 2.13 
3 1 O A HOH 585 ? ? O A HOH 640 ? ? 2.16 
4 1 O A HOH 567 ? ? O A HOH 738 ? ? 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 536 ? ? 1_555 O A HOH 536 ? ? 2_555 1.23 
2 1 O A HOH 575 ? ? 1_555 O A HOH 685 ? ? 2_556 1.90 
3 1 O A HOH 681 ? ? 1_555 O A HOH 720 ? ? 2_556 2.14 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              117 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              117 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              117 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                119.28 
_pdbx_validate_rmsd_angle.angle_target_value         111.50 
_pdbx_validate_rmsd_angle.angle_deviation            7.78 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 5   ? ? -68.84  95.35   
2 1 ASP A 33  ? ? 48.77   -134.28 
3 1 ASN A 51  ? ? -140.92 56.77   
4 1 ASN A 84  ? ? 57.45   -118.79 
5 1 TYR A 154 ? ? 62.77   -116.27 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 658 ? I HOH . 
2 1 A HOH 659 ? I HOH . 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
XDQ N3   N  N N 402 
XDQ C4   C  N R 403 
XDQ C6   C  N N 404 
XDQ C7   C  Y N 405 
XDQ C8   C  Y N 406 
XDQ N12  N  Y N 407 
XDQ C13  C  Y N 408 
XDQ C15  C  N S 409 
XDQ C20  C  Y N 410 
XDQ C21  C  Y N 411 
XDQ C22  C  Y N 412 
XDQ O1   O  N N 413 
XDQ C2   C  N N 414 
XDQ N5   N  N N 415 
XDQ C9   C  Y N 416 
XDQ N10  N  Y N 417 
XDQ C11  C  Y N 418 
XDQ C14  C  N N 419 
XDQ O16  O  N N 420 
XDQ F17  F  N N 421 
XDQ C19  C  Y N 422 
XDQ C23  C  Y N 423 
XDQ O24  O  N N 424 
XDQ C25  C  N N 425 
XDQ F26  F  N N 426 
XDQ F27  F  N N 427 
XDQ CL2  CL N N 428 
XDQ C29  C  N N 429 
XDQ C30  C  N N 430 
XDQ C31  C  N N 431 
XDQ C32  C  N N 432 
XDQ O33  O  N N 433 
XDQ C34  C  N N 434 
XDQ H1   H  N N 435 
XDQ H2   H  N N 436 
XDQ H3   H  N N 437 
XDQ H4   H  N N 438 
XDQ H5   H  N N 439 
XDQ H6   H  N N 440 
XDQ H8   H  N N 441 
XDQ H9   H  N N 442 
XDQ H10  H  N N 443 
XDQ H11  H  N N 444 
XDQ H12  H  N N 445 
XDQ H13  H  N N 446 
XDQ H14  H  N N 447 
XDQ H15  H  N N 448 
XDQ H16  H  N N 449 
XDQ H17  H  N N 450 
XDQ H18  H  N N 451 
XDQ H19  H  N N 452 
XDQ H20  H  N N 453 
XDQ H21  H  N N 454 
XDQ H22  H  N N 455 
XDQ CL1  CL N N 456 
# 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
XDQ F27 C25  sing N N 385 
XDQ C25 CL2  sing N N 386 
XDQ C25 F26  sing N N 387 
XDQ C25 O24  sing N N 388 
XDQ O33 C32  sing N N 389 
XDQ O33 C34  sing N N 390 
XDQ O24 C22  sing N N 391 
XDQ C32 C31  sing N N 392 
XDQ C34 C30  sing N N 393 
XDQ C22 C21  doub Y N 394 
XDQ C22 C23  sing Y N 395 
XDQ C31 C29  sing N N 396 
XDQ C21 C20  sing Y N 397 
XDQ C23 C19  doub Y N 398 
XDQ C30 C29  sing N N 399 
XDQ C29 N3   sing N N 400 
XDQ C20 C13  doub Y N 401 
XDQ C19 C13  sing Y N 402 
XDQ N3  C2   sing N N 403 
XDQ C13 N5   sing N N 404 
XDQ C2  O1   doub N N 405 
XDQ C2  C4   sing N N 406 
XDQ N5  C4   sing N N 407 
XDQ N5  C14  sing N N 408 
XDQ C6  C4   sing N N 409 
XDQ C4  C7   sing N N 410 
XDQ C15 C14  sing N N 411 
XDQ C15 F17  sing N N 412 
XDQ C14 O16  doub N N 413 
XDQ C7  C8   doub Y N 414 
XDQ C7  C9   sing Y N 415 
XDQ C8  N12  sing Y N 416 
XDQ C9  N10  doub Y N 417 
XDQ N12 C11  doub Y N 418 
XDQ N10 C11  sing Y N 419 
XDQ N3  H1   sing N N 420 
XDQ C6  H2   sing N N 421 
XDQ C6  H3   sing N N 422 
XDQ C6  H4   sing N N 423 
XDQ C8  H5   sing N N 424 
XDQ C15 H6   sing N N 425 
XDQ C20 H8   sing N N 426 
XDQ C21 H9   sing N N 427 
XDQ C9  H10  sing N N 428 
XDQ C11 H11  sing N N 429 
XDQ C19 H12  sing N N 430 
XDQ C23 H13  sing N N 431 
XDQ C29 H14  sing N N 432 
XDQ C30 H15  sing N N 433 
XDQ C30 H16  sing N N 434 
XDQ C31 H17  sing N N 435 
XDQ C31 H18  sing N N 436 
XDQ C32 H19  sing N N 437 
XDQ C32 H20  sing N N 438 
XDQ C34 H21  sing N N 439 
XDQ C34 H22  sing N N 440 
XDQ C15 CL1  sing N N 441 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6lu7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8WTS 
_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]   0.010156 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004886 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012349 
_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]   0.021614 
_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  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 1   ? -0.641  36.225 36.113  1.00 22.60  ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -0.988  34.930 35.561  1.00 23.21  ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -2.261  35.080 34.741  1.00 21.84  ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -2.945  36.121 34.827  1.00 17.92  ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -1.187  33.810 36.604  1.00 28.49  ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -0.131  33.791 37.557  1.00 31.79  ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -2.539  34.035 33.985  1.00 21.71  ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -3.715  33.937 33.103  1.00 21.56  ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -3.311  34.149 31.666  1.00 21.68  ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -2.223  34.659 31.388  1.00 22.54  ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -4.215  33.822 30.739  1.00 21.53  ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? -3.906  33.953 29.304  1.00 22.16  ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -5.209  34.071 28.544  1.00 21.60  ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -6.015  33.136 28.582  1.00 21.88  ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? -2.988  32.846 28.784  1.00 22.02  ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? -2.229  33.251 27.548  1.00 22.23  ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? -1.206  34.182 27.631  1.00 26.36  ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? -2.584  32.760 26.310  1.00 26.40  ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? -0.505  34.569 26.504  1.00 26.83  ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? -1.869  33.131 25.187  1.00 24.89  ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? -0.864  34.054 25.284  1.00 23.73  ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? -5.435  35.249 27.967  1.00 19.55  ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -6.687  35.561 27.284  1.00 20.63  ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? -6.425  35.977 25.825  1.00 17.64  ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? -5.331  36.491 25.501  1.00 18.58  ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -7.368  36.683 28.066  1.00 21.82  ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -7.982  36.216 29.370  1.00 21.41  ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -9.314  35.629 29.031  1.00 26.35  ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -10.075 35.271 30.218  1.00 26.33  ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -11.213 34.590 30.154  1.00 27.81  ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -11.732 34.243 28.978  1.00 27.99  ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -11.853 34.314 31.262  1.00 22.66  ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? -7.462  35.867 24.994  1.00 19.60  ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? -7.505  36.533 23.658  1.00 21.85  ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? -7.609  38.022 23.909  1.00 23.40  ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? -8.700  38.492 24.241  1.00 27.04  ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? -8.695  36.050 22.836  1.00 28.04  ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? -8.537  34.676 22.230  1.00 36.10  ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? -7.774  34.729 20.946  1.00 40.91  ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? -7.785  33.391 20.238  1.00 41.81  ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? -6.435  33.122 19.720  1.00 49.78  ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? -6.474  38.691 23.899  1.00 17.98  ? 6   MET A N   1 
ATOM   43   C  CA  A MET A 1 6   ? -6.416  40.102 24.330  0.50 20.33  ? 6   MET A CA  1 
ATOM   44   C  CA  B MET A 1 6   ? -6.350  40.092 24.339  0.50 20.19  ? 6   MET A CA  1 
ATOM   45   C  C   . MET A 1 6   ? -6.244  41.004 23.113  1.00 19.71  ? 6   MET A C   1 
ATOM   46   O  O   . MET A 1 6   ? -5.285  40.820 22.324  1.00 20.71  ? 6   MET A O   1 
ATOM   47   C  CB  A MET A 1 6   ? -5.289  40.361 25.332  0.50 20.60  ? 6   MET A CB  1 
ATOM   48   C  CB  B MET A 1 6   ? -5.094  40.185 25.209  0.50 19.88  ? 6   MET A CB  1 
ATOM   49   C  CG  A MET A 1 6   ? -5.489  41.706 25.982  0.50 22.63  ? 6   MET A CG  1 
ATOM   50   C  CG  B MET A 1 6   ? -4.813  41.564 25.688  0.50 21.75  ? 6   MET A CG  1 
ATOM   51   S  SD  A MET A 1 6   ? -4.436  42.010 27.395  0.50 24.93  ? 6   MET A SD  1 
ATOM   52   S  SD  B MET A 1 6   ? -3.490  41.627 26.904  0.50 28.49  ? 6   MET A SD  1 
ATOM   53   C  CE  A MET A 1 6   ? -2.817  42.187 26.637  0.50 28.82  ? 6   MET A CE  1 
ATOM   54   C  CE  B MET A 1 6   ? -4.121  40.538 28.172  0.50 21.43  ? 6   MET A CE  1 
ATOM   55   N  N   . ALA A 1 7   ? -7.145  41.951 22.968  1.00 18.20  ? 7   ALA A N   1 
ATOM   56   C  CA  . ALA A 1 7   ? -7.104  42.928 21.875  1.00 17.64  ? 7   ALA A CA  1 
ATOM   57   C  C   . ALA A 1 7   ? -6.360  44.147 22.365  1.00 17.59  ? 7   ALA A C   1 
ATOM   58   O  O   . ALA A 1 7   ? -6.181  44.358 23.588  1.00 17.69  ? 7   ALA A O   1 
ATOM   59   C  CB  . ALA A 1 7   ? -8.484  43.278 21.409  1.00 17.89  ? 7   ALA A CB  1 
ATOM   60   N  N   . PHE A 1 8   ? -5.871  44.972 21.464  1.00 17.04  ? 8   PHE A N   1 
ATOM   61   C  CA  . PHE A 1 8   ? -5.396  46.314 21.849  1.00 17.07  ? 8   PHE A CA  1 
ATOM   62   C  C   . PHE A 1 8   ? -6.571  47.199 22.246  1.00 17.53  ? 8   PHE A C   1 
ATOM   63   O  O   . PHE A 1 8   ? -7.688  47.062 21.795  1.00 17.49  ? 8   PHE A O   1 
ATOM   64   C  CB  . PHE A 1 8   ? -4.625  46.966 20.708  1.00 19.04  ? 8   PHE A CB  1 
ATOM   65   C  CG  . PHE A 1 8   ? -3.262  46.382 20.529  1.00 18.68  ? 8   PHE A CG  1 
ATOM   66   C  CD1 . PHE A 1 8   ? -2.263  46.702 21.426  1.00 21.08  ? 8   PHE A CD1 1 
ATOM   67   C  CD2 . PHE A 1 8   ? -3.011  45.432 19.548  1.00 22.06  ? 8   PHE A CD2 1 
ATOM   68   C  CE1 . PHE A 1 8   ? -0.994  46.175 21.276  1.00 22.51  ? 8   PHE A CE1 1 
ATOM   69   C  CE2 . PHE A 1 8   ? -1.740  44.885 19.414  1.00 21.74  ? 8   PHE A CE2 1 
ATOM   70   C  CZ  . PHE A 1 8   ? -0.747  45.266 20.284  1.00 21.98  ? 8   PHE A CZ  1 
ATOM   71   N  N   . PRO A 1 9   ? -6.336  48.168 23.144  1.00 18.16  ? 9   PRO A N   1 
ATOM   72   C  CA  . PRO A 1 9   ? -7.359  49.139 23.498  1.00 18.12  ? 9   PRO A CA  1 
ATOM   73   C  C   . PRO A 1 9   ? -7.774  49.884 22.236  1.00 18.04  ? 9   PRO A C   1 
ATOM   74   O  O   . PRO A 1 9   ? -6.897  50.228 21.405  1.00 20.66  ? 9   PRO A O   1 
ATOM   75   C  CB  . PRO A 1 9   ? -6.648  50.101 24.467  1.00 18.58  ? 9   PRO A CB  1 
ATOM   76   C  CG  . PRO A 1 9   ? -5.469  49.316 24.984  1.00 21.37  ? 9   PRO A CG  1 
ATOM   77   C  CD  . PRO A 1 9   ? -5.060  48.413 23.830  1.00 21.29  ? 9   PRO A CD  1 
ATOM   78   N  N   . SER A 1 10  ? -9.077  49.984 22.046  1.00 19.59  ? 10  SER A N   1 
ATOM   79   C  CA  . SER A 1 10  ? -9.687  50.417 20.770  1.00 17.92  ? 10  SER A CA  1 
ATOM   80   C  C   . SER A 1 10  ? -9.878  51.940 20.664  1.00 19.04  ? 10  SER A C   1 
ATOM   81   O  O   . SER A 1 10  ? -10.299 52.411 19.571  1.00 19.40  ? 10  SER A O   1 
ATOM   82   C  CB  . SER A 1 10  ? -10.921 49.651 20.513  1.00 18.09  ? 10  SER A CB  1 
ATOM   83   O  OG  . SER A 1 10  ? -11.915 49.865 21.502  1.00 19.90  ? 10  SER A OG  1 
ATOM   84   N  N   . GLY A 1 11  ? -9.656  52.714 21.727  1.00 19.13  ? 11  GLY A N   1 
ATOM   85   C  CA  . GLY A 1 11  ? -10.121 54.120 21.683  1.00 20.19  ? 11  GLY A CA  1 
ATOM   86   C  C   . GLY A 1 11  ? -9.563  54.900 20.498  1.00 19.13  ? 11  GLY A C   1 
ATOM   87   O  O   . GLY A 1 11  ? -10.322 55.718 19.928  1.00 21.19  ? 11  GLY A O   1 
ATOM   88   N  N   . LYS A 1 12  ? -8.289  54.728 20.194  1.00 19.65  ? 12  LYS A N   1 
ATOM   89   C  CA  . LYS A 1 12  ? -7.664  55.559 19.137  1.00 20.64  ? 12  LYS A CA  1 
ATOM   90   C  C   . LYS A 1 12  ? -8.365  55.300 17.812  1.00 22.26  ? 12  LYS A C   1 
ATOM   91   O  O   . LYS A 1 12  ? -8.387  56.224 16.989  1.00 22.68  ? 12  LYS A O   1 
ATOM   92   C  CB  . LYS A 1 12  ? -6.173  55.296 19.031  1.00 21.76  ? 12  LYS A CB  1 
ATOM   93   C  CG  . LYS A 1 12  ? -5.353  55.895 20.160  1.00 25.29  ? 12  LYS A CG  1 
ATOM   94   C  CD  . LYS A 1 12  ? -3.891  55.545 20.052  1.00 26.62  ? 12  LYS A CD  1 
ATOM   95   C  CE  . LYS A 1 12  ? -3.064  56.373 21.021  1.00 33.48  ? 12  LYS A CE  1 
ATOM   96   N  NZ  . LYS A 1 12  ? -3.516  56.122 22.406  1.00 38.70  ? 12  LYS A NZ  1 
ATOM   97   N  N   . VAL A 1 13  ? -8.864  54.093 17.592  1.00 19.14  ? 13  VAL A N   1 
ATOM   98   C  CA  . VAL A 1 13  ? -9.558  53.732 16.345  1.00 19.41  ? 13  VAL A CA  1 
ATOM   99   C  C   . VAL A 1 13  ? -11.005 54.216 16.405  1.00 17.79  ? 13  VAL A C   1 
ATOM   100  O  O   . VAL A 1 13  ? -11.569 54.638 15.384  1.00 19.95  ? 13  VAL A O   1 
ATOM   101  C  CB  . VAL A 1 13  ? -9.405  52.220 16.065  1.00 18.45  ? 13  VAL A CB  1 
ATOM   102  C  CG1 . VAL A 1 13  ? -10.113 51.819 14.788  1.00 19.46  ? 13  VAL A CG1 1 
ATOM   103  C  CG2 . VAL A 1 13  ? -7.938  51.905 15.948  1.00 19.64  ? 13  VAL A CG2 1 
ATOM   104  N  N   . GLU A 1 14  ? -11.683 54.090 17.560  1.00 19.24  ? 14  GLU A N   1 
ATOM   105  C  CA  . GLU A 1 14  ? -13.098 54.478 17.687  1.00 18.29  ? 14  GLU A CA  1 
ATOM   106  C  C   . GLU A 1 14  ? -13.263 55.936 17.203  1.00 19.38  ? 14  GLU A C   1 
ATOM   107  O  O   . GLU A 1 14  ? -14.260 56.230 16.566  1.00 21.77  ? 14  GLU A O   1 
ATOM   108  C  CB  . GLU A 1 14  ? -13.576 54.395 19.139  1.00 19.78  ? 14  GLU A CB  1 
ATOM   109  C  CG  . GLU A 1 14  ? -13.600 52.972 19.714  1.00 19.58  ? 14  GLU A CG  1 
ATOM   110  C  CD  . GLU A 1 14  ? -13.787 52.894 21.239  1.00 21.03  ? 14  GLU A CD  1 
ATOM   111  O  OE1 . GLU A 1 14  ? -14.651 53.595 21.725  1.00 24.06  ? 14  GLU A OE1 1 
ATOM   112  O  OE2 . GLU A 1 14  ? -13.023 52.170 21.905  1.00 21.20  ? 14  GLU A OE2 1 
ATOM   113  N  N   . GLY A 1 15  ? -12.313 56.786 17.483  1.00 21.34  ? 15  GLY A N   1 
ATOM   114  C  CA  . GLY A 1 15  ? -12.417 58.220 17.141  1.00 22.40  ? 15  GLY A CA  1 
ATOM   115  C  C   . GLY A 1 15  ? -12.243 58.450 15.647  1.00 24.37  ? 15  GLY A C   1 
ATOM   116  O  O   . GLY A 1 15  ? -12.420 59.584 15.177  1.00 22.86  ? 15  GLY A O   1 
ATOM   117  N  N   . CYS A 1 16  ? -11.928 57.397 14.893  1.00 21.25  ? 16  CYS A N   1 
ATOM   118  C  CA  . CYS A 1 16  ? -11.745 57.480 13.415  1.00 22.14  ? 16  CYS A CA  1 
ATOM   119  C  C   . CYS A 1 16  ? -12.935 56.919 12.669  1.00 20.92  ? 16  CYS A C   1 
ATOM   120  O  O   . CYS A 1 16  ? -12.920 57.060 11.419  1.00 22.84  ? 16  CYS A O   1 
ATOM   121  C  CB  . CYS A 1 16  ? -10.482 56.746 12.960  1.00 18.89  ? 16  CYS A CB  1 
ATOM   122  S  SG  . CYS A 1 16  ? -9.016  57.382 13.756  1.00 24.26  ? 16  CYS A SG  1 
ATOM   123  N  N   . MET A 1 17  ? -13.955 56.337 13.316  1.00 20.04  ? 17  MET A N   1 
ATOM   124  C  CA  . MET A 1 17  ? -14.981 55.582 12.584  1.00 21.54  ? 17  MET A CA  1 
ATOM   125  C  C   . MET A 1 17  ? -16.097 56.552 12.199  1.00 22.38  ? 17  MET A C   1 
ATOM   126  O  O   . MET A 1 17  ? -16.528 57.370 13.079  1.00 23.39  ? 17  MET A O   1 
ATOM   127  C  CB  . MET A 1 17  ? -15.538 54.384 13.364  1.00 20.98  ? 17  MET A CB  1 
ATOM   128  C  CG  . MET A 1 17  ? -14.518 53.358 13.727  1.00 20.28  ? 17  MET A CG  1 
ATOM   129  S  SD  . MET A 1 17  ? -13.479 52.804 12.344  1.00 21.91  ? 17  MET A SD  1 
ATOM   130  C  CE  . MET A 1 17  ? -14.674 52.131 11.214  1.00 22.74  ? 17  MET A CE  1 
ATOM   131  N  N   . VAL A 1 18  ? -16.499 56.501 10.943  1.00 24.62  ? 18  VAL A N   1 
ATOM   132  C  CA  . VAL A 1 18  ? -17.594 57.330 10.376  1.00 23.74  ? 18  VAL A CA  1 
ATOM   133  C  C   . VAL A 1 18  ? -18.496 56.433 9.548   1.00 24.61  ? 18  VAL A C   1 
ATOM   134  O  O   . VAL A 1 18  ? -18.174 55.250 9.248   1.00 21.52  ? 18  VAL A O   1 
ATOM   135  C  CB  . VAL A 1 18  ? -17.045 58.484 9.526   1.00 22.96  ? 18  VAL A CB  1 
ATOM   136  C  CG1 . VAL A 1 18  ? -16.114 59.380 10.309  1.00 23.19  ? 18  VAL A CG1 1 
ATOM   137  C  CG2 . VAL A 1 18  ? -16.334 57.962 8.299   1.00 25.93  ? 18  VAL A CG2 1 
ATOM   138  N  N   . GLN A 1 19  ? -19.638 56.974 9.166   1.00 24.77  ? 19  GLN A N   1 
ATOM   139  C  CA  . GLN A 1 19  ? -20.632 56.292 8.332   1.00 25.39  ? 19  GLN A CA  1 
ATOM   140  C  C   . GLN A 1 19  ? -20.534 56.843 6.912   1.00 25.18  ? 19  GLN A C   1 
ATOM   141  O  O   . GLN A 1 19  ? -20.439 58.058 6.777   1.00 27.20  ? 19  GLN A O   1 
ATOM   142  C  CB  . GLN A 1 19  ? -22.037 56.583 8.849   1.00 26.79  ? 19  GLN A CB  1 
ATOM   143  C  CG  . GLN A 1 19  ? -23.078 55.659 8.265   1.00 31.64  ? 19  GLN A CG  1 
ATOM   144  C  CD  . GLN A 1 19  ? -24.421 56.019 8.845   1.00 37.05  ? 19  GLN A CD  1 
ATOM   145  O  OE1 . GLN A 1 19  ? -24.765 57.201 8.928   1.00 45.35  ? 19  GLN A OE1 1 
ATOM   146  N  NE2 . GLN A 1 19  ? -25.173 55.005 9.248   1.00 40.99  ? 19  GLN A NE2 1 
ATOM   147  N  N   . VAL A 1 20  ? -20.544 55.966 5.925   1.00 26.26  ? 20  VAL A N   1 
ATOM   148  C  CA  . VAL A 1 20  ? -20.511 56.356 4.493   1.00 26.20  ? 20  VAL A CA  1 
ATOM   149  C  C   . VAL A 1 20  ? -21.728 55.767 3.798   1.00 28.79  ? 20  VAL A C   1 
ATOM   150  O  O   . VAL A 1 20  ? -21.938 54.563 3.808   1.00 24.76  ? 20  VAL A O   1 
ATOM   151  C  CB  . VAL A 1 20  ? -19.209 55.953 3.787   1.00 23.10  ? 20  VAL A CB  1 
ATOM   152  C  CG1 . VAL A 1 20  ? -19.236 56.513 2.392   1.00 24.07  ? 20  VAL A CG1 1 
ATOM   153  C  CG2 . VAL A 1 20  ? -17.992 56.398 4.553   1.00 22.78  ? 20  VAL A CG2 1 
ATOM   154  N  N   . THR A 1 21  ? -22.483 56.630 3.106   1.00 26.88  ? 21  THR A N   1 
ATOM   155  C  CA  . THR A 1 21  ? -23.668 56.247 2.325   1.00 29.01  ? 21  THR A CA  1 
ATOM   156  C  C   . THR A 1 21  ? -23.536 56.785 0.900   1.00 27.06  ? 21  THR A C   1 
ATOM   157  O  O   . THR A 1 21  ? -23.169 57.967 0.715   1.00 33.28  ? 21  THR A O   1 
ATOM   158  C  CB  . THR A 1 21  ? -24.966 56.814 2.935   1.00 29.84  ? 21  THR A CB  1 
ATOM   159  O  OG1 . THR A 1 21  ? -24.963 56.429 4.312   1.00 29.68  ? 21  THR A OG1 1 
ATOM   160  C  CG2 . THR A 1 21  ? -26.207 56.315 2.228   1.00 32.86  ? 21  THR A CG2 1 
ATOM   161  N  N   . CYS A 1 22  ? -23.892 55.928 -0.039  1.00 30.99  ? 22  CYS A N   1 
ATOM   162  C  CA  . CYS A 1 22  ? -23.982 56.160 -1.492  1.00 33.32  ? 22  CYS A CA  1 
ATOM   163  C  C   . CYS A 1 22  ? -25.313 55.536 -1.884  1.00 34.61  ? 22  CYS A C   1 
ATOM   164  O  O   . CYS A 1 22  ? -25.476 54.291 -1.825  1.00 38.58  ? 22  CYS A O   1 
ATOM   165  C  CB  . CYS A 1 22  ? -22.753 55.607 -2.215  1.00 36.09  ? 22  CYS A CB  1 
ATOM   166  S  SG  . CYS A 1 22  ? -22.571 56.322 -3.856  1.00 52.55  ? 22  CYS A SG  1 
ATOM   167  N  N   . GLY A 1 23  ? -26.310 56.374 -2.155  1.00 36.42  ? 23  GLY A N   1 
ATOM   168  C  CA  . GLY A 1 23  ? -27.664 55.869 -2.425  1.00 37.32  ? 23  GLY A CA  1 
ATOM   169  C  C   . GLY A 1 23  ? -28.215 55.137 -1.233  1.00 30.29  ? 23  GLY A C   1 
ATOM   170  O  O   . GLY A 1 23  ? -28.306 55.708 -0.174  1.00 39.29  ? 23  GLY A O   1 
ATOM   171  N  N   . THR A 1 24  ? -28.602 53.889 -1.421  1.00 34.72  ? 24  THR A N   1 
ATOM   172  C  CA  . THR A 1 24  ? -29.289 53.064 -0.406  1.00 36.83  ? 24  THR A CA  1 
ATOM   173  C  C   . THR A 1 24  ? -28.257 52.200 0.363   1.00 36.41  ? 24  THR A C   1 
ATOM   174  O  O   . THR A 1 24  ? -28.666 51.492 1.268   1.00 35.80  ? 24  THR A O   1 
ATOM   175  C  CB  . THR A 1 24  ? -30.404 52.277 -1.109  1.00 41.91  ? 24  THR A CB  1 
ATOM   176  O  OG1 . THR A 1 24  ? -31.256 51.786 -0.082  1.00 59.06  ? 24  THR A OG1 1 
ATOM   177  C  CG2 . THR A 1 24  ? -29.942 51.125 -1.972  1.00 41.71  ? 24  THR A CG2 1 
ATOM   178  N  N   . THR A 1 25  ? -26.966 52.293 0.035   1.00 32.75  ? 25  THR A N   1 
ATOM   179  C  CA  . THR A 1 25  ? -25.891 51.447 0.637   1.00 31.59  ? 25  THR A CA  1 
ATOM   180  C  C   . THR A 1 25  ? -25.181 52.251 1.723   1.00 28.36  ? 25  THR A C   1 
ATOM   181  O  O   . THR A 1 25  ? -24.646 53.327 1.409   1.00 29.93  ? 25  THR A O   1 
ATOM   182  C  CB  . THR A 1 25  ? -24.951 50.948 -0.462  1.00 36.67  ? 25  THR A CB  1 
ATOM   183  O  OG1 . THR A 1 25  ? -25.776 50.202 -1.355  1.00 42.69  ? 25  THR A OG1 1 
ATOM   184  C  CG2 . THR A 1 25  ? -23.815 50.095 0.055   1.00 38.92  ? 25  THR A CG2 1 
ATOM   185  N  N   . THR A 1 26  ? -25.153 51.732 2.966   1.00 27.22  ? 26  THR A N   1 
ATOM   186  C  CA  . THR A 1 26  ? -24.425 52.364 4.083   1.00 29.79  ? 26  THR A CA  1 
ATOM   187  C  C   . THR A 1 26  ? -23.389 51.354 4.607   1.00 26.81  ? 26  THR A C   1 
ATOM   188  O  O   . THR A 1 26  ? -23.707 50.189 4.713   1.00 29.27  ? 26  THR A O   1 
ATOM   189  C  CB  . THR A 1 26  ? -25.363 52.837 5.190   1.00 33.50  ? 26  THR A CB  1 
ATOM   190  O  OG1 . THR A 1 26  ? -26.174 53.882 4.634   1.00 35.91  ? 26  THR A OG1 1 
ATOM   191  C  CG2 . THR A 1 26  ? -24.621 53.381 6.383   1.00 34.50  ? 26  THR A CG2 1 
ATOM   192  N  N   . LEU A 1 27  ? -22.182 51.812 4.800   1.00 25.38  ? 27  LEU A N   1 
ATOM   193  C  CA  . LEU A 1 27  ? -21.167 50.997 5.516   1.00 22.87  ? 27  LEU A CA  1 
ATOM   194  C  C   . LEU A 1 27  ? -20.249 51.943 6.272   1.00 21.87  ? 27  LEU A C   1 
ATOM   195  O  O   . LEU A 1 27  ? -20.595 53.141 6.456   1.00 24.45  ? 27  LEU A O   1 
ATOM   196  C  CB  . LEU A 1 27  ? -20.469 50.083 4.497   1.00 23.75  ? 27  LEU A CB  1 
ATOM   197  C  CG  . LEU A 1 27  ? -19.938 50.680 3.196   1.00 21.72  ? 27  LEU A CG  1 
ATOM   198  C  CD1 . LEU A 1 27  ? -18.990 51.847 3.428   1.00 22.39  ? 27  LEU A CD1 1 
ATOM   199  C  CD2 . LEU A 1 27  ? -19.282 49.584 2.338   1.00 24.61  ? 27  LEU A CD2 1 
ATOM   200  N  N   . ASN A 1 28  ? -19.154 51.413 6.837   1.00 19.03  ? 28  ASN A N   1 
ATOM   201  C  CA  . ASN A 1 28  ? -18.272 52.171 7.715   1.00 18.31  ? 28  ASN A CA  1 
ATOM   202  C  C   . ASN A 1 28  ? -17.090 52.716 6.910   1.00 18.74  ? 28  ASN A C   1 
ATOM   203  O  O   . ASN A 1 28  ? -16.696 52.040 5.932   1.00 21.72  ? 28  ASN A O   1 
ATOM   204  C  CB  . ASN A 1 28  ? -17.709 51.235 8.799   1.00 17.66  ? 28  ASN A CB  1 
ATOM   205  C  CG  . ASN A 1 28  ? -18.817 50.568 9.575   1.00 19.96  ? 28  ASN A CG  1 
ATOM   206  O  OD1 . ASN A 1 28  ? -19.463 51.232 10.386  1.00 19.76  ? 28  ASN A OD1 1 
ATOM   207  N  ND2 . ASN A 1 28  ? -19.111 49.308 9.281   1.00 19.34  ? 28  ASN A ND2 1 
ATOM   208  N  N   . GLY A 1 29  ? -16.572 53.853 7.355   1.00 19.58  ? 29  GLY A N   1 
ATOM   209  C  CA  . GLY A 1 29  ? -15.350 54.476 6.880   1.00 18.45  ? 29  GLY A CA  1 
ATOM   210  C  C   . GLY A 1 29  ? -14.400 54.777 7.991   1.00 19.43  ? 29  GLY A C   1 
ATOM   211  O  O   . GLY A 1 29  ? -14.807 54.830 9.158   1.00 19.49  ? 29  GLY A O   1 
ATOM   212  N  N   . LEU A 1 30  ? -13.156 55.019 7.604   1.00 19.10  ? 30  LEU A N   1 
ATOM   213  C  CA  . LEU A 1 30  ? -12.039 55.328 8.490   1.00 20.39  ? 30  LEU A CA  1 
ATOM   214  C  C   . LEU A 1 30  ? -11.576 56.726 8.137   1.00 21.13  ? 30  LEU A C   1 
ATOM   215  O  O   . LEU A 1 30  ? -11.119 56.937 6.999   1.00 19.46  ? 30  LEU A O   1 
ATOM   216  C  CB  . LEU A 1 30  ? -10.913 54.294 8.314   1.00 18.08  ? 30  LEU A CB  1 
ATOM   217  C  CG  . LEU A 1 30  ? -9.762  54.470 9.270   1.00 18.17  ? 30  LEU A CG  1 
ATOM   218  C  CD1 . LEU A 1 30  ? -10.181 54.070 10.670  1.00 19.62  ? 30  LEU A CD1 1 
ATOM   219  C  CD2 . LEU A 1 30  ? -8.539  53.678 8.811   1.00 19.06  ? 30  LEU A CD2 1 
ATOM   220  N  N   . TRP A 1 31  ? -11.728 57.647 9.087   1.00 21.35  ? 31  TRP A N   1 
ATOM   221  C  CA  . TRP A 1 31  ? -11.451 59.089 8.892   1.00 20.54  ? 31  TRP A CA  1 
ATOM   222  C  C   . TRP A 1 31  ? -10.118 59.443 9.517   1.00 20.66  ? 31  TRP A C   1 
ATOM   223  O  O   . TRP A 1 31  ? -9.997  59.409 10.744  1.00 22.47  ? 31  TRP A O   1 
ATOM   224  C  CB  . TRP A 1 31  ? -12.614 59.873 9.475   1.00 22.75  ? 31  TRP A CB  1 
ATOM   225  C  CG  . TRP A 1 31  ? -12.500 61.348 9.329   1.00 24.80  ? 31  TRP A CG  1 
ATOM   226  C  CD1 . TRP A 1 31  ? -11.843 62.045 8.352   1.00 28.58  ? 31  TRP A CD1 1 
ATOM   227  C  CD2 . TRP A 1 31  ? -13.122 62.324 10.177  1.00 27.48  ? 31  TRP A CD2 1 
ATOM   228  N  NE1 . TRP A 1 31  ? -12.004 63.394 8.556   1.00 29.33  ? 31  TRP A NE1 1 
ATOM   229  C  CE2 . TRP A 1 31  ? -12.819 63.594 9.637   1.00 28.99  ? 31  TRP A CE2 1 
ATOM   230  C  CE3 . TRP A 1 31  ? -13.937 62.233 11.314  1.00 30.49  ? 31  TRP A CE3 1 
ATOM   231  C  CZ2 . TRP A 1 31  ? -13.255 64.778 10.249  1.00 29.49  ? 31  TRP A CZ2 1 
ATOM   232  C  CZ3 . TRP A 1 31  ? -14.370 63.404 11.909  1.00 31.37  ? 31  TRP A CZ3 1 
ATOM   233  C  CH2 . TRP A 1 31  ? -14.025 64.649 11.382  1.00 29.60  ? 31  TRP A CH2 1 
ATOM   234  N  N   . LEU A 1 32  ? -9.098  59.661 8.693   1.00 19.98  ? 32  LEU A N   1 
ATOM   235  C  CA  . LEU A 1 32  ? -7.737  59.968 9.115   1.00 21.78  ? 32  LEU A CA  1 
ATOM   236  C  C   . LEU A 1 32  ? -7.323  61.262 8.414   1.00 24.26  ? 32  LEU A C   1 
ATOM   237  O  O   . LEU A 1 32  ? -7.441  61.325 7.185   1.00 24.60  ? 32  LEU A O   1 
ATOM   238  C  CB  . LEU A 1 32  ? -6.796  58.820 8.751   1.00 23.90  ? 32  LEU A CB  1 
ATOM   239  C  CG  . LEU A 1 32  ? -7.062  57.502 9.463   1.00 23.92  ? 32  LEU A CG  1 
ATOM   240  C  CD1 . LEU A 1 32  ? -6.285  56.403 8.785   1.00 23.58  ? 32  LEU A CD1 1 
ATOM   241  C  CD2 . LEU A 1 32  ? -6.685  57.587 10.932  1.00 23.32  ? 32  LEU A CD2 1 
ATOM   242  N  N   . ASP A 1 33  ? -6.877  62.261 9.177   1.00 23.34  ? 33  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 33  ? -6.619  63.599 8.576   1.00 26.95  ? 33  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 33  ? -7.853  63.958 7.755   1.00 26.88  ? 33  ASP A C   1 
ATOM   245  O  O   . ASP A 1 33  ? -8.965  63.789 8.253   1.00 25.10  ? 33  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 33  ? -5.304  63.563 7.796   1.00 29.26  ? 33  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 33  ? -4.125  63.200 8.666   1.00 34.55  ? 33  ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 33  ? -4.049  63.738 9.780   1.00 39.53  ? 33  ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 33  ? -3.280  62.415 8.207   1.00 39.95  ? 33  ASP A OD2 1 
ATOM   250  N  N   . ASP A 1 34  ? -7.710  64.455 6.516   1.00 27.42  ? 34  ASP A N   1 
ATOM   251  C  CA  . ASP A 1 34  ? -8.871  64.909 5.725   1.00 26.67  ? 34  ASP A CA  1 
ATOM   252  C  C   . ASP A 1 34  ? -9.292  63.851 4.703   1.00 26.79  ? 34  ASP A C   1 
ATOM   253  O  O   . ASP A 1 34  ? -9.859  64.201 3.676   1.00 26.94  ? 34  ASP A O   1 
ATOM   254  C  CB  . ASP A 1 34  ? -8.574  66.272 5.077   1.00 31.05  ? 34  ASP A CB  1 
ATOM   255  C  CG  . ASP A 1 34  ? -7.410  66.264 4.094   1.00 36.72  ? 34  ASP A CG  1 
ATOM   256  O  OD1 . ASP A 1 34  ? -6.629  65.281 4.091   1.00 32.58  ? 34  ASP A OD1 1 
ATOM   257  O  OD2 . ASP A 1 34  ? -7.311  67.232 3.278   1.00 40.81  ? 34  ASP A OD2 1 
ATOM   258  N  N   . VAL A 1 35  ? -9.078  62.562 4.962   1.00 24.73  ? 35  VAL A N   1 
ATOM   259  C  CA  . VAL A 1 35  ? -9.505  61.470 4.037   1.00 23.07  ? 35  VAL A CA  1 
ATOM   260  C  C   . VAL A 1 35  ? -10.348 60.481 4.823   1.00 22.94  ? 35  VAL A C   1 
ATOM   261  O  O   . VAL A 1 35  ? -9.944  60.111 5.954   1.00 22.18  ? 35  VAL A O   1 
ATOM   262  C  CB  . VAL A 1 35  ? -8.321  60.748 3.367   1.00 25.93  ? 35  VAL A CB  1 
ATOM   263  C  CG1 . VAL A 1 35  ? -8.781  59.611 2.453   1.00 26.60  ? 35  VAL A CG1 1 
ATOM   264  C  CG2 . VAL A 1 35  ? -7.433  61.752 2.642   1.00 27.06  ? 35  VAL A CG2 1 
ATOM   265  N  N   . VAL A 1 36  ? -11.392 59.992 4.159   1.00 22.11  ? 36  VAL A N   1 
ATOM   266  C  CA  . VAL A 1 36  ? -12.232 58.867 4.624   1.00 24.22  ? 36  VAL A CA  1 
ATOM   267  C  C   . VAL A 1 36  ? -11.974 57.694 3.685   1.00 24.20  ? 36  VAL A C   1 
ATOM   268  O  O   . VAL A 1 36  ? -12.147 57.833 2.439   1.00 22.83  ? 36  VAL A O   1 
ATOM   269  C  CB  . VAL A 1 36  ? -13.711 59.233 4.686   1.00 24.59  ? 36  VAL A CB  1 
ATOM   270  C  CG1 . VAL A 1 36  ? -14.594 58.054 5.020   1.00 22.91  ? 36  VAL A CG1 1 
ATOM   271  C  CG2 . VAL A 1 36  ? -13.914 60.333 5.706   1.00 24.45  ? 36  VAL A CG2 1 
ATOM   272  N  N   . TYR A 1 37  ? -11.504 56.593 4.263   1.00 20.95  ? 37  TYR A N   1 
ATOM   273  C  CA  . TYR A 1 37  ? -11.243 55.323 3.531   1.00 20.11  ? 37  TYR A CA  1 
ATOM   274  C  C   . TYR A 1 37  ? -12.408 54.385 3.755   1.00 19.75  ? 37  TYR A C   1 
ATOM   275  O  O   . TYR A 1 37  ? -12.771 54.201 4.915   1.00 21.60  ? 37  TYR A O   1 
ATOM   276  C  CB  . TYR A 1 37  ? -9.968  54.648 4.047   1.00 19.98  ? 37  TYR A CB  1 
ATOM   277  C  CG  . TYR A 1 37  ? -8.769  55.533 3.961   1.00 19.68  ? 37  TYR A CG  1 
ATOM   278  C  CD1 . TYR A 1 37  ? -8.519  56.500 4.905   1.00 19.76  ? 37  TYR A CD1 1 
ATOM   279  C  CD2 . TYR A 1 37  ? -7.858  55.405 2.923   1.00 20.78  ? 37  TYR A CD2 1 
ATOM   280  C  CE1 . TYR A 1 37  ? -7.433  57.333 4.837   1.00 19.66  ? 37  TYR A CE1 1 
ATOM   281  C  CE2 . TYR A 1 37  ? -6.755  56.235 2.840   1.00 19.90  ? 37  TYR A CE2 1 
ATOM   282  C  CZ  . TYR A 1 37  ? -6.553  57.219 3.781   1.00 21.20  ? 37  TYR A CZ  1 
ATOM   283  O  OH  . TYR A 1 37  ? -5.511  58.084 3.728   1.00 26.08  ? 37  TYR A OH  1 
ATOM   284  N  N   . CYS A 1 38  ? -12.961 53.813 2.692   1.00 18.19  ? 38  CYS A N   1 
ATOM   285  C  CA  . CYS A 1 38  ? -14.022 52.813 2.764   1.00 19.10  ? 38  CYS A CA  1 
ATOM   286  C  C   . CYS A 1 38  ? -13.956 51.828 1.608   1.00 17.84  ? 38  CYS A C   1 
ATOM   287  O  O   . CYS A 1 38  ? -13.230 52.049 0.622   1.00 18.61  ? 38  CYS A O   1 
ATOM   288  C  CB  . CYS A 1 38  ? -15.390 53.469 2.881   1.00 19.56  ? 38  CYS A CB  1 
ATOM   289  S  SG  . CYS A 1 38  ? -15.935 54.214 1.321   1.00 24.29  ? 38  CYS A SG  1 
ATOM   290  N  N   . PRO A 1 39  ? -14.654 50.679 1.717   1.00 18.16  ? 39  PRO A N   1 
ATOM   291  C  CA  . PRO A 1 39  ? -14.723 49.709 0.624   1.00 18.39  ? 39  PRO A CA  1 
ATOM   292  C  C   . PRO A 1 39  ? -15.357 50.370 -0.598  1.00 18.45  ? 39  PRO A C   1 
ATOM   293  O  O   . PRO A 1 39  ? -16.387 51.045 -0.460  1.00 19.12  ? 39  PRO A O   1 
ATOM   294  C  CB  . PRO A 1 39  ? -15.553 48.558 1.188   1.00 17.80  ? 39  PRO A CB  1 
ATOM   295  C  CG  . PRO A 1 39  ? -15.360 48.695 2.661   1.00 17.84  ? 39  PRO A CG  1 
