data_8YR6
# 
_entry.id   8YR6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YR6         pdb_00008yr6 10.2210/pdb8yr6/pdb 
WWPDB D_1300045487 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2024-12-04 
3 'Structure model' 1 2 2025-01-15 
# 
_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 2 'Structure model' 'Structure summary'    
3 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' chem_comp           
2 2 'Structure model' entity              
3 2 'Structure model' pdbx_entity_nonpoly 
4 3 'Structure model' citation            
5 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' '_chem_comp.name'                   
2  2 'Structure model' '_chem_comp.pdbx_synonyms'          
3  2 'Structure model' '_entity.pdbx_description'          
4  2 'Structure model' '_pdbx_entity_nonpoly.name'         
5  3 'Structure model' '_citation.country'                 
6  3 'Structure model' '_citation.journal_abbrev'          
7  3 'Structure model' '_citation.journal_id_CSD'          
8  3 'Structure model' '_citation.journal_id_ISSN'         
9  3 'Structure model' '_citation.journal_volume'          
10 3 'Structure model' '_citation.page_first'              
11 3 'Structure model' '_citation.page_last'               
12 3 'Structure model' '_citation.pdbx_database_id_DOI'    
13 3 'Structure model' '_citation.pdbx_database_id_PubMed' 
14 3 'Structure model' '_citation.title'                   
15 3 'Structure model' '_citation.year'                    
16 3 'Structure model' '_citation_author.identifier_ORCID' 
17 3 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YR6 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-20 
_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           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'the apo protein' 
_pdbx_database_related.db_id          8YR5 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              jwkim@gist.ac.kr 
_pdbx_contact_author.name_first         Jungwook 
_pdbx_contact_author.name_last          Kim 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5213-9299 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kim, J.' 1 0000-0001-5213-9299 
'Lee, E.' 2 0009-0002-3955-9795 
'Cho, G.' 3 0000-0001-6785-616X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                eadq4624 
_citation.page_last                 eadq4624 
_citation.title                     
'Structural basis for membrane association and catalysis by phosphatidylserine synthase in Escherichia coli.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adq4624 
_citation.pdbx_database_id_PubMed   39693441 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, E.' 1 0009-0002-3955-9795 
primary 'Cho, G.' 2 0000-0001-6785-616X 
primary 'Kim, J.' 3 0000-0001-5213-9299 
# 
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 'CDP-diacylglycerol--serine O-phosphatidyltransferase' 53931.781 1  2.7.8.8 H357A ? ? 
2 non-polymer syn 'Cdp-DG(16:0/16:0)'                                    954.073   1  ?       ?     ? ? 
3 non-polymer syn 'SULFATE ION'                                          96.063    1  ?       ?     ? ? 
4 water       nat water                                                  18.015    50 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Phosphatidylserine synthase' 
# 
_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       
;MGSHHHHHHGSLSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPADFRETLLEKIASAKQRICIVALYLEQDDGGKGILNA
LYEAKRQRPELDVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGVDVPVYGVPINTREALGVLHFKGFIIDDSVLY
SGASLNDVYLHQHDKYRYDRYHLIRNRKMSDIMFEWVTQNIMNGRGVNRLDDVNRPKSPEIKNDIRLFRQELRDAAYHFQ
GDADNDQLSVTPLVGLGKSSLLNKTIFHLMPCAEQKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFYIPE
DEPFKIIGALPYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYALKGMWVDDKWMLITGNNLNPRAWRLDLENAILI
HDPQLELAPQREKELELIREHTTIVKHYRDLQSIADYPVKVRKLIRRLRRIRIDRLISRIL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSHHHHHHGSLSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPADFRETLLEKIASAKQRICIVALYLEQDDGGKGILNA
LYEAKRQRPELDVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGVDVPVYGVPINTREALGVLHFKGFIIDDSVLY
SGASLNDVYLHQHDKYRYDRYHLIRNRKMSDIMFEWVTQNIMNGRGVNRLDDVNRPKSPEIKNDIRLFRQELRDAAYHFQ
GDADNDQLSVTPLVGLGKSSLLNKTIFHLMPCAEQKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFYIPE
DEPFKIIGALPYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYALKGMWVDDKWMLITGNNLNPRAWRLDLENAILI
HDPQLELAPQREKELELIREHTTIVKHYRDLQSIADYPVKVRKLIRRLRRIRIDRLISRIL
;
_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 'Cdp-DG(16:0/16:0)' A1LZV 
3 'SULFATE ION'       SO4   
4 water               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  GLY n 
1 11  SER n 
1 12  LEU n 
1 13  SER n 
1 14  LYS n 
1 15  PHE n 
1 16  LYS n 
1 17  ARG n 
1 18  ASN n 
1 19  LYS n 
1 20  HIS n 
1 21  GLN n 
1 22  GLN n 
1 23  HIS n 
1 24  LEU n 
1 25  ALA n 
1 26  GLN n 
1 27  LEU n 
1 28  PRO n 
1 29  LYS n 
1 30  ILE n 
1 31  SER n 
1 32  GLN n 
1 33  SER n 
1 34  VAL n 
1 35  ASP n 
1 36  ASP n 
1 37  VAL n 
1 38  ASP n 
1 39  PHE n 
1 40  PHE n 
1 41  TYR n 
1 42  ALA n 
1 43  PRO n 
1 44  ALA n 
1 45  ASP n 
1 46  PHE n 
1 47  ARG n 
1 48  GLU n 
1 49  THR n 
1 50  LEU n 
1 51  LEU n 
1 52  GLU n 
1 53  LYS n 
1 54  ILE n 
1 55  ALA n 
1 56  SER n 
1 57  ALA n 
1 58  LYS n 
1 59  GLN n 
1 60  ARG n 
1 61  ILE n 
1 62  CYS n 
1 63  ILE n 
1 64  VAL n 
1 65  ALA n 
1 66  LEU n 
1 67  TYR n 
1 68  LEU n 
1 69  GLU n 
1 70  GLN n 
1 71  ASP n 
1 72  ASP n 
1 73  GLY n 
1 74  GLY n 
1 75  LYS n 
1 76  GLY n 
1 77  ILE n 
1 78  LEU n 
1 79  ASN n 
1 80  ALA n 
1 81  LEU n 
1 82  TYR n 
1 83  GLU n 
1 84  ALA n 
1 85  LYS n 
1 86  ARG n 
1 87  GLN n 
1 88  ARG n 
1 89  PRO n 
1 90  GLU n 
1 91  LEU n 
1 92  ASP n 
1 93  VAL n 
1 94  ARG n 
1 95  VAL n 
1 96  LEU n 
1 97  VAL n 
1 98  ASP n 
1 99  TRP n 
1 100 HIS n 
1 101 ARG n 
1 102 ALA n 
1 103 GLN n 
1 104 ARG n 
1 105 GLY n 
1 106 ARG n 
1 107 ILE n 
1 108 GLY n 
1 109 ALA n 
1 110 ALA n 
1 111 ALA n 
1 112 SER n 
1 113 ASN n 
1 114 THR n 
1 115 ASN n 
1 116 ALA n 
1 117 ASP n 
1 118 TRP n 
1 119 TYR n 
1 120 CYS n 
1 121 ARG n 
1 122 MET n 
1 123 ALA n 
1 124 GLN n 
1 125 GLU n 
1 126 ASN n 
1 127 PRO n 
1 128 GLY n 
1 129 VAL n 
1 130 ASP n 
1 131 VAL n 
1 132 PRO n 
1 133 VAL n 
1 134 TYR n 
1 135 GLY n 
1 136 VAL n 
1 137 PRO n 
1 138 ILE n 
1 139 ASN n 
1 140 THR n 
1 141 ARG n 
1 142 GLU n 
1 143 ALA n 
1 144 LEU n 
1 145 GLY n 
1 146 VAL n 
1 147 LEU n 
1 148 HIS n 
1 149 PHE n 
1 150 LYS n 
1 151 GLY n 
1 152 PHE n 
1 153 ILE n 
1 154 ILE n 
1 155 ASP n 
1 156 ASP n 
1 157 SER n 
1 158 VAL n 
1 159 LEU n 
1 160 TYR n 
1 161 SER n 
1 162 GLY n 
1 163 ALA n 
1 164 SER n 
1 165 LEU n 
1 166 ASN n 
1 167 ASP n 
1 168 VAL n 
1 169 TYR n 
1 170 LEU n 
1 171 HIS n 
1 172 GLN n 
1 173 HIS n 
1 174 ASP n 
1 175 LYS n 
1 176 TYR n 
1 177 ARG n 
1 178 TYR n 
1 179 ASP n 
1 180 ARG n 
1 181 TYR n 
1 182 HIS n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 ASN n 
1 187 ARG n 
1 188 LYS n 
1 189 MET n 
1 190 SER n 
1 191 ASP n 
1 192 ILE n 
1 193 MET n 
1 194 PHE n 
1 195 GLU n 
1 196 TRP n 
1 197 VAL n 
1 198 THR n 
1 199 GLN n 
1 200 ASN n 
1 201 ILE n 
1 202 MET n 
1 203 ASN n 
1 204 GLY n 
1 205 ARG n 
1 206 GLY n 
1 207 VAL n 
1 208 ASN n 
1 209 ARG n 
1 210 LEU n 
1 211 ASP n 
1 212 ASP n 
1 213 VAL n 
1 214 ASN n 
1 215 ARG n 
1 216 PRO n 
1 217 LYS n 
1 218 SER n 
1 219 PRO n 
1 220 GLU n 
1 221 ILE n 
1 222 LYS n 
1 223 ASN n 
1 224 ASP n 
1 225 ILE n 
1 226 ARG n 
1 227 LEU n 
1 228 PHE n 
1 229 ARG n 
1 230 GLN n 
1 231 GLU n 
1 232 LEU n 
1 233 ARG n 
1 234 ASP n 
1 235 ALA n 
1 236 ALA n 
1 237 TYR n 
1 238 HIS n 
1 239 PHE n 
1 240 GLN n 
1 241 GLY n 
1 242 ASP n 
1 243 ALA n 
1 244 ASP n 
1 245 ASN n 
1 246 ASP n 
1 247 GLN n 
1 248 LEU n 
1 249 SER n 
1 250 VAL n 
1 251 THR n 
1 252 PRO n 
1 253 LEU n 
1 254 VAL n 
1 255 GLY n 
1 256 LEU n 
1 257 GLY n 
1 258 LYS n 
1 259 SER n 
1 260 SER n 
1 261 LEU n 
1 262 LEU n 
1 263 ASN n 
1 264 LYS n 
1 265 THR n 
1 266 ILE n 
1 267 PHE n 
1 268 HIS n 
1 269 LEU n 
1 270 MET n 
1 271 PRO n 
1 272 CYS n 
1 273 ALA n 
1 274 GLU n 
1 275 GLN n 
1 276 LYS n 
1 277 LEU n 
1 278 THR n 
1 279 ILE n 
1 280 CYS n 
1 281 THR n 
1 282 PRO n 
1 283 TYR n 
1 284 PHE n 
1 285 ASN n 
1 286 LEU n 
1 287 PRO n 
1 288 ALA n 
1 289 ILE n 
1 290 LEU n 
1 291 VAL n 
1 292 ARG n 
1 293 ASN n 
1 294 ILE n 
1 295 ILE n 
1 296 GLN n 
1 297 LEU n 
1 298 LEU n 
1 299 ARG n 
1 300 GLU n 
1 301 GLY n 
1 302 LYS n 
1 303 LYS n 
1 304 VAL n 
1 305 GLU n 
1 306 ILE n 
1 307 ILE n 
1 308 VAL n 
1 309 GLY n 
1 310 ASP n 
1 311 LYS n 
1 312 THR n 
1 313 ALA n 
1 314 ASN n 
1 315 ASP n 
1 316 PHE n 
1 317 TYR n 
1 318 ILE n 
1 319 PRO n 
1 320 GLU n 
1 321 ASP n 
1 322 GLU n 
1 323 PRO n 
1 324 PHE n 
1 325 LYS n 
1 326 ILE n 
1 327 ILE n 
1 328 GLY n 
1 329 ALA n 
1 330 LEU n 
1 331 PRO n 
1 332 TYR n 
1 333 LEU n 
1 334 TYR n 
1 335 GLU n 
1 336 ILE n 
1 337 ASN n 
1 338 LEU n 
1 339 ARG n 
1 340 ARG n 
1 341 PHE n 
1 342 LEU n 
1 343 SER n 
1 344 ARG n 
1 345 LEU n 
1 346 GLN n 
1 347 TYR n 
1 348 TYR n 
1 349 VAL n 
1 350 ASN n 
1 351 THR n 
1 352 ASP n 
1 353 GLN n 
1 354 LEU n 
1 355 VAL n 
1 356 VAL n 
1 357 ARG n 
1 358 LEU n 
1 359 TRP n 
1 360 LYS n 
1 361 ASP n 
1 362 ASP n 
1 363 ASP n 
1 364 ASN n 
1 365 THR n 
1 366 TYR n 
1 367 ALA n 
1 368 LEU n 
1 369 LYS n 
1 370 GLY n 
1 371 MET n 
1 372 TRP n 
1 373 VAL n 
1 374 ASP n 
1 375 ASP n 
1 376 LYS n 
1 377 TRP n 
1 378 MET n 
1 379 LEU n 
1 380 ILE n 
1 381 THR n 
1 382 GLY n 
1 383 ASN n 
1 384 ASN n 
1 385 LEU n 
1 386 ASN n 
1 387 PRO n 
1 388 ARG n 
1 389 ALA n 
1 390 TRP n 
1 391 ARG n 
1 392 LEU n 
1 393 ASP n 
1 394 LEU n 
1 395 GLU n 
1 396 ASN n 
1 397 ALA n 
1 398 ILE n 
1 399 LEU n 
1 400 ILE n 
1 401 HIS n 
1 402 ASP n 
1 403 PRO n 
1 404 GLN n 
1 405 LEU n 
1 406 GLU n 
1 407 LEU n 
1 408 ALA n 
1 409 PRO n 
1 410 GLN n 
1 411 ARG n 
1 412 GLU n 
1 413 LYS n 
1 414 GLU n 
1 415 LEU n 
1 416 GLU n 
1 417 LEU n 
1 418 ILE n 
1 419 ARG n 
1 420 GLU n 
1 421 HIS n 
1 422 THR n 
1 423 THR n 
1 424 ILE n 
1 425 VAL n 
1 426 LYS n 
1 427 HIS n 
1 428 TYR n 
1 429 ARG n 
1 430 ASP n 
1 431 LEU n 
1 432 GLN n 
1 433 SER n 
1 434 ILE n 
1 435 ALA n 
1 436 ASP n 
1 437 TYR n 
1 438 PRO n 
1 439 VAL n 
1 440 LYS n 
1 441 VAL n 
1 442 ARG n 
1 443 LYS n 
1 444 LEU n 
1 445 ILE n 
1 446 ARG n 
1 447 ARG n 
1 448 LEU n 
1 449 ARG n 
1 450 ARG n 
1 451 ILE n 
1 452 ARG n 
1 453 ILE n 
1 454 ASP n 
1 455 ARG n 
1 456 LEU n 
1 457 ILE n 
1 458 SER n 
1 459 ARG n 
1 460 ILE n 
1 461 LEU 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                   461 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'pssA, pss, b2585, JW2569' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'str. K-12 substr. MG1655' 
_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      'Escherichia coli str. K-12 substr. MG1655' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     511145 
_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                 Bacterial 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_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                 Bacterial 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   'N-terminal His tag' 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'modified pLATE31' 
_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 
A1LZV non-polymer         . 'Cdp-DG(16:0/16:0)' 
;1,2-dihexadecanoyl-sn-glycero-3-cytidine-5'-diphosphate; [(2~{R})-3-[[[(2~{R},3~{S},4~{R},5~{R})-5-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-2-hexadecanoyloxy-propyl] hexadecanoate
;
'C44 H81 N3 O15 P2' 954.073 
ALA   'L-peptide linking' y ALANINE             ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE            ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE          ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'     ? 'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE            ? 'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE           ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'     ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE             ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE           ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER               ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE          ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE             ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE              ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE          ? 'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE       ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE             ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE              ? 'C3 H7 N O3'        105.093 
SO4   non-polymer         . 'SULFATE ION'       ? 'O4 S -2'           96.063  
THR   'L-peptide linking' y THREONINE           ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN          ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE            ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE              ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -9  ?   ?   ?   A . n 
A 1 2   GLY 2   -8  ?   ?   ?   A . n 
A 1 3   SER 3   -7  ?   ?   ?   A . n 
A 1 4   HIS 4   -6  ?   ?   ?   A . n 
A 1 5   HIS 5   -5  ?   ?   ?   A . n 
A 1 6   HIS 6   -4  ?   ?   ?   A . n 
A 1 7   HIS 7   -3  ?   ?   ?   A . n 
A 1 8   HIS 8   -2  ?   ?   ?   A . n 
A 1 9   HIS 9   -1  ?   ?   ?   A . n 
A 1 10  GLY 10  0   ?   ?   ?   A . n 
A 1 11  SER 11  1   ?   ?   ?   A . n 
A 1 12  LEU 12  2   ?   ?   ?   A . n 
A 1 13  SER 13  3   ?   ?   ?   A . n 
A 1 14  LYS 14  4   ?   ?   ?   A . n 
A 1 15  PHE 15  5   ?   ?   ?   A . n 
A 1 16  LYS 16  6   ?   ?   ?   A . n 
A 1 17  ARG 17  7   ?   ?   ?   A . n 
A 1 18  ASN 18  8   8   ASN ASN A . n 
A 1 19  LYS 19  9   9   LYS LYS A . n 
A 1 20  HIS 20  10  10  HIS HIS A . n 
A 1 21  GLN 21  11  11  GLN GLN A . n 
A 1 22  GLN 22  12  12  GLN GLN A . n 
A 1 23  HIS 23  13  13  HIS HIS A . n 
A 1 24  LEU 24  14  14  LEU LEU A . n 
A 1 25  ALA 25  15  15  ALA ALA A . n 
A 1 26  GLN 26  16  16  GLN GLN A . n 
A 1 27  LEU 27  17  17  LEU LEU A . n 
A 1 28  PRO 28  18  18  PRO PRO A . n 
A 1 29  LYS 29  19  19  LYS LYS A . n 
A 1 30  ILE 30  20  20  ILE ILE A . n 
A 1 31  SER 31  21  21  SER SER A . n 
A 1 32  GLN 32  22  22  GLN GLN A . n 
A 1 33  SER 33  23  23  SER SER A . n 
A 1 34  VAL 34  24  24  VAL VAL A . n 
A 1 35  ASP 35  25  25  ASP ASP A . n 
A 1 36  ASP 36  26  26  ASP ASP A . n 
A 1 37  VAL 37  27  27  VAL VAL A . n 
A 1 38  ASP 38  28  28  ASP ASP A . n 
A 1 39  PHE 39  29  29  PHE PHE A . n 
A 1 40  PHE 40  30  30  PHE PHE A . n 
A 1 41  TYR 41  31  31  TYR TYR A . n 
A 1 42  ALA 42  32  32  ALA ALA A . n 
A 1 43  PRO 43  33  33  PRO PRO A . n 
A 1 44  ALA 44  34  34  ALA ALA A . n 
A 1 45  ASP 45  35  35  ASP ASP A . n 
A 1 46  PHE 46  36  36  PHE PHE A . n 
A 1 47  ARG 47  37  37  ARG ARG A . n 
A 1 48  GLU 48  38  38  GLU GLU A . n 
A 1 49  THR 49  39  39  THR THR A . n 
A 1 50  LEU 50  40  40  LEU LEU A . n 
A 1 51  LEU 51  41  41  LEU LEU A . n 
A 1 52  GLU 52  42  42  GLU GLU A . n 
A 1 53  LYS 53  43  43  LYS LYS A . n 
A 1 54  ILE 54  44  44  ILE ILE A . n 
A 1 55  ALA 55  45  45  ALA ALA A . n 
A 1 56  SER 56  46  46  SER SER A . n 
A 1 57  ALA 57  47  47  ALA ALA A . n 
A 1 58  LYS 58  48  48  LYS LYS A . n 
A 1 59  GLN 59  49  49  GLN GLN A . n 
A 1 60  ARG 60  50  50  ARG ARG A . n 
A 1 61  ILE 61  51  51  ILE ILE A . n 
A 1 62  CYS 62  52  52  CYS CYS A . n 
A 1 63  ILE 63  53  53  ILE ILE A . n 
A 1 64  VAL 64  54  54  VAL VAL A . n 
A 1 65  ALA 65  55  55  ALA ALA A . n 
A 1 66  LEU 66  56  56  LEU LEU A . n 
A 1 67  TYR 67  57  57  TYR TYR A . n 
A 1 68  LEU 68  58  58  LEU LEU A . n 
A 1 69  GLU 69  59  59  GLU GLU A . n 
A 1 70  GLN 70  60  60  GLN GLN A . n 
A 1 71  ASP 71  61  61  ASP ASP A . n 
A 1 72  ASP 72  62  62  ASP ASP A . n 
A 1 73  GLY 73  63  63  GLY GLY A . n 
A 1 74  GLY 74  64  64  GLY GLY A . n 
A 1 75  LYS 75  65  65  LYS LYS A . n 
A 1 76  GLY 76  66  66  GLY GLY A . n 
A 1 77  ILE 77  67  67  ILE ILE A . n 
A 1 78  LEU 78  68  68  LEU LEU A . n 
A 1 79  ASN 79  69  69  ASN ASN A . n 
A 1 80  ALA 80  70  70  ALA ALA A . n 
A 1 81  LEU 81  71  71  LEU LEU A . n 
A 1 82  TYR 82  72  72  TYR TYR A . n 
A 1 83  GLU 83  73  73  GLU GLU A . n 
A 1 84  ALA 84  74  74  ALA ALA A . n 
A 1 85  LYS 85  75  75  LYS LYS A . n 
A 1 86  ARG 86  76  76  ARG ARG A . n 
A 1 87  GLN 87  77  77  GLN GLN A . n 
A 1 88  ARG 88  78  78  ARG ARG A . n 
A 1 89  PRO 89  79  79  PRO PRO A . n 
A 1 90  GLU 90  80  80  GLU GLU A . n 
A 1 91  LEU 91  81  81  LEU LEU A . n 
A 1 92  ASP 92  82  82  ASP ASP A . n 
A 1 93  VAL 93  83  83  VAL VAL A . n 
A 1 94  ARG 94  84  84  ARG ARG A . n 
A 1 95  VAL 95  85  85  VAL VAL A . n 
A 1 96  LEU 96  86  86  LEU LEU A . n 
A 1 97  VAL 97  87  87  VAL VAL A . n 
A 1 98  ASP 98  88  88  ASP ASP A . n 
A 1 99  TRP 99  89  89  TRP TRP A . n 
A 1 100 HIS 100 90  90  HIS HIS A . n 
A 1 101 ARG 101 91  91  ARG ARG A . n 
A 1 102 ALA 102 92  92  ALA ALA A . n 
A 1 103 GLN 103 93  93  GLN GLN A . n 
A 1 104 ARG 104 94  94  ARG ARG A . n 
A 1 105 GLY 105 95  95  GLY GLY A . n 
A 1 106 ARG 106 96  96  ARG ARG A . n 
A 1 107 ILE 107 97  97  ILE ILE A . n 
A 1 108 GLY 108 98  98  GLY GLY A . n 
A 1 109 ALA 109 99  99  ALA ALA A . n 
A 1 110 ALA 110 100 100 ALA ALA A . n 
A 1 111 ALA 111 101 101 ALA ALA A . n 
A 1 112 SER 112 102 102 SER SER A . n 
A 1 113 ASN 113 103 103 ASN ASN A . n 
A 1 114 THR 114 104 104 THR THR A . n 
A 1 115 ASN 115 105 105 ASN ASN A . n 
A 1 116 ALA 116 106 106 ALA ALA A . n 
A 1 117 ASP 117 107 107 ASP ASP A . n 
A 1 118 TRP 118 108 108 TRP TRP A . n 
A 1 119 TYR 119 109 109 TYR TYR A . n 
A 1 120 CYS 120 110 110 CYS CYS A . n 
A 1 121 ARG 121 111 111 ARG ARG A . n 
A 1 122 MET 122 112 112 MET MET A . n 
A 1 123 ALA 123 113 113 ALA ALA A . n 
A 1 124 GLN 124 114 114 GLN GLN A . n 
A 1 125 GLU 125 115 115 GLU GLU A . n 
A 1 126 ASN 126 116 116 ASN ASN A . n 
A 1 127 PRO 127 117 117 PRO PRO A . n 
A 1 128 GLY 128 118 118 GLY GLY A . n 
A 1 129 VAL 129 119 119 VAL VAL A . n 
A 1 130 ASP 130 120 120 ASP ASP A . n 
A 1 131 VAL 131 121 121 VAL VAL A . n 
A 1 132 PRO 132 122 122 PRO PRO A . n 
A 1 133 VAL 133 123 123 VAL VAL A . n 
A 1 134 TYR 134 124 124 TYR TYR A . n 
A 1 135 GLY 135 125 125 GLY GLY A . n 
A 1 136 VAL 136 126 126 VAL VAL A . n 
A 1 137 PRO 137 127 127 PRO PRO A . n 
A 1 138 ILE 138 128 128 ILE ILE A . n 
A 1 139 ASN 139 129 129 ASN ASN A . n 
A 1 140 THR 140 130 130 THR THR A . n 
A 1 141 ARG 141 131 131 ARG ARG A . n 
A 1 142 GLU 142 132 132 GLU GLU A . n 
A 1 143 ALA 143 133 133 ALA ALA A . n 
A 1 144 LEU 144 134 134 LEU LEU A . n 
A 1 145 GLY 145 135 135 GLY GLY A . n 
A 1 146 VAL 146 136 136 VAL VAL A . n 
A 1 147 LEU 147 137 137 LEU LEU A . n 
A 1 148 HIS 148 138 138 HIS HIS A . n 
A 1 149 PHE 149 139 139 PHE PHE A . n 
A 1 150 LYS 150 140 140 LYS LYS A . n 
A 1 151 GLY 151 141 141 GLY GLY A . n 
A 1 152 PHE 152 142 142 PHE PHE A . n 
A 1 153 ILE 153 143 143 ILE ILE A . n 
A 1 154 ILE 154 144 144 ILE ILE A . n 
A 1 155 ASP 155 145 145 ASP ASP A . n 
A 1 156 ASP 156 146 146 ASP ASP A . n 
A 1 157 SER 157 147 147 SER SER A . n 
A 1 158 VAL 158 148 148 VAL VAL A . n 
A 1 159 LEU 159 149 149 LEU LEU A . n 
A 1 160 TYR 160 150 150 TYR TYR A . n 
A 1 161 SER 161 151 151 SER SER A . n 
A 1 162 GLY 162 152 152 GLY GLY A . n 
A 1 163 ALA 163 153 153 ALA ALA A . n 
A 1 164 SER 164 154 154 SER SER A . n 
A 1 165 LEU 165 155 155 LEU LEU A . n 
A 1 166 ASN 166 156 156 ASN ASN A . n 
A 1 167 ASP 167 157 157 ASP ASP A . n 
A 1 168 VAL 168 158 158 VAL VAL A . n 
A 1 169 TYR 169 159 159 TYR TYR A . n 
A 1 170 LEU 170 160 160 LEU LEU A . n 
A 1 171 HIS 171 161 161 HIS HIS A . n 
A 1 172 GLN 172 162 162 GLN GLN A . n 
A 1 173 HIS 173 163 163 HIS HIS A . n 
A 1 174 ASP 174 164 164 ASP ASP A . n 
A 1 175 LYS 175 165 165 LYS LYS A . n 
A 1 176 TYR 176 166 166 TYR TYR A . n 
A 1 177 ARG 177 167 167 ARG ARG A . n 
A 1 178 TYR 178 168 168 TYR TYR A . n 
A 1 179 ASP 179 169 169 ASP ASP A . n 
A 1 180 ARG 180 170 170 ARG ARG A . n 
A 1 181 TYR 181 171 171 TYR TYR A . n 
A 1 182 HIS 182 172 172 HIS HIS A . n 
A 1 183 LEU 183 173 173 LEU LEU A . n 
A 1 184 ILE 184 174 174 ILE ILE A . n 
A 1 185 ARG 185 175 175 ARG ARG A . n 
A 1 186 ASN 186 176 176 ASN ASN A . n 
A 1 187 ARG 187 177 177 ARG ARG A . n 
A 1 188 LYS 188 178 178 LYS LYS A . n 
A 1 189 MET 189 179 179 MET MET A . n 
A 1 190 SER 190 180 180 SER SER A . n 
A 1 191 ASP 191 181 181 ASP ASP A . n 
A 1 192 ILE 192 182 182 ILE ILE A . n 
A 1 193 MET 193 183 183 MET MET A . n 
A 1 194 PHE 194 184 184 PHE PHE A . n 
A 1 195 GLU 195 185 185 GLU GLU A . n 
A 1 196 TRP 196 186 186 TRP TRP A . n 
A 1 197 VAL 197 187 187 VAL VAL A . n 
A 1 198 THR 198 188 188 THR THR A . n 
A 1 199 GLN 199 189 189 GLN GLN A . n 
A 1 200 ASN 200 190 190 ASN ASN A . n 
A 1 201 ILE 201 191 191 ILE ILE A . n 
A 1 202 MET 202 192 192 MET MET A . n 
A 1 203 ASN 203 193 193 ASN ASN A . n 
A 1 204 GLY 204 194 194 GLY GLY A . n 
A 1 205 ARG 205 195 195 ARG ARG A . n 
A 1 206 GLY 206 196 196 GLY GLY A . n 
A 1 207 VAL 207 197 197 VAL VAL A . n 
A 1 208 ASN 208 198 198 ASN ASN A . n 
A 1 209 ARG 209 199 199 ARG ARG A . n 
A 1 210 LEU 210 200 200 LEU LEU A . n 
A 1 211 ASP 211 201 201 ASP ASP A . n 
A 1 212 ASP 212 202 202 ASP ASP A . n 
A 1 213 VAL 213 203 203 VAL VAL A . n 
A 1 214 ASN 214 204 204 ASN ASN A . n 
A 1 215 ARG 215 205 205 ARG ARG A . n 
A 1 216 PRO 216 206 206 PRO PRO A . n 
A 1 217 LYS 217 207 207 LYS LYS A . n 
A 1 218 SER 218 208 208 SER SER A . n 
A 1 219 PRO 219 209 209 PRO PRO A . n 
A 1 220 GLU 220 210 210 GLU GLU A . n 
A 1 221 ILE 221 211 211 ILE ILE A . n 
A 1 222 LYS 222 212 212 LYS LYS A . n 
A 1 223 ASN 223 213 213 ASN ASN A . n 
A 1 224 ASP 224 214 214 ASP ASP A . n 
A 1 225 ILE 225 215 215 ILE ILE A . n 
A 1 226 ARG 226 216 216 ARG ARG A . n 
A 1 227 LEU 227 217 217 LEU LEU A . n 
A 1 228 PHE 228 218 218 PHE PHE A . n 
A 1 229 ARG 229 219 219 ARG ARG A . n 
A 1 230 GLN 230 220 220 GLN GLN A . n 
A 1 231 GLU 231 221 221 GLU GLU A . n 
A 1 232 LEU 232 222 222 LEU LEU A . n 
A 1 233 ARG 233 223 223 ARG ARG A . n 
A 1 234 ASP 234 224 224 ASP ASP A . n 
A 1 235 ALA 235 225 225 ALA ALA A . n 
A 1 236 ALA 236 226 226 ALA ALA A . n 
A 1 237 TYR 237 227 227 TYR TYR A . n 
A 1 238 HIS 238 228 228 HIS HIS A . n 
A 1 239 PHE 239 229 229 PHE PHE A . n 
A 1 240 GLN 240 230 230 GLN GLN A . n 
A 1 241 GLY 241 231 231 GLY GLY A . n 
A 1 242 ASP 242 232 232 ASP ASP A . n 
A 1 243 ALA 243 233 233 ALA ALA A . n 
A 1 244 ASP 244 234 234 ASP ASP A . n 
A 1 245 ASN 245 235 235 ASN ASN A . n 
A 1 246 ASP 246 236 236 ASP ASP A . n 
A 1 247 GLN 247 237 237 GLN GLN A . n 
A 1 248 LEU 248 238 238 LEU LEU A . n 
A 1 249 SER 249 239 239 SER SER A . n 
A 1 250 VAL 250 240 240 VAL VAL A . n 
A 1 251 THR 251 241 241 THR THR A . n 
A 1 252 PRO 252 242 242 PRO PRO A . n 
A 1 253 LEU 253 243 243 LEU LEU A . n 
A 1 254 VAL 254 244 244 VAL VAL A . n 
A 1 255 GLY 255 245 245 GLY GLY A . n 
A 1 256 LEU 256 246 246 LEU LEU A . n 
A 1 257 GLY 257 247 247 GLY GLY A . n 
A 1 258 LYS 258 248 248 LYS LYS A . n 
A 1 259 SER 259 249 249 SER SER A . n 
A 1 260 SER 260 250 250 SER SER A . n 
A 1 261 LEU 261 251 251 LEU LEU A . n 
A 1 262 LEU 262 252 252 LEU LEU A . n 
A 1 263 ASN 263 253 253 ASN ASN A . n 
A 1 264 LYS 264 254 254 LYS LYS A . n 
A 1 265 THR 265 255 255 THR THR A . n 
A 1 266 ILE 266 256 256 ILE ILE A . n 
A 1 267 PHE 267 257 257 PHE PHE A . n 
A 1 268 HIS 268 258 258 HIS HIS A . n 
A 1 269 LEU 269 259 259 LEU LEU A . n 
A 1 270 MET 270 260 260 MET MET A . n 
A 1 271 PRO 271 261 261 PRO PRO A . n 
A 1 272 CYS 272 262 262 CYS CYS A . n 
A 1 273 ALA 273 263 263 ALA ALA A . n 
A 1 274 GLU 274 264 264 GLU GLU A . n 
A 1 275 GLN 275 265 265 GLN GLN A . n 
A 1 276 LYS 276 266 266 LYS LYS A . n 
A 1 277 LEU 277 267 267 LEU LEU A . n 
A 1 278 THR 278 268 268 THR THR A . n 
A 1 279 ILE 279 269 269 ILE ILE A . n 
A 1 280 CYS 280 270 270 CYS CYS A . n 
A 1 281 THR 281 271 271 THR THR A . n 
A 1 282 PRO 282 272 272 PRO PRO A . n 
A 1 283 TYR 283 273 273 TYR TYR A . n 
A 1 284 PHE 284 274 274 PHE PHE A . n 
A 1 285 ASN 285 275 275 ASN ASN A . n 
A 1 286 LEU 286 276 276 LEU LEU A . n 
A 1 287 PRO 287 277 277 PRO PRO A . n 
A 1 288 ALA 288 278 278 ALA ALA A . n 
A 1 289 ILE 289 279 279 ILE ILE A . n 
A 1 290 LEU 290 280 280 LEU LEU A . n 
A 1 291 VAL 291 281 281 VAL VAL A . n 
A 1 292 ARG 292 282 282 ARG ARG A . n 
A 1 293 ASN 293 283 283 ASN ASN A . n 
A 1 294 ILE 294 284 284 ILE ILE A . n 
A 1 295 ILE 295 285 285 ILE ILE A . n 
A 1 296 GLN 296 286 286 GLN GLN A . n 
A 1 297 LEU 297 287 287 LEU LEU A . n 
A 1 298 LEU 298 288 288 LEU LEU A . n 
A 1 299 ARG 299 289 289 ARG ARG A . n 
A 1 300 GLU 300 290 290 GLU GLU A . n 
A 1 301 GLY 301 291 291 GLY GLY A . n 
A 1 302 LYS 302 292 292 LYS LYS A . n 
A 1 303 LYS 303 293 293 LYS LYS A . n 
A 1 304 VAL 304 294 294 VAL VAL A . n 
A 1 305 GLU 305 295 295 GLU GLU A . n 
A 1 306 ILE 306 296 296 ILE ILE A . n 
A 1 307 ILE 307 297 297 ILE ILE A . n 
A 1 308 VAL 308 298 298 VAL VAL A . n 
A 1 309 GLY 309 299 299 GLY GLY A . n 
A 1 310 ASP 310 300 300 ASP ASP A . n 
A 1 311 LYS 311 301 301 LYS LYS A . n 
A 1 312 THR 312 302 302 THR THR A . n 
A 1 313 ALA 313 303 303 ALA ALA A . n 
A 1 314 ASN 314 304 304 ASN ASN A . n 
A 1 315 ASP 315 305 305 ASP ASP A . n 
A 1 316 PHE 316 306 306 PHE PHE A . n 
A 1 317 TYR 317 307 307 TYR TYR A . n 
A 1 318 ILE 318 308 308 ILE ILE A . n 
A 1 319 PRO 319 309 309 PRO PRO A . n 
A 1 320 GLU 320 310 310 GLU GLU A . n 
A 1 321 ASP 321 311 311 ASP ASP A . n 
A 1 322 GLU 322 312 312 GLU GLU A . n 
A 1 323 PRO 323 313 313 PRO PRO A . n 
A 1 324 PHE 324 314 314 PHE PHE A . n 
A 1 325 LYS 325 315 315 LYS LYS A . n 
A 1 326 ILE 326 316 316 ILE ILE A . n 
A 1 327 ILE 327 317 317 ILE ILE A . n 
A 1 328 GLY 328 318 318 GLY GLY A . n 
A 1 329 ALA 329 319 319 ALA ALA A . n 
A 1 330 LEU 330 320 320 LEU LEU A . n 
A 1 331 PRO 331 321 321 PRO PRO A . n 
A 1 332 TYR 332 322 322 TYR TYR A . n 
A 1 333 LEU 333 323 323 LEU LEU A . n 
A 1 334 TYR 334 324 324 TYR TYR A . n 
A 1 335 GLU 335 325 325 GLU GLU A . n 
A 1 336 ILE 336 326 326 ILE ILE A . n 
A 1 337 ASN 337 327 327 ASN ASN A . n 
A 1 338 LEU 338 328 328 LEU LEU A . n 
A 1 339 ARG 339 329 329 ARG ARG A . n 
A 1 340 ARG 340 330 330 ARG ARG A . n 
A 1 341 PHE 341 331 331 PHE PHE A . n 
A 1 342 LEU 342 332 332 LEU LEU A . n 
A 1 343 SER 343 333 333 SER SER A . n 
A 1 344 ARG 344 334 334 ARG ARG A . n 
A 1 345 LEU 345 335 335 LEU LEU A . n 
A 1 346 GLN 346 336 336 GLN GLN A . n 
A 1 347 TYR 347 337 337 TYR TYR A . n 
A 1 348 TYR 348 338 338 TYR TYR A . n 
A 1 349 VAL 349 339 339 VAL VAL A . n 
A 1 350 ASN 350 340 340 ASN ASN A . n 
A 1 351 THR 351 341 341 THR THR A . n 
A 1 352 ASP 352 342 342 ASP ASP A . n 
A 1 353 GLN 353 343 343 GLN GLN A . n 
A 1 354 LEU 354 344 344 LEU LEU A . n 
A 1 355 VAL 355 345 345 VAL VAL A . n 
A 1 356 VAL 356 346 346 VAL VAL A . n 
A 1 357 ARG 357 347 347 ARG ARG A . n 
A 1 358 LEU 358 348 348 LEU LEU A . n 
A 1 359 TRP 359 349 349 TRP TRP A . n 
A 1 360 LYS 360 350 350 LYS LYS A . n 
A 1 361 ASP 361 351 351 ASP ASP A . n 
A 1 362 ASP 362 352 352 ASP ASP A . n 
A 1 363 ASP 363 353 353 ASP ASP A . n 
A 1 364 ASN 364 354 354 ASN ASN A . n 
A 1 365 THR 365 355 355 THR THR A . n 
A 1 366 TYR 366 356 356 TYR TYR A . n 
A 1 367 ALA 367 357 357 ALA ALA A . n 
A 1 368 LEU 368 358 358 LEU LEU A . n 
A 1 369 LYS 369 359 359 LYS LYS A . n 
A 1 370 GLY 370 360 360 GLY GLY A . n 
A 1 371 MET 371 361 361 MET MET A . n 
A 1 372 TRP 372 362 362 TRP TRP A . n 
A 1 373 VAL 373 363 363 VAL VAL A . n 
A 1 374 ASP 374 364 364 ASP ASP A . n 
A 1 375 ASP 375 365 365 ASP ASP A . n 
A 1 376 LYS 376 366 366 LYS LYS A . n 
A 1 377 TRP 377 367 367 TRP TRP A . n 
A 1 378 MET 378 368 368 MET MET A . n 
A 1 379 LEU 379 369 369 LEU LEU A . n 
A 1 380 ILE 380 370 370 ILE ILE A . n 
A 1 381 THR 381 371 371 THR THR A . n 
A 1 382 GLY 382 372 372 GLY GLY A . n 
A 1 383 ASN 383 373 373 ASN ASN A . n 
A 1 384 ASN 384 374 374 ASN ASN A . n 
A 1 385 LEU 385 375 375 LEU LEU A . n 
A 1 386 ASN 386 376 376 ASN ASN A . n 
A 1 387 PRO 387 377 377 PRO PRO A . n 
A 1 388 ARG 388 378 378 ARG ARG A . n 
A 1 389 ALA 389 379 379 ALA ALA A . n 
A 1 390 TRP 390 380 380 TRP TRP A . n 
A 1 391 ARG 391 381 381 ARG ARG A . n 
A 1 392 LEU 392 382 382 LEU LEU A . n 
A 1 393 ASP 393 383 383 ASP ASP A . n 
A 1 394 LEU 394 384 384 LEU LEU A . n 
A 1 395 GLU 395 385 385 GLU GLU A . n 
A 1 396 ASN 396 386 386 ASN ASN A . n 
A 1 397 ALA 397 387 387 ALA ALA A . n 
A 1 398 ILE 398 388 388 ILE ILE A . n 
A 1 399 LEU 399 389 389 LEU LEU A . n 
A 1 400 ILE 400 390 390 ILE ILE A . n 
A 1 401 HIS 401 391 391 HIS HIS A . n 
A 1 402 ASP 402 392 392 ASP ASP A . n 
A 1 403 PRO 403 393 393 PRO PRO A . n 
A 1 404 GLN 404 394 394 GLN GLN A . n 
A 1 405 LEU 405 395 395 LEU LEU A . n 
A 1 406 GLU 406 396 396 GLU GLU A . n 
A 1 407 LEU 407 397 397 LEU LEU A . n 
A 1 408 ALA 408 398 398 ALA ALA A . n 
A 1 409 PRO 409 399 399 PRO PRO A . n 
A 1 410 GLN 410 400 400 GLN GLN A . n 
A 1 411 ARG 411 401 401 ARG ARG A . n 
A 1 412 GLU 412 402 402 GLU GLU A . n 
A 1 413 LYS 413 403 403 LYS LYS A . n 
A 1 414 GLU 414 404 404 GLU GLU A . n 
A 1 415 LEU 415 405 405 LEU LEU A . n 
A 1 416 GLU 416 406 406 GLU GLU A . n 
A 1 417 LEU 417 407 407 LEU LEU A . n 
A 1 418 ILE 418 408 408 ILE ILE A . n 
A 1 419 ARG 419 409 409 ARG ARG A . n 
A 1 420 GLU 420 410 410 GLU GLU A . n 
A 1 421 HIS 421 411 411 HIS HIS A . n 
A 1 422 THR 422 412 412 THR THR A . n 
A 1 423 THR 423 413 413 THR THR A . n 
A 1 424 ILE 424 414 414 ILE ILE A . n 
A 1 425 VAL 425 415 415 VAL VAL A . n 
A 1 426 LYS 426 416 416 LYS LYS A . n 
A 1 427 HIS 427 417 417 HIS HIS A . n 
A 1 428 TYR 428 418 418 TYR TYR A . n 
A 1 429 ARG 429 419 419 ARG ARG A . n 
A 1 430 ASP 430 420 420 ASP ASP A . n 
A 1 431 LEU 431 421 421 LEU LEU A . n 
A 1 432 GLN 432 422 422 GLN GLN A . n 
A 1 433 SER 433 423 423 SER SER A . n 
A 1 434 ILE 434 424 424 ILE ILE A . n 
A 1 435 ALA 435 425 425 ALA ALA A . n 
A 1 436 ASP 436 426 426 ASP ASP A . n 
A 1 437 TYR 437 427 427 TYR TYR A . n 
A 1 438 PRO 438 428 428 PRO PRO A . n 
A 1 439 VAL 439 429 429 VAL VAL A . n 
A 1 440 LYS 440 430 430 LYS LYS A . n 
A 1 441 VAL 441 431 431 VAL VAL A . n 
A 1 442 ARG 442 432 432 ARG ARG A . n 
A 1 443 LYS 443 433 433 LYS LYS A . n 
A 1 444 LEU 444 434 434 LEU LEU A . n 
A 1 445 ILE 445 435 435 ILE ILE A . n 
A 1 446 ARG 446 436 436 ARG ARG A . n 
A 1 447 ARG 447 437 437 ARG ARG A . n 
A 1 448 LEU 448 438 438 LEU LEU A . n 
A 1 449 ARG 449 439 439 ARG ARG A . n 
A 1 450 ARG 450 440 440 ARG ARG A . n 
A 1 451 ILE 451 441 441 ILE ILE A . n 
A 1 452 ARG 452 442 442 ARG ARG A . n 
A 1 453 ILE 453 443 443 ILE ILE A . n 
A 1 454 ASP 454 444 444 ASP ASP A . n 
A 1 455 ARG 455 445 445 ARG ARG A . n 
A 1 456 LEU 456 446 446 LEU LEU A . n 
A 1 457 ILE 457 447 447 ILE ILE A . n 
A 1 458 SER 458 448 448 SER SER A . n 
A 1 459 ARG 459 449 449 ARG ARG A . n 
A 1 460 ILE 460 450 450 ILE ILE A . n 
A 1 461 LEU 461 451 451 LEU LEU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1LZV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1LZV 
_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 A1LZV 1  501 501 A1LZV 00Z A . 
C 3 SO4   1  502 1   SO4   SO4 A . 
D 4 HOH   1  601 153 HOH   HOH A . 
D 4 HOH   2  602 117 HOH   HOH A . 
D 4 HOH   3  603 182 HOH   HOH A . 
D 4 HOH   4  604 339 HOH   HOH A . 
D 4 HOH   5  605 19  HOH   HOH A . 
D 4 HOH   6  606 24  HOH   HOH A . 
D 4 HOH   7  607 4   HOH   HOH A . 
D 4 HOH   8  608 287 HOH   HOH A . 
D 4 HOH   9  609 5   HOH   HOH A . 
D 4 HOH   10 610 8   HOH   HOH A . 
D 4 HOH   11 611 116 HOH   HOH A . 
D 4 HOH   12 612 298 HOH   HOH A . 
D 4 HOH   13 613 113 HOH   HOH A . 
D 4 HOH   14 614 169 HOH   HOH A . 
D 4 HOH   15 615 6   HOH   HOH A . 
D 4 HOH   16 616 253 HOH   HOH A . 
D 4 HOH   17 617 44  HOH   HOH A . 
D 4 HOH   18 618 2   HOH   HOH A . 
D 4 HOH   19 619 14  HOH   HOH A . 
D 4 HOH   20 620 54  HOH   HOH A . 
D 4 HOH   21 621 27  HOH   HOH A . 
D 4 HOH   22 622 28  HOH   HOH A . 
D 4 HOH   23 623 16  HOH   HOH A . 
D 4 HOH   24 624 17  HOH   HOH A . 
D 4 HOH   25 625 48  HOH   HOH A . 
D 4 HOH   26 626 25  HOH   HOH A . 
D 4 HOH   27 627 12  HOH   HOH A . 
D 4 HOH   28 628 22  HOH   HOH A . 
D 4 HOH   29 629 9   HOH   HOH A . 
D 4 HOH   30 630 15  HOH   HOH A . 
D 4 HOH   31 631 18  HOH   HOH A . 
D 4 HOH   32 632 35  HOH   HOH A . 
D 4 HOH   33 633 21  HOH   HOH A . 
D 4 HOH   34 634 147 HOH   HOH A . 
D 4 HOH   35 635 11  HOH   HOH A . 
D 4 HOH   36 636 143 HOH   HOH A . 
D 4 HOH   37 637 239 HOH   HOH A . 
D 4 HOH   38 638 29  HOH   HOH A . 
D 4 HOH   39 639 13  HOH   HOH A . 
D 4 HOH   40 640 108 HOH   HOH A . 
D 4 HOH   41 641 56  HOH   HOH A . 
D 4 HOH   42 642 97  HOH   HOH A . 
D 4 HOH   43 643 211 HOH   HOH A . 
D 4 HOH   44 644 61  HOH   HOH A . 
D 4 HOH   45 645 38  HOH   HOH A . 
D 4 HOH   46 646 50  HOH   HOH A . 
D 4 HOH   47 647 33  HOH   HOH A . 
D 4 HOH   48 648 263 HOH   HOH A . 
D 4 HOH   49 649 151 HOH   HOH A . 
D 4 HOH   50 650 278 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      ? ? ? 5.8.0425 1 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxDC        ? ? ? .        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? 3.8.6    3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? DIALS       ? ? ? 3.8      4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.15   5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        6 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        7 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        8 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YR6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     160.497 
_cell.length_a_esd                 ? 
_cell.length_b                     160.497 
_cell.length_b_esd                 ? 