ATOM   296  C  CD  . PRO A 1 39  ? -15.359 50.184 2.911   1.00 19.57  ? 39  PRO A CD  1 
ATOM   297  N  N   . ARG A 1 40  ? -14.740 50.174 -1.739  1.00 18.05  ? 40  ARG A N   1 
ATOM   298  C  CA  . ARG A 1 40  ? -15.324 50.727 -2.985  1.00 19.03  ? 40  ARG A CA  1 
ATOM   299  C  C   . ARG A 1 40  ? -16.691 50.095 -3.263  1.00 20.31  ? 40  ARG A C   1 
ATOM   300  O  O   . ARG A 1 40  ? -17.451 50.720 -4.031  1.00 20.49  ? 40  ARG A O   1 
ATOM   301  C  CB  . ARG A 1 40  ? -14.348 50.595 -4.149  1.00 17.15  ? 40  ARG A CB  1 
ATOM   302  C  CG  . ARG A 1 40  ? -14.200 49.177 -4.659  1.00 17.22  ? 40  ARG A CG  1 
ATOM   303  C  CD  . ARG A 1 40  ? -13.234 49.139 -5.804  1.00 18.42  ? 40  ARG A CD  1 
ATOM   304  N  NE  . ARG A 1 40  ? -12.994 47.783 -6.178  1.00 18.46  ? 40  ARG A NE  1 
ATOM   305  C  CZ  . ARG A 1 40  ? -12.348 47.413 -7.285  1.00 20.94  ? 40  ARG A CZ  1 
ATOM   306  N  NH1 . ARG A 1 40  ? -11.897 48.329 -8.130  1.00 22.82  ? 40  ARG A NH1 1 
ATOM   307  N  NH2 . ARG A 1 40  ? -12.226 46.148 -7.592  1.00 20.81  ? 40  ARG A NH2 1 
ATOM   308  N  N   . HIS A 1 41  ? -17.050 48.933 -2.731  1.00 20.28  ? 41  HIS A N   1 
ATOM   309  C  CA  . HIS A 1 41  ? -18.348 48.283 -3.048  1.00 20.44  ? 41  HIS A CA  1 
ATOM   310  C  C   . HIS A 1 41  ? -19.509 49.122 -2.514  1.00 20.68  ? 41  HIS A C   1 
ATOM   311  O  O   . HIS A 1 41  ? -20.639 48.777 -2.832  1.00 24.45  ? 41  HIS A O   1 
ATOM   312  C  CB  . HIS A 1 41  ? -18.434 46.809 -2.627  1.00 21.08  ? 41  HIS A CB  1 
ATOM   313  C  CG  . HIS A 1 41  ? -18.398 46.537 -1.152  1.00 21.84  ? 41  HIS A CG  1 
ATOM   314  N  ND1 . HIS A 1 41  ? -19.449 46.808 -0.316  1.00 23.90  ? 41  HIS A ND1 1 
ATOM   315  C  CD2 . HIS A 1 41  ? -17.504 45.834 -0.413  1.00 22.87  ? 41  HIS A CD2 1 
ATOM   316  C  CE1 . HIS A 1 41  ? -19.167 46.393 0.924   1.00 23.11  ? 41  HIS A CE1 1 
ATOM   317  N  NE2 . HIS A 1 41  ? -17.981 45.775 0.884   1.00 24.84  ? 41  HIS A NE2 1 
ATOM   318  N  N   . VAL A 1 42  ? -19.237 50.195 -1.809  1.00 21.85  ? 42  VAL A N   1 
ATOM   319  C  CA  . VAL A 1 42  ? -20.314 51.130 -1.350  1.00 24.31  ? 42  VAL A CA  1 
ATOM   320  C  C   . VAL A 1 42  ? -20.981 51.726 -2.606  1.00 27.63  ? 42  VAL A C   1 
ATOM   321  O  O   . VAL A 1 42  ? -22.166 52.117 -2.497  1.00 26.93  ? 42  VAL A O   1 
ATOM   322  C  CB  . VAL A 1 42  ? -19.798 52.254 -0.449  1.00 24.62  ? 42  VAL A CB  1 
ATOM   323  C  CG1 . VAL A 1 42  ? -18.969 53.281 -1.162  1.00 23.23  ? 42  VAL A CG1 1 
ATOM   324  C  CG2 . VAL A 1 42  ? -20.929 52.901 0.343   1.00 24.28  ? 42  VAL A CG2 1 
ATOM   325  N  N   . ILE A 1 43  ? -20.299 51.723 -3.750  1.00 23.97  ? 43  ILE A N   1 
ATOM   326  C  CA  . ILE A 1 43  ? -20.881 52.285 -5.022  1.00 26.86  ? 43  ILE A CA  1 
ATOM   327  C  C   . ILE A 1 43  ? -21.609 51.233 -5.845  1.00 33.59  ? 43  ILE A C   1 
ATOM   328  O  O   . ILE A 1 43  ? -22.112 51.601 -6.949  1.00 35.50  ? 43  ILE A O   1 
ATOM   329  C  CB  . ILE A 1 43  ? -19.840 53.020 -5.884  1.00 23.94  ? 43  ILE A CB  1 
ATOM   330  C  CG1 . ILE A 1 43  ? -18.836 52.089 -6.564  1.00 25.48  ? 43  ILE A CG1 1 
ATOM   331  C  CG2 . ILE A 1 43  ? -19.199 54.119 -5.076  1.00 22.88  ? 43  ILE A CG2 1 
ATOM   332  C  CD1 . ILE A 1 43  ? -17.809 52.793 -7.426  1.00 26.02  ? 43  ILE A CD1 1 
ATOM   333  N  N   . CYS A 1 44  ? -21.707 49.999 -5.377  1.00 34.05  ? 44  CYS A N   1 
ATOM   334  C  CA  A CYS A 1 44  ? -22.400 48.887 -6.096  0.50 36.62  ? 44  CYS A CA  1 
ATOM   335  C  CA  B CYS A 1 44  ? -22.429 48.935 -6.104  0.50 38.32  ? 44  CYS A CA  1 
ATOM   336  C  C   . CYS A 1 44  ? -23.901 49.001 -5.744  1.00 40.00  ? 44  CYS A C   1 
ATOM   337  O  O   . CYS A 1 44  ? -24.211 49.429 -4.618  1.00 49.39  ? 44  CYS A O   1 
ATOM   338  C  CB  A CYS A 1 44  ? -21.750 47.534 -5.749  0.50 33.54  ? 44  CYS A CB  1 
ATOM   339  C  CB  B CYS A 1 44  ? -21.850 47.576 -5.781  0.50 37.43  ? 44  CYS A CB  1 
ATOM   340  S  SG  A CYS A 1 44  ? -21.809 46.209 -7.005  0.50 32.67  ? 44  CYS A SG  1 
ATOM   341  S  SG  B CYS A 1 44  ? -20.320 47.392 -6.703  0.50 40.00  ? 44  CYS A SG  1 
ATOM   342  N  N   . THR A 1 45  ? -24.774 48.691 -6.698  1.00 48.91  ? 45  THR A N   1 
ATOM   343  C  CA  . THR A 1 45  ? -26.216 48.475 -6.416  1.00 56.06  ? 45  THR A CA  1 
ATOM   344  C  C   . THR A 1 45  ? -26.473 46.986 -6.571  1.00 61.61  ? 45  THR A C   1 
ATOM   345  O  O   . THR A 1 45  ? -25.602 46.312 -7.177  1.00 45.18  ? 45  THR A O   1 
ATOM   346  C  CB  . THR A 1 45  ? -27.147 49.203 -7.386  1.00 58.80  ? 45  THR A CB  1 
ATOM   347  O  OG1 . THR A 1 45  ? -26.885 48.595 -8.652  1.00 55.49  ? 45  THR A OG1 1 
ATOM   348  C  CG2 . THR A 1 45  ? -26.932 50.702 -7.429  1.00 57.12  ? 45  THR A CG2 1 
ATOM   349  N  N   . SER A 1 46  ? -27.649 46.537 -6.130  1.00 71.91  ? 46  SER A N   1 
ATOM   350  C  CA  . SER A 1 46  ? -28.098 45.121 -6.189  1.00 81.40  ? 46  SER A CA  1 
ATOM   351  C  C   . SER A 1 46  ? -27.888 44.550 -7.598  1.00 83.53  ? 46  SER A C   1 
ATOM   352  O  O   . SER A 1 46  ? -27.539 43.354 -7.687  1.00 91.51  ? 46  SER A O   1 
ATOM   353  C  CB  . SER A 1 46  ? -29.530 44.993 -5.741  1.00 86.81  ? 46  SER A CB  1 
ATOM   354  O  OG  . SER A 1 46  ? -30.295 46.099 -6.194  1.00 91.66  ? 46  SER A OG  1 
ATOM   355  N  N   . GLU A 1 47  ? -28.059 45.365 -8.649  1.00 83.86  ? 47  GLU A N   1 
ATOM   356  C  CA  . GLU A 1 47  ? -27.905 44.918 -10.063 1.00 88.63  ? 47  GLU A CA  1 
ATOM   357  C  C   . GLU A 1 47  ? -26.416 44.804 -10.424 1.00 85.76  ? 47  GLU A C   1 
ATOM   358  O  O   . GLU A 1 47  ? -26.072 43.957 -11.270 1.00 85.90  ? 47  GLU A O   1 
ATOM   359  C  CB  . GLU A 1 47  ? -28.665 45.845 -11.017 1.00 93.13  ? 47  GLU A CB  1 
ATOM   360  C  CG  . GLU A 1 47  ? -27.910 47.096 -11.431 1.00 97.73  ? 47  GLU A CG  1 
ATOM   361  C  CD  . GLU A 1 47  ? -28.582 47.892 -12.540 1.00 101.92 ? 47  GLU A CD  1 
ATOM   362  O  OE1 . GLU A 1 47  ? -28.721 49.122 -12.383 1.00 98.98  ? 47  GLU A OE1 1 
ATOM   363  O  OE2 . GLU A 1 47  ? -28.952 47.283 -13.567 1.00 104.63 ? 47  GLU A OE2 1 
ATOM   364  N  N   . ASP A 1 48  ? -25.559 45.613 -9.804  1.00 85.64  ? 48  ASP A N   1 
ATOM   365  C  CA  . ASP A 1 48  ? -24.125 45.708 -10.180 1.00 86.67  ? 48  ASP A CA  1 
ATOM   366  C  C   . ASP A 1 48  ? -23.305 44.642 -9.435  1.00 79.74  ? 48  ASP A C   1 
ATOM   367  O  O   . ASP A 1 48  ? -22.066 44.764 -9.482  1.00 94.71  ? 48  ASP A O   1 
ATOM   368  C  CB  . ASP A 1 48  ? -23.562 47.112 -9.890  1.00 84.05  ? 48  ASP A CB  1 
ATOM   369  C  CG  . ASP A 1 48  ? -24.350 48.278 -10.478 1.00 84.53  ? 48  ASP A CG  1 
ATOM   370  O  OD1 . ASP A 1 48  ? -24.644 48.235 -11.691 1.00 90.59  ? 48  ASP A OD1 1 
ATOM   371  O  OD2 . ASP A 1 48  ? -24.647 49.237 -9.723  1.00 74.61  ? 48  ASP A OD2 1 
ATOM   372  N  N   . MET A 1 49  ? -23.911 43.629 -8.790  1.00 67.32  ? 49  MET A N   1 
ATOM   373  C  CA  . MET A 1 49  ? -23.162 42.842 -7.759  1.00 65.64  ? 49  MET A CA  1 
ATOM   374  C  C   . MET A 1 49  ? -22.368 41.679 -8.384  1.00 54.62  ? 49  MET A C   1 
ATOM   375  O  O   . MET A 1 49  ? -21.236 41.407 -7.902  1.00 41.61  ? 49  MET A O   1 
ATOM   376  C  CB  . MET A 1 49  ? -24.063 42.363 -6.612  1.00 70.99  ? 49  MET A CB  1 
ATOM   377  C  CG  . MET A 1 49  ? -23.808 43.153 -5.316  1.00 74.49  ? 49  MET A CG  1 
ATOM   378  S  SD  . MET A 1 49  ? -24.777 42.631 -3.861  1.00 78.46  ? 49  MET A SD  1 
ATOM   379  C  CE  . MET A 1 49  ? -24.307 40.905 -3.734  1.00 76.37  ? 49  MET A CE  1 
ATOM   380  N  N   . LEU A 1 50  ? -22.883 41.047 -9.440  1.00 46.23  ? 50  LEU A N   1 
ATOM   381  C  CA  . LEU A 1 50  ? -22.191 39.913 -10.114 1.00 50.36  ? 50  LEU A CA  1 
ATOM   382  C  C   . LEU A 1 50  ? -20.969 40.391 -10.904 1.00 45.10  ? 50  LEU A C   1 
ATOM   383  O  O   . LEU A 1 50  ? -19.923 39.729 -10.786 1.00 49.77  ? 50  LEU A O   1 
ATOM   384  C  CB  . LEU A 1 50  ? -23.173 39.159 -11.014 1.00 52.13  ? 50  LEU A CB  1 
ATOM   385  C  CG  . LEU A 1 50  ? -23.870 37.977 -10.342 1.00 60.25  ? 50  LEU A CG  1 
ATOM   386  C  CD1 . LEU A 1 50  ? -24.909 38.451 -9.334  1.00 62.11  ? 50  LEU A CD1 1 
ATOM   387  C  CD2 . LEU A 1 50  ? -24.506 37.073 -11.385 1.00 65.99  ? 50  LEU A CD2 1 
ATOM   388  N  N   . ASN A 1 51  ? -21.069 41.475 -11.678 1.00 42.19  ? 51  ASN A N   1 
ATOM   389  C  CA  . ASN A 1 51  ? -19.971 41.902 -12.586 1.00 46.78  ? 51  ASN A CA  1 
ATOM   390  C  C   . ASN A 1 51  ? -19.820 43.423 -12.602 1.00 46.07  ? 51  ASN A C   1 
ATOM   391  O  O   . ASN A 1 51  ? -19.802 44.032 -13.669 1.00 41.96  ? 51  ASN A O   1 
ATOM   392  C  CB  . ASN A 1 51  ? -20.184 41.327 -13.989 1.00 52.28  ? 51  ASN A CB  1 
ATOM   393  C  CG  . ASN A 1 51  ? -18.904 40.762 -14.569 1.00 61.64  ? 51  ASN A CG  1 
ATOM   394  O  OD1 . ASN A 1 51  ? -17.805 41.254 -14.291 1.00 66.23  ? 51  ASN A OD1 1 
ATOM   395  N  ND2 . ASN A 1 51  ? -19.027 39.709 -15.359 1.00 71.71  ? 51  ASN A ND2 1 
ATOM   396  N  N   . PRO A 1 52  ? -19.601 44.088 -11.442 1.00 42.56  ? 52  PRO A N   1 
ATOM   397  C  CA  . PRO A 1 52  ? -19.450 45.536 -11.434 1.00 40.50  ? 52  PRO A CA  1 
ATOM   398  C  C   . PRO A 1 52  ? -18.151 45.865 -12.168 1.00 39.43  ? 52  PRO A C   1 
ATOM   399  O  O   . PRO A 1 52  ? -17.155 45.184 -11.988 1.00 33.00  ? 52  PRO A O   1 
ATOM   400  C  CB  . PRO A 1 52  ? -19.337 45.916 -9.953  1.00 42.50  ? 52  PRO A CB  1 
ATOM   401  C  CG  . PRO A 1 52  ? -18.775 44.655 -9.312  1.00 43.48  ? 52  PRO A CG  1 
ATOM   402  C  CD  . PRO A 1 52  ? -19.355 43.501 -10.113 1.00 43.77  ? 52  PRO A CD  1 
ATOM   403  N  N   . ASN A 1 53  ? -18.182 46.894 -13.000 1.00 30.53  ? 53  ASN A N   1 
ATOM   404  C  CA  . ASN A 1 53  ? -16.935 47.557 -13.425 1.00 31.06  ? 53  ASN A CA  1 
ATOM   405  C  C   . ASN A 1 53  ? -16.756 48.789 -12.556 1.00 29.91  ? 53  ASN A C   1 
ATOM   406  O  O   . ASN A 1 53  ? -17.421 49.810 -12.785 1.00 28.55  ? 53  ASN A O   1 
ATOM   407  C  CB  . ASN A 1 53  ? -16.894 47.962 -14.901 1.00 30.11  ? 53  ASN A CB  1 
ATOM   408  C  CG  . ASN A 1 53  ? -15.518 48.480 -15.199 1.00 32.34  ? 53  ASN A CG  1 
ATOM   409  O  OD1 . ASN A 1 53  ? -15.159 49.576 -14.785 1.00 33.06  ? 53  ASN A OD1 1 
ATOM   410  N  ND2 . ASN A 1 53  ? -14.696 47.637 -15.784 1.00 41.59  ? 53  ASN A ND2 1 
ATOM   411  N  N   . TYR A 1 54  ? -15.920 48.728 -11.531 1.00 25.74  ? 54  TYR A N   1 
ATOM   412  C  CA  . TYR A 1 54  ? -15.868 49.861 -10.580 1.00 24.51  ? 54  TYR A CA  1 
ATOM   413  C  C   . TYR A 1 54  ? -15.382 51.165 -11.224 1.00 26.04  ? 54  TYR A C   1 
ATOM   414  O  O   . TYR A 1 54  ? -15.733 52.233 -10.702 1.00 25.74  ? 54  TYR A O   1 
ATOM   415  C  CB  . TYR A 1 54  ? -15.013 49.498 -9.381  1.00 24.04  ? 54  TYR A CB  1 
ATOM   416  C  CG  . TYR A 1 54  ? -15.727 48.567 -8.459  1.00 23.59  ? 54  TYR A CG  1 
ATOM   417  C  CD1 . TYR A 1 54  ? -16.674 49.065 -7.574  1.00 25.13  ? 54  TYR A CD1 1 
ATOM   418  C  CD2 . TYR A 1 54  ? -15.406 47.207 -8.389  1.00 23.52  ? 54  TYR A CD2 1 
ATOM   419  C  CE1 . TYR A 1 54  ? -17.354 48.220 -6.718  1.00 27.38  ? 54  TYR A CE1 1 
ATOM   420  C  CE2 . TYR A 1 54  ? -16.073 46.358 -7.529  1.00 23.24  ? 54  TYR A CE2 1 
ATOM   421  C  CZ  . TYR A 1 54  ? -17.008 46.876 -6.658  1.00 24.53  ? 54  TYR A CZ  1 
ATOM   422  O  OH  . TYR A 1 54  ? -17.682 46.068 -5.794  1.00 27.40  ? 54  TYR A OH  1 
ATOM   423  N  N   . GLU A 1 55  ? -14.520 51.097 -12.240 1.00 25.63  ? 55  GLU A N   1 
ATOM   424  C  CA  . GLU A 1 55  ? -14.004 52.329 -12.872 1.00 29.44  ? 55  GLU A CA  1 
ATOM   425  C  C   . GLU A 1 55  ? -15.228 52.990 -13.519 1.00 30.16  ? 55  GLU A C   1 
ATOM   426  O  O   . GLU A 1 55  ? -15.416 54.188 -13.365 1.00 27.87  ? 55  GLU A O   1 
ATOM   427  C  CB  . GLU A 1 55  ? -12.844 51.992 -13.805 1.00 35.10  ? 55  GLU A CB  1 
ATOM   428  C  CG  . GLU A 1 55  ? -12.339 53.206 -14.553 1.00 44.61  ? 55  GLU A CG  1 
ATOM   429  C  CD  . GLU A 1 55  ? -11.347 52.939 -15.675 1.00 55.83  ? 55  GLU A CD  1 
ATOM   430  O  OE1 . GLU A 1 55  ? -11.015 51.734 -15.910 1.00 55.40  ? 55  GLU A OE1 1 
ATOM   431  O  OE2 . GLU A 1 55  ? -10.915 53.943 -16.325 1.00 56.36  ? 55  GLU A OE2 1 
ATOM   432  N  N   . ASP A 1 56  ? -16.059 52.168 -14.110 1.00 29.15  ? 56  ASP A N   1 
ATOM   433  C  CA  . ASP A 1 56  ? -17.264 52.581 -14.861 1.00 34.34  ? 56  ASP A CA  1 
ATOM   434  C  C   . ASP A 1 56  ? -18.306 53.097 -13.877 1.00 33.96  ? 56  ASP A C   1 
ATOM   435  O  O   . ASP A 1 56  ? -18.915 54.153 -14.117 1.00 34.03  ? 56  ASP A O   1 
ATOM   436  C  CB  . ASP A 1 56  ? -17.732 51.417 -15.727 1.00 34.58  ? 56  ASP A CB  1 
ATOM   437  C  CG  . ASP A 1 56  ? -18.523 51.947 -16.887 1.00 38.67  ? 56  ASP A CG  1 
ATOM   438  O  OD1 . ASP A 1 56  ? -17.920 52.705 -17.655 1.00 38.00  ? 56  ASP A OD1 1 
ATOM   439  O  OD2 . ASP A 1 56  ? -19.750 51.676 -16.929 1.00 41.44  ? 56  ASP A OD2 1 
ATOM   440  N  N   . LEU A 1 57  ? -18.467 52.422 -12.740 1.00 29.39  ? 57  LEU A N   1 
ATOM   441  C  CA  . LEU A 1 57  ? -19.433 52.850 -11.710 1.00 27.51  ? 57  LEU A CA  1 
ATOM   442  C  C   . LEU A 1 57  ? -18.987 54.148 -11.064 1.00 26.89  ? 57  LEU A C   1 
ATOM   443  O  O   . LEU A 1 57  ? -19.864 55.008 -10.772 1.00 30.37  ? 57  LEU A O   1 
ATOM   444  C  CB  . LEU A 1 57  ? -19.603 51.759 -10.648 1.00 29.38  ? 57  LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 57  ? -20.363 50.524 -11.103 1.00 33.93  ? 57  LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 57  ? -20.271 49.442 -10.032 1.00 30.99  ? 57  LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 57  ? -21.821 50.840 -11.392 1.00 35.02  ? 57  LEU A CD2 1 
ATOM   448  N  N   . LEU A 1 58  ? -17.688 54.353 -10.853 1.00 23.84  ? 58  LEU A N   1 
ATOM   449  C  CA  . LEU A 1 58  ? -17.194 55.532 -10.089 1.00 23.92  ? 58  LEU A CA  1 
ATOM   450  C  C   . LEU A 1 58  ? -17.212 56.803 -10.964 1.00 25.52  ? 58  LEU A C   1 
ATOM   451  O  O   . LEU A 1 58  ? -17.477 57.875 -10.406 1.00 26.98  ? 58  LEU A O   1 
ATOM   452  C  CB  . LEU A 1 58  ? -15.767 55.314 -9.567  1.00 25.00  ? 58  LEU A CB  1 
ATOM   453  C  CG  . LEU A 1 58  ? -15.245 56.408 -8.627  1.00 27.36  ? 58  LEU A CG  1 
ATOM   454  C  CD1 . LEU A 1 58  ? -16.185 56.594 -7.442  1.00 25.68  ? 58  LEU A CD1 1 
ATOM   455  C  CD2 . LEU A 1 58  ? -13.849 56.096 -8.104  1.00 26.44  ? 58  LEU A CD2 1 
ATOM   456  N  N   . ILE A 1 59  ? -16.877 56.685 -12.246 1.00 26.64  ? 59  ILE A N   1 
ATOM   457  C  CA  . ILE A 1 59  ? -16.858 57.870 -13.164 1.00 27.90  ? 59  ILE A CA  1 
ATOM   458  C  C   . ILE A 1 59  ? -18.270 58.480 -13.202 1.00 30.62  ? 59  ILE A C   1 
ATOM   459  O  O   . ILE A 1 59  ? -18.378 59.687 -13.458 1.00 31.84  ? 59  ILE A O   1 
ATOM   460  C  CB  . ILE A 1 59  ? -16.325 57.487 -14.563 1.00 32.65  ? 59  ILE A CB  1 
ATOM   461  C  CG1 . ILE A 1 59  ? -15.817 58.715 -15.336 1.00 36.44  ? 59  ILE A CG1 1 
ATOM   462  C  CG2 . ILE A 1 59  ? -17.369 56.734 -15.360 1.00 31.31  ? 59  ILE A CG2 1 
ATOM   463  C  CD1 . ILE A 1 59  ? -14.550 58.440 -16.153 1.00 38.41  ? 59  ILE A CD1 1 
ATOM   464  N  N   . ARG A 1 60  ? -19.302 57.686 -12.912 1.00 27.39  ? 60  ARG A N   1 
ATOM   465  C  CA  . ARG A 1 60  ? -20.725 58.116 -12.923 1.00 29.80  ? 60  ARG A CA  1 
ATOM   466  C  C   . ARG A 1 60  ? -21.123 58.789 -11.620 1.00 29.14  ? 60  ARG A C   1 
ATOM   467  O  O   . ARG A 1 60  ? -22.301 59.133 -11.471 1.00 30.69  ? 60  ARG A O   1 
ATOM   468  C  CB  . ARG A 1 60  ? -21.632 56.930 -13.225 1.00 27.49  ? 60  ARG A CB  1 
ATOM   469  C  CG  . ARG A 1 60  ? -21.281 56.216 -14.516 1.00 27.65  ? 60  ARG A CG  1 
ATOM   470  C  CD  . ARG A 1 60  ? -22.190 55.039 -14.769 1.00 28.78  ? 60  ARG A CD  1 
ATOM   471  N  NE  . ARG A 1 60  ? -21.759 54.191 -15.871 1.00 30.47  ? 60  ARG A NE  1 
ATOM   472  C  CZ  . ARG A 1 60  ? -22.259 54.183 -17.105 1.00 34.53  ? 60  ARG A CZ  1 
ATOM   473  N  NH1 . ARG A 1 60  ? -23.238 55.011 -17.476 1.00 35.43  ? 60  ARG A NH1 1 
ATOM   474  N  NH2 . ARG A 1 60  ? -21.732 53.370 -18.004 1.00 32.22  ? 60  ARG A NH2 1 
ATOM   475  N  N   . LYS A 1 61  ? -20.221 58.886 -10.649 1.00 28.86  ? 61  LYS A N   1 
ATOM   476  C  CA  . LYS A 1 61  ? -20.528 59.495 -9.350  1.00 29.54  ? 61  LYS A CA  1 
ATOM   477  C  C   . LYS A 1 61  ? -19.930 60.887 -9.273  1.00 27.60  ? 61  LYS A C   1 
ATOM   478  O  O   . LYS A 1 61  ? -18.846 61.142 -9.835  1.00 35.25  ? 61  LYS A O   1 
ATOM   479  C  CB  . LYS A 1 61  ? -19.964 58.684 -8.169  1.00 32.36  ? 61  LYS A CB  1 
ATOM   480  C  CG  . LYS A 1 61  ? -20.457 57.238 -8.081  1.00 36.74  ? 61  LYS A CG  1 
ATOM   481  C  CD  . LYS A 1 61  ? -21.611 57.044 -7.151  1.00 45.72  ? 61  LYS A CD  1 
ATOM   482  C  CE  . LYS A 1 61  ? -22.530 55.922 -7.580  1.00 52.07  ? 61  LYS A CE  1 
ATOM   483  N  NZ  . LYS A 1 61  ? -23.701 55.820 -6.675  1.00 60.63  ? 61  LYS A NZ  1 
ATOM   484  N  N   . SER A 1 62  ? -20.523 61.690 -8.410  1.00 31.77  ? 62  SER A N   1 
ATOM   485  C  CA  . SER A 1 62  ? -20.001 63.017 -7.996  1.00 39.49  ? 62  SER A CA  1 
ATOM   486  C  C   . SER A 1 62  ? -19.737 63.053 -6.485  1.00 35.74  ? 62  SER A C   1 
ATOM   487  O  O   . SER A 1 62  ? -20.385 62.294 -5.762  1.00 40.39  ? 62  SER A O   1 
ATOM   488  C  CB  . SER A 1 62  ? -20.992 64.078 -8.354  1.00 40.72  ? 62  SER A CB  1 
ATOM   489  O  OG  . SER A 1 62  ? -22.159 63.866 -7.595  1.00 47.34  ? 62  SER A OG  1 
ATOM   490  N  N   . ASN A 1 63  ? -18.887 63.978 -6.047  1.00 36.27  ? 63  ASN A N   1 
ATOM   491  C  CA  . ASN A 1 63  ? -18.578 64.217 -4.614  1.00 38.49  ? 63  ASN A CA  1 
ATOM   492  C  C   . ASN A 1 63  ? -19.874 64.216 -3.821  1.00 42.53  ? 63  ASN A C   1 
ATOM   493  O  O   . ASN A 1 63  ? -19.928 63.609 -2.713  1.00 44.05  ? 63  ASN A O   1 
ATOM   494  C  CB  . ASN A 1 63  ? -17.817 65.523 -4.376  1.00 38.70  ? 63  ASN A CB  1 
ATOM   495  C  CG  . ASN A 1 63  ? -16.360 65.457 -4.787  1.00 43.68  ? 63  ASN A CG  1 
ATOM   496  O  OD1 . ASN A 1 63  ? -15.795 64.382 -4.946  1.00 38.92  ? 63  ASN A OD1 1 
ATOM   497  N  ND2 . ASN A 1 63  ? -15.730 66.608 -4.971  1.00 43.55  ? 63  ASN A ND2 1 
ATOM   498  N  N   . HIS A 1 64  ? -20.894 64.903 -4.333  1.00 37.92  ? 64  HIS A N   1 
ATOM   499  C  CA  . HIS A 1 64  ? -22.147 65.101 -3.581  1.00 34.96  ? 64  HIS A CA  1 
ATOM   500  C  C   . HIS A 1 64  ? -22.966 63.817 -3.555  1.00 34.54  ? 64  HIS A C   1 
ATOM   501  O  O   . HIS A 1 64  ? -23.910 63.811 -2.790  1.00 37.49  ? 64  HIS A O   1 
ATOM   502  C  CB  . HIS A 1 64  ? -22.893 66.346 -4.106  1.00 42.35  ? 64  HIS A CB  1 
ATOM   503  C  CG  . HIS A 1 64  ? -23.407 66.233 -5.504  1.00 51.43  ? 64  HIS A CG  1 
ATOM   504  N  ND1 . HIS A 1 64  ? -24.547 65.500 -5.829  1.00 53.97  ? 64  HIS A ND1 1 
ATOM   505  C  CD2 . HIS A 1 64  ? -22.968 66.781 -6.663  1.00 60.63  ? 64  HIS A CD2 1 
ATOM   506  C  CE1 . HIS A 1 64  ? -24.767 65.585 -7.133  1.00 54.96  ? 64  HIS A CE1 1 
ATOM   507  N  NE2 . HIS A 1 64  ? -23.821 66.381 -7.664  1.00 63.41  ? 64  HIS A NE2 1 
ATOM   508  N  N   . ASN A 1 65  ? -22.603 62.743 -4.278  1.00 36.47  ? 65  ASN A N   1 
ATOM   509  C  CA  . ASN A 1 65  ? -23.344 61.449 -4.191  1.00 34.73  ? 65  ASN A CA  1 
ATOM   510  C  C   . ASN A 1 65  ? -22.946 60.723 -2.881  1.00 36.32  ? 65  ASN A C   1 
ATOM   511  O  O   . ASN A 1 65  ? -23.662 59.806 -2.467  1.00 36.22  ? 65  ASN A O   1 
ATOM   512  C  CB  . ASN A 1 65  ? -23.121 60.508 -5.390  1.00 35.15  ? 65  ASN A CB  1 
ATOM   513  C  CG  . ASN A 1 65  ? -23.693 60.973 -6.722  1.00 37.80  ? 65  ASN A CG  1 
ATOM   514  O  OD1 . ASN A 1 65  ? -23.084 60.776 -7.769  1.00 43.03  ? 65  ASN A OD1 1 
ATOM   515  N  ND2 . ASN A 1 65  ? -24.850 61.614 -6.708  1.00 43.53  ? 65  ASN A ND2 1 
ATOM   516  N  N   . PHE A 1 66  ? -21.844 61.110 -2.253  1.00 33.37  ? 66  PHE A N   1 
ATOM   517  C  CA  . PHE A 1 66  ? -21.350 60.446 -1.021  1.00 34.76  ? 66  PHE A CA  1 
ATOM   518  C  C   . PHE A 1 66  ? -21.782 61.227 0.208   1.00 32.58  ? 66  PHE A C   1 
ATOM   519  O  O   . PHE A 1 66  ? -21.380 62.362 0.362   1.00 35.32  ? 66  PHE A O   1 
ATOM   520  C  CB  . PHE A 1 66  ? -19.830 60.341 -1.034  1.00 31.65  ? 66  PHE A CB  1 
ATOM   521  C  CG  . PHE A 1 66  ? -19.317 59.470 -2.141  1.00 32.34  ? 66  PHE A CG  1 
ATOM   522  C  CD1 . PHE A 1 66  ? -19.290 58.089 -2.004  1.00 30.28  ? 66  PHE A CD1 1 
ATOM   523  C  CD2 . PHE A 1 66  ? -18.874 60.037 -3.326  1.00 26.70  ? 66  PHE A CD2 1 
ATOM   524  C  CE1 . PHE A 1 66  ? -18.815 57.299 -3.033  1.00 30.24  ? 66  PHE A CE1 1 
ATOM   525  C  CE2 . PHE A 1 66  ? -18.383 59.247 -4.350  1.00 30.00  ? 66  PHE A CE2 1 
ATOM   526  C  CZ  . PHE A 1 66  ? -18.390 57.877 -4.218  1.00 30.36  ? 66  PHE A CZ  1 
ATOM   527  N  N   . LEU A 1 67  ? -22.497 60.575 1.103   1.00 29.43  ? 67  LEU A N   1 
ATOM   528  C  CA  . LEU A 1 67  ? -22.879 61.149 2.409   1.00 32.93  ? 67  LEU A CA  1 
ATOM   529  C  C   . LEU A 1 67  ? -22.007 60.524 3.507   1.00 30.86  ? 67  LEU A C   1 
ATOM   530  O  O   . LEU A 1 67  ? -22.119 59.317 3.737   1.00 34.87  ? 67  LEU A O   1 
ATOM   531  C  CB  . LEU A 1 67  ? -24.366 60.885 2.658   1.00 38.82  ? 67  LEU A CB  1 
ATOM   532  C  CG  . LEU A 1 67  ? -24.858 61.244 4.065   1.00 43.64  ? 67  LEU A CG  1 
ATOM   533  C  CD1 . LEU A 1 67  ? -24.597 62.706 4.411   1.00 49.22  ? 67  LEU A CD1 1 
ATOM   534  C  CD2 . LEU A 1 67  ? -26.329 60.914 4.228   1.00 47.40  ? 67  LEU A CD2 1 
ATOM   535  N  N   . VAL A 1 68  ? -21.200 61.342 4.152   1.00 29.56  ? 68  VAL A N   1 
ATOM   536  C  CA  . VAL A 1 68  ? -20.295 60.933 5.254   1.00 31.19  ? 68  VAL A CA  1 
ATOM   537  C  C   . VAL A 1 68  ? -20.741 61.631 6.528   1.00 33.44  ? 68  VAL A C   1 
ATOM   538  O  O   . VAL A 1 68  ? -20.769 62.896 6.544   1.00 33.12  ? 68  VAL A O   1 
ATOM   539  C  CB  . VAL A 1 68  ? -18.839 61.307 4.928   1.00 30.00  ? 68  VAL A CB  1 
ATOM   540  C  CG1 . VAL A 1 68  ? -17.904 60.892 6.050   1.00 31.23  ? 68  VAL A CG1 1 
ATOM   541  C  CG2 . VAL A 1 68  ? -18.403 60.744 3.586   1.00 28.80  ? 68  VAL A CG2 1 
ATOM   542  N  N   . GLN A 1 69  ? -20.964 60.843 7.587   1.00 30.73  ? 69  GLN A N   1 
ATOM   543  C  CA  . GLN A 1 69  ? -21.469 61.332 8.896   1.00 33.76  ? 69  GLN A CA  1 
ATOM   544  C  C   . GLN A 1 69  ? -20.565 60.793 10.006  1.00 30.43  ? 69  GLN A C   1 
ATOM   545  O  O   . GLN A 1 69  ? -20.364 59.546 10.048  1.00 32.06  ? 69  GLN A O   1 
ATOM   546  C  CB  . GLN A 1 69  ? -22.919 60.911 9.050   1.00 35.09  ? 69  GLN A CB  1 
ATOM   547  C  CG  . GLN A 1 69  ? -23.827 61.531 7.996   1.00 40.85  ? 69  GLN A CG  1 
ATOM   548  C  CD  . GLN A 1 69  ? -25.219 60.991 8.189   1.00 43.47  ? 69  GLN A CD  1 
ATOM   549  O  OE1 . GLN A 1 69  ? -26.015 61.582 8.902   1.00 52.40  ? 69  GLN A OE1 1 
ATOM   550  N  NE2 . GLN A 1 69  ? -25.491 59.827 7.618   1.00 47.34  ? 69  GLN A NE2 1 
ATOM   551  N  N   . ALA A 1 70  ? -19.944 61.711 10.740  1.00 30.28  ? 70  ALA A N   1 
ATOM   552  C  CA  . ALA A 1 70  ? -19.116 61.458 11.932  1.00 31.51  ? 70  ALA A CA  1 
ATOM   553  C  C   . ALA A 1 70  ? -20.001 61.768 13.127  1.00 40.21  ? 70  ALA A C   1 
ATOM   554  O  O   . ALA A 1 70  ? -20.160 62.955 13.424  1.00 36.65  ? 70  ALA A O   1 
ATOM   555  C  CB  . ALA A 1 70  ? -17.883 62.306 11.927  1.00 33.15  ? 70  ALA A CB  1 
ATOM   556  N  N   . GLY A 1 71  ? -20.646 60.743 13.688  1.00 40.69  ? 71  GLY A N   1 
ATOM   557  C  CA  . GLY A 1 71  ? -21.723 60.971 14.664  1.00 44.09  ? 71  GLY A CA  1 
ATOM   558  C  C   . GLY A 1 71  ? -22.829 61.742 13.976  1.00 49.00  ? 71  GLY A C   1 
ATOM   559  O  O   . GLY A 1 71  ? -23.316 61.246 12.954  1.00 46.30  ? 71  GLY A O   1 
ATOM   560  N  N   . ASN A 1 72  ? -23.128 62.954 14.441  1.00 52.91  ? 72  ASN A N   1 
ATOM   561  C  CA  . ASN A 1 72  ? -24.264 63.769 13.931  1.00 61.43  ? 72  ASN A CA  1 
ATOM   562  C  C   . ASN A 1 72  ? -23.745 64.912 13.065  1.00 59.00  ? 72  ASN A C   1 
ATOM   563  O  O   . ASN A 1 72  ? -24.555 65.772 12.702  1.00 73.20  ? 72  ASN A O   1 
ATOM   564  C  CB  . ASN A 1 72  ? -25.130 64.304 15.073  1.00 68.54  ? 72  ASN A CB  1 
ATOM   565  C  CG  . ASN A 1 72  ? -25.700 63.165 15.889  1.00 78.21  ? 72  ASN A CG  1 
ATOM   566  O  OD1 . ASN A 1 72  ? -26.337 62.268 15.338  1.00 82.64  ? 72  ASN A OD1 1 
ATOM   567  N  ND2 . ASN A 1 72  ? -25.427 63.154 17.183  1.00 85.07  ? 72  ASN A ND2 1 
ATOM   568  N  N   . VAL A 1 73  ? -22.456 64.918 12.738  1.00 47.60  ? 73  VAL A N   1 
ATOM   569  C  CA  . VAL A 1 73  ? -21.838 65.971 11.882  1.00 49.31  ? 73  VAL A CA  1 
ATOM   570  C  C   . VAL A 1 73  ? -21.691 65.369 10.481  1.00 51.48  ? 73  VAL A C   1 
ATOM   571  O  O   . VAL A 1 73  ? -21.086 64.286 10.378  1.00 39.27  ? 73  VAL A O   1 
ATOM   572  C  CB  . VAL A 1 73  ? -20.483 66.435 12.451  1.00 50.90  ? 73  VAL A CB  1 
ATOM   573  C  CG1 . VAL A 1 73  ? -19.896 67.584 11.646  1.00 50.88  ? 73  VAL A CG1 1 
ATOM   574  C  CG2 . VAL A 1 73  ? -20.577 66.799 13.928  1.00 52.05  ? 73  VAL A CG2 1 
ATOM   575  N  N   . GLN A 1 74  ? -22.297 65.986 9.466   1.00 50.12  ? 74  GLN A N   1 
ATOM   576  C  CA  . GLN A 1 74  ? -22.071 65.626 8.049   1.00 47.41  ? 74  GLN A CA  1 
ATOM   577  C  C   . GLN A 1 74  ? -20.681 66.141 7.700   1.00 48.84  ? 74  GLN A C   1 
ATOM   578  O  O   . GLN A 1 74  ? -20.327 67.238 8.145   1.00 50.99  ? 74  GLN A O   1 
ATOM   579  C  CB  . GLN A 1 74  ? -23.148 66.207 7.131   1.00 56.55  ? 74  GLN A CB  1 
ATOM   580  C  CG  . GLN A 1 74  ? -22.961 65.842 5.662   1.00 63.63  ? 74  GLN A CG  1 
ATOM   581  C  CD  . GLN A 1 74  ? -23.970 66.494 4.743   1.00 67.45  ? 74  GLN A CD  1 
ATOM   582  O  OE1 . GLN A 1 74  ? -24.587 67.501 5.075   1.00 76.46  ? 74  GLN A OE1 1 
ATOM   583  N  NE2 . GLN A 1 74  ? -24.141 65.926 3.560   1.00 68.30  ? 74  GLN A NE2 1 
ATOM   584  N  N   . LEU A 1 75  ? -19.885 65.349 6.996   1.00 39.69  ? 75  LEU A N   1 
ATOM   585  C  CA  . LEU A 1 75  ? -18.605 65.836 6.441   1.00 38.62  ? 75  LEU A CA  1 
ATOM   586  C  C   . LEU A 1 75  ? -18.805 66.056 4.948   1.00 41.63  ? 75  LEU A C   1 
ATOM   587  O  O   . LEU A 1 75  ? -19.340 65.143 4.264   1.00 42.68  ? 75  LEU A O   1 
ATOM   588  C  CB  . LEU A 1 75  ? -17.501 64.813 6.714   1.00 39.70  ? 75  LEU A CB  1 
ATOM   589  C  CG  . LEU A 1 75  ? -17.241 64.523 8.188   1.00 39.64  ? 75  LEU A CG  1 
ATOM   590  C  CD1 . LEU A 1 75  ? -16.191 63.432 8.315   1.00 39.00  ? 75  LEU A CD1 1 
ATOM   591  C  CD2 . LEU A 1 75  ? -16.813 65.781 8.927   1.00 40.50  ? 75  LEU A CD2 1 
ATOM   592  N  N   . ARG A 1 76  ? -18.401 67.220 4.444   1.00 39.36  ? 76  ARG A N   1 
ATOM   593  C  CA  . ARG A 1 76  ? -18.601 67.518 3.009   1.00 38.06  ? 76  ARG A CA  1 
ATOM   594  C  C   . ARG A 1 76  ? -17.457 66.847 2.237   1.00 30.42  ? 76  ARG A C   1 
ATOM   595  O  O   . ARG A 1 76  ? -16.273 67.114 2.554   1.00 31.63  ? 76  ARG A O   1 
ATOM   596  C  CB  . ARG A 1 76  ? -18.690 69.031 2.780   1.00 40.53  ? 76  ARG A CB  1 
ATOM   597  C  CG  . ARG A 1 76  ? -18.893 69.432 1.324   1.00 48.52  ? 76  ARG A CG  1 
ATOM   598  C  CD  . ARG A 1 76  ? -18.844 70.941 1.151   1.00 55.29  ? 76  ARG A CD  1 
ATOM   599  N  NE  . ARG A 1 76  ? -18.103 71.347 -0.036  1.00 69.43  ? 76  ARG A NE  1 
ATOM   600  C  CZ  . ARG A 1 76  ? -18.020 72.592 -0.501  1.00 80.44  ? 76  ARG A CZ  1 
ATOM   601  N  NH1 . ARG A 1 76  ? -18.647 73.583 0.115   1.00 92.17  ? 76  ARG A NH1 1 
ATOM   602  N  NH2 . ARG A 1 76  ? -17.314 72.838 -1.591  1.00 78.99  ? 76  ARG A NH2 1 
ATOM   603  N  N   . VAL A 1 77  ? -17.812 66.062 1.226   1.00 32.07  ? 77  VAL A N   1 
ATOM   604  C  CA  . VAL A 1 77  ? -16.826 65.387 0.348   1.00 31.22  ? 77  VAL A CA  1 
ATOM   605  C  C   . VAL A 1 77  ? -16.408 66.394 -0.725  1.00 33.56  ? 77  VAL A C   1 
ATOM   606  O  O   . VAL A 1 77  ? -17.303 66.923 -1.430  1.00 34.52  ? 77  VAL A O   1 
ATOM   607  C  CB  . VAL A 1 77  ? -17.380 64.083 -0.245  1.00 32.14  ? 77  VAL A CB  1 
ATOM   608  C  CG1 . VAL A 1 77  ? -16.406 63.468 -1.227  1.00 33.70  ? 77  VAL A CG1 1 
ATOM   609  C  CG2 . VAL A 1 77  ? -17.738 63.096 0.879   1.00 32.04  ? 77  VAL A CG2 1 
ATOM   610  N  N   . ILE A 1 78  ? -15.116 66.615 -0.853  1.00 33.89  ? 78  ILE A N   1 
ATOM   611  C  CA  . ILE A 1 78  ? -14.571 67.647 -1.780  1.00 38.49  ? 78  ILE A CA  1 
ATOM   612  C  C   . ILE A 1 78  ? -13.687 66.975 -2.817  1.00 36.38  ? 78  ILE A C   1 
ATOM   613  O  O   . ILE A 1 78  ? -13.146 67.666 -3.651  1.00 37.27  ? 78  ILE A O   1 
ATOM   614  C  CB  . ILE A 1 78  ? -13.842 68.738 -0.978  1.00 36.93  ? 78  ILE A CB  1 
ATOM   615  C  CG1 . ILE A 1 78  ? -12.677 68.179 -0.169  1.00 37.27  ? 78  ILE A CG1 1 
ATOM   616  C  CG2 . ILE A 1 78  ? -14.860 69.449 -0.113  1.00 38.23  ? 78  ILE A CG2 1 
ATOM   617  C  CD1 . ILE A 1 78  ? -11.645 69.187 0.204   1.00 38.86  ? 78  ILE A CD1 1 
ATOM   618  N  N   . GLY A 1 79  ? -13.582 65.646 -2.775  1.00 35.02  ? 79  GLY A N   1 
ATOM   619  C  CA  . GLY A 1 79  ? -12.867 64.878 -3.796  1.00 31.96  ? 79  GLY A CA  1 
ATOM   620  C  C   . GLY A 1 79  ? -13.061 63.404 -3.551  1.00 35.13  ? 79  GLY A C   1 
ATOM   621  O  O   . GLY A 1 79  ? -13.493 63.020 -2.421  1.00 30.66  ? 79  GLY A O   1 
ATOM   622  N  N   . HIS A 1 80  ? -12.829 62.606 -4.577  1.00 35.64  ? 80  HIS A N   1 
ATOM   623  C  CA  . HIS A 1 80  ? -12.919 61.137 -4.440  1.00 34.85  ? 80  HIS A CA  1 
ATOM   624  C  C   . HIS A 1 80  ? -11.931 60.504 -5.398  1.00 39.09  ? 80  HIS A C   1 
ATOM   625  O  O   . HIS A 1 80  ? -11.651 61.077 -6.484  1.00 30.68  ? 80  HIS A O   1 
ATOM   626  C  CB  . HIS A 1 80  ? -14.348 60.650 -4.641  1.00 34.08  ? 80  HIS A CB  1 
ATOM   627  C  CG  . HIS A 1 80  ? -14.902 60.923 -5.993  1.00 38.97  ? 80  HIS A CG  1 
ATOM   628  N  ND1 . HIS A 1 80  ? -15.629 62.063 -6.254  1.00 39.15  ? 80  HIS A ND1 1 
ATOM   629  C  CD2 . HIS A 1 80  ? -14.829 60.233 -7.153  1.00 43.88  ? 80  HIS A CD2 1 
ATOM   630  C  CE1 . HIS A 1 80  ? -16.010 62.056 -7.524  1.00 42.84  ? 80  HIS A CE1 1 
ATOM   631  N  NE2 . HIS A 1 80  ? -15.523 60.953 -8.103  1.00 43.78  ? 80  HIS A NE2 1 
ATOM   632  N  N   . SER A 1 81  ? -11.421 59.342 -5.022  1.00 31.35  ? 81  SER A N   1 
ATOM   633  C  CA  . SER A 1 81  ? -10.540 58.581 -5.926  1.00 29.37  ? 81  SER A CA  1 
ATOM   634  C  C   . SER A 1 81  ? -10.533 57.126 -5.502  1.00 29.41  ? 81  SER A C   1 
ATOM   635  O  O   . SER A 1 81  ? -10.809 56.829 -4.334  1.00 27.61  ? 81  SER A O   1 
ATOM   636  C  CB  . SER A 1 81  ? -9.176  59.149 -5.982  1.00 32.71  ? 81  SER A CB  1 
ATOM   637  O  OG  . SER A 1 81  ? -8.507  58.975 -4.757  1.00 38.12  ? 81  SER A OG  1 
ATOM   638  N  N   . MET A 1 82  ? -10.340 56.285 -6.479  1.00 25.53  ? 82  MET A N   1 
ATOM   639  C  CA  . MET A 1 82  ? -10.270 54.836 -6.233  1.00 26.09  ? 82  MET A CA  1 
ATOM   640  C  C   . MET A 1 82  ? -8.815  54.541 -5.947  1.00 27.29  ? 82  MET A C   1 
ATOM   641  O  O   . MET A 1 82  ? -7.955  55.044 -6.694  1.00 27.74  ? 82  MET A O   1 
ATOM   642  C  CB  . MET A 1 82  ? -10.716 54.107 -7.490  1.00 29.89  ? 82  MET A CB  1 
ATOM   643  C  CG  . MET A 1 82  ? -10.637 52.626 -7.383  1.00 36.47  ? 82  MET A CG  1 
ATOM   644  S  SD  . MET A 1 82  ? -12.252 51.995 -7.721  1.00 36.70  ? 82  MET A SD  1 
ATOM   645  C  CE  . MET A 1 82  ? -12.300 52.213 -9.501  1.00 45.91  ? 82  MET A CE  1 
ATOM   646  N  N   . GLN A 1 83  ? -8.566  53.740 -4.923  1.00 23.26  ? 83  GLN A N   1 
ATOM   647  C  CA  . GLN A 1 83  ? -7.231  53.242 -4.531  1.00 28.17  ? 83  GLN A CA  1 
ATOM   648  C  C   . GLN A 1 83  ? -7.353  51.718 -4.508  1.00 22.18  ? 83  GLN A C   1 
ATOM   649  O  O   . GLN A 1 83  ? -7.752  51.240 -3.455  1.00 19.83  ? 83  GLN A O   1 
ATOM   650  C  CB  . GLN A 1 83  ? -7.002  53.939 -3.184  1.00 36.94  ? 83  GLN A CB  1 
ATOM   651  C  CG  . GLN A 1 83  ? -5.911  53.385 -2.288  1.00 43.43  ? 83  GLN A CG  1 
ATOM   652  C  CD  . GLN A 1 83  ? -4.536  53.827 -2.701  1.00 45.44  ? 83  GLN A CD  1 
ATOM   653  O  OE1 . GLN A 1 83  ? -3.637  53.008 -2.849  1.00 48.85  ? 83  GLN A OE1 1 
ATOM   654  N  NE2 . GLN A 1 83  ? -4.351  55.127 -2.868  1.00 41.16  ? 83  GLN A NE2 1 
ATOM   655  N  N   . ASN A 1 84  ? -7.161  51.010 -5.635  1.00 20.15  ? 84  ASN A N   1 
ATOM   656  C  CA  . ASN A 1 84  ? -7.345  49.530 -5.695  1.00 18.26  ? 84  ASN A CA  1 
ATOM   657  C  C   . ASN A 1 84  ? -8.793  49.247 -5.248  1.00 19.53  ? 84  ASN A C   1 
ATOM   658  O  O   . ASN A 1 84  ? -9.678  49.848 -5.855  1.00 19.12  ? 84  ASN A O   1 
ATOM   659  C  CB  . ASN A 1 84  ? -6.270  48.850 -4.849  1.00 16.50  ? 84  ASN A CB  1 
ATOM   660  C  CG  . ASN A 1 84  ? -4.908  49.211 -5.390  1.00 19.53  ? 84  ASN A CG  1 
ATOM   661  O  OD1 . ASN A 1 84  ? -4.662  49.085 -6.586  1.00 22.53  ? 84  ASN A OD1 1 
ATOM   662  N  ND2 . ASN A 1 84  ? -4.035  49.761 -4.569  1.00 20.35  ? 84  ASN A ND2 1 
ATOM   663  N  N   . CYS A 1 85  ? -9.054  48.507 -4.173  1.00 17.04  ? 85  CYS A N   1 
ATOM   664  C  CA  . CYS A 1 85  ? -10.425 48.165 -3.753  1.00 16.30  ? 85  CYS A CA  1 
ATOM   665  C  C   . CYS A 1 85  ? -10.962 49.111 -2.661  1.00 16.33  ? 85  CYS A C   1 
ATOM   666  O  O   . CYS A 1 85  ? -12.061 48.837 -2.149  1.00 18.17  ? 85  CYS A O   1 
ATOM   667  C  CB  . CYS A 1 85  ? -10.518 46.704 -3.336  1.00 18.70  ? 85  CYS A CB  1 
ATOM   668  S  SG  . CYS A 1 85  ? -10.093 45.587 -4.678  1.00 19.22  ? 85  CYS A SG  1 
ATOM   669  N  N   . VAL A 1 86  ? -10.260 50.175 -2.316  1.00 17.78  ? 86  VAL A N   1 
ATOM   670  C  CA  . VAL A 1 86  ? -10.715 51.186 -1.333  1.00 19.42  ? 86  VAL A CA  1 
ATOM   671  C  C   . VAL A 1 86  ? -11.071 52.459 -2.118  1.00 21.75  ? 86  VAL A C   1 
ATOM   672  O  O   . VAL A 1 86  ? -10.451 52.721 -3.166  1.00 22.43  ? 86  VAL A O   1 
ATOM   673  C  CB  . VAL A 1 86  ? -9.626  51.352 -0.266  1.00 24.86  ? 86  VAL A CB  1 
ATOM   674  C  CG1 . VAL A 1 86  ? -9.625  52.653 0.486   1.00 30.77  ? 86  VAL A CG1 1 
ATOM   675  C  CG2 . VAL A 1 86  ? -9.781  50.165 0.683   1.00 24.49  ? 86  VAL A CG2 1 
ATOM   676  N  N   . LEU A 1 87  ? -12.044 53.185 -1.616  1.00 20.90  ? 87  LEU A N   1 
ATOM   677  C  CA  . LEU A 1 87  ? -12.309 54.586 -2.044  1.00 22.47  ? 87  LEU A CA  1 
ATOM   678  C  C   . LEU A 1 87  ? -11.688 55.517 -1.034  1.00 23.88  ? 87  LEU A C   1 
ATOM   679  O  O   . LEU A 1 87  ? -11.801 55.221 0.172   1.00 22.75  ? 87  LEU A O   1 
ATOM   680  C  CB  . LEU A 1 87  ? -13.811 54.871 -2.048  1.00 26.42  ? 87  LEU A CB  1 
ATOM   681  C  CG  . LEU A 1 87  ? -14.673 54.246 -3.119  1.00 33.50  ? 87  LEU A CG  1 
ATOM   682  C  CD1 . LEU A 1 87  ? -16.098 54.826 -2.992  1.00 34.42  ? 87  LEU A CD1 1 
ATOM   683  C  CD2 . LEU A 1 87  ? -14.106 54.499 -4.514  1.00 41.66  ? 87  LEU A CD2 1 
ATOM   684  N  N   . LYS A 1 88  ? -11.064 56.597 -1.505  1.00 20.95  ? 88  LYS A N   1 
ATOM   685  C  CA  . LYS A 1 88  ? -10.535 57.687 -0.692  1.00 21.28  ? 88  LYS A CA  1 
ATOM   686  C  C   . LYS A 1 88  ? -11.453 58.881 -0.915  1.00 26.97  ? 88  LYS A C   1 
ATOM   687  O  O   . LYS A 1 88  ? -11.610 59.298 -2.090  1.00 26.39  ? 88  LYS A O   1 
ATOM   688  C  CB  . LYS A 1 88  ? -9.110  57.967 -1.098  1.00 22.78  ? 88  LYS A CB  1 
ATOM   689  C  CG  . LYS A 1 88  ? -8.123  56.879 -0.684  1.00 24.99  ? 88  LYS A CG  1 
ATOM   690  C  CD  . LYS A 1 88  ? -6.722  57.134 -1.146  1.00 29.93  ? 88  LYS A CD  1 
ATOM   691  C  CE  . LYS A 1 88  ? -6.110  58.316 -0.444  1.00 37.48  ? 88  LYS A CE  1 
ATOM   692  N  NZ  . LYS A 1 88  ? -4.652  58.411 -0.687  1.00 40.78  ? 88  LYS A NZ  1 
ATOM   693  N  N   . LEU A 1 89  ? -12.183 59.257 0.117   1.00 23.55  ? 89  LEU A N   1 
ATOM   694  C  CA  . LEU A 1 89  ? -13.096 60.428 0.065   1.00 24.40  ? 89  LEU A CA  1 
ATOM   695  C  C   . LEU A 1 89  ? -12.381 61.587 0.740   1.00 27.29  ? 89  LEU A C   1 
ATOM   696  O  O   . LEU A 1 89  ? -12.140 61.511 1.946   1.00 27.96  ? 89  LEU A O   1 
ATOM   697  C  CB  . LEU A 1 89  ? -14.425 60.082 0.717   1.00 24.65  ? 89  LEU A CB  1 
ATOM   698  C  CG  . LEU A 1 89  ? -15.193 58.914 0.107   1.00 25.60  ? 89  LEU A CG  1 
ATOM   699  C  CD1 . LEU A 1 89  ? -16.529 58.712 0.802   1.00 26.58  ? 89  LEU A CD1 1 
ATOM   700  C  CD2 . LEU A 1 89  ? -15.416 59.092 -1.386  1.00 29.99  ? 89  LEU A CD2 1 
ATOM   701  N  N   . LYS A 1 90  ? -11.971 62.602 -0.025  1.00 26.37  ? 90  LYS A N   1 
ATOM   702  C  CA  . LYS A 1 90  ? -11.349 63.787 0.578   1.00 26.95  ? 90  LYS A CA  1 
ATOM   703  C  C   . LYS A 1 90  ? -12.500 64.583 1.180   1.00 27.99  ? 90  LYS A C   1 
ATOM   704  O  O   . LYS A 1 90  ? -13.537 64.714 0.508   1.00 29.22  ? 90  LYS A O   1 
ATOM   705  C  CB  . LYS A 1 90  ? -10.561 64.629 -0.425  1.00 32.74  ? 90  LYS A CB  1 
ATOM   706  C  CG  . LYS A 1 90  ? -9.636  65.640 0.239   1.00 36.29  ? 90  LYS A CG  1 
ATOM   707  C  CD  . LYS A 1 90  ? -8.867  66.472 -0.754  1.00 45.98  ? 90  LYS A CD  1 
ATOM   708  C  CE  . LYS A 1 90  ? -7.480  66.845 -0.280  1.00 50.21  ? 90  LYS A CE  1 
ATOM   709  N  NZ  . LYS A 1 90  ? -6.957  67.992 -1.061  1.00 53.37  ? 90  LYS A NZ  1 
ATOM   710  N  N   . VAL A 1 91  ? -12.342 65.007 2.429   1.00 27.85  ? 91  VAL A N   1 
ATOM   711  C  CA  . VAL A 1 91  ? -13.405 65.773 3.121   1.00 27.73  ? 91  VAL A CA  1 
ATOM   712  C  C   . VAL A 1 91  ? -12.832 67.125 3.506   1.00 29.26  ? 91  VAL A C   1 
ATOM   713  O  O   . VAL A 1 91  ? -11.593 67.264 3.546   1.00 32.05  ? 91  VAL A O   1 
ATOM   714  C  CB  . VAL A 1 91  ? -14.017 65.010 4.302   1.00 28.76  ? 91  VAL A CB  1 
ATOM   715  C  CG1 . VAL A 1 91  ? -14.904 63.867 3.823   1.00 27.29  ? 91  VAL A CG1 1 
ATOM   716  C  CG2 . VAL A 1 91  ? -12.947 64.532 5.262   1.00 30.22  ? 91  VAL A CG2 1 
ATOM   717  N  N   . ASP A 1 92  ? -13.725 68.071 3.826   1.00 34.18  ? 92  ASP A N   1 
ATOM   718  C  CA  . ASP A 1 92  ? -13.328 69.483 4.066   1.00 41.65  ? 92  ASP A CA  1 
ATOM   719  C  C   . ASP A 1 92  ? -12.740 69.647 5.469   1.00 40.69  ? 92  ASP A C   1 
ATOM   720  O  O   . ASP A 1 92  ? -12.225 70.726 5.725   1.00 42.49  ? 92  ASP A O   1 
ATOM   721  C  CB  . ASP A 1 92  ? -14.488 70.456 3.824   1.00 47.64  ? 92  ASP A CB  1 
ATOM   722  C  CG  . ASP A 1 92  ? -15.734 70.251 4.667   1.00 51.01  ? 92  ASP A CG  1 
ATOM   723  O  OD1 . ASP A 1 92  ? -15.752 69.347 5.548   1.00 56.24  ? 92  ASP A OD1 1 
ATOM   724  O  OD2 . ASP A 1 92  ? -16.706 70.996 4.415   1.00 70.43  ? 92  ASP A OD2 1 
ATOM   725  N  N   . THR A 1 93  ? -12.789 68.625 6.333   1.00 37.26  ? 93  THR A N   1 
ATOM   726  C  CA  . THR A 1 93  ? -12.374 68.732 7.760   1.00 35.16  ? 93  THR A CA  1 
ATOM   727  C  C   . THR A 1 93  ? -11.354 67.633 8.116   1.00 32.46  ? 93  THR A C   1 
ATOM   728  O  O   . THR A 1 93  ? -11.681 66.463 7.863   1.00 32.86  ? 93  THR A O   1 
ATOM   729  C  CB  . THR A 1 93  ? -13.622 68.593 8.641   1.00 37.96  ? 93  THR A CB  1 
ATOM   730  O  OG1 . THR A 1 93  ? -14.682 69.387 8.090   1.00 44.53  ? 93  THR A OG1 1 
ATOM   731  C  CG2 . THR A 1 93  ? -13.380 68.995 10.078  1.00 38.81  ? 93  THR A CG2 1 
ATOM   732  N  N   . ALA A 1 94  ? -10.201 67.986 8.675   1.00 28.14  ? 94  ALA A N   1 
ATOM   733  C  CA  . ALA A 1 94  ? -9.204  67.025 9.202   1.00 29.34  ? 94  ALA A CA  1 
ATOM   734  C  C   . ALA A 1 94  ? -9.743  66.457 10.518  1.00 32.19  ? 94  ALA A C   1 
ATOM   735  O  O   . ALA A 1 94  ? -10.380 67.178 11.299  1.00 31.21  ? 94  ALA A O   1 
ATOM   736  C  CB  . ALA A 1 94  ? -7.853  67.638 9.384   1.00 30.40  ? 94  ALA A CB  1 
ATOM   737  N  N   . ASN A 1 95  ? -9.613  65.152 10.727  1.00 28.23  ? 95  ASN A N   1 
ATOM   738  C  CA  . ASN A 1 95  ? -10.222 64.545 11.927  1.00 25.24  ? 95  ASN A CA  1 
ATOM   739  C  C   . ASN A 1 95  ? -9.356  64.958 13.106  1.00 25.21  ? 95  ASN A C   1 
ATOM   740  O  O   . ASN A 1 95  ? -8.186  64.641 13.140  1.00 24.03  ? 95  ASN A O   1 
ATOM   741  C  CB  . ASN A 1 95  ? -10.358 63.034 11.760  1.00 25.44  ? 95  ASN A CB  1 
ATOM   742  C  CG  . ASN A 1 95  ? -10.822 62.381 13.045  1.00 29.90  ? 95  ASN A CG  1 
ATOM   743  O  OD1 . ASN A 1 95  ? -11.079 63.071 14.044  1.00 24.82  ? 95  ASN A OD1 1 
ATOM   744  N  ND2 . ASN A 1 95  ? -10.920 61.062 13.013  1.00 27.80  ? 95  ASN A ND2 1 
ATOM   745  N  N   . PRO A 1 96  ? -9.869  65.712 14.114  1.00 27.61  ? 96  PRO A N   1 
ATOM   746  C  CA  . PRO A 1 96  ? -9.005  66.186 15.195  1.00 29.45  ? 96  PRO A CA  1 
ATOM   747  C  C   . PRO A 1 96  ? -8.557  65.070 16.147  1.00 27.39  ? 96  PRO A C   1 
ATOM   748  O  O   . PRO A 1 96  ? -7.643  65.260 16.902  1.00 30.17  ? 96  PRO A O   1 
ATOM   749  C  CB  . PRO A 1 96  ? -9.885  67.212 15.933  1.00 29.11  ? 96  PRO A CB  1 
ATOM   750  C  CG  . PRO A 1 96  ? -11.283 66.794 15.641  1.00 28.94  ? 96  PRO A CG  1 
ATOM   751  C  CD  . PRO A 1 96  ? -11.265 66.127 14.280  1.00 29.08  ? 96  PRO A CD  1 
ATOM   752  N  N   . LYS A 1 97  ? -9.194  63.906 16.044  1.00 28.05  ? 97  LYS A N   1 
ATOM   753  C  CA  . LYS A 1 97  ? -8.842  62.712 16.856  1.00 25.80  ? 97  LYS A CA  1 
ATOM   754  C  C   . LYS A 1 97  ? -7.950  61.768 16.046  1.00 28.03  ? 97  LYS A C   1 
ATOM   755  O  O   . LYS A 1 97  ? -7.629  60.662 16.551  1.00 26.72  ? 97  LYS A O   1 
ATOM   756  C  CB  . LYS A 1 97  ? -10.122 62.036 17.288  1.00 28.21  ? 97  LYS A CB  1 
ATOM   757  C  CG  . LYS A 1 97  ? -11.078 62.899 18.102  1.00 31.66  ? 97  LYS A CG  1 
ATOM   758  C  CD  . LYS A 1 97  ? -12.360 62.164 18.309  1.00 35.23  ? 97  LYS A CD  1 
ATOM   759  C  CE  . LYS A 1 97  ? -13.375 62.924 19.130  1.00 42.17  ? 97  LYS A CE  1 
ATOM   760  N  NZ  . LYS A 1 97  ? -14.633 62.146 19.255  1.00 48.73  ? 97  LYS A NZ  1 
ATOM   761  N  N   . THR A 1 98  ? -7.452  62.199 14.887  1.00 26.80  ? 98  THR A N   1 
ATOM   762  C  CA  . THR A 1 98  ? -6.496  61.353 14.122  1.00 25.55  ? 98  THR A CA  1 
ATOM   763  C  C   . THR A 1 98  ? -5.333  60.940 15.006  1.00 25.41  ? 98  THR A C   1 
ATOM   764  O  O   . THR A 1 98  ? -4.577  61.789 15.487  1.00 27.06  ? 98  THR A O   1 
ATOM   765  C  CB  . THR A 1 98  ? -5.948  62.030 12.851  1.00 24.33  ? 98  THR A CB  1 
ATOM   766  O  OG1 . THR A 1 98  ? -7.059  62.506 12.112  1.00 24.86  ? 98  THR A OG1 1 
ATOM   767  C  CG2 . THR A 1 98  ? -5.100  61.085 12.026  1.00 26.14  ? 98  THR A CG2 1 
ATOM   768  N  N   . PRO A 1 99  ? -5.064  59.624 15.233  1.00 21.08  ? 99  PRO A N   1 
ATOM   769  C  CA  . PRO A 1 99  ? -3.896  59.245 16.010  1.00 23.39  ? 99  PRO A CA  1 
ATOM   770  C  C   . PRO A 1 99  ? -2.673  59.242 15.105  1.00 23.58  ? 99  PRO A C   1 
ATOM   771  O  O   . PRO A 1 99  ? -2.886  59.355 13.892  1.00 26.39  ? 99  PRO A O   1 
ATOM   772  C  CB  . PRO A 1 99  ? -4.231  57.814 16.453  1.00 25.39  ? 99  PRO A CB  1 
ATOM   773  C  CG  . PRO A 1 99  ? -5.054  57.276 15.302  1.00 23.23  ? 99  PRO A CG  1 
ATOM   774  C  CD  . PRO A 1 99  ? -5.860  58.466 14.786  1.00 23.22  ? 99  PRO A CD  1 
ATOM   775  N  N   . LYS A 1 100 ? -1.486  59.073 15.670  1.00 24.58  ? 100 LYS A N   1 
ATOM   776  C  CA  . LYS A 1 100 ? -0.282  58.678 14.911  1.00 24.89  ? 100 LYS A CA  1 
ATOM   777  C  C   . LYS A 1 100 ? -0.621  57.322 14.278  1.00 24.91  ? 100 LYS A C   1 
ATOM   778  O  O   . LYS A 1 100 ? -1.170  56.453 14.980  1.00 23.13  ? 100 LYS A O   1 
ATOM   779  C  CB  . LYS A 1 100 ? 0.935   58.557 15.813  1.00 29.68  ? 100 LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 100 ? 1.376   59.896 16.378  1.00 34.51  ? 100 LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 100 ? 2.639   59.791 17.194  1.00 45.06  ? 100 LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 100 ? 2.902   61.041 18.009  1.00 51.52  ? 100 LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 100 ? 3.941   60.805 19.040  1.00 57.08  ? 100 LYS A NZ  1 
ATOM   784  N  N   . TYR A 1 101 ? -0.434  57.167 12.979  1.00 21.67  ? 101 TYR A N   1 
ATOM   785  C  CA  . TYR A 1 101 ? -0.841  55.899 12.333  1.00 19.14  ? 101 TYR A CA  1 
ATOM   786  C  C   . TYR A 1 101 ? 0.098   55.569 11.179  1.00 21.37  ? 101 TYR A C   1 
ATOM   787  O  O   . TYR A 1 101 ? 0.817   56.459 10.646  1.00 20.54  ? 101 TYR A O   1 
ATOM   788  C  CB  . TYR A 1 101 ? -2.289  55.953 11.863  1.00 20.56  ? 101 TYR A CB  1 
ATOM   789  C  CG  . TYR A 1 101 ? -2.507  56.813 10.659  1.00 21.41  ? 101 TYR A CG  1 
ATOM   790  C  CD1 . TYR A 1 101 ? -2.752  58.174 10.799  1.00 24.24  ? 101 TYR A CD1 1 
ATOM   791  C  CD2 . TYR A 1 101 ? -2.424  56.285 9.379   1.00 22.73  ? 101 TYR A CD2 1 
ATOM   792  C  CE1 . TYR A 1 101 ? -2.957  58.986 9.701   1.00 25.98  ? 101 TYR A CE1 1 
ATOM   793  C  CE2 . TYR A 1 101 ? -2.591  57.107 8.267   1.00 24.05  ? 101 TYR A CE2 1 
ATOM   794  C  CZ  . TYR A 1 101 ? -2.883  58.447 8.433   1.00 26.60  ? 101 TYR A CZ  1 
ATOM   795  O  OH  . TYR A 1 101 ? -3.020  59.252 7.335   1.00 30.19  ? 101 TYR A OH  1 
ATOM   796  N  N   . LYS A 1 102 ? 0.043   54.304 10.804  1.00 19.10  ? 102 LYS A N   1 
ATOM   797  C  CA  . LYS A 1 102 ? 0.737   53.730 9.625   1.00 21.48  ? 102 LYS A CA  1 
ATOM   798  C  C   . LYS A 1 102 ? -0.230  52.765 8.959   1.00 21.15  ? 102 LYS A C   1 
ATOM   799  O  O   . LYS A 1 102 ? -1.093  52.216 9.623   1.00 18.16  ? 102 LYS A O   1 
ATOM   800  C  CB  . LYS A 1 102 ? 1.957   52.911 10.042  1.00 24.83  ? 102 LYS A CB  1 
ATOM   801  C  CG  . LYS A 1 102 ? 3.130   53.693 10.587  1.00 31.25  ? 102 LYS A CG  1 
ATOM   802  C  CD  . LYS A 1 102 ? 4.263   52.785 10.966  1.00 37.26  ? 102 LYS A CD  1 
ATOM   803  C  CE  . LYS A 1 102 ? 3.992   51.930 12.175  1.00 46.22  ? 102 LYS A CE  1 
ATOM   804  N  NZ  . LYS A 1 102 ? 5.241   51.755 12.957  1.00 60.57  ? 102 LYS A NZ  1 
ATOM   805  N  N   . PHE A 1 103 ? -0.021  52.540 7.678   1.00 18.21  ? 103 PHE A N   1 
ATOM   806  C  CA  . PHE A 1 103 ? -0.711  51.456 6.945   1.00 16.84  ? 103 PHE A CA  1 
ATOM   807  C  C   . PHE A 1 103 ? 0.336   50.380 6.721   1.00 17.44  ? 103 PHE A C   1 
ATOM   808  O  O   . PHE A 1 103 ? 1.346   50.657 5.999   1.00 16.82  ? 103 PHE A O   1 
ATOM   809  C  CB  . PHE A 1 103 ? -1.264  52.002 5.627   1.00 18.01  ? 103 PHE A CB  1 
ATOM   810  C  CG  . PHE A 1 103 ? -2.441  52.929 5.708   1.00 17.39  ? 103 PHE A CG  1 
ATOM   811  C  CD1 . PHE A 1 103 ? -3.123  53.153 6.888   1.00 16.85  ? 103 PHE A CD1 1 
ATOM   812  C  CD2 . PHE A 1 103 ? -2.874  53.538 4.546   1.00 19.39  ? 103 PHE A CD2 1 
ATOM   813  C  CE1 . PHE A 1 103 ? -4.227  54.001 6.909   1.00 17.73  ? 103 PHE A CE1 1 
ATOM   814  C  CE2 . PHE A 1 103 ? -3.957  54.404 4.573   1.00 19.78  ? 103 PHE A CE2 1 
ATOM   815  C  CZ  . PHE A 1 103 ? -4.657  54.600 5.734   1.00 20.84  ? 103 PHE A CZ  1 
ATOM   816  N  N   . VAL A 1 104 ? 0.120   49.213 7.313   1.00 16.58  ? 104 VAL A N   1 
ATOM   817  C  CA  A VAL A 1 104 ? 1.076   48.081 7.269   0.50 18.33  ? 104 VAL A CA  1 
ATOM   818  C  CA  B VAL A 1 104 ? 1.076   48.083 7.249   0.50 18.20  ? 104 VAL A CA  1 
ATOM   819  C  C   . VAL A 1 104 ? 0.319   46.863 6.745   1.00 19.21  ? 104 VAL A C   1 
ATOM   820  O  O   . VAL A 1 104 ? -0.793  46.539 7.277   1.00 26.65  ? 104 VAL A O   1 
ATOM   821  C  CB  A VAL A 1 104 ? 1.695   47.839 8.657   0.50 18.64  ? 104 VAL A CB  1 
ATOM   822  C  CB  B VAL A 1 104 ? 1.705   47.784 8.613   0.50 18.25  ? 104 VAL A CB  1 
ATOM   823  C  CG1 A VAL A 1 104 ? 2.634   46.644 8.703   0.50 19.41  ? 104 VAL A CG1 1 
ATOM   824  C  CG1 B VAL A 1 104 ? 2.357   49.010 9.219   0.50 21.67  ? 104 VAL A CG1 1 
ATOM   825  C  CG2 A VAL A 1 104 ? 2.407   49.083 9.152   0.50 22.05  ? 104 VAL A CG2 1 
ATOM   826  C  CG2 B VAL A 1 104 ? 0.673   47.193 9.556   0.50 18.39  ? 104 VAL A CG2 1 
ATOM   827  N  N   . ARG A 1 105 ? 0.923   46.097 5.900   1.00 16.80  ? 105 ARG A N   1 
ATOM   828  C  CA  . ARG A 1 105 ? 0.295   44.843 5.488   1.00 15.16  ? 105 ARG A CA  1 
ATOM   829  C  C   . ARG A 1 105 ? 0.893   43.749 6.357   1.00 15.81  ? 105 ARG A C   1 
ATOM   830  O  O   . ARG A 1 105 ? 2.152   43.726 6.493   1.00 19.35  ? 105 ARG A O   1 
ATOM   831  C  CB  . ARG A 1 105 ? 0.549   44.596 4.011   1.00 15.60  ? 105 ARG A CB  1 
ATOM   832  C  CG  . ARG A 1 105 ? -0.169  43.392 3.477   1.00 14.55  ? 105 ARG A CG  1 
ATOM   833  C  CD  . ARG A 1 105 ? 0.095   43.246 2.002   1.00 14.10  ? 105 ARG A CD  1 
ATOM   834  N  NE  . ARG A 1 105 ? -0.580  42.086 1.444   1.00 14.55  ? 105 ARG A NE  1 
ATOM   835  C  CZ  . ARG A 1 105 ? -1.778  42.066 0.865   1.00 14.70  ? 105 ARG A CZ  1 
ATOM   836  N  NH1 . ARG A 1 105 ? -2.465  43.187 0.783   1.00 16.88  ? 105 ARG A NH1 1 
ATOM   837  N  NH2 . ARG A 1 105 ? -2.256  40.921 0.397   1.00 15.60  ? 105 ARG A NH2 1 
ATOM   838  N  N   . ILE A 1 106 ? 0.061   42.817 6.798   1.00 15.00  ? 106 ILE A N   1 
ATOM   839  C  CA  . ILE A 1 106 ? 0.563   41.696 7.628   1.00 16.81  ? 106 ILE A CA  1 
ATOM   840  C  C   . ILE A 1 106 ? 0.722   40.420 6.813   1.00 16.88  ? 106 ILE A C   1 
ATOM   841  O  O   . ILE A 1 106 ? 0.265   40.311 5.695   1.00 16.26  ? 106 ILE A O   1 
ATOM   842  C  CB  . ILE A 1 106 ? -0.308  41.504 8.881   1.00 16.97  ? 106 ILE A CB  1 
ATOM   843  C  CG1 . ILE A 1 106 ? -1.730  41.135 8.488   1.00 18.89  ? 106 ILE A CG1 1 
ATOM   844  C  CG2 . ILE A 1 106 ? -0.205  42.718 9.782   1.00 19.84  ? 106 ILE A CG2 1 
ATOM   845  C  CD1 . ILE A 1 106 ? -2.560  40.576 9.629   1.00 22.36  ? 106 ILE A CD1 1 
ATOM   846  N  N   . GLN A 1 107 ? 1.448   39.476 7.407   1.00 15.72  ? 107 GLN A N   1 
ATOM   847  C  CA  . GLN A 1 107 ? 1.700   38.136 6.902   1.00 18.24  ? 107 GLN A CA  1 
ATOM   848  C  C   . GLN A 1 107 ? 0.648   37.186 7.434   1.00 16.93  ? 107 GLN A C   1 
ATOM   849  O  O   . GLN A 1 107 ? 0.168   37.334 8.542   1.00 16.12  ? 107 GLN A O   1 
ATOM   850  C  CB  . GLN A 1 107 ? 3.055   37.667 7.421   1.00 20.77  ? 107 GLN A CB  1 
ATOM   851  C  CG  . GLN A 1 107 ? 4.203   38.457 6.849   1.00 21.59  ? 107 GLN A CG  1 
ATOM   852  C  CD  . GLN A 1 107 ? 4.352   38.018 5.422   1.00 24.24  ? 107 GLN A CD  1 
ATOM   853  O  OE1 . GLN A 1 107 ? 4.422   36.812 5.155   1.00 23.98  ? 107 GLN A OE1 1 
ATOM   854  N  NE2 . GLN A 1 107 ? 4.333   38.984 4.513   1.00 23.99  ? 107 GLN A NE2 1 
ATOM   855  N  N   . PRO A 1 108 ? 0.356   36.112 6.679   1.00 17.79  ? 108 PRO A N   1 
ATOM   856  C  CA  . PRO A 1 108 ? -0.373  34.972 7.194   1.00 18.22  ? 108 PRO A CA  1 
ATOM   857  C  C   . PRO A 1 108 ? 0.274   34.496 8.492   1.00 19.25  ? 108 PRO A C   1 
ATOM   858  O  O   . PRO A 1 108 ? 1.521   34.402 8.551   1.00 20.83  ? 108 PRO A O   1 
ATOM   859  C  CB  . PRO A 1 108 ? -0.328  33.870 6.120   1.00 20.20  ? 108 PRO A CB  1 
ATOM   860  C  CG  . PRO A 1 108 ? 0.630   34.394 5.080   1.00 25.91  ? 108 PRO A CG  1 
ATOM   861  C  CD  . PRO A 1 108 ? 0.818   35.883 5.295   1.00 20.72  ? 108 PRO A CD  1 
ATOM   862  N  N   . GLY A 1 109 ? -0.554  34.293 9.515   1.00 16.76  ? 109 GLY A N   1 
ATOM   863  C  CA  . GLY A 1 109 ? -0.127  33.857 10.862  1.00 17.65  ? 109 GLY A CA  1 
ATOM   864  C  C   . GLY A 1 109 ? -0.003  35.038 11.819  1.00 18.80  ? 109 GLY A C   1 
ATOM   865  O  O   . GLY A 1 109 ? -0.018  34.832 13.056  1.00 22.89  ? 109 GLY A O   1 
ATOM   866  N  N   . GLN A 1 110 ? 0.068   36.279 11.336  1.00 15.60  ? 110 GLN A N   1 
ATOM   867  C  CA  A GLN A 1 110 ? 0.117   37.440 12.255  0.50 16.72  ? 110 GLN A CA  1 
ATOM   868  C  CA  B GLN A 1 110 ? 0.109   37.482 12.203  0.50 16.57  ? 110 GLN A CA  1 
ATOM   869  C  C   . GLN A 1 110 ? -1.301  37.772 12.767  1.00 15.73  ? 110 GLN A C   1 
ATOM   870  O  O   . GLN A 1 110 ? -2.313  37.456 12.095  1.00 17.47  ? 110 GLN A O   1 
ATOM   871  C  CB  A GLN A 1 110 ? 0.746   38.664 11.625  0.50 18.07  ? 110 GLN A CB  1 
ATOM   872  C  CB  B GLN A 1 110 ? 0.611   38.687 11.428  0.50 17.99  ? 110 GLN A CB  1 
ATOM   873  C  CG  A GLN A 1 110 ? 2.246   38.539 11.431  0.50 19.29  ? 110 GLN A CG  1 
ATOM   874  C  CG  B GLN A 1 110 ? 0.688   39.962 12.245  0.50 17.98  ? 110 GLN A CG  1 
ATOM   875  C  CD  A GLN A 1 110 ? 2.781   39.910 11.119  0.50 22.96  ? 110 GLN A CD  1 
ATOM   876  C  CD  B GLN A 1 110 ? 1.368   39.774 13.576  0.50 23.43  ? 110 GLN A CD  1 
ATOM   877  O  OE1 A GLN A 1 110 ? 3.186   40.687 12.000  0.50 31.49  ? 110 GLN A OE1 1 
ATOM   878  O  OE1 B GLN A 1 110 ? 2.434   39.156 13.689  0.50 29.26  ? 110 GLN A OE1 1 
ATOM   879  N  NE2 A GLN A 1 110 ? 2.753   40.222 9.842   0.50 17.02  ? 110 GLN A NE2 1 
ATOM   880  N  NE2 B GLN A 1 110 ? 0.744   40.326 14.590  0.50 19.29  ? 110 GLN A NE2 1 
ATOM   881  N  N   . THR A 1 111 ? -1.366  38.351 13.945  1.00 16.96  ? 111 THR A N   1 
ATOM   882  C  CA  . THR A 1 111 ? -2.636  38.666 14.659  1.00 15.88  ? 111 THR A CA  1 
ATOM   883  C  C   . THR A 1 111 ? -2.876  40.174 14.607  1.00 16.58  ? 111 THR A C   1 
ATOM   884  O  O   . THR A 1 111 ? -1.925  40.974 14.388  1.00 18.05  ? 111 THR A O   1 
ATOM   885  C  CB  . THR A 1 111 ? -2.605  38.084 16.075  1.00 17.10  ? 111 THR A CB  1 
ATOM   886  O  OG1 . THR A 1 111 ? -1.474  38.722 16.683  1.00 18.74  ? 111 THR A OG1 1 
ATOM   887  C  CG2 . THR A 1 111 ? -2.522  36.581 16.042  1.00 18.45  ? 111 THR A CG2 1 
ATOM   888  N  N   . PHE A 1 112 ? -4.143  40.546 14.846  1.00 15.70  ? 112 PHE A N   1 
ATOM   889  C  CA  . PHE A 1 112 ? -4.536  41.953 14.930  1.00 14.95  ? 112 PHE A CA  1 
ATOM   890  C  C   . PHE A 1 112 ? -5.869  42.005 15.631  1.00 14.93  ? 112 PHE A C   1 
ATOM   891  O  O   . PHE A 1 112 ? -6.555  41.030 15.783  1.00 15.81  ? 112 PHE A O   1 
ATOM   892  C  CB  . PHE A 1 112 ? -4.597  42.600 13.551  1.00 15.91  ? 112 PHE A CB  1 
ATOM   893  C  CG  . PHE A 1 112 ? -5.499  41.870 12.594  1.00 15.79  ? 112 PHE A CG  1 
ATOM   894  C  CD1 . PHE A 1 112 ? -5.042  40.770 11.902  1.00 18.42  ? 112 PHE A CD1 1 
ATOM   895  C  CD2 . PHE A 1 112 ? -6.796  42.291 12.376  1.00 15.30  ? 112 PHE A CD2 1 
ATOM   896  C  CE1 . PHE A 1 112 ? -5.868  40.089 11.017  1.00 19.03  ? 112 PHE A CE1 1 
ATOM   897  C  CE2 . PHE A 1 112 ? -7.614  41.594 11.516  1.00 15.99  ? 112 PHE A CE2 1 
ATOM   898  C  CZ  . PHE A 1 112 ? -7.129  40.569 10.765  1.00 18.85  ? 112 PHE A CZ  1 
ATOM   899  N  N   . SER A 1 113 ? -6.155  43.198 16.100  1.00 14.05  ? 113 SER A N   1 
ATOM   900  C  CA  . SER A 1 113 ? -7.420  43.543 16.764  1.00 14.82  ? 113 SER A CA  1 
ATOM   901  C  C   . SER A 1 113 ? -8.398  44.034 15.706  1.00 15.22  ? 113 SER A C   1 
ATOM   902  O  O   . SER A 1 113 ? -7.984  44.786 14.831  1.00 16.79  ? 113 SER A O   1 
ATOM   903  C  CB  . SER A 1 113 ? -7.209  44.545 17.808  1.00 16.40  ? 113 SER A CB  1 
ATOM   904  O  OG  . SER A 1 113 ? -6.283  44.051 18.766  1.00 17.60  ? 113 SER A OG  1 
ATOM   905  N  N   . VAL A 1 114 ? -9.655  43.663 15.874  1.00 15.79  ? 114 VAL A N   1 
ATOM   906  C  CA  . VAL A 1 114 ? -10.757 44.101 14.970  1.00 14.77  ? 114 VAL A CA  1 
ATOM   907  C  C   . VAL A 1 114 ? -11.716 44.931 15.796  1.00 16.60  ? 114 VAL A C   1 
ATOM   908  O  O   . VAL A 1 114 ? -12.150 44.491 16.834  1.00 16.84  ? 114 VAL A O   1 
ATOM   909  C  CB  . VAL A 1 114 ? -11.495 42.909 14.332  1.00 16.08  ? 114 VAL A CB  1 
ATOM   910  C  CG1 . VAL A 1 114 ? -12.757 43.380 13.608  1.00 18.76  ? 114 VAL A CG1 1 
ATOM   911  C  CG2 . VAL A 1 114 ? -10.573 42.170 13.371  1.00 17.78  ? 114 VAL A CG2 1 
ATOM   912  N  N   . LEU A 1 115 ? -12.028 46.130 15.318  1.00 16.59  ? 115 LEU A N   1 
ATOM   913  C  CA  . LEU A 1 115 ? -13.130 46.927 15.905  1.00 16.45  ? 115 LEU A CA  1 
ATOM   914  C  C   . LEU A 1 115 ? -14.327 46.773 15.001  1.00 18.01  ? 115 LEU A C   1 
ATOM   915  O  O   . LEU A 1 115 ? -14.409 47.427 13.902  1.00 18.59  ? 115 LEU A O   1 
ATOM   916  C  CB  . LEU A 1 115 ? -12.691 48.374 16.068  1.00 17.86  ? 115 LEU A CB  1 
ATOM   917  C  CG  . LEU A 1 115 ? -13.745 49.291 16.676  1.00 18.08  ? 115 LEU A CG  1 
ATOM   918  C  CD1 . LEU A 1 115 ? -13.933 48.905 18.172  1.00 21.43  ? 115 LEU A CD1 1 
ATOM   919  C  CD2 . LEU A 1 115 ? -13.324 50.744 16.588  1.00 16.84  ? 115 LEU A CD2 1 
ATOM   920  N  N   . ALA A 1 116 ? -15.250 45.907 15.367  1.00 16.64  ? 116 ALA A N   1 
ATOM   921  C  CA  . ALA A 1 116 ? -16.449 45.629 14.552  1.00 17.88  ? 116 ALA A CA  1 
ATOM   922  C  C   . ALA A 1 116 ? -17.364 46.848 14.707  1.00 21.14  ? 116 ALA A C   1 
ATOM   923  O  O   . ALA A 1 116 ? -17.707 47.237 15.831  1.00 22.34  ? 116 ALA A O   1 
ATOM   924  C  CB  . ALA A 1 116 ? -17.123 44.379 14.968  1.00 19.02  ? 116 ALA A CB  1 
ATOM   925  N  N   . CYS A 1 117 ? -17.820 47.366 13.594  1.00 18.27  ? 117 CYS A N   1 
ATOM   926  C  CA  A CYS A 1 117 ? -18.630 48.603 13.567  0.50 17.81  ? 117 CYS A CA  1 
ATOM   927  C  CA  B CYS A 1 117 ? -18.564 48.647 13.533  0.50 21.35  ? 117 CYS A CA  1 
ATOM   928  C  C   . CYS A 1 117 ? -19.800 48.454 12.637  1.00 19.27  ? 117 CYS A C   1 
ATOM   929  O  O   . CYS A 1 117 ? -19.748 47.650 11.707  1.00 19.36  ? 117 CYS A O   1 
ATOM   930  C  CB  A CYS A 1 117 ? -17.837 49.784 13.067  0.50 16.16  ? 117 CYS A CB  1 
ATOM   931  C  CB  B CYS A 1 117 ? -17.516 49.689 13.146  0.50 22.94  ? 117 CYS A CB  1 
ATOM   932  S  SG  A CYS A 1 117 ? -16.506 50.282 14.160  0.50 13.82  ? 117 CYS A SG  1 
ATOM   933  S  SG  B CYS A 1 117 ? -17.893 51.436 13.463  0.50 35.80  ? 117 CYS A SG  1 
ATOM   934  N  N   . TYR A 1 118 ? -20.892 49.178 12.953  1.00 19.30  ? 118 TYR A N   1 
ATOM   935  C  CA  . TYR A 1 118 ? -22.142 49.195 12.166  1.00 21.84  ? 118 TYR A CA  1 
ATOM   936  C  C   . TYR A 1 118 ? -22.620 50.647 12.165  1.00 20.03  ? 118 TYR A C   1 
ATOM   937  O  O   . TYR A 1 118 ? -22.600 51.293 13.257  1.00 21.65  ? 118 TYR A O   1 
ATOM   938  C  CB  . TYR A 1 118 ? -23.187 48.239 12.738  1.00 21.87  ? 118 TYR A CB  1 
ATOM   939  C  CG  . TYR A 1 118 ? -22.694 46.808 12.794  1.00 21.24  ? 118 TYR A CG  1 
ATOM   940  C  CD1 . TYR A 1 118 ? -21.986 46.351 13.888  1.00 22.02  ? 118 TYR A CD1 1 
ATOM   941  C  CD2 . TYR A 1 118 ? -22.830 45.979 11.698  1.00 21.96  ? 118 TYR A CD2 1 
ATOM   942  C  CE1 . TYR A 1 118 ? -21.427 45.085 13.883  1.00 22.54  ? 118 TYR A CE1 1 
ATOM   943  C  CE2 . TYR A 1 118 ? -22.279 44.722 11.663  1.00 22.54  ? 118 TYR A CE2 1 
ATOM   944  C  CZ  . TYR A 1 118 ? -21.587 44.270 12.778  1.00 21.33  ? 118 TYR A CZ  1 
ATOM   945  O  OH  . TYR A 1 118 ? -21.034 43.034 12.704  1.00 21.96  ? 118 TYR A OH  1 
ATOM   946  N  N   . ASN A 1 119 ? -22.935 51.151 10.975  1.00 23.92  ? 119 ASN A N   1 
ATOM   947  C  CA  . ASN A 1 119 ? -23.402 52.550 10.795  1.00 24.42  ? 119 ASN A CA  1 
ATOM   948  C  C   . ASN A 1 119 ? -22.416 53.512 11.443  1.00 25.21  ? 119 ASN A C   1 
ATOM   949  O  O   . ASN A 1 119 ? -22.863 54.516 12.021  1.00 24.99  ? 119 ASN A O   1 
ATOM   950  C  CB  . ASN A 1 119 ? -24.815 52.691 11.360  1.00 28.89  ? 119 ASN A CB  1 
ATOM   951  C  CG  . ASN A 1 119 ? -25.793 51.949 10.487  1.00 33.14  ? 119 ASN A CG  1 
ATOM   952  O  OD1 . ASN A 1 119 ? -26.041 52.336 9.342   1.00 43.93  ? 119 ASN A OD1 1 
ATOM   953  N  ND2 . ASN A 1 119 ? -26.264 50.820 10.965  1.00 39.23  ? 119 ASN A ND2 1 
ATOM   954  N  N   . GLY A 1 120 ? -21.095 53.259 11.331  1.00 19.81  ? 120 GLY A N   1 
ATOM   955  C  CA  . GLY A 1 120 ? -20.053 54.166 11.842  1.00 21.80  ? 120 GLY A CA  1 
ATOM   956  C  C   . GLY A 1 120 ? -19.871 54.087 13.350  1.00 23.83  ? 120 GLY A C   1 
ATOM   957  O  O   . GLY A 1 120 ? -19.017 54.836 13.904  1.00 25.31  ? 120 GLY A O   1 
ATOM   958  N  N   . SER A 1 121 ? -20.587 53.197 14.014  1.00 21.92  ? 121 SER A N   1 
ATOM   959  C  CA  . SER A 1 121 ? -20.597 53.102 15.486  1.00 25.21  ? 121 SER A CA  1 
ATOM   960  C  C   . SER A 1 121 ? -19.996 51.769 15.936  1.00 23.23  ? 121 SER A C   1 
ATOM   961  O  O   . SER A 1 121 ? -20.475 50.703 15.549  1.00 22.98  ? 121 SER A O   1 
ATOM   962  C  CB  . SER A 1 121 ? -22.006 53.266 15.967  1.00 27.43  ? 121 SER A CB  1 
ATOM   963  O  OG  . SER A 1 121 ? -22.008 53.203 17.363  1.00 33.78  ? 121 SER A OG  1 
ATOM   964  N  N   . PRO A 1 122 ? -18.900 51.824 16.726  1.00 27.54  ? 122 PRO A N   1 
ATOM   965  C  CA  . PRO A 1 122 ? -18.230 50.615 17.232  1.00 28.37  ? 122 PRO A CA  1 
ATOM   966  C  C   . PRO A 1 122 ? -19.139 49.756 18.108  1.00 27.26  ? 122 PRO A C   1 
ATOM   967  O  O   . PRO A 1 122 ? -19.796 50.263 19.005  1.00 26.83  ? 122 PRO A O   1 
ATOM   968  C  CB  . PRO A 1 122 ? -17.055 51.177 18.029  1.00 31.46  ? 122 PRO A CB  1 
ATOM   969  C  CG  . PRO A 1 122 ? -16.788 52.524 17.393  1.00 33.72  ? 122 PRO A CG  1 
ATOM   970  C  CD  . PRO A 1 122 ? -18.178 53.050 17.092  1.00 30.01  ? 122 PRO A CD  1 
ATOM   971  N  N   . SER A 1 123 ? -19.165 48.464 17.835  1.00 26.24  ? 123 SER A N   1 
ATOM   972  C  CA  . SER A 1 123 ? -19.967 47.425 18.514  1.00 26.39  ? 123 SER A CA  1 
ATOM   973  C  C   . SER A 1 123 ? -19.084 46.614 19.484  1.00 23.14  ? 123 SER A C   1 
ATOM   974  O  O   . SER A 1 123 ? -19.519 46.299 20.590  1.00 23.43  ? 123 SER A O   1 
ATOM   975  C  CB  . SER A 1 123 ? -20.564 46.553 17.463  1.00 28.20  ? 123 SER A CB  1 
ATOM   976  O  OG  . SER A 1 123 ? -21.372 45.565 18.036  1.00 34.45  ? 123 SER A OG  1 
ATOM   977  N  N   . GLY A 1 124 ? -17.861 46.262 19.092  1.00 20.55  ? 124 GLY A N   1 
ATOM   978  C  CA  . GLY A 1 124 ? -17.042 45.364 19.898  1.00 19.53  ? 124 GLY A CA  1 
ATOM   979  C  C   . GLY A 1 124 ? -15.633 45.257 19.354  1.00 18.84  ? 124 GLY A C   1 
ATOM   980  O  O   . GLY A 1 124 ? -15.413 45.638 18.192  1.00 19.25  ? 124 GLY A O   1 