_cell.length_c                     160.497 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         8YR6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                197 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 3' 
_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                   8YR6 
_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             3.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.49 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1 M Lithium sulfate monohydrate, 0.1 M ADA pH 6.5, 12% polyethylene glycol, 2 % (w/v) 2-propanol, 0.5 %(w/v) DDM' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            297 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             LN2 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-29 
_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   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PAL/PLS BEAMLINE 5C (4A)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '5C (4A)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YR6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.44 
_reflns.d_resolution_low                               42.89 
_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                                     25695 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                40.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.98 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.260 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1041621 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.256 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.44 
_reflns_shell.d_res_low                                     2.54 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           113789 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2868 
_reflns_shell.percent_possible_obs                          100.0 
_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                               39.7 
_reflns_shell.pdbx_chi_squared                              1.03 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               5.276 
_reflns_shell.pdbx_Rpim_I_all                               0.836 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.483 
_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                                  5.209 
_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]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               65.996 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.943 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 8YR6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.44 
_refine.ls_d_res_low                             42.89 
_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                     24360 
_refine.ls_number_reflns_R_free                  1268 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.83 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21406 
_refine.ls_R_factor_R_free                       0.24698 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21233 
_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                       0.337 
_refine.pdbx_overall_ESU_R_Free                  0.242 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                             10.324 
_refine.overall_SU_ML                            0.213 
_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                       2.44 
_refine_hist.d_res_low                        42.89 
_refine_hist.number_atoms_solvent             50 
_refine_hist.number_atoms_total               3779 
_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        3660 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         69 
_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' ? 0.003  0.012  3806 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3698 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.067  1.836  5149 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.456  1.787  8472 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.700  5.000  443  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.935  5.000  41   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.892 10.000 675  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.048  0.200  562  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  4531 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  930  ? 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' ? 1.682  6.500  1775 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.682  6.500  1775 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.794  11.686 2217 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.794  11.686 2218 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.712  6.735  2031 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.709  6.732  2028 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.986  12.293 2927 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.760  61.68  4195 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.761  61.70  4191 ? 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                       2.440 
_refine_ls_shell.d_res_low                        2.503 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             91 
_refine_ls_shell.number_reflns_R_work             1745 
_refine_ls_shell.percent_reflns_obs               99.84 
_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                  0.341 
_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                  0.383 
# 
_struct.entry_id                     8YR6 
_struct.title                        'Crystal structure of E. coli phosphatidylserine synthase complexed with 16:0/16:0 CDP-DG' 
_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        8YR6 
_struct_keywords.text            
'Complex, Phospholipid metabolism, Peripheral membrane protein, Phosphatidylserine, MEMBRANE PROTEIN, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PSS_ECOLI 
_struct_ref.pdbx_db_accession          P23830 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPADFRETLLEKIASAKQRICIVALYLEQDDGGKGILNALYEAKRQRPEL
DVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGVDVPVYGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYLH
QHDKYRYDRYHLIRNRKMSDIMFEWVTQNIMNGRGVNRLDDVNRPKSPEIKNDIRLFRQELRDAAYHFQGDADNDQLSVT
PLVGLGKSSLLNKTIFHLMPCAEQKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFYIPEDEPFKIIGALP
YLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLITGNNLNPRAWRLDLENAILIHDPQLELAPQR
EKELELIREHTTIVKHYRDLQSIADYPVKVRKLIRRLRRIRIDRLISRIL
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YR6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 12 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 461 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P23830 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  451 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       451 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YR6 MET A 1   ? UNP P23830 ?   ?   'initiating methionine' -9  1  
1 8YR6 GLY A 2   ? UNP P23830 ?   ?   'expression tag'        -8  2  
1 8YR6 SER A 3   ? UNP P23830 ?   ?   'expression tag'        -7  3  
1 8YR6 HIS A 4   ? UNP P23830 ?   ?   'expression tag'        -6  4  
1 8YR6 HIS A 5   ? UNP P23830 ?   ?   'expression tag'        -5  5  
1 8YR6 HIS A 6   ? UNP P23830 ?   ?   'expression tag'        -4  6  
1 8YR6 HIS A 7   ? UNP P23830 ?   ?   'expression tag'        -3  7  
1 8YR6 HIS A 8   ? UNP P23830 ?   ?   'expression tag'        -2  8  
1 8YR6 HIS A 9   ? UNP P23830 ?   ?   'expression tag'        -1  9  
1 8YR6 GLY A 10  ? UNP P23830 ?   ?   'expression tag'        0   10 
1 8YR6 SER A 11  ? UNP P23830 ?   ?   'expression tag'        1   11 
1 8YR6 ALA A 367 ? UNP P23830 HIS 357 'engineered mutation'   357 12 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 120   ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  18440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 18  ? LEU A 27  ? ASN A 8   LEU A 17  1 ? 10 
HELX_P HELX_P2  AA2 SER A 33  ? ASP A 35  ? SER A 23  ASP A 25  5 ? 3  
HELX_P HELX_P3  AA3 ALA A 42  ? ALA A 57  ? ALA A 32  ALA A 47  1 ? 16 
HELX_P HELX_P4  AA4 ASP A 71  ? ARG A 88  ? ASP A 61  ARG A 78  1 ? 18 
HELX_P HELX_P5  AA5 HIS A 100 ? ARG A 104 ? HIS A 90  ARG A 94  5 ? 5  
HELX_P HELX_P6  AA6 THR A 114 ? ASN A 126 ? THR A 104 ASN A 116 1 ? 13 
HELX_P HELX_P7  AA7 ARG A 141 ? GLY A 145 ? ARG A 131 GLY A 135 5 ? 5  
HELX_P HELX_P8  AA8 ASN A 166 ? HIS A 171 ? ASN A 156 HIS A 161 1 ? 6  
HELX_P HELX_P9  AA9 ASN A 186 ? ILE A 201 ? ASN A 176 ILE A 191 1 ? 16 
HELX_P HELX_P10 AB1 LYS A 217 ? ARG A 233 ? LYS A 207 ARG A 223 1 ? 17 
HELX_P HELX_P11 AB2 LEU A 256 ? SER A 259 ? LEU A 246 SER A 249 5 ? 4  
HELX_P HELX_P12 AB3 SER A 260 ? MET A 270 ? SER A 250 MET A 260 1 ? 11 
HELX_P HELX_P13 AB4 PRO A 271 ? ALA A 273 ? PRO A 261 ALA A 263 5 ? 3  
HELX_P HELX_P14 AB5 PRO A 287 ? GLU A 300 ? PRO A 277 GLU A 290 1 ? 14 
HELX_P HELX_P15 AB6 LYS A 311 ? ASN A 314 ? LYS A 301 ASN A 304 5 ? 4  
HELX_P HELX_P16 AB7 LYS A 325 ? GLY A 328 ? LYS A 315 GLY A 318 5 ? 4  
HELX_P HELX_P17 AB8 ALA A 329 ? LEU A 345 ? ALA A 319 LEU A 335 1 ? 17 
HELX_P HELX_P18 AB9 LEU A 345 ? THR A 351 ? LEU A 335 THR A 341 1 ? 7  
HELX_P HELX_P19 AC1 ASN A 386 ? LEU A 392 ? ASN A 376 LEU A 382 1 ? 7  
HELX_P HELX_P20 AC2 LEU A 407 ? GLU A 420 ? LEU A 397 GLU A 410 1 ? 14 
HELX_P HELX_P21 AC3 HIS A 427 ? LEU A 431 ? HIS A 417 LEU A 421 5 ? 5  
HELX_P HELX_P22 AC4 SER A 433 ? TYR A 437 ? SER A 423 TYR A 427 5 ? 5  
HELX_P HELX_P23 AC5 PRO A 438 ? ILE A 451 ? PRO A 428 ILE A 441 1 ? 14 
HELX_P HELX_P24 AC6 ARG A 452 ? SER A 458 ? ARG A 442 SER A 448 1 ? 7  
HELX_P HELX_P25 AC7 ARG A 459 ? LEU A 461 ? ARG A 449 LEU A 451 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 9 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
# 
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 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? anti-parallel 
AA4 1 2 ? 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 ILE A 30  ? SER A 31  ? ILE A 20  SER A 21  
AA1 2 SER A 249 ? GLY A 255 ? SER A 239 GLY A 245 
AA1 3 LEU A 394 ? HIS A 401 ? LEU A 384 HIS A 391 
AA1 4 LEU A 147 ? HIS A 148 ? LEU A 137 HIS A 138 
AA2 1 ILE A 30  ? SER A 31  ? ILE A 20  SER A 21  
AA2 2 SER A 249 ? GLY A 255 ? SER A 239 GLY A 245 
AA2 3 LEU A 394 ? HIS A 401 ? LEU A 384 HIS A 391 
AA2 4 TRP A 377 ? THR A 381 ? TRP A 367 THR A 371 
AA2 5 GLY A 370 ? VAL A 373 ? GLY A 360 VAL A 363 
AA2 6 LYS A 276 ? CYS A 280 ? LYS A 266 CYS A 270 
AA2 7 LYS A 303 ? GLY A 309 ? LYS A 293 GLY A 299 
AA2 8 LEU A 354 ? TRP A 359 ? LEU A 344 TRP A 349 
AA2 9 THR A 422 ? ILE A 424 ? THR A 412 ILE A 414 
AA3 1 VAL A 37  ? PHE A 40  ? VAL A 27  PHE A 30  
AA3 2 TYR A 181 ? ARG A 185 ? TYR A 171 ARG A 175 
AA3 3 SER A 157 ? SER A 161 ? SER A 147 SER A 151 
AA3 4 GLY A 151 ? ILE A 154 ? GLY A 141 ILE A 144 
AA3 5 ARG A 60  ? VAL A 64  ? ARG A 50  VAL A 54  
AA3 6 ASP A 92  ? ASP A 98  ? ASP A 82  ASP A 88  
AA3 7 VAL A 133 ? VAL A 136 ? VAL A 123 VAL A 126 
AA3 8 ASN A 208 ? ARG A 209 ? ASN A 198 ARG A 199 
AA4 1 ARG A 177 ? TYR A 178 ? ARG A 167 TYR A 168 
AA4 2 THR A 365 ? TYR A 366 ? THR A 355 TYR A 356 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 30  ? N ILE A 20  O VAL A 250 ? O VAL A 240 
AA1 2 3 N GLY A 255 ? N GLY A 245 O GLU A 395 ? O GLU A 385 
AA1 3 4 O LEU A 394 ? O LEU A 384 N HIS A 148 ? N HIS A 138 
AA2 1 2 N ILE A 30  ? N ILE A 20  O VAL A 250 ? O VAL A 240 
AA2 2 3 N GLY A 255 ? N GLY A 245 O GLU A 395 ? O GLU A 385 
AA2 3 4 O ILE A 400 ? O ILE A 390 N MET A 378 ? N MET A 368 
AA2 4 5 O LEU A 379 ? O LEU A 369 N MET A 371 ? N MET A 361 
AA2 5 6 O GLY A 370 ? O GLY A 360 N CYS A 280 ? N CYS A 270 
AA2 6 7 N LEU A 277 ? N LEU A 267 O GLU A 305 ? O GLU A 295 
AA2 7 8 N VAL A 304 ? N VAL A 294 O VAL A 355 ? O VAL A 345 
AA2 8 9 N LEU A 358 ? N LEU A 348 O THR A 423 ? O THR A 413 
AA3 1 2 N ASP A 38  ? N ASP A 28  O LEU A 183 ? O LEU A 173 
AA3 2 3 O HIS A 182 ? O HIS A 172 N TYR A 160 ? N TYR A 150 
AA3 3 4 O LEU A 159 ? O LEU A 149 N PHE A 152 ? N PHE A 142 
AA3 4 5 O ILE A 153 ? O ILE A 143 N CYS A 62  ? N CYS A 52  
AA3 5 6 N ILE A 63  ? N ILE A 53  O LEU A 96  ? O LEU A 86  
AA3 6 7 N VAL A 95  ? N VAL A 85  O TYR A 134 ? O TYR A 124 
AA3 7 8 N GLY A 135 ? N GLY A 125 O ASN A 208 ? O ASN A 198 
AA4 1 2 N TYR A 178 ? N TYR A 168 O THR A 365 ? O THR A 355 
# 
_pdbx_entry_details.entry_id                   8YR6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   PRO 
_pdbx_validate_close_contact.auth_seq_id_1    117 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
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 GLN A 49  ? ? -128.48 -56.06  
2  1 ASP A 145 ? ? 55.20   -119.61 
3  1 HIS A 163 ? ? -122.66 -130.62 
4  1 ASP A 169 ? ? -126.44 -168.01 
5  1 ASN A 176 ? ? -160.09 103.22  
6  1 ILE A 191 ? ? -111.65 -70.96  
7  1 ASP A 201 ? ? -92.64  39.03   
8  1 ASN A 204 ? ? -98.04  33.89   
9  1 GLN A 265 ? ? -126.93 -54.08  
10 1 ASN A 275 ? ? -165.89 62.03   
11 1 ASP A 352 ? ? 52.59   -125.38 
12 1 ALA A 357 ? ? -140.02 23.84   
13 1 ASP A 364 ? ? 51.08   -130.94 
14 1 HIS A 411 ? ? -97.35  33.17   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     330 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.081 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -9 ? A MET 1  
2  1 Y 1 A GLY -8 ? A GLY 2  
3  1 Y 1 A SER -7 ? A SER 3  
4  1 Y 1 A HIS -6 ? A HIS 4  
5  1 Y 1 A HIS -5 ? A HIS 5  
6  1 Y 1 A HIS -4 ? A HIS 6  
7  1 Y 1 A HIS -3 ? A HIS 7  
8  1 Y 1 A HIS -2 ? A HIS 8  
9  1 Y 1 A HIS -1 ? A HIS 9  
10 1 Y 1 A GLY 0  ? A GLY 10 
11 1 Y 1 A SER 1  ? A SER 11 
12 1 Y 1 A LEU 2  ? A LEU 12 
13 1 Y 1 A SER 3  ? A SER 13 
14 1 Y 1 A LYS 4  ? A LYS 14 
15 1 Y 1 A PHE 5  ? A PHE 15 
16 1 Y 1 A LYS 6  ? A LYS 16 
17 1 Y 1 A ARG 7  ? A ARG 17 
# 
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 
A1LZV OCL   O N N 1   
A1LZV CBE   C N N 2   
A1LZV CBF   C N N 3   
A1LZV CBG   C N N 4   
A1LZV CBH   C N N 5   
A1LZV CBI   C N N 6   
A1LZV CBJ   C N N 7   
A1LZV CBK   C N N 8   
A1LZV CBL   C N N 9   
A1LZV CBM   C N N 10  
A1LZV CBN   C N N 11  
A1LZV CBO   C N N 12  
A1LZV CBP   C N N 13  
A1LZV CBQ   C N N 14  
A1LZV CBR   C N N 15  
A1LZV CBS   C N N 16  
A1LZV CBT   C N N 17  
A1LZV OBD   O N N 18  
A1LZV CBC   C N N 19  
A1LZV CBA   C N R 20  
A1LZV CAZ   C N N 21  
A1LZV OAY   O N N 22  
A1LZV PAV   P N N 23  
A1LZV OAW   O N N 24  
A1LZV OAX   O N N 25  
A1LZV OAU   O N N 26  
A1LZV PAR   P N N 27  
A1LZV OAS   O N N 28  
A1LZV OAT   O N N 29  
A1LZV "O5'" O N N 30  
A1LZV "C5'" C N N 31  
A1LZV "C4'" C N R 32  
A1LZV "C3'" C N S 33  
A1LZV "O3'" O N N 34  
A1LZV "C2'" C N R 35  
A1LZV "O2'" O N N 36  
A1LZV "O4'" O N N 37  
A1LZV "C1'" C N R 38  
A1LZV NAH   N N N 39  
A1LZV CAG   C N N 40  
A1LZV CAF   C N N 41  
A1LZV CAD   C N N 42  
A1LZV NAE   N N N 43  
A1LZV NAC   N N N 44  
A1LZV CAB   C N N 45  
A1LZV OAA   O N N 46  
A1LZV OBB   O N N 47  
A1LZV CBU   C N N 48  
A1LZV OCK   O N N 49  
A1LZV CBV   C N N 50  
A1LZV CBW   C N N 51  
A1LZV CBX   C N N 52  
A1LZV CBY   C N N 53  
A1LZV CBZ   C N N 54  
A1LZV CCA   C N N 55  
A1LZV CCB   C N N 56  
A1LZV CCC   C N N 57  
A1LZV CCD   C N N 58  
A1LZV CCE   C N N 59  
A1LZV CCF   C N N 60  
A1LZV CCG   C N N 61  
A1LZV CCH   C N N 62  
A1LZV CCI   C N N 63  
A1LZV CCJ   C N N 64  
A1LZV H1    H N N 65  
A1LZV H2    H N N 66  
A1LZV H3    H N N 67  
A1LZV H4    H N N 68  
A1LZV H5    H N N 69  
A1LZV H6    H N N 70  
A1LZV H7    H N N 71  
A1LZV H8    H N N 72  
A1LZV H9    H N N 73  
A1LZV H10   H N N 74  
A1LZV H11   H N N 75  
A1LZV H12   H N N 76  
A1LZV H13   H N N 77  
A1LZV H14   H N N 78  
A1LZV H15   H N N 79  
A1LZV H16   H N N 80  
A1LZV H17   H N N 81  
A1LZV H18   H N N 82  
A1LZV H19   H N N 83  
A1LZV H20   H N N 84  
A1LZV H21   H N N 85  
A1LZV H22   H N N 86  
A1LZV H23   H N N 87  
A1LZV H24   H N N 88  
A1LZV H25   H N N 89  
A1LZV H26   H N N 90  
A1LZV H27   H N N 91  
A1LZV H28   H N N 92  
A1LZV H29   H N N 93  
A1LZV H30   H N N 94  
A1LZV H31   H N N 95  
A1LZV H32   H N N 96  
A1LZV H33   H N N 97  
A1LZV H34   H N N 98  
A1LZV H35   H N N 99  
A1LZV H36   H N N 100 
A1LZV H37   H N N 101 
A1LZV H38   H N N 102 
A1LZV H39   H N N 103 
A1LZV H40   H N N 104 
A1LZV H41   H N N 105 
A1LZV H42   H N N 106 
A1LZV H43   H N N 107 
A1LZV H44   H N N 108 
A1LZV H45   H N N 109 
A1LZV H46   H N N 110 
A1LZV H47   H N N 111 
A1LZV H48   H N N 112 
A1LZV H49   H N N 113 
A1LZV H50   H N N 114 
A1LZV H51   H N N 115 
A1LZV H52   H N N 116 
A1LZV H53   H N N 117 
A1LZV H54   H N N 118 
A1LZV H55   H N N 119 
A1LZV H56   H N N 120 
A1LZV H57   H N N 121 
A1LZV H58   H N N 122 
A1LZV H59   H N N 123 
A1LZV H60   H N N 124 
A1LZV H61   H N N 125 
A1LZV H62   H N N 126 
A1LZV H63   H N N 127 
A1LZV H64   H N N 128 
A1LZV H65   H N N 129 
A1LZV H66   H N N 130 
A1LZV H67   H N N 131 
A1LZV H68   H N N 132 
A1LZV H69   H N N 133 
A1LZV H70   H N N 134 
A1LZV H71   H N N 135 
A1LZV H72   H N N 136 
A1LZV H73   H N N 137 
A1LZV H74   H N N 138 
A1LZV H75   H N N 139 
A1LZV H76   H N N 140 
A1LZV H77   H N N 141 
A1LZV H78   H N N 142 
A1LZV H79   H N N 143 
A1LZV H80   H N N 144 
A1LZV H81   H N N 145 
ALA   N     N N N 146 
ALA   CA    C N S 147 
ALA   C     C N N 148 
ALA   O     O N N 149 
ALA   CB    C N N 150 
ALA   OXT   O N N 151 
ALA   H     H N N 152 
ALA   H2    H N N 153 
ALA   HA    H N N 154 
ALA   HB1   H N N 155 
ALA   HB2   H N N 156 
ALA   HB3   H N N 157 
ALA   HXT   H N N 158 
ARG   N     N N N 159 
ARG   CA    C N S 160 
ARG   C     C N N 161 
ARG   O     O N N 162 
ARG   CB    C N N 163 
ARG   CG    C N N 164 
ARG   CD    C N N 165 
ARG   NE    N N N 166 
ARG   CZ    C N N 167 
ARG   NH1   N N N 168 
ARG   NH2   N N N 169 
ARG   OXT   O N N 170 
ARG   H     H N N 171 
ARG   H2    H N N 172 
ARG   HA    H N N 173 
ARG   HB2   H N N 174 
ARG   HB3   H N N 175 
ARG   HG2   H N N 176 
ARG   HG3   H N N 177 
ARG   HD2   H N N 178 
ARG   HD3   H N N 179 
ARG   HE    H N N 180 
ARG   HH11  H N N 181 
ARG   HH12  H N N 182 
ARG   HH21  H N N 183 
ARG   HH22  H N N 184 
ARG   HXT   H N N 185 
ASN   N     N N N 186 
ASN   CA    C N S 187 
ASN   C     C N N 188 
ASN   O     O N N 189 
ASN   CB    C N N 190 
ASN   CG    C N N 191 
ASN   OD1   O N N 192 
ASN   ND2   N N N 193 
ASN   OXT   O N N 194 
ASN   H     H N N 195 
ASN   H2    H N N 196 
ASN   HA    H N N 197 
ASN   HB2   H N N 198 
ASN   HB3   H N N 199 
ASN   HD21  H N N 200 
ASN   HD22  H N N 201 
ASN   HXT   H N N 202 
ASP   N     N N N 203 
ASP   CA    C N S 204 
ASP   C     C N N 205 
ASP   O     O N N 206 
ASP   CB    C N N 207 
ASP   CG    C N N 208 
ASP   OD1   O N N 209 
ASP   OD2   O N N 210 
ASP   OXT   O N N 211 
ASP   H     H N N 212 
ASP   H2    H N N 213 
ASP   HA    H N N 214 
ASP   HB2   H N N 215 
ASP   HB3   H N N 216 
ASP   HD2   H N N 217 
ASP   HXT   H N N 218 
CYS   N     N N N 219 
CYS   CA    C N R 220 
CYS   C     C N N 221 
CYS   O     O N N 222 
CYS   CB    C N N 223 
CYS   SG    S N N 224 
CYS   OXT   O N N 225 
CYS   H     H N N 226 
CYS   H2    H N N 227 
CYS   HA    H N N 228 
CYS   HB2   H N N 229 
CYS   HB3   H N N 230 
CYS   HG    H N N 231 
CYS   HXT   H N N 232 
GLN   N     N N N 233 
GLN   CA    C N S 234 
GLN   C     C N N 235 
GLN   O     O N N 236 
GLN   CB    C N N 237 
GLN   CG    C N N 238 
GLN   CD    C N N 239 
GLN   OE1   O N N 240 
GLN   NE2   N N N 241 
GLN   OXT   O N N 242 
GLN   H     H N N 243 
GLN   H2    H N N 244 
GLN   HA    H N N 245 
GLN   HB2   H N N 246 
GLN   HB3   H N N 247 
GLN   HG2   H N N 248 
GLN   HG3   H N N 249 
GLN   HE21  H N N 250 
GLN   HE22  H N N 251 
GLN   HXT   H N N 252 
GLU   N     N N N 253 
GLU   CA    C N S 254 
GLU   C     C N N 255 
GLU   O     O N N 256 
GLU   CB    C N N 257 
GLU   CG    C N N 258 
GLU   CD    C N N 259 
GLU   OE1   O N N 260 
GLU   OE2   O N N 261 
GLU   OXT   O N N 262 
GLU   H     H N N 263 
GLU   H2    H N N 264 
GLU   HA    H N N 265 
GLU   HB2   H N N 266 
GLU   HB3   H N N 267 
GLU   HG2   H N N 268 
GLU   HG3   H N N 269 
GLU   HE2   H N N 270 
GLU   HXT   H N N 271 
GLY   N     N N N 272 
GLY   CA    C N N 273 
GLY   C     C N N 274 
GLY   O     O N N 275 
GLY   OXT   O N N 276 
GLY   H     H N N 277 
GLY   H2    H N N 278 
GLY   HA2   H N N 279 
GLY   HA3   H N N 280 
GLY   HXT   H N N 281 
HIS   N     N N N 282 
HIS   CA    C N S 283 
HIS   C     C N N 284 
HIS   O     O N N 285 
HIS   CB    C N N 286 
HIS   CG    C Y N 287 
HIS   ND1   N Y N 288 
HIS   CD2   C Y N 289 
HIS   CE1   C Y N 290 
HIS   NE2   N Y N 291 
HIS   OXT   O N N 292 
HIS   H     H N N 293 
HIS   H2    H N N 294 
HIS   HA    H N N 295 
HIS   HB2   H N N 296 
HIS   HB3   H N N 297 
HIS   HD1   H N N 298 
HIS   HD2   H N N 299 
HIS   HE1   H N N 300 
HIS   HE2   H N N 301 
HIS   HXT   H N N 302 
HOH   O     O N N 303 
HOH   H1    H N N 304 
HOH   H2    H N N 305 
ILE   N     N N N 306 
ILE   CA    C N S 307 
ILE   C     C N N 308 
ILE   O     O N N 309 
ILE   CB    C N S 310 
ILE   CG1   C N N 311 
ILE   CG2   C N N 312 
ILE   CD1   C N N 313 
ILE   OXT   O N N 314 
ILE   H     H N N 315 
ILE   H2    H N N 316 
ILE   HA    H N N 317 
ILE   HB    H N N 318 
ILE   HG12  H N N 319 
ILE   HG13  H N N 320 
ILE   HG21  H N N 321 
ILE   HG22  H N N 322 
ILE   HG23  H N N 323 
ILE   HD11  H N N 324 
ILE   HD12  H N N 325 
ILE   HD13  H N N 326 
ILE   HXT   H N N 327 
LEU   N     N N N 328 
LEU   CA    C N S 329 
LEU   C     C N N 330 
LEU   O     O N N 331 
LEU   CB    C N N 332 
LEU   CG    C N N 333 
LEU   CD1   C N N 334 
LEU   CD2   C N N 335 
LEU   OXT   O N N 336 
LEU   H     H N N 337 
LEU   H2    H N N 338 
LEU   HA    H N N 339 
LEU   HB2   H N N 340 
LEU   HB3   H N N 341 
LEU   HG    H N N 342 
LEU   HD11  H N N 343 
LEU   HD12  H N N 344 
LEU   HD13  H N N 345 
LEU   HD21  H N N 346 
LEU   HD22  H N N 347 
LEU   HD23  H N N 348 
LEU   HXT   H N N 349 
LYS   N     N N N 350 
LYS   CA    C N S 351 
LYS   C     C N N 352 
LYS   O     O N N 353 
LYS   CB    C N N 354 
LYS   CG    C N N 355 
LYS   CD    C N N 356 
LYS   CE    C N N 357 
LYS   NZ    N N N 358 
LYS   OXT   O N N 359 
LYS   H     H N N 360 
LYS   H2    H N N 361 
LYS   HA    H N N 362 
LYS   HB2   H N N 363 
LYS   HB3   H N N 364 
LYS   HG2   H N N 365 
LYS   HG3   H N N 366 
LYS   HD2   H N N 367 
LYS   HD3   H N N 368 
LYS   HE2   H N N 369 
LYS   HE3   H N N 370 
LYS   HZ1   H N N 371 
LYS   HZ2   H N N 372 
LYS   HZ3   H N N 373 
LYS   HXT   H N N 374 
MET   N     N N N 375 
MET   CA    C N S 376 
MET   C     C N N 377 
MET   O     O N N 378 
MET   CB    C N N 379 
MET   CG    C N N 380 
MET   SD    S N N 381 
MET   CE    C N N 382 
MET   OXT   O N N 383 
MET   H     H N N 384 
MET   H2    H N N 385 
MET   HA    H N N 386 
MET   HB2   H N N 387 
MET   HB3   H N N 388 
MET   HG2   H N N 389 
MET   HG3   H N N 390 
MET   HE1   H N N 391 
MET   HE2   H N N 392 
MET   HE3   H N N 393 
MET   HXT   H N N 394 
PHE   N     N N N 395 
PHE   CA    C N S 396 
PHE   C     C N N 397 
PHE   O     O N N 398 
PHE   CB    C N N 399 
PHE   CG    C Y N 400 
PHE   CD1   C Y N 401 
PHE   CD2   C Y N 402 
PHE   CE1   C Y N 403 
PHE   CE2   C Y N 404 
PHE   CZ    C Y N 405 
PHE   OXT   O N N 406 
PHE   H     H N N 407 
PHE   H2    H N N 408 
PHE   HA    H N N 409 
PHE   HB2   H N N 410 
PHE   HB3   H N N 411 
PHE   HD1   H N N 412 
PHE   HD2   H N N 413 
PHE   HE1   H N N 414 
PHE   HE2   H N N 415 
PHE   HZ    H N N 416 
PHE   HXT   H N N 417 
PRO   N     N N N 418 
PRO   CA    C N S 419 
PRO   C     C N N 420 
PRO   O     O N N 421 
PRO   CB    C N N 422 
PRO   CG    C N N 423 
PRO   CD    C N N 424 
PRO   OXT   O N N 425 
PRO   H     H N N 426 
PRO   HA    H N N 427 
PRO   HB2   H N N 428 
PRO   HB3   H N N 429 
PRO   HG2   H N N 430 
PRO   HG3   H N N 431 
PRO   HD2   H N N 432 
PRO   HD3   H N N 433 
PRO   HXT   H N N 434 
SER   N     N N N 435 
SER   CA    C N S 436 
SER   C     C N N 437 
SER   O     O N N 438 
SER   CB    C N N 439 
SER   OG    O N N 440 
SER   OXT   O N N 441 
SER   H     H N N 442 
SER   H2    H N N 443 
SER   HA    H N N 444 
SER   HB2   H N N 445 
SER   HB3   H N N 446 
SER   HG    H N N 447 
SER   HXT   H N N 448 
SO4   S     S N N 449 
SO4   O1    O N N 450 
SO4   O2    O N N 451 
SO4   O3    O N N 452 
SO4   O4    O N N 453 
THR   N     N N N 454 
THR   CA    C N S 455 
THR   C     C N N 456 
THR   O     O N N 457 
THR   CB    C N R 458 
THR   OG1   O N N 459 
THR   CG2   C N N 460 
THR   OXT   O N N 461 
THR   H     H N N 462 
THR   H2    H N N 463 
THR   HA    H N N 464 
THR   HB    H N N 465 
THR   HG1   H N N 466 
THR   HG21  H N N 467 
THR   HG22  H N N 468 
THR   HG23  H N N 469 
THR   HXT   H N N 470 
TRP   N     N N N 471 
TRP   CA    C N S 472 
TRP   C     C N N 473 
TRP   O     O N N 474 
TRP   CB    C N N 475 
TRP   CG    C Y N 476 
TRP   CD1   C Y N 477 
TRP   CD2   C Y N 478 
TRP   NE1   N Y N 479 
TRP   CE2   C Y N 480 
TRP   CE3   C Y N 481 
TRP   CZ2   C Y N 482 
TRP   CZ3   C Y N 483 
TRP   CH2   C Y N 484 
TRP   OXT   O N N 485 
TRP   H     H N N 486 
TRP   H2    H N N 487 
TRP   HA    H N N 488 
TRP   HB2   H N N 489 
TRP   HB3   H N N 490 
TRP   HD1   H N N 491 
TRP   HE1   H N N 492 
TRP   HE3   H N N 493 
TRP   HZ2   H N N 494 
TRP   HZ3   H N N 495 
TRP   HH2   H N N 496 
TRP   HXT   H N N 497 
TYR   N     N N N 498 
TYR   CA    C N S 499 
TYR   C     C N N 500 
TYR   O     O N N 501 
TYR   CB    C N N 502 
TYR   CG    C Y N 503 
TYR   CD1   C Y N 504 
TYR   CD2   C Y N 505 
TYR   CE1   C Y N 506 
TYR   CE2   C Y N 507 
TYR   CZ    C Y N 508 
TYR   OH    O N N 509 
TYR   OXT   O N N 510 
TYR   H     H N N 511 
TYR   H2    H N N 512 
TYR   HA    H N N 513 
TYR   HB2   H N N 514 
TYR   HB3   H N N 515 
TYR   HD1   H N N 516 
TYR   HD2   H N N 517 
TYR   HE1   H N N 518 
TYR   HE2   H N N 519 
TYR   HH    H N N 520 
TYR   HXT   H N N 521 
VAL   N     N N N 522 
VAL   CA    C N S 523 
VAL   C     C N N 524 
VAL   O     O N N 525 
VAL   CB    C N N 526 
VAL   CG1   C N N 527 
VAL   CG2   C N N 528 
VAL   OXT   O N N 529 
VAL   H     H N N 530 
VAL   H2    H N N 531 
VAL   HA    H N N 532 
VAL   HB    H N N 533 
VAL   HG11  H N N 534 
VAL   HG12  H N N 535 
VAL   HG13  H N N 536 
VAL   HG21  H N N 537 
VAL   HG22  H N N 538 
VAL   HG23  H N N 539 
VAL   HXT   H N N 540 
# 
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 
A1LZV CBL   CBM   sing N N 1   
A1LZV CBL   CBK   sing N N 2   
A1LZV CBM   CBN   sing N N 3   
A1LZV CBO   CBN   sing N N 4   
A1LZV CBO   CBP   sing N N 5   
A1LZV CBQ   CBP   sing N N 6   
A1LZV CBQ   CBR   sing N N 7   
A1LZV CCE   CCF   sing N N 8   
A1LZV CCE   CCD   sing N N 9   
A1LZV CBK   CBJ   sing N N 10  
A1LZV CCF   CCG   sing N N 11  
A1LZV CBJ   CBI   sing N N 12  
A1LZV CCD   CCC   sing N N 13  
A1LZV CBR   CBS   sing N N 14  
A1LZV CBS   CBT   sing N N 15  
A1LZV CCA   CCB   sing N N 16  
A1LZV CCA   CBZ   sing N N 17  
A1LZV CCG   CCH   sing N N 18  
A1LZV CBI   CBH   sing N N 19  
A1LZV CBH   CBG   sing N N 20  
A1LZV CCB   CCC   sing N N 21  
A1LZV CCI   CCH   sing N N 22  
A1LZV CCI   CCJ   sing N N 23  
A1LZV CBZ   CBY   sing N N 24  
A1LZV CBG   CBF   sing N N 25  
A1LZV CBF   CBE   sing N N 26  
A1LZV CBY   CBX   sing N N 27  
A1LZV CBE   OBD   sing N N 28  
A1LZV CBE   OCL   doub N N 29  
A1LZV CBX   CBW   sing N N 30  
A1LZV OBD   CBC   sing N N 31  
A1LZV CBC   CBA   sing N N 32  
A1LZV CBW   CBV   sing N N 33  
A1LZV OAA   CAB   doub N N 34  
A1LZV CBV   CBU   sing N N 35  
A1LZV OBB   CBU   sing N N 36  
A1LZV OBB   CBA   sing N N 37  
A1LZV CBU   OCK   doub N N 38  
A1LZV CBA   CAZ   sing N N 39  
A1LZV CAB   NAC   sing N N 40  
A1LZV CAB   NAH   sing N N 41  
A1LZV "O3'" "C3'" sing N N 42  
A1LZV NAC   CAD   doub N N 43  
A1LZV "O4'" "C1'" sing N N 44  
A1LZV "O4'" "C4'" sing N N 45  
A1LZV "C1'" NAH   sing N N 46  
A1LZV "C1'" "C2'" sing N N 47  
A1LZV "C4'" "C3'" sing N N 48  
A1LZV "C4'" "C5'" sing N N 49  
A1LZV NAH   CAG   sing N N 50  
A1LZV CAZ   OAY   sing N N 51  
A1LZV "C3'" "C2'" sing N N 52  
A1LZV OAY   PAV   sing N N 53  
A1LZV CAD   NAE   sing N N 54  
A1LZV CAD   CAF   sing N N 55  
A1LZV "O2'" "C2'" sing N N 56  
A1LZV "C5'" "O5'" sing N N 57  
A1LZV CAG   CAF   doub N N 58  
A1LZV "O5'" PAR   sing N N 59  
A1LZV OAX   PAV   doub N N 60  
A1LZV PAV   OAW   sing N N 61  
A1LZV PAV   OAU   sing N N 62  
A1LZV OAU   PAR   sing N N 63  
A1LZV PAR   OAT   doub N N 64  
A1LZV PAR   OAS   sing N N 65  
A1LZV CBF   H1    sing N N 66  
A1LZV CBF   H2    sing N N 67  
A1LZV CBG   H3    sing N N 68  
A1LZV CBG   H4    sing N N 69  
A1LZV CBH   H5    sing N N 70  
A1LZV CBH   H6    sing N N 71  
A1LZV CBI   H7    sing N N 72  
A1LZV CBI   H8    sing N N 73  
A1LZV CBJ   H9    sing N N 74  
A1LZV CBJ   H10   sing N N 75  
A1LZV CBK   H11   sing N N 76  
A1LZV CBK   H12   sing N N 77  
A1LZV CBL   H13   sing N N 78  
A1LZV CBL   H14   sing N N 79  
A1LZV CBM   H15   sing N N 80  
A1LZV CBM   H16   sing N N 81  
A1LZV CBN   H17   sing N N 82  
A1LZV CBN   H18   sing N N 83  
A1LZV CBO   H19   sing N N 84  
A1LZV CBO   H20   sing N N 85  
A1LZV CBP   H21   sing N N 86  
A1LZV CBP   H22   sing N N 87  
A1LZV CBQ   H23   sing N N 88  
A1LZV CBQ   H24   sing N N 89  
A1LZV CBR   H25   sing N N 90  
A1LZV CBR   H26   sing N N 91  
A1LZV CBS   H27   sing N N 92  
A1LZV CBS   H28   sing N N 93  
A1LZV CBT   H29   sing N N 94  
A1LZV CBT   H30   sing N N 95  
A1LZV CBT   H31   sing N N 96  
A1LZV CBC   H32   sing N N 97  
A1LZV CBC   H33   sing N N 98  
A1LZV CBA   H34   sing N N 99  
A1LZV CAZ   H35   sing N N 100 
A1LZV CAZ   H36   sing N N 101 
A1LZV OAW   H37   sing N N 102 
A1LZV OAS   H38   sing N N 103 
A1LZV "C5'" H39   sing N N 104 
A1LZV "C5'" H40   sing N N 105 
A1LZV "C4'" H41   sing N N 106 
A1LZV "C3'" H42   sing N N 107 
A1LZV "O3'" H43   sing N N 108 
A1LZV "C2'" H44   sing N N 109 
A1LZV "O2'" H45   sing N N 110 
A1LZV "C1'" H46   sing N N 111 
A1LZV CAG   H47   sing N N 112 
A1LZV CAF   H48   sing N N 113 
A1LZV NAE   H49   sing N N 114 
A1LZV NAE   H50   sing N N 115 
A1LZV CBV   H51   sing N N 116 
A1LZV CBV   H52   sing N N 117 
A1LZV CBW   H53   sing N N 118 
A1LZV CBW   H54   sing N N 119 
A1LZV CBX   H55   sing N N 120 
A1LZV CBX   H56   sing N N 121 
A1LZV CBY   H57   sing N N 122 
A1LZV CBY   H58   sing N N 123 
A1LZV CBZ   H59   sing N N 124 
A1LZV CBZ   H60   sing N N 125 
A1LZV CCA   H61   sing N N 126 
A1LZV CCA   H62   sing N N 127 
A1LZV CCB   H63   sing N N 128 
A1LZV CCB   H64   sing N N 129 
A1LZV CCC   H65   sing N N 130 
A1LZV CCC   H66   sing N N 131 
A1LZV CCD   H67   sing N N 132 
A1LZV CCD   H68   sing N N 133 
A1LZV CCE   H69   sing N N 134 
A1LZV CCE   H70   sing N N 135 
A1LZV CCF   H71   sing N N 136 
A1LZV CCF   H72   sing N N 137 
A1LZV CCG   H73   sing N N 138 
A1LZV CCG   H74   sing N N 139 
A1LZV CCH   H75   sing N N 140 
A1LZV CCH   H76   sing N N 141 
A1LZV CCI   H77   sing N N 142 
A1LZV CCI   H78   sing N N 143 
A1LZV CCJ   H79   sing N N 144 
A1LZV CCJ   H80   sing N N 145 
A1LZV CCJ   H81   sing N N 146 
ALA   N     CA    sing N N 147 
ALA   N     H     sing N N 148 
ALA   N     H2    sing N N 149 
ALA   CA    C     sing N N 150 
ALA   CA    CB    sing N N 151 
ALA   CA    HA    sing N N 152 
ALA   C     O     doub N N 153 
ALA   C     OXT   sing N N 154 
ALA   CB    HB1   sing N N 155 
ALA   CB    HB2   sing N N 156 
ALA   CB    HB3   sing N N 157 
ALA   OXT   HXT   sing N N 158 
ARG   N     CA    sing N N 159 
ARG   N     H     sing N N 160 
ARG   N     H2    sing N N 161 
ARG   CA    C     sing N N 162 
ARG   CA    CB    sing N N 163 
ARG   CA    HA    sing N N 164 
ARG   C     O     doub N N 165 
ARG   C     OXT   sing N N 166 
ARG   CB    CG    sing N N 167 
ARG   CB    HB2   sing N N 168 
ARG   CB    HB3   sing N N 169 
ARG   CG    CD    sing N N 170 
ARG   CG    HG2   sing N N 171 
ARG   CG    HG3   sing N N 172 
ARG   CD    NE    sing N N 173 
ARG   CD    HD2   sing N N 174 
ARG   CD    HD3   sing N N 175 
ARG   NE    CZ    sing N N 176 
ARG   NE    HE    sing N N 177 
ARG   CZ    NH1   sing N N 178 
ARG   CZ    NH2   doub N N 179 
ARG   NH1   HH11  sing N N 180 
ARG   NH1   HH12  sing N N 181 
ARG   NH2   HH21  sing N N 182 
ARG   NH2   HH22  sing N N 183 
ARG   OXT   HXT   sing N N 184 
ASN   N     CA    sing N N 185 
ASN   N     H     sing N N 186 
ASN   N     H2    sing N N 187 
ASN   CA    C     sing N N 188 
ASN   CA    CB    sing N N 189 
ASN   CA    HA    sing N N 190 
ASN   C     O     doub N N 191 
ASN   C     OXT   sing N N 192 
ASN   CB    CG    sing N N 193 
ASN   CB    HB2   sing N N 194 
ASN   CB    HB3   sing N N 195 
ASN   CG    OD1   doub N N 196 
ASN   CG    ND2   sing N N 197 
ASN   ND2   HD21  sing N N 198 
ASN   ND2   HD22  sing N N 199 
ASN   OXT   HXT   sing N N 200 
ASP   N     CA    sing N N 201 
ASP   N     H     sing N N 202 
ASP   N     H2    sing N N 203 
ASP   CA    C     sing N N 204 
ASP   CA    CB    sing N N 205 
ASP   CA    HA    sing N N 206 
ASP   C     O     doub N N 207 
ASP   C     OXT   sing N N 208 
ASP   CB    CG    sing N N 209 
ASP   CB    HB2   sing N N 210 
ASP   CB    HB3   sing N N 211 
ASP   CG    OD1   doub N N 212 
ASP   CG    OD2   sing N N 213 
ASP   OD2   HD2   sing N N 214 
ASP   OXT   HXT   sing N N 215 
CYS   N     CA    sing N N 216 
CYS   N     H     sing N N 217 
CYS   N     H2    sing N N 218 
CYS   CA    C     sing N N 219 
CYS   CA    CB    sing N N 220 
CYS   CA    HA    sing N N 221 
CYS   C     O     doub N N 222 
CYS   C     OXT   sing N N 223 
CYS   CB    SG    sing N N 224 
CYS   CB    HB2   sing N N 225 
CYS   CB    HB3   sing N N 226 
CYS   SG    HG    sing N N 227 
CYS   OXT   HXT   sing N N 228 
GLN   N     CA    sing N N 229 
GLN   N     H     sing N N 230 
GLN   N     H2    sing N N 231 
GLN   CA    C     sing N N 232 
GLN   CA    CB    sing N N 233 
GLN   CA    HA    sing N N 234 
GLN   C     O     doub N N 235 
GLN   C     OXT   sing N N 236 
GLN   CB    CG    sing N N 237 
GLN   CB    HB2   sing N N 238 
GLN   CB    HB3   sing N N 239 
GLN   CG    CD    sing N N 240 
GLN   CG    HG2   sing N N 241 
GLN   CG    HG3   sing N N 242 
GLN   CD    OE1   doub N N 243 
GLN   CD    NE2   sing N N 244 
GLN   NE2   HE21  sing N N 245 
GLN   NE2   HE22  sing N N 246 
GLN   OXT   HXT   sing N N 247 
GLU   N     CA    sing N N 248 
GLU   N     H     sing N N 249 
GLU   N     H2    sing N N 250 
GLU   CA    C     sing N N 251 
GLU   CA    CB    sing N N 252 
GLU   CA    HA    sing N N 253 
GLU   C     O     doub N N 254 
GLU   C     OXT   sing N N 255 
GLU   CB    CG    sing N N 256 
GLU   CB    HB2   sing N N 257 
GLU   CB    HB3   sing N N 258 
GLU   CG    CD    sing N N 259 
GLU   CG    HG2   sing N N 260 
GLU   CG    HG3   sing N N 261 
GLU   CD    OE1   doub N N 262 
GLU   CD    OE2   sing N N 263 
GLU   OE2   HE2   sing N N 264 
GLU   OXT   HXT   sing N N 265 
GLY   N     CA    sing N N 266 
GLY   N     H     sing N N 267 
GLY   N     H2    sing N N 268 
GLY   CA    C     sing N N 269 
GLY   CA    HA2   sing N N 270 
GLY   CA    HA3   sing N N 271 
GLY   C     O     doub N N 272 
GLY   C     OXT   sing N N 273 
GLY   OXT   HXT   sing N N 274 
HIS   N     CA    sing N N 275 
HIS   N     H     sing N N 276 
HIS   N     H2    sing N N 277 
HIS   CA    C     sing N N 278 
HIS   CA    CB    sing N N 279 
HIS   CA    HA    sing N N 280 
HIS   C     O     doub N N 281 
HIS   C     OXT   sing N N 282 
HIS   CB    CG    sing N N 283 
HIS   CB    HB2   sing N N 284 
HIS   CB    HB3   sing N N 285 
HIS   CG    ND1   sing Y N 286 
HIS   CG    CD2   doub Y N 287 
HIS   ND1   CE1   doub Y N 288 
HIS   ND1   HD1   sing N N 289 
HIS   CD2   NE2   sing Y N 290 
HIS   CD2   HD2   sing N N 291 
HIS   CE1   NE2   sing Y N 292 
HIS   CE1   HE1   sing N N 293 
HIS   NE2   HE2   sing N N 294 
HIS   OXT   HXT   sing N N 295 
HOH   O     H1    sing N N 296 
HOH   O     H2    sing N N 297 
ILE   N     CA    sing N N 298 
ILE   N     H     sing N N 299 
ILE   N     H2    sing N N 300 
ILE   CA    C     sing N N 301 
ILE   CA    CB    sing N N 302 
ILE   CA    HA    sing N N 303 
ILE   C     O     doub N N 304 
ILE   C     OXT   sing N N 305 
ILE   CB    CG1   sing N N 306 
ILE   CB    CG2   sing N N 307 
ILE   CB    HB    sing N N 308 
ILE   CG1   CD1   sing N N 309 
ILE   CG1   HG12  sing N N 310 
ILE   CG1   HG13  sing N N 311 
ILE   CG2   HG21  sing N N 312 
ILE   CG2   HG22  sing N N 313 
ILE   CG2   HG23  sing N N 314 
ILE   CD1   HD11  sing N N 315 
ILE   CD1   HD12  sing N N 316 
ILE   CD1   HD13  sing N N 317 
ILE   OXT   HXT   sing N N 318 
LEU   N     CA    sing N N 319 
LEU   N     H     sing N N 320 
LEU   N     H2    sing N N 321 
LEU   CA    C     sing N N 322 
LEU   CA    CB    sing N N 323 
LEU   CA    HA    sing N N 324 
LEU   C     O     doub N N 325 
LEU   C     OXT   sing N N 326 
LEU   CB    CG    sing N N 327 
LEU   CB    HB2   sing N N 328 
LEU   CB    HB3   sing N N 329 
LEU   CG    CD1   sing N N 330 
LEU   CG    CD2   sing N N 331 
LEU   CG    HG    sing N N 332 
LEU   CD1   HD11  sing N N 333 
LEU   CD1   HD12  sing N N 334 
LEU   CD1   HD13  sing N N 335 
LEU   CD2   HD21  sing N N 336 
LEU   CD2   HD22  sing N N 337 
LEU   CD2   HD23  sing N N 338 
LEU   OXT   HXT   sing N N 339 
LYS   N     CA    sing N N 340 
LYS   N     H     sing N N 341 
LYS   N     H2    sing N N 342 
LYS   CA    C     sing N N 343 
LYS   CA    CB    sing N N 344 
LYS   CA    HA    sing N N 345 
LYS   C     O     doub N N 346 
LYS   C     OXT   sing N N 347 
LYS   CB    CG    sing N N 348 
LYS   CB    HB2   sing N N 349 
LYS   CB    HB3   sing N N 350 
LYS   CG    CD    sing N N 351 
LYS   CG    HG2   sing N N 352 
LYS   CG    HG3   sing N N 353 
LYS   CD    CE    sing N N 354 
LYS   CD    HD2   sing N N 355 
LYS   CD    HD3   sing N N 356 
LYS   CE    NZ    sing N N 357 
LYS   CE    HE2   sing N N 358 
LYS   CE    HE3   sing N N 359 
LYS   NZ    HZ1   sing N N 360 
LYS   NZ    HZ2   sing N N 361 
LYS   NZ    HZ3   sing N N 362 
LYS   OXT   HXT   sing N N 363 
MET   N     CA    sing N N 364 
MET   N     H     sing N N 365 
MET   N     H2    sing N N 366 
MET   CA    C     sing N N 367 
MET   CA    CB    sing N N 368 
MET   CA    HA    sing N N 369 
MET   C     O     doub N N 370 
MET   C     OXT   sing N N 371 
MET   CB    CG    sing N N 372 
MET   CB    HB2   sing N N 373 
MET   CB    HB3   sing N N 374 
MET   CG    SD    sing N N 375 
MET   CG    HG2   sing N N 376 
MET   CG    HG3   sing N N 377 
MET   SD    CE    sing N N 378 
MET   CE    HE1   sing N N 379 
MET   CE    HE2   sing N N 380 
MET   CE    HE3   sing N N 381 
MET   OXT   HXT   sing N N 382 
PHE   N     CA    sing N N 383 
PHE   N     H     sing N N 384 
PHE   N     H2    sing N N 385 
PHE   CA    C     sing N N 386 
PHE   CA    CB    sing N N 387 
PHE   CA    HA    sing N N 388 
PHE   C     O     doub N N 389 
PHE   C     OXT   sing N N 390 
PHE   CB    CG    sing N N 391 
PHE   CB    HB2   sing N N 392 
PHE   CB    HB3   sing N N 393 
PHE   CG    CD1   doub Y N 394 
PHE   CG    CD2   sing Y N 395 
PHE   CD1   CE1   sing Y N 396 
PHE   CD1   HD1   sing N N 397 
PHE   CD2   CE2   doub Y N 398 
PHE   CD2   HD2   sing N N 399 
PHE   CE1   CZ    doub Y N 400 
PHE   CE1   HE1   sing N N 401 
PHE   CE2   CZ    sing Y N 402 
PHE   CE2   HE2   sing N N 403 
PHE   CZ    HZ    sing N N 404 
PHE   OXT   HXT   sing N N 405 
PRO   N     CA    sing N N 406 
PRO   N     CD    sing N N 407 
PRO   N     H     sing N N 408 
PRO   CA    C     sing N N 409 
PRO   CA    CB    sing N N 410 
PRO   CA    HA    sing N N 411 
PRO   C     O     doub N N 412 
PRO   C     OXT   sing N N 413 
PRO   CB    CG    sing N N 414 
PRO   CB    HB2   sing N N 415 
PRO   CB    HB3   sing N N 416 
PRO   CG    CD    sing N N 417 
PRO   CG    HG2   sing N N 418 
PRO   CG    HG3   sing N N 419 
PRO   CD    HD2   sing N N 420 
PRO   CD    HD3   sing N N 421 
PRO   OXT   HXT   sing N N 422 
SER   N     CA    sing N N 423 
SER   N     H     sing N N 424 
SER   N     H2    sing N N 425 
SER   CA    C     sing N N 426 
SER   CA    CB    sing N N 427 
SER   CA    HA    sing N N 428 
SER   C     O     doub N N 429 
SER   C     OXT   sing N N 430 
SER   CB    OG    sing N N 431 
SER   CB    HB2   sing N N 432 
SER   CB    HB3   sing N N 433 
SER   OG    HG    sing N N 434 
SER   OXT   HXT   sing N N 435 
SO4   S     O1    doub N N 436 
SO4   S     O2    doub N N 437 
SO4   S     O3    sing N N 438 
SO4   S     O4    sing N N 439 
THR   N     CA    sing N N 440 
THR   N     H     sing N N 441 
THR   N     H2    sing N N 442 
THR   CA    C     sing N N 443 
THR   CA    CB    sing N N 444 
THR   CA    HA    sing N N 445 
THR   C     O     doub N N 446 
THR   C     OXT   sing N N 447 
THR   CB    OG1   sing N N 448 
THR   CB    CG2   sing N N 449 
THR   CB    HB    sing N N 450 
THR   OG1   HG1   sing N N 451 
THR   CG2   HG21  sing N N 452 
THR   CG2   HG22  sing N N 453 
THR   CG2   HG23  sing N N 454 
THR   OXT   HXT   sing N N 455 
TRP   N     CA    sing N N 456 
TRP   N     H     sing N N 457 
TRP   N     H2    sing N N 458 
TRP   CA    C     sing N N 459 
TRP   CA    CB    sing N N 460 
TRP   CA    HA    sing N N 461 
TRP   C     O     doub N N 462 
TRP   C     OXT   sing N N 463 
TRP   CB    CG    sing N N 464 
TRP   CB    HB2   sing N N 465 
TRP   CB    HB3   sing N N 466 
TRP   CG    CD1   doub Y N 467 
TRP   CG    CD2   sing Y N 468 
TRP   CD1   NE1   sing Y N 469 
TRP   CD1   HD1   sing N N 470 
TRP   CD2   CE2   doub Y N 471 
TRP   CD2   CE3   sing Y N 472 
TRP   NE1   CE2   sing Y N 473 
TRP   NE1   HE1   sing N N 474 
TRP   CE2   CZ2   sing Y N 475 
TRP   CE3   CZ3   doub Y N 476 
TRP   CE3   HE3   sing N N 477 
TRP   CZ2   CH2   doub Y N 478 
TRP   CZ2   HZ2   sing N N 479 
TRP   CZ3   CH2   sing Y N 480 
TRP   CZ3   HZ3   sing N N 481 
TRP   CH2   HH2   sing N N 482 
TRP   OXT   HXT   sing N N 483 
TYR   N     CA    sing N N 484 
TYR   N     H     sing N N 485 
TYR   N     H2    sing N N 486 
TYR   CA    C     sing N N 487 
TYR   CA    CB    sing N N 488 
TYR   CA    HA    sing N N 489 
TYR   C     O     doub N N 490 
TYR   C     OXT   sing N N 491 
TYR   CB    CG    sing N N 492 
TYR   CB    HB2   sing N N 493 
TYR   CB    HB3   sing N N 494 
TYR   CG    CD1   doub Y N 495 
TYR   CG    CD2   sing Y N 496 
TYR   CD1   CE1   sing Y N 497 
TYR   CD1   HD1   sing N N 498 
TYR   CD2   CE2   doub Y N 499 
TYR   CD2   HD2   sing N N 500 
TYR   CE1   CZ    doub Y N 501 
TYR   CE1   HE1   sing N N 502 
TYR   CE2   CZ    sing Y N 503 
TYR   CE2   HE2   sing N N 504 
TYR   CZ    OH    sing N N 505 
TYR   OH    HH    sing N N 506 
TYR   OXT   HXT   sing N N 507 
VAL   N     CA    sing N N 508 
VAL   N     H     sing N N 509 
VAL   N     H2    sing N N 510 
VAL   CA    C     sing N N 511 
VAL   CA    CB    sing N N 512 
VAL   CA    HA    sing N N 513 
VAL   C     O     doub N N 514 
VAL   C     OXT   sing N N 515 
VAL   CB    CG1   sing N N 516 
VAL   CB    CG2   sing N N 517 
VAL   CB    HB    sing N N 518 
VAL   CG1   HG11  sing N N 519 
VAL   CG1   HG12  sing N N 520 
VAL   CG1   HG13  sing N N 521 
VAL   CG2   HG21  sing N N 522 
VAL   CG2   HG22  sing N N 523 
VAL   CG2   HG23  sing N N 524 
VAL   OXT   HXT   sing N N 525 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Korea)' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-P23830-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YR6 
_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]   0.006231 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006231 
_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]   0.006231 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
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     . ASN   A 1 18  ? 62.507 10.141  50.189 1.00 89.75  ? 8   ASN   A N     1 
ATOM   2    C CA    . ASN   A 1 18  ? 61.168 9.486   50.192 1.00 87.76  ? 8   ASN   A CA    1 
ATOM   3    C C     . ASN   A 1 18  ? 60.215 10.328  49.344 1.00 86.98  ? 8   ASN   A C     1 
ATOM   4    O O     . ASN   A 1 18  ? 59.941 11.476  49.680 1.00 88.92  ? 8   ASN   A O     1 
ATOM   5    C CB    . ASN   A 1 18  ? 60.674 9.281   51.621 1.00 85.57  ? 8   ASN   A CB    1 
ATOM   6    C CG    . ASN   A 1 18  ? 59.396 8.479   51.682 1.00 84.19  ? 8   ASN   A CG    1 
ATOM   7    O OD1   . ASN   A 1 18  ? 58.379 8.887   51.111 1.00 82.71  ? 8   ASN   A OD1   1 
ATOM   8    N ND2   . ASN   A 1 18  ? 59.420 7.345   52.367 1.00 83.50  ? 8   ASN   A ND2   1 
ATOM   9    N N     . LYS   A 1 19  ? 59.711 9.749   48.248 1.00 85.22  ? 9   LYS   A N     1 
ATOM   10   C CA    . LYS   A 1 19  ? 58.934 10.500  47.274 1.00 85.72  ? 9   LYS   A CA    1 
ATOM   11   C C     . LYS   A 1 19  ? 57.557 10.853  47.841 1.00 82.72  ? 9   LYS   A C     1 
ATOM   12   O O     . LYS   A 1 19  ? 57.001 11.897  47.500 1.00 80.24  ? 9   LYS   A O     1 
ATOM   13   C CB    . LYS   A 1 19  ? 58.829 9.717   45.960 1.00 88.77  ? 9   LYS   A CB    1 
ATOM   14   C CG    . LYS   A 1 19  ? 58.348 10.531  44.762 1.00 92.74  ? 9   LYS   A CG    1 
ATOM   15   C CD    . LYS   A 1 19  ? 58.373 9.771   43.439 1.00 95.55  ? 9   LYS   A CD    1 
ATOM   16   C CE    . LYS   A 1 19  ? 57.825 10.553  42.280 1.00 96.92  ? 9   LYS   A CE    1 
ATOM   17   N NZ    . LYS   A 1 19  ? 56.387 10.811  42.413 1.00 97.40  ? 9   LYS   A NZ    1 
ATOM   18   N N     . HIS   A 1 20  ? 57.016 9.986   48.710 1.00 79.06  ? 10  HIS   A N     1 
ATOM   19   C CA    . HIS   A 1 20  ? 55.691 10.188  49.281 1.00 75.01  ? 10  HIS   A CA    1 
ATOM   20   C C     . HIS   A 1 20  ? 55.706 11.358  50.260 1.00 71.89  ? 10  HIS   A C     1 
ATOM   21   O O     . HIS   A 1 20  ? 54.813 12.202  50.225 1.00 66.78  ? 10  HIS   A O     1 
ATOM   22   C CB    . HIS   A 1 20  ? 55.183 8.923   49.979 1.00 72.21  ? 10  HIS   A CB    1 
ATOM   23   C CG    . HIS   A 1 20  ? 55.122 7.715   49.107 1.00 69.75  ? 10  HIS   A CG    1 
ATOM   24   N ND1   . HIS   A 1 20  ? 54.197 7.572   48.096 1.00 67.76  ? 10  HIS   A ND1   1 
ATOM   25   C CD2   . HIS   A 1 20  ? 55.867 6.602   49.091 1.00 69.06  ? 10  HIS   A CD2   1 
ATOM   26   C CE1   . HIS   A 1 20  ? 54.378 6.401   47.501 1.00 69.13  ? 10  HIS   A CE1   1 
ATOM   27   N NE2   . HIS   A 1 20  ? 55.385 5.793   48.091 1.00 69.33  ? 10  HIS   A NE2   1 
ATOM   28   N N     . GLN   A 1 21  ? 56.727 11.389  51.128 1.00 73.82  ? 11  GLN   A N     1 
ATOM   29   C CA    . GLN   A 1 21  ? 56.900 12.447  52.114 1.00 77.28  ? 11  GLN   A CA    1 
ATOM   30   C C     . GLN   A 1 21  ? 57.165 13.785  51.429 1.00 78.07  ? 11  GLN   A C     1 
ATOM   31   O O     . GLN   A 1 21  ? 56.758 14.832  51.930 1.00 77.72  ? 11  GLN   A O     1 
ATOM   32   C CB    . GLN   A 1 21  ? 58.032 12.098  53.080 1.00 78.65  ? 11  GLN   A CB    1 
ATOM   33   C CG    . GLN   A 1 21  ? 57.618 11.096  54.151 1.00 82.74  ? 11  GLN   A CG    1 
ATOM   34   C CD    . GLN   A 1 21  ? 58.780 10.513  54.923 1.00 87.25  ? 11  GLN   A CD    1 
ATOM   35   O OE1   . GLN   A 1 21  ? 59.954 10.714  54.588 1.00 87.56  ? 11  GLN   A OE1   1 
ATOM   36   N NE2   . GLN   A 1 21  ? 58.453 9.760   55.964 1.00 90.45  ? 11  GLN   A NE2   1 
ATOM   37   N N     . GLN   A 1 22  ? 57.848 13.734  50.282 1.00 78.82  ? 12  GLN   A N     1 
ATOM   38   C CA    . GLN   A 1 22  ? 58.167 14.922  49.514 1.00 79.24  ? 12  GLN   A CA    1 
ATOM   39   C C     . GLN   A 1 22  ? 56.870 15.544  48.997 1.00 76.10  ? 12  GLN   A C     1 
ATOM   40   O O     . GLN   A 1 22  ? 56.675 16.750  49.121 1.00 74.95  ? 12  GLN   A O     1 
ATOM   41   C CB    . GLN   A 1 22  ? 59.152 14.525  48.414 1.00 82.98  ? 12  GLN   A CB    1 
ATOM   42   C CG    . GLN   A 1 22  ? 59.991 15.672  47.863 1.00 84.87  ? 12  GLN   A CG    1 
ATOM   43   C CD    . GLN   A 1 22  ? 60.915 15.227  46.749 1.00 88.23  ? 12  GLN   A CD    1 
ATOM   44   O OE1   . GLN   A 1 22  ? 60.492 14.559  45.798 1.00 88.53  ? 12  GLN   A OE1   1 
ATOM   45   N NE2   . GLN   A 1 22  ? 62.192 15.568  46.861 1.00 90.56  ? 12  GLN   A NE2   1 
ATOM   46   N N     . HIS   A 1 23  ? 55.979 14.713  48.441 1.00 74.18  ? 13  HIS   A N     1 
ATOM   47   C CA    . HIS   A 1 23  ? 54.686 15.179  47.965 1.00 74.11  ? 13  HIS   A CA    1 
ATOM   48   C C     . HIS   A 1 23  ? 53.986 15.978  49.063 1.00 72.26  ? 13  HIS   A C     1 
ATOM   49   O O     . HIS   A 1 23  ? 53.525 17.091  48.818 1.00 73.06  ? 13  HIS   A O     1 
ATOM   50   C CB    . HIS   A 1 23  ? 53.817 14.008  47.494 1.00 78.32  ? 13  HIS   A CB    1 
ATOM   51   C CG    . HIS   A 1 23  ? 52.475 14.410  46.961 1.00 83.10  ? 13  HIS   A CG    1 
ATOM   52   N ND1   . HIS   A 1 23  ? 51.339 14.471  47.743 1.00 83.34  ? 13  HIS   A ND1   1 
ATOM   53   C CD2   . HIS   A 1 23  ? 52.087 14.752  45.720 1.00 85.38  ? 13  HIS   A CD2   1 
ATOM   54   C CE1   . HIS   A 1 23  ? 50.308 14.839  46.994 1.00 83.34  ? 13  HIS   A CE1   1 
ATOM   55   N NE2   . HIS   A 1 23  ? 50.739 15.015  45.762 1.00 86.28  ? 13  HIS   A NE2   1 
ATOM   56   N N     . LEU   A 1 24  ? 53.920 15.402  50.271 1.00 68.52  ? 14  LEU   A N     1 
ATOM   57   C CA    . LEU   A 1 24  ? 53.236 16.031  51.390 1.00 65.65  ? 14  LEU   A CA    1 
ATOM   58   C C     . LEU   A 1 24  ? 53.959 17.309  51.804 1.00 62.37  ? 14  LEU   A C     1 
ATOM   59   O O     . LEU   A 1 24  ? 53.316 18.298  52.132 1.00 60.80  ? 14  LEU   A O     1 
ATOM   60   C CB    . LEU   A 1 24  ? 53.121 15.075  52.575 1.00 65.99  ? 14  LEU   A CB    1 
ATOM   61   C CG    . LEU   A 1 24  ? 52.120 13.925  52.434 1.00 66.11  ? 14  LEU   A CG    1 
ATOM   62   C CD1   . LEU   A 1 24  ? 52.147 13.126  53.719 1.00 66.51  ? 14  LEU   A CD1   1 
ATOM   63   C CD2   . LEU   A 1 24  ? 50.709 14.395  52.137 1.00 66.44  ? 14  LEU   A CD2   1 
ATOM   64   N N     . ALA   A 1 25  ? 55.294 17.272  51.809 1.00 61.23  ? 15  ALA   A N     1 
ATOM   65   C CA    . ALA   A 1 25  ? 56.091 18.416  52.215 1.00 60.78  ? 15  ALA   A CA    1 
ATOM   66   C C     . ALA   A 1 25  ? 55.869 19.589  51.259 1.00 62.17  ? 15  ALA   A C     1 
ATOM   67   O O     . ALA   A 1 25  ? 55.918 20.746  51.673 1.00 61.12  ? 15  ALA   A O     1 
ATOM   68   C CB    . ALA   A 1 25  ? 57.550 18.019  52.289 1.00 59.85  ? 15  ALA   A CB    1 
ATOM   69   N N     . GLN   A 1 26  ? 55.591 19.276  49.988 1.00 64.95  ? 16  GLN   A N     1 
ATOM   70   C CA    . GLN   A 1 26  ? 55.512 20.274  48.935 1.00 67.48  ? 16  GLN   A CA    1 
ATOM   71   C C     . GLN   A 1 26  ? 54.072 20.707  48.668 1.00 67.47  ? 16  GLN   A C     1 
ATOM   72   O O     . GLN   A 1 26  ? 53.865 21.672  47.935 1.00 68.76  ? 16  GLN   A O     1 
ATOM   73   C CB    . GLN   A 1 26  ? 56.158 19.717  47.667 1.00 69.58  ? 16  GLN   A CB    1 
ATOM   74   C CG    . GLN   A 1 26  ? 57.673 19.573  47.773 1.00 71.86  ? 16  GLN   A CG    1 
ATOM   75   C CD    . GLN   A 1 26  ? 58.289 18.822  46.612 1.00 74.11  ? 16  GLN   A CD    1 
ATOM   76   O OE1   . GLN   A 1 26  ? 57.592 18.368  45.695 1.00 74.92  ? 16  GLN   A OE1   1 
ATOM   77   N NE2   . GLN   A 1 26  ? 59.609 18.688  46.640 1.00 74.63  ? 16  GLN   A NE2   1 
ATOM   78   N N     . LEU   A 1 27  ? 53.086 19.999  49.239 1.00 67.61  ? 17  LEU   A N     1 
ATOM   79   C CA    . LEU   A 1 27  ? 51.702 20.449  49.179 1.00 67.87  ? 17  LEU   A CA    1 
ATOM   80   C C     . LEU   A 1 27  ? 51.642 21.883  49.698 1.00 66.94  ? 17  LEU   A C     1 
ATOM   81   O O     . LEU   A 1 27  ? 52.190 22.168  50.761 1.00 66.22  ? 17  LEU   A O     1 
ATOM   82   C CB    . LEU   A 1 27  ? 50.744 19.579  49.996 1.00 69.08  ? 17  LEU   A CB    1 
ATOM   83   C CG    . LEU   A 1 27  ? 49.984 18.470  49.261 1.00 69.55  ? 17  LEU   A CG    1 
ATOM   84   C CD1   . LEU   A 1 27  ? 49.079 17.778  50.265 1.00 70.26  ? 17  LEU   A CD1   1 
ATOM   85   C CD2   . LEU   A 1 27  ? 49.165 18.960  48.082 1.00 69.37  ? 17  LEU   A CD2   1 
ATOM   86   N N     . PRO   A 1 28  ? 50.969 22.818  48.989 1.00 65.17  ? 18  PRO   A N     1 
ATOM   87   C CA    . PRO   A 1 28  ? 50.709 24.148  49.546 1.00 65.12  ? 18  PRO   A CA    1 
ATOM   88   C C     . PRO   A 1 28  ? 49.891 24.046  50.833 1.00 65.34  ? 18  PRO   A C     1 
ATOM   89   O O     . PRO   A 1 28  ? 48.977 23.225  50.922 1.00 65.14  ? 18  PRO   A O     1 
ATOM   90   C CB    . PRO   A 1 28  ? 49.961 24.877  48.415 1.00 64.91  ? 18  PRO   A CB    1 
ATOM   91   C CG    . PRO   A 1 28  ? 49.384 23.759  47.570 1.00 65.99  ? 18  PRO   A CG    1 
ATOM   92   C CD    . PRO   A 1 28  ? 50.421 22.650  47.633 1.00 66.08  ? 18  PRO   A CD    1 
ATOM   93   N N     . LYS   A 1 29  ? 50.238 24.880  51.823 1.00 64.28  ? 19  LYS   A N     1 
ATOM   94   C CA    . LYS   A 1 29  ? 49.655 24.790  53.153 1.00 64.44  ? 19  LYS   A CA    1 
ATOM   95   C C     . LYS   A 1 29  ? 49.270 26.174  53.662 1.00 65.77  ? 19  LYS   A C     1 
ATOM   96   O O     . LYS   A 1 29  ? 50.072 27.102  53.604 1.00 67.21  ? 19  LYS   A O     1 
ATOM   97   C CB    . LYS   A 1 29  ? 50.641 24.135  54.121 1.00 63.53  ? 19  LYS   A CB    1 
ATOM   98   C CG    . LYS   A 1 29  ? 50.945 22.706  53.743 1.00 63.90  ? 19  LYS   A CG    1 
ATOM   99   C CD    . LYS   A 1 29  ? 51.726 21.917  54.782 1.00 63.67  ? 19  LYS   A CD    1 
ATOM   100  C CE    . LYS   A 1 29  ? 52.076 20.567  54.245 1.00 63.93  ? 19  LYS   A CE    1 
ATOM   101  N NZ    . LYS   A 1 29  ? 52.894 20.648  53.029 1.00 63.85  ? 19  LYS   A NZ    1 
ATOM   102  N N     . ILE   A 1 30  ? 48.041 26.276  54.187 1.00 65.52  ? 20  ILE   A N     1 
ATOM   103  C CA    . ILE   A 1 30  ? 47.522 27.518  54.734 1.00 63.96  ? 20  ILE   A CA    1 
ATOM   104  C C     . ILE   A 1 30  ? 47.648 27.467  56.254 1.00 63.74  ? 20  ILE   A C     1 
ATOM   105  O O     . ILE   A 1 30  ? 47.153 26.536  56.884 1.00 63.11  ? 20  ILE   A O     1 
ATOM   106  C CB    . ILE   A 1 30  ? 46.064 27.733  54.292 1.00 62.92  ? 20  ILE   A CB    1 
ATOM   107  C CG1   . ILE   A 1 30  ? 45.918 27.629  52.772 1.00 62.97  ? 20  ILE   A CG1   1 
ATOM   108  C CG2   . ILE   A 1 30  ? 45.526 29.060  54.831 1.00 62.29  ? 20  ILE   A CG2   1 
ATOM   109  C CD1   . ILE   A 1 30  ? 44.488 27.441  52.301 1.00 63.31  ? 20  ILE   A CD1   1 
ATOM   110  N N     . SER   A 1 31  ? 48.294 28.485  56.836 1.00 63.62  ? 21  SER   A N     1 
ATOM   111  C CA    . SER   A 1 31  ? 48.496 28.527  58.275 1.00 64.16  ? 21  SER   A CA    1 
ATOM   112  C C     . SER   A 1 31  ? 47.145 28.574  58.980 1.00 62.22  ? 21  SER   A C     1 
ATOM   113  O O     . SER   A 1 31  ? 46.190 29.176  58.493 1.00 60.88  ? 21  SER   A O     1 
ATOM   114  C CB    . SER   A 1 31  ? 49.378 29.675  58.695 1.00 65.29  ? 21  SER   A CB    1 
ATOM   115  O OG    . SER   A 1 31  ? 48.927 30.889  58.121 1.00 68.12  ? 21  SER   A OG    1 
ATOM   116  N N     . GLN   A 1 32  ? 47.095 27.901  60.130 1.00 60.43  ? 22  GLN   A N     1 
ATOM   117  C CA    . GLN   A 1 32  ? 45.871 27.708  60.879 1.00 59.10  ? 22  GLN   A CA    1 
ATOM   118  C C     . GLN   A 1 32  ? 46.188 27.920  62.351 1.00 58.50  ? 22  GLN   A C     1 
ATOM   119  O O     . GLN   A 1 32  ? 47.173 27.382  62.850 1.00 57.87  ? 22  GLN   A O     1 
ATOM   120  C CB    . GLN   A 1 32  ? 45.363 26.286  60.644 1.00 59.47  ? 22  GLN   A CB    1 
ATOM   121  C CG    . GLN   A 1 32  ? 44.053 25.962  61.352 1.00 58.89  ? 22  GLN   A CG    1 
ATOM   122  C CD    . GLN   A 1 32  ? 42.930 26.875  60.917 1.00 58.14  ? 22  GLN   A CD    1 
ATOM   123  O OE1   . GLN   A 1 32  ? 42.664 27.025  59.720 1.00 57.01  ? 22  GLN   A OE1   1 
ATOM   124  N NE2   . GLN   A 1 32  ? 42.283 27.515  61.881 1.00 58.00  ? 22  GLN   A NE2   1 
ATOM   125  N N     . SER   A 1 33  ? 45.362 28.724  63.024 1.00 60.09  ? 23  SER   A N     1 
ATOM   126  C CA    . SER   A 1 33  ? 45.488 28.915  64.457 1.00 60.76  ? 23  SER   A CA    1 
ATOM   127  C C     . SER   A 1 33  ? 44.703 27.824  65.176 1.00 60.90  ? 23  SER   A C     1 
ATOM   128  O O     . SER   A 1 33  ? 43.567 27.538  64.812 1.00 62.55  ? 23  SER   A O     1 
ATOM   129  C CB    . SER   A 1 33  ? 45.018 30.276  64.869 1.00 60.59  ? 23  SER   A CB    1 
ATOM   130  O OG    . SER   A 1 33  ? 44.922 30.345  66.285 1.00 63.70  ? 23  SER   A OG    1 
ATOM   131  N N     . VAL   A 1 34  ? 45.316 27.238  66.209 1.00 61.47  ? 24  VAL   A N     1 
ATOM   132  C CA    . VAL   A 1 34  ? 44.687 26.186  66.993 1.00 63.13  ? 24  VAL   A CA    1 
ATOM   133  C C     . VAL   A 1 34  ? 43.351 26.671  67.564 1.00 62.75  ? 24  VAL   A C     1 
ATOM   134  O O     . VAL   A 1 34  ? 42.427 25.876  67.704 1.00 61.88  ? 24  VAL   A O     1 
ATOM   135  C CB    . VAL   A 1 34  ? 45.638 25.695  68.106 1.00 64.66  ? 24  VAL   A CB    1 
ATOM   136  C CG1   . VAL   A 1 34  ? 45.917 26.772  69.151 1.00 64.75  ? 24  VAL   A CG1   1 
ATOM   137  C CG2   . VAL   A 1 34  ? 45.129 24.420  68.774 1.00 64.39  ? 24  VAL   A CG2   1 
ATOM   138  N N     . ASP   A 1 35  ? 43.247 27.970  67.884 1.00 63.63  ? 25  ASP   A N     1 
ATOM   139  C CA    . ASP   A 1 35  ? 42.060 28.516  68.527 1.00 65.63  ? 25  ASP   A CA    1 
ATOM   140  C C     . ASP   A 1 35  ? 40.917 28.703  67.532 1.00 62.86  ? 25  ASP   A C     1 
ATOM   141  O O     . ASP   A 1 35  ? 39.780 28.918  67.944 1.00 60.93  ? 25  ASP   A O     1 
ATOM   142  C CB    . ASP   A 1 35  ? 42.364 29.816  69.253 1.00 68.52  ? 25  ASP   A CB    1 
ATOM   143  C CG    . ASP   A 1 35  ? 43.317 29.657  70.427 1.00 72.70  ? 25  ASP   A CG    1 
ATOM   144  O OD1   . ASP   A 1 35  ? 43.060 28.762  71.263 1.00 74.64  ? 25  ASP   A OD1   1 
ATOM   145  O OD2   . ASP   A 1 35  ? 44.316 30.405  70.479 1.00 75.60  ? 25  ASP   A OD2   1 
ATOM   146  N N     . ASP   A 1 36  ? 41.222 28.617  66.232 1.00 61.92  ? 26  ASP   A N     1 
ATOM   147  C CA    . ASP   A 1 36  ? 40.217 28.745  65.189 1.00 60.34  ? 26  ASP   A CA    1 
ATOM   148  C C     . ASP   A 1 36  ? 39.842 27.373  64.628 1.00 58.02  ? 26  ASP   A C     1 
ATOM   149  O O     . ASP   A 1 36  ? 39.306 27.295  63.525 1.00 57.00  ? 26  ASP   A O     1 
ATOM   150  C CB    . ASP   A 1 36  ? 40.697 29.708  64.117 1.00 61.42  ? 26  ASP   A CB    1 
ATOM   151  C CG    . ASP   A 1 36  ? 40.647 31.179  64.501 1.00 63.09  ? 26  ASP   A CG    1 
ATOM   152  O OD1   . ASP   A 1 36  ? 39.936 31.510  65.473 1.00 65.04  ? 26  ASP   A OD1   1 
ATOM   153  O OD2   . ASP   A 1 36  ? 41.323 31.980  63.826 1.00 66.45  ? 26  ASP   A OD2   1 
ATOM   154  N N     . VAL   A 1 37  ? 40.103 26.308  65.401 1.00 57.11  ? 27  VAL   A N     1 
ATOM   155  C CA    . VAL   A 1 37  ? 39.679 24.961  65.050 1.00 56.97  ? 27  VAL   A CA    1 
ATOM   156  C C     . VAL   A 1 37  ? 38.849 24.387  66.196 1.00 56.65  ? 27  VAL   A C     1 
ATOM   157  O O     . VAL   A 1 37  ? 39.336 24.268  67.319 1.00 54.46  ? 27  VAL   A O     1 
ATOM   158  C CB    . VAL   A 1 37  ? 40.878 24.047  64.739 1.00 58.45  ? 27  VAL   A CB    1 
ATOM   159  C CG1   . VAL   A 1 37  ? 40.441 22.598  64.541 1.00 59.01  ? 27  VAL   A CG1   1 
ATOM   160  C CG2   . VAL   A 1 37  ? 41.675 24.548  63.537 1.00 58.14  ? 27  VAL   A CG2   1 
ATOM   161  N N     . ASP   A 1 38  ? 37.602 24.008  65.893 1.00 56.37  ? 28  ASP   A N     1 
ATOM   162  C CA    . ASP   A 1 38  ? 36.726 23.393  66.876 1.00 55.05  ? 28  ASP   A CA    1 
ATOM   163  C C     . ASP   A 1 38  ? 36.273 22.022  66.384 1.00 53.25  ? 28  ASP   A C     1 
ATOM   164  O O     . ASP   A 1 38  ? 35.769 21.886  65.275 1.00 55.76  ? 28  ASP   A O     1 
ATOM   165  C CB    . ASP   A 1 38  ? 35.565 24.314  67.211 1.00 56.32  ? 28  ASP   A CB    1 
ATOM   166  C CG    . ASP   A 1 38  ? 35.974 25.607  67.900 1.00 57.81  ? 28  ASP   A CG    1 
ATOM   167  O OD1   . ASP   A 1 38  ? 36.517 25.536  69.020 1.00 61.14  ? 28  ASP   A OD1   1 
ATOM   168  O OD2   . ASP   A 1 38  ? 35.778 26.670  67.299 1.00 60.43  ? 28  ASP   A OD2   1 
ATOM   169  N N     . PHE   A 1 39  ? 36.462 21.006  67.230 1.00 52.16  ? 29  PHE   A N     1 
ATOM   170  C CA    . PHE   A 1 39  ? 35.872 19.698  67.015 1.00 51.43  ? 29  PHE   A CA    1 
ATOM   171  C C     . PHE   A 1 39  ? 34.509 19.642  67.694 1.00 53.01  ? 29  PHE   A C     1 
ATOM   172  O O     . PHE   A 1 39  ? 34.329 20.210  68.766 1.00 54.24  ? 29  PHE   A O     1 
ATOM   173  C CB    . PHE   A 1 39  ? 36.726 18.575  67.603 1.00 50.62  ? 29  PHE   A CB    1 
ATOM   174  C CG    . PHE   A 1 39  ? 38.002 18.260  66.841 1.00 51.39  ? 29  PHE   A CG    1 
ATOM   175  C CD1   . PHE   A 1 39  ? 38.883 19.266  66.460 1.00 51.74  ? 29  PHE   A CD1   1 
ATOM   176  C CD2   . PHE   A 1 39  ? 38.315 16.947  66.509 1.00 52.38  ? 29  PHE   A CD2   1 
ATOM   177  C CE1   . PHE   A 1 39  ? 40.047 18.963  65.771 1.00 51.72  ? 29  PHE   A CE1   1 
ATOM   178  C CE2   . PHE   A 1 39  ? 39.480 16.652  65.819 1.00 52.36  ? 29  PHE   A CE2   1 
ATOM   179  C CZ    . PHE   A 1 39  ? 40.342 17.658  65.451 1.00 51.91  ? 29  PHE   A CZ    1 
ATOM   180  N N     . PHE   A 1 40  ? 33.559 18.943  67.064 1.00 53.96  ? 30  PHE   A N     1 
ATOM   181  C CA    . PHE   A 1 40  ? 32.336 18.525  67.729 1.00 53.65  ? 30  PHE   A CA    1 
ATOM   182  C C     . PHE   A 1 40  ? 32.263 17.013  67.577 1.00 53.60  ? 30  PHE   A C     1 
ATOM   183  O O     . PHE   A 1 40  ? 32.804 16.474  66.620 1.00 55.05  ? 30  PHE   A O     1 
ATOM   184  C CB    . PHE   A 1 40  ? 31.119 19.259  67.164 1.00 54.09  ? 30  PHE   A CB    1 
ATOM   185  C CG    . PHE   A 1 40  ? 31.243 20.775  67.201 1.00 55.96  ? 30  PHE   A CG    1 
ATOM   186  C CD1   . PHE   A 1 40  ? 30.903 21.492  68.344 1.00 57.23  ? 30  PHE   A CD1   1 
ATOM   187  C CD2   . PHE   A 1 40  ? 31.695 21.483  66.092 1.00 56.91  ? 30  PHE   A CD2   1 
ATOM   188  C CE1   . PHE   A 1 40  ? 31.019 22.875  68.378 1.00 56.72  ? 30  PHE   A CE1   1 
ATOM   189  C CE2   . PHE   A 1 40  ? 31.816 22.866  66.136 1.00 57.28  ? 30  PHE   A CE2   1 
ATOM   190  C CZ    . PHE   A 1 40  ? 31.476 23.558  67.277 1.00 56.77  ? 30  PHE   A CZ    1 
ATOM   191  N N     . TYR   A 1 41  ? 31.618 16.342  68.533 1.00 51.76  ? 31  TYR   A N     1 
ATOM   192  C CA    . TYR   A 1 41  ? 31.776 14.907  68.681 1.00 49.57  ? 31  TYR   A CA    1 
ATOM   193  C C     . TYR   A 1 41  ? 30.446 14.171  68.566 1.00 49.04  ? 31  TYR   A C     1 
ATOM   194  O O     . TYR   A 1 41  ? 30.423 12.959  68.744 1.00 49.20  ? 31  TYR   A O     1 
ATOM   195  C CB    . TYR   A 1 41  ? 32.419 14.672  70.049 1.00 49.92  ? 31  TYR   A CB    1 
ATOM   196  C CG    . TYR   A 1 41  ? 33.703 15.459  70.266 1.00 49.45  ? 31  TYR   A CG    1 
ATOM   197  C CD1   . TYR   A 1 41  ? 33.674 16.766  70.741 1.00 48.86  ? 31  TYR   A CD1   1 
ATOM   198  C CD2   . TYR   A 1 41  ? 34.946 14.899  69.990 1.00 48.48  ? 31  TYR   A CD2   1 
ATOM   199  C CE1   . TYR   A 1 41  ? 34.840 17.489  70.934 1.00 47.57  ? 31  TYR   A CE1   1 
ATOM   200  C CE2   . TYR   A 1 41  ? 36.119 15.611  70.187 1.00 47.76  ? 31  TYR   A CE2   1 
ATOM   201  C CZ    . TYR   A 1 41  ? 36.067 16.910  70.655 1.00 48.18  ? 31  TYR   A CZ    1 
ATOM   202  O OH    . TYR   A 1 41  ? 37.227 17.612  70.841 1.00 50.40  ? 31  TYR   A OH    1 
ATOM   203  N N     . ALA   A 1 42  ? 29.356 14.885  68.255 1.00 50.37  ? 32  ALA   A N     1 
ATOM   204  C CA    . ALA   A 1 42  ? 28.031 14.280  68.204 1.00 51.56  ? 32  ALA   A CA    1 
ATOM   205  C C     . ALA   A 1 42  ? 27.154 14.998  67.186 1.00 51.45  ? 32  ALA   A C     1 
ATOM   206  O O     . ALA   A 1 42  ? 27.241 16.216  67.048 1.00 52.43  ? 32  ALA   A O     1 
ATOM   207  C CB    . ALA   A 1 42  ? 27.386 14.316  69.573 1.00 51.94  ? 32  ALA   A CB    1 
ATOM   208  N N     . PRO   A 1 43  ? 26.254 14.273  66.485 1.00 52.13  ? 33  PRO   A N     1 
ATOM   209  C CA    . PRO   A 1 43  ? 25.371 14.883  65.484 1.00 55.10  ? 33  PRO   A CA    1 
ATOM   210  C C     . PRO   A 1 43  ? 24.578 16.104  65.954 1.00 57.11  ? 33  PRO   A C     1 
ATOM   211  O O     . PRO   A 1 43  ? 24.423 17.074  65.211 1.00 59.18  ? 33  PRO   A O     1 
ATOM   212  C CB    . PRO   A 1 43  ? 24.415 13.762  65.050 1.00 53.02  ? 33  PRO   A CB    1 
ATOM   213  C CG    . PRO   A 1 43  ? 25.021 12.475  65.566 1.00 52.73  ? 33  PRO   A CG    1 
ATOM   214  C CD    . PRO   A 1 43  ? 26.067 12.822  66.607 1.00 52.18  ? 33  PRO   A CD    1 
ATOM   215  N N     . ALA   A 1 44  ? 24.048 16.038  67.180 1.00 57.19  ? 34  ALA   A N     1 
ATOM   216  C CA    . ALA   A 1 44  ? 23.208 17.103  67.703 1.00 56.56  ? 34  ALA   A CA    1 
ATOM   217  C C     . ALA   A 1 44  ? 24.023 18.387  67.845 1.00 56.21  ? 34  ALA   A C     1 
ATOM   218  O O     . ALA   A 1 44  ? 23.545 19.461  67.499 1.00 56.21  ? 34  ALA   A O     1 
ATOM   219  C CB    . ALA   A 1 44  ? 22.592 16.682  69.019 1.00 56.19  ? 34  ALA   A CB    1 
ATOM   220  N N     . ASP   A 1 45  ? 25.259 18.262  68.338 1.00 55.61  ? 35  ASP   A N     1 
ATOM   221  C CA    . ASP   A 1 45  ? 26.139 19.405  68.522 1.00 56.34  ? 35  ASP   A CA    1 
ATOM   222  C C     . ASP   A 1 45  ? 26.437 20.063  67.178 1.00 56.59  ? 35  ASP   A C     1 
ATOM   223  O O     . ASP   A 1 45  ? 26.526 21.288  67.081 1.00 57.06  ? 35  ASP   A O     1 
ATOM   224  C CB    . ASP   A 1 45  ? 27.424 18.989  69.217 1.00 57.66  ? 35  ASP   A CB    1 
ATOM   225  C CG    . ASP   A 1 45  ? 27.236 18.414  70.610 1.00 59.35  ? 35  ASP   A CG    1 
ATOM   226  O OD1   . ASP   A 1 45  ? 26.143 18.606  71.177 1.00 61.61  ? 35  ASP   A OD1   1 
ATOM   227  O OD2   . ASP   A 1 45  ? 28.172 17.755  71.100 1.00 62.30  ? 35  ASP   A OD2   1 
ATOM   228  N N     . PHE   A 1 46  ? 26.602 19.226  66.151 1.00 55.32  ? 36  PHE   A N     1 
ATOM   229  C CA    . PHE   A 1 46  ? 26.827 19.682  64.790 1.00 53.89  ? 36  PHE   A CA    1 
ATOM   230  C C     . PHE   A 1 46  ? 25.622 20.487  64.312 1.00 53.78  ? 36  PHE   A C     1 
ATOM   231  O O     . PHE   A 1 46  ? 25.788 21.594  63.800 1.00 54.64  ? 36  PHE   A O     1 
ATOM   232  C CB    . PHE   A 1 46  ? 27.145 18.428  63.971 1.00 54.59  ? 36  PHE   A CB    1 
ATOM   233  C CG    . PHE   A 1 46  ? 26.924 18.529  62.471 1.00 54.10  ? 36  PHE   A CG    1 
ATOM   234  C CD1   . PHE   A 1 46  ? 27.750 19.318  61.680 1.00 54.22  ? 36  PHE   A CD1   1 
ATOM   235  C CD2   . PHE   A 1 46  ? 25.929 17.781  61.855 1.00 54.74  ? 36  PHE   A CD2   1 
ATOM   236  C CE1   . PHE   A 1 46  ? 27.561 19.384  60.311 1.00 54.72  ? 36  PHE   A CE1   1 
ATOM   237  C CE2   . PHE   A 1 46  ? 25.746 17.845  60.485 1.00 56.23  ? 36  PHE   A CE2   1 
ATOM   238  C CZ    . PHE   A 1 46  ? 26.562 18.644  59.716 1.00 56.48  ? 36  PHE   A CZ    1 
ATOM   239  N N     . ARG   A 1 47  ? 24.419 19.927  64.499 1.00 51.59  ? 37  ARG   A N     1 
ATOM   240  C CA    . ARG   A 1 47  ? 23.183 20.613  64.169 1.00 51.73  ? 37  ARG   A CA    1 
ATOM   241  C C     . ARG   A 1 47  ? 23.137 21.987  64.839 1.00 51.80  ? 37  ARG   A C     1 
ATOM   242  O O     . ARG   A 1 47  ? 22.877 22.996  64.189 1.00 52.88  ? 37  ARG   A O     1 
ATOM   243  C CB    . ARG   A 1 47  ? 21.986 19.776  64.631 1.00 53.91  ? 37  ARG   A CB    1 
ATOM   244  C CG    . ARG   A 1 47  ? 20.624 20.394  64.344 1.00 54.99  ? 37  ARG   A CG    1 
ATOM   245  C CD    . ARG   A 1 47  ? 19.483 19.668  65.048 1.00 54.72  ? 37  ARG   A CD    1 
ATOM   246  N NE    . ARG   A 1 47  ? 19.520 19.863  66.503 1.00 54.36  ? 37  ARG   A NE    1 
ATOM   247  C CZ    . ARG   A 1 47  ? 19.454 18.904  67.422 1.00 53.68  ? 37  ARG   A CZ    1 
ATOM   248  N NH1   . ARG   A 1 47  ? 19.318 17.638  67.062 1.00 53.33  ? 37  ARG   A NH1   1 
ATOM   249  N NH2   . ARG   A 1 47  ? 19.521 19.218  68.703 1.00 53.06  ? 37  ARG   A NH2   1 
ATOM   250  N N     . GLU   A 1 48  ? 23.378 22.023  66.152 1.00 51.32  ? 38  GLU   A N     1 
ATOM   251  C CA    . GLU   A 1 48  ? 23.232 23.254  66.910 1.00 50.69  ? 38  GLU   A CA    1 
ATOM   252  C C     . GLU   A 1 48  ? 24.265 24.264  66.417 1.00 50.90  ? 38  GLU   A C     1 
ATOM   253  O O     . GLU   A 1 48  ? 23.925 25.418  66.168 1.00 52.71  ? 38  GLU   A O     1 
ATOM   254  C CB    . GLU   A 1 48  ? 23.288 22.977  68.414 1.00 50.48  ? 38  GLU   A CB    1 
ATOM   255  C CG    . GLU   A 1 48  ? 22.109 22.152  68.925 1.00 50.94  ? 38  GLU   A CG    1 
ATOM   256  C CD    . GLU   A 1 48  ? 20.747 22.794  68.703 1.00 54.00  ? 38  GLU   A CD    1 
ATOM   257  O OE1   . GLU   A 1 48  ? 20.515 23.880  69.289 1.00 56.06  ? 38  GLU   A OE1   1 
ATOM   258  O OE2   . GLU   A 1 48  ? 19.925 22.228  67.939 1.00 52.91  ? 38  GLU   A OE2   1 
ATOM   259  N N     . THR   A 1 49  ? 25.514 23.816  66.237 1.00 50.89  ? 39  THR   A N     1 
ATOM   260  C CA    . THR   A 1 49  ? 26.562 24.676  65.710 1.00 51.53  ? 39  THR   A CA    1 
ATOM   261  C C     . THR   A 1 49  ? 26.124 25.284  64.376 1.00 52.42  ? 39  THR   A C     1 
ATOM   262  O O     . THR   A 1 49  ? 26.338 26.466  64.132 1.00 51.31  ? 39  THR   A O     1 
ATOM   263  C CB    . THR   A 1 49  ? 27.856 23.885  65.550 1.00 51.52  ? 39  THR   A CB    1 
ATOM   264  O OG1   . THR   A 1 49  ? 28.137 23.374  66.847 1.00 53.79  ? 39  THR   A OG1   1 
ATOM   265  C CG2   . THR   A 1 49  ? 29.014 24.749  65.089 1.00 51.76  ? 39  THR   A CG2   1 
ATOM   266  N N     . LEU   A 1 50  ? 25.530 24.467  63.499 1.00 52.90  ? 40  LEU   A N     1 
ATOM   267  C CA    . LEU   A 1 50  ? 25.124 24.949  62.190 1.00 52.60  ? 40  LEU   A CA    1 
ATOM   268  C C     . LEU   A 1 50  ? 24.072 26.045  62.365 1.00 53.44  ? 40  LEU   A C     1 
ATOM   269  O O     . LEU   A 1 50  ? 24.161 27.096  61.734 1.00 53.47  ? 40  LEU   A O     1 
ATOM   270  C CB    . LEU   A 1 50  ? 24.626 23.804  61.307 1.00 51.14  ? 40  LEU   A CB    1 
ATOM   271  C CG    . LEU   A 1 50  ? 24.060 24.205  59.941 1.00 50.64  ? 40  LEU   A CG    1 
ATOM   272  C CD1   . LEU   A 1 50  ? 25.053 25.011  59.117 1.00 50.13  ? 40  LEU   A CD1   1 
ATOM   273  C CD2   . LEU   A 1 50  ? 23.622 22.970  59.185 1.00 51.13  ? 40  LEU   A CD2   1 
ATOM   274  N N     . LEU   A 1 51  ? 23.090 25.806  63.242 1.00 54.31  ? 41  LEU   A N     1 
ATOM   275  C CA    . LEU   A 1 51  ? 22.036 26.780  63.480 1.00 53.13  ? 41  LEU   A CA    1 
ATOM   276  C C     . LEU   A 1 51  ? 22.626 28.041  64.116 1.00 53.21  ? 41  LEU   A C     1 
ATOM   277  O O     . LEU   A 1 51  ? 22.235 29.147  63.747 1.00 52.63  ? 41  LEU   A O     1 
ATOM   278  C CB    . LEU   A 1 51  ? 20.929 26.151  64.325 1.00 52.76  ? 41  LEU   A CB    1 
ATOM   279  C CG    . LEU   A 1 51  ? 20.126 25.029  63.652 1.00 52.89  ? 41  LEU   A CG    1 
ATOM   280  C CD1   . LEU   A 1 51  ? 19.319 24.195  64.635 1.00 51.90  ? 41  LEU   A CD1   1 
ATOM   281  C CD2   . LEU   A 1 51  ? 19.201 25.601  62.592 1.00 52.83  ? 41  LEU   A CD2   1 
ATOM   282  N N     . GLU   A 1 52  ? 23.589 27.872  65.038 1.00 54.51  ? 42  GLU   A N     1 
ATOM   283  C CA    . GLU   A 1 52  ? 24.264 29.000  65.670 1.00 55.16  ? 42  GLU   A CA    1 
ATOM   284  C C     . GLU   A 1 52  ? 24.865 29.914  64.605 1.00 55.18  ? 42  GLU   A C     1 
ATOM   285  O O     . GLU   A 1 52  ? 24.706 31.128  64.678 1.00 57.20  ? 42  GLU   A O     1 
ATOM   286  C CB    . GLU   A 1 52  ? 25.398 28.618  66.626 1.00 55.16  ? 42  GLU   A CB    1 
ATOM   287  C CG    . GLU   A 1 52  ? 24.943 28.046  67.968 1.00 56.38  ? 42  GLU   A CG    1 
ATOM   288  C CD    . GLU   A 1 52  ? 26.077 27.621  68.895 1.00 57.70  ? 42  GLU   A CD    1 
ATOM   289  O OE1   . GLU   A 1 52  ? 27.258 27.833  68.547 1.00 58.21  ? 42  GLU   A OE1   1 
ATOM   290  O OE2   . GLU   A 1 52  ? 25.791 27.071  69.979 1.00 59.52  ? 42  GLU   A OE2   1 
ATOM   291  N N     . LYS   A 1 53  ? 25.550 29.318  63.622 1.00 55.98  ? 43  LYS   A N     1 
ATOM   292  C CA    . LYS   A 1 53  ? 26.330 30.064  62.645 1.00 56.03  ? 43  LYS   A CA    1 
ATOM   293  C C     . LYS   A 1 53  ? 25.441 30.678  61.563 1.00 57.02  ? 43  LYS   A C     1 
ATOM   294  O O     . LYS   A 1 53  ? 25.785 31.726  61.022 1.00 58.23  ? 43  LYS   A O     1 
ATOM   295  C CB    . LYS   A 1 53  ? 27.393 29.163  62.012 1.00 56.00  ? 43  LYS   A CB    1 
ATOM   296  C CG    . LYS   A 1 53  ? 28.477 28.714  62.963 1.00 56.73  ? 43  LYS   A CG    1 
ATOM   297  C CD    . LYS   A 1 53  ? 29.376 29.850  63.419 1.00 59.52  ? 43  LYS   A CD    1 
ATOM   298  C CE    . LYS   A 1 53  ? 30.497 29.324  64.246 1.00 63.90  ? 43  LYS   A CE    1 
ATOM   299  N NZ    . LYS   A 1 53  ? 31.357 30.390  64.761 1.00 66.84  ? 43  LYS   A NZ    1 
ATOM   300  N N     . ILE   A 1 54  ? 24.312 30.028  61.245 1.00 57.10  ? 44  ILE   A N     1 
ATOM   301  C CA    . ILE   A 1 54  ? 23.365 30.561  60.275 1.00 55.82  ? 44  ILE   A CA    1 
ATOM   302  C C     . ILE   A 1 54  ? 22.804 31.889  60.782 1.00 57.47  ? 44  ILE   A C     1 
ATOM   303  O O     . ILE   A 1 54  ? 22.714 32.852  60.018 1.00 61.56  ? 44  ILE   A O     1 
ATOM   304  C CB    . ILE   A 1 54  ? 22.254 29.541  59.956 1.00 54.45  ? 44  ILE   A CB    1 
ATOM   305  C CG1   . ILE   A 1 54  ? 22.793 28.380  59.105 1.00 53.51  ? 44  ILE   A CG1   1 
ATOM   306  C CG2   . ILE   A 1 54  ? 21.062 30.219  59.279 1.00 53.78  ? 44  ILE   A CG2   1 
ATOM   307  C CD1   . ILE   A 1 54  ? 21.882 27.167  59.041 1.00 52.65  ? 44  ILE   A CD1   1 
ATOM   308  N N     . ALA   A 1 55  ? 22.432 31.935  62.068 1.00 56.82  ? 45  ALA   A N     1 
ATOM   309  C CA    . ALA   A 1 55  ? 21.847 33.130  62.661 1.00 55.47  ? 45  ALA   A CA    1 
ATOM   310  C C     . ALA   A 1 55  ? 22.885 34.249  62.762 1.00 56.33  ? 45  ALA   A C     1 
ATOM   311  O O     . ALA   A 1 55  ? 22.532 35.424  62.668 1.00 58.37  ? 45  ALA   A O     1 
ATOM   312  C CB    . ALA   A 1 55  ? 21.257 32.796  64.016 1.00 54.54  ? 45  ALA   A CB    1 
ATOM   313  N N     . SER   A 1 56  ? 24.160 33.866  62.925 1.00 55.71  ? 46  SER   A N     1 
ATOM   314  C CA    . SER   A 1 56  ? 25.245 34.791  63.210 1.00 56.46  ? 46  SER   A CA    1 
ATOM   315  C C     . SER   A 1 56  ? 25.901 35.324  61.940 1.00 54.14  ? 46  SER   A C     1 
ATOM   316  O O     . SER   A 1 56  ? 26.655 36.286  62.024 1.00 54.47  ? 46  SER   A O     1 
ATOM   317  C CB    . SER   A 1 56  ? 26.291 34.138  64.079 1.00 59.89  ? 46  SER   A CB    1 
ATOM   318  O OG    . SER   A 1 56  ? 25.723 33.633  65.279 1.00 66.52  ? 46  SER   A OG    1 
ATOM   319  N N     . ALA   A 1 57  ? 25.649 34.698  60.782 1.00 53.78  ? 47  ALA   A N     1 
ATOM   320  C CA    . ALA   A 1 57  ? 26.388 35.011  59.565 1.00 54.75  ? 47  ALA   A CA    1 
ATOM   321  C C     . ALA   A 1 57  ? 26.055 36.421  59.073 1.00 56.19  ? 47  ALA   A C     1 
ATOM   322  O O     . ALA   A 1 57  ? 24.896 36.828  59.090 1.00 54.55  ? 47  ALA   A O     1 
ATOM   323  C CB    . ALA   A 1 57  ? 26.102 33.978  58.498 1.00 53.75  ? 47  ALA   A CB    1 
ATOM   324  N N     . LYS   A 1 58  ? 27.090 37.141  58.614 1.00 60.99  ? 48  LYS   A N     1 
ATOM   325  C CA    . LYS   A 1 58  ? 26.976 38.540  58.229 1.00 64.92  ? 48  LYS   A CA    1 
ATOM   326  C C     . LYS   A 1 58  ? 27.312 38.766  56.751 1.00 64.58  ? 48  LYS   A C     1 
ATOM   327  O O     . LYS   A 1 58  ? 27.063 39.856  56.243 1.00 65.44  ? 48  LYS   A O     1 
ATOM   328  C CB    . LYS   A 1 58  ? 27.882 39.387  59.133 1.00 68.24  ? 48  LYS   A CB    1 
ATOM   329  C CG    . LYS   A 1 58  ? 27.331 39.670  60.531 1.00 71.70  ? 48  LYS   A CG    1 
ATOM   330  C CD    . LYS   A 1 58  ? 28.306 40.337  61.498 1.00 75.11  ? 48  LYS   A CD    1 
ATOM   331  C CE    . LYS   A 1 58  ? 28.792 41.699  61.079 1.00 77.63  ? 48  LYS   A CE    1 