ATOM   981  N  N   . VAL A 1 125 ? -14.776 44.659 20.164  1.00 17.33  ? 125 VAL A N   1 
ATOM   982  C  CA  . VAL A 1 125 ? -13.351 44.490 19.795  1.00 17.01  ? 125 VAL A CA  1 
ATOM   983  C  C   . VAL A 1 125 ? -12.951 43.067 20.072  1.00 18.76  ? 125 VAL A C   1 
ATOM   984  O  O   . VAL A 1 125 ? -13.375 42.481 21.071  1.00 18.63  ? 125 VAL A O   1 
ATOM   985  C  CB  . VAL A 1 125 ? -12.451 45.556 20.441  1.00 20.91  ? 125 VAL A CB  1 
ATOM   986  C  CG1 . VAL A 1 125 ? -12.381 45.440 21.937  1.00 25.76  ? 125 VAL A CG1 1 
ATOM   987  C  CG2 . VAL A 1 125 ? -11.037 45.556 19.871  1.00 23.39  ? 125 VAL A CG2 1 
ATOM   988  N  N   . TYR A 1 126 ? -12.256 42.466 19.122  1.00 17.22  ? 126 TYR A N   1 
ATOM   989  C  CA  . TYR A 1 126 ? -11.782 41.078 19.306  1.00 15.99  ? 126 TYR A CA  1 
ATOM   990  C  C   . TYR A 1 126 ? -10.455 40.912 18.585  1.00 17.79  ? 126 TYR A C   1 
ATOM   991  O  O   . TYR A 1 126 ? -10.107 41.724 17.729  1.00 18.39  ? 126 TYR A O   1 
ATOM   992  C  CB  . TYR A 1 126 ? -12.837 40.051 18.910  1.00 16.67  ? 126 TYR A CB  1 
ATOM   993  C  CG  . TYR A 1 126 ? -13.327 40.166 17.499  1.00 18.12  ? 126 TYR A CG  1 
ATOM   994  C  CD1 . TYR A 1 126 ? -12.619 39.650 16.436  1.00 19.59  ? 126 TYR A CD1 1 
ATOM   995  C  CD2 . TYR A 1 126 ? -14.511 40.831 17.256  1.00 20.21  ? 126 TYR A CD2 1 
ATOM   996  C  CE1 . TYR A 1 126 ? -13.084 39.818 15.135  1.00 18.41  ? 126 TYR A CE1 1 
ATOM   997  C  CE2 . TYR A 1 126 ? -14.988 40.984 15.971  1.00 21.12  ? 126 TYR A CE2 1 
ATOM   998  C  CZ  . TYR A 1 126 ? -14.260 40.493 14.912  1.00 21.21  ? 126 TYR A CZ  1 
ATOM   999  O  OH  . TYR A 1 126 ? -14.745 40.581 13.641  1.00 27.25  ? 126 TYR A OH  1 
ATOM   1000 N  N   . GLN A 1 127 ? -9.766  39.837 18.964  1.00 17.83  ? 127 GLN A N   1 
ATOM   1001 C  CA  . GLN A 1 127 ? -8.525  39.440 18.266  1.00 17.92  ? 127 GLN A CA  1 
ATOM   1002 C  C   . GLN A 1 127 ? -8.780  38.435 17.176  1.00 18.83  ? 127 GLN A C   1 
ATOM   1003 O  O   . GLN A 1 127 ? -9.589  37.485 17.346  1.00 21.65  ? 127 GLN A O   1 
ATOM   1004 C  CB  . GLN A 1 127 ? -7.571  38.661 19.154  1.00 23.62  ? 127 GLN A CB  1 
ATOM   1005 C  CG  . GLN A 1 127 ? -6.600  39.438 19.963  1.00 26.48  ? 127 GLN A CG  1 
ATOM   1006 C  CD  . GLN A 1 127 ? -5.738  40.409 19.207  1.00 25.35  ? 127 GLN A CD  1 
ATOM   1007 O  OE1 . GLN A 1 127 ? -6.148  41.537 19.034  1.00 25.09  ? 127 GLN A OE1 1 
ATOM   1008 N  NE2 . GLN A 1 127 ? -4.499  40.049 18.915  1.00 25.35  ? 127 GLN A NE2 1 
ATOM   1009 N  N   . CYS A 1 128 ? -7.983  38.511 16.127  1.00 19.34  ? 128 CYS A N   1 
ATOM   1010 C  CA  A CYS A 1 128 ? -8.056  37.691 14.897  0.50 20.53  ? 128 CYS A CA  1 
ATOM   1011 C  CA  B CYS A 1 128 ? -7.936  37.355 15.214  0.50 21.24  ? 128 CYS A CA  1 
ATOM   1012 C  C   . CYS A 1 128 ? -6.624  37.370 14.453  1.00 20.03  ? 128 CYS A C   1 
ATOM   1013 O  O   . CYS A 1 128 ? -5.745  38.121 14.829  1.00 20.03  ? 128 CYS A O   1 
ATOM   1014 C  CB  A CYS A 1 128 ? -8.702  38.485 13.767  0.50 23.17  ? 128 CYS A CB  1 
ATOM   1015 C  CB  B CYS A 1 128 ? -9.093  37.361 14.244  0.50 24.64  ? 128 CYS A CB  1 
ATOM   1016 S  SG  A CYS A 1 128 ? -10.433 38.073 13.499  0.50 25.84  ? 128 CYS A SG  1 
ATOM   1017 S  SG  B CYS A 1 128 ? -9.056  38.885 13.296  0.50 28.10  ? 128 CYS A SG  1 
ATOM   1018 N  N   . ALA A 1 129 ? -6.471  36.345 13.643  1.00 21.08  ? 129 ALA A N   1 
ATOM   1019 C  CA  . ALA A 1 129 ? -5.235  36.079 12.884  1.00 18.69  ? 129 ALA A CA  1 
ATOM   1020 C  C   . ALA A 1 129 ? -5.563  36.104 11.397  1.00 18.08  ? 129 ALA A C   1 
ATOM   1021 O  O   . ALA A 1 129 ? -6.629  35.653 10.979  1.00 20.01  ? 129 ALA A O   1 
ATOM   1022 C  CB  . ALA A 1 129 ? -4.639  34.759 13.267  1.00 20.94  ? 129 ALA A CB  1 
ATOM   1023 N  N   . MET A 1 130 ? -4.585  36.509 10.625  1.00 16.73  ? 130 MET A N   1 
ATOM   1024 C  CA  . MET A 1 130 ? -4.592  36.239 9.169   1.00 17.63  ? 130 MET A CA  1 
ATOM   1025 C  C   . MET A 1 130 ? -4.293  34.751 8.975   1.00 16.62  ? 130 MET A C   1 
ATOM   1026 O  O   . MET A 1 130 ? -3.217  34.282 9.417   1.00 16.44  ? 130 MET A O   1 
ATOM   1027 C  CB  . MET A 1 130 ? -3.591  37.152 8.490   1.00 18.79  ? 130 MET A CB  1 
ATOM   1028 C  CG  . MET A 1 130 ? -3.561  37.056 6.955   1.00 19.04  ? 130 MET A CG  1 
ATOM   1029 S  SD  . MET A 1 130 ? -5.153  37.394 6.131   1.00 19.63  ? 130 MET A SD  1 
ATOM   1030 C  CE  . MET A 1 130 ? -5.375  39.104 6.604   1.00 17.43  ? 130 MET A CE  1 
ATOM   1031 N  N   . ARG A 1 131 ? -5.262  33.984 8.460   1.00 15.74  ? 131 ARG A N   1 
ATOM   1032 C  CA  . ARG A 1 131 ? -5.074  32.537 8.245   1.00 15.14  ? 131 ARG A CA  1 
ATOM   1033 C  C   . ARG A 1 131 ? -4.097  32.325 7.107   1.00 15.73  ? 131 ARG A C   1 
ATOM   1034 O  O   . ARG A 1 131 ? -3.900  33.184 6.237   1.00 15.06  ? 131 ARG A O   1 
ATOM   1035 C  CB  . ARG A 1 131 ? -6.377  31.839 7.903   1.00 17.28  ? 131 ARG A CB  1 
ATOM   1036 C  CG  . ARG A 1 131 ? -7.452  31.955 8.960   1.00 17.89  ? 131 ARG A CG  1 
ATOM   1037 C  CD  . ARG A 1 131 ? -7.075  31.507 10.362  1.00 17.89  ? 131 ARG A CD  1 
ATOM   1038 N  NE  . ARG A 1 131 ? -6.481  30.209 10.302  1.00 16.78  ? 131 ARG A NE  1 
ATOM   1039 C  CZ  . ARG A 1 131 ? -5.881  29.644 11.330  1.00 19.58  ? 131 ARG A CZ  1 
ATOM   1040 N  NH1 . ARG A 1 131 ? -5.917  30.248 12.499  1.00 19.06  ? 131 ARG A NH1 1 
ATOM   1041 N  NH2 . ARG A 1 131 ? -5.254  28.484 11.163  1.00 18.48  ? 131 ARG A NH2 1 
ATOM   1042 N  N   . PRO A 1 132 ? -3.407  31.163 7.070   1.00 14.97  ? 132 PRO A N   1 
ATOM   1043 C  CA  . PRO A 1 132 ? -2.554  30.830 5.936   1.00 14.90  ? 132 PRO A CA  1 
ATOM   1044 C  C   . PRO A 1 132 ? -3.250  30.929 4.570   1.00 16.03  ? 132 PRO A C   1 
ATOM   1045 O  O   . PRO A 1 132 ? -2.556  31.159 3.598   1.00 16.59  ? 132 PRO A O   1 
ATOM   1046 C  CB  . PRO A 1 132 ? -2.113  29.382 6.271   1.00 15.82  ? 132 PRO A CB  1 
ATOM   1047 C  CG  . PRO A 1 132 ? -2.072  29.375 7.775   1.00 15.54  ? 132 PRO A CG  1 
ATOM   1048 C  CD  . PRO A 1 132 ? -3.328  30.161 8.154   1.00 16.51  ? 132 PRO A CD  1 
ATOM   1049 N  N   . ASN A 1 133 ? -4.568  30.691 4.537   1.00 16.10  ? 133 ASN A N   1 
ATOM   1050 C  CA  . ASN A 1 133 ? -5.338  30.819 3.268   1.00 15.35  ? 133 ASN A CA  1 
ATOM   1051 C  C   . ASN A 1 133 ? -5.857  32.256 3.077   1.00 17.15  ? 133 ASN A C   1 
ATOM   1052 O  O   . ASN A 1 133 ? -6.639  32.458 2.148   1.00 16.40  ? 133 ASN A O   1 
ATOM   1053 C  CB  . ASN A 1 133 ? -6.460  29.802 3.192   1.00 17.11  ? 133 ASN A CB  1 
ATOM   1054 C  CG  . ASN A 1 133 ? -7.612  30.102 4.138   1.00 16.11  ? 133 ASN A CG  1 
ATOM   1055 O  OD1 . ASN A 1 133 ? -7.591  31.069 4.928   1.00 15.16  ? 133 ASN A OD1 1 
ATOM   1056 N  ND2 . ASN A 1 133 ? -8.604  29.239 4.135   1.00 18.77  ? 133 ASN A ND2 1 
ATOM   1057 N  N   . PHE A 1 134 ? -5.351  33.234 3.836   1.00 14.65  ? 134 PHE A N   1 
ATOM   1058 C  CA  . PHE A 1 134 ? -5.627  34.680 3.675   1.00 16.39  ? 134 PHE A CA  1 
ATOM   1059 C  C   . PHE A 1 134 ? -7.066  35.048 3.961   1.00 16.17  ? 134 PHE A C   1 
ATOM   1060 O  O   . PHE A 1 134 ? -7.522  36.122 3.493   1.00 21.18  ? 134 PHE A O   1 
ATOM   1061 C  CB  . PHE A 1 134 ? -5.200  35.159 2.295   1.00 17.33  ? 134 PHE A CB  1 
ATOM   1062 C  CG  . PHE A 1 134 ? -3.713  35.316 2.142   1.00 17.97  ? 134 PHE A CG  1 
ATOM   1063 C  CD1 . PHE A 1 134 ? -3.050  36.388 2.751   1.00 18.69  ? 134 PHE A CD1 1 
ATOM   1064 C  CD2 . PHE A 1 134 ? -2.988  34.400 1.392   1.00 20.16  ? 134 PHE A CD2 1 
ATOM   1065 C  CE1 . PHE A 1 134 ? -1.682  36.562 2.568   1.00 22.10  ? 134 PHE A CE1 1 
ATOM   1066 C  CE2 . PHE A 1 134 ? -1.627  34.574 1.196   1.00 21.24  ? 134 PHE A CE2 1 
ATOM   1067 C  CZ  . PHE A 1 134 ? -0.971  35.644 1.808   1.00 21.96  ? 134 PHE A CZ  1 
ATOM   1068 N  N   . THR A 1 135 ? -7.794  34.206 4.650   1.00 14.53  ? 135 THR A N   1 
ATOM   1069 C  CA  . THR A 1 135 ? -9.070  34.616 5.255   1.00 14.34  ? 135 THR A CA  1 
ATOM   1070 C  C   . THR A 1 135 ? -8.852  35.036 6.703   1.00 17.33  ? 135 THR A C   1 
ATOM   1071 O  O   . THR A 1 135 ? -7.764  34.699 7.282   1.00 15.90  ? 135 THR A O   1 
ATOM   1072 C  CB  . THR A 1 135 ? -10.075 33.462 5.131   1.00 15.15  ? 135 THR A CB  1 
ATOM   1073 O  OG1 . THR A 1 135 ? -9.779  32.344 5.966   1.00 15.51  ? 135 THR A OG1 1 
ATOM   1074 C  CG2 . THR A 1 135 ? -10.195 32.973 3.707   1.00 17.52  ? 135 THR A CG2 1 
ATOM   1075 N  N   . ILE A 1 136 ? -9.887  35.606 7.334   1.00 15.88  ? 136 ILE A N   1 
ATOM   1076 C  CA  . ILE A 1 136 ? -9.886  35.779 8.800   1.00 17.37  ? 136 ILE A CA  1 
ATOM   1077 C  C   . ILE A 1 136 ? -11.157 35.179 9.336   1.00 17.81  ? 136 ILE A C   1 
ATOM   1078 O  O   . ILE A 1 136 ? -12.173 35.196 8.640   1.00 17.38  ? 136 ILE A O   1 
ATOM   1079 C  CB  . ILE A 1 136 ? -9.628  37.225 9.240   1.00 22.60  ? 136 ILE A CB  1 
ATOM   1080 C  CG1 . ILE A 1 136 ? -10.864 38.100 9.070   1.00 20.23  ? 136 ILE A CG1 1 
ATOM   1081 C  CG2 . ILE A 1 136 ? -8.451  37.806 8.466   1.00 21.25  ? 136 ILE A CG2 1 
ATOM   1082 C  CD1 . ILE A 1 136 ? -10.711 39.424 9.750   1.00 22.39  ? 136 ILE A CD1 1 
ATOM   1083 N  N   . LYS A 1 137 ? -11.055 34.528 10.468  1.00 16.51  ? 137 LYS A N   1 
ATOM   1084 C  CA  . LYS A 1 137 ? -12.227 33.963 11.174  1.00 18.59  ? 137 LYS A CA  1 
ATOM   1085 C  C   . LYS A 1 137 ? -12.758 35.072 12.053  1.00 16.95  ? 137 LYS A C   1 
ATOM   1086 O  O   . LYS A 1 137 ? -12.453 35.127 13.240  1.00 19.01  ? 137 LYS A O   1 
ATOM   1087 C  CB  . LYS A 1 137 ? -11.816 32.687 11.922  1.00 21.64  ? 137 LYS A CB  1 
ATOM   1088 C  CG  . LYS A 1 137 ? -11.322 31.585 10.993  1.00 28.40  ? 137 LYS A CG  1 
ATOM   1089 C  CD  . LYS A 1 137 ? -11.023 30.280 11.685  1.00 36.76  ? 137 LYS A CD  1 
ATOM   1090 C  CE  . LYS A 1 137 ? -10.584 29.185 10.733  1.00 44.82  ? 137 LYS A CE  1 
ATOM   1091 N  NZ  . LYS A 1 137 ? -9.987  28.023 11.447  1.00 50.10  ? 137 LYS A NZ  1 
ATOM   1092 N  N   . GLY A 1 138 ? -13.459 36.022 11.437  1.00 16.43  ? 138 GLY A N   1 
ATOM   1093 C  CA  . GLY A 1 138 ? -13.995 37.185 12.126  1.00 17.42  ? 138 GLY A CA  1 
ATOM   1094 C  C   . GLY A 1 138 ? -15.356 36.890 12.705  1.00 18.12  ? 138 GLY A C   1 
ATOM   1095 O  O   . GLY A 1 138 ? -15.834 35.755 12.685  1.00 19.28  ? 138 GLY A O   1 
ATOM   1096 N  N   . SER A 1 139 ? -15.903 37.934 13.259  1.00 16.79  ? 139 SER A N   1 
ATOM   1097 C  CA  . SER A 1 139 ? -17.319 37.963 13.694  1.00 16.61  ? 139 SER A CA  1 
ATOM   1098 C  C   . SER A 1 139 ? -17.913 39.244 13.109  1.00 16.42  ? 139 SER A C   1 
ATOM   1099 O  O   . SER A 1 139 ? -17.670 40.304 13.621  1.00 17.40  ? 139 SER A O   1 
ATOM   1100 C  CB  . SER A 1 139 ? -17.474 37.884 15.182  1.00 17.54  ? 139 SER A CB  1 
ATOM   1101 O  OG  . SER A 1 139 ? -18.866 37.915 15.523  1.00 19.92  ? 139 SER A OG  1 
ATOM   1102 N  N   . PHE A 1 140 ? -18.665 39.084 12.045  1.00 16.89  ? 140 PHE A N   1 
ATOM   1103 C  CA  . PHE A 1 140 ? -19.185 40.228 11.263  1.00 17.28  ? 140 PHE A CA  1 
ATOM   1104 C  C   . PHE A 1 140 ? -20.563 39.892 10.713  1.00 18.45  ? 140 PHE A C   1 
ATOM   1105 O  O   . PHE A 1 140 ? -20.778 38.794 10.193  1.00 19.26  ? 140 PHE A O   1 
ATOM   1106 C  CB  . PHE A 1 140 ? -18.242 40.490 10.100  1.00 17.31  ? 140 PHE A CB  1 
ATOM   1107 C  CG  . PHE A 1 140 ? -16.895 41.090 10.369  1.00 17.08  ? 140 PHE A CG  1 
ATOM   1108 C  CD1 . PHE A 1 140 ? -16.731 42.274 11.052  1.00 18.00  ? 140 PHE A CD1 1 
ATOM   1109 C  CD2 . PHE A 1 140 ? -15.765 40.443 9.899   1.00 17.83  ? 140 PHE A CD2 1 
ATOM   1110 C  CE1 . PHE A 1 140 ? -15.503 42.875 11.177  1.00 17.95  ? 140 PHE A CE1 1 
ATOM   1111 C  CE2 . PHE A 1 140 ? -14.523 41.015 10.084  1.00 18.13  ? 140 PHE A CE2 1 
ATOM   1112 C  CZ  . PHE A 1 140 ? -14.404 42.248 10.659  1.00 18.12  ? 140 PHE A CZ  1 
ATOM   1113 N  N   . LEU A 1 141 ? -21.449 40.874 10.857  1.00 20.04  ? 141 LEU A N   1 
ATOM   1114 C  CA  . LEU A 1 141 ? -22.816 40.837 10.314  1.00 22.58  ? 141 LEU A CA  1 
ATOM   1115 C  C   . LEU A 1 141 ? -22.971 41.784 9.132   1.00 22.49  ? 141 LEU A C   1 
ATOM   1116 O  O   . LEU A 1 141 ? -22.055 42.545 8.799   1.00 21.77  ? 141 LEU A O   1 
ATOM   1117 C  CB  . LEU A 1 141 ? -23.759 41.188 11.460  1.00 24.23  ? 141 LEU A CB  1 
ATOM   1118 C  CG  . LEU A 1 141 ? -23.649 40.254 12.659  1.00 24.61  ? 141 LEU A CG  1 
ATOM   1119 C  CD1 . LEU A 1 141 ? -24.480 40.796 13.806  1.00 27.30  ? 141 LEU A CD1 1 
ATOM   1120 C  CD2 . LEU A 1 141 ? -24.109 38.836 12.323  1.00 25.61  ? 141 LEU A CD2 1 
ATOM   1121 N  N   . ASN A 1 142 ? -24.122 41.707 8.463   1.00 23.11  ? 142 ASN A N   1 
ATOM   1122 C  CA  A ASN A 1 142 ? -24.463 42.674 7.392   0.50 24.01  ? 142 ASN A CA  1 
ATOM   1123 C  CA  B ASN A 1 142 ? -24.518 42.686 7.420   0.50 24.35  ? 142 ASN A CA  1 
ATOM   1124 C  C   . ASN A 1 142 ? -24.161 44.090 7.920   1.00 21.53  ? 142 ASN A C   1 
ATOM   1125 O  O   . ASN A 1 142 ? -24.554 44.430 9.084   1.00 25.48  ? 142 ASN A O   1 
ATOM   1126 C  CB  A ASN A 1 142 ? -25.893 42.455 6.894   0.50 25.98  ? 142 ASN A CB  1 
ATOM   1127 C  CB  B ASN A 1 142 ? -26.015 42.611 7.115   0.50 26.81  ? 142 ASN A CB  1 
ATOM   1128 C  CG  A ASN A 1 142 ? -26.268 43.408 5.781   0.50 26.94  ? 142 ASN A CG  1 
ATOM   1129 C  CG  B ASN A 1 142 ? -26.446 41.338 6.422   0.50 29.29  ? 142 ASN A CG  1 
ATOM   1130 O  OD1 A ASN A 1 142 ? -25.491 43.646 4.862   0.50 31.44  ? 142 ASN A OD1 1 
ATOM   1131 O  OD1 B ASN A 1 142 ? -27.632 41.154 6.168   0.50 34.21  ? 142 ASN A OD1 1 
ATOM   1132 N  ND2 A ASN A 1 142 ? -27.459 43.979 5.873   0.50 31.40  ? 142 ASN A ND2 1 
ATOM   1133 N  ND2 B ASN A 1 142 ? -25.522 40.446 6.119   0.50 26.97  ? 142 ASN A ND2 1 
ATOM   1134 N  N   . GLY A 1 143 ? -23.477 44.907 7.117   1.00 19.50  ? 143 GLY A N   1 
ATOM   1135 C  CA  . GLY A 1 143 ? -23.172 46.300 7.444   1.00 20.39  ? 143 GLY A CA  1 
ATOM   1136 C  C   . GLY A 1 143 ? -21.839 46.485 8.144   1.00 21.68  ? 143 GLY A C   1 
ATOM   1137 O  O   . GLY A 1 143 ? -21.524 47.607 8.462   1.00 20.31  ? 143 GLY A O   1 
ATOM   1138 N  N   . SER A 1 144 ? -21.070 45.413 8.355   1.00 19.03  ? 144 SER A N   1 
ATOM   1139 C  CA  . SER A 1 144 ? -19.784 45.512 9.077   1.00 19.35  ? 144 SER A CA  1 
ATOM   1140 C  C   . SER A 1 144 ? -18.676 45.967 8.123   1.00 18.24  ? 144 SER A C   1 
ATOM   1141 O  O   . SER A 1 144 ? -17.624 46.329 8.598   1.00 17.30  ? 144 SER A O   1 
ATOM   1142 C  CB  . SER A 1 144 ? -19.393 44.170 9.633   1.00 17.44  ? 144 SER A CB  1 
ATOM   1143 O  OG  . SER A 1 144 ? -19.389 43.227 8.603   1.00 19.51  ? 144 SER A OG  1 
ATOM   1144 N  N   . CYS A 1 145 ? -18.941 45.966 6.827   1.00 18.02  ? 145 CYS A N   1 
ATOM   1145 C  CA  . CYS A 1 145 ? -17.904 46.312 5.841   1.00 19.32  ? 145 CYS A CA  1 
ATOM   1146 C  C   . CYS A 1 145 ? -17.326 47.690 6.134   1.00 18.19  ? 145 CYS A C   1 
ATOM   1147 O  O   . CYS A 1 145 ? -18.069 48.649 6.537   1.00 19.23  ? 145 CYS A O   1 
ATOM   1148 C  CB  . CYS A 1 145 ? -18.478 46.234 4.439   1.00 20.48  ? 145 CYS A CB  1 
ATOM   1149 S  SG  . CYS A 1 145 ? -19.060 44.617 4.020   1.00 24.88  ? 145 CYS A SG  1 
ATOM   1150 N  N   . GLY A 1 146 ? -16.003 47.839 6.017   1.00 15.65  ? 146 GLY A N   1 
ATOM   1151 C  CA  . GLY A 1 146 ? -15.276 49.045 6.389   1.00 17.27  ? 146 GLY A CA  1 
ATOM   1152 C  C   . GLY A 1 146 ? -14.746 49.025 7.817   1.00 16.77  ? 146 GLY A C   1 
ATOM   1153 O  O   . GLY A 1 146 ? -13.929 49.904 8.174   1.00 17.70  ? 146 GLY A O   1 
ATOM   1154 N  N   . SER A 1 147 ? -15.213 48.106 8.668   1.00 16.10  ? 147 SER A N   1 
ATOM   1155 C  CA  . SER A 1 147 ? -14.556 47.850 9.991   1.00 16.36  ? 147 SER A CA  1 
ATOM   1156 C  C   . SER A 1 147 ? -13.069 47.534 9.727   1.00 15.21  ? 147 SER A C   1 
ATOM   1157 O  O   . SER A 1 147 ? -12.749 46.893 8.702   1.00 15.94  ? 147 SER A O   1 
ATOM   1158 C  CB  . SER A 1 147 ? -15.197 46.708 10.681  1.00 16.60  ? 147 SER A CB  1 
ATOM   1159 O  OG  . SER A 1 147 ? -16.564 46.906 11.039  1.00 18.45  ? 147 SER A OG  1 
ATOM   1160 N  N   . VAL A 1 148 ? -12.197 47.940 10.631  1.00 16.30  ? 148 VAL A N   1 
ATOM   1161 C  CA  . VAL A 1 148 ? -10.746 47.790 10.460  1.00 14.51  ? 148 VAL A CA  1 
ATOM   1162 C  C   . VAL A 1 148 ? -10.106 46.945 11.537  1.00 15.70  ? 148 VAL A C   1 
ATOM   1163 O  O   . VAL A 1 148 ? -10.615 46.823 12.638  1.00 16.75  ? 148 VAL A O   1 
ATOM   1164 C  CB  . VAL A 1 148 ? -10.029 49.121 10.350  1.00 16.35  ? 148 VAL A CB  1 
ATOM   1165 C  CG1 . VAL A 1 148 ? -10.540 49.901 9.130   1.00 16.37  ? 148 VAL A CG1 1 
ATOM   1166 C  CG2 . VAL A 1 148 ? -10.091 49.906 11.603  1.00 18.26  ? 148 VAL A CG2 1 
ATOM   1167 N  N   . GLY A 1 149 ? -8.983  46.382 11.110  1.00 15.47  ? 149 GLY A N   1 
ATOM   1168 C  CA  . GLY A 1 149 ? -8.094  45.622 11.979  1.00 14.37  ? 149 GLY A CA  1 
ATOM   1169 C  C   . GLY A 1 149 ? -6.790  46.383 12.130  1.00 15.50  ? 149 GLY A C   1 
ATOM   1170 O  O   . GLY A 1 149 ? -6.355  47.115 11.189  1.00 15.36  ? 149 GLY A O   1 
ATOM   1171 N  N   . PHE A 1 150 ? -6.185  46.261 13.306  1.00 15.56  ? 150 PHE A N   1 
ATOM   1172 C  CA  . PHE A 1 150 ? -5.056  47.122 13.688  1.00 16.39  ? 150 PHE A CA  1 
ATOM   1173 C  C   . PHE A 1 150 ? -4.232  46.465 14.796  1.00 16.75  ? 150 PHE A C   1 
ATOM   1174 O  O   . PHE A 1 150 ? -4.727  45.587 15.485  1.00 17.33  ? 150 PHE A O   1 
ATOM   1175 C  CB  . PHE A 1 150 ? -5.486  48.524 14.107  1.00 16.64  ? 150 PHE A CB  1 
ATOM   1176 C  CG  . PHE A 1 150 ? -6.412  48.505 15.289  1.00 17.52  ? 150 PHE A CG  1 
ATOM   1177 C  CD1 . PHE A 1 150 ? -7.740  48.132 15.167  1.00 17.28  ? 150 PHE A CD1 1 
ATOM   1178 C  CD2 . PHE A 1 150 ? -5.876  48.692 16.557  1.00 19.08  ? 150 PHE A CD2 1 
ATOM   1179 C  CE1 . PHE A 1 150 ? -8.542  47.996 16.299  1.00 20.15  ? 150 PHE A CE1 1 
ATOM   1180 C  CE2 . PHE A 1 150 ? -6.693  48.637 17.677  1.00 20.65  ? 150 PHE A CE2 1 
ATOM   1181 C  CZ  . PHE A 1 150 ? -7.989  48.242 17.554  1.00 21.05  ? 150 PHE A CZ  1 
ATOM   1182 N  N   . ASN A 1 151 ? -3.001  46.931 14.898  1.00 17.52  ? 151 ASN A N   1 
ATOM   1183 C  CA  . ASN A 1 151 ? -2.107  46.700 16.058  1.00 19.68  ? 151 ASN A CA  1 
ATOM   1184 C  C   . ASN A 1 151 ? -1.686  48.075 16.557  1.00 20.25  ? 151 ASN A C   1 
ATOM   1185 O  O   . ASN A 1 151 ? -1.834  49.053 15.841  1.00 20.41  ? 151 ASN A O   1 
ATOM   1186 C  CB  . ASN A 1 151 ? -0.914  45.830 15.670  1.00 20.69  ? 151 ASN A CB  1 
ATOM   1187 C  CG  . ASN A 1 151 ? -1.343  44.384 15.524  1.00 23.51  ? 151 ASN A CG  1 
ATOM   1188 O  OD1 . ASN A 1 151 ? -1.840  43.799 16.493  1.00 29.03  ? 151 ASN A OD1 1 
ATOM   1189 N  ND2 . ASN A 1 151 ? -1.405  43.885 14.306  1.00 20.91  ? 151 ASN A ND2 1 
ATOM   1190 N  N   . ILE A 1 152 ? -1.286  48.171 17.814  1.00 20.53  ? 152 ILE A N   1 
ATOM   1191 C  CA  . ILE A 1 152 ? -0.809  49.465 18.352  1.00 23.57  ? 152 ILE A CA  1 
ATOM   1192 C  C   . ILE A 1 152 ? 0.595   49.192 18.864  1.00 29.04  ? 152 ILE A C   1 
ATOM   1193 O  O   . ILE A 1 152 ? 0.804   48.164 19.506  1.00 28.30  ? 152 ILE A O   1 
ATOM   1194 C  CB  . ILE A 1 152 ? -1.755  50.021 19.435  1.00 27.01  ? 152 ILE A CB  1 
ATOM   1195 C  CG1 . ILE A 1 152 ? -3.162  50.222 18.888  1.00 28.91  ? 152 ILE A CG1 1 
ATOM   1196 C  CG2 . ILE A 1 152 ? -1.160  51.317 19.975  1.00 27.37  ? 152 ILE A CG2 1 
ATOM   1197 C  CD1 . ILE A 1 152 ? -4.154  50.793 19.882  1.00 34.54  ? 152 ILE A CD1 1 
ATOM   1198 N  N   . ASP A 1 153 ? 1.530   50.056 18.501  1.00 32.24  ? 153 ASP A N   1 
ATOM   1199 C  CA  . ASP A 1 153 ? 2.906   50.057 19.046  1.00 36.29  ? 153 ASP A CA  1 
ATOM   1200 C  C   . ASP A 1 153 ? 3.112   51.452 19.631  1.00 35.75  ? 153 ASP A C   1 
ATOM   1201 O  O   . ASP A 1 153 ? 3.116   52.413 18.865  1.00 36.35  ? 153 ASP A O   1 
ATOM   1202 C  CB  . ASP A 1 153 ? 3.908   49.730 17.946  1.00 44.05  ? 153 ASP A CB  1 
ATOM   1203 C  CG  . ASP A 1 153 ? 5.336   49.580 18.444  1.00 55.04  ? 153 ASP A CG  1 
ATOM   1204 O  OD1 . ASP A 1 153 ? 5.521   49.432 19.681  1.00 57.19  ? 153 ASP A OD1 1 
ATOM   1205 O  OD2 . ASP A 1 153 ? 6.253   49.581 17.586  1.00 64.26  ? 153 ASP A OD2 1 
ATOM   1206 N  N   . TYR A 1 154 ? 3.233   51.541 20.950  1.00 44.41  ? 154 TYR A N   1 
ATOM   1207 C  CA  . TYR A 1 154 ? 3.337   52.813 21.695  1.00 44.96  ? 154 TYR A CA  1 
ATOM   1208 C  C   . TYR A 1 154 ? 2.038   53.582 21.468  1.00 39.97  ? 154 TYR A C   1 
ATOM   1209 O  O   . TYR A 1 154 ? 1.008   53.093 21.902  1.00 45.40  ? 154 TYR A O   1 
ATOM   1210 C  CB  . TYR A 1 154 ? 4.619   53.542 21.286  1.00 57.80  ? 154 TYR A CB  1 
ATOM   1211 C  CG  . TYR A 1 154 ? 5.417   54.041 22.462  1.00 76.90  ? 154 TYR A CG  1 
ATOM   1212 C  CD1 . TYR A 1 154 ? 5.493   55.397 22.767  1.00 89.00  ? 154 TYR A CD1 1 
ATOM   1213 C  CD2 . TYR A 1 154 ? 6.081   53.146 23.289  1.00 82.53  ? 154 TYR A CD2 1 
ATOM   1214 C  CE1 . TYR A 1 154 ? 6.227   55.852 23.854  1.00 92.35  ? 154 TYR A CE1 1 
ATOM   1215 C  CE2 . TYR A 1 154 ? 6.817   53.584 24.378  1.00 90.27  ? 154 TYR A CE2 1 
ATOM   1216 C  CZ  . TYR A 1 154 ? 6.890   54.941 24.663  1.00 95.40  ? 154 TYR A CZ  1 
ATOM   1217 O  OH  . TYR A 1 154 ? 7.607   55.374 25.742  1.00 92.67  ? 154 TYR A OH  1 
ATOM   1218 N  N   . ASP A 1 155 ? 2.102   54.747 20.826  1.00 36.43  ? 155 ASP A N   1 
ATOM   1219 C  CA  . ASP A 1 155 ? 0.924   55.624 20.593  1.00 39.25  ? 155 ASP A CA  1 
ATOM   1220 C  C   . ASP A 1 155 ? 0.496   55.518 19.122  1.00 32.32  ? 155 ASP A C   1 
ATOM   1221 O  O   . ASP A 1 155 ? -0.391  56.290 18.714  1.00 32.01  ? 155 ASP A O   1 
ATOM   1222 C  CB  . ASP A 1 155 ? 1.258   57.071 20.980  1.00 47.27  ? 155 ASP A CB  1 
ATOM   1223 C  CG  . ASP A 1 155 ? 2.547   57.595 20.355  1.00 52.32  ? 155 ASP A CG  1 
ATOM   1224 O  OD1 . ASP A 1 155 ? 3.229   56.816 19.629  1.00 49.09  ? 155 ASP A OD1 1 
ATOM   1225 O  OD2 . ASP A 1 155 ? 2.865   58.782 20.599  1.00 63.92  ? 155 ASP A OD2 1 
ATOM   1226 N  N   . CYS A 1 156 ? 1.101   54.599 18.357  1.00 28.31  ? 156 CYS A N   1 
ATOM   1227 C  CA  . CYS A 1 156 ? 0.946   54.576 16.879  1.00 26.83  ? 156 CYS A CA  1 
ATOM   1228 C  C   . CYS A 1 156 ? 0.094   53.394 16.439  1.00 24.08  ? 156 CYS A C   1 
ATOM   1229 O  O   . CYS A 1 156 ? 0.456   52.234 16.764  1.00 22.79  ? 156 CYS A O   1 
ATOM   1230 C  CB  . CYS A 1 156 ? 2.286   54.478 16.191  1.00 28.37  ? 156 CYS A CB  1 
ATOM   1231 S  SG  . CYS A 1 156 ? 2.128   54.627 14.392  1.00 31.01  ? 156 CYS A SG  1 
ATOM   1232 N  N   . VAL A 1 157 ? -0.997  53.684 15.754  1.00 19.16  ? 157 VAL A N   1 
ATOM   1233 C  CA  . VAL A 1 157 ? -1.904  52.638 15.232  1.00 19.84  ? 157 VAL A CA  1 
ATOM   1234 C  C   . VAL A 1 157 ? -1.403  52.174 13.857  1.00 19.89  ? 157 VAL A C   1 
ATOM   1235 O  O   . VAL A 1 157 ? -1.312  52.999 12.922  1.00 19.30  ? 157 VAL A O   1 
ATOM   1236 C  CB  . VAL A 1 157 ? -3.341  53.131 15.155  1.00 19.53  ? 157 VAL A CB  1 
ATOM   1237 C  CG1 . VAL A 1 157 ? -4.277  52.064 14.684  1.00 19.88  ? 157 VAL A CG1 1 
ATOM   1238 C  CG2 . VAL A 1 157 ? -3.773  53.737 16.492  1.00 22.69  ? 157 VAL A CG2 1 
ATOM   1239 N  N   . SER A 1 158 ? -1.093  50.899 13.761  1.00 17.97  ? 158 SER A N   1 
ATOM   1240 C  CA  . SER A 1 158 ? -0.763  50.227 12.475  1.00 17.75  ? 158 SER A CA  1 
ATOM   1241 C  C   . SER A 1 158 ? -2.015  49.576 11.951  1.00 19.04  ? 158 SER A C   1 
ATOM   1242 O  O   . SER A 1 158 ? -2.334  48.496 12.455  1.00 18.40  ? 158 SER A O   1 
ATOM   1243 C  CB  . SER A 1 158 ? 0.338   49.224 12.645  1.00 19.09  ? 158 SER A CB  1 
ATOM   1244 O  OG  . SER A 1 158 ? 1.542   49.947 12.881  1.00 23.21  ? 158 SER A OG  1 
ATOM   1245 N  N   . PHE A 1 159 ? -2.685  50.222 11.000  1.00 16.83  ? 159 PHE A N   1 
ATOM   1246 C  CA  . PHE A 1 159 ? -3.879  49.639 10.371  1.00 16.34  ? 159 PHE A CA  1 
ATOM   1247 C  C   . PHE A 1 159 ? -3.417  48.595 9.367   1.00 15.54  ? 159 PHE A C   1 
ATOM   1248 O  O   . PHE A 1 159 ? -2.563  48.898 8.487   1.00 16.81  ? 159 PHE A O   1 
ATOM   1249 C  CB  . PHE A 1 159 ? -4.704  50.712 9.672   1.00 17.07  ? 159 PHE A CB  1 
ATOM   1250 C  CG  . PHE A 1 159 ? -5.288  51.725 10.612  1.00 17.57  ? 159 PHE A CG  1 
ATOM   1251 C  CD1 . PHE A 1 159 ? -6.412  51.391 11.328  1.00 17.48  ? 159 PHE A CD1 1 
ATOM   1252 C  CD2 . PHE A 1 159 ? -4.768  52.994 10.760  1.00 17.67  ? 159 PHE A CD2 1 
ATOM   1253 C  CE1 . PHE A 1 159 ? -7.014  52.296 12.179  1.00 17.44  ? 159 PHE A CE1 1 
ATOM   1254 C  CE2 . PHE A 1 159 ? -5.363  53.897 11.618  1.00 17.04  ? 159 PHE A CE2 1 
ATOM   1255 C  CZ  . PHE A 1 159 ? -6.479  53.536 12.343  1.00 18.18  ? 159 PHE A CZ  1 
ATOM   1256 N  N   . CYS A 1 160 ? -3.996  47.409 9.442   1.00 15.35  ? 160 CYS A N   1 
ATOM   1257 C  CA  . CYS A 1 160 ? -3.580  46.290 8.564   1.00 16.77  ? 160 CYS A CA  1 
ATOM   1258 C  C   . CYS A 1 160 ? -4.745  45.707 7.795   1.00 17.23  ? 160 CYS A C   1 
ATOM   1259 O  O   . CYS A 1 160 ? -4.510  44.874 6.913   1.00 18.08  ? 160 CYS A O   1 
ATOM   1260 C  CB  . CYS A 1 160 ? -2.837  45.192 9.325   1.00 17.32  ? 160 CYS A CB  1 
ATOM   1261 S  SG  . CYS A 1 160 ? -3.738  44.525 10.742  1.00 17.31  ? 160 CYS A SG  1 
ATOM   1262 N  N   . TYR A 1 161 ? -5.998  45.973 8.158   1.00 15.10  ? 161 TYR A N   1 
ATOM   1263 C  CA  . TYR A 1 161 ? -7.122  45.232 7.542   1.00 15.91  ? 161 TYR A CA  1 
ATOM   1264 C  C   . TYR A 1 161 ? -8.318  46.161 7.447   1.00 15.43  ? 161 TYR A C   1 
ATOM   1265 O  O   . TYR A 1 161 ? -8.601  46.907 8.423   1.00 15.71  ? 161 TYR A O   1 
ATOM   1266 C  CB  . TYR A 1 161 ? -7.464  43.961 8.335   1.00 15.82  ? 161 TYR A CB  1 
ATOM   1267 C  CG  . TYR A 1 161 ? -8.663  43.173 7.852   1.00 14.17  ? 161 TYR A CG  1 
ATOM   1268 C  CD1 . TYR A 1 161 ? -8.527  42.262 6.828   1.00 13.95  ? 161 TYR A CD1 1 
ATOM   1269 C  CD2 . TYR A 1 161 ? -9.942  43.327 8.386   1.00 13.60  ? 161 TYR A CD2 1 
ATOM   1270 C  CE1 . TYR A 1 161 ? -9.564  41.453 6.426   1.00 13.86  ? 161 TYR A CE1 1 
ATOM   1271 C  CE2 . TYR A 1 161 ? -11.004 42.566 7.941   1.00 14.85  ? 161 TYR A CE2 1 
ATOM   1272 C  CZ  . TYR A 1 161 ? -10.842 41.662 6.923   1.00 13.59  ? 161 TYR A CZ  1 
ATOM   1273 O  OH  . TYR A 1 161 ? -11.838 40.882 6.408   1.00 16.26  ? 161 TYR A OH  1 
ATOM   1274 N  N   . MET A 1 162 ? -9.005  46.094 6.311   1.00 14.06  ? 162 MET A N   1 
ATOM   1275 C  CA  . MET A 1 162 ? -10.373 46.644 6.144   1.00 14.30  ? 162 MET A CA  1 
ATOM   1276 C  C   . MET A 1 162 ? -11.283 45.524 5.652   1.00 14.39  ? 162 MET A C   1 
ATOM   1277 O  O   . MET A 1 162 ? -10.928 44.770 4.763   1.00 14.33  ? 162 MET A O   1 
ATOM   1278 C  CB  . MET A 1 162 ? -10.430 47.850 5.216   1.00 16.66  ? 162 MET A CB  1 
ATOM   1279 C  CG  . MET A 1 162 ? -11.817 48.381 5.208   1.00 17.56  ? 162 MET A CG  1 
ATOM   1280 S  SD  . MET A 1 162 ? -11.922 49.958 4.282   1.00 19.79  ? 162 MET A SD  1 
ATOM   1281 C  CE  . MET A 1 162 ? -11.536 51.113 5.577   1.00 22.27  ? 162 MET A CE  1 
ATOM   1282 N  N   . HIS A 1 163 ? -12.432 45.390 6.312   1.00 14.51  ? 163 HIS A N   1 
ATOM   1283 C  CA  . HIS A 1 163 ? -13.378 44.289 6.068   1.00 14.42  ? 163 HIS A CA  1 
ATOM   1284 C  C   . HIS A 1 163 ? -14.185 44.562 4.795   1.00 15.55  ? 163 HIS A C   1 
ATOM   1285 O  O   . HIS A 1 163 ? -14.790 45.636 4.707   1.00 16.73  ? 163 HIS A O   1 
ATOM   1286 C  CB  . HIS A 1 163 ? -14.330 44.131 7.242   1.00 14.66  ? 163 HIS A CB  1 
ATOM   1287 C  CG  . HIS A 1 163 ? -15.206 42.953 7.006   1.00 15.27  ? 163 HIS A CG  1 
ATOM   1288 N  ND1 . HIS A 1 163 ? -14.719 41.727 6.636   1.00 14.85  ? 163 HIS A ND1 1 
ATOM   1289 C  CD2 . HIS A 1 163 ? -16.553 42.844 7.021   1.00 15.77  ? 163 HIS A CD2 1 
ATOM   1290 C  CE1 . HIS A 1 163 ? -15.715 40.897 6.440   1.00 16.45  ? 163 HIS A CE1 1 
ATOM   1291 N  NE2 . HIS A 1 163 ? -16.878 41.571 6.709   1.00 15.42  ? 163 HIS A NE2 1 
ATOM   1292 N  N   . HIS A 1 164 ? -14.206 43.615 3.881   1.00 16.55  ? 164 HIS A N   1 
ATOM   1293 C  CA  . HIS A 1 164 ? -14.967 43.752 2.618   1.00 15.91  ? 164 HIS A CA  1 
ATOM   1294 C  C   . HIS A 1 164 ? -16.042 42.709 2.420   1.00 19.13  ? 164 HIS A C   1 
ATOM   1295 O  O   . HIS A 1 164 ? -17.044 43.053 1.791   1.00 22.62  ? 164 HIS A O   1 
ATOM   1296 C  CB  . HIS A 1 164 ? -14.113 43.734 1.376   1.00 14.75  ? 164 HIS A CB  1 
ATOM   1297 C  CG  . HIS A 1 164 ? -13.274 44.928 1.218   1.00 16.18  ? 164 HIS A CG  1 
ATOM   1298 N  ND1 . HIS A 1 164 ? -13.381 45.750 0.107   1.00 17.02  ? 164 HIS A ND1 1 
ATOM   1299 C  CD2 . HIS A 1 164 ? -12.255 45.421 1.972   1.00 15.87  ? 164 HIS A CD2 1 
ATOM   1300 C  CE1 . HIS A 1 164 ? -12.515 46.741 0.250   1.00 16.55  ? 164 HIS A CE1 1 
ATOM   1301 N  NE2 . HIS A 1 164 ? -11.760 46.538 1.361   1.00 15.86  ? 164 HIS A NE2 1 
ATOM   1302 N  N   A MET A 1 165 ? -15.858 41.466 2.832   0.50 17.83  ? 165 MET A N   1 
ATOM   1303 N  N   B MET A 1 165 ? -15.872 41.474 2.895   0.50 18.87  ? 165 MET A N   1 
ATOM   1304 C  CA  A MET A 1 165 ? -16.938 40.510 2.532   0.50 19.89  ? 165 MET A CA  1 
ATOM   1305 C  CA  B MET A 1 165 ? -16.590 40.326 2.291   0.50 21.44  ? 165 MET A CA  1 
ATOM   1306 C  C   A MET A 1 165 ? -16.849 39.252 3.369   0.50 19.44  ? 165 MET A C   1 
ATOM   1307 C  C   B MET A 1 165 ? -16.770 39.158 3.274   0.50 20.31  ? 165 MET A C   1 
ATOM   1308 O  O   A MET A 1 165 ? -15.814 38.969 4.002   0.50 17.45  ? 165 MET A O   1 
ATOM   1309 O  O   B MET A 1 165 ? -15.804 38.807 3.958   0.50 17.45  ? 165 MET A O   1 
ATOM   1310 C  CB  A MET A 1 165 ? -16.894 40.108 1.060   0.50 20.86  ? 165 MET A CB  1 
ATOM   1311 C  CB  B MET A 1 165 ? -15.758 39.870 1.089   0.50 25.19  ? 165 MET A CB  1 
ATOM   1312 C  CG  A MET A 1 165 ? -15.583 39.520 0.710   0.50 23.35  ? 165 MET A CG  1 
ATOM   1313 C  CG  B MET A 1 165 ? -16.216 38.574 0.516   0.50 28.10  ? 165 MET A CG  1 
ATOM   1314 S  SD  A MET A 1 165 ? -15.290 39.636 -1.049  0.50 27.23  ? 165 MET A SD  1 
ATOM   1315 S  SD  B MET A 1 165 ? -17.651 38.888 -0.504  0.50 33.96  ? 165 MET A SD  1 
ATOM   1316 C  CE  A MET A 1 165 ? -16.774 38.920 -1.743  0.50 25.06  ? 165 MET A CE  1 
ATOM   1317 C  CE  B MET A 1 165 ? -17.304 40.540 -1.132  0.50 30.05  ? 165 MET A CE  1 
ATOM   1318 N  N   . GLU A 1 166 ? -17.941 38.523 3.319   1.00 19.51  ? 166 GLU A N   1 
ATOM   1319 C  CA  . GLU A 1 166 ? -18.053 37.203 3.960   1.00 18.48  ? 166 GLU A CA  1 
ATOM   1320 C  C   . GLU A 1 166 ? -18.091 36.167 2.849   1.00 19.72  ? 166 GLU A C   1 
ATOM   1321 O  O   . GLU A 1 166 ? -18.913 36.335 1.911   1.00 22.34  ? 166 GLU A O   1 
ATOM   1322 C  CB  . GLU A 1 166 ? -19.270 37.180 4.881   1.00 18.30  ? 166 GLU A CB  1 
ATOM   1323 C  CG  . GLU A 1 166 ? -19.386 35.847 5.581   1.00 20.73  ? 166 GLU A CG  1 
ATOM   1324 C  CD  . GLU A 1 166 ? -20.397 35.766 6.710   1.00 23.74  ? 166 GLU A CD  1 