ATOM   332  N NZ    . LYS   A 1 58  ? 27.742 42.720  61.151 1.00 78.61  ? 48  LYS   A NZ    1 
ATOM   333  N N     . GLN   A 1 59  ? 27.860 37.758  56.056 1.00 64.13  ? 49  GLN   A N     1 
ATOM   334  C CA    . GLN   A 1 59  ? 28.332 37.936  54.687 1.00 63.98  ? 49  GLN   A CA    1 
ATOM   335  C C     . GLN   A 1 59  ? 27.749 36.869  53.765 1.00 60.21  ? 49  GLN   A C     1 
ATOM   336  O O     . GLN   A 1 59  ? 27.146 37.201  52.750 1.00 59.37  ? 49  GLN   A O     1 
ATOM   337  C CB    . GLN   A 1 59  ? 29.850 37.818  54.550 1.00 67.26  ? 49  GLN   A CB    1 
ATOM   338  C CG    . GLN   A 1 59  ? 30.643 38.644  55.554 1.00 70.68  ? 49  GLN   A CG    1 
ATOM   339  C CD    . GLN   A 1 59  ? 32.058 38.139  55.741 1.00 76.73  ? 49  GLN   A CD    1 
ATOM   340  O OE1   . GLN   A 1 59  ? 32.523 37.217  55.053 1.00 76.98  ? 49  GLN   A OE1   1 
ATOM   341  N NE2   . GLN   A 1 59  ? 32.753 38.749  56.691 1.00 78.75  ? 49  GLN   A NE2   1 
ATOM   342  N N     . ARG   A 1 60  ? 27.962 35.591  54.103 1.00 58.82  ? 50  ARG   A N     1 
ATOM   343  C CA    . ARG   A 1 60  ? 27.644 34.508  53.187 1.00 57.69  ? 50  ARG   A CA    1 
ATOM   344  C C     . ARG   A 1 60  ? 27.364 33.207  53.936 1.00 56.65  ? 50  ARG   A C     1 
ATOM   345  O O     . ARG   A 1 60  ? 27.901 32.953  55.015 1.00 54.34  ? 50  ARG   A O     1 
ATOM   346  C CB    . ARG   A 1 60  ? 28.793 34.291  52.195 1.00 57.17  ? 50  ARG   A CB    1 
ATOM   347  C CG    . ARG   A 1 60  ? 30.073 33.783  52.841 1.00 56.27  ? 50  ARG   A CG    1 
ATOM   348  C CD    . ARG   A 1 60  ? 31.263 33.848  51.908 1.00 55.79  ? 50  ARG   A CD    1 
ATOM   349  N NE    . ARG   A 1 60  ? 32.477 33.446  52.626 1.00 55.81  ? 50  ARG   A NE    1 
ATOM   350  C CZ    . ARG   A 1 60  ? 33.710 33.530  52.149 1.00 56.50  ? 50  ARG   A CZ    1 
ATOM   351  N NH1   . ARG   A 1 60  ? 33.911 33.948  50.916 1.00 57.36  ? 50  ARG   A NH1   1 
ATOM   352  N NH2   . ARG   A 1 60  ? 34.745 33.194  52.901 1.00 57.40  ? 50  ARG   A NH2   1 
ATOM   353  N N     . ILE   A 1 61  ? 26.503 32.392  53.317 1.00 56.85  ? 51  ILE   A N     1 
ATOM   354  C CA    . ILE   A 1 61  ? 26.219 31.035  53.750 1.00 56.31  ? 51  ILE   A CA    1 
ATOM   355  C C     . ILE   A 1 61  ? 26.145 30.176  52.493 1.00 57.27  ? 51  ILE   A C     1 
ATOM   356  O O     . ILE   A 1 61  ? 25.215 30.325  51.704 1.00 58.40  ? 51  ILE   A O     1 
ATOM   357  C CB    . ILE   A 1 61  ? 24.909 30.956  54.559 1.00 54.78  ? 51  ILE   A CB    1 
ATOM   358  C CG1   . ILE   A 1 61  ? 24.907 31.922  55.747 1.00 54.14  ? 51  ILE   A CG1   1 
ATOM   359  C CG2   . ILE   A 1 61  ? 24.631 29.514  54.995 1.00 54.61  ? 51  ILE   A CG2   1 
ATOM   360  C CD1   . ILE   A 1 61  ? 23.583 31.996  56.486 1.00 54.02  ? 51  ILE   A CD1   1 
ATOM   361  N N     . CYS   A 1 62  ? 27.137 29.298  52.314 1.00 57.32  ? 52  CYS   A N     1 
ATOM   362  C CA    . CYS   A 1 62  ? 27.153 28.351  51.212 1.00 57.36  ? 52  CYS   A CA    1 
ATOM   363  C C     . CYS   A 1 62  ? 27.030 26.939  51.773 1.00 56.23  ? 52  CYS   A C     1 
ATOM   364  O O     . CYS   A 1 62  ? 27.966 26.431  52.383 1.00 56.29  ? 52  CYS   A O     1 
ATOM   365  C CB    . CYS   A 1 62  ? 28.424 28.497  50.381 1.00 59.79  ? 52  CYS   A CB    1 
ATOM   366  S SG    . CYS   A 1 62  ? 28.416 27.513  48.860 1.00 61.89  ? 52  CYS   A SG    1 
ATOM   367  N N     . ILE   A 1 63  ? 25.858 26.330  51.566 1.00 57.41  ? 53  ILE   A N     1 
ATOM   368  C CA    . ILE   A 1 63  ? 25.585 24.969  51.995 1.00 56.21  ? 53  ILE   A CA    1 
ATOM   369  C C     . ILE   A 1 63  ? 25.693 24.050  50.782 1.00 55.42  ? 53  ILE   A C     1 
ATOM   370  O O     . ILE   A 1 63  ? 24.826 24.060  49.911 1.00 52.79  ? 53  ILE   A O     1 
ATOM   371  C CB    . ILE   A 1 63  ? 24.197 24.867  52.657 1.00 56.66  ? 53  ILE   A CB    1 
ATOM   372  C CG1   . ILE   A 1 63  ? 24.038 25.848  53.831 1.00 56.23  ? 53  ILE   A CG1   1 
ATOM   373  C CG2   . ILE   A 1 63  ? 23.892 23.429  53.075 1.00 57.16  ? 53  ILE   A CG2   1 
ATOM   374  C CD1   . ILE   A 1 63  ? 25.031 25.652  54.963 1.00 55.99  ? 53  ILE   A CD1   1 
ATOM   375  N N     . VAL   A 1 64  ? 26.770 23.262  50.746 1.00 56.45  ? 54  VAL   A N     1 
ATOM   376  C CA    . VAL   A 1 64  ? 26.909 22.174  49.794 1.00 57.46  ? 54  VAL   A CA    1 
ATOM   377  C C     . VAL   A 1 64  ? 26.698 20.863  50.549 1.00 57.70  ? 54  VAL   A C     1 
ATOM   378  O O     . VAL   A 1 64  ? 27.342 20.619  51.568 1.00 60.16  ? 54  VAL   A O     1 
ATOM   379  C CB    . VAL   A 1 64  ? 28.280 22.208  49.091 1.00 59.14  ? 54  VAL   A CB    1 
ATOM   380  C CG1   . VAL   A 1 64  ? 28.385 21.143  48.006 1.00 59.93  ? 54  VAL   A CG1   1 
ATOM   381  C CG2   . VAL   A 1 64  ? 28.590 23.583  48.510 1.00 60.28  ? 54  VAL   A CG2   1 
ATOM   382  N N     . ALA   A 1 65  ? 25.784 20.028  50.045 1.00 57.11  ? 55  ALA   A N     1 
ATOM   383  C CA    . ALA   A 1 65  ? 25.487 18.739  50.650 1.00 56.31  ? 55  ALA   A CA    1 
ATOM   384  C C     . ALA   A 1 65  ? 24.962 17.793  49.578 1.00 56.15  ? 55  ALA   A C     1 
ATOM   385  O O     . ALA   A 1 65  ? 24.382 18.252  48.599 1.00 57.78  ? 55  ALA   A O     1 
ATOM   386  C CB    . ALA   A 1 65  ? 24.475 18.909  51.761 1.00 54.95  ? 55  ALA   A CB    1 
ATOM   387  N N     . LEU   A 1 66  ? 25.158 16.484  49.777 1.00 55.49  ? 56  LEU   A N     1 
ATOM   388  C CA    . LEU   A 1 66  ? 24.590 15.485  48.886 1.00 56.49  ? 56  LEU   A CA    1 
ATOM   389  C C     . LEU   A 1 66  ? 23.083 15.714  48.781 1.00 56.74  ? 56  LEU   A C     1 
ATOM   390  O O     . LEU   A 1 66  ? 22.536 15.738  47.680 1.00 58.61  ? 56  LEU   A O     1 
ATOM   391  C CB    . LEU   A 1 66  ? 24.909 14.061  49.344 1.00 57.27  ? 56  LEU   A CB    1 
ATOM   392  C CG    . LEU   A 1 66  ? 24.391 12.930  48.445 1.00 56.68  ? 56  LEU   A CG    1 
ATOM   393  C CD1   . LEU   A 1 66  ? 25.041 12.961  47.067 1.00 57.09  ? 56  LEU   A CD1   1 
ATOM   394  C CD2   . LEU   A 1 66  ? 24.615 11.581  49.097 1.00 56.47  ? 56  LEU   A CD2   1 
ATOM   395  N N     . TYR   A 1 67  ? 22.413 15.897  49.924 1.00 57.14  ? 57  TYR   A N     1 
ATOM   396  C CA    . TYR   A 1 67  ? 21.001 16.232  49.893 1.00 58.44  ? 57  TYR   A CA    1 
ATOM   397  C C     . TYR   A 1 67  ? 20.578 16.997  51.143 1.00 59.56  ? 57  TYR   A C     1 
ATOM   398  O O     . TYR   A 1 67  ? 21.263 16.998  52.162 1.00 58.52  ? 57  TYR   A O     1 
ATOM   399  C CB    . TYR   A 1 67  ? 20.153 14.974  49.696 1.00 59.55  ? 57  TYR   A CB    1 
ATOM   400  C CG    . TYR   A 1 67  ? 20.286 13.898  50.764 1.00 60.65  ? 57  TYR   A CG    1 
ATOM   401  C CD1   . TYR   A 1 67  ? 21.369 13.027  50.772 1.00 60.70  ? 57  TYR   A CD1   1 
ATOM   402  C CD2   . TYR   A 1 67  ? 19.299 13.715  51.725 1.00 61.45  ? 57  TYR   A CD2   1 
ATOM   403  C CE1   . TYR   A 1 67  ? 21.485 12.030  51.726 1.00 61.36  ? 57  TYR   A CE1   1 
ATOM   404  C CE2   . TYR   A 1 67  ? 19.395 12.711  52.676 1.00 62.87  ? 57  TYR   A CE2   1 
ATOM   405  C CZ    . TYR   A 1 67  ? 20.492 11.867  52.676 1.00 62.04  ? 57  TYR   A CZ    1 
ATOM   406  O OH    . TYR   A 1 67  ? 20.599 10.881  53.610 1.00 60.24  ? 57  TYR   A OH    1 
ATOM   407  N N     . LEU   A 1 68  ? 19.432 17.673  51.002 1.00 61.36  ? 58  LEU   A N     1 
ATOM   408  C CA    . LEU   A 1 68  ? 18.764 18.383  52.075 1.00 62.17  ? 58  LEU   A CA    1 
ATOM   409  C C     . LEU   A 1 68  ? 17.324 17.893  52.098 1.00 61.15  ? 58  LEU   A C     1 
ATOM   410  O O     . LEU   A 1 68  ? 16.534 18.278  51.243 1.00 61.58  ? 58  LEU   A O     1 
ATOM   411  C CB    . LEU   A 1 68  ? 18.868 19.887  51.813 1.00 64.40  ? 58  LEU   A CB    1 
ATOM   412  C CG    . LEU   A 1 68  ? 18.005 20.806  52.685 1.00 66.49  ? 58  LEU   A CG    1 
ATOM   413  C CD1   . LEU   A 1 68  ? 18.324 20.632  54.156 1.00 66.81  ? 58  LEU   A CD1   1 
ATOM   414  C CD2   . LEU   A 1 68  ? 18.186 22.265  52.280 1.00 67.99  ? 58  LEU   A CD2   1 
ATOM   415  N N     . GLU   A 1 69  ? 17.015 17.026  53.069 1.00 62.86  ? 59  GLU   A N     1 
ATOM   416  C CA    . GLU   A 1 69  ? 15.796 16.230  53.052 1.00 63.55  ? 59  GLU   A CA    1 
ATOM   417  C C     . GLU   A 1 69  ? 14.613 17.071  53.518 1.00 64.23  ? 59  GLU   A C     1 
ATOM   418  O O     . GLU   A 1 69  ? 14.789 17.999  54.300 1.00 65.62  ? 59  GLU   A O     1 
ATOM   419  C CB    . GLU   A 1 69  ? 15.973 15.021  53.971 1.00 62.23  ? 59  GLU   A CB    1 
ATOM   420  C CG    . GLU   A 1 69  ? 14.856 13.989  53.849 1.00 62.55  ? 59  GLU   A CG    1 
ATOM   421  C CD    . GLU   A 1 69  ? 14.851 13.223  52.541 1.00 61.88  ? 59  GLU   A CD    1 
ATOM   422  O OE1   . GLU   A 1 69  ? 15.853 13.269  51.800 1.00 63.31  ? 59  GLU   A OE1   1 
ATOM   423  O OE2   . GLU   A 1 69  ? 13.830 12.572  52.268 1.00 60.92  ? 59  GLU   A OE2   1 
ATOM   424  N N     . GLN   A 1 70  ? 13.405 16.723  53.053 1.00 66.32  ? 60  GLN   A N     1 
ATOM   425  C CA    . GLN   A 1 70  ? 12.193 17.356  53.549 1.00 68.11  ? 60  GLN   A CA    1 
ATOM   426  C C     . GLN   A 1 70  ? 11.694 16.599  54.781 1.00 66.89  ? 60  GLN   A C     1 
ATOM   427  O O     . GLN   A 1 70  ? 10.601 16.039  54.786 1.00 67.46  ? 60  GLN   A O     1 
ATOM   428  C CB    . GLN   A 1 70  ? 11.132 17.532  52.459 1.00 69.39  ? 60  GLN   A CB    1 
ATOM   429  C CG    . GLN   A 1 70  ? 10.389 16.270  52.034 1.00 71.77  ? 60  GLN   A CG    1 
ATOM   430  C CD    . GLN   A 1 70  ? 9.055  16.579  51.382 1.00 72.31  ? 60  GLN   A CD    1 
ATOM   431  O OE1   . GLN   A 1 70  ? 8.188  17.238  51.971 1.00 69.99  ? 60  GLN   A OE1   1 
ATOM   432  N NE2   . GLN   A 1 70  ? 8.879  16.125  50.150 1.00 72.16  ? 60  GLN   A NE2   1 
ATOM   433  N N     . ASP   A 1 71  ? 12.507 16.610  55.841 1.00 63.49  ? 61  ASP   A N     1 
ATOM   434  C CA    . ASP   A 1 71  ? 12.106 16.075  57.131 1.00 61.94  ? 61  ASP   A CA    1 
ATOM   435  C C     . ASP   A 1 71  ? 12.305 17.176  58.169 1.00 60.92  ? 61  ASP   A C     1 
ATOM   436  O O     . ASP   A 1 71  ? 12.673 18.294  57.812 1.00 60.43  ? 61  ASP   A O     1 
ATOM   437  C CB    . ASP   A 1 71  ? 12.819 14.761  57.415 1.00 60.87  ? 61  ASP   A CB    1 
ATOM   438  C CG    . ASP   A 1 71  ? 14.339 14.806  57.385 1.00 59.65  ? 61  ASP   A CG    1 
ATOM   439  O OD1   . ASP   A 1 71  ? 14.903 15.916  57.468 1.00 58.09  ? 61  ASP   A OD1   1 
ATOM   440  O OD2   . ASP   A 1 71  ? 14.943 13.723  57.275 1.00 59.13  ? 61  ASP   A OD2   1 
ATOM   441  N N     . ASP   A 1 72  ? 12.047 16.862  59.443 1.00 59.82  ? 62  ASP   A N     1 
ATOM   442  C CA    . ASP   A 1 72  ? 12.140 17.855  60.500 1.00 61.54  ? 62  ASP   A CA    1 
ATOM   443  C C     . ASP   A 1 72  ? 13.550 18.443  60.534 1.00 62.77  ? 62  ASP   A C     1 
ATOM   444  O O     . ASP   A 1 72  ? 13.719 19.633  60.802 1.00 62.87  ? 62  ASP   A O     1 
ATOM   445  C CB    . ASP   A 1 72  ? 11.705 17.282  61.839 1.00 63.04  ? 62  ASP   A CB    1 
ATOM   446  C CG    . ASP   A 1 72  ? 10.207 17.062  62.003 1.00 65.19  ? 62  ASP   A CG    1 
ATOM   447  O OD1   . ASP   A 1 72  ? 9.448  17.450  61.089 1.00 63.23  ? 62  ASP   A OD1   1 
ATOM   448  O OD2   . ASP   A 1 72  ? 9.809  16.498  63.044 1.00 67.38  ? 62  ASP   A OD2   1 
ATOM   449  N N     . GLY   A 1 73  ? 14.552 17.598  60.256 1.00 61.33  ? 63  GLY   A N     1 
ATOM   450  C CA    . GLY   A 1 73  ? 15.939 18.025  60.234 1.00 59.80  ? 63  GLY   A CA    1 
ATOM   451  C C     . GLY   A 1 73  ? 16.176 19.046  59.130 1.00 59.28  ? 63  GLY   A C     1 
ATOM   452  O O     . GLY   A 1 73  ? 16.600 20.165  59.406 1.00 57.41  ? 63  GLY   A O     1 
ATOM   453  N N     . GLY   A 1 74  ? 15.880 18.643  57.887 1.00 59.28  ? 64  GLY   A N     1 
ATOM   454  C CA    . GLY   A 1 74  ? 16.079 19.496  56.728 1.00 58.71  ? 64  GLY   A CA    1 
ATOM   455  C C     . GLY   A 1 74  ? 15.330 20.821  56.869 1.00 59.69  ? 64  GLY   A C     1 
ATOM   456  O O     . GLY   A 1 74  ? 15.881 21.880  56.567 1.00 56.38  ? 64  GLY   A O     1 
ATOM   457  N N     . LYS   A 1 75  ? 14.074 20.733  57.334 1.00 60.66  ? 65  LYS   A N     1 
ATOM   458  C CA    . LYS   A 1 75  ? 13.218 21.890  57.545 1.00 60.88  ? 65  LYS   A CA    1 
ATOM   459  C C     . LYS   A 1 75  ? 13.869 22.840  58.545 1.00 60.44  ? 65  LYS   A C     1 
ATOM   460  O O     . LYS   A 1 75  ? 13.883 24.053  58.333 1.00 61.35  ? 65  LYS   A O     1 
ATOM   461  C CB    . LYS   A 1 75  ? 11.832 21.459  58.044 1.00 63.73  ? 65  LYS   A CB    1 
ATOM   462  C CG    . LYS   A 1 75  ? 10.937 20.868  56.961 1.00 66.52  ? 65  LYS   A CG    1 
ATOM   463  C CD    . LYS   A 1 75  ? 9.759  20.032  57.440 1.00 68.29  ? 65  LYS   A CD    1 
ATOM   464  C CE    . LYS   A 1 75  ? 9.057  19.391  56.280 1.00 70.06  ? 65  LYS   A CE    1 
ATOM   465  N NZ    . LYS   A 1 75  ? 8.017  18.464  56.734 1.00 72.31  ? 65  LYS   A NZ    1 
ATOM   466  N N     . GLY   A 1 76  ? 14.399 22.273  59.635 1.00 57.45  ? 66  GLY   A N     1 
ATOM   467  C CA    . GLY   A 1 76  ? 15.067 23.060  60.655 1.00 57.41  ? 66  GLY   A CA    1 
ATOM   468  C C     . GLY   A 1 76  ? 16.115 23.973  60.029 1.00 57.58  ? 66  GLY   A C     1 
ATOM   469  O O     . GLY   A 1 76  ? 16.136 25.177  60.287 1.00 58.12  ? 66  GLY   A O     1 
ATOM   470  N N     . ILE   A 1 77  ? 16.948 23.376  59.172 1.00 55.67  ? 67  ILE   A N     1 
ATOM   471  C CA    . ILE   A 1 77  ? 18.079 24.067  58.583 1.00 56.88  ? 67  ILE   A CA    1 
ATOM   472  C C     . ILE   A 1 77  ? 17.579 25.082  57.558 1.00 57.02  ? 67  ILE   A C     1 
ATOM   473  O O     . ILE   A 1 77  ? 18.047 26.215  57.547 1.00 57.02  ? 67  ILE   A O     1 
ATOM   474  C CB    . ILE   A 1 77  ? 19.080 23.070  57.969 1.00 56.54  ? 67  ILE   A CB    1 
ATOM   475  C CG1   . ILE   A 1 77  ? 19.503 21.985  58.966 1.00 54.60  ? 67  ILE   A CG1   1 
ATOM   476  C CG2   . ILE   A 1 77  ? 20.291 23.809  57.396 1.00 57.53  ? 67  ILE   A CG2   1 
ATOM   477  C CD1   . ILE   A 1 77  ? 20.147 22.519  60.231 1.00 53.66  ? 67  ILE   A CD1   1 
ATOM   478  N N     . LEU   A 1 78  ? 16.629 24.676  56.706 1.00 58.15  ? 68  LEU   A N     1 
ATOM   479  C CA    . LEU   A 1 78  ? 16.153 25.536  55.630 1.00 58.52  ? 68  LEU   A CA    1 
ATOM   480  C C     . LEU   A 1 78  ? 15.392 26.733  56.209 1.00 58.94  ? 68  LEU   A C     1 
ATOM   481  O O     . LEU   A 1 78  ? 15.637 27.863  55.793 1.00 60.50  ? 68  LEU   A O     1 
ATOM   482  C CB    . LEU   A 1 78  ? 15.309 24.747  54.629 1.00 58.10  ? 68  LEU   A CB    1 
ATOM   483  C CG    . LEU   A 1 78  ? 15.008 25.450  53.300 1.00 58.81  ? 68  LEU   A CG    1 
ATOM   484  C CD1   . LEU   A 1 78  ? 16.271 25.826  52.535 1.00 59.44  ? 68  LEU   A CD1   1 
ATOM   485  C CD2   . LEU   A 1 78  ? 14.122 24.576  52.435 1.00 59.12  ? 68  LEU   A CD2   1 
ATOM   486  N N     . ASN   A 1 79  ? 14.492 26.488  57.176 1.00 57.92  ? 69  ASN   A N     1 
ATOM   487  C CA    . ASN   A 1 79  ? 13.798 27.554  57.888 1.00 57.92  ? 69  ASN   A CA    1 
ATOM   488  C C     . ASN   A 1 79  ? 14.789 28.587  58.425 1.00 57.02  ? 69  ASN   A C     1 
ATOM   489  O O     . ASN   A 1 79  ? 14.556 29.792  58.322 1.00 56.33  ? 69  ASN   A O     1 
ATOM   490  C CB    . ASN   A 1 79  ? 12.986 27.033  59.068 1.00 59.14  ? 69  ASN   A CB    1 
ATOM   491  C CG    . ASN   A 1 79  ? 11.801 26.193  58.654 1.00 60.95  ? 69  ASN   A CG    1 
ATOM   492  O OD1   . ASN   A 1 79  ? 11.346 26.264  57.507 1.00 61.62  ? 69  ASN   A OD1   1 
ATOM   493  N ND2   . ASN   A 1 79  ? 11.279 25.401  59.581 1.00 62.43  ? 69  ASN   A ND2   1 
ATOM   494  N N     . ALA   A 1 80  ? 15.890 28.102  59.008 1.00 55.24  ? 70  ALA   A N     1 
ATOM   495  C CA    . ALA   A 1 80  ? 16.886 28.973  59.611 1.00 56.23  ? 70  ALA   A CA    1 
ATOM   496  C C     . ALA   A 1 80  ? 17.593 29.801  58.540 1.00 56.64  ? 70  ALA   A C     1 
ATOM   497  O O     . ALA   A 1 80  ? 17.947 30.950  58.791 1.00 57.83  ? 70  ALA   A O     1 
ATOM   498  C CB    . ALA   A 1 80  ? 17.867 28.159  60.426 1.00 56.19  ? 70  ALA   A CB    1 
ATOM   499  N N     . LEU   A 1 81  ? 17.794 29.206  57.358 1.00 57.76  ? 71  LEU   A N     1 
ATOM   500  C CA    . LEU   A 1 81  ? 18.398 29.894  56.226 1.00 58.42  ? 71  LEU   A CA    1 
ATOM   501  C C     . LEU   A 1 81  ? 17.478 31.014  55.744 1.00 58.25  ? 71  LEU   A C     1 
ATOM   502  O O     . LEU   A 1 81  ? 17.920 32.152  55.595 1.00 56.43  ? 71  LEU   A O     1 
ATOM   503  C CB    . LEU   A 1 81  ? 18.709 28.896  55.110 1.00 58.12  ? 71  LEU   A CB    1 
ATOM   504  C CG    . LEU   A 1 81  ? 19.829 27.893  55.414 1.00 57.30  ? 71  LEU   A CG    1 
ATOM   505  C CD1   . LEU   A 1 81  ? 19.881 26.802  54.365 1.00 58.09  ? 71  LEU   A CD1   1 
ATOM   506  C CD2   . LEU   A 1 81  ? 21.171 28.589  55.517 1.00 56.18  ? 71  LEU   A CD2   1 
ATOM   507  N N     . TYR   A 1 82  ? 16.199 30.685  55.525 1.00 59.55  ? 72  TYR   A N     1 
ATOM   508  C CA    . TYR   A 1 82  ? 15.200 31.673  55.143 1.00 60.11  ? 72  TYR   A CA    1 
ATOM   509  C C     . TYR   A 1 82  ? 15.164 32.796  56.182 1.00 60.82  ? 72  TYR   A C     1 
ATOM   510  O O     . TYR   A 1 82  ? 15.082 33.971  55.826 1.00 60.24  ? 72  TYR   A O     1 
ATOM   511  C CB    . TYR   A 1 82  ? 13.829 31.016  54.933 1.00 60.13  ? 72  TYR   A CB    1 
ATOM   512  C CG    . TYR   A 1 82  ? 13.591 30.463  53.530 1.00 61.81  ? 72  TYR   A CG    1 
ATOM   513  C CD1   . TYR   A 1 82  ? 13.160 31.289  52.495 1.00 62.80  ? 72  TYR   A CD1   1 
ATOM   514  C CD2   . TYR   A 1 82  ? 13.793 29.118  53.233 1.00 62.03  ? 72  TYR   A CD2   1 
ATOM   515  C CE1   . TYR   A 1 82  ? 12.942 30.797  51.216 1.00 62.30  ? 72  TYR   A CE1   1 
ATOM   516  C CE2   . TYR   A 1 82  ? 13.576 28.615  51.958 1.00 61.68  ? 72  TYR   A CE2   1 
ATOM   517  C CZ    . TYR   A 1 82  ? 13.147 29.456  50.947 1.00 60.17  ? 72  TYR   A CZ    1 
ATOM   518  O OH    . TYR   A 1 82  ? 12.933 28.969  49.692 1.00 59.44  ? 72  TYR   A OH    1 
ATOM   519  N N     . GLU   A 1 83  ? 15.248 32.431  57.466 1.00 61.71  ? 73  GLU   A N     1 
ATOM   520  C CA    . GLU   A 1 83  ? 15.154 33.404  58.540 1.00 62.31  ? 73  GLU   A CA    1 
ATOM   521  C C     . GLU   A 1 83  ? 16.373 34.324  58.513 1.00 63.58  ? 73  GLU   A C     1 
ATOM   522  O O     . GLU   A 1 83  ? 16.238 35.530  58.717 1.00 65.09  ? 73  GLU   A O     1 
ATOM   523  C CB    . GLU   A 1 83  ? 14.989 32.700  59.887 1.00 63.24  ? 73  GLU   A CB    1 
ATOM   524  C CG    . GLU   A 1 83  ? 14.879 33.661  61.069 1.00 65.38  ? 73  GLU   A CG    1 
ATOM   525  C CD    . GLU   A 1 83  ? 13.726 34.655  61.024 1.00 67.37  ? 73  GLU   A CD    1 
ATOM   526  O OE1   . GLU   A 1 83  ? 12.761 34.454  60.250 1.00 69.23  ? 73  GLU   A OE1   1 
ATOM   527  O OE2   . GLU   A 1 83  ? 13.817 35.655  61.768 1.00 66.69  ? 73  GLU   A OE2   1 
ATOM   528  N N     . ALA   A 1 84  ? 17.556 33.753  58.250 1.00 62.62  ? 74  ALA   A N     1 
ATOM   529  C CA    . ALA   A 1 84  ? 18.786 34.529  58.200 1.00 63.63  ? 74  ALA   A CA    1 
ATOM   530  C C     . ALA   A 1 84  ? 18.716 35.567  57.081 1.00 64.94  ? 74  ALA   A C     1 
ATOM   531  O O     . ALA   A 1 84  ? 19.091 36.722  57.283 1.00 65.27  ? 74  ALA   A O     1 
ATOM   532  C CB    . ALA   A 1 84  ? 19.979 33.613  58.024 1.00 63.82  ? 74  ALA   A CB    1 
ATOM   533  N N     . LYS   A 1 85  ? 18.237 35.136  55.906 1.00 64.66  ? 75  LYS   A N     1 
ATOM   534  C CA    . LYS   A 1 85  ? 18.121 35.996  54.739 1.00 65.09  ? 75  LYS   A CA    1 
ATOM   535  C C     . LYS   A 1 85  ? 17.079 37.086  54.992 1.00 67.26  ? 75  LYS   A C     1 
ATOM   536  O O     . LYS   A 1 85  ? 17.243 38.221  54.546 1.00 66.80  ? 75  LYS   A O     1 
ATOM   537  C CB    . LYS   A 1 85  ? 17.752 35.144  53.519 1.00 64.93  ? 75  LYS   A CB    1 
ATOM   538  C CG    . LYS   A 1 85  ? 17.584 35.896  52.203 1.00 65.24  ? 75  LYS   A CG    1 
ATOM   539  C CD    . LYS   A 1 85  ? 18.879 36.415  51.588 1.00 66.41  ? 75  LYS   A CD    1 
ATOM   540  C CE    . LYS   A 1 85  ? 18.628 37.109  50.287 1.00 66.85  ? 75  LYS   A CE    1 
ATOM   541  N NZ    . LYS   A 1 85  ? 19.863 37.455  49.582 1.00 66.70  ? 75  LYS   A NZ    1 
ATOM   542  N N     . ARG   A 1 86  ? 16.010 36.728  55.713 1.00 67.56  ? 76  ARG   A N     1 
ATOM   543  C CA    . ARG   A 1 86  ? 14.951 37.668  56.039 1.00 67.74  ? 76  ARG   A CA    1 
ATOM   544  C C     . ARG   A 1 86  ? 15.497 38.820  56.881 1.00 66.92  ? 76  ARG   A C     1 
ATOM   545  O O     . ARG   A 1 86  ? 15.103 39.963  56.680 1.00 66.77  ? 76  ARG   A O     1 
ATOM   546  C CB    . ARG   A 1 86  ? 13.817 36.934  56.759 1.00 71.08  ? 76  ARG   A CB    1 
ATOM   547  C CG    . ARG   A 1 86  ? 12.623 37.803  57.127 1.00 73.78  ? 76  ARG   A CG    1 
ATOM   548  C CD    . ARG   A 1 86  ? 11.489 36.951  57.664 1.00 74.76  ? 76  ARG   A CD    1 
ATOM   549  N NE    . ARG   A 1 86  ? 11.016 36.055  56.602 1.00 78.33  ? 76  ARG   A NE    1 
ATOM   550  C CZ    . ARG   A 1 86  ? 11.089 34.725  56.588 1.00 79.85  ? 76  ARG   A CZ    1 
ATOM   551  N NH1   . ARG   A 1 86  ? 11.570 34.060  57.628 1.00 80.42  ? 76  ARG   A NH1   1 
ATOM   552  N NH2   . ARG   A 1 86  ? 10.670 34.061  55.523 1.00 79.89  ? 76  ARG   A NH2   1 
ATOM   553  N N     . GLN   A 1 87  ? 16.402 38.514  57.818 1.00 67.66  ? 77  GLN   A N     1 
ATOM   554  C CA    . GLN   A 1 87  ? 16.922 39.502  58.755 1.00 66.23  ? 77  GLN   A CA    1 
ATOM   555  C C     . GLN   A 1 87  ? 18.146 40.216  58.184 1.00 66.25  ? 77  GLN   A C     1 
ATOM   556  O O     . GLN   A 1 87  ? 18.572 41.232  58.729 1.00 65.23  ? 77  GLN   A O     1 
ATOM   557  C CB    . GLN   A 1 87  ? 17.308 38.825  60.070 1.00 66.74  ? 77  GLN   A CB    1 
ATOM   558  C CG    . GLN   A 1 87  ? 16.143 38.140  60.779 1.00 66.91  ? 77  GLN   A CG    1 
ATOM   559  C CD    . GLN   A 1 87  ? 15.098 39.107  61.294 1.00 67.06  ? 77  GLN   A CD    1 
ATOM   560  O OE1   . GLN   A 1 87  ? 15.328 40.316  61.420 1.00 66.64  ? 77  GLN   A OE1   1 
ATOM   561  N NE2   . GLN   A 1 87  ? 13.936 38.567  61.621 1.00 68.17  ? 77  GLN   A NE2   1 
ATOM   562  N N     . ARG   A 1 88  ? 18.726 39.654  57.115 1.00 67.36  ? 78  ARG   A N     1 
ATOM   563  C CA    . ARG   A 1 88  ? 19.847 40.267  56.420 1.00 67.74  ? 78  ARG   A CA    1 
ATOM   564  C C     . ARG   A 1 88  ? 19.697 39.996  54.924 1.00 68.95  ? 78  ARG   A C     1 
ATOM   565  O O     . ARG   A 1 88  ? 20.327 39.092  54.379 1.00 64.95  ? 78  ARG   A O     1 
ATOM   566  C CB    . ARG   A 1 88  ? 21.176 39.768  57.001 1.00 67.28  ? 78  ARG   A CB    1 
ATOM   567  C CG    . ARG   A 1 88  ? 22.393 40.499  56.452 1.00 68.21  ? 78  ARG   A CG    1 
ATOM   568  C CD    . ARG   A 1 88  ? 23.690 40.080  57.124 1.00 67.56  ? 78  ARG   A CD    1 
ATOM   569  N NE    . ARG   A 1 88  ? 23.794 40.590  58.495 1.00 68.13  ? 78  ARG   A NE    1 
ATOM   570  C CZ    . ARG   A 1 88  ? 24.141 41.826  58.845 1.00 67.83  ? 78  ARG   A CZ    1 
ATOM   571  N NH1   . ARG   A 1 88  ? 24.494 42.718  57.932 1.00 66.76  ? 78  ARG   A NH1   1 
ATOM   572  N NH2   . ARG   A 1 88  ? 24.154 42.159  60.124 1.00 67.62  ? 78  ARG   A NH2   1 
ATOM   573  N N     . PRO   A 1 89  ? 18.835 40.766  54.219 1.00 72.70  ? 79  PRO   A N     1 
ATOM   574  C CA    . PRO   A 1 89  ? 18.615 40.570  52.783 1.00 73.74  ? 79  PRO   A CA    1 
ATOM   575  C C     . PRO   A 1 89  ? 19.892 40.550  51.946 1.00 72.35  ? 79  PRO   A C     1 
ATOM   576  O O     . PRO   A 1 89  ? 19.969 39.816  50.967 1.00 71.74  ? 79  PRO   A O     1 
ATOM   577  C CB    . PRO   A 1 89  ? 17.703 41.751  52.401 1.00 75.69  ? 79  PRO   A CB    1 
ATOM   578  C CG    . PRO   A 1 89  ? 16.984 42.101  53.690 1.00 75.80  ? 79  PRO   A CG    1 
ATOM   579  C CD    . PRO   A 1 89  ? 18.013 41.853  54.778 1.00 73.79  ? 79  PRO   A CD    1 
ATOM   580  N N     . GLU   A 1 90  ? 20.889 41.346  52.349 1.00 72.40  ? 80  GLU   A N     1 
ATOM   581  C CA    . GLU   A 1 90  ? 22.128 41.479  51.595 1.00 74.98  ? 80  GLU   A CA    1 
ATOM   582  C C     . GLU   A 1 90  ? 23.033 40.260  51.803 1.00 72.72  ? 80  GLU   A C     1 
ATOM   583  O O     . GLU   A 1 90  ? 24.103 40.180  51.205 1.00 71.83  ? 80  GLU   A O     1 
ATOM   584  C CB    . GLU   A 1 90  ? 22.839 42.797  51.924 1.00 78.26  ? 80  GLU   A CB    1 
ATOM   585  C CG    . GLU   A 1 90  ? 23.374 42.919  53.352 1.00 82.34  ? 80  GLU   A CG    1 
ATOM   586  C CD    . GLU   A 1 90  ? 22.424 43.433  54.428 1.00 85.45  ? 80  GLU   A CD    1 
ATOM   587  O OE1   . GLU   A 1 90  ? 21.184 43.482  54.245 1.00 79.85  ? 80  GLU   A OE1   1 
ATOM   588  O OE2   . GLU   A 1 90  ? 22.977 43.813  55.483 1.00 90.28  ? 80  GLU   A OE2   1 
ATOM   589  N N     . LEU   A 1 91  ? 22.604 39.313  52.647 1.00 71.36  ? 81  LEU   A N     1 
ATOM   590  C CA    . LEU   A 1 91  ? 23.349 38.088  52.897 1.00 69.30  ? 81  LEU   A CA    1 
ATOM   591  C C     . LEU   A 1 91  ? 23.303 37.205  51.651 1.00 67.13  ? 81  LEU   A C     1 
ATOM   592  O O     . LEU   A 1 91  ? 22.240 37.000  51.073 1.00 67.50  ? 81  LEU   A O     1 
ATOM   593  C CB    . LEU   A 1 91  ? 22.737 37.387  54.112 1.00 68.88  ? 81  LEU   A CB    1 
ATOM   594  C CG    . LEU   A 1 91  ? 23.534 36.237  54.734 1.00 67.81  ? 81  LEU   A CG    1 
ATOM   595  C CD1   . LEU   A 1 91  ? 24.822 36.712  55.382 1.00 67.63  ? 81  LEU   A CD1   1 
ATOM   596  C CD2   . LEU   A 1 91  ? 22.662 35.515  55.750 1.00 66.77  ? 81  LEU   A CD2   1 
ATOM   597  N N     . ASP   A 1 92  ? 24.469 36.688  51.252 1.00 65.20  ? 82  ASP   A N     1 
ATOM   598  C CA    . ASP   A 1 92  ? 24.588 35.810  50.100 1.00 64.27  ? 82  ASP   A CA    1 
ATOM   599  C C     . ASP   A 1 92  ? 24.388 34.363  50.549 1.00 65.71  ? 82  ASP   A C     1 
ATOM   600  O O     . ASP   A 1 92  ? 25.303 33.761  51.108 1.00 66.37  ? 82  ASP   A O     1 
ATOM   601  C CB    . ASP   A 1 92  ? 25.939 36.020  49.435 1.00 63.52  ? 82  ASP   A CB    1 
ATOM   602  C CG    . ASP   A 1 92  ? 26.238 35.160  48.217 1.00 62.69  ? 82  ASP   A CG    1 
ATOM   603  O OD1   . ASP   A 1 92  ? 25.323 34.462  47.745 1.00 61.87  ? 82  ASP   A OD1   1 
ATOM   604  O OD2   . ASP   A 1 92  ? 27.397 35.194  47.760 1.00 63.86  ? 82  ASP   A OD2   1 
ATOM   605  N N     . VAL   A 1 93  ? 23.195 33.813  50.283 1.00 65.97  ? 83  VAL   A N     1 
ATOM   606  C CA    . VAL   A 1 93  ? 22.807 32.497  50.769 1.00 68.02  ? 83  VAL   A CA    1 
ATOM   607  C C     . VAL   A 1 93  ? 22.566 31.572  49.580 1.00 70.08  ? 83  VAL   A C     1 
ATOM   608  O O     . VAL   A 1 93  ? 21.748 31.880  48.721 1.00 73.45  ? 83  VAL   A O     1 
ATOM   609  C CB    . VAL   A 1 93  ? 21.545 32.574  51.650 1.00 68.19  ? 83  VAL   A CB    1 
ATOM   610  C CG1   . VAL   A 1 93  ? 21.141 31.204  52.180 1.00 67.06  ? 83  VAL   A CG1   1 
ATOM   611  C CG2   . VAL   A 1 93  ? 21.709 33.567  52.795 1.00 68.54  ? 83  VAL   A CG2   1 
ATOM   612  N N     . ARG   A 1 94  ? 23.253 30.423  49.565 1.00 71.69  ? 84  ARG   A N     1 
ATOM   613  C CA    . ARG   A 1 94  ? 23.144 29.455  48.485 1.00 73.07  ? 84  ARG   A CA    1 
ATOM   614  C C     . ARG   A 1 94  ? 23.073 28.051  49.081 1.00 69.11  ? 84  ARG   A C     1 
ATOM   615  O O     . ARG   A 1 94  ? 23.811 27.738  50.013 1.00 67.85  ? 84  ARG   A O     1 
ATOM   616  C CB    . ARG   A 1 94  ? 24.352 29.495  47.537 1.00 79.61  ? 84  ARG   A CB    1 
ATOM   617  C CG    . ARG   A 1 94  ? 24.851 30.863  47.087 1.00 85.38  ? 84  ARG   A CG    1 
ATOM   618  C CD    . ARG   A 1 94  ? 23.900 31.571  46.128 1.00 88.71  ? 84  ARG   A CD    1 
ATOM   619  N NE    . ARG   A 1 94  ? 24.408 32.881  45.698 1.00 92.09  ? 84  ARG   A NE    1 
ATOM   620  C CZ    . ARG   A 1 94  ? 23.900 33.610  44.704 1.00 95.24  ? 84  ARG   A CZ    1 
ATOM   621  N NH1   . ARG   A 1 94  ? 22.933 33.116  43.950 1.00 94.00  ? 84  ARG   A NH1   1 
ATOM   622  N NH2   . ARG   A 1 94  ? 24.376 34.820  44.447 1.00 95.27  ? 84  ARG   A NH2   1 
ATOM   623  N N     . VAL   A 1 95  ? 22.183 27.217  48.528 1.00 66.43  ? 85  VAL   A N     1 
ATOM   624  C CA    . VAL   A 1 95  ? 22.174 25.787  48.797 1.00 64.61  ? 85  VAL   A CA    1 
ATOM   625  C C     . VAL   A 1 95  ? 22.504 25.056  47.498 1.00 63.88  ? 85  VAL   A C     1 
ATOM   626  O O     . VAL   A 1 95  ? 21.903 25.331  46.463 1.00 64.11  ? 85  VAL   A O     1 
ATOM   627  C CB    . VAL   A 1 95  ? 20.830 25.297  49.367 1.00 62.15  ? 85  VAL   A CB    1 
ATOM   628  C CG1   . VAL   A 1 95  ? 20.820 23.788  49.581 1.00 60.67  ? 85  VAL   A CG1   1 
ATOM   629  C CG2   . VAL   A 1 95  ? 20.464 26.027  50.653 1.00 62.77  ? 85  VAL   A CG2   1 
ATOM   630  N N     . LEU   A 1 96  ? 23.464 24.128  47.566 1.00 62.47  ? 86  LEU   A N     1 
ATOM   631  C CA    . LEU   A 1 96  ? 23.810 23.284  46.436 1.00 62.90  ? 86  LEU   A CA    1 
ATOM   632  C C     . LEU   A 1 96  ? 23.736 21.827  46.875 1.00 63.92  ? 86  LEU   A C     1 
ATOM   633  O O     . LEU   A 1 96  ? 24.474 21.414  47.764 1.00 66.88  ? 86  LEU   A O     1 
ATOM   634  C CB    . LEU   A 1 96  ? 25.204 23.621  45.914 1.00 64.18  ? 86  LEU   A CB    1 
ATOM   635  C CG    . LEU   A 1 96  ? 25.339 24.922  45.119 1.00 64.45  ? 86  LEU   A CG    1 
ATOM   636  C CD1   . LEU   A 1 96  ? 25.525 26.134  46.011 1.00 65.16  ? 86  LEU   A CD1   1 
ATOM   637  C CD2   . LEU   A 1 96  ? 26.485 24.805  44.138 1.00 64.76  ? 86  LEU   A CD2   1 
ATOM   638  N N     . VAL   A 1 97  ? 22.848 21.060  46.235 1.00 63.86  ? 87  VAL   A N     1 
ATOM   639  C CA    . VAL   A 1 97  ? 22.721 19.636  46.495 1.00 63.03  ? 87  VAL   A CA    1 
ATOM   640  C C     . VAL   A 1 97  ? 22.804 18.888  45.167 1.00 64.04  ? 87  VAL   A C     1 
ATOM   641  O O     . VAL   A 1 97  ? 22.871 19.513  44.110 1.00 63.28  ? 87  VAL   A O     1 
ATOM   642  C CB    . VAL   A 1 97  ? 21.410 19.342  47.245 1.00 62.44  ? 87  VAL   A CB    1 
ATOM   643  C CG1   . VAL   A 1 97  ? 21.348 20.091  48.569 1.00 63.27  ? 87  VAL   A CG1   1 
ATOM   644  C CG2   . VAL   A 1 97  ? 20.179 19.654  46.404 1.00 62.42  ? 87  VAL   A CG2   1 
ATOM   645  N N     . ASP   A 1 98  ? 22.801 17.551  45.230 1.00 63.38  ? 88  ASP   A N     1 
ATOM   646  C CA    . ASP   A 1 98  ? 22.864 16.735  44.030 1.00 62.35  ? 88  ASP   A CA    1 
ATOM   647  C C     . ASP   A 1 98  ? 21.560 16.892  43.252 1.00 65.23  ? 88  ASP   A C     1 
ATOM   648  O O     . ASP   A 1 98  ? 20.471 16.785  43.821 1.00 63.67  ? 88  ASP   A O     1 
ATOM   649  C CB    . ASP   A 1 98  ? 23.148 15.276  44.344 1.00 61.06  ? 88  ASP   A CB    1 
ATOM   650  C CG    . ASP   A 1 98  ? 23.550 14.423  43.148 1.00 60.30  ? 88  ASP   A CG    1 
ATOM   651  O OD1   . ASP   A 1 98  ? 24.725 14.511  42.735 1.00 59.84  ? 88  ASP   A OD1   1 
ATOM   652  O OD2   . ASP   A 1 98  ? 22.683 13.690  42.632 1.00 59.81  ? 88  ASP   A OD2   1 
ATOM   653  N N     . TRP   A 1 99  ? 21.711 17.147  41.945 1.00 67.22  ? 89  TRP   A N     1 
ATOM   654  C CA    . TRP   A 1 99  ? 20.607 17.332  41.014 1.00 68.93  ? 89  TRP   A CA    1 
ATOM   655  C C     . TRP   A 1 99  ? 19.708 16.095  40.977 1.00 65.85  ? 89  TRP   A C     1 
ATOM   656  O O     . TRP   A 1 99  ? 18.484 16.208  41.021 1.00 63.82  ? 89  TRP   A O     1 
ATOM   657  C CB    . TRP   A 1 99  ? 21.172 17.653  39.620 1.00 72.38  ? 89  TRP   A CB    1 
ATOM   658  C CG    . TRP   A 1 99  ? 20.177 17.519  38.498 1.00 76.08  ? 89  TRP   A CG    1 
ATOM   659  C CD1   . TRP   A 1 99  ? 20.019 16.449  37.669 1.00 78.05  ? 89  TRP   A CD1   1 
ATOM   660  C CD2   . TRP   A 1 99  ? 19.191 18.493  38.091 1.00 80.39  ? 89  TRP   A CD2   1 
ATOM   661  N NE1   . TRP   A 1 99  ? 19.008 16.684  36.776 1.00 81.34  ? 89  TRP   A NE1   1 
ATOM   662  C CE2   . TRP   A 1 99  ? 18.483 17.929  37.007 1.00 81.96  ? 89  TRP   A CE2   1 
ATOM   663  C CE3   . TRP   A 1 99  ? 18.842 19.776  38.530 1.00 82.51  ? 89  TRP   A CE3   1 
ATOM   664  C CZ2   . TRP   A 1 99  ? 17.450 18.608  36.363 1.00 82.39  ? 89  TRP   A CZ2   1 
ATOM   665  C CZ3   . TRP   A 1 99  ? 17.819 20.443  37.893 1.00 83.59  ? 89  TRP   A CZ3   1 
ATOM   666  C CH2   . TRP   A 1 99  ? 17.135 19.866  36.824 1.00 83.14  ? 89  TRP   A CH2   1 
ATOM   667  N N     . HIS   A 1 100 ? 20.330 14.915  40.888 1.00 65.52  ? 90  HIS   A N     1 
ATOM   668  C CA    . HIS   A 1 100 ? 19.603 13.668  40.711 1.00 66.55  ? 90  HIS   A CA    1 
ATOM   669  C C     . HIS   A 1 100 ? 18.961 13.211  42.017 1.00 67.13  ? 90  HIS   A C     1 
ATOM   670  O O     . HIS   A 1 100 ? 17.822 12.757  42.004 1.00 68.29  ? 90  HIS   A O     1 
ATOM   671  C CB    . HIS   A 1 100 ? 20.516 12.568  40.162 1.00 66.25  ? 90  HIS   A CB    1 
ATOM   672  C CG    . HIS   A 1 100 ? 20.970 12.808  38.763 1.00 66.97  ? 90  HIS   A CG    1 
ATOM   673  N ND1   . HIS   A 1 100 ? 20.103 12.774  37.691 1.00 65.15  ? 90  HIS   A ND1   1 
ATOM   674  C CD2   . HIS   A 1 100 ? 22.178 13.103  38.261 1.00 67.07  ? 90  HIS   A CD2   1 
ATOM   675  C CE1   . HIS   A 1 100 ? 20.782 13.021  36.583 1.00 65.89  ? 90  HIS   A CE1   1 
ATOM   676  N NE2   . HIS   A 1 100 ? 22.044 13.221  36.905 1.00 65.40  ? 90  HIS   A NE2   1 
ATOM   677  N N     . ARG   A 1 101 ? 19.699 13.311  43.130 1.00 68.73  ? 91  ARG   A N     1 
ATOM   678  C CA    . ARG   A 1 101 ? 19.211 12.813  44.408 1.00 68.36  ? 91  ARG   A CA    1 
ATOM   679  C C     . ARG   A 1 101 ? 18.000 13.628  44.855 1.00 65.96  ? 91  ARG   A C     1 
ATOM   680  O O     . ARG   A 1 101 ? 17.074 13.081  45.447 1.00 64.60  ? 91  ARG   A O     1 
ATOM   681  C CB    . ARG   A 1 101 ? 20.310 12.831  45.478 1.00 69.76  ? 91  ARG   A CB    1 
ATOM   682  C CG    . ARG   A 1 101 ? 19.870 12.360  46.857 1.00 71.22  ? 91  ARG   A CG    1 
ATOM   683  C CD    . ARG   A 1 101 ? 19.344 10.930  46.883 1.00 72.68  ? 91  ARG   A CD    1 
ATOM   684  N NE    . ARG   A 1 101 ? 18.825 10.592  48.212 1.00 73.74  ? 91  ARG   A NE    1 
ATOM   685  C CZ    . ARG   A 1 101 ? 17.714 11.082  48.752 1.00 76.07  ? 91  ARG   A CZ    1 
ATOM   686  N NH1   . ARG   A 1 101 ? 16.860 11.773  48.018 1.00 78.83  ? 91  ARG   A NH1   1 
ATOM   687  N NH2   . ARG   A 1 101 ? 17.441 10.855  50.025 1.00 76.10  ? 91  ARG   A NH2   1 
ATOM   688  N N     . ALA   A 1 102 ? 18.018 14.931  44.553 1.00 65.38  ? 92  ALA   A N     1 
ATOM   689  C CA    . ALA   A 1 102 ? 16.977 15.848  44.987 1.00 67.04  ? 92  ALA   A CA    1 
ATOM   690  C C     . ALA   A 1 102 ? 15.641 15.554  44.307 1.00 68.49  ? 92  ALA   A C     1 
ATOM   691  O O     . ALA   A 1 102 ? 14.598 15.985  44.799 1.00 66.28  ? 92  ALA   A O     1 
ATOM   692  C CB    . ALA   A 1 102 ? 17.416 17.272  44.716 1.00 67.18  ? 92  ALA   A CB    1 
ATOM   693  N N     . GLN   A 1 103 ? 15.679 14.833  43.175 1.00 71.95  ? 93  GLN   A N     1 
ATOM   694  C CA    . GLN   A 1 103 ? 14.500 14.622  42.346 1.00 73.71  ? 93  GLN   A CA    1 
ATOM   695  C C     . GLN   A 1 103 ? 14.046 13.161  42.390 1.00 72.52  ? 93  GLN   A C     1 
ATOM   696  O O     . GLN   A 1 103 ? 13.544 12.639  41.398 1.00 71.56  ? 93  GLN   A O     1 
ATOM   697  C CB    . GLN   A 1 103 ? 14.820 15.072  40.920 1.00 73.45  ? 93  GLN   A CB    1 
ATOM   698  C CG    . GLN   A 1 103 ? 14.984 16.580  40.770 1.00 73.99  ? 93  GLN   A CG    1 
ATOM   699  C CD    . GLN   A 1 103 ? 15.350 16.990  39.362 1.00 73.96  ? 93  GLN   A CD    1 
ATOM   700  O OE1   . GLN   A 1 103 ? 16.464 16.747  38.886 1.00 74.41  ? 93  GLN   A OE1   1 
ATOM   701  N NE2   . GLN   A 1 103 ? 14.407 17.614  38.674 1.00 75.76  ? 93  GLN   A NE2   1 
ATOM   702  N N     . ARG   A 1 104 ? 14.196 12.512  43.549 1.00 73.17  ? 94  ARG   A N     1 
ATOM   703  C CA    . ARG   A 1 104 ? 13.700 11.158  43.735 1.00 73.17  ? 94  ARG   A CA    1 
ATOM   704  C C     . ARG   A 1 104 ? 13.616 10.849  45.229 1.00 74.47  ? 94  ARG   A C     1 
ATOM   705  O O     . ARG   A 1 104 ? 14.258 11.516  46.037 1.00 72.30  ? 94  ARG   A O     1 
ATOM   706  C CB    . ARG   A 1 104 ? 14.596 10.142  43.013 1.00 72.29  ? 94  ARG   A CB    1 
ATOM   707  C CG    . ARG   A 1 104 ? 16.027 10.065  43.527 1.00 72.02  ? 94  ARG   A CG    1 
ATOM   708  C CD    . ARG   A 1 104 ? 16.816 8.932   42.897 1.00 71.94  ? 94  ARG   A CD    1 
ATOM   709  N NE    . ARG   A 1 104 ? 18.079 8.652   43.594 1.00 73.55  ? 94  ARG   A NE    1 
ATOM   710  C CZ    . ARG   A 1 104 ? 18.216 8.074   44.792 1.00 73.28  ? 94  ARG   A CZ    1 
ATOM   711  N NH1   . ARG   A 1 104 ? 17.157 7.702   45.494 1.00 73.32  ? 94  ARG   A NH1   1 
ATOM   712  N NH2   . ARG   A 1 104 ? 19.423 7.866   45.290 1.00 70.86  ? 94  ARG   A NH2   1 
ATOM   713  N N     . GLY   A 1 105 ? 12.808 9.837   45.572 1.00 78.28  ? 95  GLY   A N     1 
ATOM   714  C CA    . GLY   A 1 105 ? 12.804 9.245   46.901 1.00 79.82  ? 95  GLY   A CA    1 
ATOM   715  C C     . GLY   A 1 105 ? 13.854 8.139   47.000 1.00 83.34  ? 95  GLY   A C     1 
ATOM   716  O O     . GLY   A 1 105 ? 14.567 7.864   46.036 1.00 81.32  ? 95  GLY   A O     1 
ATOM   717  N N     . ARG   A 1 106 ? 13.937 7.501   48.171 1.00 88.22  ? 96  ARG   A N     1 
ATOM   718  C CA    . ARG   A 1 106 ? 14.921 6.457   48.413 1.00 89.80  ? 96  ARG   A CA    1 
ATOM   719  C C     . ARG   A 1 106 ? 14.663 5.278   47.475 1.00 90.90  ? 96  ARG   A C     1 
ATOM   720  O O     . ARG   A 1 106 ? 13.530 5.054   47.051 1.00 90.82  ? 96  ARG   A O     1 
ATOM   721  C CB    . ARG   A 1 106 ? 14.903 6.063   49.895 1.00 90.61  ? 96  ARG   A CB    1 
ATOM   722  C CG    . ARG   A 1 106 ? 15.464 7.158   50.793 1.00 91.99  ? 96  ARG   A CG    1 
ATOM   723  C CD    . ARG   A 1 106 ? 15.390 6.865   52.290 1.00 92.51  ? 96  ARG   A CD    1 
ATOM   724  N NE    . ARG   A 1 106 ? 15.997 5.583   52.667 1.00 91.85  ? 96  ARG   A NE    1 
ATOM   725  C CZ    . ARG   A 1 106 ? 17.241 5.406   53.104 1.00 91.26  ? 96  ARG   A CZ    1 
ATOM   726  N NH1   . ARG   A 1 106 ? 18.112 6.401   53.082 1.00 92.07  ? 96  ARG   A NH1   1 
ATOM   727  N NH2   . ARG   A 1 106 ? 17.625 4.214   53.527 1.00 89.40  ? 96  ARG   A NH2   1 
ATOM   728  N N     . ILE   A 1 107 ? 15.740 4.544   47.157 1.00 91.81  ? 97  ILE   A N     1 
ATOM   729  C CA    . ILE   A 1 107 ? 15.702 3.421   46.232 1.00 92.73  ? 97  ILE   A CA    1 
ATOM   730  C C     . ILE   A 1 107 ? 14.986 2.250   46.901 1.00 95.43  ? 97  ILE   A C     1 
ATOM   731  O O     . ILE   A 1 107 ? 15.422 1.775   47.948 1.00 93.71  ? 97  ILE   A O     1 
ATOM   732  C CB    . ILE   A 1 107 ? 17.122 3.010   45.793 1.00 91.79  ? 97  ILE   A CB    1 
ATOM   733  C CG1   . ILE   A 1 107 ? 17.886 4.159   45.127 1.00 90.25  ? 97  ILE   A CG1   1 
ATOM   734  C CG2   . ILE   A 1 107 ? 17.073 1.773   44.891 1.00 91.95  ? 97  ILE   A CG2   1 
ATOM   735  C CD1   . ILE   A 1 107 ? 19.382 3.918   45.008 1.00 88.55  ? 97  ILE   A CD1   1 
ATOM   736  N N     . GLY   A 1 108 ? 13.905 1.776   46.268 1.00 99.54  ? 98  GLY   A N     1 
ATOM   737  C CA    . GLY   A 1 108 ? 13.110 0.679   46.797 1.00 101.63 ? 98  GLY   A CA    1 
ATOM   738  C C     . GLY   A 1 108 ? 12.132 1.146   47.875 1.00 102.37 ? 98  GLY   A C     1 
ATOM   739  O O     . GLY   A 1 108 ? 11.655 0.333   48.664 1.00 104.73 ? 98  GLY   A O     1 
ATOM   740  N N     . ALA   A 1 109 ? 11.851 2.457   47.902 1.00 101.84 ? 99  ALA   A N     1 
ATOM   741  C CA    . ALA   A 1 109 ? 10.834 3.034   48.768 1.00 102.36 ? 99  ALA   A CA    1 
ATOM   742  C C     . ALA   A 1 109 ? 9.675  3.538   47.907 1.00 104.08 ? 99  ALA   A C     1 
ATOM   743  O O     . ALA   A 1 109 ? 9.746  3.484   46.679 1.00 100.60 ? 99  ALA   A O     1 
ATOM   744  C CB    . ALA   A 1 109 ? 11.442 4.138   49.613 1.00 99.33  ? 99  ALA   A CB    1 
ATOM   745  N N     . ALA   A 1 110 ? 8.608  4.019   48.561 1.00 105.98 ? 100 ALA   A N     1 
ATOM   746  C CA    . ALA   A 1 110 ? 7.399  4.451   47.872 1.00 108.11 ? 100 ALA   A CA    1 
ATOM   747  C C     . ALA   A 1 110 ? 7.622  5.810   47.207 1.00 110.01 ? 100 ALA   A C     1 
ATOM   748  O O     . ALA   A 1 110 ? 7.767  6.816   47.900 1.00 113.87 ? 100 ALA   A O     1 
ATOM   749  C CB    . ALA   A 1 110 ? 6.244  4.501   48.852 1.00 105.91 ? 100 ALA   A CB    1 
ATOM   750  N N     . ALA   A 1 111 ? 7.633  5.830   45.864 1.00 107.98 ? 101 ALA   A N     1 
ATOM   751  C CA    . ALA   A 1 111 ? 7.788  7.059   45.096 1.00 106.48 ? 101 ALA   A CA    1 
ATOM   752  C C     . ALA   A 1 111 ? 6.894  8.149   45.685 1.00 104.79 ? 101 ALA   A C     1 
ATOM   753  O O     . ALA   A 1 111 ? 5.694  7.937   45.851 1.00 103.50 ? 101 ALA   A O     1 
ATOM   754  C CB    . ALA   A 1 111 ? 7.471  6.806   43.634 1.00 104.17 ? 101 ALA   A CB    1 
ATOM   755  N N     . SER   A 1 112 ? 7.493  9.306   46.002 1.00 101.44 ? 102 SER   A N     1 
ATOM   756  C CA    . SER   A 1 112 ? 6.845  10.307  46.837 1.00 97.89  ? 102 SER   A CA    1 
ATOM   757  C C     . SER   A 1 112 ? 7.128  11.717  46.322 1.00 95.58  ? 102 SER   A C     1 
ATOM   758  O O     . SER   A 1 112 ? 7.703  11.889  45.248 1.00 95.78  ? 102 SER   A O     1 
ATOM   759  C CB    . SER   A 1 112 ? 7.286  10.158  48.274 1.00 95.81  ? 102 SER   A CB    1 
ATOM   760  O OG    . SER   A 1 112 ? 6.633  11.102  49.112 1.00 94.08  ? 102 SER   A OG    1 
ATOM   761  N N     . ASN   A 1 113 ? 6.681  12.715  47.098 1.00 92.19  ? 103 ASN   A N     1 
ATOM   762  C CA    . ASN   A 1 113 ? 7.067  14.106  46.913 1.00 90.09  ? 103 ASN   A CA    1 
ATOM   763  C C     . ASN   A 1 113 ? 8.578  14.242  47.087 1.00 85.79  ? 103 ASN   A C     1 
ATOM   764  O O     . ASN   A 1 113 ? 9.114  13.808  48.104 1.00 84.89  ? 103 ASN   A O     1 
ATOM   765  C CB    . ASN   A 1 113 ? 6.361  15.020  47.912 1.00 91.48  ? 103 ASN   A CB    1 
ATOM   766  C CG    . ASN   A 1 113 ? 5.023  15.539  47.438 1.00 95.49  ? 103 ASN   A CG    1 
ATOM   767  O OD1   . ASN   A 1 113 ? 4.325  16.218  48.200 1.00 94.44  ? 103 ASN   A OD1   1 
ATOM   768  N ND2   . ASN   A 1 113 ? 4.646  15.259  46.198 1.00 96.64  ? 103 ASN   A ND2   1 
ATOM   769  N N     . THR   A 1 114 ? 9.251  14.857  46.103 1.00 79.69  ? 104 THR   A N     1 
ATOM   770  C CA    . THR   A 1 114 ? 10.702 14.982  46.126 1.00 75.42  ? 104 THR   A CA    1 
ATOM   771  C C     . THR   A 1 114 ? 11.109 16.210  46.935 1.00 73.07  ? 104 THR   A C     1 
ATOM   772  O O     . THR   A 1 114 ? 10.284 17.056  47.275 1.00 74.94  ? 104 THR   A O     1 
ATOM   773  C CB    . THR   A 1 114 ? 11.278 15.056  44.711 1.00 72.91  ? 104 THR   A CB    1 
ATOM   774  O OG1   . THR   A 1 114 ? 10.685 16.198  44.102 1.00 71.64  ? 104 THR   A OG1   1 
ATOM   775  C CG2   . THR   A 1 114 ? 11.017 13.801  43.899 1.00 71.83  ? 104 THR   A CG2   1 
ATOM   776  N N     . ASN   A 1 115 ? 12.408 16.291  47.229 1.00 69.26  ? 105 ASN   A N     1 
ATOM   777  C CA    . ASN   A 1 115 ? 12.965 17.427  47.938 1.00 67.22  ? 105 ASN   A CA    1 
ATOM   778  C C     . ASN   A 1 115 ? 12.865 18.664  47.051 1.00 66.92  ? 105 ASN   A C     1 
ATOM   779  O O     . ASN   A 1 115 ? 12.643 19.765  47.548 1.00 64.84  ? 105 ASN   A O     1 
ATOM   780  C CB    . ASN   A 1 115 ? 14.403 17.166  48.376 1.00 66.07  ? 105 ASN   A CB    1 
ATOM   781  C CG    . ASN   A 1 115 ? 14.518 16.029  49.366 1.00 63.95  ? 105 ASN   A CG    1 
ATOM   782  O OD1   . ASN   A 1 115 ? 13.655 15.865  50.236 1.00 61.95  ? 105 ASN   A OD1   1 
ATOM   783  N ND2   . ASN   A 1 115 ? 15.575 15.236  49.255 1.00 63.04  ? 105 ASN   A ND2   1 
ATOM   784  N N     . ALA   A 1 116 ? 13.036 18.463  45.738 1.00 68.19  ? 106 ALA   A N     1 
ATOM   785  C CA    . ALA   A 1 116 ? 12.968 19.546  44.768 1.00 68.24  ? 106 ALA   A CA    1 
ATOM   786  C C     . ALA   A 1 116 ? 11.577 20.180  44.773 1.00 70.00  ? 106 ALA   A C     1 
ATOM   787  O O     . ALA   A 1 116 ? 11.469 21.408  44.750 1.00 71.54  ? 106 ALA   A O     1 
ATOM   788  C CB    . ALA   A 1 116 ? 13.354 19.045  43.393 1.00 68.54  ? 106 ALA   A CB    1 
ATOM   789  N N     . ASP   A 1 117 ? 10.526 19.343  44.806 1.00 68.86  ? 107 ASP   A N     1 
ATOM   790  C CA    . ASP   A 1 117 ? 9.161  19.830  44.947 1.00 68.73  ? 107 ASP   A CA    1 
ATOM   791  C C     . ASP   A 1 117 ? 9.075  20.664  46.217 1.00 66.12  ? 107 ASP   A C     1 
ATOM   792  O O     . ASP   A 1 117 ? 8.539  21.768  46.202 1.00 66.05  ? 107 ASP   A O     1 
ATOM   793  C CB    . ASP   A 1 117 ? 8.121  18.719  45.004 1.00 71.78  ? 107 ASP   A CB    1 
ATOM   794  C CG    . ASP   A 1 117 ? 7.965  17.867  43.750 1.00 75.26  ? 107 ASP   A CG    1 
ATOM   795  O OD1   . ASP   A 1 117 ? 7.998  18.442  42.638 1.00 75.83  ? 107 ASP   A OD1   1 
ATOM   796  O OD2   . ASP   A 1 117 ? 7.783  16.636  43.895 1.00 75.96  ? 107 ASP   A OD2   1 
ATOM   797  N N     . TRP   A 1 118 ? 9.636  20.115  47.302 1.00 65.20  ? 108 TRP   A N     1 
ATOM   798  C CA    . TRP   A 1 118 ? 9.627  20.760  48.605 1.00 62.97  ? 108 TRP   A CA    1 
ATOM   799  C C     . TRP   A 1 118 ? 10.301 22.130  48.532 1.00 61.44  ? 108 TRP   A C     1 
ATOM   800  O O     . TRP   A 1 118 ? 9.750  23.115  49.018 1.00 57.91  ? 108 TRP   A O     1 
ATOM   801  C CB    . TRP   A 1 118 ? 10.305 19.857  49.643 1.00 62.60  ? 108 TRP   A CB    1 
ATOM   802  C CG    . TRP   A 1 118 ? 10.393 20.477  51.009 1.00 62.30  ? 108 TRP   A CG    1 
ATOM   803  C CD1   . TRP   A 1 118 ? 9.381  21.039  51.728 1.00 62.47  ? 108 TRP   A CD1   1 
ATOM   804  C CD2   . TRP   A 1 118 ? 11.589 20.641  51.797 1.00 63.08  ? 108 TRP   A CD2   1 
ATOM   805  N NE1   . TRP   A 1 118 ? 9.858  21.518  52.919 1.00 63.73  ? 108 TRP   A NE1   1 
ATOM   806  C CE2   . TRP   A 1 118 ? 11.207 21.292  52.989 1.00 63.04  ? 108 TRP   A CE2   1 
ATOM   807  C CE3   . TRP   A 1 118 ? 12.933 20.295  51.617 1.00 64.00  ? 108 TRP   A CE3   1 
ATOM   808  C CZ2   . TRP   A 1 118 ? 12.125 21.602  53.989 1.00 63.06  ? 108 TRP   A CZ2   1 
ATOM   809  C CZ3   . TRP   A 1 118 ? 13.838 20.606  52.607 1.00 64.27  ? 108 TRP   A CZ3   1 
ATOM   810  C CH2   . TRP   A 1 118 ? 13.438 21.251  53.777 1.00 62.25  ? 108 TRP   A CH2   1 
ATOM   811  N N     . TYR   A 1 119 ? 11.486 22.181  47.910 1.00 62.67  ? 109 TYR   A N     1 
ATOM   812  C CA    . TYR   A 1 119 ? 12.212 23.428  47.723 1.00 64.32  ? 109 TYR   A CA    1 
ATOM   813  C C     . TYR   A 1 119 ? 11.311 24.470  47.057 1.00 67.14  ? 109 TYR   A C     1 
ATOM   814  O O     . TYR   A 1 119 ? 11.348 25.638  47.436 1.00 67.07  ? 109 TYR   A O     1 
ATOM   815  C CB    . TYR   A 1 119 ? 13.479 23.226  46.887 1.00 64.60  ? 109 TYR   A CB    1 
ATOM   816  C CG    . TYR   A 1 119 ? 14.491 22.220  47.422 1.00 63.81  ? 109 TYR   A CG    1 
ATOM   817  C CD1   . TYR   A 1 119 ? 14.629 21.970  48.784 1.00 65.00  ? 109 TYR   A CD1   1 
ATOM   818  C CD2   . TYR   A 1 119 ? 15.316 21.520  46.553 1.00 63.08  ? 109 TYR   A CD2   1 
ATOM   819  C CE1   . TYR   A 1 119 ? 15.553 21.052  49.261 1.00 64.40  ? 109 TYR   A CE1   1 
ATOM   820  C CE2   . TYR   A 1 119 ? 16.244 20.603  47.017 1.00 64.42  ? 109 TYR   A CE2   1 
ATOM   821  C CZ    . TYR   A 1 119 ? 16.366 20.372  48.374 1.00 63.88  ? 109 TYR   A CZ    1 
ATOM   822  O OH    . TYR   A 1 119 ? 17.284 19.468  48.816 1.00 65.42  ? 109 TYR   A OH    1 
ATOM   823  N N     . CYS   A 1 120 ? 10.501 24.036  46.076 1.00 69.21  ? 110 CYS   A N     1 
ATOM   824  C CA    . CYS   A 1 120 ? 9.569  24.913  45.378 1.00 67.98  ? 110 CYS   A CA    1 
ATOM   825  C C     . CYS   A 1 120 ? 8.484  25.430  46.320 1.00 68.40  ? 110 CYS   A C     1 
ATOM   826  O O     . CYS   A 1 120 ? 8.196  26.623  46.313 1.00 67.99  ? 110 CYS   A O     1 
ATOM   827  C CB    . CYS   A 1 120 ? 8.932  24.223  44.179 1.00 67.80  ? 110 CYS   A CB    1 
ATOM   828  S SG    . CYS   A 1 120 ? 10.149 23.690  42.950 1.00 68.04  ? 110 CYS   A SG    1 
ATOM   829  N N     . ARG   A 1 121 ? 7.881  24.541  47.121 1.00 69.67  ? 111 ARG   A N     1 
ATOM   830  C CA    . ARG   A 1 121 ? 6.854  24.953  48.067 1.00 71.19  ? 111 ARG   A CA    1 
ATOM   831  C C     . ARG   A 1 121 ? 7.430  25.959  49.062 1.00 71.11  ? 111 ARG   A C     1 
ATOM   832  O O     . ARG   A 1 121 ? 6.757  26.921  49.426 1.00 73.10  ? 111 ARG   A O     1 
ATOM   833  C CB    . ARG   A 1 121 ? 6.225  23.783  48.834 1.00 73.92  ? 111 ARG   A CB    1 
ATOM   834  C CG    . ARG   A 1 121 ? 5.322  22.886  48.000 1.00 75.98  ? 111 ARG   A CG    1 
ATOM   835  C CD    . ARG   A 1 121 ? 4.396  22.036  48.864 1.00 78.53  ? 111 ARG   A CD    1 
ATOM   836  N NE    . ARG   A 1 121 ? 5.095  21.168  49.820 1.00 79.78  ? 111 ARG   A NE    1 
ATOM   837  C CZ    . ARG   A 1 121 ? 5.856  20.118  49.514 1.00 82.04  ? 111 ARG   A CZ    1 
ATOM   838  N NH1   . ARG   A 1 121 ? 6.014  19.737  48.256 1.00 83.82  ? 111 ARG   A NH1   1 
ATOM   839  N NH2   . ARG   A 1 121 ? 6.460  19.443  50.477 1.00 82.88  ? 111 ARG   A NH2   1 
ATOM   840  N N     . MET   A 1 122 ? 8.678  25.731  49.488 1.00 71.43  ? 112 MET   A N     1 
ATOM   841  C CA    . MET   A 1 122 ? 9.331  26.572  50.481 1.00 71.20  ? 112 MET   A CA    1 
ATOM   842  C C     . MET   A 1 122 ? 9.537  27.987  49.940 1.00 70.54  ? 112 MET   A C     1 
ATOM   843  O O     . MET   A 1 122 ? 9.358  28.955  50.675 1.00 70.61  ? 112 MET   A O     1 
ATOM   844  C CB    . MET   A 1 122 ? 10.669 25.966  50.918 1.00 70.42  ? 112 MET   A CB    1 
ATOM   845  C CG    . MET   A 1 122 ? 10.517 24.787  51.861 1.00 70.69  ? 112 MET   A CG    1 
ATOM   846  S SD    . MET   A 1 122 ? 9.825  25.260  53.459 1.00 70.44  ? 112 MET   A SD    1 
ATOM   847  C CE    . MET   A 1 122 ? 11.119 26.260  54.207 1.00 70.00  ? 112 MET   A CE    1 
ATOM   848  N N     . ALA   A 1 123 ? 9.917  28.100  48.662 1.00 70.62  ? 113 ALA   A N     1 
ATOM   849  C CA    . ALA   A 1 123 ? 10.052 29.397  48.018 1.00 71.86  ? 113 ALA   A CA    1 
ATOM   850  C C     . ALA   A 1 123 ? 8.700  30.110  47.999 1.00 75.34  ? 113 ALA   A C     1 
ATOM   851  O O     . ALA   A 1 123 ? 8.609  31.267  48.405 1.00 75.67  ? 113 ALA   A O     1 
ATOM   852  C CB    . ALA   A 1 123 ? 10.628 29.239  46.627 1.00 69.79  ? 113 ALA   A CB    1 
ATOM   853  N N     . GLN   A 1 124 ? 7.652  29.395  47.562 1.00 78.42  ? 114 GLN   A N     1 
ATOM   854  C CA    . GLN   A 1 124 ? 6.299  29.934  47.484 1.00 81.52  ? 114 GLN   A CA    1 
ATOM   855  C C     . GLN   A 1 124 ? 5.836  30.406  48.863 1.00 83.07  ? 114 GLN   A C     1 
ATOM   856  O O     . GLN   A 1 124 ? 5.281  31.495  48.991 1.00 82.89  ? 114 GLN   A O     1 
ATOM   857  C CB    . GLN   A 1 124 ? 5.330  28.887  46.931 1.00 83.81  ? 114 GLN   A CB    1 
ATOM   858  C CG    . GLN   A 1 124 ? 5.617  28.465  45.492 1.00 86.86  ? 114 GLN   A CG    1 
ATOM   859  C CD    . GLN   A 1 124 ? 5.095  27.084  45.143 1.00 90.25  ? 114 GLN   A CD    1 
ATOM   860  O OE1   . GLN   A 1 124 ? 4.332  26.461  45.895 1.00 91.12  ? 114 GLN   A OE1   1 
ATOM   861  N NE2   . GLN   A 1 124 ? 5.509  26.584  43.987 1.00 90.12  ? 114 GLN   A NE2   1 
ATOM   862  N N     . GLU   A 1 125 ? 6.090  29.587  49.892 1.00 84.69  ? 115 GLU   A N     1 
ATOM   863  C CA    . GLU   A 1 125 ? 5.626  29.853  51.247 1.00 85.58  ? 115 GLU   A CA    1 
ATOM   864  C C     . GLU   A 1 125 ? 6.411  30.999  51.897 1.00 85.13  ? 115 GLU   A C     1 
ATOM   865  O O     . GLU   A 1 125 ? 5.981  31.521  52.924 1.00 83.35  ? 115 GLU   A O     1 
ATOM   866  C CB    . GLU   A 1 125 ? 5.708  28.564  52.072 1.00 87.28  ? 115 GLU   A CB    1 
ATOM   867  C CG    . GLU   A 1 125 ? 4.691  27.500  51.661 1.00 89.26  ? 115 GLU   A CG    1 
ATOM   868  C CD    . GLU   A 1 125 ? 5.012  26.066  52.070 1.00 92.32  ? 115 GLU   A CD    1 
ATOM   869  O OE1   . GLU   A 1 125 ? 5.998  25.841  52.804 1.00 92.00  ? 115 GLU   A OE1   1 
ATOM   870  O OE2   . GLU   A 1 125 ? 4.276  25.153  51.636 1.00 93.89  ? 115 GLU   A OE2   1 
ATOM   871  N N     . ASN   A 1 126 ? 7.564  31.377  51.317 1.00 85.48  ? 116 ASN   A N     1 
ATOM   872  C CA    . ASN   A 1 126 ? 8.375  32.485  51.809 1.00 84.21  ? 116 ASN   A CA    1 
ATOM   873  C C     . ASN   A 1 126 ? 8.574  33.523  50.702 1.00 84.26  ? 116 ASN   A C     1 
ATOM   874  O O     . ASN   A 1 126 ? 9.677  33.658  50.173 1.00 84.26  ? 116 ASN   A O     1 
ATOM   875  C CB    . ASN   A 1 126 ? 9.742  32.017  52.296 1.00 82.31  ? 116 ASN   A CB    1 
ATOM   876  C CG    . ASN   A 1 126 ? 9.659  31.146  53.525 1.00 81.80  ? 116 ASN   A CG    1 
ATOM   877  O OD1   . ASN   A 1 126 ? 9.997  31.602  54.620 1.00 82.11  ? 116 ASN   A OD1   1 
ATOM   878  N ND2   . ASN   A 1 126 ? 9.223  29.904  53.371 1.00 81.78  ? 116 ASN   A ND2   1 
ATOM   879  N N     . PRO   A 1 127 ? 7.537  34.314  50.336 1.00 83.64  ? 117 PRO   A N     1 
ATOM   880  C CA    . PRO   A 1 127 ? 7.560  35.079  49.084 1.00 82.52  ? 117 PRO   A CA    1 
ATOM   881  C C     . PRO   A 1 127 ? 8.645  36.151  48.972 1.00 79.70  ? 117 PRO   A C     1 
ATOM   882  O O     . PRO   A 1 127 ? 9.165  36.383  47.882 1.00 77.06  ? 117 PRO   A O     1 
ATOM   883  C CB    . PRO   A 1 127 ? 6.144  35.697  49.002 1.00 82.97  ? 117 PRO   A CB    1 
ATOM   884  C CG    . PRO   A 1 127 ? 5.322  34.912  50.005 1.00 85.03  ? 117 PRO   A CG    1 
ATOM   885  C CD    . PRO   A 1 127 ? 6.297  34.520  51.102 1.00 84.03  ? 117 PRO   A CD    1 
ATOM   886  N N     . GLY   A 1 128 ? 8.981  36.803  50.092 1.00 75.17  ? 118 GLY   A N     1 
ATOM   887  C CA    . GLY   A 1 128 ? 9.882  37.945  50.068 1.00 74.08  ? 118 GLY   A CA    1 
ATOM   888  C C     . GLY   A 1 128 ? 11.361 37.553  50.016 1.00 74.22  ? 118 GLY   A C     1 
ATOM   889  O O     . GLY   A 1 128 ? 12.199 38.379  49.663 1.00 72.84  ? 118 GLY   A O     1 
ATOM   890  N N     . VAL   A 1 129 ? 11.678 36.294  50.347 1.00 73.86  ? 119 VAL   A N     1 
ATOM   891  C CA    . VAL   A 1 129 ? 13.032 35.904  50.709 1.00 72.70  ? 119 VAL   A CA    1 
ATOM   892  C C     . VAL   A 1 129 ? 13.583 34.891  49.704 1.00 70.93  ? 119 VAL   A C     1 
ATOM   893  O O     . VAL   A 1 129 ? 12.943 33.879  49.433 1.00 70.59  ? 119 VAL   A O     1 
ATOM   894  C CB    . VAL   A 1 129 ? 12.994 35.338  52.143 1.00 73.31  ? 119 VAL   A CB    1 
ATOM   895  C CG1   . VAL   A 1 129 ? 14.372 34.920  52.638 1.00 72.33  ? 119 VAL   A CG1   1 
ATOM   896  C CG2   . VAL   A 1 129 ? 12.362 36.321  53.123 1.00 73.00  ? 119 VAL   A CG2   1 
ATOM   897  N N     . ASP   A 1 130 ? 14.793 35.164  49.190 1.00 71.23  ? 120 ASP   A N     1 
ATOM   898  C CA    . ASP   A 1 130 ? 15.444 34.327  48.192 1.00 73.72  ? 120 ASP   A CA    1 
ATOM   899  C C     . ASP   A 1 130 ? 16.554 33.488  48.817 1.00 71.64  ? 120 ASP   A C     1 
ATOM   900  O O     . ASP   A 1 130 ? 17.602 34.024  49.180 1.00 68.01  ? 120 ASP   A O     1 
ATOM   901  C CB    . ASP   A 1 130 ? 16.055 35.150  47.072 1.00 76.50  ? 120 ASP   A CB    1 
ATOM   902  C CG    . ASP   A 1 130 ? 15.032 35.839  46.186 1.00 81.81  ? 120 ASP   A CG    1 
ATOM   903  O OD1   . ASP   A 1 130 ? 14.253 35.112  45.530 1.00 84.81  ? 120 ASP   A OD1   1 
ATOM   904  O OD2   . ASP   A 1 130 ? 15.004 37.088  46.192 1.00 83.72  ? 120 ASP   A OD2   1 
ATOM   905  N N     . VAL   A 1 131 ? 16.299 32.173  48.906 1.00 69.21  ? 121 VAL   A N     1 
ATOM   906  C CA    . VAL   A 1 131 ? 17.313 31.178  49.219 1.00 68.55  ? 121 VAL   A CA    1 
ATOM   907  C C     . VAL   A 1 131 ? 17.403 30.228  48.024 1.00 67.84  ? 121 VAL   A C     1 
ATOM   908  O O     . VAL   A 1 131 ? 16.750 29.182  47.998 1.00 64.79  ? 121 VAL   A O     1 
ATOM   909  C CB    . VAL   A 1 131 ? 17.024 30.424  50.535 1.00 69.26  ? 121 VAL   A CB    1 
ATOM   910  C CG1   . VAL   A 1 131 ? 18.123 29.421  50.869 1.00 68.74  ? 121 VAL   A CG1   1 
ATOM   911  C CG2   . VAL   A 1 131 ? 16.820 31.380  51.706 1.00 68.46  ? 121 VAL   A CG2   1 
ATOM   912  N N     . PRO   A 1 132 ? 18.188 30.591  46.979 1.00 68.28  ? 122 PRO   A N     1 
ATOM   913  C CA    . PRO   A 1 132 ? 18.387 29.726  45.816 1.00 67.03  ? 122 PRO   A CA    1 
ATOM   914  C C     . PRO   A 1 132 ? 18.845 28.327  46.213 1.00 65.26  ? 122 PRO   A C     1 
ATOM   915  O O     . PRO   A 1 132 ? 19.813 28.186  46.956 1.00 64.51  ? 122 PRO   A O     1 
ATOM   916  C CB    . PRO   A 1 132 ? 19.471 30.469  45.008 1.00 67.67  ? 122 PRO   A CB    1 
ATOM   917  C CG    . PRO   A 1 132 ? 19.302 31.917  45.393 1.00 67.40  ? 122 PRO   A CG    1 
ATOM   918  C CD    . PRO   A 1 132 ? 18.912 31.867  46.855 1.00 68.59  ? 122 PRO   A CD    1 
ATOM   919  N N     . VAL   A 1 133 ? 18.128 27.311  45.719 1.00 65.68  ? 123 VAL   A N     1 
ATOM   920  C CA    . VAL   A 1 133 ? 18.558 25.925  45.824 1.00 66.08  ? 123 VAL   A CA    1 
ATOM   921  C C     . VAL   A 1 133 ? 18.949 25.434  44.429 1.00 65.61  ? 123 VAL   A C     1 
ATOM   922  O O     . VAL   A 1 133 ? 18.106 25.293  43.545 1.00 63.90  ? 123 VAL   A O     1 
ATOM   923  C CB    . VAL   A 1 133 ? 17.489 25.015  46.458 1.00 66.71  ? 123 VAL   A CB    1 
ATOM   924  C CG1   . VAL   A 1 133 ? 18.041 23.620  46.733 1.00 67.41  ? 123 VAL   A CG1   1 
ATOM   925  C CG2   . VAL   A 1 133 ? 16.910 25.620  47.732 1.00 66.61  ? 123 VAL   A CG2   1 
ATOM   926  N N     . TYR   A 1 134 ? 20.248 25.184  44.245 1.00 67.00  ? 124 TYR   A N     1 
ATOM   927  C CA    . TYR   A 1 134 ? 20.785 24.686  42.991 1.00 67.94  ? 124 TYR   A CA    1 
ATOM   928  C C     . TYR   A 1 134 ? 20.914 23.165  43.059 1.00 66.98  ? 124 TYR   A C     1 
ATOM   929  O O     . TYR   A 1 134 ? 21.136 22.605  44.130 1.00 66.78  ? 124 TYR   A O     1 
ATOM   930  C CB    . TYR   A 1 134 ? 22.135 25.364  42.740 1.00 68.07  ? 124 TYR   A CB    1 
ATOM   931  C CG    . TYR   A 1 134 ? 22.078 26.870  42.515 1.00 69.24  ? 124 TYR   A CG    1 
ATOM   932  C CD1   . TYR   A 1 134 ? 21.930 27.398  41.237 1.00 69.41  ? 124 TYR   A CD1   1 
ATOM   933  C CD2   . TYR   A 1 134 ? 22.191 27.765  43.575 1.00 70.09  ? 124 TYR   A CD2   1 
ATOM   934  C CE1   . TYR   A 1 134 ? 21.883 28.766  41.020 1.00 69.79  ? 124 TYR   A CE1   1 
ATOM   935  C CE2   . TYR   A 1 134 ? 22.146 29.136  43.370 1.00 70.13  ? 124 TYR   A CE2   1 
ATOM   936  C CZ    . TYR   A 1 134 ? 21.994 29.637  42.089 1.00 70.61  ? 124 TYR   A CZ    1 
ATOM   937  O OH    . TYR   A 1 134 ? 21.945 30.984  41.870 1.00 76.46  ? 124 TYR   A OH    1 
ATOM   938  N N     . GLY   A 1 135 ? 20.773 22.513  41.898 1.00 66.77  ? 125 GLY   A N     1 
ATOM   939  C CA    . GLY   A 1 135 ? 20.985 21.081  41.762 1.00 66.96  ? 125 GLY   A CA    1 
ATOM   940  C C     . GLY   A 1 135 ? 22.183 20.811  40.857 1.00 67.81  ? 125 GLY   A C     1 
ATOM   941  O O     . GLY   A 1 135 ? 22.214 21.292  39.728 1.00 71.87  ? 125 GLY   A O     1 
ATOM   942  N N     . VAL   A 1 136 ? 23.153 20.036  41.359 1.00 66.65  ? 126 VAL   A N     1 
ATOM   943  C CA    . VAL   A 1 136 ? 24.440 19.870  40.698 1.00 65.80  ? 126 VAL   A CA    1 
ATOM   944  C C     . VAL   A 1 136 ? 24.564 18.435  40.190 1.00 68.63  ? 126 VAL   A C     1 
ATOM   945  O O     . VAL   A 1 136 ? 24.734 17.514  40.985 1.00 70.33  ? 126 VAL   A O     1 
ATOM   946  C CB    . VAL   A 1 136 ? 25.596 20.225  41.653 1.00 64.40  ? 126 VAL   A CB    1 
ATOM   947  C CG1   . VAL   A 1 136 ? 26.957 19.890  41.059 1.00 64.06  ? 126 VAL   A CG1   1 
ATOM   948  C CG2   . VAL   A 1 136 ? 25.553 21.686  42.086 1.00 64.24  ? 126 VAL   A CG2   1 
ATOM   949  N N     . PRO   A 1 137 ? 24.497 18.196  38.857 1.00 71.37  ? 127 PRO   A N     1 
ATOM   950  C CA    . PRO   A 1 137 ? 24.705 16.861  38.295 1.00 69.93  ? 127 PRO   A CA    1 
ATOM   951  C C     . PRO   A 1 137 ? 26.174 16.656  37.943 1.00 69.83  ? 127 PRO   A C     1 
ATOM   952  O O     . PRO   A 1 137 ? 26.740 17.424  37.171 1.00 69.39  ? 127 PRO   A O     1 
ATOM   953  C CB    . PRO   A 1 137 ? 23.803 16.913  37.060 1.00 70.02  ? 127 PRO   A CB    1 
ATOM   954  C CG    . PRO   A 1 137 ? 23.944 18.343  36.571 1.00 70.59  ? 127 PRO   A CG    1 
ATOM   955  C CD    . PRO   A 1 137 ? 24.213 19.191  37.810 1.00 71.38  ? 127 PRO   A CD    1 
ATOM   956  N N     . ILE   A 1 138 ? 26.783 15.624  38.534 1.00 70.93  ? 128 ILE   A N     1 
ATOM   957  C CA    . ILE   A 1 138 ? 28.175 15.285  38.279 1.00 70.13  ? 128 ILE   A CA    1 
ATOM   958  C C     . ILE   A 1 138 ? 28.235 14.275  37.131 1.00 71.07  ? 128 ILE   A C     1 
ATOM   959  O O     . ILE   A 1 138 ? 29.290 14.071  36.531 1.00 70.56  ? 128 ILE   A O     1 
ATOM   960  C CB    . ILE   A 1 138 ? 28.842 14.789  39.581 1.00 66.69  ? 128 ILE   A CB    1 
ATOM   961  C CG1   . ILE   A 1 138 ? 28.833 15.883  40.652 1.00 66.31  ? 128 ILE   A CG1   1 
ATOM   962  C CG2   . ILE   A 1 138 ? 30.257 14.256  39.349 1.00 65.45  ? 128 ILE   A CG2   1 
ATOM   963  C CD1   . ILE   A 1 138 ? 29.529 17.170  40.251 1.00 66.15  ? 128 ILE   A CD1   1 
ATOM   964  N N     . ASN   A 1 139 ? 27.087 13.658  36.820 1.00 71.80  ? 129 ASN   A N     1 
ATOM   965  C CA    . ASN   A 1 139 ? 26.961 12.812  35.646 1.00 73.88  ? 129 ASN   A CA    1 
ATOM   966  C C     . ASN   A 1 139 ? 25.482 12.721  35.274 1.00 73.40  ? 129 ASN   A C     1 
ATOM   967  O O     . ASN   A 1 139 ? 24.619 13.130  36.049 1.00 71.60  ? 129 ASN   A O     1 
ATOM   968  C CB    . ASN   A 1 139 ? 27.620 11.452  35.871 1.00 75.81  ? 129 ASN   A CB    1 
ATOM   969  C CG    . ASN   A 1 139 ? 28.165 10.850  34.595 1.00 76.70  ? 129 ASN   A CG    1 
ATOM   970  O OD1   . ASN   A 1 139 ? 27.774 11.258  33.496 1.00 79.00  ? 129 ASN   A OD1   1 
ATOM   971  N ND2   . ASN   A 1 139 ? 29.057 9.879   34.711 1.00 75.62  ? 129 ASN   A ND2   1 
ATOM   972  N N     . THR   A 1 140 ? 25.211 12.194  34.074 1.00 74.13  ? 130 THR   A N     1 
ATOM   973  C CA    . THR   A 1 140 ? 23.868 12.155  33.513 1.00 73.99  ? 130 THR   A CA    1 
ATOM   974  C C     . THR   A 1 140 ? 23.034 11.104  34.240 1.00 75.25  ? 130 THR   A C     1 
ATOM   975  O O     . THR   A 1 140 ? 21.812 11.220  34.304 1.00 74.44  ? 130 THR   A O     1 
ATOM   976  C CB    . THR   A 1 140 ? 23.944 11.869  32.014 1.00 73.24  ? 130 THR   A CB    1 
ATOM   977  O OG1   . THR   A 1 140 ? 24.676 10.653  31.888 1.00 73.43  ? 130 THR   A OG1   1 
ATOM   978  C CG2   . THR   A 1 140 ? 24.650 12.972  31.246 1.00 72.92  ? 130 THR   A CG2   1 
ATOM   979  N N     . ARG   A 1 141 ? 23.710 10.066  34.748 1.00 77.76  ? 131 ARG   A N     1 
ATOM   980  C CA    . ARG   A 1 141 ? 23.104 9.114   35.664 1.00 82.39  ? 131 ARG   A CA    1 
ATOM   981  C C     . ARG   A 1 141 ? 23.727 9.298   37.046 1.00 79.65  ? 131 ARG   A C     1 
ATOM   982  O O     . ARG   A 1 141 ? 24.945 9.428   37.163 1.00 82.63  ? 131 ARG   A O     1 
ATOM   983  C CB    . ARG   A 1 141 ? 23.282 7.675   35.162 1.00 87.07  ? 131 ARG   A CB    1 
ATOM   984  C CG    . ARG   A 1 141 ? 22.418 7.318   33.961 1.00 91.11  ? 131 ARG   A CG    1 
ATOM   985  C CD    . ARG   A 1 141 ? 22.557 5.858   33.539 1.00 93.47  ? 131 ARG   A CD    1 
ATOM   986  N NE    . ARG   A 1 141 ? 21.601 5.501   32.483 1.00 97.44  ? 131 ARG   A NE    1 
ATOM   987  C CZ    . ARG   A 1 141 ? 21.609 5.962   31.231 1.00 99.45  ? 131 ARG   A CZ    1 
ATOM   988  N NH1   . ARG   A 1 141 ? 22.608 6.713   30.797 1.00 100.34 ? 131 ARG   A NH1   1 
ATOM   989  N NH2   . ARG   A 1 141 ? 20.625 5.651   30.402 1.00 99.25  ? 131 ARG   A NH2   1 
ATOM   990  N N     . GLU   A 1 142 ? 22.878 9.299   38.082 1.00 76.10  ? 132 GLU   A N     1 
ATOM   991  C CA    . GLU   A 1 142 ? 23.316 9.453   39.463 1.00 73.03  ? 132 GLU   A CA    1 
ATOM   992  C C     . GLU   A 1 142 ? 24.382 8.410   39.801 1.00 71.32  ? 132 GLU   A C     1 
ATOM   993  O O     . GLU   A 1 142 ? 25.380 8.730   40.448 1.00 68.53  ? 132 GLU   A O     1 
ATOM   994  C CB    . GLU   A 1 142 ? 22.121 9.328   40.409 1.00 71.87  ? 132 GLU   A CB    1 
ATOM   995  C CG    . GLU   A 1 142 ? 22.426 9.755   41.842 1.00 72.04  ? 132 GLU   A CG    1 
ATOM   996  C CD    . GLU   A 1 142 ? 21.239 9.703   42.789 1.00 72.76  ? 132 GLU   A CD    1 
ATOM   997  O OE1   . GLU   A 1 142 ? 20.081 9.765   42.308 1.00 71.20  ? 132 GLU   A OE1   1 
ATOM   998  O OE2   . GLU   A 1 142 ? 21.472 9.564   44.012 1.00 72.93  ? 132 GLU   A OE2   1 
ATOM   999  N N     . ALA   A 1 143 ? 24.176 7.175   39.322 1.00 67.33  ? 133 ALA   A N     1 
ATOM   1000 C CA    . ALA   A 1 143 ? 25.011 6.039   39.676 1.00 65.66  ? 133 ALA   A CA    1 
ATOM   1001 C C     . ALA   A 1 143 ? 26.447 6.215   39.184 1.00 65.81  ? 133 ALA   A C     1 
ATOM   1002 O O     . ALA   A 1 143 ? 27.345 5.514   39.649 1.00 63.28  ? 133 ALA   A O     1 
ATOM   1003 C CB    . ALA   A 1 143 ? 24.400 4.773   39.120 1.00 65.25  ? 133 ALA   A CB    1 
ATOM   1004 N N     . LEU   A 1 144 ? 26.663 7.130   38.233 1.00 68.10  ? 134 LEU   A N     1 
ATOM   1005 C CA    . LEU   A 1 144 ? 27.981 7.312   37.650 1.00 69.83  ? 134 LEU   A CA    1 
ATOM   1006 C C     . LEU   A 1 144 ? 28.600 8.634   38.101 1.00 68.39  ? 134 LEU   A C     1 
ATOM   1007 O O     . LEU   A 1 144 ? 29.674 8.995   37.630 1.00 69.47  ? 134 LEU   A O     1 
ATOM   1008 C CB    . LEU   A 1 144 ? 27.876 7.212   36.127 1.00 73.17  ? 134 LEU   A CB    1 
ATOM   1009 C CG    . LEU   A 1 144 ? 27.381 5.869   35.568 1.00 76.13  ? 134 LEU   A CG    1 
ATOM   1010 C CD1   . LEU   A 1 144 ? 27.408 5.870   34.042 1.00 76.24  ? 134 LEU   A CD1   1 
ATOM   1011 C CD2   . LEU   A 1 144 ? 28.179 4.684   36.105 1.00 75.79  ? 134 LEU   A CD2   1 
ATOM   1012 N N     . GLY   A 1 145 ? 27.953 9.335   39.040 1.00 68.59  ? 135 GLY   A N     1 
ATOM   1013 C CA    . GLY   A 1 145 ? 28.519 10.558  39.589 1.00 68.37  ? 135 GLY   A CA    1 
ATOM   1014 C C     . GLY   A 1 145 ? 27.507 11.327  40.437 1.00 68.24  ? 135 GLY   A C     1 
ATOM   1015 O O     . GLY   A 1 145 ? 26.358 11.491  40.027 1.00 69.26  ? 135 GLY   A O     1 
ATOM   1016 N N     . VAL   A 1 146 ? 27.953 11.796  41.615 1.00 66.33  ? 136 VAL   A N     1 
ATOM   1017 C CA    . VAL   A 1 146 ? 27.142 12.642  42.481 1.00 63.06  ? 136 VAL   A CA    1 
ATOM   1018 C C     . VAL   A 1 146 ? 28.014 13.732  43.103 1.00 61.18  ? 136 VAL   A C     1 
ATOM   1019 O O     . VAL   A 1 146 ? 29.240 13.613  43.175 1.00 59.06  ? 136 VAL   A O     1 
ATOM   1020 C CB    . VAL   A 1 146 ? 26.409 11.862  43.587 1.00 62.68  ? 136 VAL   A CB    1 
ATOM   1021 C CG1   . VAL   A 1 146 ? 25.363 10.918  43.015 1.00 62.75  ? 136 VAL   A CG1   1 
ATOM   1022 C CG2   . VAL   A 1 146 ? 27.377 11.113  44.495 1.00 64.31  ? 136 VAL   A CG2   1 
ATOM   1023 N N     . LEU   A 1 147 ? 27.341 14.793  43.564 1.00 59.94  ? 137 LEU   A N     1 
ATOM   1024 C CA    . LEU   A 1 147 ? 27.981 15.873  44.295 1.00 59.15  ? 137 LEU   A CA    1 
ATOM   1025 C C     . LEU   A 1 147 ? 28.348 15.373  45.688 1.00 58.39  ? 137 LEU   A C     1 
ATOM   1026 O O     . LEU   A 1 147 ? 27.485 15.297  46.556 1.00 57.36  ? 137 LEU   A O     1 
ATOM   1027 C CB    . LEU   A 1 147 ? 27.023 17.060  44.370 1.00 58.89  ? 137 LEU   A CB    1 
ATOM   1028 C CG    . LEU   A 1 147 ? 27.514 18.276  45.159 1.00 58.51  ? 137 LEU   A CG    1 
ATOM   1029 C CD1   . LEU   A 1 147 ? 28.612 19.004  44.407 1.00 57.61  ? 137 LEU   A CD1   1 
ATOM   1030 C CD2   . LEU   A 1 147 ? 26.349 19.201  45.466 1.00 58.49  ? 137 LEU   A CD2   1 
ATOM   1031 N N     . HIS   A 1 148 ? 29.627 15.024  45.872 1.00 58.79  ? 138 HIS   A N     1 
ATOM   1032 C CA    . HIS   A 1 148 ? 30.133 14.525  47.140 1.00 58.26  ? 138 HIS   A CA    1 
ATOM   1033 C C     . HIS   A 1 148 ? 31.076 15.561  47.754 1.00 57.40  ? 138 HIS   A C     1 
ATOM   1034 O O     . HIS   A 1 148 ? 31.863 15.240  48.644 1.00 53.46  ? 138 HIS   A O     1 
ATOM   1035 C CB    . HIS   A 1 148 ? 30.805 13.165  46.931 1.00 58.90  ? 138 HIS   A CB    1 
ATOM   1036 C CG    . HIS   A 1 148 ? 30.610 12.229  48.070 1.00 60.36  ? 138 HIS   A CG    1 
ATOM   1037 N ND1   . HIS   A 1 148 ? 31.617 11.701  48.851 1.00 60.14  ? 138 HIS   A ND1   1 
ATOM   1038 C CD2   . HIS   A 1 148 ? 29.470 11.695  48.514 1.00 60.34  ? 138 HIS   A CD2   1 
ATOM   1039 C CE1   . HIS   A 1 148 ? 31.085 10.886  49.749 1.00 59.73  ? 138 HIS   A CE1   1 
ATOM   1040 N NE2   . HIS   A 1 148 ? 29.786 10.872  49.561 1.00 62.39  ? 138 HIS   A NE2   1 
ATOM   1041 N N     . PHE   A 1 149 ? 31.002 16.795  47.235 1.00 57.06  ? 139 PHE   A N     1 
ATOM   1042 C CA    . PHE   A 1 149 ? 31.674 17.943  47.814 1.00 56.78  ? 139 PHE   A CA    1 
ATOM   1043 C C     . PHE   A 1 149 ? 31.034 18.252  49.166 1.00 58.59  ? 139 PHE   A C     1 
ATOM   1044 O O     . PHE   A 1 149 ? 29.809 18.372  49.273 1.00 57.44  ? 139 PHE   A O     1 
ATOM   1045 C CB    . PHE   A 1 149 ? 31.553 19.118  46.840 1.00 56.95  ? 139 PHE   A CB    1 
ATOM   1046 C CG    . PHE   A 1 149 ? 32.461 20.306  47.124 1.00 56.29  ? 139 PHE   A CG    1 
ATOM   1047 C CD1   . PHE   A 1 149 ? 33.722 20.386  46.547 1.00 56.45  ? 139 PHE   A CD1   1 
ATOM   1048 C CD2   . PHE   A 1 149 ? 32.045 21.346  47.944 1.00 56.46  ? 139 PHE   A CD2   1 
ATOM   1049 C CE1   . PHE   A 1 149 ? 34.547 21.470  46.798 1.00 57.61  ? 139 PHE   A CE1   1 
ATOM   1050 C CE2   . PHE   A 1 149 ? 32.872 22.431  48.190 1.00 56.76  ? 139 PHE   A CE2   1 
ATOM   1051 C CZ    . PHE   A 1 149 ? 34.121 22.490  47.619 1.00 57.42  ? 139 PHE   A CZ    1 
ATOM   1052 N N     . LYS   A 1 150 ? 31.882 18.346  50.197 1.00 57.12  ? 140 LYS   A N     1 
ATOM   1053 C CA    . LYS   A 1 150 ? 31.421 18.656  51.538 1.00 57.21  ? 140 LYS   A CA    1 
ATOM   1054 C C     . LYS   A 1 150 ? 31.859 20.068  51.913 1.00 56.34  ? 140 LYS   A C     1 
ATOM   1055 O O     . LYS   A 1 150 ? 32.828 20.595  51.374 1.00 55.34  ? 140 LYS   A O     1 
ATOM   1056 C CB    . LYS   A 1 150 ? 31.961 17.625  52.531 1.00 56.78  ? 140 LYS   A CB    1 
ATOM   1057 C CG    . LYS   A 1 150 ? 31.630 16.185  52.201 1.00 57.37  ? 140 LYS   A CG    1 
ATOM   1058 C CD    . LYS   A 1 150 ? 30.146 15.913  52.001 1.00 56.97  ? 140 LYS   A CD    1 
ATOM   1059 C CE    . LYS   A 1 150 ? 29.906 14.476  51.694 1.00 56.83  ? 140 LYS   A CE    1 
ATOM   1060 N NZ    . LYS   A 1 150 ? 28.499 14.241  51.361 1.00 58.61  ? 140 LYS   A NZ    1 
ATOM   1061 N N     . GLY   A 1 151 ? 31.114 20.679  52.834 1.00 57.13  ? 141 GLY   A N     1 
ATOM   1062 C CA    . GLY   A 1 151 ? 31.486 21.972  53.377 1.00 58.20  ? 141 GLY   A CA    1 
ATOM   1063 C C     . GLY   A 1 151 ? 30.276 22.888  53.489 1.00 57.38  ? 141 GLY   A C     1 
ATOM   1064 O O     . GLY   A 1 151 ? 29.518 23.045  52.533 1.00 56.68  ? 141 GLY   A O     1 
ATOM   1065 N N     . PHE   A 1 152 ? 30.092 23.444  54.688 1.00 57.23  ? 142 PHE   A N     1 
ATOM   1066 C CA    . PHE   A 1 152 ? 29.197 24.567  54.890 1.00 56.90  ? 142 PHE   A CA    1 
ATOM   1067 C C     . PHE   A 1 152 ? 30.091 25.782  55.091 1.00 57.02  ? 142 PHE   A C     1 
ATOM   1068 O O     . PHE   A 1 152 ? 30.828 25.847  56.071 1.00 57.87  ? 142 PHE   A O     1 
ATOM   1069 C CB    . PHE   A 1 152 ? 28.261 24.310  56.074 1.00 56.50  ? 142 PHE   A CB    1 
ATOM   1070 C CG    . PHE   A 1 152 ? 27.522 22.980  56.043 1.00 57.13  ? 142 PHE   A CG    1 
ATOM   1071 C CD1   . PHE   A 1 152 ? 27.172 22.372  54.839 1.00 57.70  ? 142 PHE   A CD1   1 
ATOM   1072 C CD2   . PHE   A 1 152 ? 27.182 22.334  57.226 1.00 57.35  ? 142 PHE   A CD2   1 
ATOM   1073 C CE1   . PHE   A 1 152 ? 26.495 21.161  54.825 1.00 57.22  ? 142 PHE   A CE1   1 
ATOM   1074 C CE2   . PHE   A 1 152 ? 26.498 21.128  57.204 1.00 56.57  ? 142 PHE   A CE2   1 
ATOM   1075 C CZ    . PHE   A 1 152 ? 26.157 20.545  56.007 1.00 57.22  ? 142 PHE   A CZ    1 
ATOM   1076 N N     . ILE   A 1 153 ? 30.074 26.704  54.129 1.00 56.01  ? 143 ILE   A N     1 
ATOM   1077 C CA    . ILE   A 1 153 ? 30.972 27.843  54.184 1.00 58.34  ? 143 ILE   A CA    1 
ATOM   1078 C C     . ILE   A 1 153 ? 30.183 29.031  54.722 1.00 57.81  ? 143 ILE   A C     1 
ATOM   1079 O O     . ILE   A 1 153 ? 29.268 29.522  54.067 1.00 56.50  ? 143 ILE   A O     1 
ATOM   1080 C CB    . ILE   A 1 153 ? 31.617 28.112  52.813 1.00 58.39  ? 143 ILE   A CB    1 
ATOM   1081 C CG1   . ILE   A 1 153 ? 32.303 26.850  52.273 1.00 59.10  ? 143 ILE   A CG1   1 
ATOM   1082 C CG2   . ILE   A 1 153 ? 32.581 29.296  52.899 1.00 58.25  ? 143 ILE   A CG2   1 
ATOM   1083 C CD1   . ILE   A 1 153 ? 32.519 26.844  50.771 1.00 61.13  ? 143 ILE   A CD1   1 
ATOM   1084 N N     . ILE   A 1 154 ? 30.524 29.448  55.945 1.00 57.10  ? 144 ILE   A N     1 
ATOM   1085 C CA    . ILE   A 1 154 ? 29.804 30.515  56.611 1.00 57.64  ? 144 ILE   A CA    1 
ATOM   1086 C C     . ILE   A 1 154 ? 30.810 31.596  56.989 1.00 58.02  ? 144 ILE   A C     1 
ATOM   1087 O O     . ILE   A 1 154 ? 31.646 31.392  57.866 1.00 59.58  ? 144 ILE   A O     1 
ATOM   1088 C CB    . ILE   A 1 154 ? 29.018 29.977  57.818 1.00 56.80  ? 144 ILE   A CB    1 
ATOM   1089 C CG1   . ILE   A 1 154 ? 28.130 28.796  57.415 1.00 56.50  ? 144 ILE   A CG1   1 
ATOM   1090 C CG2   . ILE   A 1 154 ? 28.215 31.098  58.475 1.00 57.29  ? 144 ILE   A CG2   1 
ATOM   1091 C CD1   . ILE   A 1 154 ? 27.362 28.163  58.559 1.00 56.78  ? 144 ILE   A CD1   1 
ATOM   1092 N N     . ASP   A 1 155 ? 30.727 32.724  56.276 1.00 57.46  ? 145 ASP   A N     1 
ATOM   1093 C CA    . ASP   A 1 155 ? 31.642 33.839  56.440 1.00 59.14  ? 145 ASP   A CA    1 
ATOM   1094 C C     . ASP   A 1 155 ? 33.075 33.343  56.262 1.00 58.59  ? 145 ASP   A C     1 
ATOM   1095 O O     . ASP   A 1 155 ? 33.414 32.811  55.209 1.00 59.11  ? 145 ASP   A O     1 
ATOM   1096 C CB    . ASP   A 1 155 ? 31.332 34.601  57.720 1.00 59.90  ? 145 ASP   A CB    1 
ATOM   1097 C CG    . ASP   A 1 155 ? 30.005 35.345  57.707 1.00 61.53  ? 145 ASP   A CG    1 
ATOM   1098 O OD1   . ASP   A 1 155 ? 29.295 35.274  56.678 1.00 63.06  ? 145 ASP   A OD1   1 
ATOM   1099 O OD2   . ASP   A 1 155 ? 29.696 36.005  58.716 1.00 63.93  ? 145 ASP   A OD2   1 
ATOM   1100 N N     . ASP   A 1 156 ? 33.897 33.497  57.303 1.00 57.82  ? 146 ASP   A N     1 
ATOM   1101 C CA    . ASP   A 1 156 ? 35.314 33.182  57.227 1.00 57.76  ? 146 ASP   A CA    1 
ATOM   1102 C C     . ASP   A 1 156 ? 35.568 31.733  57.648 1.00 55.21  ? 146 ASP   A C     1 
ATOM   1103 O O     . ASP   A 1 156 ? 36.723 31.333  57.792 1.00 51.88  ? 146 ASP   A O     1 
ATOM   1104 C CB    . ASP   A 1 156 ? 36.119 34.155  58.075 1.00 59.18  ? 146 ASP   A CB    1 
ATOM   1105 C CG    . ASP   A 1 156 ? 35.647 34.319  59.515 1.00 62.40  ? 146 ASP   A CG    1 
ATOM   1106 O OD1   . ASP   A 1 156 ? 34.621 33.694  59.884 1.00 63.07  ? 146 ASP   A OD1   1 
ATOM   1107 O OD2   . ASP   A 1 156 ? 36.306 35.075  60.262 1.00 64.96  ? 146 ASP   A OD2   1 
ATOM   1108 N N     . SER   A 1 157 ? 34.495 30.948  57.830 1.00 51.81  ? 147 SER   A N     1 
ATOM   1109 C CA    . SER   A 1 157 ? 34.610 29.633  58.437 1.00 52.48  ? 147 SER   A CA    1 
ATOM   1110 C C     . SER   A 1 157 ? 34.011 28.561  57.533 1.00 50.86  ? 147 SER   A C     1 
ATOM   1111 O O     . SER   A 1 157 ? 33.124 28.842  56.730 1.00 52.43  ? 147 SER   A O     1 
ATOM   1112 C CB    . SER   A 1 157 ? 33.948 29.602  59.795 1.00 52.34  ? 147 SER   A CB    1 
ATOM   1113 O OG    . SER   A 1 157 ? 34.512 30.573  60.662 1.00 53.75  ? 147 SER   A OG    1 
ATOM   1114 N N     . VAL   A 1 158 ? 34.490 27.324  57.713 1.00 49.57  ? 148 VAL   A N     1 
ATOM   1115 C CA    . VAL   A 1 158 ? 33.887 26.152  57.104 1.00 50.79  ? 148 VAL   A CA    1 
ATOM   1116 C C     . VAL   A 1 158 ? 33.538 25.170  58.219 1.00 50.43  ? 148 VAL   A C     1 
ATOM   1117 O O     . VAL   A 1 158 ? 34.423 24.712  58.934 1.00 50.38  ? 148 VAL   A O     1 
ATOM   1118 C CB    . VAL   A 1 158 ? 34.792 25.478  56.051 1.00 52.06  ? 148 VAL   A CB    1 
ATOM   1119 C CG1   . VAL   A 1 158 ? 34.104 24.297  55.375 1.00 51.89  ? 148 VAL   A CG1   1 
ATOM   1120 C CG2   . VAL   A 1 158 ? 35.278 26.468  55.001 1.00 52.43  ? 148 VAL   A CG2   1 
ATOM   1121 N N     . LEU   A 1 159 ? 32.239 24.888  58.377 1.00 50.77  ? 149 LEU   A N     1 
ATOM   1122 C CA    . LEU   A 1 159 ? 31.789 23.757  59.167 1.00 51.21  ? 149 LEU   A CA    1 