ATOM   1325 O  OE1 . GLU A 1 166 ? -21.345 34.949 6.560   1.00 28.90  ? 166 GLU A OE1 1 
ATOM   1326 O  OE2 . GLU A 1 166 ? -20.205 36.415 7.736   1.00 22.31  ? 166 GLU A OE2 1 
ATOM   1327 N  N   . LEU A 1 167 ? -17.301 35.114 2.993   1.00 19.14  ? 167 LEU A N   1 
ATOM   1328 C  CA  . LEU A 1 167 ? -17.249 33.955 2.095   1.00 21.31  ? 167 LEU A CA  1 
ATOM   1329 C  C   . LEU A 1 167 ? -18.265 32.911 2.516   1.00 22.35  ? 167 LEU A C   1 
ATOM   1330 O  O   . LEU A 1 167 ? -18.818 32.965 3.626   1.00 23.04  ? 167 LEU A O   1 
ATOM   1331 C  CB  . LEU A 1 167 ? -15.826 33.413 2.079   1.00 22.21  ? 167 LEU A CB  1 
ATOM   1332 C  CG  . LEU A 1 167 ? -14.812 34.380 1.491   1.00 22.20  ? 167 LEU A CG  1 
ATOM   1333 C  CD1 . LEU A 1 167 ? -13.411 33.896 1.829   1.00 21.72  ? 167 LEU A CD1 1 
ATOM   1334 C  CD2 . LEU A 1 167 ? -14.990 34.471 -0.014  1.00 25.37  ? 167 LEU A CD2 1 
ATOM   1335 N  N   . PRO A 1 168 ? -18.592 31.965 1.618   1.00 25.91  ? 168 PRO A N   1 
ATOM   1336 C  CA  . PRO A 1 168 ? -19.672 31.009 1.898   1.00 26.91  ? 168 PRO A CA  1 
ATOM   1337 C  C   . PRO A 1 168 ? -19.520 30.145 3.154   1.00 27.31  ? 168 PRO A C   1 
ATOM   1338 O  O   . PRO A 1 168 ? -20.536 29.823 3.714   1.00 26.69  ? 168 PRO A O   1 
ATOM   1339 C  CB  . PRO A 1 168 ? -19.702 30.143 0.637   1.00 28.19  ? 168 PRO A CB  1 
ATOM   1340 C  CG  . PRO A 1 168 ? -19.189 31.040 -0.438  1.00 28.94  ? 168 PRO A CG  1 
ATOM   1341 C  CD  . PRO A 1 168 ? -18.115 31.893 0.232   1.00 24.32  ? 168 PRO A CD  1 
ATOM   1342 N  N   . THR A 1 169 ? -18.300 29.868 3.636   1.00 24.98  ? 169 THR A N   1 
ATOM   1343 C  CA  . THR A 1 169 ? -18.042 29.085 4.876   1.00 27.28  ? 169 THR A CA  1 
ATOM   1344 C  C   . THR A 1 169 ? -18.189 29.968 6.129   1.00 23.87  ? 169 THR A C   1 
ATOM   1345 O  O   . THR A 1 169 ? -18.021 29.446 7.229   1.00 24.76  ? 169 THR A O   1 
ATOM   1346 C  CB  . THR A 1 169 ? -16.659 28.412 4.864   1.00 26.71  ? 169 THR A CB  1 
ATOM   1347 O  OG1 . THR A 1 169 ? -15.664 29.358 4.471   1.00 26.29  ? 169 THR A OG1 1 
ATOM   1348 C  CG2 . THR A 1 169 ? -16.611 27.235 3.924   1.00 27.77  ? 169 THR A CG2 1 
ATOM   1349 N  N   . GLY A 1 170 ? -18.468 31.259 5.969   1.00 20.30  ? 170 GLY A N   1 
ATOM   1350 C  CA  . GLY A 1 170 ? -18.692 32.207 7.064   1.00 21.95  ? 170 GLY A CA  1 
ATOM   1351 C  C   . GLY A 1 170 ? -17.407 32.856 7.551   1.00 21.57  ? 170 GLY A C   1 
ATOM   1352 O  O   . GLY A 1 170 ? -17.427 33.453 8.610   1.00 23.10  ? 170 GLY A O   1 
ATOM   1353 N  N   . VAL A 1 171 ? -16.302 32.695 6.830   1.00 19.13  ? 171 VAL A N   1 
ATOM   1354 C  CA  . VAL A 1 171 ? -15.030 33.372 7.162   1.00 18.07  ? 171 VAL A CA  1 
ATOM   1355 C  C   . VAL A 1 171 ? -14.993 34.597 6.283   1.00 17.56  ? 171 VAL A C   1 
ATOM   1356 O  O   . VAL A 1 171 ? -15.915 34.783 5.417   1.00 17.09  ? 171 VAL A O   1 
ATOM   1357 C  CB  . VAL A 1 171 ? -13.812 32.467 6.917   1.00 16.55  ? 171 VAL A CB  1 
ATOM   1358 C  CG1 . VAL A 1 171 ? -13.897 31.226 7.801   1.00 19.37  ? 171 VAL A CG1 1 
ATOM   1359 C  CG2 . VAL A 1 171 ? -13.641 32.119 5.449   1.00 16.85  ? 171 VAL A CG2 1 
ATOM   1360 N  N   . HIS A 1 172 ? -14.007 35.442 6.513   1.00 15.69  ? 172 HIS A N   1 
ATOM   1361 C  CA  . HIS A 1 172 ? -14.065 36.852 6.064   1.00 16.13  ? 172 HIS A CA  1 
ATOM   1362 C  C   . HIS A 1 172 ? -12.845 37.214 5.220   1.00 16.95  ? 172 HIS A C   1 
ATOM   1363 O  O   . HIS A 1 172 ? -11.757 36.582 5.363   1.00 16.45  ? 172 HIS A O   1 
ATOM   1364 C  CB  . HIS A 1 172 ? -14.161 37.749 7.278   1.00 16.28  ? 172 HIS A CB  1 
ATOM   1365 C  CG  . HIS A 1 172 ? -15.418 37.479 8.016   1.00 16.51  ? 172 HIS A CG  1 
ATOM   1366 N  ND1 . HIS A 1 172 ? -15.426 36.789 9.241   1.00 16.18  ? 172 HIS A ND1 1 
ATOM   1367 C  CD2 . HIS A 1 172 ? -16.706 37.700 7.647   1.00 18.79  ? 172 HIS A CD2 1 
ATOM   1368 C  CE1 . HIS A 1 172 ? -16.704 36.630 9.620   1.00 16.78  ? 172 HIS A CE1 1 
ATOM   1369 N  NE2 . HIS A 1 172 ? -17.520 37.154 8.630   1.00 19.57  ? 172 HIS A NE2 1 
ATOM   1370 N  N   . ALA A 1 173 ? -13.049 38.143 4.282   1.00 15.70  ? 173 ALA A N   1 
ATOM   1371 C  CA  . ALA A 1 173 ? -11.978 38.581 3.395   1.00 15.31  ? 173 ALA A CA  1 
ATOM   1372 C  C   . ALA A 1 173 ? -11.988 40.077 3.321   1.00 16.42  ? 173 ALA A C   1 
ATOM   1373 O  O   . ALA A 1 173 ? -13.013 40.735 3.394   1.00 15.83  ? 173 ALA A O   1 
ATOM   1374 C  CB  . ALA A 1 173 ? -12.127 37.920 2.062   1.00 17.00  ? 173 ALA A CB  1 
ATOM   1375 N  N   . GLY A 1 174 ? -10.804 40.623 3.161   1.00 14.62  ? 174 GLY A N   1 
ATOM   1376 C  CA  . GLY A 1 174 ? -10.670 42.061 3.046   1.00 14.35  ? 174 GLY A CA  1 
ATOM   1377 C  C   . GLY A 1 174 ? -9.322  42.446 2.545   1.00 12.69  ? 174 GLY A C   1 
ATOM   1378 O  O   . GLY A 1 174 ? -8.604  41.611 2.013   1.00 14.14  ? 174 GLY A O   1 
ATOM   1379 N  N   . THR A 1 175 ? -9.010  43.703 2.730   1.00 14.11  ? 175 THR A N   1 
ATOM   1380 C  CA  . THR A 1 175 ? -7.864  44.339 2.098   1.00 14.15  ? 175 THR A CA  1 
ATOM   1381 C  C   . THR A 1 175 ? -6.963  44.929 3.157   1.00 14.45  ? 175 THR A C   1 
ATOM   1382 O  O   . THR A 1 175 ? -7.393  45.094 4.306   1.00 15.32  ? 175 THR A O   1 
ATOM   1383 C  CB  . THR A 1 175 ? -8.270  45.493 1.165   1.00 14.28  ? 175 THR A CB  1 
ATOM   1384 O  OG1 . THR A 1 175 ? -8.856  46.588 1.866   1.00 15.59  ? 175 THR A OG1 1 
ATOM   1385 C  CG2 . THR A 1 175 ? -9.120  44.960 0.037   1.00 15.09  ? 175 THR A CG2 1 
ATOM   1386 N  N   . ASP A 1 176 ? -5.741  45.295 2.758   1.00 12.95  ? 176 ASP A N   1 
ATOM   1387 C  CA  . ASP A 1 176 ? -4.947  46.259 3.518   1.00 14.40  ? 176 ASP A CA  1 
ATOM   1388 C  C   . ASP A 1 176 ? -5.558  47.667 3.295   1.00 15.24  ? 176 ASP A C   1 
ATOM   1389 O  O   . ASP A 1 176 ? -6.549  47.813 2.535   1.00 15.68  ? 176 ASP A O   1 
ATOM   1390 C  CB  . ASP A 1 176 ? -3.480  46.099 3.185   1.00 15.56  ? 176 ASP A CB  1 
ATOM   1391 C  CG  . ASP A 1 176 ? -3.042  46.429 1.797   1.00 18.81  ? 176 ASP A CG  1 
ATOM   1392 O  OD1 . ASP A 1 176 ? -3.733  47.207 1.094   1.00 16.47  ? 176 ASP A OD1 1 
ATOM   1393 O  OD2 . ASP A 1 176 ? -1.962  45.941 1.404   1.00 19.56  ? 176 ASP A OD2 1 
ATOM   1394 N  N   . LEU A 1 177 ? -4.988  48.676 3.956   1.00 16.30  ? 177 LEU A N   1 
ATOM   1395 C  CA  . LEU A 1 177 ? -5.569  50.044 3.876   1.00 16.85  ? 177 LEU A CA  1 
ATOM   1396 C  C   . LEU A 1 177 ? -5.114  50.720 2.590   1.00 17.90  ? 177 LEU A C   1 
ATOM   1397 O  O   . LEU A 1 177 ? -5.590  51.835 2.338   1.00 17.98  ? 177 LEU A O   1 
ATOM   1398 C  CB  . LEU A 1 177 ? -5.258  50.886 5.127   1.00 17.65  ? 177 LEU A CB  1 
ATOM   1399 C  CG  . LEU A 1 177 ? -6.369  50.806 6.189   1.00 17.68  ? 177 LEU A CG  1 
ATOM   1400 C  CD1 . LEU A 1 177 ? -7.645  51.474 5.720   1.00 19.42  ? 177 LEU A CD1 1 
ATOM   1401 C  CD2 . LEU A 1 177 ? -6.634  49.348 6.617   1.00 19.59  ? 177 LEU A CD2 1 
ATOM   1402 N  N   . GLU A 1 178 ? -4.286  50.068 1.767   1.00 17.33  ? 178 GLU A N   1 
ATOM   1403 C  CA  . GLU A 1 178 ? -4.035  50.562 0.394   1.00 19.22  ? 178 GLU A CA  1 
ATOM   1404 C  C   . GLU A 1 178 ? -4.984  49.928 -0.600  1.00 16.14  ? 178 GLU A C   1 
ATOM   1405 O  O   . GLU A 1 178 ? -4.826  50.178 -1.773  1.00 18.56  ? 178 GLU A O   1 
ATOM   1406 C  CB  . GLU A 1 178 ? -2.627  50.219 -0.063  1.00 20.58  ? 178 GLU A CB  1 
ATOM   1407 C  CG  . GLU A 1 178 ? -1.591  50.489 0.960   1.00 23.18  ? 178 GLU A CG  1 
ATOM   1408 C  CD  . GLU A 1 178 ? -1.324  51.933 1.185   1.00 24.96  ? 178 GLU A CD  1 
ATOM   1409 O  OE1 . GLU A 1 178 ? -1.896  52.792 0.470   1.00 26.86  ? 178 GLU A OE1 1 
ATOM   1410 O  OE2 . GLU A 1 178 ? -0.426  52.172 2.038   1.00 34.12  ? 178 GLU A OE2 1 
ATOM   1411 N  N   . GLY A 1 179 ? -5.948  49.152 -0.153  1.00 14.37  ? 179 GLY A N   1 
ATOM   1412 C  CA  . GLY A 1 179 ? -7.009  48.526 -0.930  1.00 16.94  ? 179 GLY A CA  1 
ATOM   1413 C  C   . GLY A 1 179 ? -6.627  47.256 -1.637  1.00 16.42  ? 179 GLY A C   1 
ATOM   1414 O  O   . GLY A 1 179 ? -7.341  46.821 -2.511  1.00 15.96  ? 179 GLY A O   1 
ATOM   1415 N  N   . ASN A 1 180 ? -5.503  46.651 -1.259  1.00 15.70  ? 180 ASN A N   1 
ATOM   1416 C  CA  . ASN A 1 180 ? -5.057  45.407 -1.903  1.00 16.87  ? 180 ASN A CA  1 
ATOM   1417 C  C   . ASN A 1 180 ? -5.583  44.234 -1.103  1.00 15.48  ? 180 ASN A C   1 
ATOM   1418 O  O   . ASN A 1 180 ? -5.218  44.109 0.112   1.00 15.00  ? 180 ASN A O   1 
ATOM   1419 C  CB  . ASN A 1 180 ? -3.552  45.370 -2.044  1.00 15.90  ? 180 ASN A CB  1 
ATOM   1420 C  CG  . ASN A 1 180 ? -3.034  46.551 -2.858  1.00 17.45  ? 180 ASN A CG  1 
ATOM   1421 O  OD1 . ASN A 1 180 ? -3.364  46.688 -4.015  1.00 20.06  ? 180 ASN A OD1 1 
ATOM   1422 N  ND2 . ASN A 1 180 ? -2.307  47.420 -2.217  1.00 18.84  ? 180 ASN A ND2 1 
ATOM   1423 N  N   . PHE A 1 181 ? -6.300  43.327 -1.745  1.00 14.77  ? 181 PHE A N   1 
ATOM   1424 C  CA  . PHE A 1 181 ? -6.897  42.169 -1.044  1.00 15.44  ? 181 PHE A CA  1 
ATOM   1425 C  C   . PHE A 1 181 ? -5.800  41.307 -0.423  1.00 15.48  ? 181 PHE A C   1 
ATOM   1426 O  O   . PHE A 1 181 ? -4.703  41.150 -0.988  1.00 14.93  ? 181 PHE A O   1 
ATOM   1427 C  CB  . PHE A 1 181 ? -7.788  41.291 -1.920  1.00 16.12  ? 181 PHE A CB  1 
ATOM   1428 C  CG  . PHE A 1 181 ? -9.264  41.578 -1.736  1.00 15.37  ? 181 PHE A CG  1 
ATOM   1429 C  CD1 . PHE A 1 181 ? -10.021 40.924 -0.782  1.00 16.83  ? 181 PHE A CD1 1 
ATOM   1430 C  CD2 . PHE A 1 181 ? -9.878  42.508 -2.543  1.00 15.83  ? 181 PHE A CD2 1 
ATOM   1431 C  CE1 . PHE A 1 181 ? -11.367 41.212 -0.602  1.00 15.91  ? 181 PHE A CE1 1 
ATOM   1432 C  CE2 . PHE A 1 181 ? -11.212 42.792 -2.379  1.00 16.71  ? 181 PHE A CE2 1 
ATOM   1433 C  CZ  . PHE A 1 181 ? -11.961 42.167 -1.405  1.00 15.06  ? 181 PHE A CZ  1 
ATOM   1434 N  N   . TYR A 1 182 ? -6.103  40.768 0.726   1.00 14.50  ? 182 TYR A N   1 
ATOM   1435 C  CA  . TYR A 1 182 ? -5.444  39.562 1.241   1.00 13.01  ? 182 TYR A CA  1 
ATOM   1436 C  C   . TYR A 1 182 ? -6.055  38.381 0.490   1.00 15.03  ? 182 TYR A C   1 
ATOM   1437 O  O   . TYR A 1 182 ? -7.245  38.167 0.573   1.00 15.52  ? 182 TYR A O   1 
ATOM   1438 C  CB  . TYR A 1 182 ? -5.583  39.469 2.759   1.00 13.90  ? 182 TYR A CB  1 
ATOM   1439 C  CG  . TYR A 1 182 ? -4.837  40.504 3.531   1.00 13.01  ? 182 TYR A CG  1 
ATOM   1440 C  CD1 . TYR A 1 182 ? -3.479  40.337 3.821   1.00 13.56  ? 182 TYR A CD1 1 
ATOM   1441 C  CD2 . TYR A 1 182 ? -5.474  41.642 3.999   1.00 13.12  ? 182 TYR A CD2 1 
ATOM   1442 C  CE1 . TYR A 1 182 ? -2.779  41.268 4.595   1.00 14.85  ? 182 TYR A CE1 1 
ATOM   1443 C  CE2 . TYR A 1 182 ? -4.788  42.580 4.740   1.00 13.16  ? 182 TYR A CE2 1 
ATOM   1444 C  CZ  . TYR A 1 182 ? -3.449  42.372 5.063   1.00 14.79  ? 182 TYR A CZ  1 
ATOM   1445 O  OH  . TYR A 1 182 ? -2.798  43.270 5.805   1.00 14.55  ? 182 TYR A OH  1 
ATOM   1446 N  N   . GLY A 1 183 ? -5.237  37.584 -0.166  1.00 14.21  ? 183 GLY A N   1 
ATOM   1447 C  CA  . GLY A 1 183 ? -5.724  36.351 -0.766  1.00 14.94  ? 183 GLY A CA  1 
ATOM   1448 C  C   . GLY A 1 183 ? -6.385  36.622 -2.116  1.00 15.67  ? 183 GLY A C   1 
ATOM   1449 O  O   . GLY A 1 183 ? -6.405  37.764 -2.610  1.00 19.15  ? 183 GLY A O   1 
ATOM   1450 N  N   . PRO A 1 184 ? -6.863  35.547 -2.748  1.00 17.59  ? 184 PRO A N   1 
ATOM   1451 C  CA  . PRO A 1 184 ? -7.343  35.588 -4.127  1.00 18.58  ? 184 PRO A CA  1 
ATOM   1452 C  C   . PRO A 1 184 ? -8.789  36.087 -4.276  1.00 23.18  ? 184 PRO A C   1 
ATOM   1453 O  O   . PRO A 1 184 ? -9.424  35.977 -5.343  1.00 26.94  ? 184 PRO A O   1 
ATOM   1454 C  CB  . PRO A 1 184 ? -7.143  34.129 -4.566  1.00 21.32  ? 184 PRO A CB  1 
ATOM   1455 C  CG  . PRO A 1 184 ? -7.396  33.370 -3.294  1.00 23.34  ? 184 PRO A CG  1 
ATOM   1456 C  CD  . PRO A 1 184 ? -6.725  34.178 -2.224  1.00 20.89  ? 184 PRO A CD  1 
ATOM   1457 N  N   . PHE A 1 185 ? -9.214  36.863 -3.330  1.00 20.07  ? 185 PHE A N   1 
ATOM   1458 C  CA  . PHE A 1 185 ? -10.639 37.242 -3.228  1.00 18.57  ? 185 PHE A CA  1 
ATOM   1459 C  C   . PHE A 1 185 ? -10.831 38.570 -3.949  1.00 20.71  ? 185 PHE A C   1 
ATOM   1460 O  O   . PHE A 1 185 ? -9.901  39.331 -4.170  1.00 20.68  ? 185 PHE A O   1 
ATOM   1461 C  CB  . PHE A 1 185 ? -11.051 37.270 -1.775  1.00 18.48  ? 185 PHE A CB  1 
ATOM   1462 C  CG  . PHE A 1 185 ? -10.688 36.002 -1.063  1.00 16.67  ? 185 PHE A CG  1 
ATOM   1463 C  CD1 . PHE A 1 185 ? -11.280 34.813 -1.401  1.00 17.43  ? 185 PHE A CD1 1 
ATOM   1464 C  CD2 . PHE A 1 185 ? -9.709  35.978 -0.086  1.00 17.19  ? 185 PHE A CD2 1 
ATOM   1465 C  CE1 . PHE A 1 185 ? -10.887 33.623 -0.808  1.00 19.88  ? 185 PHE A CE1 1 
ATOM   1466 C  CE2 . PHE A 1 185 ? -9.330  34.792 0.499   1.00 17.24  ? 185 PHE A CE2 1 
ATOM   1467 C  CZ  . PHE A 1 185 ? -9.926  33.613 0.157   1.00 18.27  ? 185 PHE A CZ  1 
ATOM   1468 N  N   . VAL A 1 186 ? -12.064 38.745 -4.415  1.00 20.98  ? 186 VAL A N   1 
ATOM   1469 C  CA  . VAL A 1 186 ? -12.504 39.974 -5.112  1.00 20.86  ? 186 VAL A CA  1 
ATOM   1470 C  C   . VAL A 1 186 ? -13.782 40.490 -4.467  1.00 21.56  ? 186 VAL A C   1 
ATOM   1471 O  O   . VAL A 1 186 ? -14.542 39.732 -3.904  1.00 23.51  ? 186 VAL A O   1 
ATOM   1472 C  CB  . VAL A 1 186 ? -12.689 39.689 -6.607  1.00 21.95  ? 186 VAL A CB  1 
ATOM   1473 C  CG1 . VAL A 1 186 ? -11.358 39.331 -7.229  1.00 24.23  ? 186 VAL A CG1 1 
ATOM   1474 C  CG2 . VAL A 1 186 ? -13.678 38.564 -6.802  1.00 25.11  ? 186 VAL A CG2 1 
ATOM   1475 N  N   . ASP A 1 187 ? -14.009 41.789 -4.658  1.00 20.84  ? 187 ASP A N   1 
ATOM   1476 C  CA  . ASP A 1 187 ? -15.175 42.517 -4.100  1.00 19.46  ? 187 ASP A CA  1 
ATOM   1477 C  C   . ASP A 1 187 ? -16.300 42.477 -5.140  1.00 23.54  ? 187 ASP A C   1 
ATOM   1478 O  O   . ASP A 1 187 ? -16.715 43.521 -5.592  1.00 23.87  ? 187 ASP A O   1 
ATOM   1479 C  CB  . ASP A 1 187 ? -14.774 43.917 -3.670  1.00 20.29  ? 187 ASP A CB  1 
ATOM   1480 C  CG  . ASP A 1 187 ? -14.064 44.793 -4.700  1.00 18.62  ? 187 ASP A CG  1 
ATOM   1481 O  OD1 . ASP A 1 187 ? -13.550 44.274 -5.756  1.00 21.33  ? 187 ASP A OD1 1 
ATOM   1482 O  OD2 . ASP A 1 187 ? -13.945 45.997 -4.397  1.00 21.41  ? 187 ASP A OD2 1 
ATOM   1483 N  N   . ARG A 1 188 ? -16.796 41.297 -5.403  1.00 23.66  ? 188 ARG A N   1 
ATOM   1484 C  CA  . ARG A 1 188 ? -18.039 41.096 -6.189  1.00 28.18  ? 188 ARG A CA  1 
ATOM   1485 C  C   . ARG A 1 188 ? -18.606 39.737 -5.816  1.00 30.74  ? 188 ARG A C   1 
ATOM   1486 O  O   . ARG A 1 188 ? -17.940 38.978 -5.106  1.00 28.65  ? 188 ARG A O   1 
ATOM   1487 C  CB  . ARG A 1 188 ? -17.761 41.257 -7.688  1.00 36.69  ? 188 ARG A CB  1 
ATOM   1488 C  CG  . ARG A 1 188 ? -16.715 40.326 -8.267  1.00 40.20  ? 188 ARG A CG  1 
ATOM   1489 C  CD  . ARG A 1 188 ? -16.503 40.529 -9.770  1.00 48.18  ? 188 ARG A CD  1 
ATOM   1490 N  NE  . ARG A 1 188 ? -15.094 40.836 -10.044 1.00 52.78  ? 188 ARG A NE  1 
ATOM   1491 C  CZ  . ARG A 1 188 ? -14.195 40.012 -10.589 1.00 57.78  ? 188 ARG A CZ  1 
ATOM   1492 N  NH1 . ARG A 1 188 ? -14.534 38.797 -10.994 1.00 59.28  ? 188 ARG A NH1 1 
ATOM   1493 N  NH2 . ARG A 1 188 ? -12.946 40.420 -10.739 1.00 63.68  ? 188 ARG A NH2 1 
ATOM   1494 N  N   . GLN A 1 189 ? -19.843 39.456 -6.226  1.00 28.52  ? 189 GLN A N   1 
ATOM   1495 C  CA  . GLN A 1 189 ? -20.453 38.127 -6.012  1.00 32.77  ? 189 GLN A CA  1 
ATOM   1496 C  C   . GLN A 1 189 ? -19.922 37.164 -7.085  1.00 29.97  ? 189 GLN A C   1 
ATOM   1497 O  O   . GLN A 1 189 ? -20.131 37.399 -8.296  1.00 35.33  ? 189 GLN A O   1 
ATOM   1498 C  CB  . GLN A 1 189 ? -21.971 38.258 -6.053  1.00 32.82  ? 189 GLN A CB  1 
ATOM   1499 C  CG  . GLN A 1 189 ? -22.640 36.936 -5.743  1.00 39.21  ? 189 GLN A CG  1 
ATOM   1500 C  CD  . GLN A 1 189 ? -24.068 37.114 -5.288  1.00 49.72  ? 189 GLN A CD  1 
ATOM   1501 O  OE1 . GLN A 1 189 ? -24.669 36.185 -4.748  1.00 68.20  ? 189 GLN A OE1 1 
ATOM   1502 N  NE2 . GLN A 1 189 ? -24.625 38.302 -5.494  1.00 55.17  ? 189 GLN A NE2 1 
ATOM   1503 N  N   . THR A 1 190 ? -19.153 36.155 -6.685  1.00 31.04  ? 190 THR A N   1 
ATOM   1504 C  CA  . THR A 1 190 ? -18.569 35.153 -7.616  1.00 29.79  ? 190 THR A CA  1 
ATOM   1505 C  C   . THR A 1 190 ? -18.690 33.796 -6.940  1.00 31.29  ? 190 THR A C   1 
ATOM   1506 O  O   . THR A 1 190 ? -19.351 33.742 -5.858  1.00 31.37  ? 190 THR A O   1 
ATOM   1507 C  CB  . THR A 1 190 ? -17.122 35.461 -8.039  1.00 34.78  ? 190 THR A CB  1 
ATOM   1508 O  OG1 . THR A 1 190 ? -16.280 35.221 -6.906  1.00 34.35  ? 190 THR A OG1 1 
ATOM   1509 C  CG2 . THR A 1 190 ? -16.883 36.865 -8.541  1.00 34.04  ? 190 THR A CG2 1 
ATOM   1510 N  N   . ALA A 1 191 ? -18.063 32.765 -7.537  1.00 33.38  ? 191 ALA A N   1 
ATOM   1511 C  CA  . ALA A 1 191 ? -18.007 31.390 -6.968  1.00 34.55  ? 191 ALA A CA  1 
ATOM   1512 C  C   . ALA A 1 191 ? -16.830 31.268 -5.985  1.00 35.64  ? 191 ALA A C   1 
ATOM   1513 O  O   . ALA A 1 191 ? -16.479 30.143 -5.628  1.00 37.27  ? 191 ALA A O   1 
ATOM   1514 C  CB  . ALA A 1 191 ? -17.880 30.357 -8.067  1.00 34.04  ? 191 ALA A CB  1 
ATOM   1515 N  N   . GLN A 1 192 ? -16.236 32.382 -5.554  1.00 30.11  ? 192 GLN A N   1 
ATOM   1516 C  CA  . GLN A 1 192 ? -14.991 32.344 -4.746  1.00 27.80  ? 192 GLN A CA  1 
ATOM   1517 C  C   . GLN A 1 192 ? -15.218 31.641 -3.406  1.00 25.60  ? 192 GLN A C   1 
ATOM   1518 O  O   . GLN A 1 192 ? -16.251 31.777 -2.726  1.00 23.50  ? 192 GLN A O   1 
ATOM   1519 C  CB  . GLN A 1 192 ? -14.420 33.751 -4.591  1.00 27.69  ? 192 GLN A CB  1 
ATOM   1520 C  CG  . GLN A 1 192 ? -15.279 34.687 -3.764  1.00 26.54  ? 192 GLN A CG  1 
ATOM   1521 C  CD  . GLN A 1 192 ? -14.732 36.088 -3.881  1.00 28.24  ? 192 GLN A CD  1 
ATOM   1522 O  OE1 . GLN A 1 192 ? -13.545 36.287 -4.144  1.00 23.71  ? 192 GLN A OE1 1 
ATOM   1523 N  NE2 . GLN A 1 192 ? -15.619 37.069 -3.813  1.00 30.00  ? 192 GLN A NE2 1 
ATOM   1524 N  N   . ALA A 1 193 ? -14.226 30.864 -3.005  1.00 26.80  ? 193 ALA A N   1 
ATOM   1525 C  CA  . ALA A 1 193 ? -14.315 30.104 -1.752  1.00 26.09  ? 193 ALA A CA  1 
ATOM   1526 C  C   . ALA A 1 193 ? -12.923 30.117 -1.141  1.00 22.43  ? 193 ALA A C   1 
ATOM   1527 O  O   . ALA A 1 193 ? -11.907 30.198 -1.882  1.00 25.34  ? 193 ALA A O   1 
ATOM   1528 C  CB  . ALA A 1 193 ? -14.832 28.718 -1.991  1.00 30.40  ? 193 ALA A CB  1 
ATOM   1529 N  N   . ALA A 1 194 ? -12.897 30.110 0.165   1.00 23.48  ? 194 ALA A N   1 
ATOM   1530 C  CA  . ALA A 1 194 ? -11.631 29.958 0.913   1.00 22.35  ? 194 ALA A CA  1 
ATOM   1531 C  C   . ALA A 1 194 ? -10.980 28.653 0.417   1.00 27.48  ? 194 ALA A C   1 
ATOM   1532 O  O   . ALA A 1 194 ? -11.674 27.615 0.282   1.00 22.87  ? 194 ALA A O   1 
ATOM   1533 C  CB  . ALA A 1 194 ? -11.985 29.929 2.358   1.00 23.34  ? 194 ALA A CB  1 
ATOM   1534 N  N   . GLY A 1 195 ? -9.689  28.679 0.130   1.00 26.61  ? 195 GLY A N   1 
ATOM   1535 C  CA  . GLY A 1 195 ? -8.979  27.426 -0.167  1.00 25.29  ? 195 GLY A CA  1 
ATOM   1536 C  C   . GLY A 1 195 ? -8.720  26.660 1.114   1.00 26.99  ? 195 GLY A C   1 
ATOM   1537 O  O   . GLY A 1 195 ? -9.086  27.137 2.218   1.00 26.07  ? 195 GLY A O   1 
ATOM   1538 N  N   . THR A 1 196 ? -8.056  25.514 1.017   1.00 25.66  ? 196 THR A N   1 
ATOM   1539 C  CA  . THR A 1 196 ? -7.707  24.728 2.214   1.00 25.37  ? 196 THR A CA  1 
ATOM   1540 C  C   . THR A 1 196 ? -6.774  25.555 3.116   1.00 24.24  ? 196 THR A C   1 
ATOM   1541 O  O   . THR A 1 196 ? -5.885  26.300 2.641   1.00 26.35  ? 196 THR A O   1 
ATOM   1542 C  CB  . THR A 1 196 ? -7.100  23.375 1.845   1.00 30.56  ? 196 THR A CB  1 
ATOM   1543 O  OG1 . THR A 1 196 ? -5.896  23.680 1.140   1.00 38.80  ? 196 THR A OG1 1 
ATOM   1544 C  CG2 . THR A 1 196 ? -8.060  22.552 1.015   1.00 28.48  ? 196 THR A CG2 1 
ATOM   1545 N  N   . ASP A 1 197 ? -7.039  25.463 4.394   1.00 22.61  ? 197 ASP A N   1 
ATOM   1546 C  CA  . ASP A 1 197 ? -6.255  26.185 5.416   1.00 22.60  ? 197 ASP A CA  1 
ATOM   1547 C  C   . ASP A 1 197 ? -5.354  25.171 6.120   1.00 22.06  ? 197 ASP A C   1 
ATOM   1548 O  O   . ASP A 1 197 ? -5.616  23.957 6.040   1.00 23.51  ? 197 ASP A O   1 
ATOM   1549 C  CB  . ASP A 1 197 ? -7.173  26.853 6.419   1.00 21.68  ? 197 ASP A CB  1 
ATOM   1550 C  CG  . ASP A 1 197 ? -6.525  28.026 7.134   1.00 20.82  ? 197 ASP A CG  1 
ATOM   1551 O  OD1 . ASP A 1 197 ? -5.522  28.589 6.593   1.00 21.17  ? 197 ASP A OD1 1 
ATOM   1552 O  OD2 . ASP A 1 197 ? -7.072  28.396 8.192   1.00 21.93  ? 197 ASP A OD2 1 
ATOM   1553 N  N   . THR A 1 198 ? -4.386  25.705 6.821   1.00 20.55  ? 198 THR A N   1 
ATOM   1554 C  CA  . THR A 1 198 ? -3.448  24.947 7.659   1.00 19.44  ? 198 THR A CA  1 
ATOM   1555 C  C   . THR A 1 198 ? -3.336  25.623 9.013   1.00 19.89  ? 198 THR A C   1 
ATOM   1556 O  O   . THR A 1 198 ? -3.841  26.699 9.200   1.00 19.60  ? 198 THR A O   1 
ATOM   1557 C  CB  . THR A 1 198 ? -2.096  24.861 6.978   1.00 22.57  ? 198 THR A CB  1 
ATOM   1558 O  OG1 . THR A 1 198 ? -1.703  26.182 6.593   1.00 24.27  ? 198 THR A OG1 1 
ATOM   1559 C  CG2 . THR A 1 198 ? -2.145  23.944 5.775   1.00 26.22  ? 198 THR A CG2 1 
ATOM   1560 N  N   . THR A 1 199 ? -2.762  24.907 9.950   1.00 18.27  ? 199 THR A N   1 
ATOM   1561 C  CA  . THR A 1 199 ? -2.508  25.367 11.305  1.00 17.15  ? 199 THR A CA  1 
ATOM   1562 C  C   . THR A 1 199 ? -1.199  26.121 11.326  1.00 18.39  ? 199 THR A C   1 
ATOM   1563 O  O   . THR A 1 199 ? -0.219  25.640 10.703  1.00 20.29  ? 199 THR A O   1 
ATOM   1564 C  CB  . THR A 1 199 ? -2.576  24.181 12.259  1.00 18.58  ? 199 THR A CB  1 
ATOM   1565 O  OG1 . THR A 1 199 ? -3.894  23.628 12.191  1.00 20.77  ? 199 THR A OG1 1 
ATOM   1566 C  CG2 . THR A 1 199 ? -2.197  24.640 13.644  1.00 19.98  ? 199 THR A CG2 1 
ATOM   1567 N  N   . ILE A 1 200 ? -1.151  27.237 12.059  1.00 16.99  ? 200 ILE A N   1 
ATOM   1568 C  CA  . ILE A 1 200 ? 0.049   28.110 12.168  1.00 16.22  ? 200 ILE A CA  1 
ATOM   1569 C  C   . ILE A 1 200 ? 0.980   27.564 13.261  1.00 16.30  ? 200 ILE A C   1 
ATOM   1570 O  O   . ILE A 1 200 ? 0.864   27.936 14.396  1.00 16.46  ? 200 ILE A O   1 
ATOM   1571 C  CB  . ILE A 1 200 ? -0.334  29.571 12.474  1.00 17.04  ? 200 ILE A CB  1 
ATOM   1572 C  CG1 . ILE A 1 200 ? -1.398  30.067 11.479  1.00 18.32  ? 200 ILE A CG1 1 
ATOM   1573 C  CG2 . ILE A 1 200 ? 0.892   30.402 12.430  1.00 18.76  ? 200 ILE A CG2 1 
ATOM   1574 C  CD1 . ILE A 1 200 ? -2.266  31.152 12.055  1.00 16.37  ? 200 ILE A CD1 1 
ATOM   1575 N  N   . THR A 1 201 ? 1.900   26.700 12.841  1.00 16.29  ? 201 THR A N   1 
ATOM   1576 C  CA  . THR A 1 201 ? 2.815   25.923 13.717  1.00 16.26  ? 201 THR A CA  1 
ATOM   1577 C  C   . THR A 1 201 ? 3.583   26.818 14.665  1.00 16.93  ? 201 THR A C   1 
ATOM   1578 O  O   . THR A 1 201 ? 3.577   26.510 15.885  1.00 17.72  ? 201 THR A O   1 
ATOM   1579 C  CB  . THR A 1 201 ? 3.782   25.131 12.832  1.00 15.36  ? 201 THR A CB  1 
ATOM   1580 O  OG1 . THR A 1 201 ? 2.998   24.432 11.876  1.00 17.75  ? 201 THR A OG1 1 
ATOM   1581 C  CG2 . THR A 1 201 ? 4.619   24.239 13.732  1.00 19.26  ? 201 THR A CG2 1 
ATOM   1582 N  N   . VAL A 1 202 ? 4.186   27.925 14.204  1.00 15.33  ? 202 VAL A N   1 
ATOM   1583 C  CA  . VAL A 1 202 ? 5.005   28.780 15.088  1.00 17.48  ? 202 VAL A CA  1 
ATOM   1584 C  C   . VAL A 1 202 ? 4.129   29.346 16.217  1.00 16.12  ? 202 VAL A C   1 
ATOM   1585 O  O   . VAL A 1 202 ? 4.603   29.451 17.327  1.00 15.81  ? 202 VAL A O   1 
ATOM   1586 C  CB  . VAL A 1 202 ? 5.726   29.876 14.315  1.00 17.04  ? 202 VAL A CB  1 
ATOM   1587 C  CG1 . VAL A 1 202 ? 4.705   30.840 13.657  1.00 16.97  ? 202 VAL A CG1 1 
ATOM   1588 C  CG2 . VAL A 1 202 ? 6.728   30.567 15.192  1.00 18.01  ? 202 VAL A CG2 1 
ATOM   1589 N  N   . ASN A 1 203 ? 2.864   29.649 15.927  1.00 16.48  ? 203 ASN A N   1 
ATOM   1590 C  CA  . ASN A 1 203 ? 1.920   30.160 16.927  1.00 15.70  ? 203 ASN A CA  1 
ATOM   1591 C  C   . ASN A 1 203 ? 1.577   29.066 17.958  1.00 15.04  ? 203 ASN A C   1 
ATOM   1592 O  O   . ASN A 1 203 ? 1.483   29.392 19.127  1.00 15.47  ? 203 ASN A O   1 
ATOM   1593 C  CB  . ASN A 1 203 ? 0.697   30.766 16.264  1.00 15.01  ? 203 ASN A CB  1 
ATOM   1594 C  CG  . ASN A 1 203 ? 0.978   32.052 15.512  1.00 17.12  ? 203 ASN A CG  1 
ATOM   1595 O  OD1 . ASN A 1 203 ? 2.092   32.586 15.471  1.00 14.59  ? 203 ASN A OD1 1 
ATOM   1596 N  ND2 . ASN A 1 203 ? -0.077  32.623 14.957  1.00 16.30  ? 203 ASN A ND2 1 
ATOM   1597 N  N   . VAL A 1 204 ? 1.327   27.875 17.514  1.00 15.51  ? 204 VAL A N   1 
ATOM   1598 C  CA  . VAL A 1 204 ? 1.020   26.772 18.462  1.00 17.07  ? 204 VAL A CA  1 
ATOM   1599 C  C   . VAL A 1 204 ? 2.218   26.624 19.404  1.00 16.52  ? 204 VAL A C   1 
ATOM   1600 O  O   . VAL A 1 204 ? 2.008   26.530 20.602  1.00 15.56  ? 204 VAL A O   1 
ATOM   1601 C  CB  . VAL A 1 204 ? 0.746   25.462 17.759  1.00 17.60  ? 204 VAL A CB  1 
ATOM   1602 C  CG1 . VAL A 1 204 ? 0.579   24.323 18.771  1.00 20.05  ? 204 VAL A CG1 1 
ATOM   1603 C  CG2 . VAL A 1 204 ? -0.433  25.535 16.789  1.00 18.06  ? 204 VAL A CG2 1 
ATOM   1604 N  N   . LEU A 1 205 ? 3.449   26.694 18.885  1.00 17.78  ? 205 LEU A N   1 
ATOM   1605 C  CA  . LEU A 1 205 ? 4.623   26.582 19.803  1.00 19.21  ? 205 LEU A CA  1 
ATOM   1606 C  C   . LEU A 1 205 ? 4.676   27.767 20.768  1.00 18.34  ? 205 LEU A C   1 
ATOM   1607 O  O   . LEU A 1 205 ? 4.955   27.622 21.950  1.00 18.28  ? 205 LEU A O   1 
ATOM   1608 C  CB  . LEU A 1 205 ? 5.905   26.486 18.963  1.00 18.01  ? 205 LEU A CB  1 
ATOM   1609 C  CG  . LEU A 1 205 ? 5.998   25.199 18.166  1.00 18.49  ? 205 LEU A CG  1 
ATOM   1610 C  CD1 . LEU A 1 205 ? 7.080   25.307 17.128  1.00 19.60  ? 205 LEU A CD1 1 
ATOM   1611 C  CD2 . LEU A 1 205 ? 6.323   23.999 19.053  1.00 18.07  ? 205 LEU A CD2 1 
ATOM   1612 N  N   . ALA A 1 206 ? 4.433   28.972 20.285  1.00 16.63  ? 206 ALA A N   1 
ATOM   1613 C  CA  . ALA A 1 206 ? 4.387   30.160 21.141  1.00 16.42  ? 206 ALA A CA  1 
ATOM   1614 C  C   . ALA A 1 206 ? 3.441   29.918 22.318  1.00 17.28  ? 206 ALA A C   1 
ATOM   1615 O  O   . ALA A 1 206 ? 3.771   30.321 23.427  1.00 15.88  ? 206 ALA A O   1 
ATOM   1616 C  CB  . ALA A 1 206 ? 3.955   31.352 20.320  1.00 16.73  ? 206 ALA A CB  1 
ATOM   1617 N  N   . TRP A 1 207 ? 2.264   29.417 22.007  1.00 16.09  ? 207 TRP A N   1 
ATOM   1618 C  CA  . TRP A 1 207 ? 1.179   29.182 22.973  1.00 16.18  ? 207 TRP A CA  1 
ATOM   1619 C  C   . TRP A 1 207 ? 1.562   28.063 23.963  1.00 19.10  ? 207 TRP A C   1 
ATOM   1620 O  O   . TRP A 1 207 ? 1.307   28.227 25.162  1.00 18.73  ? 207 TRP A O   1 
ATOM   1621 C  CB  . TRP A 1 207 ? -0.099  28.942 22.210  1.00 18.01  ? 207 TRP A CB  1 
ATOM   1622 C  CG  . TRP A 1 207 ? -1.267  28.494 23.019  1.00 17.83  ? 207 TRP A CG  1 
ATOM   1623 C  CD1 . TRP A 1 207 ? -2.139  29.247 23.750  1.00 20.05  ? 207 TRP A CD1 1 
ATOM   1624 C  CD2 . TRP A 1 207 ? -1.715  27.146 23.087  1.00 18.10  ? 207 TRP A CD2 1 
ATOM   1625 N  NE1 . TRP A 1 207 ? -3.098  28.438 24.286  1.00 20.23  ? 207 TRP A NE1 1 
ATOM   1626 C  CE2 . TRP A 1 207 ? -2.886  27.148 23.885  1.00 19.22  ? 207 TRP A CE2 1 
ATOM   1627 C  CE3 . TRP A 1 207 ? -1.238  25.946 22.560  1.00 21.70  ? 207 TRP A CE3 1 
ATOM   1628 C  CZ2 . TRP A 1 207 ? -3.603  25.967 24.093  1.00 20.46  ? 207 TRP A CZ2 1 
ATOM   1629 C  CZ3 . TRP A 1 207 ? -1.939  24.790 22.780  1.00 20.48  ? 207 TRP A CZ3 1 
ATOM   1630 C  CH2 . TRP A 1 207 ? -3.081  24.813 23.563  1.00 19.62  ? 207 TRP A CH2 1 
ATOM   1631 N  N   . LEU A 1 208 ? 2.297   27.080 23.507  1.00 16.74  ? 208 LEU A N   1 
ATOM   1632 C  CA  . LEU A 1 208 ? 2.856   26.073 24.465  1.00 16.92  ? 208 LEU A CA  1 
ATOM   1633 C  C   . LEU A 1 208 ? 3.877   26.744 25.375  1.00 20.96  ? 208 LEU A C   1 
ATOM   1634 O  O   . LEU A 1 208 ? 3.877   26.455 26.595  1.00 19.08  ? 208 LEU A O   1 
ATOM   1635 C  CB  . LEU A 1 208 ? 3.449   24.900 23.685  1.00 18.20  ? 208 LEU A CB  1 
ATOM   1636 C  CG  . LEU A 1 208 ? 2.467   24.015 22.925  1.00 18.49  ? 208 LEU A CG  1 
ATOM   1637 C  CD1 . LEU A 1 208 ? 3.141   22.966 22.064  1.00 20.66  ? 208 LEU A CD1 1 
ATOM   1638 C  CD2 . LEU A 1 208 ? 1.441   23.346 23.828  1.00 19.56  ? 208 LEU A CD2 1 
ATOM   1639 N  N   . TYR A 1 209 ? 4.696   27.667 24.876  1.00 18.12  ? 209 TYR A N   1 
ATOM   1640 C  CA  . TYR A 1 209 ? 5.591   28.436 25.763  1.00 18.28  ? 209 TYR A CA  1 
ATOM   1641 C  C   . TYR A 1 209 ? 4.766   29.269 26.756  1.00 20.83  ? 209 TYR A C   1 
ATOM   1642 O  O   . TYR A 1 209 ? 5.122   29.414 27.945  1.00 20.43  ? 209 TYR A O   1 
ATOM   1643 C  CB  . TYR A 1 209 ? 6.550   29.308 24.984  1.00 19.72  ? 209 TYR A CB  1 
ATOM   1644 C  CG  . TYR A 1 209 ? 7.747   28.598 24.421  1.00 22.11  ? 209 TYR A CG  1 
ATOM   1645 C  CD1 . TYR A 1 209 ? 8.745   28.136 25.271  1.00 24.09  ? 209 TYR A CD1 1 
ATOM   1646 C  CD2 . TYR A 1 209 ? 7.877   28.349 23.065  1.00 20.96  ? 209 TYR A CD2 1 
ATOM   1647 C  CE1 . TYR A 1 209 ? 9.869   27.508 24.761  1.00 24.05  ? 209 TYR A CE1 1 
ATOM   1648 C  CE2 . TYR A 1 209 ? 8.961   27.643 22.551  1.00 22.75  ? 209 TYR A CE2 1 
ATOM   1649 C  CZ  . TYR A 1 209 ? 9.961   27.222 23.412  1.00 25.65  ? 209 TYR A CZ  1 
ATOM   1650 O  OH  . TYR A 1 209 ? 11.072  26.568 22.945  1.00 25.27  ? 209 TYR A OH  1 
ATOM   1651 N  N   . ALA A 1 210 ? 3.699   29.923 26.292  1.00 16.55  ? 210 ALA A N   1 
ATOM   1652 C  CA  . ALA A 1 210 ? 2.808   30.684 27.209  1.00 18.45  ? 210 ALA A CA  1 
ATOM   1653 C  C   . ALA A 1 210 ? 2.346   29.793 28.364  1.00 21.11  ? 210 ALA A C   1 
ATOM   1654 O  O   . ALA A 1 210 ? 2.323   30.256 29.534  1.00 21.66  ? 210 ALA A O   1 
ATOM   1655 C  CB  . ALA A 1 210 ? 1.596   31.230 26.459  1.00 19.73  ? 210 ALA A CB  1 
ATOM   1656 N  N   . ALA A 1 211 ? 1.962   28.565 28.038  1.00 19.95  ? 211 ALA A N   1 
ATOM   1657 C  CA  . ALA A 1 211 ? 1.438   27.605 29.025  1.00 23.24  ? 211 ALA A CA  1 
ATOM   1658 C  C   . ALA A 1 211 ? 2.552   27.338 30.048  1.00 22.81  ? 211 ALA A C   1 
ATOM   1659 O  O   . ALA A 1 211 ? 2.264   27.386 31.275  1.00 23.38  ? 211 ALA A O   1 
ATOM   1660 C  CB  . ALA A 1 211 ? 0.890   26.395 28.327  1.00 21.61  ? 211 ALA A CB  1 
ATOM   1661 N  N   . VAL A 1 212 ? 3.787   27.145 29.584  1.00 22.16  ? 212 VAL A N   1 
ATOM   1662 C  CA  . VAL A 1 212 ? 4.933   26.875 30.503  1.00 23.60  ? 212 VAL A CA  1 
ATOM   1663 C  C   . VAL A 1 212 ? 5.210   28.092 31.366  1.00 27.17  ? 212 VAL A C   1 
ATOM   1664 O  O   . VAL A 1 212 ? 5.424   27.916 32.617  1.00 30.37  ? 212 VAL A O   1 
ATOM   1665 C  CB  . VAL A 1 212 ? 6.183   26.447 29.707  1.00 23.58  ? 212 VAL A CB  1 
ATOM   1666 C  CG1 . VAL A 1 212 ? 7.401   26.384 30.619  1.00 25.93  ? 212 VAL A CG1 1 
ATOM   1667 C  CG2 . VAL A 1 212 ? 5.913   25.100 29.065  1.00 21.53  ? 212 VAL A CG2 1 