ATOM   1123 C C     . LEU   A 1 159 ? 31.804 22.539  58.250 1.00 51.64  ? 149 LEU   A C     1 
ATOM   1124 O O     . LEU   A 1 159 ? 30.994 22.457  57.328 1.00 52.35  ? 149 LEU   A O     1 
ATOM   1125 C CB    . LEU   A 1 159 ? 30.401 24.012  59.755 1.00 50.76  ? 149 LEU   A CB    1 
ATOM   1126 C CG    . LEU   A 1 159 ? 29.811 22.883  60.608 1.00 51.31  ? 149 LEU   A CG    1 
ATOM   1127 C CD1   . LEU   A 1 159 ? 30.712 22.526  61.787 1.00 52.15  ? 149 LEU   A CD1   1 
ATOM   1128 C CD2   . LEU   A 1 159 ? 28.420 23.260  61.095 1.00 50.81  ? 149 LEU   A CD2   1 
ATOM   1129 N N     . TYR   A 1 160 ? 32.748 21.622  58.499 1.00 52.10  ? 150 TYR   A N     1 
ATOM   1130 C CA    . TYR   A 1 160 ? 33.040 20.540  57.573 1.00 52.52  ? 150 TYR   A CA    1 
ATOM   1131 C C     . TYR   A 1 160 ? 32.553 19.221  58.155 1.00 50.85  ? 150 TYR   A C     1 
ATOM   1132 O O     . TYR   A 1 160 ? 32.881 18.883  59.287 1.00 52.73  ? 150 TYR   A O     1 
ATOM   1133 C CB    . TYR   A 1 160 ? 34.531 20.398  57.248 1.00 53.37  ? 150 TYR   A CB    1 
ATOM   1134 C CG    . TYR   A 1 160 ? 34.775 19.505  56.038 1.00 54.04  ? 150 TYR   A CG    1 
ATOM   1135 C CD1   . TYR   A 1 160 ? 34.701 20.024  54.750 1.00 54.14  ? 150 TYR   A CD1   1 
ATOM   1136 C CD2   . TYR   A 1 160 ? 35.039 18.144  56.177 1.00 53.62  ? 150 TYR   A CD2   1 
ATOM   1137 C CE1   . TYR   A 1 160 ? 34.899 19.224  53.636 1.00 53.71  ? 150 TYR   A CE1   1 
ATOM   1138 C CE2   . TYR   A 1 160 ? 35.236 17.331  55.070 1.00 53.35  ? 150 TYR   A CE2   1 
ATOM   1139 C CZ    . TYR   A 1 160 ? 35.167 17.877  53.797 1.00 53.26  ? 150 TYR   A CZ    1 
ATOM   1140 O OH    . TYR   A 1 160 ? 35.353 17.121  52.682 1.00 51.83  ? 150 TYR   A OH    1 
ATOM   1141 N N     . SER   A 1 161 ? 31.798 18.478  57.342 1.00 50.16  ? 151 SER   A N     1 
ATOM   1142 C CA    . SER   A 1 161 ? 31.281 17.174  57.713 1.00 49.70  ? 151 SER   A CA    1 
ATOM   1143 C C     . SER   A 1 161 ? 30.888 16.393  56.462 1.00 50.44  ? 151 SER   A C     1 
ATOM   1144 O O     . SER   A 1 161 ? 30.547 16.970  55.431 1.00 51.93  ? 151 SER   A O     1 
ATOM   1145 C CB    . SER   A 1 161 ? 30.107 17.315  58.634 1.00 49.19  ? 151 SER   A CB    1 
ATOM   1146 O OG    . SER   A 1 161 ? 29.456 16.065  58.819 1.00 50.47  ? 151 SER   A OG    1 
ATOM   1147 N N     . GLY   A 1 162 ? 30.882 15.065  56.579 1.00 50.46  ? 152 GLY   A N     1 
ATOM   1148 C CA    . GLY   A 1 162 ? 30.342 14.227  55.523 1.00 51.24  ? 152 GLY   A CA    1 
ATOM   1149 C C     . GLY   A 1 162 ? 28.816 14.285  55.484 1.00 51.55  ? 152 GLY   A C     1 
ATOM   1150 O O     . GLY   A 1 162 ? 28.200 13.842  54.518 1.00 52.18  ? 152 GLY   A O     1 
ATOM   1151 N N     . ALA   A 1 163 ? 28.213 14.827  56.546 1.00 51.11  ? 153 ALA   A N     1 
ATOM   1152 C CA    . ALA   A 1 163 ? 26.785 14.702  56.766 1.00 52.11  ? 153 ALA   A CA    1 
ATOM   1153 C C     . ALA   A 1 163 ? 25.986 15.449  55.704 1.00 51.10  ? 153 ALA   A C     1 
ATOM   1154 O O     . ALA   A 1 163 ? 26.311 16.571  55.335 1.00 52.97  ? 153 ALA   A O     1 
ATOM   1155 C CB    . ALA   A 1 163 ? 26.433 15.202  58.151 1.00 52.38  ? 153 ALA   A CB    1 
ATOM   1156 N N     . SER   A 1 164 ? 24.927 14.794  55.228 1.00 52.96  ? 154 SER   A N     1 
ATOM   1157 C CA    . SER   A 1 164 ? 23.829 15.476  54.568 1.00 53.44  ? 154 SER   A CA    1 
ATOM   1158 C C     . SER   A 1 164 ? 22.881 16.013  55.639 1.00 53.92  ? 154 SER   A C     1 
ATOM   1159 O O     . SER   A 1 164 ? 23.168 15.911  56.831 1.00 55.49  ? 154 SER   A O     1 
ATOM   1160 C CB    . SER   A 1 164 ? 23.142 14.557  53.581 1.00 53.18  ? 154 SER   A CB    1 
ATOM   1161 O OG    . SER   A 1 164 ? 24.015 14.234  52.507 1.00 51.04  ? 154 SER   A OG    1 
ATOM   1162 N N     . LEU   A 1 165 ? 21.764 16.609  55.213 1.00 52.96  ? 155 LEU   A N     1 
ATOM   1163 C CA    . LEU   A 1 165 ? 20.905 17.342  56.123 1.00 52.65  ? 155 LEU   A CA    1 
ATOM   1164 C C     . LEU   A 1 165 ? 19.538 16.674  56.189 1.00 53.48  ? 155 LEU   A C     1 
ATOM   1165 O O     . LEU   A 1 165 ? 18.679 16.908  55.342 1.00 53.86  ? 155 LEU   A O     1 
ATOM   1166 C CB    . LEU   A 1 165 ? 20.835 18.785  55.636 1.00 52.94  ? 155 LEU   A CB    1 
ATOM   1167 C CG    . LEU   A 1 165 ? 22.162 19.547  55.660 1.00 53.04  ? 155 LEU   A CG    1 
ATOM   1168 C CD1   . LEU   A 1 165 ? 22.025 20.917  55.018 1.00 54.47  ? 155 LEU   A CD1   1 
ATOM   1169 C CD2   . LEU   A 1 165 ? 22.662 19.665  57.089 1.00 53.23  ? 155 LEU   A CD2   1 
ATOM   1170 N N     . ASN   A 1 166 ? 19.365 15.840  57.219 1.00 54.43  ? 156 ASN   A N     1 
ATOM   1171 C CA    . ASN   A 1 166 ? 18.123 15.124  57.447 1.00 55.68  ? 156 ASN   A CA    1 
ATOM   1172 C C     . ASN   A 1 166 ? 18.010 14.820  58.939 1.00 57.19  ? 156 ASN   A C     1 
ATOM   1173 O O     . ASN   A 1 166 ? 18.778 15.354  59.738 1.00 56.80  ? 156 ASN   A O     1 
ATOM   1174 C CB    . ASN   A 1 166 ? 18.035 13.890  56.552 1.00 55.92  ? 156 ASN   A CB    1 
ATOM   1175 C CG    . ASN   A 1 166 ? 19.062 12.836  56.889 1.00 56.26  ? 156 ASN   A CG    1 
ATOM   1176 O OD1   . ASN   A 1 166 ? 19.844 12.990  57.833 1.00 57.04  ? 156 ASN   A OD1   1 
ATOM   1177 N ND2   . ASN   A 1 166 ? 19.079 11.759  56.121 1.00 57.34  ? 156 ASN   A ND2   1 
ATOM   1178 N N     . ASP   A 1 167 ? 17.056 13.949  59.293 1.00 58.10  ? 157 ASP   A N     1 
ATOM   1179 C CA    . ASP   A 1 167 ? 16.782 13.616  60.681 1.00 58.06  ? 157 ASP   A CA    1 
ATOM   1180 C C     . ASP   A 1 167 ? 18.007 12.972  61.319 1.00 55.33  ? 157 ASP   A C     1 
ATOM   1181 O O     . ASP   A 1 167 ? 18.516 13.487  62.309 1.00 54.92  ? 157 ASP   A O     1 
ATOM   1182 C CB    . ASP   A 1 167 ? 15.547 12.738  60.817 1.00 59.22  ? 157 ASP   A CB    1 
ATOM   1183 C CG    . ASP   A 1 167 ? 14.220 13.476  60.726 1.00 60.12  ? 157 ASP   A CG    1 
ATOM   1184 O OD1   . ASP   A 1 167 ? 14.245 14.675  60.386 1.00 59.23  ? 157 ASP   A OD1   1 
ATOM   1185 O OD2   . ASP   A 1 167 ? 13.177 12.855  61.026 1.00 62.81  ? 157 ASP   A OD2   1 
ATOM   1186 N N     . VAL   A 1 168 ? 18.464 11.858  60.738 1.00 53.57  ? 158 VAL   A N     1 
ATOM   1187 C CA    . VAL   A 1 168 ? 19.460 11.011  61.378 1.00 52.20  ? 158 VAL   A CA    1 
ATOM   1188 C C     . VAL   A 1 168 ? 20.814 11.724  61.396 1.00 51.24  ? 158 VAL   A C     1 
ATOM   1189 O O     . VAL   A 1 168 ? 21.532 11.658  62.387 1.00 53.00  ? 158 VAL   A O     1 
ATOM   1190 C CB    . VAL   A 1 168 ? 19.544 9.605   60.741 1.00 51.98  ? 158 VAL   A CB    1 
ATOM   1191 C CG1   . VAL   A 1 168 ? 18.229 8.844   60.889 1.00 50.93  ? 158 VAL   A CG1   1 
ATOM   1192 C CG2   . VAL   A 1 168 ? 19.975 9.623   59.277 1.00 50.57  ? 158 VAL   A CG2   1 
ATOM   1193 N N     . TYR   A 1 169 ? 21.165 12.432  60.321 1.00 52.10  ? 159 TYR   A N     1 
ATOM   1194 C CA    . TYR   A 1 169 ? 22.453 13.106  60.262 1.00 52.04  ? 159 TYR   A CA    1 
ATOM   1195 C C     . TYR   A 1 169 ? 22.498 14.240  61.285 1.00 51.40  ? 159 TYR   A C     1 
ATOM   1196 O O     . TYR   A 1 169 ? 23.574 14.596  61.760 1.00 50.21  ? 159 TYR   A O     1 
ATOM   1197 C CB    . TYR   A 1 169 ? 22.791 13.686  58.882 1.00 52.27  ? 159 TYR   A CB    1 
ATOM   1198 C CG    . TYR   A 1 169 ? 23.541 12.764  57.929 1.00 52.46  ? 159 TYR   A CG    1 
ATOM   1199 C CD1   . TYR   A 1 169 ? 24.833 12.341  58.213 1.00 52.23  ? 159 TYR   A CD1   1 
ATOM   1200 C CD2   . TYR   A 1 169 ? 22.989 12.374  56.715 1.00 53.02  ? 159 TYR   A CD2   1 
ATOM   1201 C CE1   . TYR   A 1 169 ? 25.535 11.522  57.343 1.00 51.23  ? 159 TYR   A CE1   1 
ATOM   1202 C CE2   . TYR   A 1 169 ? 23.680 11.554  55.836 1.00 51.83  ? 159 TYR   A CE2   1 
ATOM   1203 C CZ    . TYR   A 1 169 ? 24.959 11.134  56.148 1.00 50.80  ? 159 TYR   A CZ    1 
ATOM   1204 O OH    . TYR   A 1 169 ? 25.649 10.333  55.287 1.00 48.93  ? 159 TYR   A OH    1 
ATOM   1205 N N     . LEU   A 1 170 ? 21.337 14.833  61.587 1.00 52.62  ? 160 LEU   A N     1 
ATOM   1206 C CA    . LEU   A 1 170 ? 21.271 15.950  62.518 1.00 54.36  ? 160 LEU   A CA    1 
ATOM   1207 C C     . LEU   A 1 170 ? 20.823 15.462  63.896 1.00 53.18  ? 160 LEU   A C     1 
ATOM   1208 O O     . LEU   A 1 170 ? 20.729 16.256  64.826 1.00 52.85  ? 160 LEU   A O     1 
ATOM   1209 C CB    . LEU   A 1 170 ? 20.344 17.032  61.959 1.00 55.26  ? 160 LEU   A CB    1 
ATOM   1210 C CG    . LEU   A 1 170 ? 20.798 17.709  60.659 1.00 56.02  ? 160 LEU   A CG    1 
ATOM   1211 C CD1   . LEU   A 1 170 ? 19.710 18.597  60.075 1.00 56.22  ? 160 LEU   A CD1   1 
ATOM   1212 C CD2   . LEU   A 1 170 ? 22.060 18.525  60.884 1.00 56.17  ? 160 LEU   A CD2   1 
ATOM   1213 N N     . HIS   A 1 171 ? 20.589 14.149  64.023 1.00 54.15  ? 161 HIS   A N     1 
ATOM   1214 C CA    . HIS   A 1 171 ? 20.030 13.549  65.226 1.00 56.15  ? 161 HIS   A CA    1 
ATOM   1215 C C     . HIS   A 1 171 ? 18.832 14.367  65.709 1.00 57.56  ? 161 HIS   A C     1 
ATOM   1216 O O     . HIS   A 1 171 ? 18.786 14.801  66.857 1.00 56.99  ? 161 HIS   A O     1 
ATOM   1217 C CB    . HIS   A 1 171 ? 21.123 13.354  66.283 1.00 56.48  ? 161 HIS   A CB    1 
ATOM   1218 C CG    . HIS   A 1 171 ? 20.730 12.456  67.407 1.00 56.60  ? 161 HIS   A CG    1 
ATOM   1219 N ND1   . HIS   A 1 171 ? 21.533 12.247  68.505 1.00 57.09  ? 161 HIS   A ND1   1 
ATOM   1220 C CD2   . HIS   A 1 171 ? 19.660 11.667  67.576 1.00 56.35  ? 161 HIS   A CD2   1 
ATOM   1221 C CE1   . HIS   A 1 171 ? 20.941 11.381  69.318 1.00 57.09  ? 161 HIS   A CE1   1 
ATOM   1222 N NE2   . HIS   A 1 171 ? 19.803 11.016  68.771 1.00 56.04  ? 161 HIS   A NE2   1 
ATOM   1223 N N     . GLN   A 1 172 ? 17.863 14.559  64.810 1.00 58.34  ? 162 GLN   A N     1 
ATOM   1224 C CA    . GLN   A 1 172 ? 16.683 15.362  65.084 1.00 59.60  ? 162 GLN   A CA    1 
ATOM   1225 C C     . GLN   A 1 172 ? 15.797 14.656  66.108 1.00 59.51  ? 162 GLN   A C     1 
ATOM   1226 O O     . GLN   A 1 172 ? 15.223 15.304  66.979 1.00 57.24  ? 162 GLN   A O     1 
ATOM   1227 C CB    . GLN   A 1 172 ? 15.902 15.600  63.789 1.00 58.65  ? 162 GLN   A CB    1 
ATOM   1228 C CG    . GLN   A 1 172 ? 14.982 16.815  63.824 1.00 58.79  ? 162 GLN   A CG    1 
ATOM   1229 C CD    . GLN   A 1 172 ? 15.735 18.110  64.029 1.00 59.99  ? 162 GLN   A CD    1 
ATOM   1230 O OE1   . GLN   A 1 172 ? 16.869 18.271  63.568 1.00 62.78  ? 162 GLN   A OE1   1 
ATOM   1231 N NE2   . GLN   A 1 172 ? 15.131 19.038  64.755 1.00 60.63  ? 162 GLN   A NE2   1 
ATOM   1232 N N     . HIS   A 1 173 ? 15.689 13.328  65.975 1.00 62.44  ? 163 HIS   A N     1 
ATOM   1233 C CA    . HIS   A 1 173 ? 14.813 12.512  66.800 1.00 63.59  ? 163 HIS   A CA    1 
ATOM   1234 C C     . HIS   A 1 173 ? 15.666 11.450  67.492 1.00 66.02  ? 163 HIS   A C     1 
ATOM   1235 O O     . HIS   A 1 173 ? 16.695 11.785  68.069 1.00 65.09  ? 163 HIS   A O     1 
ATOM   1236 C CB    . HIS   A 1 173 ? 13.620 12.044  65.956 1.00 63.29  ? 163 HIS   A CB    1 
ATOM   1237 C CG    . HIS   A 1 173 ? 12.737 13.178  65.551 1.00 64.46  ? 163 HIS   A CG    1 
ATOM   1238 N ND1   . HIS   A 1 173 ? 12.333 14.149  66.447 1.00 63.46  ? 163 HIS   A ND1   1 
ATOM   1239 C CD2   . HIS   A 1 173 ? 12.179 13.504  64.376 1.00 65.19  ? 163 HIS   A CD2   1 
ATOM   1240 C CE1   . HIS   A 1 173 ? 11.570 15.034  65.822 1.00 63.42  ? 163 HIS   A CE1   1 
ATOM   1241 N NE2   . HIS   A 1 173 ? 11.464 14.665  64.562 1.00 64.81  ? 163 HIS   A NE2   1 
ATOM   1242 N N     . ASP   A 1 174 ? 15.249 10.180  67.426 1.00 71.67  ? 164 ASP   A N     1 
ATOM   1243 C CA    . ASP   A 1 174 ? 15.814 9.144   68.278 1.00 76.11  ? 164 ASP   A CA    1 
ATOM   1244 C C     . ASP   A 1 174 ? 16.970 8.432   67.578 1.00 73.36  ? 164 ASP   A C     1 
ATOM   1245 O O     . ASP   A 1 174 ? 17.883 7.958   68.248 1.00 77.18  ? 164 ASP   A O     1 
ATOM   1246 C CB    . ASP   A 1 174 ? 14.729 8.209   68.792 1.00 80.77  ? 164 ASP   A CB    1 
ATOM   1247 C CG    . ASP   A 1 174 ? 13.720 8.867   69.725 1.00 87.06  ? 164 ASP   A CG    1 
ATOM   1248 O OD1   . ASP   A 1 174 ? 14.155 9.416   70.763 1.00 92.98  ? 164 ASP   A OD1   1 
ATOM   1249 O OD2   . ASP   A 1 174 ? 12.511 8.849   69.402 1.00 88.33  ? 164 ASP   A OD2   1 
ATOM   1250 N N     . LYS   A 1 175 ? 16.931 8.357   66.242 1.00 69.69  ? 165 LYS   A N     1 
ATOM   1251 C CA    . LYS   A 1 175 ? 17.982 7.702   65.482 1.00 68.60  ? 165 LYS   A CA    1 
ATOM   1252 C C     . LYS   A 1 175 ? 18.986 8.750   65.004 1.00 64.33  ? 165 LYS   A C     1 
ATOM   1253 O O     . LYS   A 1 175 ? 18.632 9.908   64.806 1.00 65.58  ? 165 LYS   A O     1 
ATOM   1254 C CB    . LYS   A 1 175 ? 17.378 6.916   64.311 1.00 72.17  ? 165 LYS   A CB    1 
ATOM   1255 C CG    . LYS   A 1 175 ? 18.341 5.943   63.630 1.00 76.41  ? 165 LYS   A CG    1 
ATOM   1256 C CD    . LYS   A 1 175 ? 17.879 5.359   62.299 1.00 78.20  ? 165 LYS   A CD    1 
ATOM   1257 C CE    . LYS   A 1 175 ? 16.704 4.451   62.431 1.00 79.60  ? 165 LYS   A CE    1 
ATOM   1258 N NZ    . LYS   A 1 175 ? 16.485 3.715   61.185 1.00 81.44  ? 165 LYS   A NZ    1 
ATOM   1259 N N     . TYR   A 1 176 ? 20.243 8.330   64.817 1.00 61.11  ? 166 TYR   A N     1 
ATOM   1260 C CA    . TYR   A 1 176 ? 21.277 9.197   64.282 1.00 57.05  ? 166 TYR   A CA    1 
ATOM   1261 C C     . TYR   A 1 176 ? 22.171 8.424   63.316 1.00 56.89  ? 166 TYR   A C     1 
ATOM   1262 O O     . TYR   A 1 176 ? 22.229 7.194   63.342 1.00 55.88  ? 166 TYR   A O     1 
ATOM   1263 C CB    . TYR   A 1 176 ? 22.132 9.804   65.396 1.00 55.90  ? 166 TYR   A CB    1 
ATOM   1264 C CG    . TYR   A 1 176 ? 23.140 8.881   66.067 1.00 54.48  ? 166 TYR   A CG    1 
ATOM   1265 C CD1   . TYR   A 1 176 ? 22.781 8.098   67.157 1.00 54.22  ? 166 TYR   A CD1   1 
ATOM   1266 C CD2   . TYR   A 1 176 ? 24.465 8.832   65.647 1.00 53.77  ? 166 TYR   A CD2   1 
ATOM   1267 C CE1   . TYR   A 1 176 ? 23.698 7.274   67.788 1.00 54.10  ? 166 TYR   A CE1   1 
ATOM   1268 C CE2   . TYR   A 1 176 ? 25.394 8.016   66.272 1.00 53.14  ? 166 TYR   A CE2   1 
ATOM   1269 C CZ    . TYR   A 1 176 ? 25.010 7.237   67.350 1.00 53.98  ? 166 TYR   A CZ    1 
ATOM   1270 O OH    . TYR   A 1 176 ? 25.919 6.430   67.975 1.00 54.07  ? 166 TYR   A OH    1 
ATOM   1271 N N     . ARG   A 1 177 ? 22.879 9.190   62.478 1.00 56.90  ? 167 ARG   A N     1 
ATOM   1272 C CA    . ARG   A 1 177 ? 23.870 8.669   61.553 1.00 55.74  ? 167 ARG   A CA    1 
ATOM   1273 C C     . ARG   A 1 177 ? 25.204 9.307   61.920 1.00 53.02  ? 167 ARG   A C     1 
ATOM   1274 O O     . ARG   A 1 177 ? 25.327 10.534  61.922 1.00 52.07  ? 167 ARG   A O     1 
ATOM   1275 C CB    . ARG   A 1 177 ? 23.419 8.957   60.115 1.00 58.37  ? 167 ARG   A CB    1 
ATOM   1276 C CG    . ARG   A 1 177 ? 24.360 8.492   59.013 1.00 61.10  ? 167 ARG   A CG    1 
ATOM   1277 C CD    . ARG   A 1 177 ? 23.660 8.388   57.657 1.00 63.80  ? 167 ARG   A CD    1 
ATOM   1278 N NE    . ARG   A 1 177 ? 24.549 7.939   56.575 1.00 66.68  ? 167 ARG   A NE    1 
ATOM   1279 C CZ    . ARG   A 1 177 ? 25.139 6.742   56.504 1.00 68.94  ? 167 ARG   A CZ    1 
ATOM   1280 N NH1   . ARG   A 1 177 ? 24.911 5.842   57.442 1.00 68.90  ? 167 ARG   A NH1   1 
ATOM   1281 N NH2   . ARG   A 1 177 ? 25.950 6.436   55.500 1.00 68.65  ? 167 ARG   A NH2   1 
ATOM   1282 N N     . TYR   A 1 178 ? 26.181 8.462   62.262 1.00 50.55  ? 168 TYR   A N     1 
ATOM   1283 C CA    . TYR   A 1 178 ? 27.427 8.927   62.847 1.00 49.87  ? 168 TYR   A CA    1 
ATOM   1284 C C     . TYR   A 1 178 ? 28.344 9.464   61.750 1.00 50.44  ? 168 TYR   A C     1 
ATOM   1285 O O     . TYR   A 1 178 ? 28.738 8.723   60.856 1.00 52.39  ? 168 TYR   A O     1 
ATOM   1286 C CB    . TYR   A 1 178 ? 28.054 7.765   63.624 1.00 49.21  ? 168 TYR   A CB    1 
ATOM   1287 C CG    . TYR   A 1 178 ? 29.104 8.127   64.668 1.00 49.28  ? 168 TYR   A CG    1 
ATOM   1288 C CD1   . TYR   A 1 178 ? 29.185 9.405   65.216 1.00 48.33  ? 168 TYR   A CD1   1 
ATOM   1289 C CD2   . TYR   A 1 178 ? 30.004 7.170   65.133 1.00 49.05  ? 168 TYR   A CD2   1 
ATOM   1290 C CE1   . TYR   A 1 178 ? 30.133 9.719   66.175 1.00 48.41  ? 168 TYR   A CE1   1 
ATOM   1291 C CE2   . TYR   A 1 178 ? 30.965 7.477   66.084 1.00 48.56  ? 168 TYR   A CE2   1 
ATOM   1292 C CZ    . TYR   A 1 178 ? 31.022 8.754   66.611 1.00 48.99  ? 168 TYR   A CZ    1 
ATOM   1293 O OH    . TYR   A 1 178 ? 31.948 9.076   67.552 1.00 51.55  ? 168 TYR   A OH    1 
ATOM   1294 N N     . ASP   A 1 179 ? 28.661 10.762  61.827 1.00 51.03  ? 169 ASP   A N     1 
ATOM   1295 C CA    . ASP   A 1 179 ? 29.629 11.399  60.946 1.00 51.04  ? 169 ASP   A CA    1 
ATOM   1296 C C     . ASP   A 1 179 ? 30.659 12.100  61.834 1.00 49.96  ? 169 ASP   A C     1 
ATOM   1297 O O     . ASP   A 1 179 ? 30.700 11.858  63.038 1.00 52.90  ? 169 ASP   A O     1 
ATOM   1298 C CB    . ASP   A 1 179 ? 28.932 12.296  59.928 1.00 51.43  ? 169 ASP   A CB    1 
ATOM   1299 C CG    . ASP   A 1 179 ? 29.660 12.497  58.602 1.00 51.73  ? 169 ASP   A CG    1 
ATOM   1300 O OD1   . ASP   A 1 179 ? 30.814 12.971  58.637 1.00 51.37  ? 169 ASP   A OD1   1 
ATOM   1301 O OD2   . ASP   A 1 179 ? 29.069 12.178  57.542 1.00 51.08  ? 169 ASP   A OD2   1 
ATOM   1302 N N     . ARG   A 1 180 ? 31.498 12.952  61.236 1.00 48.18  ? 170 ARG   A N     1 
ATOM   1303 C CA    . ARG   A 1 180 ? 32.438 13.776  61.977 1.00 47.53  ? 170 ARG   A CA    1 
ATOM   1304 C C     . ARG   A 1 180 ? 32.164 15.240  61.670 1.00 48.07  ? 170 ARG   A C     1 
ATOM   1305 O O     . ARG   A 1 180 ? 31.579 15.554  60.635 1.00 50.98  ? 170 ARG   A O     1 
ATOM   1306 C CB    . ARG   A 1 180 ? 33.886 13.450  61.608 1.00 47.26  ? 170 ARG   A CB    1 
ATOM   1307 C CG    . ARG   A 1 180 ? 34.244 12.010  61.933 1.00 48.78  ? 170 ARG   A CG    1 
ATOM   1308 C CD    . ARG   A 1 180 ? 35.580 11.672  61.322 1.00 50.15  ? 170 ARG   A CD    1 
ATOM   1309 N NE    . ARG   A 1 180 ? 36.648 12.453  61.953 1.00 50.54  ? 170 ARG   A NE    1 
ATOM   1310 C CZ    . ARG   A 1 180 ? 37.878 12.548  61.484 1.00 50.59  ? 170 ARG   A CZ    1 
ATOM   1311 N NH1   . ARG   A 1 180 ? 38.194 11.964  60.341 1.00 51.11  ? 170 ARG   A NH1   1 
ATOM   1312 N NH2   . ARG   A 1 180 ? 38.784 13.234  62.154 1.00 51.47  ? 170 ARG   A NH2   1 
ATOM   1313 N N     . TYR   A 1 181 ? 32.617 16.122  62.566 1.00 48.39  ? 171 TYR   A N     1 
ATOM   1314 C CA    . TYR   A 1 181 ? 32.194 17.510  62.542 1.00 48.99  ? 171 TYR   A CA    1 
ATOM   1315 C C     . TYR   A 1 181 ? 33.357 18.394  62.981 1.00 49.97  ? 171 TYR   A C     1 
ATOM   1316 O O     . TYR   A 1 181 ? 33.750 18.365  64.143 1.00 50.76  ? 171 TYR   A O     1 
ATOM   1317 C CB    . TYR   A 1 181 ? 30.955 17.631  63.435 1.00 48.96  ? 171 TYR   A CB    1 
ATOM   1318 C CG    . TYR   A 1 181 ? 30.043 16.409  63.415 1.00 50.82  ? 171 TYR   A CG    1 
ATOM   1319 C CD1   . TYR   A 1 181 ? 29.113 16.218  62.402 1.00 50.45  ? 171 TYR   A CD1   1 
ATOM   1320 C CD2   . TYR   A 1 181 ? 30.126 15.433  64.407 1.00 52.02  ? 171 TYR   A CD2   1 
ATOM   1321 C CE1   . TYR   A 1 181 ? 28.285 15.107  62.380 1.00 51.44  ? 171 TYR   A CE1   1 
ATOM   1322 C CE2   . TYR   A 1 181 ? 29.311 14.312  64.392 1.00 51.22  ? 171 TYR   A CE2   1 
ATOM   1323 C CZ    . TYR   A 1 181 ? 28.386 14.152  63.377 1.00 51.94  ? 171 TYR   A CZ    1 
ATOM   1324 O OH    . TYR   A 1 181 ? 27.579 13.054  63.357 1.00 52.99  ? 171 TYR   A OH    1 
ATOM   1325 N N     . HIS   A 1 182 ? 33.898 19.179  62.041 1.00 50.48  ? 172 HIS   A N     1 
ATOM   1326 C CA    . HIS   A 1 182 ? 34.983 20.101  62.336 1.00 50.93  ? 172 HIS   A CA    1 
ATOM   1327 C C     . HIS   A 1 182 ? 34.612 21.490  61.828 1.00 52.04  ? 172 HIS   A C     1 
ATOM   1328 O O     . HIS   A 1 182 ? 34.242 21.652  60.668 1.00 52.37  ? 172 HIS   A O     1 
ATOM   1329 C CB    . HIS   A 1 182 ? 36.300 19.607  61.727 1.00 49.90  ? 172 HIS   A CB    1 
ATOM   1330 C CG    . HIS   A 1 182 ? 36.687 18.253  62.203 1.00 48.89  ? 172 HIS   A CG    1 
ATOM   1331 N ND1   . HIS   A 1 182 ? 36.275 17.108  61.560 1.00 49.39  ? 172 HIS   A ND1   1 
ATOM   1332 C CD2   . HIS   A 1 182 ? 37.408 17.854  63.253 1.00 49.39  ? 172 HIS   A CD2   1 
ATOM   1333 C CE1   . HIS   A 1 182 ? 36.745 16.054  62.207 1.00 50.03  ? 172 HIS   A CE1   1 
ATOM   1334 N NE2   . HIS   A 1 182 ? 37.438 16.482  63.242 1.00 50.42  ? 172 HIS   A NE2   1 
ATOM   1335 N N     . LEU   A 1 183 ? 34.707 22.482  62.720 1.00 52.24  ? 173 LEU   A N     1 
ATOM   1336 C CA    . LEU   A 1 183 ? 34.576 23.875  62.340 1.00 52.08  ? 173 LEU   A CA    1 
ATOM   1337 C C     . LEU   A 1 183 ? 35.969 24.490  62.290 1.00 53.64  ? 173 LEU   A C     1 
ATOM   1338 O O     . LEU   A 1 183 ? 36.716 24.412  63.267 1.00 52.88  ? 173 LEU   A O     1 
ATOM   1339 C CB    . LEU   A 1 183 ? 33.684 24.617  63.328 1.00 52.37  ? 173 LEU   A CB    1 
ATOM   1340 C CG    . LEU   A 1 183 ? 33.572 26.127  63.102 1.00 52.87  ? 173 LEU   A CG    1 
ATOM   1341 C CD1   . LEU   A 1 183 ? 32.821 26.413  61.814 1.00 53.02  ? 173 LEU   A CD1   1 
ATOM   1342 C CD2   . LEU   A 1 183 ? 32.913 26.814  64.287 1.00 53.08  ? 173 LEU   A CD2   1 
ATOM   1343 N N     . ILE   A 1 184 ? 36.296 25.108  61.147 1.00 53.95  ? 174 ILE   A N     1 
ATOM   1344 C CA    . ILE   A 1 184 ? 37.588 25.736  60.946 1.00 53.52  ? 174 ILE   A CA    1 
ATOM   1345 C C     . ILE   A 1 184 ? 37.362 27.177  60.486 1.00 55.52  ? 174 ILE   A C     1 
ATOM   1346 O O     . ILE   A 1 184 ? 36.884 27.417  59.376 1.00 55.08  ? 174 ILE   A O     1 
ATOM   1347 C CB    . ILE   A 1 184 ? 38.438 24.906  59.963 1.00 54.04  ? 174 ILE   A CB    1 
ATOM   1348 C CG1   . ILE   A 1 184 ? 38.727 23.501  60.521 1.00 54.62  ? 174 ILE   A CG1   1 
ATOM   1349 C CG2   . ILE   A 1 184 ? 39.733 25.635  59.599 1.00 54.13  ? 174 ILE   A CG2   1 
ATOM   1350 C CD1   . ILE   A 1 184 ? 39.185 22.490  59.485 1.00 54.64  ? 174 ILE   A CD1   1 
ATOM   1351 N N     . ARG   A 1 185 ? 37.689 28.131  61.370 1.00 57.20  ? 175 ARG   A N     1 
ATOM   1352 C CA    . ARG   A 1 185 ? 37.739 29.537  61.007 1.00 59.18  ? 175 ARG   A CA    1 
ATOM   1353 C C     . ARG   A 1 185 ? 39.068 29.780  60.299 1.00 57.92  ? 175 ARG   A C     1 
ATOM   1354 O O     . ARG   A 1 185 ? 40.127 29.623  60.901 1.00 54.49  ? 175 ARG   A O     1 
ATOM   1355 C CB    . ARG   A 1 185 ? 37.566 30.463  62.218 1.00 62.64  ? 175 ARG   A CB    1 
ATOM   1356 C CG    . ARG   A 1 185 ? 37.545 31.943  61.855 1.00 67.32  ? 175 ARG   A CG    1 
ATOM   1357 C CD    . ARG   A 1 185 ? 37.709 32.898  63.030 1.00 70.21  ? 175 ARG   A CD    1 
ATOM   1358 N NE    . ARG   A 1 185 ? 36.572 32.880  63.956 1.00 76.53  ? 175 ARG   A NE    1 
ATOM   1359 C CZ    . ARG   A 1 185 ? 35.357 33.368  63.700 1.00 80.60  ? 175 ARG   A CZ    1 
ATOM   1360 N NH1   . ARG   A 1 185 ? 35.107 33.932  62.531 1.00 83.36  ? 175 ARG   A NH1   1 
ATOM   1361 N NH2   . ARG   A 1 185 ? 34.398 33.301  64.613 1.00 77.28  ? 175 ARG   A NH2   1 
ATOM   1362 N N     . ASN   A 1 186 ? 38.989 30.116  59.006 1.00 59.57  ? 176 ASN   A N     1 
ATOM   1363 C CA    . ASN   A 1 186 ? 40.155 30.398  58.185 1.00 59.26  ? 176 ASN   A CA    1 
ATOM   1364 C C     . ASN   A 1 186 ? 39.692 31.201  56.977 1.00 60.33  ? 176 ASN   A C     1 
ATOM   1365 O O     . ASN   A 1 186 ? 39.098 30.641  56.058 1.00 61.21  ? 176 ASN   A O     1 
ATOM   1366 C CB    . ASN   A 1 186 ? 40.874 29.120  57.764 1.00 60.91  ? 176 ASN   A CB    1 
ATOM   1367 C CG    . ASN   A 1 186 ? 42.241 29.383  57.169 1.00 60.91  ? 176 ASN   A CG    1 
ATOM   1368 O OD1   . ASN   A 1 186 ? 42.367 30.105  56.170 1.00 58.82  ? 176 ASN   A OD1   1 
ATOM   1369 N ND2   . ASN   A 1 186 ? 43.277 28.803  57.763 1.00 59.03  ? 176 ASN   A ND2   1 
ATOM   1370 N N     . ARG   A 1 187 ? 39.950 32.513  57.013 1.00 61.74  ? 177 ARG   A N     1 
ATOM   1371 C CA    . ARG   A 1 187 ? 39.554 33.431  55.956 1.00 63.66  ? 177 ARG   A CA    1 
ATOM   1372 C C     . ARG   A 1 187 ? 40.014 32.894  54.599 1.00 63.65  ? 177 ARG   A C     1 
ATOM   1373 O O     . ARG   A 1 187 ? 39.201 32.736  53.686 1.00 61.51  ? 177 ARG   A O     1 
ATOM   1374 C CB    . ARG   A 1 187 ? 40.095 34.834  56.278 1.00 65.49  ? 177 ARG   A CB    1 
ATOM   1375 C CG    . ARG   A 1 187 ? 40.019 35.894  55.184 1.00 67.22  ? 177 ARG   A CG    1 
ATOM   1376 C CD    . ARG   A 1 187 ? 38.631 36.065  54.578 1.00 69.99  ? 177 ARG   A CD    1 
ATOM   1377 N NE    . ARG   A 1 187 ? 37.634 36.530  55.548 1.00 73.47  ? 177 ARG   A NE    1 
ATOM   1378 C CZ    . ARG   A 1 187 ? 36.319 36.561  55.349 1.00 74.66  ? 177 ARG   A CZ    1 
ATOM   1379 N NH1   . ARG   A 1 187 ? 35.794 36.138  54.210 1.00 74.69  ? 177 ARG   A NH1   1 
ATOM   1380 N NH2   . ARG   A 1 187 ? 35.528 37.008  56.306 1.00 75.14  ? 177 ARG   A NH2   1 
ATOM   1381 N N     . LYS   A 1 188 ? 41.314 32.593  54.483 1.00 64.34  ? 178 LYS   A N     1 
ATOM   1382 C CA    . LYS   A 1 188 ? 41.914 32.247  53.202 1.00 65.63  ? 178 LYS   A CA    1 
ATOM   1383 C C     . LYS   A 1 188 ? 41.328 30.951  52.642 1.00 65.03  ? 178 LYS   A C     1 
ATOM   1384 O O     . LYS   A 1 188 ? 41.046 30.875  51.449 1.00 65.48  ? 178 LYS   A O     1 
ATOM   1385 C CB    . LYS   A 1 188 ? 43.435 32.127  53.316 1.00 67.90  ? 178 LYS   A CB    1 
ATOM   1386 C CG    . LYS   A 1 188 ? 44.141 31.946  51.983 1.00 71.48  ? 178 LYS   A CG    1 
ATOM   1387 C CD    . LYS   A 1 188 ? 45.655 32.080  52.090 1.00 74.45  ? 178 LYS   A CD    1 
ATOM   1388 C CE    . LYS   A 1 188 ? 46.354 31.841  50.789 1.00 74.26  ? 178 LYS   A CE    1 
ATOM   1389 N NZ    . LYS   A 1 188 ? 47.805 31.894  50.988 1.00 74.00  ? 178 LYS   A NZ    1 
ATOM   1390 N N     . MET   A 1 189 ? 41.142 29.942  53.506 1.00 64.89  ? 179 MET   A N     1 
ATOM   1391 C CA    . MET   A 1 189 ? 40.680 28.631  53.075 1.00 62.54  ? 179 MET   A CA    1 
ATOM   1392 C C     . MET   A 1 189 ? 39.220 28.696  52.643 1.00 62.55  ? 179 MET   A C     1 
ATOM   1393 O O     . MET   A 1 189 ? 38.848 28.098  51.636 1.00 62.74  ? 179 MET   A O     1 
ATOM   1394 C CB    . MET   A 1 189 ? 40.785 27.583  54.188 1.00 61.40  ? 179 MET   A CB    1 
ATOM   1395 C CG    . MET   A 1 189 ? 40.407 26.191  53.723 1.00 61.36  ? 179 MET   A CG    1 
ATOM   1396 S SD    . MET   A 1 189 ? 40.667 24.916  54.969 1.00 59.42  ? 179 MET   A SD    1 
ATOM   1397 C CE    . MET   A 1 189 ? 39.186 25.157  55.957 1.00 59.89  ? 179 MET   A CE    1 
ATOM   1398 N N     . SER   A 1 190 ? 38.398 29.391  53.439 1.00 61.70  ? 180 SER   A N     1 
ATOM   1399 C CA    . SER   A 1 190 ? 36.971 29.472  53.178 1.00 60.70  ? 180 SER   A CA    1 
ATOM   1400 C C     . SER   A 1 190 ? 36.729 30.269  51.901 1.00 58.18  ? 180 SER   A C     1 
ATOM   1401 O O     . SER   A 1 190 ? 35.862 29.917  51.108 1.00 55.08  ? 180 SER   A O     1 
ATOM   1402 C CB    . SER   A 1 190 ? 36.228 30.052  54.353 1.00 60.50  ? 180 SER   A CB    1 
ATOM   1403 O OG    . SER   A 1 190 ? 36.816 31.273  54.776 1.00 62.20  ? 180 SER   A OG    1 
ATOM   1404 N N     . ASP   A 1 191 ? 37.518 31.332  51.715 1.00 59.63  ? 181 ASP   A N     1 
ATOM   1405 C CA    . ASP   A 1 191 ? 37.495 32.109  50.487 1.00 60.03  ? 181 ASP   A CA    1 
ATOM   1406 C C     . ASP   A 1 191 ? 37.802 31.188  49.311 1.00 60.43  ? 181 ASP   A C     1 
ATOM   1407 O O     . ASP   A 1 191 ? 37.052 31.167  48.341 1.00 61.05  ? 181 ASP   A O     1 
ATOM   1408 C CB    . ASP   A 1 191 ? 38.450 33.294  50.543 1.00 60.38  ? 181 ASP   A CB    1 
ATOM   1409 C CG    . ASP   A 1 191 ? 37.947 34.541  51.260 1.00 61.24  ? 181 ASP   A CG    1 
ATOM   1410 O OD1   . ASP   A 1 191 ? 36.804 34.530  51.770 1.00 59.74  ? 181 ASP   A OD1   1 
ATOM   1411 O OD2   . ASP   A 1 191 ? 38.703 35.531  51.291 1.00 64.45  ? 181 ASP   A OD2   1 
ATOM   1412 N N     . ILE   A 1 192 ? 38.890 30.413  49.417 1.00 61.00  ? 182 ILE   A N     1 
ATOM   1413 C CA    . ILE   A 1 192 ? 39.307 29.521  48.344 1.00 60.51  ? 182 ILE   A CA    1 
ATOM   1414 C C     . ILE   A 1 192 ? 38.183 28.542  48.025 1.00 59.97  ? 182 ILE   A C     1 
ATOM   1415 O O     . ILE   A 1 192 ? 37.886 28.306  46.858 1.00 65.24  ? 182 ILE   A O     1 
ATOM   1416 C CB    . ILE   A 1 192 ? 40.614 28.785  48.693 1.00 61.75  ? 182 ILE   A CB    1 
ATOM   1417 C CG1   . ILE   A 1 192 ? 41.814 29.731  48.671 1.00 61.07  ? 182 ILE   A CG1   1 
ATOM   1418 C CG2   . ILE   A 1 192 ? 40.829 27.592  47.761 1.00 62.33  ? 182 ILE   A CG2   1 
ATOM   1419 C CD1   . ILE   A 1 192 ? 43.024 29.214  49.426 1.00 61.68  ? 182 ILE   A CD1   1 
ATOM   1420 N N     . MET   A 1 193 ? 37.566 27.971  49.060 1.00 59.99  ? 183 MET   A N     1 
ATOM   1421 C CA    . MET   A 1 193 ? 36.509 26.994  48.856 1.00 61.06  ? 183 MET   A CA    1 
ATOM   1422 C C     . MET   A 1 193 ? 35.257 27.674  48.301 1.00 61.12  ? 183 MET   A C     1 
ATOM   1423 O O     . MET   A 1 193 ? 34.629 27.139  47.394 1.00 61.23  ? 183 MET   A O     1 
ATOM   1424 C CB    . MET   A 1 193 ? 36.197 26.229  50.148 1.00 61.57  ? 183 MET   A CB    1 
ATOM   1425 C CG    . MET   A 1 193 ? 37.260 25.208  50.521 1.00 60.45  ? 183 MET   A CG    1 
ATOM   1426 S SD    . MET   A 1 193 ? 36.935 24.315  52.054 1.00 56.75  ? 183 MET   A SD    1 
ATOM   1427 C CE    . MET   A 1 193 ? 35.441 23.414  51.620 1.00 55.67  ? 183 MET   A CE    1 
ATOM   1428 N N     . PHE   A 1 194 ? 34.905 28.852  48.834 1.00 62.26  ? 184 PHE   A N     1 
ATOM   1429 C CA    . PHE   A 1 194 ? 33.695 29.552  48.421 1.00 63.93  ? 184 PHE   A CA    1 
ATOM   1430 C C     . PHE   A 1 194 ? 33.800 29.951  46.947 1.00 64.63  ? 184 PHE   A C     1 
ATOM   1431 O O     . PHE   A 1 194 ? 32.869 29.725  46.179 1.00 63.89  ? 184 PHE   A O     1 
ATOM   1432 C CB    . PHE   A 1 194 ? 33.407 30.778  49.300 1.00 63.81  ? 184 PHE   A CB    1 
ATOM   1433 C CG    . PHE   A 1 194 ? 32.137 31.531  48.921 1.00 63.14  ? 184 PHE   A CG    1 
ATOM   1434 C CD1   . PHE   A 1 194 ? 30.894 31.126  49.398 1.00 62.18  ? 184 PHE   A CD1   1 
ATOM   1435 C CD2   . PHE   A 1 194 ? 32.186 32.638  48.077 1.00 62.44  ? 184 PHE   A CD2   1 
ATOM   1436 C CE1   . PHE   A 1 194 ? 29.738 31.806  49.041 1.00 61.12  ? 184 PHE   A CE1   1 
ATOM   1437 C CE2   . PHE   A 1 194 ? 31.027 33.311  47.723 1.00 61.10  ? 184 PHE   A CE2   1 
ATOM   1438 C CZ    . PHE   A 1 194 ? 29.806 32.891  48.203 1.00 60.78  ? 184 PHE   A CZ    1 
ATOM   1439 N N     . GLU   A 1 195 ? 34.935 30.548  46.564 1.00 68.54  ? 185 GLU   A N     1 
ATOM   1440 C CA    . GLU   A 1 195 ? 35.147 31.044  45.210 1.00 71.33  ? 185 GLU   A CA    1 
ATOM   1441 C C     . GLU   A 1 195 ? 35.142 29.884  44.214 1.00 71.31  ? 185 GLU   A C     1 
ATOM   1442 O O     . GLU   A 1 195 ? 34.536 29.994  43.150 1.00 70.98  ? 185 GLU   A O     1 
ATOM   1443 C CB    . GLU   A 1 195 ? 36.462 31.820  45.103 1.00 72.88  ? 185 GLU   A CB    1 
ATOM   1444 C CG    . GLU   A 1 195 ? 36.445 33.176  45.809 1.00 74.79  ? 185 GLU   A CG    1 
ATOM   1445 C CD    . GLU   A 1 195 ? 37.824 33.723  46.157 1.00 77.83  ? 185 GLU   A CD    1 
ATOM   1446 O OE1   . GLU   A 1 195 ? 38.821 33.041  45.833 1.00 83.92  ? 185 GLU   A OE1   1 
ATOM   1447 O OE2   . GLU   A 1 195 ? 37.922 34.813  46.765 1.00 77.03  ? 185 GLU   A OE2   1 
ATOM   1448 N N     . TRP   A 1 196 ? 35.826 28.783  44.569 1.00 70.39  ? 186 TRP   A N     1 
ATOM   1449 C CA    . TRP   A 1 196 ? 35.859 27.589  43.736 1.00 68.32  ? 186 TRP   A CA    1 
ATOM   1450 C C     . TRP   A 1 196 ? 34.438 27.121  43.437 1.00 66.45  ? 186 TRP   A C     1 
ATOM   1451 O O     . TRP   A 1 196 ? 34.123 26.791  42.299 1.00 64.74  ? 186 TRP   A O     1 
ATOM   1452 C CB    . TRP   A 1 196 ? 36.670 26.463  44.399 1.00 67.50  ? 186 TRP   A CB    1 
ATOM   1453 C CG    . TRP   A 1 196 ? 36.937 25.289  43.487 1.00 65.82  ? 186 TRP   A CG    1 
ATOM   1454 C CD1   . TRP   A 1 196 ? 38.100 25.031  42.825 1.00 64.46  ? 186 TRP   A CD1   1 
ATOM   1455 C CD2   . TRP   A 1 196 ? 36.022 24.230  43.114 1.00 63.82  ? 186 TRP   A CD2   1 
ATOM   1456 N NE1   . TRP   A 1 196 ? 37.981 23.889  42.079 1.00 64.23  ? 186 TRP   A NE1   1 
ATOM   1457 C CE2   . TRP   A 1 196 ? 36.720 23.380  42.229 1.00 63.84  ? 186 TRP   A CE2   1 
ATOM   1458 C CE3   . TRP   A 1 196 ? 34.695 23.915  43.434 1.00 63.65  ? 186 TRP   A CE3   1 
ATOM   1459 C CZ2   . TRP   A 1 196 ? 36.135 22.242  41.671 1.00 64.47  ? 186 TRP   A CZ2   1 
ATOM   1460 C CZ3   . TRP   A 1 196 ? 34.117 22.795  42.877 1.00 63.31  ? 186 TRP   A CZ3   1 
ATOM   1461 C CH2   . TRP   A 1 196 ? 34.829 21.968  42.010 1.00 63.73  ? 186 TRP   A CH2   1 
ATOM   1462 N N     . VAL   A 1 197 ? 33.591 27.081  44.471 1.00 68.11  ? 187 VAL   A N     1 
ATOM   1463 C CA    . VAL   A 1 197 ? 32.212 26.651  44.310 1.00 70.52  ? 187 VAL   A CA    1 
ATOM   1464 C C     . VAL   A 1 197 ? 31.502 27.611  43.360 1.00 72.71  ? 187 VAL   A C     1 
ATOM   1465 O O     . VAL   A 1 197 ? 30.741 27.169  42.504 1.00 73.37  ? 187 VAL   A O     1 
ATOM   1466 C CB    . VAL   A 1 197 ? 31.464 26.533  45.653 1.00 70.06  ? 187 VAL   A CB    1 
ATOM   1467 C CG1   . VAL   A 1 197 ? 29.973 26.276  45.460 1.00 69.44  ? 187 VAL   A CG1   1 
ATOM   1468 C CG2   . VAL   A 1 197 ? 32.069 25.449  46.537 1.00 71.29  ? 187 VAL   A CG2   1 
ATOM   1469 N N     . THR   A 1 198 ? 31.761 28.917  43.519 1.00 75.09  ? 188 THR   A N     1 
ATOM   1470 C CA    . THR   A 1 198 ? 31.126 29.940  42.701 1.00 75.75  ? 188 THR   A CA    1 
ATOM   1471 C C     . THR   A 1 198 ? 31.578 29.773  41.248 1.00 73.05  ? 188 THR   A C     1 
ATOM   1472 O O     . THR   A 1 198 ? 30.753 29.690  40.341 1.00 69.80  ? 188 THR   A O     1 
ATOM   1473 C CB    . THR   A 1 198 ? 31.438 31.336  43.252 1.00 76.67  ? 188 THR   A CB    1 
ATOM   1474 O OG1   . THR   A 1 198 ? 31.143 31.357  44.646 1.00 75.59  ? 188 THR   A OG1   1 
ATOM   1475 C CG2   . THR   A 1 198 ? 30.599 32.424  42.604 1.00 77.43  ? 188 THR   A CG2   1 
ATOM   1476 N N     . GLN   A 1 199 ? 32.895 29.688  41.037 1.00 73.23  ? 189 GLN   A N     1 
ATOM   1477 C CA    . GLN   A 1 199 ? 33.462 29.658  39.696 1.00 74.24  ? 189 GLN   A CA    1 
ATOM   1478 C C     . GLN   A 1 199 ? 33.146 28.349  38.969 1.00 72.80  ? 189 GLN   A C     1 
ATOM   1479 O O     . GLN   A 1 199 ? 32.821 28.378  37.787 1.00 74.15  ? 189 GLN   A O     1 
ATOM   1480 C CB    . GLN   A 1 199 ? 34.973 29.903  39.734 1.00 76.48  ? 189 GLN   A CB    1 
ATOM   1481 C CG    . GLN   A 1 199 ? 35.353 31.367  39.933 1.00 78.91  ? 189 GLN   A CG    1 
ATOM   1482 C CD    . GLN   A 1 199 ? 34.873 32.279  38.820 1.00 82.71  ? 189 GLN   A CD    1 
ATOM   1483 O OE1   . GLN   A 1 199 ? 34.604 31.853  37.689 1.00 84.06  ? 189 GLN   A OE1   1 
ATOM   1484 N NE2   . GLN   A 1 199 ? 34.779 33.564  39.126 1.00 83.94  ? 189 GLN   A NE2   1 
ATOM   1485 N N     . ASN   A 1 200 ? 33.245 27.205  39.656 1.00 73.29  ? 190 ASN   A N     1 
ATOM   1486 C CA    . ASN   A 1 200 ? 33.258 25.919  38.974 1.00 72.94  ? 190 ASN   A CA    1 
ATOM   1487 C C     . ASN   A 1 200 ? 31.892 25.236  39.019 1.00 74.63  ? 190 ASN   A C     1 
ATOM   1488 O O     . ASN   A 1 200 ? 31.628 24.368  38.193 1.00 75.21  ? 190 ASN   A O     1 
ATOM   1489 C CB    . ASN   A 1 200 ? 34.369 25.024  39.510 1.00 71.90  ? 190 ASN   A CB    1 
ATOM   1490 C CG    . ASN   A 1 200 ? 35.734 25.573  39.171 1.00 73.24  ? 190 ASN   A CG    1 
ATOM   1491 O OD1   . ASN   A 1 200 ? 36.184 25.465  38.025 1.00 76.97  ? 190 ASN   A OD1   1 
ATOM   1492 N ND2   . ASN   A 1 200 ? 36.413 26.160  40.144 1.00 73.35  ? 190 ASN   A ND2   1 
ATOM   1493 N N     . ILE   A 1 201 ? 31.028 25.610  39.972 1.00 77.95  ? 191 ILE   A N     1 
ATOM   1494 C CA    . ILE   A 1 201 ? 29.716 24.988  40.078 1.00 82.62  ? 191 ILE   A CA    1 
ATOM   1495 C C     . ILE   A 1 201 ? 28.640 26.010  39.709 1.00 89.01  ? 191 ILE   A C     1 
ATOM   1496 O O     . ILE   A 1 201 ? 28.024 25.900  38.653 1.00 93.36  ? 191 ILE   A O     1 
ATOM   1497 C CB    . ILE   A 1 201 ? 29.475 24.387  41.477 1.00 81.73  ? 191 ILE   A CB    1 
ATOM   1498 C CG1   . ILE   A 1 201 ? 30.575 23.409  41.894 1.00 82.64  ? 191 ILE   A CG1   1 
ATOM   1499 C CG2   . ILE   A 1 201 ? 28.099 23.726  41.538 1.00 82.05  ? 191 ILE   A CG2   1 
ATOM   1500 C CD1   . ILE   A 1 201 ? 30.592 22.112  41.103 1.00 83.48  ? 191 ILE   A CD1   1 
ATOM   1501 N N     . MET   A 1 202 ? 28.434 26.999  40.588 1.00 94.52  ? 192 MET   A N     1 
ATOM   1502 C CA    . MET   A 1 202 ? 27.329 27.945  40.498 1.00 96.88  ? 192 MET   A CA    1 
ATOM   1503 C C     . MET   A 1 202 ? 27.043 28.329  39.047 1.00 97.80  ? 192 MET   A C     1 
ATOM   1504 O O     . MET   A 1 202 ? 25.969 28.020  38.531 1.00 94.97  ? 192 MET   A O     1 
ATOM   1505 C CB    . MET   A 1 202 ? 27.640 29.203  41.316 1.00 98.26  ? 192 MET   A CB    1 
ATOM   1506 C CG    . MET   A 1 202 ? 27.373 29.032  42.787 1.00 98.75  ? 192 MET   A CG    1 
ATOM   1507 S SD    . MET   A 1 202 ? 25.597 29.048  43.087 1.00 100.42 ? 192 MET   A SD    1 
ATOM   1508 C CE    . MET   A 1 202 ? 25.356 30.829  43.125 1.00 98.75  ? 192 MET   A CE    1 
ATOM   1509 N N     . ASN   A 1 203 ? 27.996 29.029  38.416 1.00 97.81  ? 193 ASN   A N     1 
ATOM   1510 C CA    . ASN   A 1 203 ? 27.936 29.285  36.984 1.00 99.50  ? 193 ASN   A CA    1 
ATOM   1511 C C     . ASN   A 1 203 ? 28.721 28.177  36.282 1.00 98.83  ? 193 ASN   A C     1 
ATOM   1512 O O     . ASN   A 1 203 ? 29.941 28.085  36.401 1.00 95.85  ? 193 ASN   A O     1 
ATOM   1513 C CB    . ASN   A 1 203 ? 28.349 30.710  36.614 1.00 98.77  ? 193 ASN   A CB    1 
ATOM   1514 C CG    . ASN   A 1 203 ? 29.569 31.202  37.358 1.00 96.69  ? 193 ASN   A CG    1 
ATOM   1515 O OD1   . ASN   A 1 203 ? 30.691 30.770  37.073 1.00 91.92  ? 193 ASN   A OD1   1 
ATOM   1516 N ND2   . ASN   A 1 203 ? 29.377 32.121  38.294 1.00 96.12  ? 193 ASN   A ND2   1 
ATOM   1517 N N     . GLY   A 1 204 ? 27.976 27.327  35.569 1.00 98.34  ? 194 GLY   A N     1 
ATOM   1518 C CA    . GLY   A 1 204 ? 28.489 26.099  34.987 1.00 98.89  ? 194 GLY   A CA    1 
ATOM   1519 C C     . GLY   A 1 204 ? 27.356 25.365  34.277 1.00 101.53 ? 194 GLY   A C     1 
ATOM   1520 O O     . GLY   A 1 204 ? 26.203 25.464  34.691 1.00 100.42 ? 194 GLY   A O     1 
ATOM   1521 N N     . ARG   A 1 205 ? 27.701 24.630  33.215 1.00 103.09 ? 195 ARG   A N     1 
ATOM   1522 C CA    . ARG   A 1 205 ? 26.729 24.192  32.225 1.00 104.81 ? 195 ARG   A CA    1 
ATOM   1523 C C     . ARG   A 1 205 ? 25.571 23.436  32.879 1.00 99.76  ? 195 ARG   A C     1 
ATOM   1524 O O     . ARG   A 1 205 ? 24.407 23.759  32.641 1.00 95.93  ? 195 ARG   A O     1 
ATOM   1525 C CB    . ARG   A 1 205 ? 27.415 23.330  31.157 1.00 109.80 ? 195 ARG   A CB    1 
ATOM   1526 C CG    . ARG   A 1 205 ? 28.482 24.029  30.324 1.00 114.90 ? 195 ARG   A CG    1 
ATOM   1527 C CD    . ARG   A 1 205 ? 27.965 25.227  29.525 1.00 118.15 ? 195 ARG   A CD    1 
ATOM   1528 N NE    . ARG   A 1 205 ? 28.956 25.723  28.562 1.00 120.35 ? 195 ARG   A NE    1 
ATOM   1529 C CZ    . ARG   A 1 205 ? 30.124 26.282  28.872 1.00 121.05 ? 195 ARG   A CZ    1 
ATOM   1530 N NH1   . ARG   A 1 205 ? 30.420 26.574  30.127 1.00 122.23 ? 195 ARG   A NH1   1 
ATOM   1531 N NH2   . ARG   A 1 205 ? 30.995 26.565  27.920 1.00 119.41 ? 195 ARG   A NH2   1 
ATOM   1532 N N     . GLY   A 1 206 ? 25.904 22.441  33.712 1.00 95.29  ? 196 GLY   A N     1 
ATOM   1533 C CA    . GLY   A 1 206 ? 24.943 21.440  34.150 1.00 91.52  ? 196 GLY   A CA    1 
ATOM   1534 C C     . GLY   A 1 206 ? 24.020 21.933  35.262 1.00 87.51  ? 196 GLY   A C     1 
ATOM   1535 O O     . GLY   A 1 206 ? 22.927 21.399  35.435 1.00 85.37  ? 196 GLY   A O     1 
ATOM   1536 N N     . VAL   A 1 207 ? 24.458 22.955  36.005 1.00 86.24  ? 197 VAL   A N     1 
ATOM   1537 C CA    . VAL   A 1 207 ? 23.802 23.349  37.242 1.00 86.29  ? 197 VAL   A CA    1 
ATOM   1538 C C     . VAL   A 1 207 ? 22.483 24.057  36.931 1.00 83.20  ? 197 VAL   A C     1 
ATOM   1539 O O     . VAL   A 1 207 ? 22.463 25.054  36.215 1.00 82.42  ? 197 VAL   A O     1 
ATOM   1540 C CB    . VAL   A 1 207 ? 24.741 24.238  38.080 1.00 88.43  ? 197 VAL   A CB    1 
ATOM   1541 C CG1   . VAL   A 1 207 ? 24.130 24.605  39.429 1.00 88.42  ? 197 VAL   A CG1   1 
ATOM   1542 C CG2   . VAL   A 1 207 ? 26.104 23.580  38.270 1.00 89.28  ? 197 VAL   A CG2   1 
ATOM   1543 N N     . ASN   A 1 208 ? 21.390 23.527  37.491 1.00 82.48  ? 198 ASN   A N     1 
ATOM   1544 C CA    . ASN   A 1 208 ? 20.060 24.088  37.322 1.00 82.58  ? 198 ASN   A CA    1 
ATOM   1545 C C     . ASN   A 1 208 ? 19.381 24.194  38.680 1.00 81.44  ? 198 ASN   A C     1 
ATOM   1546 O O     . ASN   A 1 208 ? 19.751 23.488  39.613 1.00 82.47  ? 198 ASN   A O     1 
ATOM   1547 C CB    . ASN   A 1 208 ? 19.199 23.253  36.382 1.00 85.73  ? 198 ASN   A CB    1 
ATOM   1548 C CG    . ASN   A 1 208 ? 19.670 23.347  34.951 1.00 87.90  ? 198 ASN   A CG    1 
ATOM   1549 O OD1   . ASN   A 1 208 ? 19.052 24.045  34.138 1.00 88.50  ? 198 ASN   A OD1   1 
ATOM   1550 N ND2   . ASN   A 1 208 ? 20.766 22.674  34.635 1.00 87.88  ? 198 ASN   A ND2   1 
ATOM   1551 N N     . ARG   A 1 209 ? 18.363 25.060  38.757 1.00 80.46  ? 199 ARG   A N     1 
ATOM   1552 C CA    . ARG   A 1 209 ? 17.723 25.406  40.015 1.00 78.72  ? 199 ARG   A CA    1 
ATOM   1553 C C     . ARG   A 1 209 ? 16.576 24.440  40.298 1.00 78.54  ? 199 ARG   A C     1 
ATOM   1554 O O     . ARG   A 1 209 ? 15.677 24.275  39.478 1.00 81.61  ? 199 ARG   A O     1 
ATOM   1555 C CB    . ARG   A 1 209 ? 17.285 26.876  40.002 1.00 77.52  ? 199 ARG   A CB    1 
ATOM   1556 C CG    . ARG   A 1 209 ? 18.466 27.822  40.175 1.00 77.08  ? 199 ARG   A CG    1 
ATOM   1557 C CD    . ARG   A 1 209 ? 18.084 29.254  40.508 1.00 76.76  ? 199 ARG   A CD    1 
ATOM   1558 N NE    . ARG   A 1 209 ? 17.294 29.369  41.740 1.00 75.61  ? 199 ARG   A NE    1 
ATOM   1559 C CZ    . ARG   A 1 209 ? 16.955 30.517  42.313 1.00 73.44  ? 199 ARG   A CZ    1 
ATOM   1560 N NH1   . ARG   A 1 209 ? 17.533 31.642  41.943 1.00 75.42  ? 199 ARG   A NH1   1 
ATOM   1561 N NH2   . ARG   A 1 209 ? 16.073 30.538  43.292 1.00 72.92  ? 199 ARG   A NH2   1 
ATOM   1562 N N     . LEU   A 1 210 ? 16.626 23.822  41.486 1.00 77.27  ? 200 LEU   A N     1 
ATOM   1563 C CA    . LEU   A 1 210 ? 15.676 22.801  41.892 1.00 74.80  ? 200 LEU   A CA    1 
ATOM   1564 C C     . LEU   A 1 210 ? 14.411 23.445  42.447 1.00 73.73  ? 200 LEU   A C     1 
ATOM   1565 O O     . LEU   A 1 210 ? 13.384 22.780  42.569 1.00 72.57  ? 200 LEU   A O     1 
ATOM   1566 C CB    . LEU   A 1 210 ? 16.336 21.906  42.939 1.00 73.79  ? 200 LEU   A CB    1 
ATOM   1567 C CG    . LEU   A 1 210 ? 17.548 21.102  42.464 1.00 72.52  ? 200 LEU   A CG    1 
ATOM   1568 C CD1   . LEU   A 1 210 ? 18.260 20.457  43.636 1.00 71.41  ? 200 LEU   A CD1   1 
ATOM   1569 C CD2   . LEU   A 1 210 ? 17.118 20.054  41.456 1.00 73.41  ? 200 LEU   A CD2   1 
ATOM   1570 N N     . ASP   A 1 211 ? 14.497 24.736  42.791 1.00 73.83  ? 201 ASP   A N     1 
ATOM   1571 C CA    . ASP   A 1 211 ? 13.391 25.433  43.428 1.00 74.38  ? 201 ASP   A CA    1 
ATOM   1572 C C     . ASP   A 1 211 ? 12.533 26.111  42.363 1.00 76.01  ? 201 ASP   A C     1 
ATOM   1573 O O     . ASP   A 1 211 ? 12.037 27.212  42.577 1.00 78.49  ? 201 ASP   A O     1 
ATOM   1574 C CB    . ASP   A 1 211 ? 13.885 26.373  44.518 1.00 73.96  ? 201 ASP   A CB    1 
ATOM   1575 C CG    . ASP   A 1 211 ? 14.896 27.432  44.100 1.00 75.62  ? 201 ASP   A CG    1 
ATOM   1576 O OD1   . ASP   A 1 211 ? 15.299 27.438  42.914 1.00 75.43  ? 201 ASP   A OD1   1 
ATOM   1577 O OD2   . ASP   A 1 211 ? 15.281 28.242  44.975 1.00 75.46  ? 201 ASP   A OD2   1 
ATOM   1578 N N     . ASP   A 1 212 ? 12.346 25.418  41.232 1.00 77.42  ? 202 ASP   A N     1 
ATOM   1579 C CA    . ASP   A 1 212 ? 11.569 25.905  40.103 1.00 76.57  ? 202 ASP   A CA    1 
ATOM   1580 C C     . ASP   A 1 212 ? 10.763 24.737  39.543 1.00 77.87  ? 202 ASP   A C     1 
ATOM   1581 O O     . ASP   A 1 212 ? 11.339 23.714  39.183 1.00 79.27  ? 202 ASP   A O     1 
ATOM   1582 C CB    . ASP   A 1 212 ? 12.484 26.489  39.040 1.00 76.76  ? 202 ASP   A CB    1 
ATOM   1583 C CG    . ASP   A 1 212 ? 11.813 26.933  37.748 1.00 75.90  ? 202 ASP   A CG    1 
ATOM   1584 O OD1   . ASP   A 1 212 ? 10.601 27.239  37.780 1.00 74.57  ? 202 ASP   A OD1   1 
ATOM   1585 O OD2   . ASP   A 1 212 ? 12.507 26.935  36.713 1.00 75.48  ? 202 ASP   A OD2   1 
ATOM   1586 N N     . VAL   A 1 213 ? 9.436  24.899  39.457 1.00 80.01  ? 203 VAL   A N     1 
ATOM   1587 C CA    . VAL   A 1 213 ? 8.551  23.800  39.094 1.00 80.67  ? 203 VAL   A CA    1 
ATOM   1588 C C     . VAL   A 1 213 ? 8.808  23.401  37.638 1.00 81.42  ? 203 VAL   A C     1 
ATOM   1589 O O     . VAL   A 1 213 ? 8.656  22.233  37.276 1.00 80.95  ? 203 VAL   A O     1 
ATOM   1590 C CB    . VAL   A 1 213 ? 7.070  24.148  39.343 1.00 82.02  ? 203 VAL   A CB    1 
ATOM   1591 C CG1   . VAL   A 1 213 ? 6.155  22.956  39.076 1.00 82.30  ? 203 VAL   A CG1   1 
ATOM   1592 C CG2   . VAL   A 1 213 ? 6.838  24.678  40.757 1.00 81.80  ? 203 VAL   A CG2   1 
ATOM   1593 N N     . ASN   A 1 214 ? 9.228  24.372  36.815 1.00 81.83  ? 204 ASN   A N     1 
ATOM   1594 C CA    . ASN   A 1 214 ? 9.546  24.123  35.418 1.00 82.80  ? 204 ASN   A CA    1 
ATOM   1595 C C     . ASN   A 1 214 ? 11.051 23.945  35.234 1.00 85.02  ? 204 ASN   A C     1 
ATOM   1596 O O     . ASN   A 1 214 ? 11.597 24.333  34.201 1.00 82.53  ? 204 ASN   A O     1 
ATOM   1597 C CB    . ASN   A 1 214 ? 9.055  25.248  34.514 1.00 82.70  ? 204 ASN   A CB    1 
ATOM   1598 C CG    . ASN   A 1 214 ? 7.581  25.508  34.688 1.00 82.71  ? 204 ASN   A CG    1 
ATOM   1599 O OD1   . ASN   A 1 214 ? 7.186  26.648  34.947 1.00 81.67  ? 204 ASN   A OD1   1 
ATOM   1600 N ND2   . ASN   A 1 214 ? 6.762  24.473  34.560 1.00 83.48  ? 204 ASN   A ND2   1 
ATOM   1601 N N     . ARG   A 1 215 ? 11.716 23.357  36.237 1.00 86.42  ? 205 ARG   A N     1 
ATOM   1602 C CA    . ARG   A 1 215 ? 13.098 22.935  36.082 1.00 83.40  ? 205 ARG   A CA    1 
ATOM   1603 C C     . ARG   A 1 215 ? 13.156 21.886  34.973 1.00 83.70  ? 205 ARG   A C     1 
ATOM   1604 O O     . ARG   A 1 215 ? 12.240 21.076  34.837 1.00 79.97  ? 205 ARG   A O     1 
ATOM   1605 C CB    . ARG   A 1 215 ? 13.670 22.386  37.395 1.00 81.20  ? 205 ARG   A CB    1 
ATOM   1606 C CG    . ARG   A 1 215 ? 12.938 21.180  37.970 1.00 79.36  ? 205 ARG   A CG    1 
ATOM   1607 C CD    . ARG   A 1 215 ? 13.468 20.774  39.336 1.00 76.63  ? 205 ARG   A CD    1 
ATOM   1608 N NE    . ARG   A 1 215 ? 12.588 19.791  39.975 1.00 74.58  ? 205 ARG   A NE    1 
ATOM   1609 C CZ    . ARG   A 1 215 ? 11.381 20.038  40.469 1.00 73.04  ? 205 ARG   A CZ    1 
ATOM   1610 N NH1   . ARG   A 1 215 ? 10.933 21.279  40.559 1.00 72.42  ? 205 ARG   A NH1   1 
ATOM   1611 N NH2   . ARG   A 1 215 ? 10.639 19.039  40.914 1.00 72.59  ? 205 ARG   A NH2   1 
ATOM   1612 N N     . PRO   A 1 216 ? 14.227 21.868  34.147 1.00 87.63  ? 206 PRO   A N     1 
ATOM   1613 C CA    . PRO   A 1 216 ? 14.328 20.909  33.046 1.00 90.54  ? 206 PRO   A CA    1 
ATOM   1614 C C     . PRO   A 1 216 ? 14.443 19.467  33.530 1.00 95.69  ? 206 PRO   A C     1 
ATOM   1615 O O     . PRO   A 1 216 ? 14.716 19.225  34.704 1.00 96.70  ? 206 PRO   A O     1 
ATOM   1616 C CB    . PRO   A 1 216 ? 15.591 21.369  32.297 1.00 90.13  ? 206 PRO   A CB    1 
ATOM   1617 C CG    . PRO   A 1 216 ? 16.417 22.069  33.353 1.00 89.00  ? 206 PRO   A CG    1 
ATOM   1618 C CD    . PRO   A 1 216 ? 15.399 22.754  34.243 1.00 88.31  ? 206 PRO   A CD    1 
ATOM   1619 N N     . LYS   A 1 217 ? 14.204 18.520  32.614 1.00 102.65 ? 207 LYS   A N     1 
ATOM   1620 C CA    . LYS   A 1 217 ? 14.541 17.123  32.836 1.00 107.38 ? 207 LYS   A CA    1 
ATOM   1621 C C     . LYS   A 1 217 ? 15.940 16.873  32.274 1.00 110.80 ? 207 LYS   A C     1 
ATOM   1622 O O     . LYS   A 1 217 ? 16.516 17.748  31.627 1.00 110.19 ? 207 LYS   A O     1 
ATOM   1623 C CB    . LYS   A 1 217 ? 13.480 16.179  32.254 1.00 109.03 ? 207 LYS   A CB    1 
ATOM   1624 C CG    . LYS   A 1 217 ? 12.310 15.848  33.175 1.00 111.47 ? 207 LYS   A CG    1 
ATOM   1625 C CD    . LYS   A 1 217 ? 11.236 16.923  33.291 1.00 112.33 ? 207 LYS   A CD    1 
ATOM   1626 C CE    . LYS   A 1 217 ? 10.042 16.420  34.046 1.00 112.96 ? 207 LYS   A CE    1 
ATOM   1627 N NZ    . LYS   A 1 217 ? 8.914  17.352  33.992 1.00 113.37 ? 207 LYS   A NZ    1 
ATOM   1628 N N     . SER   A 1 218 ? 16.474 15.674  32.539 1.00 113.39 ? 208 SER   A N     1 
ATOM   1629 C CA    . SER   A 1 218 ? 17.864 15.354  32.252 1.00 114.62 ? 208 SER   A CA    1 
ATOM   1630 C C     . SER   A 1 218 ? 18.138 15.252  30.748 1.00 116.31 ? 208 SER   A C     1 
ATOM   1631 O O     . SER   A 1 218 ? 19.218 15.646  30.308 1.00 116.99 ? 208 SER   A O     1 
ATOM   1632 C CB    . SER   A 1 218 ? 18.303 14.105  32.988 1.00 114.33 ? 208 SER   A CB    1 
ATOM   1633 O OG    . SER   A 1 218 ? 17.416 13.019  32.765 1.00 115.76 ? 208 SER   A OG    1 
ATOM   1634 N N     . PRO   A 1 219 ? 17.212 14.739  29.897 1.00 116.51 ? 209 PRO   A N     1 
ATOM   1635 C CA    . PRO   A 1 219 ? 17.478 14.653  28.457 1.00 113.10 ? 209 PRO   A CA    1 
ATOM   1636 C C     . PRO   A 1 219 ? 17.905 15.973  27.813 1.00 109.34 ? 209 PRO   A C     1 
ATOM   1637 O O     . PRO   A 1 219 ? 18.703 15.972  26.878 1.00 110.10 ? 209 PRO   A O     1 
ATOM   1638 C CB    . PRO   A 1 219 ? 16.141 14.133  27.893 1.00 114.51 ? 209 PRO   A CB    1 
ATOM   1639 C CG    . PRO   A 1 219 ? 15.534 13.355  29.039 1.00 114.53 ? 209 PRO   A CG    1 
ATOM   1640 C CD    . PRO   A 1 219 ? 15.888 14.195  30.252 1.00 115.90 ? 209 PRO   A CD    1 
ATOM   1641 N N     . GLU   A 1 220 ? 17.391 17.093  28.336 1.00 105.25 ? 210 GLU   A N     1 
ATOM   1642 C CA    . GLU   A 1 220 ? 17.621 18.406  27.753 1.00 101.78 ? 210 GLU   A CA    1 
ATOM   1643 C C     . GLU   A 1 220 ? 19.025 18.914  28.078 1.00 100.61 ? 210 GLU   A C     1 
ATOM   1644 O O     . GLU   A 1 220 ? 19.576 19.714  27.325 1.00 99.34  ? 210 GLU   A O     1 
ATOM   1645 C CB    . GLU   A 1 220 ? 16.635 19.450  28.278 1.00 101.07 ? 210 GLU   A CB    1 
ATOM   1646 C CG    . GLU   A 1 220 ? 15.173 19.022  28.198 1.00 101.58 ? 210 GLU   A CG    1 
ATOM   1647 C CD    . GLU   A 1 220 ? 14.209 20.070  28.719 1.00 102.07 ? 210 GLU   A CD    1 
ATOM   1648 O OE1   . GLU   A 1 220 ? 14.587 21.263  28.780 1.00 101.06 ? 210 GLU   A OE1   1 
ATOM   1649 O OE2   . GLU   A 1 220 ? 13.085 19.674  29.094 1.00 101.72 ? 210 GLU   A OE2   1 
ATOM   1650 N N     . ILE   A 1 221 ? 19.588 18.469  29.208 1.00 100.83 ? 211 ILE   A N     1 
ATOM   1651 C CA    . ILE   A 1 221 ? 20.851 19.005  29.700 1.00 101.48 ? 211 ILE   A CA    1 
ATOM   1652 C C     . ILE   A 1 221 ? 21.938 17.932  29.642 1.00 100.73 ? 211 ILE   A C     1 
ATOM   1653 O O     . ILE   A 1 221 ? 23.029 18.135  30.169 1.00 97.06  ? 211 ILE   A O     1 
ATOM   1654 C CB    . ILE   A 1 221 ? 20.686 19.592  31.118 1.00 102.80 ? 211 ILE   A CB    1 
ATOM   1655 C CG1   . ILE   A 1 221 ? 19.914 18.646  32.052 1.00 104.70 ? 211 ILE   A CG1   1 
ATOM   1656 C CG2   . ILE   A 1 221 ? 20.037 20.975  31.053 1.00 102.20 ? 211 ILE   A CG2   1 
ATOM   1657 C CD1   . ILE   A 1 221 ? 19.861 19.098  33.502 1.00 105.14 ? 211 ILE   A CD1   1 
ATOM   1658 N N     . LYS   A 1 222 ? 21.651 16.823  28.945 1.00 101.83 ? 212 LYS   A N     1 
ATOM   1659 C CA    . LYS   A 1 222 ? 22.527 15.662  28.899 1.00 101.46 ? 212 LYS   A CA    1 
ATOM   1660 C C     . LYS   A 1 222 ? 23.903 16.064  28.366 1.00 100.95 ? 212 LYS   A C     1 
ATOM   1661 O O     . LYS   A 1 222 ? 24.925 15.567  28.841 1.00 97.90  ? 212 LYS   A O     1 
ATOM   1662 C CB    . LYS   A 1 222 ? 21.817 14.584  28.069 1.00 103.31 ? 212 LYS   A CB    1 
ATOM   1663 C CG    . LYS   A 1 222 ? 22.371 13.159  28.136 1.00 104.19 ? 212 LYS   A CG    1 
ATOM   1664 C CD    . LYS   A 1 222 ? 23.557 12.868  27.223 1.00 104.92 ? 212 LYS   A CD    1 
ATOM   1665 C CE    . LYS   A 1 222 ? 23.223 12.938  25.764 1.00 104.20 ? 212 LYS   A CE    1 
ATOM   1666 N NZ    . LYS   A 1 222 ? 24.437 12.967  24.946 1.00 105.58 ? 212 LYS   A NZ    1 
ATOM   1667 N N     . ASN   A 1 223 ? 23.923 16.986  27.394 1.00 102.98 ? 213 ASN   A N     1 
ATOM   1668 C CA    . ASN   A 1 223 ? 25.159 17.405  26.749 1.00 105.24 ? 213 ASN   A CA    1 
ATOM   1669 C C     . ASN   A 1 223 ? 25.838 18.499  27.577 1.00 103.28 ? 213 ASN   A C     1 
ATOM   1670 O O     . ASN   A 1 223 ? 27.063 18.614  27.563 1.00 102.37 ? 213 ASN   A O     1 
ATOM   1671 C CB    . ASN   A 1 223 ? 24.906 17.811  25.299 1.00 106.76 ? 213 ASN   A CB    1 
ATOM   1672 C CG    . ASN   A 1 223 ? 26.159 17.750  24.455 1.00 108.51 ? 213 ASN   A CG    1 
ATOM   1673 O OD1   . ASN   A 1 223 ? 27.002 18.652  24.523 1.00 106.07 ? 213 ASN   A OD1   1 
ATOM   1674 N ND2   . ASN   A 1 223 ? 26.297 16.710  23.643 1.00 109.02 ? 213 ASN   A ND2   1 
ATOM   1675 N N     . ASP   A 1 224 ? 25.040 19.309  28.288 1.00 102.50 ? 214 ASP   A N     1 
ATOM   1676 C CA    . ASP   A 1 224 ? 25.569 20.282  29.236 1.00 99.26  ? 214 ASP   A CA    1 
ATOM   1677 C C     . ASP   A 1 224 ? 26.331 19.558  30.349 1.00 98.17  ? 214 ASP   A C     1 
ATOM   1678 O O     . ASP   A 1 224 ? 27.401 20.003  30.765 1.00 93.17  ? 214 ASP   A O     1 
ATOM   1679 C CB    . ASP   A 1 224 ? 24.471 21.176  29.799 1.00 96.84  ? 214 ASP   A CB    1 
ATOM   1680 C CG    . ASP   A 1 224 ? 24.070 22.376  28.950 1.00 92.94  ? 214 ASP   A CG    1 
ATOM   1681 O OD1   . ASP   A 1 224 ? 24.950 23.213  28.664 1.00 89.60  ? 214 ASP   A OD1   1 
ATOM   1682 O OD2   . ASP   A 1 224 ? 22.872 22.478  28.607 1.00 90.38  ? 214 ASP   A OD2   1 
ATOM   1683 N N     . ILE   A 1 225 ? 25.770 18.435  30.819 1.00 97.57  ? 215 ILE   A N     1 
ATOM   1684 C CA    . ILE   A 1 225 ? 26.353 17.660  31.905 1.00 96.73  ? 215 ILE   A CA    1 
ATOM   1685 C C     . ILE   A 1 225 ? 27.677 17.043  31.452 1.00 100.43 ? 215 ILE   A C     1 
ATOM   1686 O O     . ILE   A 1 225 ? 28.619 16.963  32.241 1.00 102.31 ? 215 ILE   A O     1 
ATOM   1687 C CB    . ILE   A 1 225 ? 25.355 16.597  32.404 1.00 90.88  ? 215 ILE   A CB    1 
ATOM   1688 C CG1   . ILE   A 1 225 ? 24.125 17.247  33.046 1.00 88.11  ? 215 ILE   A CG1   1 
ATOM   1689 C CG2   . ILE   A 1 225 ? 26.033 15.618  33.362 1.00 90.94  ? 215 ILE   A CG2   1 
ATOM   1690 C CD1   . ILE   A 1 225 ? 22.969 16.296  33.302 1.00 86.85  ? 215 ILE   A CD1   1 
ATOM   1691 N N     . ARG   A 1 226 ? 27.737 16.611  30.185 1.00 102.01 ? 216 ARG   A N     1 
ATOM   1692 C CA    . ARG   A 1 226 ? 28.922 15.972  29.631 1.00 104.02 ? 216 ARG   A CA    1 
ATOM   1693 C C     . ARG   A 1 226 ? 30.102 16.947  29.653 1.00 102.26 ? 216 ARG   A C     1 
ATOM   1694 O O     . ARG   A 1 226 ? 31.209 16.571  30.042 1.00 98.96  ? 216 ARG   A O     1 
ATOM   1695 C CB    . ARG   A 1 226 ? 28.597 15.439  28.228 1.00 108.49 ? 216 ARG   A CB    1 
ATOM   1696 C CG    . ARG   A 1 226 ? 29.659 14.580  27.548 1.00 112.06 ? 216 ARG   A CG    1 
ATOM   1697 C CD    . ARG   A 1 226 ? 30.787 15.368  26.873 1.00 113.92 ? 216 ARG   A CD    1 
ATOM   1698 N NE    . ARG   A 1 226 ? 30.310 16.255  25.803 1.00 115.67 ? 216 ARG   A NE    1 
ATOM   1699 C CZ    . ARG   A 1 226 ? 31.006 17.235  25.226 1.00 116.38 ? 216 ARG   A CZ    1 
ATOM   1700 N NH1   . ARG   A 1 226 ? 32.239 17.513  25.622 1.00 117.19 ? 216 ARG   A NH1   1 
ATOM   1701 N NH2   . ARG   A 1 226 ? 30.458 17.948  24.257 1.00 115.45 ? 216 ARG   A NH2   1 
ATOM   1702 N N     . LEU   A 1 227 ? 29.857 18.196  29.232 1.00 99.74  ? 217 LEU   A N     1 
ATOM   1703 C CA    . LEU   A 1 227 ? 30.894 19.216  29.158 1.00 98.45  ? 217 LEU   A CA    1 
ATOM   1704 C C     . LEU   A 1 227 ? 31.246 19.707  30.562 1.00 94.45  ? 217 LEU   A C     1 
ATOM   1705 O O     . LEU   A 1 227 ? 32.386 20.089  30.823 1.00 92.57  ? 217 LEU   A O     1 
ATOM   1706 C CB    . LEU   A 1 227 ? 30.422 20.362  28.261 1.00 101.60 ? 217 LEU   A CB    1 
ATOM   1707 C CG    . LEU   A 1 227 ? 31.430 21.487  27.997 1.00 103.22 ? 217 LEU   A CG    1 
ATOM   1708 C CD1   . LEU   A 1 227 ? 32.627 21.006  27.189 1.00 103.27 ? 217 LEU   A CD1   1 
ATOM   1709 C CD2   . LEU   A 1 227 ? 30.753 22.653  27.296 1.00 104.06 ? 217 LEU   A CD2   1 
ATOM   1710 N N     . PHE   A 1 228 ? 30.249 19.711  31.455 1.00 91.12  ? 218 PHE   A N     1 
ATOM   1711 C CA    . PHE   A 1 228 ? 30.460 20.079  32.846 1.00 85.96  ? 218 PHE   A CA    1 
ATOM   1712 C C     . PHE   A 1 228 ? 31.467 19.114  33.465 1.00 84.08  ? 218 PHE   A C     1 
ATOM   1713 O O     . PHE   A 1 228 ? 32.483 19.535  34.018 1.00 79.79  ? 218 PHE   A O     1 
ATOM   1714 C CB    . PHE   A 1 228 ? 29.105 20.072  33.561 1.00 84.81  ? 218 PHE   A CB    1 
ATOM   1715 C CG    . PHE   A 1 228 ? 29.122 20.435  35.040 1.00 82.45  ? 218 PHE   A CG    1 
ATOM   1716 C CD1   . PHE   A 1 228 ? 30.034 21.355  35.550 1.00 80.87  ? 218 PHE   A CD1   1 
ATOM   1717 C CD2   . PHE   A 1 228 ? 28.209 19.860  35.916 1.00 81.12  ? 218 PHE   A CD2   1 
ATOM   1718 C CE1   . PHE   A 1 228 ? 30.038 21.680  36.896 1.00 79.96  ? 218 PHE   A CE1   1 
ATOM   1719 C CE2   . PHE   A 1 228 ? 28.215 20.193  37.261 1.00 81.11  ? 218 PHE   A CE2   1 
ATOM   1720 C CZ    . PHE   A 1 228 ? 29.130 21.099  37.748 1.00 80.47  ? 218 PHE   A CZ    1 
ATOM   1721 N N     . ARG   A 1 229 ? 31.176 17.815  33.331 1.00 81.56  ? 219 ARG   A N     1 
ATOM   1722 C CA    . ARG   A 1 229 ? 32.027 16.766  33.863 1.00 81.57  ? 219 ARG   A CA    1 
ATOM   1723 C C     . ARG   A 1 229 ? 33.446 16.887  33.306 1.00 85.90  ? 219 ARG   A C     1 
ATOM   1724 O O     . ARG   A 1 229 ? 34.410 16.655  34.031 1.00 88.59  ? 219 ARG   A O     1 
ATOM   1725 C CB    . ARG   A 1 229 ? 31.402 15.405  33.545 1.00 79.23  ? 219 ARG   A CB    1 
ATOM   1726 C CG    . ARG   A 1 229 ? 32.206 14.229  34.075 1.00 77.05  ? 219 ARG   A CG    1 
ATOM   1727 C CD    . ARG   A 1 229 ? 31.424 12.929  34.036 1.00 77.42  ? 219 ARG   A CD    1 
ATOM   1728 N NE    . ARG   A 1 229 ? 32.197 11.905  34.745 1.00 78.25  ? 219 ARG   A NE    1 
ATOM   1729 C CZ    . ARG   A 1 229 ? 32.022 11.549  36.015 1.00 79.38  ? 219 ARG   A CZ    1 
ATOM   1730 N NH1   . ARG   A 1 229 ? 31.023 12.038  36.731 1.00 79.16  ? 219 ARG   A NH1   1 
ATOM   1731 N NH2   . ARG   A 1 229 ? 32.856 10.692  36.572 1.00 79.80  ? 219 ARG   A NH2   1 
ATOM   1732 N N     . GLN   A 1 230 ? 33.566 17.246  32.020 1.00 89.91  ? 220 GLN   A N     1 
ATOM   1733 C CA    . GLN   A 1 230 ? 34.859 17.332  31.355 1.00 92.63  ? 220 GLN   A CA    1 
ATOM   1734 C C     . GLN   A 1 230 ? 35.667 18.510  31.905 1.00 90.40  ? 220 GLN   A C     1 
ATOM   1735 O O     . GLN   A 1 230 ? 36.896 18.463  31.914 1.00 90.12  ? 220 GLN   A O     1 
ATOM   1736 C CB    . GLN   A 1 230 ? 34.687 17.460  29.839 1.00 95.82  ? 220 GLN   A CB    1 
ATOM   1737 C CG    . GLN   A 1 230 ? 35.967 17.231  29.038 1.00 96.87  ? 220 GLN   A CG    1 
ATOM   1738 C CD    . GLN   A 1 230 ? 35.967 17.940  27.699 1.00 96.56  ? 220 GLN   A CD    1 
ATOM   1739 O OE1   . GLN   A 1 230 ? 36.080 19.169  27.623 1.00 94.81  ? 220 GLN   A OE1   1 
ATOM   1740 N NE2   . GLN   A 1 230 ? 35.852 17.171  26.624 1.00 95.78  ? 220 GLN   A NE2   1 
ATOM   1741 N N     . GLU   A 1 231 ? 34.978 19.572  32.347 1.00 89.59  ? 221 GLU   A N     1 
ATOM   1742 C CA    . GLU   A 1 231 ? 35.643 20.709  32.966 1.00 87.43  ? 221 GLU   A CA    1 
ATOM   1743 C C     . GLU   A 1 231 ? 36.038 20.353  34.400 1.00 85.06  ? 221 GLU   A C     1 
ATOM   1744 O O     . GLU   A 1 231 ? 37.117 20.739  34.850 1.00 83.46  ? 221 GLU   A O     1 
ATOM   1745 C CB    . GLU   A 1 231 ? 34.774 21.965  32.891 1.00 88.95  ? 221 GLU   A CB    1 
ATOM   1746 C CG    . GLU   A 1 231 ? 35.518 23.231  33.316 1.00 91.10  ? 221 GLU   A CG    1 
ATOM   1747 C CD    . GLU   A 1 231 ? 35.013 24.536  32.716 1.00 93.37  ? 221 GLU   A CD    1 
ATOM   1748 O OE1   . GLU   A 1 231 ? 34.011 24.519  31.966 1.00 95.19  ? 221 GLU   A OE1   1 
ATOM   1749 O OE2   . GLU   A 1 231 ? 35.640 25.583  32.991 1.00 92.77  ? 221 GLU   A OE2   1 
ATOM   1750 N N     . LEU   A 1 232 ? 35.171 19.595  35.092 1.00 82.91  ? 222 LEU   A N     1 
ATOM   1751 C CA    . LEU   A 1 232 ? 35.418 19.157  36.461 1.00 81.20  ? 222 LEU   A CA    1 
ATOM   1752 C C     . LEU   A 1 232 ? 36.498 18.076  36.502 1.00 80.96  ? 222 LEU   A C     1 
ATOM   1753 O O     . LEU   A 1 232 ? 37.089 17.842  37.551 1.00 80.39  ? 222 LEU   A O     1 
ATOM   1754 C CB    . LEU   A 1 232 ? 34.134 18.661  37.126 1.00 79.01  ? 222 LEU   A CB    1 
ATOM   1755 C CG    . LEU   A 1 232 ? 33.143 19.735  37.587 1.00 77.55  ? 222 LEU   A CG    1 
ATOM   1756 C CD1   . LEU   A 1 232 ? 31.937 19.067  38.225 1.00 76.90  ? 222 LEU   A CD1   1 
ATOM   1757 C CD2   . LEU   A 1 232 ? 33.775 20.731  38.547 1.00 75.46  ? 222 LEU   A CD2   1 
ATOM   1758 N N     . ARG   A 1 233 ? 36.751 17.411  35.370 1.00 80.36  ? 223 ARG   A N     1 
ATOM   1759 C CA    . ARG   A 1 233 ? 37.861 16.478  35.268 1.00 80.86  ? 223 ARG   A CA    1 
ATOM   1760 C C     . ARG   A 1 233 ? 39.161 17.206  35.614 1.00 80.10  ? 223 ARG   A C     1 
ATOM   1761 O O     . ARG   A 1 233 ? 40.139 16.584  36.024 1.00 75.98  ? 223 ARG   A O     1 
ATOM   1762 C CB    . ARG   A 1 233 ? 37.862 15.878  33.858 1.00 83.41  ? 223 ARG   A CB    1 
ATOM   1763 C CG    . ARG   A 1 233 ? 38.997 14.922  33.527 1.00 86.62  ? 223 ARG   A CG    1 
ATOM   1764 C CD    . ARG   A 1 233 ? 38.989 14.598  32.043 1.00 90.98  ? 223 ARG   A CD    1 
ATOM   1765 N NE    . ARG   A 1 233 ? 40.206 13.898  31.616 1.00 93.33  ? 223 ARG   A NE    1 
ATOM   1766 C CZ    . ARG   A 1 233 ? 40.601 13.771  30.353 1.00 94.44  ? 223 ARG   A CZ    1 
ATOM   1767 N NH1   . ARG   A 1 233 ? 39.873 14.281  29.374 1.00 95.94  ? 223 ARG   A NH1   1 
ATOM   1768 N NH2   . ARG   A 1 233 ? 41.731 13.145  30.072 1.00 93.19  ? 223 ARG   A NH2   1 
ATOM   1769 N N     . ASP   A 1 234 ? 39.152 18.535  35.456 1.00 81.61  ? 224 ASP   A N     1 
ATOM   1770 C CA    . ASP   A 1 234 ? 40.297 19.373  35.771 1.00 84.69  ? 224 ASP   A CA    1 
ATOM   1771 C C     . ASP   A 1 234 ? 40.155 19.986  37.168 1.00 84.86  ? 224 ASP   A C     1 
ATOM   1772 O O     . ASP   A 1 234 ? 40.918 20.887  37.522 1.00 83.39  ? 224 ASP   A O     1 
ATOM   1773 C CB    . ASP   A 1 234 ? 40.453 20.452  34.712 1.00 87.88  ? 224 ASP   A CB    1 
ATOM   1774 C CG    . ASP   A 1 234 ? 41.857 21.015  34.558 1.00 92.02  ? 224 ASP   A CG    1 
ATOM   1775 O OD1   . ASP   A 1 234 ? 42.731 20.274  34.055 1.00 93.29  ? 224 ASP   A OD1   1 
ATOM   1776 O OD2   . ASP   A 1 234 ? 42.066 22.181  34.955 1.00 96.22  ? 224 ASP   A OD2   1 
ATOM   1777 N N     . ALA   A 1 235 ? 39.205 19.475  37.969 1.00 82.77  ? 225 ALA   A N     1 
ATOM   1778 C CA    . ALA   A 1 235 ? 38.810 20.100  39.223 1.00 81.36  ? 225 ALA   A CA    1 
ATOM   1779 C C     . ALA   A 1 235 ? 39.995 20.186  40.180 1.00 78.95  ? 225 ALA   A C     1 
ATOM   1780 O O     . ALA   A 1 235 ? 40.528 19.163  40.604 1.00 78.25  ? 225 ALA   A O     1 
ATOM   1781 C CB    . ALA   A 1 235 ? 37.675 19.329  39.860 1.00 82.18  ? 225 ALA   A CB    1 
ATOM   1782 N N     . ALA   A 1 236 ? 40.387 21.417  40.526 1.00 75.06  ? 226 ALA   A N     1 
ATOM   1783 C CA    . ALA   A 1 236 ? 41.447 21.626  41.495 1.00 75.14  ? 226 ALA   A CA    1 
ATOM   1784 C C     . ALA   A 1 236 ? 41.324 23.019  42.110 1.00 73.30  ? 226 ALA   A C     1 
ATOM   1785 O O     . ALA   A 1 236 ? 40.673 23.896  41.547 1.00 72.99  ? 226 ALA   A O     1 
ATOM   1786 C CB    . ALA   A 1 236 ? 42.801 21.414  40.844 1.00 73.92  ? 226 ALA   A CB    1 
ATOM   1787 N N     . TYR   A 1 237 ? 41.922 23.174  43.297 1.00 69.59  ? 227 TYR   A N     1 
ATOM   1788 C CA    . TYR   A 1 237 ? 42.132 24.468  43.919 1.00 68.02  ? 227 TYR   A CA    1 
ATOM   1789 C C     . TYR   A 1 237 ? 43.499 24.978  43.486 1.00 67.03  ? 227 TYR   A C     1 
ATOM   1790 O O     . TYR   A 1 237 ? 44.404 24.181  43.271 1.00 68.44  ? 227 TYR   A O     1 
ATOM   1791 C CB    . TYR   A 1 237 ? 42.136 24.382  45.450 1.00 66.26  ? 227 TYR   A CB    1 
ATOM   1792 C CG    . TYR   A 1 237 ? 40.838 23.946  46.115 1.00 64.48  ? 227 TYR   A CG    1 
ATOM   1793 C CD1   . TYR   A 1 237 ? 39.618 24.519  45.779 1.00 63.30  ? 227 TYR   A CD1   1 
ATOM   1794 C CD2   . TYR   A 1 237 ? 40.838 22.958  47.093 1.00 64.61  ? 227 TYR   A CD2   1 
ATOM   1795 C CE1   . TYR   A 1 237 ? 38.442 24.129  46.402 1.00 62.55  ? 227 TYR   A CE1   1 
ATOM   1796 C CE2   . TYR   A 1 237 ? 39.669 22.555  47.718 1.00 63.17  ? 227 TYR   A CE2   1 
ATOM   1797 C CZ    . TYR   A 1 237 ? 38.467 23.146  47.376 1.00 61.49  ? 227 TYR   A CZ    1 
ATOM   1798 O OH    . TYR   A 1 237 ? 37.323 22.748  48.001 1.00 60.08  ? 227 TYR   A OH    1 
ATOM   1799 N N     . HIS   A 1 238 ? 43.647 26.303  43.397 1.00 67.20  ? 228 HIS   A N     1 
ATOM   1800 C CA    . HIS   A 1 238 ? 44.939 26.909  43.123 1.00 66.95  ? 228 HIS   A CA    1 
ATOM   1801 C C     . HIS   A 1 238 ? 45.149 28.074  44.084 1.00 64.59  ? 228 HIS   A C     1 
ATOM   1802 O O     . HIS   A 1 238 ? 44.407 29.049  44.051 1.00 68.46  ? 228 HIS   A O     1 
ATOM   1803 C CB    . HIS   A 1 238 ? 45.041 27.303  41.645 1.00 67.41  ? 228 HIS   A CB    1 
ATOM   1804 C CG    . HIS   A 1 238 ? 44.841 26.136  40.737 1.00 70.01  ? 228 HIS   A CG    1 
ATOM   1805 N ND1   . HIS   A 1 238 ? 43.668 25.906  40.048 1.00 71.03  ? 228 HIS   A ND1   1 
ATOM   1806 C CD2   . HIS   A 1 238 ? 45.662 25.120  40.431 1.00 70.51  ? 228 HIS   A CD2   1 
ATOM   1807 C CE1   . HIS   A 1 238 ? 43.789 24.789  39.341 1.00 72.94  ? 228 HIS   A CE1   1 
ATOM   1808 N NE2   . HIS   A 1 238 ? 44.991 24.292  39.564 1.00 72.66  ? 228 HIS   A NE2   1 
ATOM   1809 N N     . PHE   A 1 239 ? 46.161 27.952  44.946 1.00 61.74  ? 229 PHE   A N     1 
ATOM   1810 C CA    . PHE   A 1 239 ? 46.448 28.972  45.938 1.00 61.98  ? 229 PHE   A CA    1 
ATOM   1811 C C     . PHE   A 1 239 ? 47.920 28.870  46.313 1.00 63.84  ? 229 PHE   A C     1 
ATOM   1812 O O     . PHE   A 1 239 ? 48.522 27.812  46.159 1.00 66.05  ? 229 PHE   A O     1 
ATOM   1813 C CB    . PHE   A 1 239 ? 45.554 28.800  47.171 1.00 61.25  ? 229 PHE   A CB    1 
ATOM   1814 C CG    . PHE   A 1 239 ? 45.731 27.475  47.904 1.00 59.44  ? 229 PHE   A CG    1 
ATOM   1815 C CD1   . PHE   A 1 239 ? 46.667 27.342  48.924 1.00 59.46  ? 229 PHE   A CD1   1 
ATOM   1816 C CD2   . PHE   A 1 239 ? 44.970 26.362  47.561 1.00 57.31  ? 229 PHE   A CD2   1 
ATOM   1817 C CE1   . PHE   A 1 239 ? 46.826 26.133  49.586 1.00 59.58  ? 229 PHE   A CE1   1 
ATOM   1818 C CE2   . PHE   A 1 239 ? 45.138 25.156  48.224 1.00 57.18  ? 229 PHE   A CE2   1 
ATOM   1819 C CZ    . PHE   A 1 239 ? 46.064 25.042  49.232 1.00 57.45  ? 229 PHE   A CZ    1 
ATOM   1820 N N     . GLN   A 1 240 ? 48.480 29.981  46.795 1.00 66.99  ? 230 GLN   A N     1 
ATOM   1821 C CA    . GLN   A 1 240 ? 49.845 30.003  47.291 1.00 70.92  ? 230 GLN   A CA    1 
ATOM   1822 C C     . GLN   A 1 240 ? 49.828 29.529  48.740 1.00 69.99  ? 230 GLN   A C     1 
ATOM   1823 O O     . GLN   A 1 240 ? 48.936 29.899  49.498 1.00 69.58  ? 230 GLN   A O     1 
ATOM   1824 C CB    . GLN   A 1 240 ? 50.447 31.408  47.203 1.00 75.20  ? 230 GLN   A CB    1 
ATOM   1825 C CG    . GLN   A 1 240 ? 50.499 31.991  45.792 1.00 78.38  ? 230 GLN   A CG    1 
ATOM   1826 C CD    . GLN   A 1 240 ? 51.463 31.266  44.877 1.00 79.60  ? 230 GLN   A CD    1 
ATOM   1827 O OE1   . GLN   A 1 240 ? 51.059 30.506  43.989 1.00 81.28  ? 230 GLN   A OE1   1 
ATOM   1828 N NE2   . GLN   A 1 240 ? 52.752 31.482  45.095 1.00 79.32  ? 230 GLN   A NE2   1 
ATOM   1829 N N     . GLY   A 1 241 ? 50.810 28.701  49.109 1.00 68.86  ? 231 GLY   A N     1 
ATOM   1830 C CA    . GLY   A 1 241 ? 51.017 28.339  50.500 1.00 67.84  ? 231 GLY   A CA    1 
ATOM   1831 C C     . GLY   A 1 241 ? 51.615 29.513  51.267 1.00 67.74  ? 231 GLY   A C     1 
ATOM   1832 O O     . GLY   A 1 241 ? 52.361 30.299  50.695 1.00 70.53  ? 231 GLY   A O     1 
ATOM   1833 N N     . ASP   A 1 242 ? 51.263 29.635  52.551 1.00 68.55  ? 232 ASP   A N     1 
ATOM   1834 C CA    . ASP   A 1 242 ? 51.812 30.679  53.403 1.00 68.97  ? 232 ASP   A CA    1 
ATOM   1835 C C     . ASP   A 1 242 ? 52.328 30.096  54.720 1.00 69.26  ? 232 ASP   A C     1 
ATOM   1836 O O     . ASP   A 1 242 ? 52.673 30.846  55.632 1.00 71.12  ? 232 ASP   A O     1 
ATOM   1837 C CB    . ASP   A 1 242 ? 50.783 31.771  53.648 1.00 69.58  ? 232 ASP   A CB    1 
ATOM   1838 C CG    . ASP   A 1 242 ? 49.484 31.305  54.286 1.00 68.85  ? 232 ASP   A CG    1 
ATOM   1839 O OD1   . ASP   A 1 242 ? 49.518 30.927  55.472 1.00 68.01  ? 232 ASP   A OD1   1 
ATOM   1840 O OD2   . ASP   A 1 242 ? 48.456 31.306  53.582 1.00 70.97  ? 232 ASP   A OD2   1 
ATOM   1841 N N     . ALA   A 1 243 ? 52.394 28.763  54.814 1.00 67.73  ? 233 ALA   A N     1 
ATOM   1842 C CA    . ALA   A 1 243 ? 52.821 28.102  56.035 1.00 67.12  ? 233 ALA   A CA    1 
ATOM   1843 C C     . ALA   A 1 243 ? 53.869 27.048  55.701 1.00 66.51  ? 233 ALA   A C     1 
ATOM   1844 O O     . ALA   A 1 243 ? 53.811 26.427  54.642 1.00 63.91  ? 233 ALA   A O     1 
ATOM   1845 C CB    . ALA   A 1 243 ? 51.632 27.484  56.737 1.00 66.23  ? 233 ALA   A CB    1 
ATOM   1846 N N     . ASP   A 1 244 ? 54.803 26.857  56.639 1.00 67.60  ? 234 ASP   A N     1 
ATOM   1847 C CA    . ASP   A 1 244 ? 55.857 25.862  56.528 1.00 68.82  ? 234 ASP   A CA    1 
ATOM   1848 C C     . ASP   A 1 244 ? 55.398 24.557  57.179 1.00 68.76  ? 234 ASP   A C     1 
ATOM   1849 O O     . ASP   A 1 244 ? 54.340 24.500  57.806 1.00 67.54  ? 234 ASP   A O     1 
ATOM   1850 C CB    . ASP   A 1 244 ? 57.149 26.391  57.131 1.00 68.76  ? 234 ASP   A CB    1 
ATOM   1851 C CG    . ASP   A 1 244 ? 57.582 27.761  56.628 1.00 68.14  ? 234 ASP   A CG    1 
ATOM   1852 O OD1   . ASP   A 1 244 ? 57.667 27.938  55.396 1.00 67.92  ? 234 ASP   A OD1   1 
ATOM   1853 O OD2   . ASP   A 1 244 ? 57.834 28.640  57.474 1.00 68.01  ? 234 ASP   A OD2   1 
ATOM   1854 N N     . ASN   A 1 245 ? 56.227 23.515  57.051 1.00 67.93  ? 235 ASN   A N     1 
ATOM   1855 C CA    . ASN   A 1 245 ? 55.856 22.173  57.472 1.00 67.77  ? 235 ASN   A CA    1 
ATOM   1856 C C     . ASN   A 1 245 ? 56.130 21.953  58.960 1.00 66.68  ? 235 ASN   A C     1 
ATOM   1857 O O     . ASN   A 1 245 ? 56.083 20.816  59.422 1.00 68.13  ? 235 ASN   A O     1 
ATOM   1858 C CB    . ASN   A 1 245 ? 56.559 21.112  56.629 1.00 66.78  ? 235 ASN   A CB    1 
ATOM   1859 C CG    . ASN   A 1 245 ? 56.252 21.270  55.160 1.00 68.38  ? 235 ASN   A CG    1 
ATOM   1860 O OD1   . ASN   A 1 245 ? 57.132 21.106  54.310 1.00 69.71  ? 235 ASN   A OD1   1 
ATOM   1861 N ND2   . ASN   A 1 245 ? 55.009 21.581  54.837 1.00 68.09  ? 235 ASN   A ND2   1 
ATOM   1862 N N     . ASP   A 1 246 ? 56.398 23.023  59.718 1.00 65.07  ? 236 ASP   A N     1 
ATOM   1863 C CA    . ASP   A 1 246 ? 56.573 22.881  61.155 1.00 65.81  ? 236 ASP   A CA    1 
ATOM   1864 C C     . ASP   A 1 246 ? 55.538 23.712  61.916 1.00 66.05  ? 236 ASP   A C     1 
ATOM   1865 O O     . ASP   A 1 246 ? 55.731 24.009  63.092 1.00 67.57  ? 236 ASP   A O     1 
ATOM   1866 C CB    . ASP   A 1 246 ? 58.003 23.185  61.568 1.00 65.40  ? 236 ASP   A CB    1 
ATOM   1867 C CG    . ASP   A 1 246 ? 58.432 24.634  61.408 1.00 66.73  ? 236 ASP   A CG    1 
ATOM   1868 O OD1   . ASP   A 1 246 ? 57.706 25.385  60.721 1.00 68.22  ? 236 ASP   A OD1   1 
ATOM   1869 O OD2   . ASP   A 1 246 ? 59.474 24.998  61.989 1.00 68.40  ? 236 ASP   A OD2   1 
ATOM   1870 N N     . GLN   A 1 247 ? 54.423 24.054  61.260 1.00 66.62  ? 237 GLN   A N     1 
ATOM   1871 C CA    . GLN   A 1 247 ? 53.348 24.782  61.915 1.00 67.20  ? 237 GLN   A CA    1 
ATOM   1872 C C     . GLN   A 1 247 ? 52.000 24.208  61.478 1.00 64.93  ? 237 GLN   A C     1 
ATOM   1873 O O     . GLN   A 1 247 ? 51.868 23.666  60.380 1.00 64.13  ? 237 GLN   A O     1 
ATOM   1874 C CB    . GLN   A 1 247 ? 53.482 26.279  61.629 1.00 69.41  ? 237 GLN   A CB    1 
ATOM   1875 C CG    . GLN   A 1 247 ? 53.389 26.636  60.149 1.00 72.44  ? 237 GLN   A CG    1 
ATOM   1876 C CD    . GLN   A 1 247 ? 53.707 28.086  59.855 1.00 74.50  ? 237 GLN   A CD    1 
ATOM   1877 O OE1   . GLN   A 1 247 ? 54.866 28.514  59.899 1.00 76.32  ? 237 GLN   A OE1   1 
ATOM   1878 N NE2   . GLN   A 1 247 ? 52.680 28.854  59.519 1.00 75.17  ? 237 GLN   A NE2   1 
ATOM   1879 N N     . LEU   A 1 248 ? 51.010 24.325  62.373 1.00 62.71  ? 238 LEU   A N     1 
ATOM   1880 C CA    . LEU   A 1 248 ? 49.647 23.894  62.110 1.00 59.43  ? 238 LEU   A CA    1 
ATOM   1881 C C     . LEU   A 1 248 ? 49.167 24.519  60.804 1.00 59.39  ? 238 LEU   A C     1 
ATOM   1882 O O     . LEU   A 1 248 ? 49.300 25.725  60.598 1.00 60.24  ? 238 LEU   A O     1 
ATOM   1883 C CB    . LEU   A 1 248 ? 48.751 24.299  63.281 1.00 58.52  ? 238 LEU   A CB    1 
ATOM   1884 C CG    . LEU   A 1 248 ? 47.296 23.818  63.224 1.00 57.39  ? 238 LEU   A CG    1 
ATOM   1885 C CD1   . LEU   A 1 248 ? 47.189 22.303  63.350 1.00 55.67  ? 238 LEU   A CD1   1 
ATOM   1886 C CD2   . LEU   A 1 248 ? 46.476 24.501  64.305 1.00 57.06  ? 238 LEU   A CD2   1 
ATOM   1887 N N     . SER   A 1 249 ? 48.612 23.685  59.922 1.00 58.47  ? 239 SER   A N     1 
ATOM   1888 C CA    . SER   A 1 249 ? 48.139 24.155  58.631 1.00 57.94  ? 239 SER   A CA    1 
ATOM   1889 C C     . SER   A 1 249 ? 46.923 23.351  58.185 1.00 54.87  ? 239 SER   A C     1 
ATOM   1890 O O     . SER   A 1 249 ? 46.638 22.287  58.725 1.00 53.77  ? 239 SER   A O     1 
ATOM   1891 C CB    . SER   A 1 249 ? 49.230 24.087  57.596 1.00 58.37  ? 239 SER   A CB    1 
ATOM   1892 O OG    . SER   A 1 249 ? 49.621 22.743  57.355 1.00 58.38  ? 239 SER   A OG    1 
ATOM   1893 N N     . VAL   A 1 250 ? 46.217 23.892  57.192 1.00 54.64  ? 240 VAL   A N     1 
ATOM   1894 C CA    . VAL   A 1 250 ? 45.146 23.190  56.506 1.00 54.57  ? 240 VAL   A CA    1 
ATOM   1895 C C     . VAL   A 1 250 ? 45.430 23.285  55.013 1.00 53.93  ? 240 VAL   A C     1 
ATOM   1896 O O     . VAL   A 1 250 ? 45.928 24.307  54.544 1.00 53.46  ? 240 VAL   A O     1 
ATOM   1897 C CB    . VAL   A 1 250 ? 43.748 23.746  56.835 1.00 53.11  ? 240 VAL   A CB    1 
ATOM   1898 C CG1   . VAL   A 1 250 ? 43.325 23.401  58.253 1.00 53.42  ? 240 VAL   A CG1   1 
ATOM   1899 C CG2   . VAL   A 1 250 ? 43.663 25.250  56.599 1.00 53.98  ? 240 VAL   A CG2   1 
ATOM   1900 N N     . THR   A 1 251 ? 45.127 22.203  54.290 1.00 54.95  ? 241 THR   A N     1 
ATOM   1901 C CA    . THR   A 1 251 ? 45.248 22.176  52.841 1.00 55.78  ? 241 THR   A CA    1 
ATOM   1902 C C     . THR   A 1 251 ? 43.917 21.717  52.260 1.00 55.43  ? 241 THR   A C     1 
ATOM   1903 O O     . THR   A 1 251 ? 43.626 20.526  52.282 1.00 56.93  ? 241 THR   A O     1 
ATOM   1904 C CB    . THR   A 1 251 ? 46.379 21.239  52.413 1.00 55.67  ? 241 THR   A CB    1 
ATOM   1905 O OG1   . THR   A 1 251 ? 47.596 21.782  52.917 1.00 55.64  ? 241 THR   A OG1   1 
ATOM   1906 C CG2   . THR   A 1 251 ? 46.472 21.098  50.904 1.00 56.45  ? 241 THR   A CG2   1 
ATOM   1907 N N     . PRO   A 1 252 ? 43.065 22.625  51.729 1.00 56.73  ? 242 PRO   A N     1 
ATOM   1908 C CA    . PRO   A 1 252 ? 41.840 22.204  51.054 1.00 57.64  ? 242 PRO   A CA    1 
ATOM   1909 C C     . PRO   A 1 252 ? 42.225 21.422  49.801 1.00 57.78  ? 242 PRO   A C     1 
ATOM   1910 O O     . PRO   A 1 252 ? 43.187 21.767  49.118 1.00 57.82  ? 242 PRO   A O     1 
ATOM   1911 C CB    . PRO   A 1 252 ? 41.091 23.516  50.758 1.00 58.15  ? 242 PRO   A CB    1 
ATOM   1912 C CG    . PRO   A 1 252 ? 42.187 24.558  50.717 1.00 58.81  ? 242 PRO   A CG    1 
ATOM   1913 C CD    . PRO   A 1 252 ? 43.226 24.088  51.733 1.00 58.61  ? 242 PRO   A CD    1 