ATOM   1668 N  N   . ILE A 1 213 ? 5.183   29.287 30.790  1.00 26.03  ? 213 ILE A N   1 
ATOM   1669 C  CA  . ILE A 1 213 ? 5.444   30.556 31.528  1.00 25.99  ? 213 ILE A CA  1 
ATOM   1670 C  C   . ILE A 1 213 ? 4.429   30.638 32.666  1.00 30.01  ? 213 ILE A C   1 
ATOM   1671 O  O   . ILE A 1 213 ? 4.826   31.125 33.804  1.00 29.68  ? 213 ILE A O   1 
ATOM   1672 C  CB  . ILE A 1 213 ? 5.428   31.779 30.578  1.00 27.59  ? 213 ILE A CB  1 
ATOM   1673 C  CG1 . ILE A 1 213 ? 6.636   31.724 29.641  1.00 26.44  ? 213 ILE A CG1 1 
ATOM   1674 C  CG2 . ILE A 1 213 ? 5.396   33.078 31.367  1.00 28.13  ? 213 ILE A CG2 1 
ATOM   1675 C  CD1 . ILE A 1 213 ? 6.721   32.754 28.534  1.00 28.39  ? 213 ILE A CD1 1 
ATOM   1676 N  N   . ASN A 1 214 ? 3.206   30.172 32.379  1.00 28.49  ? 214 ASN A N   1 
ATOM   1677 C  CA  . ASN A 1 214 ? 2.005   30.276 33.257  1.00 34.88  ? 214 ASN A CA  1 
ATOM   1678 C  C   . ASN A 1 214 ? 2.025   29.117 34.235  1.00 34.07  ? 214 ASN A C   1 
ATOM   1679 O  O   . ASN A 1 214 ? 1.065   28.965 35.007  1.00 36.88  ? 214 ASN A O   1 
ATOM   1680 C  CB  . ASN A 1 214 ? 0.674   30.284 32.499  1.00 35.91  ? 214 ASN A CB  1 
ATOM   1681 C  CG  . ASN A 1 214 ? 0.146   31.691 32.417  1.00 47.02  ? 214 ASN A CG  1 
ATOM   1682 O  OD1 . ASN A 1 214 ? -0.649  32.094 33.269  1.00 46.30  ? 214 ASN A OD1 1 
ATOM   1683 N  ND2 . ASN A 1 214 ? 0.685   32.457 31.484  1.00 47.61  ? 214 ASN A ND2 1 
ATOM   1684 N  N   . GLY A 1 215 ? 3.097   28.347 34.192  1.00 27.40  ? 215 GLY A N   1 
ATOM   1685 C  CA  . GLY A 1 215 ? 3.420   27.380 35.244  1.00 31.38  ? 215 GLY A CA  1 
ATOM   1686 C  C   . GLY A 1 215 ? 2.839   26.012 34.966  1.00 33.57  ? 215 GLY A C   1 
ATOM   1687 O  O   . GLY A 1 215 ? 2.863   25.186 35.885  1.00 40.39  ? 215 GLY A O   1 
ATOM   1688 N  N   . ASP A 1 216 ? 2.451   25.734 33.727  1.00 33.04  ? 216 ASP A N   1 
ATOM   1689 C  CA  . ASP A 1 216 ? 1.949   24.400 33.308  1.00 30.74  ? 216 ASP A CA  1 
ATOM   1690 C  C   . ASP A 1 216 ? 2.973   23.676 32.409  1.00 35.93  ? 216 ASP A C   1 
ATOM   1691 O  O   . ASP A 1 216 ? 3.299   24.225 31.318  1.00 36.26  ? 216 ASP A O   1 
ATOM   1692 C  CB  . ASP A 1 216 ? 0.639   24.578 32.577  1.00 27.37  ? 216 ASP A CB  1 
ATOM   1693 C  CG  . ASP A 1 216 ? -0.122  23.283 32.397  1.00 33.02  ? 216 ASP A CG  1 
ATOM   1694 O  OD1 . ASP A 1 216 ? 0.435   22.200 32.736  1.00 39.19  ? 216 ASP A OD1 1 
ATOM   1695 O  OD2 . ASP A 1 216 ? -1.270  23.355 31.929  1.00 35.06  ? 216 ASP A OD2 1 
ATOM   1696 N  N   . ARG A 1 217 ? 3.414   22.465 32.798  1.00 33.35  ? 217 ARG A N   1 
ATOM   1697 C  CA  . ARG A 1 217 ? 4.439   21.680 32.055  1.00 29.77  ? 217 ARG A CA  1 
ATOM   1698 C  C   . ARG A 1 217 ? 3.930   20.311 31.579  1.00 25.33  ? 217 ARG A C   1 
ATOM   1699 O  O   . ARG A 1 217 ? 4.748   19.566 31.060  1.00 26.26  ? 217 ARG A O   1 
ATOM   1700 C  CB  . ARG A 1 217 ? 5.697   21.549 32.935  1.00 32.45  ? 217 ARG A CB  1 
ATOM   1701 C  CG  . ARG A 1 217 ? 6.334   22.887 33.283  1.00 33.02  ? 217 ARG A CG  1 
ATOM   1702 C  CD  . ARG A 1 217 ? 7.692   22.906 33.926  1.00 27.78  ? 217 ARG A CD  1 
ATOM   1703 N  NE  . ARG A 1 217 ? 8.666   22.025 33.328  1.00 29.15  ? 217 ARG A NE  1 
ATOM   1704 C  CZ  . ARG A 1 217 ? 9.831   22.386 32.809  1.00 33.38  ? 217 ARG A CZ  1 
ATOM   1705 N  NH1 . ARG A 1 217 ? 10.221  23.653 32.766  1.00 37.15  ? 217 ARG A NH1 1 
ATOM   1706 N  NH2 . ARG A 1 217 ? 10.618  21.438 32.313  1.00 41.52  ? 217 ARG A NH2 1 
ATOM   1707 N  N   . TRP A 1 218 ? 2.663   19.947 31.696  1.00 25.73  ? 218 TRP A N   1 
ATOM   1708 C  CA  . TRP A 1 218 ? 2.202   18.528 31.645  1.00 27.04  ? 218 TRP A CA  1 
ATOM   1709 C  C   . TRP A 1 218 ? 2.563   17.864 30.325  1.00 30.16  ? 218 TRP A C   1 
ATOM   1710 O  O   . TRP A 1 218 ? 2.717   16.629 30.261  1.00 23.97  ? 218 TRP A O   1 
ATOM   1711 C  CB  . TRP A 1 218 ? 0.702   18.333 31.950  1.00 27.56  ? 218 TRP A CB  1 
ATOM   1712 C  CG  . TRP A 1 218 ? -0.303  18.749 30.914  1.00 28.51  ? 218 TRP A CG  1 
ATOM   1713 C  CD1 . TRP A 1 218 ? -1.072  19.885 30.965  1.00 29.08  ? 218 TRP A CD1 1 
ATOM   1714 C  CD2 . TRP A 1 218 ? -0.745  18.026 29.752  1.00 26.81  ? 218 TRP A CD2 1 
ATOM   1715 N  NE1 . TRP A 1 218 ? -1.913  19.931 29.892  1.00 25.43  ? 218 TRP A NE1 1 
ATOM   1716 C  CE2 . TRP A 1 218 ? -1.726  18.829 29.116  1.00 27.02  ? 218 TRP A CE2 1 
ATOM   1717 C  CE3 . TRP A 1 218 ? -0.360  16.843 29.109  1.00 26.88  ? 218 TRP A CE3 1 
ATOM   1718 C  CZ2 . TRP A 1 218 ? -2.312  18.477 27.911  1.00 25.77  ? 218 TRP A CZ2 1 
ATOM   1719 C  CZ3 . TRP A 1 218 ? -0.965  16.479 27.932  1.00 30.04  ? 218 TRP A CZ3 1 
ATOM   1720 C  CH2 . TRP A 1 218 ? -1.935  17.292 27.338  1.00 29.44  ? 218 TRP A CH2 1 
ATOM   1721 N  N   . PHE A 1 219 ? 2.559   18.640 29.250  1.00 26.38  ? 219 PHE A N   1 
ATOM   1722 C  CA  . PHE A 1 219 ? 2.648   18.113 27.872  1.00 25.87  ? 219 PHE A CA  1 
ATOM   1723 C  C   . PHE A 1 219 ? 4.119   17.975 27.454  1.00 24.68  ? 219 PHE A C   1 
ATOM   1724 O  O   . PHE A 1 219 ? 4.370   17.488 26.326  1.00 23.36  ? 219 PHE A O   1 
ATOM   1725 C  CB  . PHE A 1 219 ? 1.894   19.066 26.918  1.00 23.02  ? 219 PHE A CB  1 
ATOM   1726 C  CG  . PHE A 1 219 ? 2.211   20.503 27.179  1.00 24.17  ? 219 PHE A CG  1 
ATOM   1727 C  CD1 . PHE A 1 219 ? 3.333   21.104 26.642  1.00 21.61  ? 219 PHE A CD1 1 
ATOM   1728 C  CD2 . PHE A 1 219 ? 1.411   21.257 28.016  1.00 23.34  ? 219 PHE A CD2 1 
ATOM   1729 C  CE1 . PHE A 1 219 ? 3.671   22.406 26.953  1.00 23.44  ? 219 PHE A CE1 1 
ATOM   1730 C  CE2 . PHE A 1 219 ? 1.739   22.569 28.314  1.00 24.14  ? 219 PHE A CE2 1 
ATOM   1731 C  CZ  . PHE A 1 219 ? 2.863   23.150 27.787  1.00 25.85  ? 219 PHE A CZ  1 
ATOM   1732 N  N   . LEU A 1 220 ? 5.060   18.405 28.291  1.00 21.25  ? 220 LEU A N   1 
ATOM   1733 C  CA  . LEU A 1 220 ? 6.494   18.378 27.935  1.00 22.77  ? 220 LEU A CA  1 
ATOM   1734 C  C   . LEU A 1 220 ? 6.964   16.932 27.979  1.00 24.86  ? 220 LEU A C   1 
ATOM   1735 O  O   . LEU A 1 220 ? 6.288   16.092 28.598  1.00 23.83  ? 220 LEU A O   1 
ATOM   1736 C  CB  . LEU A 1 220 ? 7.332   19.254 28.864  1.00 22.85  ? 220 LEU A CB  1 
ATOM   1737 C  CG  . LEU A 1 220 ? 7.055   20.755 28.848  1.00 24.29  ? 220 LEU A CG  1 
ATOM   1738 C  CD1 . LEU A 1 220 ? 7.972   21.428 29.825  1.00 24.42  ? 220 LEU A CD1 1 
ATOM   1739 C  CD2 . LEU A 1 220 ? 7.243   21.339 27.454  1.00 23.07  ? 220 LEU A CD2 1 
ATOM   1740 N  N   . ASN A 1 221 ? 8.095   16.662 27.346  1.00 29.28  ? 221 ASN A N   1 
ATOM   1741 C  CA  . ASN A 1 221 ? 8.642   15.281 27.368  1.00 28.59  ? 221 ASN A CA  1 
ATOM   1742 C  C   . ASN A 1 221 ? 10.152  15.375 27.274  1.00 28.13  ? 221 ASN A C   1 
ATOM   1743 O  O   . ASN A 1 221 ? 10.680  16.514 27.212  1.00 26.37  ? 221 ASN A O   1 
ATOM   1744 C  CB  . ASN A 1 221 ? 8.032   14.385 26.296  1.00 28.40  ? 221 ASN A CB  1 
ATOM   1745 C  CG  . ASN A 1 221 ? 8.296   14.870 24.872  1.00 29.62  ? 221 ASN A CG  1 
ATOM   1746 O  OD1 . ASN A 1 221 ? 9.359   15.382 24.550  1.00 30.59  ? 221 ASN A OD1 1 
ATOM   1747 N  ND2 . ASN A 1 221 ? 7.335   14.656 23.993  1.00 33.54  ? 221 ASN A ND2 1 
ATOM   1748 N  N   . ARG A 1 222 ? 10.795  14.197 27.389  1.00 28.72  ? 222 ARG A N   1 
ATOM   1749 C  CA  . ARG A 1 222 ? 12.272  14.091 27.493  1.00 31.95  ? 222 ARG A CA  1 
ATOM   1750 C  C   . ARG A 1 222 ? 12.872  13.990 26.105  1.00 35.86  ? 222 ARG A C   1 
ATOM   1751 O  O   . ARG A 1 222 ? 14.093  13.863 26.021  1.00 40.12  ? 222 ARG A O   1 
ATOM   1752 C  CB  . ARG A 1 222 ? 12.671  12.858 28.315  1.00 34.07  ? 222 ARG A CB  1 
ATOM   1753 C  CG  . ARG A 1 222 ? 12.397  11.517 27.644  1.00 36.28  ? 222 ARG A CG  1 
ATOM   1754 C  CD  . ARG A 1 222 ? 12.971  10.357 28.453  1.00 43.87  ? 222 ARG A CD  1 
ATOM   1755 N  NE  . ARG A 1 222 ? 13.123  9.134  27.673  1.00 50.90  ? 222 ARG A NE  1 
ATOM   1756 C  CZ  . ARG A 1 222 ? 12.132  8.327  27.275  1.00 59.95  ? 222 ARG A CZ  1 
ATOM   1757 N  NH1 . ARG A 1 222 ? 10.865  8.588  27.572  1.00 65.41  ? 222 ARG A NH1 1 
ATOM   1758 N  NH2 . ARG A 1 222 ? 12.423  7.243  26.574  1.00 57.51  ? 222 ARG A NH2 1 
ATOM   1759 N  N   . PHE A 1 223 ? 12.044  14.067 25.064  1.00 34.11  ? 223 PHE A N   1 
ATOM   1760 C  CA  . PHE A 1 223 ? 12.494  13.848 23.675  1.00 32.52  ? 223 PHE A CA  1 
ATOM   1761 C  C   . PHE A 1 223 ? 12.864  15.175 23.023  1.00 31.53  ? 223 PHE A C   1 
ATOM   1762 O  O   . PHE A 1 223 ? 12.479  16.276 23.482  1.00 32.91  ? 223 PHE A O   1 
ATOM   1763 C  CB  . PHE A 1 223 ? 11.442  13.124 22.866  1.00 32.14  ? 223 PHE A CB  1 
ATOM   1764 C  CG  . PHE A 1 223 ? 11.033  11.801 23.438  1.00 41.68  ? 223 PHE A CG  1 
ATOM   1765 C  CD1 . PHE A 1 223 ? 11.962  10.778 23.584  1.00 48.89  ? 223 PHE A CD1 1 
ATOM   1766 C  CD2 . PHE A 1 223 ? 9.711   11.562 23.775  1.00 45.91  ? 223 PHE A CD2 1 
ATOM   1767 C  CE1 . PHE A 1 223 ? 11.576  9.544  24.085  1.00 49.58  ? 223 PHE A CE1 1 
ATOM   1768 C  CE2 . PHE A 1 223 ? 9.334   10.332 24.291  1.00 54.11  ? 223 PHE A CE2 1 
ATOM   1769 C  CZ  . PHE A 1 223 ? 10.266  9.328  24.443  1.00 48.64  ? 223 PHE A CZ  1 
ATOM   1770 N  N   . THR A 1 224 ? 13.669  15.045 21.981  1.00 31.68  ? 224 THR A N   1 
ATOM   1771 C  CA  . THR A 1 224 ? 13.928  16.135 21.029  1.00 32.61  ? 224 THR A CA  1 
ATOM   1772 C  C   . THR A 1 224 ? 13.680  15.602 19.614  1.00 29.31  ? 224 THR A C   1 
ATOM   1773 O  O   . THR A 1 224 ? 13.308  14.445 19.394  1.00 32.96  ? 224 THR A O   1 
ATOM   1774 C  CB  . THR A 1 224 ? 15.306  16.754 21.270  1.00 35.82  ? 224 THR A CB  1 
ATOM   1775 O  OG1 . THR A 1 224 ? 15.329  18.046 20.658  1.00 35.05  ? 224 THR A OG1 1 
ATOM   1776 C  CG2 . THR A 1 224 ? 16.431  15.914 20.704  1.00 41.15  ? 224 THR A CG2 1 
ATOM   1777 N  N   . THR A 1 225 ? 13.792  16.479 18.654  1.00 32.50  ? 225 THR A N   1 
ATOM   1778 C  CA  . THR A 1 225 ? 13.539  16.121 17.247  1.00 31.33  ? 225 THR A CA  1 
ATOM   1779 C  C   . THR A 1 225 ? 14.418  17.016 16.408  1.00 27.89  ? 225 THR A C   1 
ATOM   1780 O  O   . THR A 1 225 ? 14.926  18.030 16.937  1.00 29.31  ? 225 THR A O   1 
ATOM   1781 C  CB  . THR A 1 225 ? 12.079  16.336 16.852  1.00 31.54  ? 225 THR A CB  1 
ATOM   1782 O  OG1 . THR A 1 225 ? 11.991  15.976 15.472  1.00 32.78  ? 225 THR A OG1 1 
ATOM   1783 C  CG2 . THR A 1 225 ? 11.623  17.766 17.075  1.00 30.82  ? 225 THR A CG2 1 
ATOM   1784 N  N   . THR A 1 226 ? 14.633  16.604 15.160  1.00 31.28  ? 226 THR A N   1 
ATOM   1785 C  CA  . THR A 1 226 ? 15.232  17.500 14.161  1.00 32.11  ? 226 THR A CA  1 
ATOM   1786 C  C   . THR A 1 226 ? 14.087  18.353 13.624  1.00 28.11  ? 226 THR A C   1 
ATOM   1787 O  O   . THR A 1 226 ? 12.934  17.875 13.612  1.00 28.46  ? 226 THR A O   1 
ATOM   1788 C  CB  . THR A 1 226 ? 15.975  16.752 13.048  1.00 30.82  ? 226 THR A CB  1 
ATOM   1789 O  OG1 . THR A 1 226 ? 15.017  16.017 12.301  1.00 34.20  ? 226 THR A OG1 1 
ATOM   1790 C  CG2 . THR A 1 226 ? 17.047  15.820 13.583  1.00 33.98  ? 226 THR A CG2 1 
ATOM   1791 N  N   . LEU A 1 227 ? 14.441  19.519 13.110  1.00 31.70  ? 227 LEU A N   1 
ATOM   1792 C  CA  . LEU A 1 227 ? 13.501  20.355 12.325  1.00 29.75  ? 227 LEU A CA  1 
ATOM   1793 C  C   . LEU A 1 227 ? 12.906  19.575 11.141  1.00 33.11  ? 227 LEU A C   1 
ATOM   1794 O  O   . LEU A 1 227 ? 11.672  19.535 11.000  1.00 27.27  ? 227 LEU A O   1 
ATOM   1795 C  CB  . LEU A 1 227 ? 14.246  21.627 11.954  1.00 30.63  ? 227 LEU A CB  1 
ATOM   1796 C  CG  . LEU A 1 227 ? 13.392  22.707 11.306  1.00 33.22  ? 227 LEU A CG  1 
ATOM   1797 C  CD1 . LEU A 1 227 ? 12.305  23.150 12.294  1.00 34.94  ? 227 LEU A CD1 1 
ATOM   1798 C  CD2 . LEU A 1 227 ? 14.255  23.886 10.915  1.00 37.64  ? 227 LEU A CD2 1 
ATOM   1799 N  N   . ASN A 1 228 ? 13.729  18.855 10.364  1.00 33.83  ? 228 ASN A N   1 
ATOM   1800 C  CA  . ASN A 1 228 ? 13.240  18.111 9.187   1.00 34.72  ? 228 ASN A CA  1 
ATOM   1801 C  C   . ASN A 1 228 ? 12.254  17.052 9.661   1.00 31.07  ? 228 ASN A C   1 
ATOM   1802 O  O   . ASN A 1 228 ? 11.192  16.907 9.058   1.00 32.51  ? 228 ASN A O   1 
ATOM   1803 C  CB  . ASN A 1 228 ? 14.404  17.565 8.339   1.00 42.97  ? 228 ASN A CB  1 
ATOM   1804 C  CG  . ASN A 1 228 ? 15.243  18.636 7.644   1.00 53.69  ? 228 ASN A CG  1 
ATOM   1805 O  OD1 . ASN A 1 228 ? 16.078  18.318 6.798   1.00 62.38  ? 228 ASN A OD1 1 
ATOM   1806 N  ND2 . ASN A 1 228 ? 15.050  19.915 7.946   1.00 54.27  ? 228 ASN A ND2 1 
ATOM   1807 N  N   . ASP A 1 229 ? 12.574  16.301 10.724  1.00 32.15  ? 229 ASP A N   1 
ATOM   1808 C  CA  . ASP A 1 229 ? 11.683  15.214 11.196  1.00 31.24  ? 229 ASP A CA  1 
ATOM   1809 C  C   . ASP A 1 229 ? 10.375  15.818 11.755  1.00 28.14  ? 229 ASP A C   1 
ATOM   1810 O  O   . ASP A 1 229 ? 9.336   15.168 11.684  1.00 28.88  ? 229 ASP A O   1 
ATOM   1811 C  CB  . ASP A 1 229 ? 12.381  14.326 12.241  1.00 36.62  ? 229 ASP A CB  1 
ATOM   1812 C  CG  . ASP A 1 229 ? 13.366  13.314 11.670  1.00 46.82  ? 229 ASP A CG  1 
ATOM   1813 O  OD1 . ASP A 1 229 ? 13.214  12.936 10.493  1.00 47.10  ? 229 ASP A OD1 1 
ATOM   1814 O  OD2 . ASP A 1 229 ? 14.315  12.940 12.403  1.00 46.49  ? 229 ASP A OD2 1 
ATOM   1815 N  N   . PHE A 1 230 ? 10.465  16.978 12.373  1.00 26.60  ? 230 PHE A N   1 
ATOM   1816 C  CA  . PHE A 1 230 ? 9.257   17.652 12.911  1.00 25.81  ? 230 PHE A CA  1 
ATOM   1817 C  C   . PHE A 1 230 ? 8.356   18.010 11.723  1.00 27.01  ? 230 PHE A C   1 
ATOM   1818 O  O   . PHE A 1 230 ? 7.197   17.606 11.754  1.00 29.71  ? 230 PHE A O   1 
ATOM   1819 C  CB  . PHE A 1 230 ? 9.621   18.859 13.769  1.00 25.30  ? 230 PHE A CB  1 
ATOM   1820 C  CG  . PHE A 1 230 ? 8.361   19.580 14.163  1.00 23.94  ? 230 PHE A CG  1 
ATOM   1821 C  CD1 . PHE A 1 230 ? 7.528   19.050 15.127  1.00 25.11  ? 230 PHE A CD1 1 
ATOM   1822 C  CD2 . PHE A 1 230 ? 7.947   20.689 13.465  1.00 25.42  ? 230 PHE A CD2 1 
ATOM   1823 C  CE1 . PHE A 1 230 ? 6.331   19.668 15.453  1.00 27.29  ? 230 PHE A CE1 1 
ATOM   1824 C  CE2 . PHE A 1 230 ? 6.767   21.325 13.820  1.00 23.97  ? 230 PHE A CE2 1 
ATOM   1825 C  CZ  . PHE A 1 230 ? 5.952   20.800 14.777  1.00 23.47  ? 230 PHE A CZ  1 
ATOM   1826 N  N   . ASN A 1 231 ? 8.926   18.641 10.700  1.00 33.06  ? 231 ASN A N   1 
ATOM   1827 C  CA  . ASN A 1 231 ? 8.206   19.077 9.472   1.00 31.92  ? 231 ASN A CA  1 
ATOM   1828 C  C   . ASN A 1 231 ? 7.555   17.877 8.794   1.00 37.15  ? 231 ASN A C   1 
ATOM   1829 O  O   . ASN A 1 231 ? 6.373   18.011 8.382   1.00 41.58  ? 231 ASN A O   1 
ATOM   1830 C  CB  . ASN A 1 231 ? 9.098   19.951 8.598   1.00 34.30  ? 231 ASN A CB  1 
ATOM   1831 C  CG  . ASN A 1 231 ? 9.138   21.354 9.141   1.00 32.15  ? 231 ASN A CG  1 
ATOM   1832 O  OD1 . ASN A 1 231 ? 8.084   21.883 9.504   1.00 40.09  ? 231 ASN A OD1 1 
ATOM   1833 N  ND2 . ASN A 1 231 ? 10.313  21.899 9.344   1.00 32.61  ? 231 ASN A ND2 1 
ATOM   1834 N  N   . LEU A 1 232 ? 8.200   16.708 8.796   1.00 33.70  ? 232 LEU A N   1 
ATOM   1835 C  CA  . LEU A 1 232 ? 7.571   15.494 8.226   1.00 36.22  ? 232 LEU A CA  1 
ATOM   1836 C  C   . LEU A 1 232 ? 6.299   15.179 9.005   1.00 37.37  ? 232 LEU A C   1 
ATOM   1837 O  O   . LEU A 1 232 ? 5.274   14.916 8.344   1.00 38.05  ? 232 LEU A O   1 
ATOM   1838 C  CB  . LEU A 1 232 ? 8.541   14.306 8.232   1.00 37.80  ? 232 LEU A CB  1 
ATOM   1839 C  CG  . LEU A 1 232 ? 9.685   14.382 7.226   1.00 41.87  ? 232 LEU A CG  1 
ATOM   1840 C  CD1 . LEU A 1 232 ? 10.690  13.259 7.473   1.00 41.25  ? 232 LEU A CD1 1 
ATOM   1841 C  CD2 . LEU A 1 232 ? 9.166   14.335 5.791   1.00 38.89  ? 232 LEU A CD2 1 
ATOM   1842 N  N   . VAL A 1 233 ? 6.328   15.238 10.348  1.00 34.89  ? 233 VAL A N   1 
ATOM   1843 C  CA  . VAL A 1 233 ? 5.095   14.974 11.145  1.00 38.97  ? 233 VAL A CA  1 
ATOM   1844 C  C   . VAL A 1 233 ? 4.099   16.129 10.925  1.00 39.58  ? 233 VAL A C   1 
ATOM   1845 O  O   . VAL A 1 233 ? 2.926   15.794 10.629  1.00 43.38  ? 233 VAL A O   1 
ATOM   1846 C  CB  . VAL A 1 233 ? 5.407   14.723 12.630  1.00 42.33  ? 233 VAL A CB  1 
ATOM   1847 C  CG1 . VAL A 1 233 ? 4.127   14.608 13.455  1.00 45.39  ? 233 VAL A CG1 1 
ATOM   1848 C  CG2 . VAL A 1 233 ? 6.273   13.491 12.819  1.00 42.30  ? 233 VAL A CG2 1 
ATOM   1849 N  N   . ALA A 1 234 ? 4.554   17.394 10.960  1.00 45.91  ? 234 ALA A N   1 
ATOM   1850 C  CA  . ALA A 1 234 ? 3.730   18.622 10.767  1.00 49.63  ? 234 ALA A CA  1 
ATOM   1851 C  C   . ALA A 1 234 ? 2.883   18.498 9.496   1.00 47.14  ? 234 ALA A C   1 
ATOM   1852 O  O   . ALA A 1 234 ? 1.633   18.519 9.641   1.00 46.90  ? 234 ALA A O   1 
ATOM   1853 C  CB  . ALA A 1 234 ? 4.579   19.879 10.683  1.00 49.34  ? 234 ALA A CB  1 
ATOM   1854 N  N   . MET A 1 235 ? 3.538   18.427 8.323   1.00 42.49  ? 235 MET A N   1 
ATOM   1855 C  CA  . MET A 1 235 ? 2.902   18.207 6.993   1.00 41.24  ? 235 MET A CA  1 
ATOM   1856 C  C   . MET A 1 235 ? 1.758   17.200 7.144   1.00 40.36  ? 235 MET A C   1 
ATOM   1857 O  O   . MET A 1 235 ? 0.637   17.488 6.694   1.00 34.31  ? 235 MET A O   1 
ATOM   1858 C  CB  . MET A 1 235 ? 3.886   17.672 5.950   1.00 50.91  ? 235 MET A CB  1 
ATOM   1859 C  CG  . MET A 1 235 ? 4.379   18.729 4.952   1.00 67.67  ? 235 MET A CG  1 
ATOM   1860 S  SD  . MET A 1 235 ? 5.085   18.005 3.416   1.00 79.84  ? 235 MET A SD  1 
ATOM   1861 C  CE  . MET A 1 235 ? 3.655   17.958 2.336   1.00 72.81  ? 235 MET A CE  1 
ATOM   1862 N  N   . LYS A 1 236 ? 2.010   16.054 7.791   1.00 39.87  ? 236 LYS A N   1 
ATOM   1863 C  CA  . LYS A 1 236 ? 0.994   14.972 7.912   1.00 38.24  ? 236 LYS A CA  1 
ATOM   1864 C  C   . LYS A 1 236 ? -0.257  15.499 8.615   1.00 36.34  ? 236 LYS A C   1 
ATOM   1865 O  O   . LYS A 1 236 ? -1.344  15.008 8.304   1.00 38.39  ? 236 LYS A O   1 
ATOM   1866 C  CB  . LYS A 1 236 ? 1.590   13.772 8.662   1.00 45.34  ? 236 LYS A CB  1 
ATOM   1867 C  CG  . LYS A 1 236 ? 1.062   12.397 8.279   1.00 56.12  ? 236 LYS A CG  1 
ATOM   1868 C  CD  . LYS A 1 236 ? 1.914   11.264 8.871   1.00 60.23  ? 236 LYS A CD  1 
ATOM   1869 C  CE  . LYS A 1 236 ? 1.395   9.872  8.564   1.00 65.36  ? 236 LYS A CE  1 
ATOM   1870 N  NZ  . LYS A 1 236 ? 2.355   8.836  9.018   1.00 65.18  ? 236 LYS A NZ  1 
ATOM   1871 N  N   . TYR A 1 237 ? -0.148  16.462 9.545   1.00 35.47  ? 237 TYR A N   1 
ATOM   1872 C  CA  . TYR A 1 237 ? -1.319  16.957 10.315  1.00 31.84  ? 237 TYR A CA  1 
ATOM   1873 C  C   . TYR A 1 237 ? -1.767  18.328 9.780   1.00 33.71  ? 237 TYR A C   1 
ATOM   1874 O  O   . TYR A 1 237 ? -2.538  18.982 10.500  1.00 31.31  ? 237 TYR A O   1 
ATOM   1875 C  CB  . TYR A 1 237 ? -1.027  17.030 11.816  1.00 32.42  ? 237 TYR A CB  1 
ATOM   1876 C  CG  . TYR A 1 237 ? -0.889  15.667 12.447  1.00 32.54  ? 237 TYR A CG  1 
ATOM   1877 C  CD1 . TYR A 1 237 ? 0.296   14.967 12.345  1.00 35.15  ? 237 TYR A CD1 1 
ATOM   1878 C  CD2 . TYR A 1 237 ? -1.976  15.048 13.041  1.00 31.99  ? 237 TYR A CD2 1 
ATOM   1879 C  CE1 . TYR A 1 237 ? 0.419   13.694 12.879  1.00 36.01  ? 237 TYR A CE1 1 
ATOM   1880 C  CE2 . TYR A 1 237 ? -1.869  13.778 13.584  1.00 35.39  ? 237 TYR A CE2 1 
ATOM   1881 C  CZ  . TYR A 1 237 ? -0.662  13.110 13.505  1.00 34.60  ? 237 TYR A CZ  1 
ATOM   1882 O  OH  . TYR A 1 237 ? -0.538  11.855 14.030  1.00 40.63  ? 237 TYR A OH  1 
ATOM   1883 N  N   . ASN A 1 238 ? -1.350  18.721 8.574   1.00 30.88  ? 238 ASN A N   1 
ATOM   1884 C  CA  . ASN A 1 238 ? -1.917  19.945 7.949   1.00 30.64  ? 238 ASN A CA  1 
ATOM   1885 C  C   . ASN A 1 238 ? -1.427  21.160 8.767   1.00 26.40  ? 238 ASN A C   1 
ATOM   1886 O  O   . ASN A 1 238 ? -2.173  22.154 8.917   1.00 24.27  ? 238 ASN A O   1 
ATOM   1887 C  CB  . ASN A 1 238 ? -3.446  19.883 7.962   1.00 35.00  ? 238 ASN A CB  1 
ATOM   1888 C  CG  . ASN A 1 238 ? -4.119  20.832 7.001   1.00 45.33  ? 238 ASN A CG  1 
ATOM   1889 O  OD1 . ASN A 1 238 ? -5.110  21.476 7.352   1.00 46.58  ? 238 ASN A OD1 1 
ATOM   1890 N  ND2 . ASN A 1 238 ? -3.600  20.930 5.789   1.00 52.64  ? 238 ASN A ND2 1 
ATOM   1891 N  N   . TYR A 1 239 ? -0.213  21.077 9.275   1.00 22.08  ? 239 TYR A N   1 
ATOM   1892 C  CA  . TYR A 1 239 ? 0.510   22.195 9.905   1.00 21.49  ? 239 TYR A CA  1 
ATOM   1893 C  C   . TYR A 1 239 ? 1.440   22.856 8.888   1.00 22.56  ? 239 TYR A C   1 
ATOM   1894 O  O   . TYR A 1 239 ? 2.083   22.187 8.021   1.00 21.43  ? 239 TYR A O   1 
ATOM   1895 C  CB  . TYR A 1 239 ? 1.284   21.693 11.134  1.00 21.15  ? 239 TYR A CB  1 
ATOM   1896 C  CG  . TYR A 1 239 ? 0.512   21.677 12.426  1.00 17.82  ? 239 TYR A CG  1 
ATOM   1897 C  CD1 . TYR A 1 239 ? -0.681  20.970 12.544  1.00 21.40  ? 239 TYR A CD1 1 
ATOM   1898 C  CD2 . TYR A 1 239 ? 0.987   22.325 13.556  1.00 18.35  ? 239 TYR A CD2 1 
ATOM   1899 C  CE1 . TYR A 1 239 ? -1.418  21.001 13.721  1.00 20.15  ? 239 TYR A CE1 1 
ATOM   1900 C  CE2 . TYR A 1 239 ? 0.284   22.324 14.736  1.00 18.16  ? 239 TYR A CE2 1 
ATOM   1901 C  CZ  . TYR A 1 239 ? -0.921  21.668 14.829  1.00 20.64  ? 239 TYR A CZ  1 
ATOM   1902 O  OH  . TYR A 1 239 ? -1.585  21.722 16.026  1.00 22.66  ? 239 TYR A OH  1 
ATOM   1903 N  N   . GLU A 1 240 ? 1.554   24.173 8.980   1.00 21.50  ? 240 GLU A N   1 
ATOM   1904 C  CA  . GLU A 1 240 ? 2.526   24.981 8.205   1.00 24.94  ? 240 GLU A CA  1 
ATOM   1905 C  C   . GLU A 1 240 ? 3.937   24.490 8.493   1.00 25.25  ? 240 GLU A C   1 
ATOM   1906 O  O   . GLU A 1 240 ? 4.285   24.089 9.605   1.00 21.07  ? 240 GLU A O   1 
ATOM   1907 C  CB  . GLU A 1 240 ? 2.456   26.483 8.526   1.00 25.03  ? 240 GLU A CB  1 
ATOM   1908 C  CG  . GLU A 1 240 ? 1.250   27.168 7.851   1.00 29.49  ? 240 GLU A CG  1 
ATOM   1909 C  CD  . GLU A 1 240 ? 1.331   27.219 6.327   1.00 31.33  ? 240 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A 1 240 ? 0.575   26.468 5.642   1.00 29.88  ? 240 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A 1 240 ? 2.174   27.993 5.812   1.00 37.22  ? 240 GLU A OE2 1 
ATOM   1912 N  N   . PRO A 1 241 ? 4.860   24.564 7.520   1.00 29.71  ? 241 PRO A N   1 
ATOM   1913 C  CA  . PRO A 1 241 ? 6.265   24.324 7.808   1.00 28.17  ? 241 PRO A CA  1 
ATOM   1914 C  C   . PRO A 1 241 ? 6.813   25.254 8.880   1.00 29.34  ? 241 PRO A C   1 
ATOM   1915 O  O   . PRO A 1 241 ? 6.468   26.446 8.965   1.00 28.38  ? 241 PRO A O   1 
ATOM   1916 C  CB  . PRO A 1 241 ? 6.964   24.600 6.457   1.00 31.69  ? 241 PRO A CB  1 
ATOM   1917 C  CG  . PRO A 1 241 ? 5.878   24.357 5.459   1.00 30.99  ? 241 PRO A CG  1 
ATOM   1918 C  CD  . PRO A 1 241 ? 4.604   24.876 6.103   1.00 30.93  ? 241 PRO A CD  1 
ATOM   1919 N  N   . LEU A 1 242 ? 7.620   24.696 9.765   1.00 24.94  ? 242 LEU A N   1 
ATOM   1920 C  CA  . LEU A 1 242 ? 8.375   25.508 10.725  1.00 24.70  ? 242 LEU A CA  1 
ATOM   1921 C  C   . LEU A 1 242 ? 9.758   25.755 10.126  1.00 29.51  ? 242 LEU A C   1 
ATOM   1922 O  O   . LEU A 1 242 ? 10.406  24.766 9.734   1.00 27.01  ? 242 LEU A O   1 
ATOM   1923 C  CB  . LEU A 1 242 ? 8.448   24.768 12.070  1.00 22.81  ? 242 LEU A CB  1 
ATOM   1924 C  CG  . LEU A 1 242 ? 8.974   25.594 13.229  1.00 24.31  ? 242 LEU A CG  1 
ATOM   1925 C  CD1 . LEU A 1 242 ? 7.918   26.572 13.710  1.00 24.84  ? 242 LEU A CD1 1 
ATOM   1926 C  CD2 . LEU A 1 242 ? 9.381   24.665 14.343  1.00 25.52  ? 242 LEU A CD2 1 
ATOM   1927 N  N   . THR A 1 243 ? 10.184  27.006 10.075  1.00 30.63  ? 243 THR A N   1 
ATOM   1928 C  CA  . THR A 1 243 ? 11.455  27.412 9.440   1.00 31.78  ? 243 THR A CA  1 
ATOM   1929 C  C   . THR A 1 243 ? 12.480  27.712 10.520  1.00 33.06  ? 243 THR A C   1 
ATOM   1930 O  O   . THR A 1 243 ? 12.101  27.915 11.672  1.00 29.80  ? 243 THR A O   1 
ATOM   1931 C  CB  . THR A 1 243 ? 11.270  28.637 8.538   1.00 29.18  ? 243 THR A CB  1 
ATOM   1932 O  OG1 . THR A 1 243 ? 11.006  29.756 9.378   1.00 31.80  ? 243 THR A OG1 1 
ATOM   1933 C  CG2 . THR A 1 243 ? 10.211  28.441 7.483   1.00 32.47  ? 243 THR A CG2 1 
ATOM   1934 N  N   . GLN A 1 244 ? 13.765  27.758 10.164  1.00 30.62  ? 244 GLN A N   1 
ATOM   1935 C  CA  . GLN A 1 244 ? 14.823  28.155 11.104  1.00 33.15  ? 244 GLN A CA  1 
ATOM   1936 C  C   . GLN A 1 244 ? 14.555  29.570 11.631  1.00 31.06  ? 244 GLN A C   1 
ATOM   1937 O  O   . GLN A 1 244 ? 14.932  29.865 12.802  1.00 36.20  ? 244 GLN A O   1 
ATOM   1938 C  CB  . GLN A 1 244 ? 16.210  28.010 10.456  1.00 35.20  ? 244 GLN A CB  1 
ATOM   1939 C  CG  . GLN A 1 244 ? 17.305  28.536 11.371  1.00 38.70  ? 244 GLN A CG  1 
ATOM   1940 C  CD  . GLN A 1 244 ? 17.357  27.715 12.633  1.00 36.80  ? 244 GLN A CD  1 
ATOM   1941 O  OE1 . GLN A 1 244 ? 17.148  26.498 12.607  1.00 39.80  ? 244 GLN A OE1 1 
ATOM   1942 N  NE2 . GLN A 1 244 ? 17.626  28.376 13.739  1.00 41.15  ? 244 GLN A NE2 1 
ATOM   1943 N  N   . ASP A 1 245 ? 13.968  30.445 10.818  1.00 34.72  ? 245 ASP A N   1 
ATOM   1944 C  CA  . ASP A 1 245 ? 13.678  31.833 11.266  1.00 35.01  ? 245 ASP A CA  1 
ATOM   1945 C  C   . ASP A 1 245 ? 12.627  31.781 12.382  1.00 30.47  ? 245 ASP A C   1 
ATOM   1946 O  O   . ASP A 1 245 ? 12.822  32.508 13.377  1.00 33.48  ? 245 ASP A O   1 
ATOM   1947 C  CB  . ASP A 1 245 ? 13.211  32.726 10.126  1.00 36.30  ? 245 ASP A CB  1 
ATOM   1948 C  CG  . ASP A 1 245 ? 14.346  33.092 9.182   1.00 41.99  ? 245 ASP A CG  1 
ATOM   1949 O  OD1 . ASP A 1 245 ? 15.588  32.848 9.557   1.00 41.34  ? 245 ASP A OD1 1 
ATOM   1950 O  OD2 . ASP A 1 245 ? 14.009  33.600 8.083   1.00 42.51  ? 245 ASP A OD2 1 
ATOM   1951 N  N   . HIS A 1 246 ? 11.604  30.939 12.213  1.00 31.10  ? 246 HIS A N   1 
ATOM   1952 C  CA  . HIS A 1 246 ? 10.564  30.656 13.245  1.00 29.82  ? 246 HIS A CA  1 
ATOM   1953 C  C   . HIS A 1 246 ? 11.246  30.177 14.522  1.00 32.07  ? 246 HIS A C   1 
ATOM   1954 O  O   . HIS A 1 246 ? 10.915  30.710 15.581  1.00 31.01  ? 246 HIS A O   1 
ATOM   1955 C  CB  . HIS A 1 246 ? 9.586   29.596 12.790  1.00 26.33  ? 246 HIS A CB  1 
ATOM   1956 C  CG  . HIS A 1 246 ? 8.647   29.993 11.717  1.00 24.00  ? 246 HIS A CG  1 
ATOM   1957 N  ND1 . HIS A 1 246 ? 8.141   29.071 10.849  1.00 25.10  ? 246 HIS A ND1 1 
ATOM   1958 C  CD2 . HIS A 1 246 ? 8.057   31.183 11.415  1.00 24.44  ? 246 HIS A CD2 1 
ATOM   1959 C  CE1 . HIS A 1 246 ? 7.285   29.657 10.021  1.00 24.94  ? 246 HIS A CE1 1 
ATOM   1960 N  NE2 . HIS A 1 246 ? 7.217   30.955 10.382  1.00 24.77  ? 246 HIS A NE2 1 
ATOM   1961 N  N   . VAL A 1 247 ? 12.199  29.231 14.412  1.00 31.35  ? 247 VAL A N   1 
ATOM   1962 C  CA  . VAL A 1 247 ? 13.039  28.760 15.562  1.00 34.14  ? 247 VAL A CA  1 
ATOM   1963 C  C   . VAL A 1 247 ? 13.709  29.975 16.208  1.00 34.42  ? 247 VAL A C   1 
ATOM   1964 O  O   . VAL A 1 247 ? 13.624  30.101 17.452  1.00 32.63  ? 247 VAL A O   1 
ATOM   1965 C  CB  . VAL A 1 247 ? 14.043  27.660 15.150  1.00 30.80  ? 247 VAL A CB  1 
ATOM   1966 C  CG1 . VAL A 1 247 ? 14.971  27.254 16.274  1.00 33.15  ? 247 VAL A CG1 1 
ATOM   1967 C  CG2 . VAL A 1 247 ? 13.335  26.431 14.617  1.00 30.97  ? 247 VAL A CG2 1 
ATOM   1968 N  N   . ASP A 1 248 ? 14.293  30.887 15.408  1.00 36.71  ? 248 ASP A N   1 
ATOM   1969 C  CA  . ASP A 1 248 ? 15.022  32.064 15.954  1.00 38.68  ? 248 ASP A CA  1 
ATOM   1970 C  C   . ASP A 1 248 ? 14.026  33.047 16.579  1.00 33.87  ? 248 ASP A C   1 
ATOM   1971 O  O   . ASP A 1 248 ? 14.305  33.603 17.650  1.00 32.54  ? 248 ASP A O   1 
ATOM   1972 C  CB  . ASP A 1 248 ? 15.971  32.640 14.900  1.00 42.69  ? 248 ASP A CB  1 
ATOM   1973 C  CG  . ASP A 1 248 ? 17.047  31.642 14.498  1.00 45.91  ? 248 ASP A CG  1 
ATOM   1974 O  OD1 . ASP A 1 248 ? 17.647  31.025 15.408  1.00 45.47  ? 248 ASP A OD1 1 
ATOM   1975 O  OD2 . ASP A 1 248 ? 17.221  31.436 13.279  1.00 56.28  ? 248 ASP A OD2 1 
ATOM   1976 N  N   . ILE A 1 249 ? 12.836  33.182 16.011  1.00 34.61  ? 249 ILE A N   1 
ATOM   1977 C  CA  . ILE A 1 249 ? 11.791  34.083 16.594  1.00 33.17  ? 249 ILE A CA  1 
ATOM   1978 C  C   . ILE A 1 249 ? 11.322  33.543 17.958  1.00 29.18  ? 249 ILE A C   1 
ATOM   1979 O  O   . ILE A 1 249 ? 10.989  34.377 18.856  1.00 31.71  ? 249 ILE A O   1 
ATOM   1980 C  CB  . ILE A 1 249 ? 10.623  34.273 15.612  1.00 34.60  ? 249 ILE A CB  1 
ATOM   1981 C  CG1 . ILE A 1 249 ? 11.055  35.129 14.424  1.00 33.94  ? 249 ILE A CG1 1 
ATOM   1982 C  CG2 . ILE A 1 249 ? 9.435   34.890 16.305  1.00 34.38  ? 249 ILE A CG2 1 
ATOM   1983 C  CD1 . ILE A 1 249 ? 10.321  34.799 13.166  1.00 30.31  ? 249 ILE A CD1 1 
ATOM   1984 N  N   . LEU A 1 250 ? 11.304  32.225 18.124  1.00 29.29  ? 250 LEU A N   1 
ATOM   1985 C  CA  . LEU A 1 250 ? 10.926  31.557 19.401  1.00 26.77  ? 250 LEU A CA  1 
ATOM   1986 C  C   . LEU A 1 250 ? 12.105  31.575 20.403  1.00 29.55  ? 250 LEU A C   1 
ATOM   1987 O  O   . LEU A 1 250 ? 11.866  31.263 21.553  1.00 28.61  ? 250 LEU A O   1 
ATOM   1988 C  CB  . LEU A 1 250 ? 10.481  30.118 19.111  1.00 24.34  ? 250 LEU A CB  1 
ATOM   1989 C  CG  . LEU A 1 250 ? 9.162   29.962 18.361  1.00 23.29  ? 250 LEU A CG  1 
ATOM   1990 C  CD1 . LEU A 1 250 ? 8.985   28.554 17.880  1.00 23.87  ? 250 LEU A CD1 1 
ATOM   1991 C  CD2 . LEU A 1 250 ? 7.988   30.363 19.262  1.00 23.28  ? 250 LEU A CD2 1 
ATOM   1992 N  N   . GLY A 1 251 ? 13.284  32.064 20.008  1.00 31.36  ? 251 GLY A N   1 
ATOM   1993 C  CA  . GLY A 1 251 ? 14.489  32.199 20.863  1.00 33.90  ? 251 GLY A CA  1 
ATOM   1994 C  C   . GLY A 1 251 ? 14.200  32.768 22.244  1.00 31.87  ? 251 GLY A C   1 
ATOM   1995 O  O   . GLY A 1 251 ? 14.472  32.121 23.257  1.00 32.93  ? 251 GLY A O   1 
ATOM   1996 N  N   . PRO A 1 252 ? 13.695  34.018 22.336  1.00 32.45  ? 252 PRO A N   1 
ATOM   1997 C  CA  . PRO A 1 252 ? 13.483  34.652 23.633  1.00 35.27  ? 252 PRO A CA  1 
ATOM   1998 C  C   . PRO A 1 252 ? 12.555  33.831 24.549  1.00 30.51  ? 252 PRO A C   1 
ATOM   1999 O  O   . PRO A 1 252 ? 12.803  33.781 25.722  1.00 32.84  ? 252 PRO A O   1 
ATOM   2000 C  CB  . PRO A 1 252 ? 12.879  36.016 23.260  1.00 36.50  ? 252 PRO A CB  1 
ATOM   2001 C  CG  . PRO A 1 252 ? 13.363  36.274 21.860  1.00 36.99  ? 252 PRO A CG  1 
ATOM   2002 C  CD  . PRO A 1 252 ? 13.409  34.914 21.215  1.00 35.57  ? 252 PRO A CD  1 
ATOM   2003 N  N   . LEU A 1 253 ? 11.488  33.214 24.015  1.00 27.50  ? 253 LEU A N   1 
ATOM   2004 C  CA  . LEU A 1 253 ? 10.570  32.403 24.829  1.00 22.63  ? 253 LEU A CA  1 
ATOM   2005 C  C   . LEU A 1 253 ? 11.322  31.143 25.244  1.00 24.42  ? 253 LEU A C   1 
ATOM   2006 O  O   . LEU A 1 253 ? 11.161  30.683 26.368  1.00 25.22  ? 253 LEU A O   1 
ATOM   2007 C  CB  . LEU A 1 253 ? 9.341   32.009 23.989  1.00 23.61  ? 253 LEU A CB  1 
ATOM   2008 C  CG  . LEU A 1 253 ? 8.315   33.137 23.775  1.00 26.03  ? 253 LEU A CG  1 
ATOM   2009 C  CD1 . LEU A 1 253 ? 7.222   32.634 22.830  1.00 23.98  ? 253 LEU A CD1 1 
ATOM   2010 C  CD2 . LEU A 1 253 ? 7.751   33.634 25.069  1.00 28.22  ? 253 LEU A CD2 1 
ATOM   2011 N  N   . SER A 1 254 ? 12.126  30.607 24.337  1.00 26.89  ? 254 SER A N   1 
ATOM   2012 C  CA  . SER A 1 254 ? 12.987  29.425 24.644  1.00 30.74  ? 254 SER A CA  1 
ATOM   2013 C  C   . SER A 1 254 ? 13.936  29.771 25.813  1.00 30.65  ? 254 SER A C   1 
ATOM   2014 O  O   . SER A 1 254 ? 14.022  29.008 26.757  1.00 31.74  ? 254 SER A O   1 
ATOM   2015 C  CB  . SER A 1 254 ? 13.744  28.989 23.420  1.00 32.63  ? 254 SER A CB  1 
ATOM   2016 O  OG  . SER A 1 254 ? 14.473  27.818 23.672  1.00 36.48  ? 254 SER A OG  1 
ATOM   2017 N  N   . ALA A 1 255 ? 14.572  30.925 25.772  1.00 35.09  ? 255 ALA A N   1 
ATOM   2018 C  CA  . ALA A 1 255 ? 15.532  31.384 26.804  1.00 38.10  ? 255 ALA A CA  1 
ATOM   2019 C  C   . ALA A 1 255 ? 14.799  31.633 28.127  1.00 40.00  ? 255 ALA A C   1 
ATOM   2020 O  O   . ALA A 1 255 ? 15.338  31.302 29.174  1.00 35.20  ? 255 ALA A O   1 
ATOM   2021 C  CB  . ALA A 1 255 ? 16.246  32.631 26.325  1.00 42.49  ? 255 ALA A CB  1 
ATOM   2022 N  N   . GLN A 1 256 ? 13.593  32.203 28.097  1.00 36.40  ? 256 GLN A N   1 
ATOM   2023 C  CA  . GLN A 1 256 ? 12.873  32.550 29.350  1.00 35.40  ? 256 GLN A CA  1 
ATOM   2024 C  C   . GLN A 1 256 ? 12.531  31.254 30.098  1.00 35.31  ? 256 GLN A C   1 
ATOM   2025 O  O   . GLN A 1 256 ? 12.603  31.258 31.350  1.00 37.00  ? 256 GLN A O   1 
ATOM   2026 C  CB  . GLN A 1 256 ? 11.611  33.369 29.054  1.00 36.53  ? 256 GLN A CB  1 
ATOM   2027 C  CG  . GLN A 1 256 ? 11.027  34.043 30.287  1.00 42.38  ? 256 GLN A CG  1 
ATOM   2028 C  CD  . GLN A 1 256 ? 9.741   34.786 29.989  1.00 45.65  ? 256 GLN A CD  1 
ATOM   2029 O  OE1 . GLN A 1 256 ? 9.583   35.366 28.918  1.00 45.19  ? 256 GLN A OE1 1 
ATOM   2030 N  NE2 . GLN A 1 256 ? 8.798   34.750 30.923  1.00 40.77  ? 256 GLN A NE2 1 
ATOM   2031 N  N   . THR A 1 257 ? 12.188  30.182 29.377  1.00 28.66  ? 257 THR A N   1 
ATOM   2032 C  CA  . THR A 1 257 ? 11.572  28.973 29.955  1.00 25.95  ? 257 THR A CA  1 
ATOM   2033 C  C   . THR A 1 257 ? 12.631  27.866 30.116  1.00 26.93  ? 257 THR A C   1 
ATOM   2034 O  O   . THR A 1 257 ? 12.315  26.856 30.768  1.00 28.43  ? 257 THR A O   1 
ATOM   2035 C  CB  . THR A 1 257 ? 10.460  28.425 29.066  1.00 26.40  ? 257 THR A CB  1 
ATOM   2036 O  OG1 . THR A 1 257 ? 11.004  28.074 27.791  1.00 26.55  ? 257 THR A OG1 1 
ATOM   2037 C  CG2 . THR A 1 257 ? 9.320   29.414 28.922  1.00 26.47  ? 257 THR A CG2 1 
ATOM   2038 N  N   . GLY A 1 258 ? 13.775  28.028 29.449  1.00 32.25  ? 258 GLY A N   1 
ATOM   2039 C  CA  . GLY A 1 258 ? 14.837  27.004 29.366  1.00 34.87  ? 258 GLY A CA  1 
ATOM   2040 C  C   . GLY A 1 258 ? 14.416  25.777 28.578  1.00 37.09  ? 258 GLY A C   1 
ATOM   2041 O  O   . GLY A 1 258 ? 14.994  24.712 28.784  1.00 37.55  ? 258 GLY A O   1 
ATOM   2042 N  N   . ILE A 1 259 ? 13.431  25.879 27.691  1.00 31.30  ? 259 ILE A N   1 
ATOM   2043 C  CA  . ILE A 1 259 ? 13.012  24.726 26.852  1.00 29.21  ? 259 ILE A CA  1 
ATOM   2044 C  C   . ILE A 1 259 ? 13.444  25.035 25.429  1.00 33.22  ? 259 ILE A C   1 
ATOM   2045 O  O   . ILE A 1 259 ? 13.000  26.058 24.875  1.00 27.55  ? 259 ILE A O   1 
ATOM   2046 C  CB  . ILE A 1 259 ? 11.515  24.459 26.981  1.00 28.86  ? 259 ILE A CB  1 
ATOM   2047 C  CG1 . ILE A 1 259 ? 11.153  24.142 28.430  1.00 30.08  ? 259 ILE A CG1 1 
ATOM   2048 C  CG2 . ILE A 1 259 ? 11.058  23.383 26.015  1.00 28.51  ? 259 ILE A CG2 1 
ATOM   2049 C  CD1 . ILE A 1 259 ? 9.696   24.169 28.664  1.00 34.58  ? 259 ILE A CD1 1 
ATOM   2050 N  N   . ALA A 1 260 ? 14.377  24.237 24.915  1.00 29.44  ? 260 ALA A N   1 
ATOM   2051 C  CA  . ALA A 1 260 ? 14.884  24.376 23.532  1.00 29.36  ? 260 ALA A CA  1 
ATOM   2052 C  C   . ALA A 1 260 ? 13.706  24.286 22.573  1.00 24.89  ? 260 ALA A C   1 
ATOM   2053 O  O   . ALA A 1 260 ? 12.778  23.481 22.799  1.00 23.71  ? 260 ALA A O   1 
ATOM   2054 C  CB  . ALA A 1 260 ? 15.887  23.288 23.215  1.00 29.31  ? 260 ALA A CB  1 
ATOM   2055 N  N   . VAL A 1 261 ? 13.772  25.029 21.487  1.00 27.03  ? 261 VAL A N   1 
ATOM   2056 C  CA  . VAL A 1 261 ? 12.633  25.042 20.536  1.00 24.24  ? 261 VAL A CA  1 
ATOM   2057 C  C   . VAL A 1 261 ? 12.403  23.634 20.025  1.00 23.15  ? 261 VAL A C   1 
ATOM   2058 O  O   . VAL A 1 261 ? 11.295  23.212 19.922  1.00 20.66  ? 261 VAL A O   1 
ATOM   2059 C  CB  . VAL A 1 261 ? 12.885  26.024 19.386  1.00 25.93  ? 261 VAL A CB  1 
ATOM   2060 C  CG1 . VAL A 1 261 ? 11.820  25.876 18.312  1.00 25.57  ? 261 VAL A CG1 1 
ATOM   2061 C  CG2 . VAL A 1 261 ? 13.001  27.439 19.907  1.00 26.51  ? 261 VAL A CG2 1 
ATOM   2062 N  N   . LEU A 1 262 ? 13.453  22.893 19.633  1.00 23.13  ? 262 LEU A N   1 
ATOM   2063 C  CA  . LEU A 1 262 ? 13.197  21.548 19.075  1.00 22.99  ? 262 LEU A CA  1 
ATOM   2064 C  C   . LEU A 1 262 ? 12.669  20.583 20.142  1.00 21.23  ? 262 LEU A C   1 
ATOM   2065 O  O   . LEU A 1 262 ? 12.048  19.608 19.767  1.00 24.50  ? 262 LEU A O   1 
ATOM   2066 C  CB  . LEU A 1 262 ? 14.493  21.039 18.428  1.00 23.92  ? 262 LEU A CB  1 
ATOM   2067 C  CG  . LEU A 1 262 ? 14.839  21.812 17.168  1.00 24.33  ? 262 LEU A CG  1 
ATOM   2068 C  CD1 . LEU A 1 262 ? 16.250  21.452 16.699  1.00 28.36  ? 262 LEU A CD1 1 
ATOM   2069 C  CD2 . LEU A 1 262 ? 13.798  21.594 16.078  1.00 25.11  ? 262 LEU A CD2 1 
ATOM   2070 N  N   . ASP A 1 263 ? 12.899  20.851 21.432  1.00 22.82  ? 263 ASP A N   1 
ATOM   2071 C  CA  . ASP A 1 263 ? 12.311  20.043 22.530  1.00 25.03  ? 263 ASP A CA  1 
ATOM   2072 C  C   . ASP A 1 263 ? 10.807  20.370 22.626  1.00 21.06  ? 263 ASP A C   1 
ATOM   2073 O  O   . ASP A 1 263 ? 10.008  19.466 22.701  1.00 22.89  ? 263 ASP A O   1 
ATOM   2074 C  CB  . ASP A 1 263 ? 13.015  20.335 23.865  1.00 29.15  ? 263 ASP A CB  1 
ATOM   2075 C  CG  . ASP A 1 263 ? 14.437  19.791 23.960  1.00 34.18  ? 263 ASP A CG  1 
ATOM   2076 O  OD1 . ASP A 1 263 ? 14.850  19.106 23.019  1.00 33.09  ? 263 ASP A OD1 1 
ATOM   2077 O  OD2 . ASP A 1 263 ? 15.095  20.057 24.982  1.00 36.70  ? 263 ASP A OD2 1 
ATOM   2078 N  N   . MET A 1 264 ? 10.448  21.624 22.405  1.00 22.16  ? 264 MET A N   1 
ATOM   2079 C  CA  . MET A 1 264 ? 9.017   21.981 22.350  1.00 21.98  ? 264 MET A CA  1 
ATOM   2080 C  C   . MET A 1 264 ? 8.390   21.406 21.091  1.00 21.73  ? 264 MET A C   1 
ATOM   2081 O  O   . MET A 1 264 ? 7.264   20.919 21.160  1.00 20.41  ? 264 MET A O   1 
ATOM   2082 C  CB  . MET A 1 264 ? 8.804   23.495 22.408  1.00 21.70  ? 264 MET A CB  1 
ATOM   2083 C  CG  . MET A 1 264 ? 7.325   23.824 22.676  1.00 21.86  ? 264 MET A CG  1 
ATOM   2084 S  SD  . MET A 1 264 ? 6.785   23.364 24.350  1.00 21.45  ? 264 MET A SD  1 
ATOM   2085 C  CE  . MET A 1 264 ? 7.349   24.773 25.235  1.00 20.53  ? 264 MET A CE  1 
ATOM   2086 N  N   . CYS A 1 265 ? 9.133   21.311 19.974  1.00 21.06  ? 265 CYS A N   1 
ATOM   2087 C  CA  . CYS A 1 265 ? 8.621   20.594 18.777  1.00 22.74  ? 265 CYS A CA  1 
ATOM   2088 C  C   . CYS A 1 265 ? 8.346   19.120 19.095  1.00 20.09  ? 265 CYS A C   1 
ATOM   2089 O  O   . CYS A 1 265 ? 7.396   18.561 18.579  1.00 21.78  ? 265 CYS A O   1 
ATOM   2090 C  CB  . CYS A 1 265 ? 9.624   20.739 17.629  1.00 22.64  ? 265 CYS A CB  1 
ATOM   2091 S  SG  . CYS A 1 265 ? 9.733   22.425 16.969  1.00 23.41  ? 265 CYS A SG  1 
ATOM   2092 N  N   . ALA A 1 266 ? 9.190   18.456 19.920  1.00 22.47  ? 266 ALA A N   1 
ATOM   2093 C  CA  . ALA A 1 266 ? 8.997   17.041 20.271  1.00 22.29  ? 266 ALA A CA  1 
ATOM   2094 C  C   . ALA A 1 266 ? 7.707   16.907 21.089  1.00 20.51  ? 266 ALA A C   1 
ATOM   2095 O  O   . ALA A 1 266 ? 6.983   15.937 20.847  1.00 24.73  ? 266 ALA A O   1 
ATOM   2096 C  CB  . ALA A 1 266 ? 10.212  16.547 21.039  1.00 22.34  ? 266 ALA A CB  1 
ATOM   2097 N  N   . SER A 1 267 ? 7.460   17.884 21.972  1.00 23.64  ? 267 SER A N   1 
ATOM   2098 C  CA  . SER A 1 267 ? 6.230   17.974 22.785  1.00 24.78  ? 267 SER A CA  1 
ATOM   2099 C  C   . SER A 1 267 ? 5.036   18.064 21.837  1.00 22.40  ? 267 SER A C   1 
ATOM   2100 O  O   . SER A 1 267 ? 4.056   17.267 21.968  1.00 22.95  ? 267 SER A O   1 
ATOM   2101 C  CB  . SER A 1 267 ? 6.331   19.131 23.751  1.00 28.86  ? 267 SER A CB  1 
ATOM   2102 O  OG  . SER A 1 267 ? 5.102   19.340 24.441  1.00 32.52  ? 267 SER A OG  1 
ATOM   2103 N  N   . LEU A 1 268 ? 5.099   19.017 20.897  1.00 22.03  ? 268 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 268 ? 3.995   19.213 19.917  1.00 22.18  ? 268 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 268 ? 3.773   17.936 19.098  1.00 22.58  ? 268 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 268 ? 2.622   17.490 18.884  1.00 25.13  ? 268 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 268 ? 4.305   20.445 19.038  1.00 21.57  ? 268 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 268 ? 3.269   20.740 17.947  1.00 22.73  ? 268 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 268 ? 1.830   20.725 18.468  1.00 22.38  ? 268 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 268 ? 3.613   22.047 17.242  1.00 21.57  ? 268 LEU A CD2 1 
ATOM   2111 N  N   . LYS A 1 269 ? 4.842   17.303 18.613  1.00 25.61  ? 269 LYS A N   1 
ATOM   2112 C  CA  . LYS A 1 269 ? 4.717   16.038 17.849  1.00 27.00  ? 269 LYS A CA  1 
ATOM   2113 C  C   . LYS A 1 269 ? 3.890   15.049 18.665  1.00 23.33  ? 269 LYS A C   1 
ATOM   2114 O  O   . LYS A 1 269 ? 3.013   14.444 18.104  1.00 25.53  ? 269 LYS A O   1 
ATOM   2115 C  CB  . LYS A 1 269 ? 6.093   15.447 17.532  1.00 33.01  ? 269 LYS A CB  1 
ATOM   2116 C  CG  . LYS A 1 269 ? 6.071   14.091 16.828  1.00 34.83  ? 269 LYS A CG  1 
ATOM   2117 C  CD  . LYS A 1 269 ? 7.470   13.485 16.622  1.00 42.63  ? 269 LYS A CD  1 
ATOM   2118 C  CE  . LYS A 1 269 ? 8.509   14.472 16.117  1.00 45.48  ? 269 LYS A CE  1 
ATOM   2119 N  NZ  . LYS A 1 269 ? 9.774   13.807 15.707  1.00 49.96  ? 269 LYS A NZ  1 
ATOM   2120 N  N   . GLU A 1 270 ? 4.194   14.899 19.955  1.00 26.70  ? 270 GLU A N   1 
ATOM   2121 C  CA  . GLU A 1 270 ? 3.539   13.903 20.837  1.00 29.88  ? 270 GLU A CA  1 
ATOM   2122 C  C   . GLU A 1 270 ? 2.069   14.288 21.012  1.00 28.67  ? 270 GLU A C   1 
ATOM   2123 O  O   . GLU A 1 270 ? 1.193   13.409 20.947  1.00 29.59  ? 270 GLU A O   1 
ATOM   2124 C  CB  . GLU A 1 270 ? 4.289   13.818 22.167  1.00 32.09  ? 270 GLU A CB  1 
ATOM   2125 C  CG  . GLU A 1 270 ? 3.749   12.806 23.141  1.00 35.58  ? 270 GLU A CG  1 
ATOM   2126 C  CD  . GLU A 1 270 ? 4.660   12.636 24.367  1.00 41.38  ? 270 GLU A CD  1 
ATOM   2127 O  OE1 . GLU A 1 270 ? 4.668   13.529 25.236  1.00 42.18  ? 270 GLU A OE1 1 
ATOM   2128 O  OE2 . GLU A 1 270 ? 5.446   11.652 24.399  1.00 48.94  ? 270 GLU A OE2 1 
ATOM   2129 N  N   . LEU A 1 271 ? 1.803   15.583 21.129  1.00 26.10  ? 271 LEU A N   1 
ATOM   2130 C  CA  . LEU A 1 271 ? 0.405   16.063 21.284  1.00 24.05  ? 271 LEU A CA  1 
ATOM   2131 C  C   . LEU A 1 271 ? -0.337  15.776 19.986  1.00 24.81  ? 271 LEU A C   1 
ATOM   2132 O  O   . LEU A 1 271 ? -1.491  15.437 20.060  1.00 26.91  ? 271 LEU A O   1 
ATOM   2133 C  CB  . LEU A 1 271 ? 0.435   17.546 21.600  1.00 23.93  ? 271 LEU A CB  1 
ATOM   2134 C  CG  . LEU A 1 271 ? 0.791   17.939 23.022  1.00 24.71  ? 271 LEU A CG  1 
ATOM   2135 C  CD1 . LEU A 1 271 ? 0.948   19.441 23.120  1.00 24.04  ? 271 LEU A CD1 1 
ATOM   2136 C  CD2 . LEU A 1 271 ? -0.259  17.427 23.996  1.00 28.48  ? 271 LEU A CD2 1 
ATOM   2137 N  N   . LEU A 1 272 ? 0.309   15.910 18.825  1.00 26.31  ? 272 LEU A N   1 
ATOM   2138 C  CA  . LEU A 1 272 ? -0.349  15.624 17.526  1.00 26.11  ? 272 LEU A CA  1 
ATOM   2139 C  C   . LEU A 1 272 ? -0.607  14.117 17.394  1.00 29.26  ? 272 LEU A C   1 
ATOM   2140 O  O   . LEU A 1 272 ? -1.622  13.753 16.783  1.00 32.72  ? 272 LEU A O   1 
ATOM   2141 C  CB  . LEU A 1 272 ? 0.511   16.118 16.358  1.00 25.45  ? 272 LEU A CB  1 
ATOM   2142 C  CG  . LEU A 1 272 ? 0.527   17.642 16.184  1.00 28.50  ? 272 LEU A CG  1 
ATOM   2143 C  CD1 . LEU A 1 272 ? 1.418   18.022 15.019  1.00 29.09  ? 272 LEU A CD1 1 
ATOM   2144 C  CD2 . LEU A 1 272 ? -0.871  18.194 15.965  1.00 27.51  ? 272 LEU A CD2 1 
ATOM   2145 N  N   . GLN A 1 273 ? 0.309   13.270 17.874  1.00 33.35  ? 273 GLN A N   1 
ATOM   2146 C  CA  . GLN A 1 273 ? 0.176   11.788 17.706  1.00 33.36  ? 273 GLN A CA  1 
ATOM   2147 C  C   . GLN A 1 273 ? -0.765  11.200 18.767  1.00 34.70  ? 273 GLN A C   1 
ATOM   2148 O  O   . GLN A 1 273 ? -1.424  10.197 18.483  1.00 39.12  ? 273 GLN A O   1 
ATOM   2149 C  CB  . GLN A 1 273 ? 1.552   11.124 17.745  1.00 36.78  ? 273 GLN A CB  1 
ATOM   2150 C  CG  . GLN A 1 273 ? 2.378   11.379 16.494  1.00 36.71  ? 273 GLN A CG  1 
ATOM   2151 C  CD  . GLN A 1 273 ? 3.848   11.043 16.658  1.00 41.57  ? 273 GLN A CD  1 
ATOM   2152 O  OE1 . GLN A 1 273 ? 4.377   10.916 17.766  1.00 48.92  ? 273 GLN A OE1 1 
ATOM   2153 N  NE2 . GLN A 1 273 ? 4.545   10.938 15.538  1.00 43.98  ? 273 GLN A NE2 1 
ATOM   2154 N  N   . ASN A 1 274 ? -0.844  11.782 19.958  1.00 36.73  ? 274 ASN A N   1 
ATOM   2155 C  CA  . ASN A 1 274 ? -1.627  11.170 21.061  1.00 40.56  ? 274 ASN A CA  1 
ATOM   2156 C  C   . ASN A 1 274 ? -2.897  11.964 21.353  1.00 43.11  ? 274 ASN A C   1 
ATOM   2157 O  O   . ASN A 1 274 ? -3.767  11.408 22.022  1.00 42.53  ? 274 ASN A O   1 
ATOM   2158 C  CB  . ASN A 1 274 ? -0.772  11.023 22.314  1.00 44.12  ? 274 ASN A CB  1 
ATOM   2159 C  CG  . ASN A 1 274 ? 0.418   10.140 22.031  1.00 49.54  ? 274 ASN A CG  1 
ATOM   2160 O  OD1 . ASN A 1 274 ? 0.298   9.148  21.315  1.00 51.69  ? 274 ASN A OD1 1 
ATOM   2161 N  ND2 . ASN A 1 274 ? 1.571   10.514 22.549  1.00 59.60  ? 274 ASN A ND2 1 
ATOM   2162 N  N   . GLY A 1 275 ? -3.006  13.209 20.890  1.00 41.90  ? 275 GLY A N   1 
ATOM   2163 C  CA  . GLY A 1 275 ? -4.038  14.126 21.405  1.00 41.28  ? 275 GLY A CA  1 
ATOM   2164 C  C   . GLY A 1 275 ? -3.762  14.477 22.858  1.00 38.91  ? 275 GLY A C   1 
ATOM   2165 O  O   . GLY A 1 275 ? -2.641  14.198 23.346  1.00 40.07  ? 275 GLY A O   1 
ATOM   2166 N  N   . MET A 1 276 ? -4.727  15.127 23.509  1.00 41.54  ? 276 MET A N   1 
ATOM   2167 C  CA  . MET A 1 276 ? -4.608  15.712 24.867  1.00 47.25  ? 276 MET A CA  1 
ATOM   2168 C  C   . MET A 1 276 ? -5.201  14.767 25.915  1.00 47.87  ? 276 MET A C   1 
ATOM   2169 O  O   . MET A 1 276 ? -4.923  14.989 27.105  1.00 48.53  ? 276 MET A O   1 
ATOM   2170 C  CB  . MET A 1 276 ? -5.347  17.048 24.934  1.00 51.84  ? 276 MET A CB  1 
ATOM   2171 C  CG  . MET A 1 276 ? -4.669  18.129 24.149  1.00 53.86  ? 276 MET A CG  1 
ATOM   2172 S  SD  . MET A 1 276 ? -5.121  19.777 24.708  1.00 61.58  ? 276 MET A SD  1 
ATOM   2173 C  CE  . MET A 1 276 ? -4.506  20.670 23.290  1.00 54.55  ? 276 MET A CE  1 
ATOM   2174 N  N   . ASN A 1 277 ? -5.977  13.765 25.483  1.00 56.72  ? 277 ASN A N   1 
ATOM   2175 C  CA  . ASN A 1 277 ? -6.497  12.667 26.343  1.00 61.99  ? 277 ASN A CA  1 
ATOM   2176 C  C   . ASN A 1 277 ? -7.323  13.296 27.476  1.00 54.55  ? 277 ASN A C   1 
ATOM   2177 O  O   . ASN A 1 277 ? -7.003  13.057 28.652  1.00 56.22  ? 277 ASN A O   1 
ATOM   2178 C  CB  . ASN A 1 277 ? -5.330  11.790 26.823  1.00 67.90  ? 277 ASN A CB  1 
ATOM   2179 C  CG  . ASN A 1 277 ? -5.761  10.520 27.530  1.00 74.81  ? 277 ASN A CG  1 
ATOM   2180 O  OD1 . ASN A 1 277 ? -6.632  9.794  27.047  1.00 72.70  ? 277 ASN A OD1 1 
ATOM   2181 N  ND2 . ASN A 1 277 ? -5.153  10.241 28.675  1.00 72.14  ? 277 ASN A ND2 1 
ATOM   2182 N  N   . GLY A 1 278 ? -8.292  14.152 27.133  1.00 51.79  ? 278 GLY A N   1 
ATOM   2183 C  CA  . GLY A 1 278 ? -9.191  14.809 28.102  1.00 54.22  ? 278 GLY A CA  1 
ATOM   2184 C  C   . GLY A 1 278 ? -8.532  15.906 28.939  1.00 56.89  ? 278 GLY A C   1 
ATOM   2185 O  O   . GLY A 1 278 ? -9.203  16.413 29.853  1.00 58.56  ? 278 GLY A O   1 
ATOM   2186 N  N   . ARG A 1 279 ? -7.293  16.311 28.647  1.00 49.27  ? 279 ARG A N   1 
ATOM   2187 C  CA  . ARG A 1 279 ? -6.595  17.380 29.403  1.00 45.05  ? 279 ARG A CA  1 
ATOM   2188 C  C   . ARG A 1 279 ? -6.768  18.710 28.660  1.00 35.60  ? 279 ARG A C   1 
ATOM   2189 O  O   . ARG A 1 279 ? -7.205  18.702 27.511  1.00 35.23  ? 279 ARG A O   1 
ATOM   2190 C  CB  . ARG A 1 279 ? -5.128  16.996 29.575  1.00 50.56  ? 279 ARG A CB  1 
ATOM   2191 C  CG  . ARG A 1 279 ? -4.943  15.624 30.210  1.00 54.09  ? 279 ARG A CG  1 
ATOM   2192 C  CD  . ARG A 1 279 ? -3.509  15.378 30.622  1.00 63.78  ? 279 ARG A CD  1 
ATOM   2193 N  NE  . ARG A 1 279 ? -3.126  16.350 31.648  1.00 71.36  ? 279 ARG A NE  1 
ATOM   2194 C  CZ  . ARG A 1 279 ? -2.580  16.069 32.832  1.00 76.27  ? 279 ARG A CZ  1 
ATOM   2195 N  NH1 . ARG A 1 279 ? -2.311  14.820 33.180  1.00 74.41  ? 279 ARG A NH1 1 
ATOM   2196 N  NH2 . ARG A 1 279 ? -2.280  17.060 33.658  1.00 76.72  ? 279 ARG A NH2 1 
ATOM   2197 N  N   . THR A 1 280 ? -6.446  19.815 29.309  1.00 35.52  ? 280 THR A N   1 
ATOM   2198 C  CA  . THR A 1 280 ? -6.485  21.149 28.654  1.00 31.20  ? 280 THR A CA  1 
ATOM   2199 C  C   . THR A 1 280 ? -5.122  21.826 28.777  1.00 27.31  ? 280 THR A C   1 
ATOM   2200 O  O   . THR A 1 280 ? -4.291  21.490 29.665  1.00 25.41  ? 280 THR A O   1 
ATOM   2201 C  CB  . THR A 1 280 ? -7.615  22.009 29.234  1.00 33.73  ? 280 THR A CB  1 
ATOM   2202 O  OG1 . THR A 1 280 ? -7.366  22.178 30.628  1.00 33.86  ? 280 THR A OG1 1 
ATOM   2203 C  CG2 . THR A 1 280 ? -8.988  21.415 29.003  1.00 35.47  ? 280 THR A CG2 1 
ATOM   2204 N  N   . ILE A 1 281 ? -4.874  22.784 27.901  1.00 21.76  ? 281 ILE A N   1 
ATOM   2205 C  CA  . ILE A 1 281 ? -3.734  23.712 27.988  1.00 20.97  ? 281 ILE A CA  1 
ATOM   2206 C  C   . ILE A 1 281 ? -4.310  25.117 27.954  1.00 22.06  ? 281 ILE A C   1 
ATOM   2207 O  O   . ILE A 1 281 ? -5.037  25.426 26.983  1.00 20.87  ? 281 ILE A O   1 
ATOM   2208 C  CB  . ILE A 1 281 ? -2.736  23.451 26.837  1.00 20.31  ? 281 ILE A CB  1 
ATOM   2209 C  CG1 . ILE A 1 281 ? -2.235  22.005 26.885  1.00 24.55  ? 281 ILE A CG1 1 
ATOM   2210 C  CG2 . ILE A 1 281 ? -1.620  24.478 26.855  1.00 20.37  ? 281 ILE A CG2 1 
ATOM   2211 C  CD1 . ILE A 1 281 ? -1.282  21.660 25.760  1.00 23.54  ? 281 ILE A CD1 1 
ATOM   2212 N  N   . LEU A 1 282 ? -3.967  25.921 28.965  1.00 21.75  ? 282 LEU A N   1 
ATOM   2213 C  CA  . LEU A 1 282 ? -4.468  27.297 29.042  1.00 22.95  ? 282 LEU A CA  1 
ATOM   2214 C  C   . LEU A 1 282 ? -5.962  27.294 28.739  1.00 25.08  ? 282 LEU A C   1 
ATOM   2215 O  O   . LEU A 1 282 ? -6.435  28.212 28.021  1.00 24.24  ? 282 LEU A O   1 
ATOM   2216 C  CB  . LEU A 1 282 ? -3.646  28.148 28.086  1.00 21.78  ? 282 LEU A CB  1 
ATOM   2217 C  CG  . LEU A 1 282 ? -2.258  28.485 28.611  1.00 23.89  ? 282 LEU A CG  1 
ATOM   2218 C  CD1 . LEU A 1 282 ? -1.412  29.147 27.541  1.00 24.85  ? 282 LEU A CD1 1 
ATOM   2219 C  CD2 . LEU A 1 282 ? -2.275  29.333 29.894  1.00 26.38  ? 282 LEU A CD2 1 
ATOM   2220 N  N   . GLY A 1 283 ? -6.678  26.320 29.313  1.00 25.89  ? 283 GLY A N   1 
ATOM   2221 C  CA  . GLY A 1 283 ? -8.152  26.337 29.231  1.00 25.99  ? 283 GLY A CA  1 
ATOM   2222 C  C   . GLY A 1 283 ? -8.697  25.912 27.887  1.00 26.00  ? 283 GLY A C   1 
ATOM   2223 O  O   . GLY A 1 283 ? -9.893  26.028 27.673  1.00 30.89  ? 283 GLY A O   1 
ATOM   2224 N  N   . SER A 1 284 ? -7.874  25.495 26.934  1.00 22.78  ? 284 SER A N   1 
ATOM   2225 C  CA  . SER A 1 284 ? -8.318  24.946 25.634  1.00 22.09  ? 284 SER A CA  1 
ATOM   2226 C  C   . SER A 1 284 ? -8.142  23.421 25.562  1.00 22.97  ? 284 SER A C   1 
ATOM   2227 O  O   . SER A 1 284 ? -7.120  22.904 26.109  1.00 25.18  ? 284 SER A O   1 
ATOM   2228 C  CB  . SER A 1 284 ? -7.580  25.627 24.509  1.00 22.04  ? 284 SER A CB  1 
ATOM   2229 O  OG  . SER A 1 284 ? -8.116  25.202 23.260  1.00 27.33  ? 284 SER A OG  1 
ATOM   2230 N  N   . ALA A 1 285 ? -9.017  22.751 24.817  1.00 22.28  ? 285 ALA A N   1 
ATOM   2231 C  CA  . ALA A 1 285 ? -8.961  21.308 24.532  1.00 27.21  ? 285 ALA A CA  1 
ATOM   2232 C  C   . ALA A 1 285 ? -8.432  21.101 23.126  1.00 27.06  ? 285 ALA A C   1 
ATOM   2233 O  O   . ALA A 1 285 ? -8.417  19.929 22.690  1.00 29.16  ? 285 ALA A O   1 
ATOM   2234 C  CB  . ALA A 1 285 ? -10.309 20.643 24.722  1.00 30.90  ? 285 ALA A CB  1 
ATOM   2235 N  N   . LEU A 1 286 ? -7.989  22.180 22.453  1.00 23.87  ? 286 LEU A N   1 
ATOM   2236 C  CA  A LEU A 1 286 ? -7.422  22.209 21.080  0.50 22.92  ? 286 LEU A CA  1 
ATOM   2237 C  CA  B LEU A 1 286 ? -7.286  22.000 21.164  0.50 22.30  ? 286 LEU A CA  1 
ATOM   2238 C  C   . LEU A 1 286 ? -6.049  22.891 21.145  1.00 20.15  ? 286 LEU A C   1 
ATOM   2239 O  O   . LEU A 1 286 ? -5.832  23.666 22.084  1.00 20.43  ? 286 LEU A O   1 
ATOM   2240 C  CB  A LEU A 1 286 ? -8.312  23.055 20.152  0.50 24.27  ? 286 LEU A CB  1 
ATOM   2241 C  CB  B LEU A 1 286 ? -8.216  22.237 19.964  0.50 24.17  ? 286 LEU A CB  1 
ATOM   2242 C  CG  A LEU A 1 286 ? -9.650  22.489 19.689  0.50 24.54  ? 286 LEU A CG  1 
ATOM   2243 C  CG  B LEU A 1 286 ? -8.970  23.563 19.884  0.50 26.32  ? 286 LEU A CG  1 
ATOM   2244 C  CD1 A LEU A 1 286 ? -10.245 23.348 18.583  0.50 25.82  ? 286 LEU A CD1 1 
ATOM   2245 C  CD1 B LEU A 1 286 ? -9.994  23.690 20.987  0.50 31.60  ? 286 LEU A CD1 1 
ATOM   2246 C  CD2 A LEU A 1 286 ? -9.521  21.054 19.224  0.50 26.33  ? 286 LEU A CD2 1 
ATOM   2247 C  CD2 B LEU A 1 286 ? -8.029  24.762 19.870  0.50 25.78  ? 286 LEU A CD2 1 
ATOM   2248 N  N   . LEU A 1 287 ? -5.211  22.657 20.145  1.00 20.57  ? 287 LEU A N   1 
ATOM   2249 C  CA  . LEU A 1 287 ? -3.933  23.378 20.040  1.00 20.41  ? 287 LEU A CA  1 
ATOM   2250 C  C   . LEU A 1 287 ? -4.230  24.746 19.395  1.00 19.63  ? 287 LEU A C   1 
ATOM   2251 O  O   . LEU A 1 287 ? -4.553  24.785 18.216  1.00 26.49  ? 287 LEU A O   1 
ATOM   2252 C  CB  . LEU A 1 287 ? -2.979  22.491 19.238  1.00 21.09  ? 287 LEU A CB  1 
ATOM   2253 C  CG  . LEU A 1 287 ? -2.732  21.104 19.854  1.00 22.78  ? 287 LEU A CG  1 
ATOM   2254 C  CD1 . LEU A 1 287 ? -2.002  20.155 18.907  1.00 25.95  ? 287 LEU A CD1 1 
ATOM   2255 C  CD2 . LEU A 1 287 ? -1.939  21.225 21.138  1.00 25.56  ? 287 LEU A CD2 1 
ATOM   2256 N  N   . GLU A 1 288 ? -4.082  25.807 20.173  1.00 18.97  ? 288 GLU A N   1 
ATOM   2257 C  CA  . GLU A 1 288 ? -4.437  27.181 19.763  1.00 19.62  ? 288 GLU A CA  1 
ATOM   2258 C  C   . GLU A 1 288 ? -3.335  27.712 18.849  1.00 17.04  ? 288 GLU A C   1 
ATOM   2259 O  O   . GLU A 1 288 ? -2.164  27.700 19.240  1.00 16.45  ? 288 GLU A O   1 
ATOM   2260 C  CB  . GLU A 1 288 ? -4.644  28.049 20.997  1.00 20.16  ? 288 GLU A CB  1 
ATOM   2261 C  CG  . GLU A 1 288 ? -5.836  27.591 21.829  1.00 23.90  ? 288 GLU A CG  1 
ATOM   2262 C  CD  . GLU A 1 288 ? -7.192  27.902 21.196  1.00 35.44  ? 288 GLU A CD  1 
ATOM   2263 O  OE1 . GLU A 1 288 ? -8.205  27.191 21.527  1.00 37.00  ? 288 GLU A OE1 1 
ATOM   2264 O  OE2 . GLU A 1 288 ? -7.258  28.926 20.475  1.00 26.38  ? 288 GLU A OE2 1 
ATOM   2265 N  N   . ASP A 1 289 ? -3.734  28.332 17.731  1.00 18.01  ? 289 ASP A N   1 
ATOM   2266 C  CA  . ASP A 1 289 ? -2.729  28.855 16.762  1.00 16.39  ? 289 ASP A CA  1 
ATOM   2267 C  C   . ASP A 1 289 ? -2.915  30.357 16.471  1.00 16.34  ? 289 ASP A C   1 
ATOM   2268 O  O   . ASP A 1 289 ? -2.306  30.772 15.492  1.00 15.63  ? 289 ASP A O   1 
ATOM   2269 C  CB  . ASP A 1 289 ? -2.713  27.989 15.506  1.00 16.37  ? 289 ASP A CB  1 
ATOM   2270 C  CG  . ASP A 1 289 ? -3.795  28.275 14.475  1.00 17.20  ? 289 ASP A CG  1 
ATOM   2271 O  OD1 . ASP A 1 289 ? -4.866  28.789 14.900  1.00 17.92  ? 289 ASP A OD1 1 
ATOM   2272 O  OD2 . ASP A 1 289 ? -3.564  27.906 13.306  1.00 18.45  ? 289 ASP A OD2 1 
ATOM   2273 N  N   . GLU A 1 290 ? -3.689  31.112 17.249  1.00 17.17  ? 290 GLU A N   1 
ATOM   2274 C  CA  . GLU A 1 290 ? -3.904  32.546 16.943  1.00 18.07  ? 290 GLU A CA  1 
ATOM   2275 C  C   . GLU A 1 290 ? -3.233  33.412 18.013  1.00 19.31  ? 290 GLU A C   1 
ATOM   2276 O  O   . GLU A 1 290 ? -3.627  34.577 18.185  1.00 18.54  ? 290 GLU A O   1 
ATOM   2277 C  CB  . GLU A 1 290 ? -5.381  32.864 16.638  1.00 18.79  ? 290 GLU A CB  1 
ATOM   2278 C  CG  . GLU A 1 290 ? -5.862  32.177 15.362  1.00 18.95  ? 290 GLU A CG  1 
ATOM   2279 C  CD  . GLU A 1 290 ? -7.075  32.821 14.700  1.00 21.83  ? 290 GLU A CD  1 
ATOM   2280 O  OE1 . GLU A 1 290 ? -7.620  33.784 15.333  1.00 20.55  ? 290 GLU A OE1 1 
ATOM   2281 O  OE2 . GLU A 1 290 ? -7.486  32.330 13.604  1.00 20.50  ? 290 GLU A OE2 1 
ATOM   2282 N  N   . PHE A 1 291 ? -2.155  32.923 18.635  1.00 16.80  ? 291 PHE A N   1 
ATOM   2283 C  CA  . PHE A 1 291 ? -1.249  33.767 19.439  1.00 15.79  ? 291 PHE A CA  1 
ATOM   2284 C  C   . PHE A 1 291 ? 0.154   33.710 18.825  1.00 15.88  ? 291 PHE A C   1 
ATOM   2285 O  O   . PHE A 1 291 ? 0.715   32.601 18.749  1.00 17.44  ? 291 PHE A O   1 
ATOM   2286 C  CB  . PHE A 1 291 ? -1.152  33.356 20.913  1.00 17.19  ? 291 PHE A CB  1 
ATOM   2287 C  CG  . PHE A 1 291 ? -2.472  33.371 21.641  1.00 19.22  ? 291 PHE A CG  1 
ATOM   2288 C  CD1 . PHE A 1 291 ? -2.957  34.552 22.178  1.00 23.58  ? 291 PHE A CD1 1 
ATOM   2289 C  CD2 . PHE A 1 291 ? -3.230  32.223 21.772  1.00 20.76  ? 291 PHE A CD2 1 
ATOM   2290 C  CE1 . PHE A 1 291 ? -4.153  34.550 22.898  1.00 23.01  ? 291 PHE A CE1 1 
ATOM   2291 C  CE2 . PHE A 1 291 ? -4.418  32.224 22.496  1.00 25.19  ? 291 PHE A CE2 1 
ATOM   2292 C  CZ  . PHE A 1 291 ? -4.873  33.392 23.046  1.00 25.83  ? 291 PHE A CZ  1 
ATOM   2293 N  N   . THR A 1 292 ? 0.701   34.852 18.481  1.00 16.20  ? 292 THR A N   1 
ATOM   2294 C  CA  . THR A 1 292 ? 2.065   34.930 17.926  1.00 16.45  ? 292 THR A CA  1 
ATOM   2295 C  C   . THR A 1 292 ? 3.053   34.905 19.094  1.00 17.02  ? 292 THR A C   1 
ATOM   2296 O  O   . THR A 1 292 ? 2.706   35.227 20.230  1.00 17.52  ? 292 THR A O   1 
ATOM   2297 C  CB  . THR A 1 292 ? 2.263   36.169 17.064  1.00 19.52  ? 292 THR A CB  1 
ATOM   2298 O  OG1 . THR A 1 292 ? 2.237   37.278 17.965  1.00 20.71  ? 292 THR A OG1 1 
ATOM   2299 C  CG2 . THR A 1 292 ? 1.237   36.324 15.958  1.00 17.32  ? 292 THR A CG2 1 
ATOM   2300 N  N   . PRO A 1 293 ? 4.328   34.664 18.801  1.00 17.49  ? 293 PRO A N   1 
ATOM   2301 C  CA  . PRO A 1 293 ? 5.370   34.838 19.810  1.00 19.63  ? 293 PRO A CA  1 
ATOM   2302 C  C   . PRO A 1 293 ? 5.356   36.220 20.453  1.00 20.67  ? 293 PRO A C   1 
ATOM   2303 O  O   . PRO A 1 293 ? 5.497   36.317 21.659  1.00 22.84  ? 293 PRO A O   1 
ATOM   2304 C  CB  . PRO A 1 293 ? 6.648   34.553 19.005  1.00 19.01  ? 293 PRO A CB  1 
ATOM   2305 C  CG  . PRO A 1 293 ? 6.197   33.574 17.964  1.00 19.14  ? 293 PRO A CG  1 
ATOM   2306 C  CD  . PRO A 1 293 ? 4.823   34.061 17.553  1.00 19.96  ? 293 PRO A CD  1 
ATOM   2307 N  N   . PHE A 1 294 ? 5.079   37.259 19.672  1.00 22.60  ? 294 PHE A N   1 
ATOM   2308 C  CA  . PHE A 1 294 ? 4.999   38.636 20.191  1.00 25.10  ? 294 PHE A CA  1 
ATOM   2309 C  C   . PHE A 1 294 ? 3.837   38.736 21.183  1.00 21.50  ? 294 PHE A C   1 
ATOM   2310 O  O   . PHE A 1 294 ? 3.949   39.405 22.189  1.00 24.00  ? 294 PHE A O   1 
ATOM   2311 C  CB  . PHE A 1 294 ? 4.787   39.644 19.065  1.00 27.09  ? 294 PHE A CB  1 
ATOM   2312 C  CG  . PHE A 1 294 ? 4.373   41.010 19.563  1.00 34.49  ? 294 PHE A CG  1 
ATOM   2313 C  CD1 . PHE A 1 294 ? 3.030   41.318 19.776  1.00 41.82  ? 294 PHE A CD1 1 
ATOM   2314 C  CD2 . PHE A 1 294 ? 5.325   41.974 19.873  1.00 40.93  ? 294 PHE A CD2 1 
ATOM   2315 C  CE1 . PHE A 1 294 ? 2.648   42.569 20.252  1.00 43.91  ? 294 PHE A CE1 1 
ATOM   2316 C  CE2 . PHE A 1 294 ? 4.943   43.220 20.355  1.00 40.29  ? 294 PHE A CE2 1 
ATOM   2317 C  CZ  . PHE A 1 294 ? 3.611   43.510 20.555  1.00 41.02  ? 294 PHE A CZ  1 
ATOM   2318 N  N   . ASP A 1 295 ? 2.664   38.200 20.829  1.00 20.61  ? 295 ASP A N   1 
ATOM   2319 C  CA  . ASP A 1 295 ? 1.436   38.210 21.661  1.00 20.86  ? 295 ASP A CA  1 
ATOM   2320 C  C   . ASP A 1 295 ? 1.776   37.581 23.024  1.00 21.92  ? 295 ASP A C   1 
ATOM   2321 O  O   . ASP A 1 295 ? 1.171   37.942 24.058  1.00 22.25  ? 295 ASP A O   1 
ATOM   2322 C  CB  . ASP A 1 295 ? 0.307   37.415 21.016  1.00 20.13  ? 295 ASP A CB  1 
ATOM   2323 C  CG  . ASP A 1 295 ? -0.224  38.062 19.745  1.00 24.19  ? 295 ASP A CG  1 
ATOM   2324 O  OD1 . ASP A 1 295 ? 0.016   39.286 19.580  1.00 25.70  ? 295 ASP A OD1 1 
ATOM   2325 O  OD2 . ASP A 1 295 ? -0.819  37.318 18.929  1.00 22.24  ? 295 ASP A OD2 1 
ATOM   2326 N  N   . VAL A 1 296 ? 2.557   36.506 22.995  1.00 20.66  ? 296 VAL A N   1 
ATOM   2327 C  CA  . VAL A 1 296 ? 2.852   35.772 24.248  1.00 19.39  ? 296 VAL A CA  1 
ATOM   2328 C  C   . VAL A 1 296 ? 3.758   36.661 25.108  1.00 22.04  ? 296 VAL A C   1 
ATOM   2329 O  O   . VAL A 1 296 ? 3.460   36.875 26.280  1.00 24.45  ? 296 VAL A O   1 
ATOM   2330 C  CB  . VAL A 1 296 ? 3.461   34.392 23.958  1.00 19.52  ? 296 VAL A CB  1 
ATOM   2331 C  CG1 . VAL A 1 296 ? 4.046   33.832 25.256  1.00 21.45  ? 296 VAL A CG1 1 
ATOM   2332 C  CG2 . VAL A 1 296 ? 2.407   33.502 23.342  1.00 18.82  ? 296 VAL A CG2 1 
ATOM   2333 N  N   . VAL A 1 297 ? 4.828   37.179 24.546  1.00 23.21  ? 297 VAL A N   1 
ATOM   2334 C  CA  . VAL A 1 297 ? 5.750   38.101 25.274  1.00 26.00  ? 297 VAL A CA  1 
ATOM   2335 C  C   . VAL A 1 297 ? 4.978   39.351 25.756  1.00 28.71  ? 297 VAL A C   1 
ATOM   2336 O  O   . VAL A 1 297 ? 5.158   39.758 26.906  1.00 31.30  ? 297 VAL A O   1 
ATOM   2337 C  CB  . VAL A 1 297 ? 6.940   38.452 24.372  1.00 26.78  ? 297 VAL A CB  1 
ATOM   2338 C  CG1 . VAL A 1 297 ? 7.763   39.594 24.931  1.00 30.80  ? 297 VAL A CG1 1 
ATOM   2339 C  CG2 . VAL A 1 297 ? 7.780   37.222 24.140  1.00 29.06  ? 297 VAL A CG2 1 
ATOM   2340 N  N   . ARG A 1 298 ? 4.081   39.920 24.956  1.00 29.07  ? 298 ARG A N   1 
ATOM   2341 C  CA  . ARG A 1 298 ? 3.289   41.130 25.314  1.00 30.93  ? 298 ARG A CA  1 
ATOM   2342 C  C   . ARG A 1 298 ? 2.441   40.838 26.551  1.00 30.36  ? 298 ARG A C   1 
ATOM   2343 O  O   . ARG A 1 298 ? 2.367   41.692 27.463  1.00 32.93  ? 298 ARG A O   1 
ATOM   2344 C  CB  . ARG A 1 298 ? 2.442   41.611 24.127  1.00 34.20  ? 298 ARG A CB  1 
ATOM   2345 C  CG  . ARG A 1 298 ? 1.379   42.661 24.449  1.00 38.90  ? 298 ARG A CG  1 
ATOM   2346 C  CD  . ARG A 1 298 ? 0.262   42.688 23.393  1.00 42.23  ? 298 ARG A CD  1 
ATOM   2347 N  NE  . ARG A 1 298 ? -0.882  43.484 23.838  1.00 42.29  ? 298 ARG A NE  1 
ATOM   2348 C  CZ  . ARG A 1 298 ? -2.113  43.418 23.340  1.00 37.53  ? 298 ARG A CZ  1 
ATOM   2349 N  NH1 . ARG A 1 298 ? -2.436  42.623 22.329  1.00 47.84  ? 298 ARG A NH1 1 
ATOM   2350 N  NH2 . ARG A 1 298 ? -3.036  44.172 23.863  1.00 34.51  ? 298 ARG A NH2 1 
ATOM   2351 N  N   . GLN A 1 299 ? 1.856   39.664 26.623  1.00 27.73  ? 299 GLN A N   1 
ATOM   2352 C  CA  . GLN A 1 299 ? 0.848   39.308 27.628  1.00 26.03  ? 299 GLN A CA  1 
ATOM   2353 C  C   . GLN A 1 299 ? 1.446   38.656 28.866  1.00 30.52  ? 299 GLN A C   1 
ATOM   2354 O  O   . GLN A 1 299 ? 1.000   39.017 29.993  1.00 28.42  ? 299 GLN A O   1 
ATOM   2355 C  CB  . GLN A 1 299 ? -0.198  38.392 27.010  1.00 27.06  ? 299 GLN A CB  1 
ATOM   2356 C  CG  . GLN A 1 299 ? -1.393  38.340 27.927  1.00 23.52  ? 299 GLN A CG  1 
ATOM   2357 C  CD  . GLN A 1 299 ? -2.586  37.597 27.394  1.00 21.54  ? 299 GLN A CD  1 
ATOM   2358 O  OE1 . GLN A 1 299 ? -3.416  37.170 28.186  1.00 20.01  ? 299 GLN A OE1 1 
ATOM   2359 N  NE2 . GLN A 1 299 ? -2.733  37.513 26.077  1.00 19.12  ? 299 GLN A NE2 1 
ATOM   2360 N  N   . CYS A 1 300 ? 2.460   37.806 28.703  1.00 26.85  ? 300 CYS A N   1 
ATOM   2361 C  CA  . CYS A 1 300 ? 2.980   36.965 29.800  1.00 29.16  ? 300 CYS A CA  1 
ATOM   2362 C  C   . CYS A 1 300 ? 4.044   37.721 30.581  1.00 35.91  ? 300 CYS A C   1 
ATOM   2363 O  O   . CYS A 1 300 ? 4.567   38.715 30.090  1.00 32.03  ? 300 CYS A O   1 
ATOM   2364 C  CB  . CYS A 1 300 ? 3.556   35.638 29.340  1.00 28.38  ? 300 CYS A CB  1 
ATOM   2365 S  SG  . CYS A 1 300 ? 2.296   34.500 28.741  1.00 32.79  ? 300 CYS A SG  1 
ATOM   2366 N  N   . SER A 1 301 ? 4.249   37.300 31.822  1.00 42.55  ? 301 SER A N   1 
ATOM   2367 C  CA  . SER A 1 301 ? 5.313   37.842 32.692  1.00 48.52  ? 301 SER A CA  1 
ATOM   2368 C  C   . SER A 1 301 ? 6.641   37.611 31.963  1.00 47.46  ? 301 SER A C   1 
ATOM   2369 O  O   . SER A 1 301 ? 6.706   36.630 31.146  1.00 41.35  ? 301 SER A O   1 
ATOM   2370 C  CB  . SER A 1 301 ? 5.309   37.184 34.051  1.00 47.99  ? 301 SER A CB  1 
ATOM   2371 O  OG  . SER A 1 301 ? 6.388   37.670 34.842  1.00 46.12  ? 301 SER A OG  1 
ATOM   2372 N  N   . GLY A 1 302 ? 7.627   38.466 32.256  1.00 48.23  ? 302 GLY A N   1 
ATOM   2373 C  CA  . GLY A 1 302 ? 9.045   38.305 31.874  1.00 51.87  ? 302 GLY A CA  1 
ATOM   2374 C  C   . GLY A 1 302 ? 9.780   37.434 32.878  1.00 52.14  ? 302 GLY A C   1 
ATOM   2375 O  O   . GLY A 1 302 ? 11.017  37.304 32.736  1.00 57.05  ? 302 GLY A O   1 
ATOM   2376 N  N   . VAL A 1 303 ? 9.036   36.861 33.845  1.00 53.73  ? 303 VAL A N   1 
ATOM   2377 C  CA  . VAL A 1 303 ? 9.488   35.831 34.833  1.00 56.25  ? 303 VAL A CA  1 
ATOM   2378 C  C   . VAL A 1 303 ? 8.579   34.585 34.738  1.00 58.65  ? 303 VAL A C   1 
ATOM   2379 O  O   . VAL A 1 303 ? 7.328   34.696 34.980  1.00 47.34  ? 303 VAL A O   1 
ATOM   2380 C  CB  . VAL A 1 303 ? 9.475   36.408 36.264  1.00 58.37  ? 303 VAL A CB  1 
ATOM   2381 C  CG1 . VAL A 1 303 ? 10.069  35.437 37.285  1.00 56.98  ? 303 VAL A CG1 1 
ATOM   2382 C  CG2 . VAL A 1 303 ? 10.165  37.771 36.325  1.00 55.97  ? 303 VAL A CG2 1 
ATOM   2383 N  N   . THR A 1 304 ? 9.194   33.431 34.447  1.00 58.04  ? 304 THR A N   1 
ATOM   2384 C  CA  . THR A 1 304 ? 8.555   32.081 34.398  1.00 63.90  ? 304 THR A CA  1 
ATOM   2385 C  C   . THR A 1 304 ? 8.198   31.627 35.820  1.00 69.22  ? 304 THR A C   1 
ATOM   2386 O  O   . THR A 1 304 ? 8.982   31.918 36.769  1.00 62.63  ? 304 THR A O   1 
ATOM   2387 C  CB  . THR A 1 304 ? 9.469   31.068 33.687  1.00 59.96  ? 304 THR A CB  1 
ATOM   2388 O  OG1 . THR A 1 304 ? 9.788   31.662 32.430  1.00 53.08  ? 304 THR A OG1 1 
ATOM   2389 C  CG2 . THR A 1 304 ? 8.850   29.700 33.477  1.00 60.80  ? 304 THR A CG2 1 
ATOM   2390 N  N   . PHE A 1 305 ? 7.060   30.940 35.956  1.00 72.33  ? 305 PHE A N   1 
ATOM   2391 C  CA  . PHE A 1 305 ? 6.531   30.438 37.249  1.00 72.22  ? 305 PHE A CA  1 
ATOM   2392 C  C   . PHE A 1 305 ? 6.953   28.970 37.410  1.00 67.62  ? 305 PHE A C   1 
ATOM   2393 O  O   . PHE A 1 305 ? 6.432   28.063 36.762  1.00 59.84  ? 305 PHE A O   1 
ATOM   2394 C  CB  . PHE A 1 305 ? 5.019   30.684 37.311  1.00 71.89  ? 305 PHE A CB  1 
ATOM   2395 C  CG  . PHE A 1 305 ? 4.349   30.256 38.593  1.00 73.88  ? 305 PHE A CG  1 
ATOM   2396 C  CD1 . PHE A 1 305 ? 4.972   30.442 39.823  1.00 73.98  ? 305 PHE A CD1 1 
ATOM   2397 C  CD2 . PHE A 1 305 ? 3.083   29.685 38.569  1.00 67.96  ? 305 PHE A CD2 1 
ATOM   2398 C  CE1 . PHE A 1 305 ? 4.351   30.042 40.997  1.00 74.09  ? 305 PHE A CE1 1 
ATOM   2399 C  CE2 . PHE A 1 305 ? 2.460   29.300 39.743  1.00 68.87  ? 305 PHE A CE2 1 
ATOM   2400 C  CZ  . PHE A 1 305 ? 3.096   29.476 40.954  1.00 73.64  ? 305 PHE A CZ  1 
HETATM 2401 N  N3  . XDQ B 2 .   ? -21.992 39.657 1.238   1.00 27.86  ? 401 XDQ A N3  1 
HETATM 2402 C  C4  . XDQ B 2 .   ? -22.036 41.225 3.305   1.00 23.90  ? 401 XDQ A C4  1 
HETATM 2403 C  C6  . XDQ B 2 .   ? -23.583 41.134 3.290   1.00 25.98  ? 401 XDQ A C6  1 
HETATM 2404 C  C7  . XDQ B 2 .   ? -21.441 40.752 4.672   1.00 23.03  ? 401 XDQ A C7  1 
HETATM 2405 C  C8  . XDQ B 2 .   ? -20.110 41.065 5.045   1.00 20.11  ? 401 XDQ A C8  1 
HETATM 2406 N  N12 . XDQ B 2 .   ? -19.610 40.612 6.231   1.00 20.70  ? 401 XDQ A N12 1 
HETATM 2407 C  C13 . XDQ B 2 .   ? -21.194 42.932 1.734   1.00 21.14  ? 401 XDQ A C13 1 
HETATM 2408 C  C15 . XDQ B 2 .   ? -20.936 44.911 3.826   1.00 28.02  ? 401 XDQ A C15 1 
HETATM 2409 C  C20 . XDQ B 2 .   ? -22.245 43.475 0.979   1.00 26.10  ? 401 XDQ A C20 1 
HETATM 2410 C  C21 . XDQ B 2 .   ? -22.028 43.794 -0.334  1.00 26.15  ? 401 XDQ A C21 1 
HETATM 2411 C  C22 . XDQ B 2 .   ? -20.804 43.708 -0.950  1.00 24.57  ? 401 XDQ A C22 1 
HETATM 2412 O  O1  . XDQ B 2 .   ? -20.137 40.065 2.349   1.00 22.27  ? 401 XDQ A O1  1 
HETATM 2413 C  C2  . XDQ B 2 .   ? -21.352 40.280 2.274   1.00 26.81  ? 401 XDQ A C2  1 
HETATM 2414 N  N5  . XDQ B 2 .   ? -21.588 42.602 3.044   1.00 22.09  ? 401 XDQ A N5  1 
HETATM 2415 C  C9  . XDQ B 2 .   ? -22.193 40.041 5.608   1.00 22.71  ? 401 XDQ A C9  1 
HETATM 2416 N  N10 . XDQ B 2 .   ? -21.663 39.639 6.750   1.00 22.41  ? 401 XDQ A N10 1 
HETATM 2417 C  C11 . XDQ B 2 .   ? -20.402 39.950 7.055   1.00 19.21  ? 401 XDQ A C11 1 
HETATM 2418 C  C14 . XDQ B 2 .   ? -21.631 43.577 4.002   1.00 25.75  ? 401 XDQ A C14 1 
HETATM 2419 O  O16 . XDQ B 2 .   ? -22.122 43.333 5.110   1.00 26.88  ? 401 XDQ A O16 1 
HETATM 2420 F  F17 . XDQ B 2 .   ? -21.374 45.758 4.828   1.00 29.59  ? 401 XDQ A F17 1 
HETATM 2421 C  C19 . XDQ B 2 .   ? -19.999 42.876 1.103   1.00 18.54  ? 401 XDQ A C19 1 
HETATM 2422 C  C23 . XDQ B 2 .   ? -19.786 43.218 -0.186  1.00 21.54  ? 401 XDQ A C23 1 
HETATM 2423 O  O24 . XDQ B 2 .   ? -20.655 44.130 -2.248  1.00 27.52  ? 401 XDQ A O24 1 
HETATM 2424 C  C25 . XDQ B 2 .   ? -19.901 43.552 -3.301  1.00 36.52  ? 401 XDQ A C25 1 
HETATM 2425 F  F26 . XDQ B 2 .   ? -18.561 43.435 -3.008  1.00 40.48  ? 401 XDQ A F26 1 
HETATM 2426 F  F27 . XDQ B 2 .   ? -20.260 44.061 -4.620  1.00 27.16  ? 401 XDQ A F27 1 
HETATM 2427 CL CL2 . XDQ B 2 .   ? -20.307 41.866 -3.244  1.00 44.37  ? 401 XDQ A CL2 1 
HETATM 2428 C  C29 . XDQ B 2 .   ? -21.312 38.760 0.292   1.00 29.55  ? 401 XDQ A C29 1 
HETATM 2429 C  C30 . XDQ B 2 .   ? -22.286 37.651 -0.055  1.00 34.70  ? 401 XDQ A C30 1 
HETATM 2430 C  C31 . XDQ B 2 .   ? -20.894 39.556 -0.941  1.00 36.30  ? 401 XDQ A C31 1 
HETATM 2431 C  C32 . XDQ B 2 .   ? -20.343 38.527 -1.962  1.00 38.90  ? 401 XDQ A C32 1 
HETATM 2432 O  O33 . XDQ B 2 .   ? -21.509 37.757 -2.296  1.00 40.09  ? 401 XDQ A O33 1 
HETATM 2433 C  C34 . XDQ B 2 .   ? -21.828 36.846 -1.261  1.00 37.60  ? 401 XDQ A C34 1 
HETATM 2434 C  C1  . EDO C 3 .   ? 1.087   56.308 -2.283  1.00 58.13  ? 402 EDO A C1  1 
HETATM 2435 O  O1  . EDO C 3 .   ? -0.329  56.472 -2.239  1.00 50.82  ? 402 EDO A O1  1 
HETATM 2436 C  C2  . EDO C 3 .   ? 1.794   57.333 -3.120  1.00 59.43  ? 402 EDO A C2  1 
HETATM 2437 O  O2  . EDO C 3 .   ? 1.153   57.651 -4.363  1.00 62.73  ? 402 EDO A O2  1 
HETATM 2438 C  C1  . EDO D 3 .   ? -27.653 61.324 11.701  1.00 64.59  ? 403 EDO A C1  1 
HETATM 2439 O  O1  . EDO D 3 .   ? -28.476 61.472 10.564  1.00 61.31  ? 403 EDO A O1  1 
HETATM 2440 C  C2  . EDO D 3 .   ? -27.475 59.898 12.098  1.00 65.82  ? 403 EDO A C2  1 
HETATM 2441 O  O2  . EDO D 3 .   ? -26.203 59.590 12.635  1.00 65.93  ? 403 EDO A O2  1 
HETATM 2442 CL CL  . CL  E 4 .   ? -10.241 34.593 25.919  1.00 34.67  ? 404 CL  A CL  1 
HETATM 2443 CL CL  . CL  F 4 .   ? -5.865  20.795 18.007  1.00 44.65  ? 405 CL  A CL  1 
HETATM 2444 CL CL  . CL  G 4 .   ? -24.140 68.452 9.224   1.00 76.59  ? 406 CL  A CL  1 
HETATM 2445 CL CL  . CL  H 4 .   ? -15.655 29.861 1.695   1.00 36.47  ? 407 CL  A CL  1 
HETATM 2446 O  O   . HOH I 5 .   ? -2.169  25.351 31.195  1.00 36.00  ? 501 HOH A O   1 
HETATM 2447 O  O   . HOH I 5 .   ? 13.246  21.370 7.969   1.00 37.68  ? 502 HOH A O   1 
HETATM 2448 O  O   . HOH I 5 .   ? -21.214 64.182 3.271   1.00 36.04  ? 503 HOH A O   1 
HETATM 2449 O  O   . HOH I 5 .   ? 15.265  21.893 26.477  1.00 31.87  ? 504 HOH A O   1 
HETATM 2450 O  O   . HOH I 5 .   ? -23.310 52.842 -8.601  1.00 48.48  ? 505 HOH A O   1 
HETATM 2451 O  O   . HOH I 5 .   ? -8.808  17.589 23.170  1.00 44.82  ? 506 HOH A O   1 
HETATM 2452 O  O   . HOH I 5 .   ? -10.493 26.391 21.477  1.00 45.07  ? 507 HOH A O   1 
HETATM 2453 O  O   . HOH I 5 .   ? -2.465  11.310 15.402  1.00 56.60  ? 508 HOH A O   1 
HETATM 2454 O  O   . HOH I 5 .   ? 1.307   31.850 37.165  1.00 37.84  ? 509 HOH A O   1 
HETATM 2455 O  O   . HOH I 5 .   ? -16.462 60.121 -10.642 1.00 39.58  ? 510 HOH A O   1 
HETATM 2456 O  O   . HOH I 5 .   ? 4.726   51.409 15.365  1.00 54.13  ? 511 HOH A O   1 
HETATM 2457 O  O   . HOH I 5 .   ? -6.050  30.572 19.031  1.00 23.53  ? 512 HOH A O   1 
HETATM 2458 O  O   . HOH I 5 .   ? -7.493  39.164 -4.854  1.00 23.04  ? 513 HOH A O   1 
HETATM 2459 O  O   . HOH I 5 .   ? 2.683   14.867 26.003  1.00 40.68  ? 514 HOH A O   1 
HETATM 2460 O  O   . HOH I 5 .   ? -11.733 35.060 -5.737  1.00 33.87  ? 515 HOH A O   1 
HETATM 2461 O  O   . HOH I 5 .   ? -7.754  34.953 17.574  1.00 32.60  ? 516 HOH A O   1 
HETATM 2462 O  O   . HOH I 5 .   ? -6.103  24.794 16.202  1.00 43.10  ? 517 HOH A O   1 
HETATM 2463 O  O   . HOH I 5 .   ? -19.781 42.097 14.711  1.00 27.02  ? 518 HOH A O   1 
HETATM 2464 O  O   . HOH I 5 .   ? -1.535  58.583 18.540  1.00 29.82  ? 519 HOH A O   1 
HETATM 2465 O  O   . HOH I 5 .   ? -4.349  21.916 10.269  1.00 46.86  ? 520 HOH A O   1 
HETATM 2466 O  O   . HOH I 5 .   ? 3.257   27.552 3.517   1.00 39.17  ? 521 HOH A O   1 
HETATM 2467 O  O   . HOH I 5 .   ? -23.399 42.306 -12.416 1.00 50.36  ? 522 HOH A O   1 
HETATM 2468 O  O   . HOH I 5 .   ? 17.487  19.198 19.817  1.00 40.23  ? 523 HOH A O   1 
HETATM 2469 O  O   . HOH I 5 .   ? 10.219  34.304 21.327  1.00 30.52  ? 524 HOH A O   1 
HETATM 2470 O  O   . HOH I 5 .   ? 5.577   28.207 7.285   1.00 41.47  ? 525 HOH A O   1 
HETATM 2471 O  O   . HOH I 5 .   ? -21.457 33.098 4.743   1.00 40.82  ? 526 HOH A O   1 
HETATM 2472 O  O   . HOH I 5 .   ? -22.668 47.067 -12.912 1.00 44.77  ? 527 HOH A O   1 
HETATM 2473 O  O   . HOH I 5 .   ? 4.530   10.507 20.333  1.00 61.40  ? 528 HOH A O   1 
HETATM 2474 O  O   . HOH I 5 .   ? -28.446 53.139 3.589   1.00 43.13  ? 529 HOH A O   1 
HETATM 2475 O  O   . HOH I 5 .   ? -4.630  45.083 -5.639  1.00 35.04  ? 530 HOH A O   1 
HETATM 2476 O  O   . HOH I 5 .   ? -14.013 27.013 1.274   1.00 36.39  ? 531 HOH A O   1 
HETATM 2477 O  O   . HOH I 5 .   ? -3.103  18.362 5.694   1.00 52.60  ? 532 HOH A O   1 
HETATM 2478 O  O   . HOH I 5 .   ? -5.020  22.394 14.213  1.00 40.22  ? 533 HOH A O   1 
HETATM 2479 O  O   . HOH I 5 .   ? 6.712   26.467 34.384  1.00 29.96  ? 534 HOH A O   1 
HETATM 2480 O  O   . HOH I 5 .   ? -1.930  41.465 17.690  1.00 30.10  ? 535 HOH A O   1 
HETATM 2481 O  O   . HOH I 5 .   ? -0.401  46.951 -0.468  1.00 28.81  ? 536 HOH A O   1 
HETATM 2482 O  O   . HOH I 5 .   ? -13.421 28.514 5.554   1.00 30.31  ? 537 HOH A O   1 
HETATM 2483 O  O   . HOH I 5 .   ? -18.831 32.490 -3.604  1.00 39.17  ? 538 HOH A O   1 
HETATM 2484 O  O   . HOH I 5 .   ? -14.613 56.086 22.589  1.00 39.53  ? 539 HOH A O   1 
HETATM 2485 O  O   . HOH I 5 .   ? 1.733   39.692 17.027  1.00 25.97  ? 540 HOH A O   1 
HETATM 2486 O  O   . HOH I 5 .   ? -13.351 49.520 12.692  1.00 23.22  ? 541 HOH A O   1 
HETATM 2487 O  O   . HOH I 5 .   ? -8.904  58.641 17.915  1.00 30.96  ? 542 HOH A O   1 
HETATM 2488 O  O   . HOH I 5 .   ? -5.869  12.006 23.517  1.00 46.02  ? 543 HOH A O   1 
HETATM 2489 O  O   . HOH I 5 .   ? -10.662 69.683 12.101  1.00 44.14  ? 544 HOH A O   1 
HETATM 2490 O  O   . HOH I 5 .   ? 2.227   50.573 15.365  1.00 42.29  ? 545 HOH A O   1 
HETATM 2491 O  O   . HOH I 5 .   ? -21.127 38.942 14.586  1.00 30.29  ? 546 HOH A O   1 
HETATM 2492 O  O   . HOH I 5 .   ? -22.727 49.608 16.430  1.00 44.17  ? 547 HOH A O   1 
HETATM 2493 O  O   . HOH I 5 .   ? 9.720   31.839 8.343   1.00 32.61  ? 548 HOH A O   1 
HETATM 2494 O  O   . HOH I 5 .   ? 4.059   21.749 6.291   1.00 41.25  ? 549 HOH A O   1 
HETATM 2495 O  O   . HOH I 5 .   ? -22.462 54.449 -10.567 1.00 37.98  ? 550 HOH A O   1 
HETATM 2496 O  O   . HOH I 5 .   ? -22.928 49.877 8.480   1.00 25.77  ? 551 HOH A O   1 
HETATM 2497 O  O   . HOH I 5 .   ? -7.785  31.048 0.192   1.00 28.42  ? 552 HOH A O   1 
HETATM 2498 O  O   . HOH I 5 .   ? -23.713 58.327 5.714   1.00 29.76  ? 553 HOH A O   1 
HETATM 2499 O  O   . HOH I 5 .   ? -4.430  18.088 12.171  1.00 52.92  ? 554 HOH A O   1 
HETATM 2500 O  O   . HOH I 5 .   ? -8.224  36.055 -7.738  1.00 31.45  ? 555 HOH A O   1 
HETATM 2501 O  O   . HOH I 5 .   ? -9.487  68.901 3.271   1.00 45.92  ? 556 HOH A O   1 
HETATM 2502 O  O   . HOH I 5 .   ? -5.981  24.403 31.197  1.00 38.82  ? 557 HOH A O   1 
HETATM 2503 O  O   . HOH I 5 .   ? 12.877  24.453 31.820  1.00 34.35  ? 558 HOH A O   1 
HETATM 2504 O  O   . HOH I 5 .   ? 2.037   35.980 36.008  1.00 34.28  ? 559 HOH A O   1 
HETATM 2505 O  O   . HOH I 5 .   ? -4.065  20.681 15.920  1.00 26.72  ? 560 HOH A O   1 
HETATM 2506 O  O   . HOH I 5 .   ? 17.639  29.905 29.167  1.00 48.14  ? 561 HOH A O   1 
HETATM 2507 O  O   . HOH I 5 .   ? 8.198   13.588 20.343  1.00 32.19  ? 562 HOH A O   1 
HETATM 2508 O  O   . HOH I 5 .   ? -4.983  64.436 15.804  1.00 44.63  ? 563 HOH A O   1 
HETATM 2509 O  O   . HOH I 5 .   ? -20.528 48.010 -13.778 1.00 36.29  ? 564 HOH A O   1 
HETATM 2510 O  O   . HOH I 5 .   ? -24.503 52.150 -3.879  1.00 45.73  ? 565 HOH A O   1 
HETATM 2511 O  O   . HOH I 5 .   ? 3.268   34.159 13.587  1.00 20.69  ? 566 HOH A O   1 
HETATM 2512 O  O   . HOH I 5 .   ? 3.517   35.178 10.233  1.00 42.11  ? 567 HOH A O   1 
HETATM 2513 O  O   . HOH I 5 .   ? -8.868  38.393 2.821   1.00 16.16  ? 568 HOH A O   1 
HETATM 2514 O  O   . HOH I 5 .   ? -8.718  34.283 12.072  1.00 18.77  ? 569 HOH A O   1 
HETATM 2515 O  O   . HOH I 5 .   ? -3.719  15.437 16.329  1.00 41.54  ? 570 HOH A O   1 
HETATM 2516 O  O   . HOH I 5 .   ? 0.958   21.700 5.581   1.00 42.09  ? 571 HOH A O   1 
HETATM 2517 O  O   . HOH I 5 .   ? 17.648  18.161 17.135  1.00 41.61  ? 572 HOH A O   1 
HETATM 2518 O  O   . HOH I 5 .   ? -6.326  30.714 29.816  1.00 36.68  ? 573 HOH A O   1 
HETATM 2519 O  O   . HOH I 5 .   ? -3.459  37.339 19.666  1.00 24.99  ? 574 HOH A O   1 
HETATM 2520 O  O   . HOH I 5 .   ? -11.344 38.440 24.971  1.00 34.78  ? 575 HOH A O   1 
HETATM 2521 O  O   . HOH I 5 .   ? -1.343  39.035 23.885  1.00 24.64  ? 576 HOH A O   1 
HETATM 2522 O  O   . HOH I 5 .   ? -0.357  36.239 32.640  1.00 29.08  ? 577 HOH A O   1 
HETATM 2523 O  O   . HOH I 5 .   ? -9.219  30.705 -2.136  1.00 31.70  ? 578 HOH A O   1 
HETATM 2524 O  O   . HOH I 5 .   ? 0.189   31.265 3.490   1.00 27.12  ? 579 HOH A O   1 
HETATM 2525 O  O   . HOH I 5 .   ? -4.721  54.080 1.007   1.00 31.08  ? 580 HOH A O   1 
HETATM 2526 O  O   . HOH I 5 .   ? 1.559   30.671 5.658   1.00 28.53  ? 581 HOH A O   1 
HETATM 2527 O  O   . HOH I 5 .   ? 13.090  17.492 25.874  1.00 45.83  ? 582 HOH A O   1 
HETATM 2528 O  O   . HOH I 5 .   ? 4.806   32.160 9.815   1.00 37.10  ? 583 HOH A O   1 
HETATM 2529 O  O   . HOH I 5 .   ? -14.962 46.813 -1.969  1.00 19.70  ? 584 HOH A O   1 
HETATM 2530 O  O   . HOH I 5 .   ? -20.360 34.349 0.656   1.00 40.18  ? 585 HOH A O   1 
HETATM 2531 O  O   . HOH I 5 .   ? -19.213 57.890 13.449  1.00 33.97  ? 586 HOH A O   1 
HETATM 2532 O  O   . HOH I 5 .   ? 1.085   50.121 3.304   1.00 22.08  ? 587 HOH A O   1 
HETATM 2533 O  O   . HOH I 5 .   ? -13.358 63.548 15.529  1.00 40.21  ? 588 HOH A O   1 
HETATM 2534 O  O   . HOH I 5 .   ? -3.253  42.092 -3.143  1.00 16.57  ? 589 HOH A O   1 
HETATM 2535 O  O   . HOH I 5 .   ? -6.577  28.612 17.064  1.00 39.09  ? 590 HOH A O   1 
HETATM 2536 O  O   . HOH I 5 .   ? -2.671  48.588 5.481   1.00 22.38  ? 591 HOH A O   1 
HETATM 2537 O  O   . HOH I 5 .   ? -13.423 55.980 -12.642 1.00 33.91  ? 592 HOH A O   1 
HETATM 2538 O  O   . HOH I 5 .   ? 1.206   40.175 3.073   1.00 18.73  ? 593 HOH A O   1 
HETATM 2539 O  O   . HOH I 5 .   ? -9.857  28.310 8.041   1.00 35.40  ? 594 HOH A O   1 
HETATM 2540 O  O   . HOH I 5 .   ? -11.232 42.866 -6.420  1.00 28.64  ? 595 HOH A O   1 
HETATM 2541 O  O   . HOH I 5 .   ? -5.716  46.768 -7.735  1.00 39.53  ? 596 HOH A O   1 
HETATM 2542 O  O   . HOH I 5 .   ? 3.442   47.931 12.523  1.00 34.04  ? 597 HOH A O   1 
HETATM 2543 O  O   . HOH I 5 .   ? -8.846  29.436 27.315  1.00 45.18  ? 598 HOH A O   1 
HETATM 2544 O  O   . HOH I 5 .   ? 9.642   12.392 11.535  1.00 43.42  ? 599 HOH A O   1 
HETATM 2545 O  O   . HOH I 5 .   ? -10.805 29.740 6.141   1.00 25.61  ? 600 HOH A O   1 
HETATM 2546 O  O   . HOH I 5 .   ? 9.689   18.330 25.245  1.00 35.43  ? 601 HOH A O   1 
HETATM 2547 O  O   . HOH I 5 .   ? -1.220  30.343 19.291  1.00 15.29  ? 602 HOH A O   1 
HETATM 2548 O  O   . HOH I 5 .   ? -5.192  60.125 5.634   1.00 27.85  ? 603 HOH A O   1 
HETATM 2549 O  O   . HOH I 5 .   ? 9.308   25.976 34.061  1.00 35.77  ? 604 HOH A O   1 
HETATM 2550 O  O   . HOH I 5 .   ? -26.020 39.719 9.078   1.00 39.59  ? 605 HOH A O   1 
HETATM 2551 O  O   . HOH I 5 .   ? 4.383   39.730 15.642  1.00 48.37  ? 606 HOH A O   1 
HETATM 2552 O  O   . HOH I 5 .   ? -7.695  29.160 23.487  1.00 48.34  ? 607 HOH A O   1 
HETATM 2553 O  O   . HOH I 5 .   ? 16.503  24.392 14.377  1.00 39.32  ? 608 HOH A O   1 
HETATM 2554 O  O   . HOH I 5 .   ? -9.056  49.905 -8.611  1.00 31.65  ? 609 HOH A O   1 
HETATM 2555 O  O   . HOH I 5 .   ? -20.428 65.021 0.465   1.00 43.62  ? 610 HOH A O   1 
HETATM 2556 O  O   . HOH I 5 .   ? -9.600  70.669 9.348   1.00 47.51  ? 611 HOH A O   1 
HETATM 2557 O  O   . HOH I 5 .   ? 16.949  17.997 25.569  1.00 49.66  ? 612 HOH A O   1 
HETATM 2558 O  O   . HOH I 5 .   ? 10.975  19.328 27.354  1.00 34.15  ? 613 HOH A O   1 
HETATM 2559 O  O   . HOH I 5 .   ? -5.694  29.159 25.455  1.00 23.34  ? 614 HOH A O   1 
HETATM 2560 O  O   . HOH I 5 .   ? -5.409  27.556 0.144   1.00 33.76  ? 615 HOH A O   1 
HETATM 2561 O  O   . HOH I 5 .   ? -23.405 37.687 7.849   1.00 32.18  ? 616 HOH A O   1 
HETATM 2562 O  O   . HOH I 5 .   ? -15.769 53.027 24.275  1.00 26.03  ? 617 HOH A O   1 
HETATM 2563 O  O   . HOH I 5 .   ? -2.507  30.739 0.786   1.00 33.31  ? 618 HOH A O   1 
HETATM 2564 O  O   . HOH I 5 .   ? -6.772  43.602 -4.538  1.00 19.33  ? 619 HOH A O   1 
HETATM 2565 O  O   . HOH I 5 .   ? -10.739 25.893 4.179   1.00 45.27  ? 620 HOH A O   1 
HETATM 2566 O  O   . HOH I 5 .   ? 9.317   11.491 14.102  1.00 46.09  ? 621 HOH A O   1 
HETATM 2567 O  O   . HOH I 5 .   ? 3.160   35.802 2.799   1.00 26.88  ? 622 HOH A O   1 
HETATM 2568 O  O   . HOH I 5 .   ? -17.722 65.441 -8.213  1.00 49.64  ? 623 HOH A O   1 
HETATM 2569 O  O   . HOH I 5 .   ? -21.209 50.439 -14.792 1.00 45.24  ? 624 HOH A O   1 
HETATM 2570 O  O   . HOH I 5 .   ? -15.580 33.556 10.805  1.00 22.30  ? 625 HOH A O   1 
HETATM 2571 O  O   . HOH I 5 .   ? -11.827 42.567 -9.187  1.00 34.29  ? 626 HOH A O   1 
HETATM 2572 O  O   . HOH I 5 .   ? -14.359 42.974 -8.191  1.00 34.29  ? 627 HOH A O   1 
HETATM 2573 O  O   . HOH I 5 .   ? 17.238  20.177 12.973  1.00 37.89  ? 628 HOH A O   1 
HETATM 2574 O  O   . HOH I 5 .   ? 16.601  19.159 10.426  1.00 33.57  ? 629 HOH A O   1 
HETATM 2575 O  O   . HOH I 5 .   ? -6.933  33.553 31.707  1.00 26.72  ? 630 HOH A O   1 
HETATM 2576 O  O   . HOH I 5 .   ? 16.308  26.356 20.936  1.00 35.01  ? 631 HOH A O   1 
HETATM 2577 O  O   . HOH I 5 .   ? -10.147 57.319 -9.208  1.00 30.41  ? 632 HOH A O   1 
HETATM 2578 O  O   . HOH I 5 .   ? -26.691 49.247 3.100   1.00 42.18  ? 633 HOH A O   1 
HETATM 2579 O  O   . HOH I 5 .   ? 5.651   35.476 7.461   1.00 29.80  ? 634 HOH A O   1 
HETATM 2580 O  O   . HOH I 5 .   ? -5.737  19.155 32.084  1.00 48.50  ? 635 HOH A O   1 
HETATM 2581 O  O   . HOH I 5 .   ? 1.247   24.087 4.051   1.00 42.02  ? 636 HOH A O   1 
HETATM 2582 O  O   . HOH I 5 .   ? -18.447 36.248 -3.821  1.00 28.76  ? 637 HOH A O   1 
HETATM 2583 O  O   . HOH I 5 .   ? 10.315  13.554 18.593  1.00 36.09  ? 638 HOH A O   1 
HETATM 2584 O  O   . HOH I 5 .   ? -12.143 30.493 -5.057  1.00 29.47  ? 639 HOH A O   1 
HETATM 2585 O  O   . HOH I 5 .   ? -21.580 35.128 2.255   1.00 48.69  ? 640 HOH A O   1 
HETATM 2586 O  O   . HOH I 5 .   ? -6.427  52.306 -8.186  1.00 37.35  ? 641 HOH A O   1 
HETATM 2587 O  O   . HOH I 5 .   ? 15.497  16.384 26.686  1.00 45.43  ? 642 HOH A O   1 
HETATM 2588 O  O   . HOH I 5 .   ? 4.606   28.084 11.271  1.00 19.71  ? 643 HOH A O   1 
HETATM 2589 O  O   . HOH I 5 .   ? 2.108   54.124 6.340   1.00 30.51  ? 644 HOH A O   1 
HETATM 2590 O  O   . HOH I 5 .   ? -13.705 66.312 -7.135  1.00 43.79  ? 645 HOH A O   1 
HETATM 2591 O  O   . HOH I 5 .   ? 4.288   41.772 5.561   1.00 24.15  ? 646 HOH A O   1 
HETATM 2592 O  O   . HOH I 5 .   ? 15.994  29.669 19.208  1.00 52.86  ? 647 HOH A O   1 
HETATM 2593 O  O   . HOH I 5 .   ? -0.887  45.911 12.023  1.00 26.69  ? 648 HOH A O   1 
HETATM 2594 O  O   . HOH I 5 .   ? -12.508 64.015 -7.202  1.00 34.77  ? 649 HOH A O   1 
HETATM 2595 O  O   . HOH I 5 .   ? 14.842  12.331 21.462  1.00 41.50  ? 650 HOH A O   1 
HETATM 2596 O  O   . HOH I 5 .   ? -3.836  38.192 22.411  1.00 22.62  ? 651 HOH A O   1 
HETATM 2597 O  O   . HOH I 5 .   ? -21.903 56.891 13.629  1.00 39.50  ? 652 HOH A O   1 
HETATM 2598 O  O   . HOH I 5 .   ? -24.771 40.373 0.264   1.00 39.82  ? 653 HOH A O   1 
HETATM 2599 O  O   . HOH I 5 .   ? -9.932  40.424 -10.411 1.00 54.09  ? 654 HOH A O   1 
HETATM 2600 O  O   . HOH I 5 .   ? -7.400  25.084 -1.927  1.00 37.80  ? 655 HOH A O   1 
HETATM 2601 O  O   . HOH I 5 .   ? -13.779 46.557 -11.618 1.00 35.24  ? 656 HOH A O   1 
HETATM 2602 O  O   . HOH I 5 .   ? 2.205   35.305 32.903  1.00 31.28  ? 657 HOH A O   1 
HETATM 2603 O  O   . HOH I 5 .   ? -0.000  38.897 0.000   0.50 19.27  ? 658 HOH A O   1 
HETATM 2604 O  O   A HOH I 5 .   ? -11.128 24.190 23.133  0.50 19.85  ? 659 HOH A O   1 
HETATM 2605 O  O   . HOH I 5 .   ? -11.908 48.841 -15.360 1.00 40.52  ? 660 HOH A O   1 
HETATM 2606 O  O   . HOH I 5 .   ? 0.665   59.662 11.558  1.00 33.55  ? 661 HOH A O   1 
HETATM 2607 O  O   . HOH I 5 .   ? -3.007  26.991 3.525   1.00 38.64  ? 662 HOH A O   1 
HETATM 2608 O  O   . HOH I 5 .   ? 5.697   53.360 17.448  1.00 57.23  ? 663 HOH A O   1 
HETATM 2609 O  O   . HOH I 5 .   ? -13.501 31.729 28.631  1.00 39.74  ? 664 HOH A O   1 
HETATM 2610 O  O   . HOH I 5 .   ? -23.190 31.343 4.180   1.00 64.34  ? 665 HOH A O   1 
HETATM 2611 O  O   . HOH I 5 .   ? 4.833   41.721 8.103   1.00 38.99  ? 666 HOH A O   1 
HETATM 2612 O  O   . HOH I 5 .   ? 11.712  18.163 6.273   1.00 43.16  ? 667 HOH A O   1 
HETATM 2613 O  O   . HOH I 5 .   ? 18.243  26.952 16.433  1.00 53.95  ? 668 HOH A O   1 
HETATM 2614 O  O   . HOH I 5 .   ? 16.234  24.277 19.486  1.00 30.16  ? 669 HOH A O   1 
HETATM 2615 O  O   . HOH I 5 .   ? -20.420 67.223 -6.350  1.00 50.96  ? 670 HOH A O   1 
HETATM 2616 O  O   . HOH I 5 .   ? -1.198  61.655 12.638  1.00 36.84  ? 671 HOH A O   1 
HETATM 2617 O  O   . HOH I 5 .   ? -13.297 35.944 -11.395 1.00 49.79  ? 672 HOH A O   1 
HETATM 2618 O  O   . HOH I 5 .   ? 2.470   10.641 13.192  1.00 46.47  ? 673 HOH A O   1 
HETATM 2619 O  O   . HOH I 5 .   ? -27.315 51.624 -3.707  1.00 57.67  ? 674 HOH A O   1 
HETATM 2620 O  O   . HOH I 5 .   ? 1.290   31.253 8.453   1.00 26.70  ? 675 HOH A O   1 
HETATM 2621 O  O   . HOH I 5 .   ? -0.797  48.063 3.435   1.00 31.96  ? 676 HOH A O   1 
HETATM 2622 O  O   . HOH I 5 .   ? -2.368  37.944 -1.451  1.00 17.52  ? 677 HOH A O   1 
HETATM 2623 O  O   . HOH I 5 .   ? 5.694   37.302 16.553  1.00 24.58  ? 678 HOH A O   1 
HETATM 2624 O  O   . HOH I 5 .   ? -10.908 37.970 -10.749 1.00 46.30  ? 679 HOH A O   1 
HETATM 2625 O  O   . HOH I 5 .   ? 3.929   52.154 7.131   1.00 33.57  ? 680 HOH A O   1 
HETATM 2626 O  O   . HOH I 5 .   ? -4.190  53.011 22.732  1.00 47.17  ? 681 HOH A O   1 
HETATM 2627 O  O   . HOH I 5 .   ? -8.699  41.879 -5.693  1.00 30.78  ? 682 HOH A O   1 
HETATM 2628 O  O   . HOH I 5 .   ? -14.992 61.450 15.616  1.00 47.94  ? 683 HOH A O   1 
HETATM 2629 O  O   . HOH I 5 .   ? -9.923  67.823 -3.926  1.00 53.10  ? 684 HOH A O   1 
HETATM 2630 O  O   . HOH I 5 .   ? -11.002 36.880 20.221  1.00 47.54  ? 685 HOH A O   1 
HETATM 2631 O  O   B HOH I 5 .   ? 3.266   40.676 9.835   1.00 27.23  ? 686 HOH A O   1 
HETATM 2632 O  O   . HOH I 5 .   ? -26.482 47.025 9.663   1.00 50.95  ? 687 HOH A O   1 
HETATM 2633 O  O   . HOH I 5 .   ? 2.079   43.348 14.470  1.00 41.69  ? 688 HOH A O   1 
HETATM 2634 O  O   . HOH I 5 .   ? -18.652 30.973 10.467  1.00 45.25  ? 689 HOH A O   1 
HETATM 2635 O  O   . HOH I 5 .   ? -27.994 57.936 9.296   1.00 42.98  ? 690 HOH A O   1 
HETATM 2636 O  O   . HOH I 5 .   ? 8.718   56.076 28.805  1.00 40.55  ? 691 HOH A O   1 
HETATM 2637 O  O   . HOH I 5 .   ? -14.827 58.779 19.693  1.00 46.37  ? 692 HOH A O   1 
HETATM 2638 O  O   . HOH I 5 .   ? 0.604   48.959 22.865  1.00 49.48  ? 693 HOH A O   1 
HETATM 2639 O  O   . HOH I 5 .   ? 1.491   43.947 17.449  1.00 39.95  ? 694 HOH A O   1 
HETATM 2640 O  O   . HOH I 5 .   ? -0.765  42.010 29.810  1.00 42.34  ? 695 HOH A O   1 
HETATM 2641 O  O   . HOH I 5 .   ? -9.837  59.181 20.121  1.00 37.30  ? 696 HOH A O   1 
HETATM 2642 O  O   . HOH I 5 .   ? -9.297  61.844 -2.907  1.00 56.23  ? 697 HOH A O   1 
HETATM 2643 O  O   . HOH I 5 .   ? -12.496 59.102 -9.282  1.00 44.38  ? 698 HOH A O   1 
HETATM 2644 O  O   . HOH I 5 .   ? -23.498 51.329 -14.736 1.00 48.83  ? 699 HOH A O   1 
HETATM 2645 O  O   . HOH I 5 .   ? -4.998  30.726 32.264  1.00 41.80  ? 700 HOH A O   1 
HETATM 2646 O  O   . HOH I 5 .   ? 6.467   21.015 6.461   1.00 41.21  ? 701 HOH A O   1 
HETATM 2647 O  O   . HOH I 5 .   ? -13.844 58.438 -11.600 1.00 34.51  ? 702 HOH A O   1 
HETATM 2648 O  O   . HOH I 5 .   ? -21.861 30.449 6.971   1.00 52.67  ? 703 HOH A O   1 
HETATM 2649 O  O   . HOH I 5 .   ? 2.410   32.772 39.938  1.00 60.73  ? 704 HOH A O   1 
HETATM 2650 O  O   . HOH I 5 .   ? 8.055   31.269 6.843   1.00 36.29  ? 705 HOH A O   1 
HETATM 2651 O  O   . HOH I 5 .   ? -14.378 36.675 -13.962 1.00 42.64  ? 706 HOH A O   1 
HETATM 2652 O  O   . HOH I 5 .   ? -28.368 57.828 6.574   1.00 52.72  ? 707 HOH A O   1 
HETATM 2653 O  O   . HOH I 5 .   ? 7.140   34.414 11.579  1.00 38.45  ? 708 HOH A O   1 
HETATM 2654 O  O   . HOH I 5 .   ? 9.016   34.083 9.754   1.00 33.05  ? 709 HOH A O   1 
HETATM 2655 O  O   . HOH I 5 .   ? 13.407  20.922 28.179  1.00 39.69  ? 710 HOH A O   1 
HETATM 2656 O  O   . HOH I 5 .   ? 3.957   33.508 11.232  1.00 35.90  ? 711 HOH A O   1 
HETATM 2657 O  O   . HOH I 5 .   ? 15.263  29.091 32.864  1.00 49.69  ? 712 HOH A O   1 
HETATM 2658 O  O   . HOH I 5 .   ? -22.328 47.302 2.065   1.00 43.87  ? 713 HOH A O   1 
HETATM 2659 O  O   . HOH I 5 .   ? -9.451  64.309 -4.391  1.00 49.78  ? 714 HOH A O   1 
HETATM 2660 O  O   . HOH I 5 .   ? 5.707   48.330 11.333  1.00 49.51  ? 715 HOH A O   1 
HETATM 2661 O  O   . HOH I 5 .   ? 1.681   45.390 12.481  1.00 43.00  ? 716 HOH A O   1 
HETATM 2662 O  O   . HOH I 5 .   ? 8.632   18.444 5.239   1.00 52.40  ? 717 HOH A O   1 
HETATM 2663 O  O   . HOH I 5 .   ? -2.452  11.894 10.606  1.00 48.29  ? 718 HOH A O   1 
HETATM 2664 O  O   . HOH I 5 .   ? 17.722  22.589 12.823  1.00 39.70  ? 719 HOH A O   1 
HETATM 2665 O  O   . HOH I 5 .   ? -19.510 51.652 22.724  1.00 44.79  ? 720 HOH A O   1 
HETATM 2666 O  O   . HOH I 5 .   ? -15.626 31.278 11.463  1.00 43.54  ? 721 HOH A O   1 
HETATM 2667 O  O   . HOH I 5 .   ? 3.394   29.961 9.637   1.00 29.21  ? 722 HOH A O   1 
HETATM 2668 O  O   . HOH I 5 .   ? -8.309  45.407 -8.244  1.00 46.01  ? 723 HOH A O   1 
HETATM 2669 O  O   . HOH I 5 .   ? -4.922  25.892 -2.154  1.00 41.05  ? 724 HOH A O   1 
HETATM 2670 O  O   . HOH I 5 .   ? -2.523  28.246 0.684   1.00 44.08  ? 725 HOH A O   1 
HETATM 2671 O  O   . HOH I 5 .   ? -29.566 63.346 17.681  1.00 50.36  ? 726 HOH A O   1 
HETATM 2672 O  O   . HOH I 5 .   ? -10.985 30.264 30.778  1.00 49.73  ? 727 HOH A O   1 
HETATM 2673 O  O   . HOH I 5 .   ? -7.411  61.509 -1.618  1.00 44.31  ? 728 HOH A O   1 
HETATM 2674 O  O   . HOH I 5 .   ? -11.346 23.479 -0.690  1.00 51.95  ? 729 HOH A O   1 
HETATM 2675 O  O   . HOH I 5 .   ? 10.088  23.209 5.302   1.00 43.34  ? 730 HOH A O   1 
HETATM 2676 O  O   . HOH I 5 .   ? 3.784   31.936 5.113   1.00 34.44  ? 731 HOH A O   1 
HETATM 2677 O  O   . HOH I 5 .   ? -24.327 53.374 -12.470 1.00 37.58  ? 732 HOH A O   1 
HETATM 2678 O  O   . HOH I 5 .   ? -29.002 50.748 5.761   1.00 52.92  ? 733 HOH A O   1 
HETATM 2679 O  O   . HOH I 5 .   ? -13.900 27.430 7.982   1.00 40.59  ? 734 HOH A O   1 
HETATM 2680 O  O   . HOH I 5 .   ? -7.290  21.889 -2.614  1.00 38.50  ? 735 HOH A O   1 
HETATM 2681 O  O   . HOH I 5 .   ? -29.667 54.087 11.139  1.00 51.52  ? 736 HOH A O   1 
HETATM 2682 O  O   . HOH I 5 .   ? -26.551 44.609 13.036  1.00 53.01  ? 737 HOH A O   1 
HETATM 2683 O  O   . HOH I 5 .   ? 5.377   36.253 9.822   1.00 42.15  ? 738 HOH A O   1 
HETATM 2684 O  O   . HOH I 5 .   ? 8.373   21.399 5.049   1.00 44.96  ? 739 HOH A O   1 
HETATM 2685 O  O   . HOH I 5 .   ? 0.772   27.510 1.260   1.00 41.48  ? 740 HOH A O   1 
HETATM 2686 O  O   . HOH I 5 .   ? 17.256  24.848 16.829  1.00 42.77  ? 741 HOH A O   1 
HETATM 2687 O  O   . HOH I 5 .   ? 18.741  19.035 14.637  1.00 42.35  ? 742 HOH A O   1 
HETATM 2688 O  O   . HOH I 5 .   ? -5.222  18.066 19.671  1.00 47.91  ? 743 HOH A O   1 
HETATM 2689 O  O   . HOH I 5 .   ? -7.537  40.447 -7.951  1.00 44.15  ? 744 HOH A O   1 
HETATM 2690 O  O   . HOH I 5 .   ? -1.152  22.784 2.326   1.00 47.53  ? 745 HOH A O   1 
HETATM 2691 O  O   . HOH I 5 .   ? -11.448 55.128 -11.148 1.00 34.76  ? 746 HOH A O   1 
HETATM 2692 O  O   . HOH I 5 .   ? 18.006  21.988 20.119  1.00 42.68  ? 747 HOH A O   1 
HETATM 2693 O  O   . HOH I 5 .   ? 6.231   34.281 14.104  1.00 39.46  ? 748 HOH A O   1 
HETATM 2694 O  O   . HOH I 5 .   ? 7.813   57.779 20.912  1.00 55.39  ? 749 HOH A O   1 
HETATM 2695 O  O   . HOH I 5 .   ? -9.455  25.797 -3.830  1.00 37.20  ? 750 HOH A O   1 
HETATM 2696 O  O   . HOH I 5 .   ? -28.930 55.167 14.745  1.00 42.52  ? 751 HOH A O   1 
# 