ATOM   1914 N N     . LEU   A 1 253 ? 41.490 20.334  49.556 1.00 57.69  ? 243 LEU   A N     1 
ATOM   1915 C CA    . LEU   A 1 253 ? 41.709 19.455  48.421 1.00 56.29  ? 243 LEU   A CA    1 
ATOM   1916 C C     . LEU   A 1 253 ? 40.352 19.171  47.789 1.00 56.73  ? 243 LEU   A C     1 
ATOM   1917 O O     . LEU   A 1 253 ? 39.378 18.954  48.504 1.00 56.32  ? 243 LEU   A O     1 
ATOM   1918 C CB    . LEU   A 1 253 ? 42.376 18.166  48.896 1.00 55.15  ? 243 LEU   A CB    1 
ATOM   1919 C CG    . LEU   A 1 253 ? 43.767 18.317  49.517 1.00 55.24  ? 243 LEU   A CG    1 
ATOM   1920 C CD1   . LEU   A 1 253 ? 44.145 17.091  50.323 1.00 55.88  ? 243 LEU   A CD1   1 
ATOM   1921 C CD2   . LEU   A 1 253 ? 44.800 18.579  48.437 1.00 55.95  ? 243 LEU   A CD2   1 
ATOM   1922 N N     . VAL   A 1 254 ? 40.307 19.210  46.454 1.00 57.63  ? 244 VAL   A N     1 
ATOM   1923 C CA    . VAL   A 1 254 ? 39.121 18.866  45.687 1.00 58.49  ? 244 VAL   A CA    1 
ATOM   1924 C C     . VAL   A 1 254 ? 39.597 18.035  44.506 1.00 60.10  ? 244 VAL   A C     1 
ATOM   1925 O O     . VAL   A 1 254 ? 40.738 18.191  44.072 1.00 64.53  ? 244 VAL   A O     1 
ATOM   1926 C CB    . VAL   A 1 254 ? 38.336 20.103  45.208 1.00 58.61  ? 244 VAL   A CB    1 
ATOM   1927 C CG1   . VAL   A 1 254 ? 39.184 21.008  44.323 1.00 60.71  ? 244 VAL   A CG1   1 
ATOM   1928 C CG2   . VAL   A 1 254 ? 37.048 19.730  44.487 1.00 58.10  ? 244 VAL   A CG2   1 
ATOM   1929 N N     . GLY   A 1 255 ? 38.724 17.163  43.993 1.00 59.52  ? 245 GLY   A N     1 
ATOM   1930 C CA    . GLY   A 1 255 ? 39.107 16.320  42.877 1.00 59.91  ? 245 GLY   A CA    1 
ATOM   1931 C C     . GLY   A 1 255 ? 37.928 15.578  42.259 1.00 60.00  ? 245 GLY   A C     1 
ATOM   1932 O O     . GLY   A 1 255 ? 36.870 15.431  42.872 1.00 57.36  ? 245 GLY   A O     1 
ATOM   1933 N N     . LEU   A 1 256 ? 38.140 15.141  41.014 1.00 60.53  ? 246 LEU   A N     1 
ATOM   1934 C CA    . LEU   A 1 256 ? 37.263 14.190  40.360 1.00 62.25  ? 246 LEU   A CA    1 
ATOM   1935 C C     . LEU   A 1 256 ? 38.101 13.334  39.416 1.00 64.50  ? 246 LEU   A C     1 
ATOM   1936 O O     . LEU   A 1 256 ? 38.744 13.863  38.513 1.00 69.42  ? 246 LEU   A O     1 
ATOM   1937 C CB    . LEU   A 1 256 ? 36.140 14.915  39.626 1.00 62.10  ? 246 LEU   A CB    1 
ATOM   1938 C CG    . LEU   A 1 256 ? 35.238 14.040  38.749 1.00 63.95  ? 246 LEU   A CG    1 
ATOM   1939 C CD1   . LEU   A 1 256 ? 34.792 12.774  39.453 1.00 64.63  ? 246 LEU   A CD1   1 
ATOM   1940 C CD2   . LEU   A 1 256 ? 34.020 14.826  38.299 1.00 65.04  ? 246 LEU   A CD2   1 
ATOM   1941 N N     . GLY   A 1 257 ? 38.110 12.020  39.668 1.00 65.42  ? 247 GLY   A N     1 
ATOM   1942 C CA    . GLY   A 1 257 ? 38.723 11.051  38.775 1.00 65.85  ? 247 GLY   A CA    1 
ATOM   1943 C C     . GLY   A 1 257 ? 40.221 10.905  39.027 1.00 68.47  ? 247 GLY   A C     1 
ATOM   1944 O O     . GLY   A 1 257 ? 40.710 11.198  40.117 1.00 67.45  ? 247 GLY   A O     1 
ATOM   1945 N N     . LYS   A 1 258 ? 40.927 10.461  37.981 1.00 72.64  ? 248 LYS   A N     1 
ATOM   1946 C CA    . LYS   A 1 258 ? 42.339 10.111  38.038 1.00 75.98  ? 248 LYS   A CA    1 
ATOM   1947 C C     . LYS   A 1 258 ? 43.210 11.344  38.283 1.00 74.27  ? 248 LYS   A C     1 
ATOM   1948 O O     . LYS   A 1 258 ? 44.315 11.220  38.805 1.00 72.88  ? 248 LYS   A O     1 
ATOM   1949 C CB    . LYS   A 1 258 ? 42.741 9.328   36.777 1.00 82.08  ? 248 LYS   A CB    1 
ATOM   1950 C CG    . LYS   A 1 258 ? 42.280 9.841   35.399 1.00 85.89  ? 248 LYS   A CG    1 
ATOM   1951 C CD    . LYS   A 1 258 ? 43.233 10.776  34.658 1.00 89.16  ? 248 LYS   A CD    1 
ATOM   1952 C CE    . LYS   A 1 258 ? 42.758 11.098  33.262 1.00 89.97  ? 248 LYS   A CE    1 
ATOM   1953 N NZ    . LYS   A 1 258 ? 43.844 11.523  32.370 1.00 89.75  ? 248 LYS   A NZ    1 
ATOM   1954 N N     . SER   A 1 259 ? 42.700 12.530  37.933 1.00 74.89  ? 249 SER   A N     1 
ATOM   1955 C CA    . SER   A 1 259 ? 43.452 13.766  38.083 1.00 76.34  ? 249 SER   A CA    1 
ATOM   1956 C C     . SER   A 1 259 ? 43.323 14.346  39.495 1.00 74.75  ? 249 SER   A C     1 
ATOM   1957 O O     . SER   A 1 259 ? 43.994 15.322  39.823 1.00 76.48  ? 249 SER   A O     1 
ATOM   1958 C CB    . SER   A 1 259 ? 43.029 14.772  37.032 1.00 78.29  ? 249 SER   A CB    1 
ATOM   1959 O OG    . SER   A 1 259 ? 41.630 15.016  37.078 1.00 80.77  ? 249 SER   A OG    1 
ATOM   1960 N N     . SER   A 1 260 ? 42.470 13.745  40.335 1.00 71.81  ? 250 SER   A N     1 
ATOM   1961 C CA    . SER   A 1 260 ? 42.202 14.248  41.674 1.00 67.68  ? 250 SER   A CA    1 
ATOM   1962 C C     . SER   A 1 260 ? 43.496 14.370  42.476 1.00 66.48  ? 250 SER   A C     1 
ATOM   1963 O O     . SER   A 1 260 ? 44.222 13.390  42.634 1.00 67.53  ? 250 SER   A O     1 
ATOM   1964 C CB    . SER   A 1 260 ? 41.211 13.356  42.379 1.00 66.82  ? 250 SER   A CB    1 
ATOM   1965 O OG    . SER   A 1 260 ? 41.044 13.733  43.736 1.00 65.36  ? 250 SER   A OG    1 
ATOM   1966 N N     . LEU   A 1 261 ? 43.771 15.582  42.976 1.00 64.72  ? 251 LEU   A N     1 
ATOM   1967 C CA    . LEU   A 1 261 ? 44.894 15.816  43.872 1.00 64.00  ? 251 LEU   A CA    1 
ATOM   1968 C C     . LEU   A 1 261 ? 44.603 15.184  45.236 1.00 62.07  ? 251 LEU   A C     1 
ATOM   1969 O O     . LEU   A 1 261 ? 45.518 14.767  45.946 1.00 60.31  ? 251 LEU   A O     1 
ATOM   1970 C CB    . LEU   A 1 261 ? 45.155 17.319  43.985 1.00 65.14  ? 251 LEU   A CB    1 
ATOM   1971 C CG    . LEU   A 1 261 ? 46.309 17.740  44.903 1.00 66.40  ? 251 LEU   A CG    1 
ATOM   1972 C CD1   . LEU   A 1 261 ? 47.646 17.181  44.450 1.00 67.18  ? 251 LEU   A CD1   1 
ATOM   1973 C CD2   . LEU   A 1 261 ? 46.382 19.249  45.007 1.00 66.55  ? 251 LEU   A CD2   1 
ATOM   1974 N N     . LEU   A 1 262 ? 43.314 15.129  45.592 1.00 60.54  ? 252 LEU   A N     1 
ATOM   1975 C CA    . LEU   A 1 262 ? 42.857 14.463  46.801 1.00 59.93  ? 252 LEU   A CA    1 
ATOM   1976 C C     . LEU   A 1 262 ? 43.293 13.000  46.791 1.00 59.64  ? 252 LEU   A C     1 
ATOM   1977 O O     . LEU   A 1 262 ? 43.909 12.533  47.749 1.00 58.41  ? 252 LEU   A O     1 
ATOM   1978 C CB    . LEU   A 1 262 ? 41.337 14.586  46.889 1.00 60.11  ? 252 LEU   A CB    1 
ATOM   1979 C CG    . LEU   A 1 262 ? 40.660 13.809  48.020 1.00 59.52  ? 252 LEU   A CG    1 
ATOM   1980 C CD1   . LEU   A 1 262 ? 41.198 14.255  49.367 1.00 59.85  ? 252 LEU   A CD1   1 
ATOM   1981 C CD2   . LEU   A 1 262 ? 39.159 13.985  47.939 1.00 59.87  ? 252 LEU   A CD2   1 
ATOM   1982 N N     . ASN   A 1 263 ? 42.959 12.292  45.702 1.00 59.54  ? 253 ASN   A N     1 
ATOM   1983 C CA    . ASN   A 1 263 ? 43.263 10.874  45.566 1.00 59.66  ? 253 ASN   A CA    1 
ATOM   1984 C C     . ASN   A 1 263 ? 44.774 10.649  45.640 1.00 60.72  ? 253 ASN   A C     1 
ATOM   1985 O O     . ASN   A 1 263 ? 45.224 9.724   46.317 1.00 61.64  ? 253 ASN   A O     1 
ATOM   1986 C CB    . ASN   A 1 263 ? 42.658 10.288  44.295 1.00 58.86  ? 253 ASN   A CB    1 
ATOM   1987 C CG    . ASN   A 1 263 ? 41.146 10.291  44.308 1.00 58.51  ? 253 ASN   A CG    1 
ATOM   1988 O OD1   . ASN   A 1 263 ? 40.518 10.630  45.316 1.00 57.29  ? 253 ASN   A OD1   1 
ATOM   1989 N ND2   . ASN   A 1 263 ? 40.535 9.919   43.195 1.00 59.39  ? 253 ASN   A ND2   1 
ATOM   1990 N N     . LYS   A 1 264 ? 45.554 11.505  44.967 1.00 60.46  ? 254 LYS   A N     1 
ATOM   1991 C CA    . LYS   A 1 264 ? 47.006 11.391  45.000 1.00 62.75  ? 254 LYS   A CA    1 
ATOM   1992 C C     . LYS   A 1 264 ? 47.514 11.649  46.414 1.00 60.45  ? 254 LYS   A C     1 
ATOM   1993 O O     . LYS   A 1 264 ? 48.447 10.989  46.861 1.00 62.37  ? 254 LYS   A O     1 
ATOM   1994 C CB    . LYS   A 1 264 ? 47.703 12.336  44.015 1.00 65.65  ? 254 LYS   A CB    1 
ATOM   1995 C CG    . LYS   A 1 264 ? 47.443 11.984  42.563 1.00 71.62  ? 254 LYS   A CG    1 
ATOM   1996 C CD    . LYS   A 1 264 ? 47.743 13.083  41.551 1.00 75.38  ? 254 LYS   A CD    1 
ATOM   1997 C CE    . LYS   A 1 264 ? 47.129 12.753  40.224 1.00 79.02  ? 254 LYS   A CE    1 
ATOM   1998 N NZ    . LYS   A 1 264 ? 47.285 13.838  39.254 1.00 81.90  ? 254 LYS   A NZ    1 
ATOM   1999 N N     . THR   A 1 265 ? 46.906 12.615  47.109 1.00 57.99  ? 255 THR   A N     1 
ATOM   2000 C CA    . THR   A 1 265 ? 47.310 12.928  48.470 1.00 57.13  ? 255 THR   A CA    1 
ATOM   2001 C C     . THR   A 1 265 ? 46.909 11.782  49.401 1.00 54.55  ? 255 THR   A C     1 
ATOM   2002 O O     . THR   A 1 265 ? 47.674 11.421  50.290 1.00 53.95  ? 255 THR   A O     1 
ATOM   2003 C CB    . THR   A 1 265 ? 46.708 14.263  48.905 1.00 58.59  ? 255 THR   A CB    1 
ATOM   2004 O OG1   . THR   A 1 265 ? 47.118 15.211  47.923 1.00 59.46  ? 255 THR   A OG1   1 
ATOM   2005 C CG2   . THR   A 1 265 ? 47.201 14.697  50.274 1.00 58.91  ? 255 THR   A CG2   1 
ATOM   2006 N N     . ILE   A 1 266 ? 45.719 11.205  49.190 1.00 53.19  ? 256 ILE   A N     1 
ATOM   2007 C CA    . ILE   A 1 266 ? 45.320 10.001  49.904 1.00 53.87  ? 256 ILE   A CA    1 
ATOM   2008 C C     . ILE   A 1 266 ? 46.358 8.903   49.671 1.00 55.18  ? 256 ILE   A C     1 
ATOM   2009 O O     . ILE   A 1 266 ? 46.785 8.247   50.620 1.00 54.61  ? 256 ILE   A O     1 
ATOM   2010 C CB    . ILE   A 1 266 ? 43.900 9.558   49.508 1.00 53.14  ? 256 ILE   A CB    1 
ATOM   2011 C CG1   . ILE   A 1 266 ? 42.845 10.522  50.074 1.00 52.86  ? 256 ILE   A CG1   1 
ATOM   2012 C CG2   . ILE   A 1 266 ? 43.640 8.116   49.946 1.00 52.99  ? 256 ILE   A CG2   1 
ATOM   2013 C CD1   . ILE   A 1 266 ? 41.458 10.365  49.481 1.00 52.56  ? 256 ILE   A CD1   1 
ATOM   2014 N N     . PHE   A 1 267 ? 46.777 8.739   48.409 1.00 57.65  ? 257 PHE   A N     1 
ATOM   2015 C CA    . PHE   A 1 267 ? 47.745 7.722   48.027 1.00 59.28  ? 257 PHE   A CA    1 
ATOM   2016 C C     . PHE   A 1 267 ? 49.045 7.889   48.813 1.00 60.15  ? 257 PHE   A C     1 
ATOM   2017 O O     . PHE   A 1 267 ? 49.516 6.926   49.412 1.00 61.51  ? 257 PHE   A O     1 
ATOM   2018 C CB    . PHE   A 1 267 ? 47.997 7.745   46.515 1.00 59.85  ? 257 PHE   A CB    1 
ATOM   2019 C CG    . PHE   A 1 267 ? 49.188 6.905   46.072 1.00 60.48  ? 257 PHE   A CG    1 
ATOM   2020 C CD1   . PHE   A 1 267 ? 49.126 5.515   46.089 1.00 60.46  ? 257 PHE   A CD1   1 
ATOM   2021 C CD2   . PHE   A 1 267 ? 50.370 7.505   45.646 1.00 61.96  ? 257 PHE   A CD2   1 
ATOM   2022 C CE1   . PHE   A 1 267 ? 50.217 4.750   45.699 1.00 60.56  ? 257 PHE   A CE1   1 
ATOM   2023 C CE2   . PHE   A 1 267 ? 51.459 6.734   45.256 1.00 62.17  ? 257 PHE   A CE2   1 
ATOM   2024 C CZ    . PHE   A 1 267 ? 51.379 5.358   45.284 1.00 60.90  ? 257 PHE   A CZ    1 
ATOM   2025 N N     . HIS   A 1 268 ? 49.621 9.100   48.806 1.00 61.43  ? 258 HIS   A N     1 
ATOM   2026 C CA    . HIS   A 1 268 ? 50.939 9.334   49.388 1.00 63.08  ? 258 HIS   A CA    1 
ATOM   2027 C C     . HIS   A 1 268 ? 50.898 9.436   50.919 1.00 61.46  ? 258 HIS   A C     1 
ATOM   2028 O O     . HIS   A 1 268 ? 51.933 9.282   51.568 1.00 59.47  ? 258 HIS   A O     1 
ATOM   2029 C CB    . HIS   A 1 268 ? 51.598 10.592  48.802 1.00 66.28  ? 258 HIS   A CB    1 
ATOM   2030 C CG    . HIS   A 1 268 ? 52.022 10.495  47.367 1.00 69.30  ? 258 HIS   A CG    1 
ATOM   2031 N ND1   . HIS   A 1 268 ? 53.124 9.778   46.952 1.00 69.18  ? 258 HIS   A ND1   1 
ATOM   2032 C CD2   . HIS   A 1 268 ? 51.496 11.035  46.256 1.00 68.73  ? 258 HIS   A CD2   1 
ATOM   2033 C CE1   . HIS   A 1 268 ? 53.241 9.880   45.638 1.00 68.33  ? 258 HIS   A CE1   1 
ATOM   2034 N NE2   . HIS   A 1 268 ? 52.266 10.644  45.196 1.00 67.98  ? 258 HIS   A NE2   1 
ATOM   2035 N N     . LEU   A 1 269 ? 49.724 9.724   51.502 1.00 59.64  ? 259 LEU   A N     1 
ATOM   2036 C CA    . LEU   A 1 269 ? 49.605 9.849   52.950 1.00 58.72  ? 259 LEU   A CA    1 
ATOM   2037 C C     . LEU   A 1 269 ? 49.977 8.527   53.614 1.00 58.11  ? 259 LEU   A C     1 
ATOM   2038 O O     . LEU   A 1 269 ? 50.827 8.489   54.502 1.00 57.46  ? 259 LEU   A O     1 
ATOM   2039 C CB    . LEU   A 1 269 ? 48.198 10.268  53.373 1.00 58.44  ? 259 LEU   A CB    1 
ATOM   2040 C CG    . LEU   A 1 269 ? 47.914 11.770  53.458 1.00 56.35  ? 259 LEU   A CG    1 
ATOM   2041 C CD1   . LEU   A 1 269 ? 46.414 12.012  53.504 1.00 55.27  ? 259 LEU   A CD1   1 
ATOM   2042 C CD2   . LEU   A 1 269 ? 48.594 12.368  54.668 1.00 56.05  ? 259 LEU   A CD2   1 
ATOM   2043 N N     . MET   A 1 270 ? 49.332 7.448   53.160 1.00 58.05  ? 260 MET   A N     1 
ATOM   2044 C CA    . MET   A 1 270 ? 49.400 6.163   53.833 1.00 57.45  ? 260 MET   A CA    1 
ATOM   2045 C C     . MET   A 1 270 ? 50.858 5.751   54.055 1.00 57.45  ? 260 MET   A C     1 
ATOM   2046 O O     . MET   A 1 270 ? 51.233 5.451   55.186 1.00 56.91  ? 260 MET   A O     1 
ATOM   2047 C CB    . MET   A 1 270 ? 48.644 5.089   53.045 1.00 57.41  ? 260 MET   A CB    1 
ATOM   2048 C CG    . MET   A 1 270 ? 47.169 5.360   52.891 1.00 57.34  ? 260 MET   A CG    1 
ATOM   2049 S SD    . MET   A 1 270 ? 46.349 3.953   52.121 1.00 57.87  ? 260 MET   A SD    1 
ATOM   2050 C CE    . MET   A 1 270 ? 44.693 4.643   52.024 1.00 60.20  ? 260 MET   A CE    1 
ATOM   2051 N N     . PRO   A 1 271 ? 51.725 5.722   53.011 1.00 57.65  ? 261 PRO   A N     1 
ATOM   2052 C CA    . PRO   A 1 271 ? 53.137 5.374   53.189 1.00 57.53  ? 261 PRO   A CA    1 
ATOM   2053 C C     . PRO   A 1 271 ? 53.943 6.303   54.091 1.00 57.56  ? 261 PRO   A C     1 
ATOM   2054 O O     . PRO   A 1 271 ? 55.038 5.934   54.500 1.00 59.44  ? 261 PRO   A O     1 
ATOM   2055 C CB    . PRO   A 1 271 ? 53.731 5.369   51.765 1.00 57.68  ? 261 PRO   A CB    1 
ATOM   2056 C CG    . PRO   A 1 271 ? 52.541 5.338   50.841 1.00 58.15  ? 261 PRO   A CG    1 
ATOM   2057 C CD    . PRO   A 1 271 ? 51.397 5.979   51.600 1.00 58.60  ? 261 PRO   A CD    1 
ATOM   2058 N N     . CYS   A 1 272 ? 53.426 7.504   54.384 1.00 57.18  ? 262 CYS   A N     1 
ATOM   2059 C CA    . CYS   A 1 272 ? 54.141 8.434   55.244 1.00 59.06  ? 262 CYS   A CA    1 
ATOM   2060 C C     . CYS   A 1 272 ? 53.992 8.056   56.717 1.00 59.70  ? 262 CYS   A C     1 
ATOM   2061 O O     . CYS   A 1 272 ? 54.653 8.643   57.569 1.00 61.09  ? 262 CYS   A O     1 
ATOM   2062 C CB    . CYS   A 1 272 ? 53.686 9.867   55.014 1.00 61.37  ? 262 CYS   A CB    1 
ATOM   2063 S SG    . CYS   A 1 272 ? 54.031 10.458  53.336 1.00 66.61  ? 262 CYS   A SG    1 
ATOM   2064 N N     . ALA   A 1 273 ? 53.129 7.082   57.021 1.00 61.31  ? 263 ALA   A N     1 
ATOM   2065 C CA    . ALA   A 1 273 ? 52.946 6.636   58.393 1.00 63.01  ? 263 ALA   A CA    1 
ATOM   2066 C C     . ALA   A 1 273 ? 54.239 6.011   58.919 1.00 63.35  ? 263 ALA   A C     1 
ATOM   2067 O O     . ALA   A 1 273 ? 54.741 5.049   58.348 1.00 62.29  ? 263 ALA   A O     1 
ATOM   2068 C CB    . ALA   A 1 273 ? 51.784 5.671   58.465 1.00 62.33  ? 263 ALA   A CB    1 
ATOM   2069 N N     . GLU   A 1 274 ? 54.784 6.588   59.995 1.00 64.29  ? 264 GLU   A N     1 
ATOM   2070 C CA    . GLU   A 1 274 ? 55.971 6.061   60.649 1.00 65.61  ? 264 GLU   A CA    1 
ATOM   2071 C C     . GLU   A 1 274 ? 55.600 5.010   61.697 1.00 64.39  ? 264 GLU   A C     1 
ATOM   2072 O O     . GLU   A 1 274 ? 56.412 4.133   61.988 1.00 62.00  ? 264 GLU   A O     1 
ATOM   2073 C CB    . GLU   A 1 274 ? 56.778 7.184   61.304 1.00 69.66  ? 264 GLU   A CB    1 
ATOM   2074 C CG    . GLU   A 1 274 ? 57.422 8.140   60.304 1.00 72.39  ? 264 GLU   A CG    1 
ATOM   2075 C CD    . GLU   A 1 274 ? 58.443 7.486   59.391 1.00 75.92  ? 264 GLU   A CD    1 
ATOM   2076 O OE1   . GLU   A 1 274 ? 58.964 6.403   59.744 1.00 78.82  ? 264 GLU   A OE1   1 
ATOM   2077 O OE2   . GLU   A 1 274 ? 58.689 8.051   58.304 1.00 78.97  ? 264 GLU   A OE2   1 
ATOM   2078 N N     . GLN   A 1 275 ? 54.388 5.118   62.268 1.00 62.76  ? 265 GLN   A N     1 
ATOM   2079 C CA    . GLN   A 1 275 ? 53.929 4.236   63.333 1.00 61.32  ? 265 GLN   A CA    1 
ATOM   2080 C C     . GLN   A 1 275 ? 52.582 3.614   62.977 1.00 57.94  ? 265 GLN   A C     1 
ATOM   2081 O O     . GLN   A 1 275 ? 52.430 2.396   63.041 1.00 57.00  ? 265 GLN   A O     1 
ATOM   2082 C CB    . GLN   A 1 275 ? 53.738 4.950   64.673 1.00 64.72  ? 265 GLN   A CB    1 
ATOM   2083 C CG    . GLN   A 1 275 ? 54.986 5.012   65.546 1.00 68.56  ? 265 GLN   A CG    1 
ATOM   2084 C CD    . GLN   A 1 275 ? 56.064 5.910   64.982 1.00 72.91  ? 265 GLN   A CD    1 
ATOM   2085 O OE1   . GLN   A 1 275 ? 57.165 5.458   64.644 1.00 75.65  ? 265 GLN   A OE1   1 
ATOM   2086 N NE2   . GLN   A 1 275 ? 55.753 7.194   64.867 1.00 74.06  ? 265 GLN   A NE2   1 
ATOM   2087 N N     . LYS   A 1 276 ? 51.595 4.456   62.646 1.00 55.51  ? 266 LYS   A N     1 
ATOM   2088 C CA    . LYS   A 1 276 ? 50.223 3.985   62.567 1.00 55.97  ? 266 LYS   A CA    1 
ATOM   2089 C C     . LYS   A 1 276 ? 49.418 4.756   61.525 1.00 55.05  ? 266 LYS   A C     1 
ATOM   2090 O O     . LYS   A 1 276 ? 49.550 5.968   61.395 1.00 56.66  ? 266 LYS   A O     1 
ATOM   2091 C CB    . LYS   A 1 276 ? 49.571 4.128   63.945 1.00 56.53  ? 266 LYS   A CB    1 
ATOM   2092 C CG    . LYS   A 1 276 ? 48.204 3.480   64.082 1.00 56.96  ? 266 LYS   A CG    1 
ATOM   2093 C CD    . LYS   A 1 276 ? 47.580 3.642   65.461 1.00 57.53  ? 266 LYS   A CD    1 
ATOM   2094 C CE    . LYS   A 1 276 ? 46.238 2.994   65.501 1.00 60.16  ? 266 LYS   A CE    1 
ATOM   2095 N NZ    . LYS   A 1 276 ? 45.586 3.153   66.801 1.00 61.31  ? 266 LYS   A NZ    1 
ATOM   2096 N N     . LEU   A 1 277 ? 48.557 4.027   60.812 1.00 54.11  ? 267 LEU   A N     1 
ATOM   2097 C CA    . LEU   A 1 277 ? 47.551 4.623   59.951 1.00 54.20  ? 267 LEU   A CA    1 
ATOM   2098 C C     . LEU   A 1 277 ? 46.166 4.205   60.441 1.00 54.27  ? 267 LEU   A C     1 
ATOM   2099 O O     . LEU   A 1 277 ? 45.943 3.022   60.689 1.00 53.19  ? 267 LEU   A O     1 
ATOM   2100 C CB    . LEU   A 1 277 ? 47.803 4.147   58.522 1.00 53.43  ? 267 LEU   A CB    1 
ATOM   2101 C CG    . LEU   A 1 277 ? 46.718 4.495   57.500 1.00 53.26  ? 267 LEU   A CG    1 
ATOM   2102 C CD1   . LEU   A 1 277 ? 46.712 5.985   57.206 1.00 52.83  ? 267 LEU   A CD1   1 
ATOM   2103 C CD2   . LEU   A 1 277 ? 46.892 3.678   56.231 1.00 53.36  ? 267 LEU   A CD2   1 
ATOM   2104 N N     . THR   A 1 278 ? 45.246 5.175   60.574 1.00 54.50  ? 268 THR   A N     1 
ATOM   2105 C CA    . THR   A 1 278 ? 43.846 4.886   60.856 1.00 54.70  ? 268 THR   A CA    1 
ATOM   2106 C C     . THR   A 1 278 ? 42.977 5.393   59.705 1.00 54.24  ? 268 THR   A C     1 
ATOM   2107 O O     . THR   A 1 278 ? 43.140 6.519   59.248 1.00 52.68  ? 268 THR   A O     1 
ATOM   2108 C CB    . THR   A 1 278 ? 43.407 5.507   62.181 1.00 55.36  ? 268 THR   A CB    1 
ATOM   2109 O OG1   . THR   A 1 278 ? 44.175 4.894   63.212 1.00 56.17  ? 268 THR   A OG1   1 
ATOM   2110 C CG2   . THR   A 1 278 ? 41.938 5.258   62.466 1.00 55.47  ? 268 THR   A CG2   1 
ATOM   2111 N N     . ILE   A 1 279 ? 42.024 4.550   59.290 1.00 54.43  ? 269 ILE   A N     1 
ATOM   2112 C CA    . ILE   A 1 279 ? 41.138 4.812   58.170 1.00 54.83  ? 269 ILE   A CA    1 
ATOM   2113 C C     . ILE   A 1 279 ? 39.703 4.620   58.646 1.00 51.50  ? 269 ILE   A C     1 
ATOM   2114 O O     . ILE   A 1 279 ? 39.418 3.635   59.314 1.00 49.52  ? 269 ILE   A O     1 
ATOM   2115 C CB    . ILE   A 1 279 ? 41.461 3.845   57.015 1.00 60.42  ? 269 ILE   A CB    1 
ATOM   2116 C CG1   . ILE   A 1 279 ? 42.852 4.078   56.451 1.00 64.31  ? 269 ILE   A CG1   1 
ATOM   2117 C CG2   . ILE   A 1 279 ? 40.400 3.899   55.918 1.00 62.13  ? 269 ILE   A CG2   1 
ATOM   2118 C CD1   . ILE   A 1 279 ? 43.049 5.453   55.848 1.00 66.03  ? 269 ILE   A CD1   1 
ATOM   2119 N N     . CYS   A 1 280 ? 38.817 5.555   58.284 1.00 51.69  ? 270 CYS   A N     1 
ATOM   2120 C CA    . CYS   A 1 280 ? 37.378 5.377   58.413 1.00 51.69  ? 270 CYS   A CA    1 
ATOM   2121 C C     . CYS   A 1 280 ? 36.751 5.342   57.020 1.00 52.24  ? 270 CYS   A C     1 
ATOM   2122 O O     . CYS   A 1 280 ? 37.096 6.151   56.164 1.00 55.66  ? 270 CYS   A O     1 
ATOM   2123 C CB    . CYS   A 1 280 ? 36.732 6.509   59.209 1.00 52.26  ? 270 CYS   A CB    1 
ATOM   2124 S SG    . CYS   A 1 280 ? 37.035 6.457   60.998 1.00 51.87  ? 270 CYS   A SG    1 
ATOM   2125 N N     . THR   A 1 281 ? 35.836 4.393   56.797 1.00 51.24  ? 271 THR   A N     1 
ATOM   2126 C CA    . THR   A 1 281 ? 34.946 4.432   55.650 1.00 50.32  ? 271 THR   A CA    1 
ATOM   2127 C C     . THR   A 1 281 ? 33.668 3.670   55.996 1.00 50.56  ? 271 THR   A C     1 
ATOM   2128 O O     . THR   A 1 281 ? 33.721 2.626   56.643 1.00 51.05  ? 271 THR   A O     1 
ATOM   2129 C CB    . THR   A 1 281 ? 35.643 3.861   54.414 1.00 51.39  ? 271 THR   A CB    1 
ATOM   2130 O OG1   . THR   A 1 281 ? 34.654 3.796   53.391 1.00 51.11  ? 271 THR   A OG1   1 
ATOM   2131 C CG2   . THR   A 1 281 ? 36.209 2.469   54.632 1.00 51.75  ? 271 THR   A CG2   1 
ATOM   2132 N N     . PRO   A 1 282 ? 32.477 4.169   55.589 1.00 52.01  ? 272 PRO   A N     1 
ATOM   2133 C CA    . PRO   A 1 282 ? 31.228 3.424   55.749 1.00 53.62  ? 272 PRO   A CA    1 
ATOM   2134 C C     . PRO   A 1 282 ? 30.918 2.468   54.603 1.00 53.68  ? 272 PRO   A C     1 
ATOM   2135 O O     . PRO   A 1 282 ? 29.902 1.781   54.643 1.00 56.07  ? 272 PRO   A O     1 
ATOM   2136 C CB    . PRO   A 1 282 ? 30.219 4.562   55.812 1.00 53.74  ? 272 PRO   A CB    1 
ATOM   2137 C CG    . PRO   A 1 282 ? 30.753 5.551   54.808 1.00 54.63  ? 272 PRO   A CG    1 
ATOM   2138 C CD    . PRO   A 1 282 ? 32.267 5.469   54.936 1.00 53.39  ? 272 PRO   A CD    1 
ATOM   2139 N N     . TYR   A 1 283 ? 31.792 2.459   53.586 1.00 53.89  ? 273 TYR   A N     1 
ATOM   2140 C CA    . TYR   A 1 283 ? 31.669 1.582   52.431 1.00 53.11  ? 273 TYR   A CA    1 
ATOM   2141 C C     . TYR   A 1 283 ? 33.043 0.983   52.135 1.00 54.14  ? 273 TYR   A C     1 
ATOM   2142 O O     . TYR   A 1 283 ? 33.834 1.554   51.379 1.00 53.66  ? 273 TYR   A O     1 
ATOM   2143 C CB    . TYR   A 1 283 ? 31.089 2.394   51.270 1.00 52.16  ? 273 TYR   A CB    1 
ATOM   2144 C CG    . TYR   A 1 283 ? 29.764 3.085   51.573 1.00 51.75  ? 273 TYR   A CG    1 
ATOM   2145 C CD1   . TYR   A 1 283 ? 28.603 2.351   51.778 1.00 51.21  ? 273 TYR   A CD1   1 
ATOM   2146 C CD2   . TYR   A 1 283 ? 29.672 4.472   51.642 1.00 51.90  ? 273 TYR   A CD2   1 
ATOM   2147 C CE1   . TYR   A 1 283 ? 27.395 2.973   52.056 1.00 52.76  ? 273 TYR   A CE1   1 
ATOM   2148 C CE2   . TYR   A 1 283 ? 28.471 5.104   51.927 1.00 51.64  ? 273 TYR   A CE2   1 
ATOM   2149 C CZ    . TYR   A 1 283 ? 27.327 4.354   52.127 1.00 51.66  ? 273 TYR   A CZ    1 
ATOM   2150 O OH    . TYR   A 1 283 ? 26.138 4.963   52.401 1.00 52.00  ? 273 TYR   A OH    1 
ATOM   2151 N N     . PHE   A 1 284 ? 33.331 -0.159  52.769 1.00 54.56  ? 274 PHE   A N     1 
ATOM   2152 C CA    . PHE   A 1 284 ? 34.651 -0.758  52.684 1.00 55.42  ? 274 PHE   A CA    1 
ATOM   2153 C C     . PHE   A 1 284 ? 34.782 -1.467  51.341 1.00 55.43  ? 274 PHE   A C     1 
ATOM   2154 O O     . PHE   A 1 284 ? 34.167 -2.503  51.112 1.00 57.53  ? 274 PHE   A O     1 
ATOM   2155 C CB    . PHE   A 1 284 ? 34.942 -1.728  53.828 1.00 55.59  ? 274 PHE   A CB    1 
ATOM   2156 C CG    . PHE   A 1 284 ? 36.371 -2.244  53.789 1.00 56.36  ? 274 PHE   A CG    1 
ATOM   2157 C CD1   . PHE   A 1 284 ? 37.411 -1.487  54.313 1.00 57.46  ? 274 PHE   A CD1   1 
ATOM   2158 C CD2   . PHE   A 1 284 ? 36.675 -3.469  53.209 1.00 58.54  ? 274 PHE   A CD2   1 
ATOM   2159 C CE1   . PHE   A 1 284 ? 38.716 -1.950  54.270 1.00 58.71  ? 274 PHE   A CE1   1 
ATOM   2160 C CE2   . PHE   A 1 284 ? 37.983 -3.928  53.166 1.00 58.72  ? 274 PHE   A CE2   1 
ATOM   2161 C CZ    . PHE   A 1 284 ? 38.999 -3.169  53.699 1.00 59.31  ? 274 PHE   A CZ    1 
ATOM   2162 N N     . ASN   A 1 285 ? 35.610 -0.889  50.472 1.00 55.83  ? 275 ASN   A N     1 
ATOM   2163 C CA    . ASN   A 1 285 ? 35.788 -1.349  49.107 1.00 56.33  ? 275 ASN   A CA    1 
ATOM   2164 C C     . ASN   A 1 285 ? 37.043 -0.675  48.565 1.00 54.52  ? 275 ASN   A C     1 
ATOM   2165 O O     . ASN   A 1 285 ? 36.969 0.126   47.642 1.00 56.14  ? 275 ASN   A O     1 
ATOM   2166 C CB    . ASN   A 1 285 ? 34.554 -1.039  48.263 1.00 56.51  ? 275 ASN   A CB    1 
ATOM   2167 C CG    . ASN   A 1 285 ? 34.636 -1.585  46.858 1.00 55.94  ? 275 ASN   A CG    1 
ATOM   2168 O OD1   . ASN   A 1 285 ? 35.549 -2.350  46.538 1.00 56.13  ? 275 ASN   A OD1   1 
ATOM   2169 N ND2   . ASN   A 1 285 ? 33.687 -1.214  46.009 1.00 57.35  ? 275 ASN   A ND2   1 
ATOM   2170 N N     . LEU   A 1 286 ? 38.183 -0.961  49.196 1.00 53.91  ? 276 LEU   A N     1 
ATOM   2171 C CA    . LEU   A 1 286 ? 39.410 -0.238  48.912 1.00 55.31  ? 276 LEU   A CA    1 
ATOM   2172 C C     . LEU   A 1 286 ? 39.877 -0.579  47.498 1.00 57.24  ? 276 LEU   A C     1 
ATOM   2173 O O     . LEU   A 1 286 ? 39.921 -1.749  47.122 1.00 57.49  ? 276 LEU   A O     1 
ATOM   2174 C CB    . LEU   A 1 286 ? 40.488 -0.563  49.948 1.00 54.61  ? 276 LEU   A CB    1 
ATOM   2175 C CG    . LEU   A 1 286 ? 40.230 -0.079  51.381 1.00 54.12  ? 276 LEU   A CG    1 
ATOM   2176 C CD1   . LEU   A 1 286 ? 41.301 -0.596  52.335 1.00 52.47  ? 276 LEU   A CD1   1 
ATOM   2177 C CD2   . LEU   A 1 286 ? 40.147 1.439   51.448 1.00 53.60  ? 276 LEU   A CD2   1 
ATOM   2178 N N     . PRO   A 1 287 ? 40.198 0.436   46.662 1.00 58.30  ? 277 PRO   A N     1 
ATOM   2179 C CA    . PRO   A 1 287 ? 40.947 0.209   45.426 1.00 58.03  ? 277 PRO   A CA    1 
ATOM   2180 C C     . PRO   A 1 287 ? 42.280 -0.484  45.699 1.00 58.24  ? 277 PRO   A C     1 
ATOM   2181 O O     . PRO   A 1 287 ? 42.927 -0.222  46.712 1.00 58.74  ? 277 PRO   A O     1 
ATOM   2182 C CB    . PRO   A 1 287 ? 41.148 1.618   44.842 1.00 58.67  ? 277 PRO   A CB    1 
ATOM   2183 C CG    . PRO   A 1 287 ? 40.055 2.453   45.470 1.00 58.91  ? 277 PRO   A CG    1 
ATOM   2184 C CD    . PRO   A 1 287 ? 39.810 1.843   46.838 1.00 58.57  ? 277 PRO   A CD    1 
ATOM   2185 N N     . ALA   A 1 288 ? 42.686 -1.338  44.755 1.00 58.34  ? 278 ALA   A N     1 
ATOM   2186 C CA    . ALA   A 1 288 ? 43.863 -2.177  44.895 1.00 59.14  ? 278 ALA   A CA    1 
ATOM   2187 C C     . ALA   A 1 288 ? 45.078 -1.361  45.338 1.00 58.62  ? 278 ALA   A C     1 
ATOM   2188 O O     . ALA   A 1 288 ? 45.871 -1.827  46.155 1.00 58.49  ? 278 ALA   A O     1 
ATOM   2189 C CB    . ALA   A 1 288 ? 44.127 -2.893  43.586 1.00 60.21  ? 278 ALA   A CB    1 
ATOM   2190 N N     . ILE   A 1 289 ? 45.220 -0.142  44.809 1.00 57.27  ? 279 ILE   A N     1 
ATOM   2191 C CA    . ILE   A 1 289 ? 46.408 0.651   45.083 1.00 59.55  ? 279 ILE   A CA    1 
ATOM   2192 C C     . ILE   A 1 289 ? 46.469 1.013   46.571 1.00 60.36  ? 279 ILE   A C     1 
ATOM   2193 O O     . ILE   A 1 289 ? 47.557 1.114   47.143 1.00 60.50  ? 279 ILE   A O     1 
ATOM   2194 C CB    . ILE   A 1 289 ? 46.473 1.890   44.166 1.00 61.07  ? 279 ILE   A CB    1 
ATOM   2195 C CG1   . ILE   A 1 289 ? 47.878 2.500   44.168 1.00 62.63  ? 279 ILE   A CG1   1 
ATOM   2196 C CG2   . ILE   A 1 289 ? 45.397 2.918   44.523 1.00 61.09  ? 279 ILE   A CG2   1 
ATOM   2197 C CD1   . ILE   A 1 289 ? 48.065 3.650   43.194 1.00 64.48  ? 279 ILE   A CD1   1 
ATOM   2198 N N     . LEU   A 1 290 ? 45.299 1.193   47.201 1.00 58.23  ? 280 LEU   A N     1 
ATOM   2199 C CA    . LEU   A 1 290 ? 45.250 1.542   48.611 1.00 57.78  ? 280 LEU   A CA    1 
ATOM   2200 C C     . LEU   A 1 290 ? 45.522 0.304   49.466 1.00 59.18  ? 280 LEU   A C     1 
ATOM   2201 O O     . LEU   A 1 290 ? 46.161 0.402   50.515 1.00 58.29  ? 280 LEU   A O     1 
ATOM   2202 C CB    . LEU   A 1 290 ? 43.912 2.198   48.951 1.00 56.38  ? 280 LEU   A CB    1 
ATOM   2203 C CG    . LEU   A 1 290 ? 43.635 3.554   48.291 1.00 55.47  ? 280 LEU   A CG    1 
ATOM   2204 C CD1   . LEU   A 1 290 ? 42.401 4.204   48.896 1.00 53.79  ? 280 LEU   A CD1   1 
ATOM   2205 C CD2   . LEU   A 1 290 ? 44.830 4.497   48.374 1.00 55.47  ? 280 LEU   A CD2   1 
ATOM   2206 N N     . VAL   A 1 291 ? 45.050 -0.862  49.008 1.00 60.05  ? 281 VAL   A N     1 
ATOM   2207 C CA    . VAL   A 1 291 ? 45.290 -2.113  49.713 1.00 59.35  ? 281 VAL   A CA    1 
ATOM   2208 C C     . VAL   A 1 291 ? 46.791 -2.406  49.730 1.00 60.75  ? 281 VAL   A C     1 
ATOM   2209 O O     . VAL   A 1 291 ? 47.307 -2.881  50.739 1.00 62.37  ? 281 VAL   A O     1 
ATOM   2210 C CB    . VAL   A 1 291 ? 44.482 -3.273  49.099 1.00 58.21  ? 281 VAL   A CB    1 
ATOM   2211 C CG1   . VAL   A 1 291 ? 44.815 -4.614  49.743 1.00 57.20  ? 281 VAL   A CG1   1 
ATOM   2212 C CG2   . VAL   A 1 291 ? 42.982 -3.006  49.172 1.00 58.25  ? 281 VAL   A CG2   1 
ATOM   2213 N N     . ARG   A 1 292 ? 47.489 -2.107  48.622 1.00 62.07  ? 282 ARG   A N     1 
ATOM   2214 C CA    . ARG   A 1 292 ? 48.922 -2.339  48.525 1.00 62.00  ? 282 ARG   A CA    1 
ATOM   2215 C C     . ARG   A 1 292 ? 49.673 -1.461  49.522 1.00 60.88  ? 282 ARG   A C     1 
ATOM   2216 O O     . ARG   A 1 292 ? 50.658 -1.901  50.104 1.00 62.10  ? 282 ARG   A O     1 
ATOM   2217 C CB    . ARG   A 1 292 ? 49.479 -2.086  47.119 1.00 65.97  ? 282 ARG   A CB    1 
ATOM   2218 C CG    . ARG   A 1 292 ? 49.441 -3.296  46.195 1.00 69.97  ? 282 ARG   A CG    1 
ATOM   2219 C CD    . ARG   A 1 292 ? 50.371 -3.128  44.994 1.00 74.64  ? 282 ARG   A CD    1 
ATOM   2220 N NE    . ARG   A 1 292 ? 49.938 -2.082  44.057 1.00 76.53  ? 282 ARG   A NE    1 
ATOM   2221 C CZ    . ARG   A 1 292 ? 48.870 -2.136  43.262 1.00 76.69  ? 282 ARG   A CZ    1 
ATOM   2222 N NH1   . ARG   A 1 292 ? 48.119 -3.225  43.209 1.00 76.72  ? 282 ARG   A NH1   1 
ATOM   2223 N NH2   . ARG   A 1 292 ? 48.558 -1.094  42.508 1.00 76.67  ? 282 ARG   A NH2   1 
ATOM   2224 N N     . ASN   A 1 293 ? 49.222 -0.212  49.688 1.00 60.57  ? 283 ASN   A N     1 
ATOM   2225 C CA    . ASN   A 1 293 ? 49.789 0.697   50.674 1.00 59.39  ? 283 ASN   A CA    1 
ATOM   2226 C C     . ASN   A 1 293 ? 49.721 0.073   52.068 1.00 58.39  ? 283 ASN   A C     1 
ATOM   2227 O O     . ASN   A 1 293 ? 50.698 0.092   52.817 1.00 57.73  ? 283 ASN   A O     1 
ATOM   2228 C CB    . ASN   A 1 293 ? 49.074 2.046   50.667 1.00 59.99  ? 283 ASN   A CB    1 
ATOM   2229 C CG    . ASN   A 1 293 ? 49.628 3.023   49.655 1.00 61.12  ? 283 ASN   A CG    1 
ATOM   2230 O OD1   . ASN   A 1 293 ? 50.741 2.849   49.145 1.00 59.79  ? 283 ASN   A OD1   1 
ATOM   2231 N ND2   . ASN   A 1 293 ? 48.890 4.091   49.392 1.00 63.01  ? 283 ASN   A ND2   1 
ATOM   2232 N N     . ILE   A 1 294 ? 48.546 -0.466  52.406 1.00 58.25  ? 284 ILE   A N     1 
ATOM   2233 C CA    . ILE   A 1 294 ? 48.291 -1.031  53.719 1.00 57.54  ? 284 ILE   A CA    1 
ATOM   2234 C C     . ILE   A 1 294 ? 49.216 -2.228  53.941 1.00 57.55  ? 284 ILE   A C     1 
ATOM   2235 O O     . ILE   A 1 294 ? 49.860 -2.320  54.981 1.00 56.43  ? 284 ILE   A O     1 
ATOM   2236 C CB    . ILE   A 1 294 ? 46.795 -1.378  53.866 1.00 55.96  ? 284 ILE   A CB    1 
ATOM   2237 C CG1   . ILE   A 1 294 ? 45.949 -0.105  53.946 1.00 55.34  ? 284 ILE   A CG1   1 
ATOM   2238 C CG2   . ILE   A 1 294 ? 46.553 -2.294  55.066 1.00 56.17  ? 284 ILE   A CG2   1 
ATOM   2239 C CD1   . ILE   A 1 294 ? 44.451 -0.333  53.843 1.00 55.50  ? 284 ILE   A CD1   1 
ATOM   2240 N N     . ILE   A 1 295 ? 49.300 -3.119  52.944 1.00 59.93  ? 285 ILE   A N     1 
ATOM   2241 C CA    . ILE   A 1 295 ? 50.151 -4.300  53.020 1.00 61.12  ? 285 ILE   A CA    1 
ATOM   2242 C C     . ILE   A 1 295 ? 51.607 -3.888  53.228 1.00 59.21  ? 285 ILE   A C     1 
ATOM   2243 O O     . ILE   A 1 295 ? 52.333 -4.542  53.971 1.00 60.46  ? 285 ILE   A O     1 
ATOM   2244 C CB    . ILE   A 1 295 ? 49.986 -5.188  51.770 1.00 62.85  ? 285 ILE   A CB    1 
ATOM   2245 C CG1   . ILE   A 1 295 ? 48.618 -5.868  51.756 1.00 64.81  ? 285 ILE   A CG1   1 
ATOM   2246 C CG2   . ILE   A 1 295 ? 51.117 -6.213  51.673 1.00 63.67  ? 285 ILE   A CG2   1 
ATOM   2247 C CD1   . ILE   A 1 295 ? 48.317 -6.657  50.493 1.00 64.98  ? 285 ILE   A CD1   1 
ATOM   2248 N N     . GLN   A 1 296 ? 52.034 -2.829  52.535 1.00 59.38  ? 286 GLN   A N     1 
ATOM   2249 C CA    . GLN   A 1 296 ? 53.385 -2.310  52.671 1.00 62.35  ? 286 GLN   A CA    1 
ATOM   2250 C C     . GLN   A 1 296 ? 53.618 -1.914  54.129 1.00 60.99  ? 286 GLN   A C     1 
ATOM   2251 O O     . GLN   A 1 296 ? 54.580 -2.366  54.749 1.00 58.99  ? 286 GLN   A O     1 
ATOM   2252 C CB    . GLN   A 1 296 ? 53.574 -1.158  51.681 1.00 66.49  ? 286 GLN   A CB    1 
ATOM   2253 C CG    . GLN   A 1 296 ? 54.912 -0.434  51.786 1.00 71.79  ? 286 GLN   A CG    1 
ATOM   2254 C CD    . GLN   A 1 296 ? 56.070 -1.237  51.235 1.00 77.96  ? 286 GLN   A CD    1 
ATOM   2255 O OE1   . GLN   A 1 296 ? 56.476 -2.265  51.794 1.00 80.51  ? 286 GLN   A OE1   1 
ATOM   2256 N NE2   . GLN   A 1 296 ? 56.624 -0.760  50.129 1.00 79.67  ? 286 GLN   A NE2   1 
ATOM   2257 N N     . LEU   A 1 297 ? 52.710 -1.090  54.674 1.00 61.30  ? 287 LEU   A N     1 
ATOM   2258 C CA    . LEU   A 1 297 ? 52.807 -0.621  56.051 1.00 59.46  ? 287 LEU   A CA    1 
ATOM   2259 C C     . LEU   A 1 297 ? 52.921 -1.810  57.003 1.00 56.07  ? 287 LEU   A C     1 
ATOM   2260 O O     . LEU   A 1 297 ? 53.801 -1.833  57.861 1.00 53.85  ? 287 LEU   A O     1 
ATOM   2261 C CB    . LEU   A 1 297 ? 51.613 0.265   56.411 1.00 58.25  ? 287 LEU   A CB    1 
ATOM   2262 C CG    . LEU   A 1 297 ? 51.580 1.656   55.771 1.00 56.27  ? 287 LEU   A CG    1 
ATOM   2263 C CD1   . LEU   A 1 297 ? 50.216 2.294   55.962 1.00 56.02  ? 287 LEU   A CD1   1 
ATOM   2264 C CD2   . LEU   A 1 297 ? 52.666 2.542   56.351 1.00 55.96  ? 287 LEU   A CD2   1 
ATOM   2265 N N     . LEU   A 1 298 ? 52.032 -2.794  56.828 1.00 53.68  ? 288 LEU   A N     1 
ATOM   2266 C CA    . LEU   A 1 298 ? 52.015 -3.978  57.673 1.00 53.35  ? 288 LEU   A CA    1 
ATOM   2267 C C     . LEU   A 1 298 ? 53.357 -4.703  57.599 1.00 54.75  ? 288 LEU   A C     1 
ATOM   2268 O O     . LEU   A 1 298 ? 53.893 -5.138  58.618 1.00 54.49  ? 288 LEU   A O     1 
ATOM   2269 C CB    . LEU   A 1 298 ? 50.859 -4.881  57.250 1.00 50.95  ? 288 LEU   A CB    1 
ATOM   2270 C CG    . LEU   A 1 298 ? 49.455 -4.335  57.524 1.00 49.81  ? 288 LEU   A CG    1 
ATOM   2271 C CD1   . LEU   A 1 298 ? 48.433 -5.323  57.022 1.00 50.32  ? 288 LEU   A CD1   1 
ATOM   2272 C CD2   . LEU   A 1 298 ? 49.216 -4.028  58.991 1.00 50.21  ? 288 LEU   A CD2   1 
ATOM   2273 N N     . ARG   A 1 299 ? 53.912 -4.790  56.387 1.00 56.94  ? 289 ARG   A N     1 
ATOM   2274 C CA    . ARG   A 1 299 ? 55.173 -5.478  56.161 1.00 57.57  ? 289 ARG   A CA    1 
ATOM   2275 C C     . ARG   A 1 299 ? 56.364 -4.713  56.742 1.00 57.59  ? 289 ARG   A C     1 
ATOM   2276 O O     . ARG   A 1 299 ? 57.420 -5.306  56.943 1.00 56.94  ? 289 ARG   A O     1 
ATOM   2277 C CB    . ARG   A 1 299 ? 55.305 -5.745  54.660 1.00 57.69  ? 289 ARG   A CB    1 
ATOM   2278 C CG    . ARG   A 1 299 ? 54.455 -6.942  54.265 1.00 58.53  ? 289 ARG   A CG    1 
ATOM   2279 C CD    . ARG   A 1 299 ? 54.473 -7.171  52.778 1.00 58.62  ? 289 ARG   A CD    1 
ATOM   2280 N NE    . ARG   A 1 299 ? 53.719 -8.379  52.436 1.00 57.34  ? 289 ARG   A NE    1 
ATOM   2281 C CZ    . ARG   A 1 299 ? 53.390 -8.730  51.205 1.00 58.00  ? 289 ARG   A CZ    1 
ATOM   2282 N NH1   . ARG   A 1 299 ? 53.728 -7.970  50.177 1.00 58.15  ? 289 ARG   A NH1   1 
ATOM   2283 N NH2   . ARG   A 1 299 ? 52.706 -9.841  51.005 1.00 59.00  ? 289 ARG   A NH2   1 
ATOM   2284 N N     . GLU   A 1 300 ? 56.196 -3.412  57.016 1.00 59.12  ? 290 GLU   A N     1 
ATOM   2285 C CA    . GLU   A 1 300 ? 57.227 -2.607  57.656 1.00 59.16  ? 290 GLU   A CA    1 
ATOM   2286 C C     . GLU   A 1 300 ? 57.075 -2.623  59.180 1.00 59.35  ? 290 GLU   A C     1 
ATOM   2287 O O     . GLU   A 1 300 ? 57.770 -1.882  59.870 1.00 61.56  ? 290 GLU   A O     1 
ATOM   2288 C CB    . GLU   A 1 300 ? 57.173 -1.177  57.114 1.00 60.49  ? 290 GLU   A CB    1 
ATOM   2289 C CG    . GLU   A 1 300 ? 57.618 -1.060  55.659 1.00 62.97  ? 290 GLU   A CG    1 
ATOM   2290 C CD    . GLU   A 1 300 ? 57.303 0.252   54.953 1.00 65.65  ? 290 GLU   A CD    1 
ATOM   2291 O OE1   . GLU   A 1 300 ? 56.555 1.093   55.497 1.00 66.64  ? 290 GLU   A OE1   1 
ATOM   2292 O OE2   . GLU   A 1 300 ? 57.817 0.428   53.828 1.00 67.78  ? 290 GLU   A OE2   1 
ATOM   2293 N N     . GLY   A 1 301 ? 56.160 -3.450  59.706 1.00 59.14  ? 291 GLY   A N     1 
ATOM   2294 C CA    . GLY   A 1 301 ? 56.007 -3.625  61.144 1.00 58.89  ? 291 GLY   A CA    1 
ATOM   2295 C C     . GLY   A 1 301 ? 55.100 -2.566  61.775 1.00 61.34  ? 291 GLY   A C     1 
ATOM   2296 O O     . GLY   A 1 301 ? 54.987 -2.501  62.998 1.00 63.34  ? 291 GLY   A O     1 
ATOM   2297 N N     . LYS   A 1 302 ? 54.435 -1.759  60.935 1.00 60.68  ? 292 LYS   A N     1 
ATOM   2298 C CA    . LYS   A 1 302 ? 53.627 -0.642  61.397 1.00 59.11  ? 292 LYS   A CA    1 
ATOM   2299 C C     . LYS   A 1 302 ? 52.197 -1.109  61.658 1.00 58.11  ? 292 LYS   A C     1 
ATOM   2300 O O     . LYS   A 1 302 ? 51.831 -2.222  61.300 1.00 56.41  ? 292 LYS   A O     1 
ATOM   2301 C CB    . LYS   A 1 302 ? 53.667 0.472   60.347 1.00 60.67  ? 292 LYS   A CB    1 
ATOM   2302 C CG    . LYS   A 1 302 ? 55.073 0.880   59.931 1.00 61.77  ? 292 LYS   A CG    1 
ATOM   2303 C CD    . LYS   A 1 302 ? 55.153 2.257   59.286 1.00 63.21  ? 292 LYS   A CD    1 
ATOM   2304 C CE    . LYS   A 1 302 ? 56.559 2.734   59.053 1.00 63.39  ? 292 LYS   A CE    1 
ATOM   2305 N NZ    . LYS   A 1 302 ? 57.009 2.449   57.689 1.00 64.21  ? 292 LYS   A NZ    1 
ATOM   2306 N N     . LYS   A 1 303 ? 51.396 -0.234  62.278 1.00 58.31  ? 293 LYS   A N     1 
ATOM   2307 C CA    . LYS   A 1 303 ? 50.039 -0.572  62.670 1.00 59.50  ? 293 LYS   A CA    1 
ATOM   2308 C C     . LYS   A 1 303 ? 49.057 0.082   61.700 1.00 56.95  ? 293 LYS   A C     1 
ATOM   2309 O O     . LYS   A 1 303 ? 49.283 1.192   61.231 1.00 58.61  ? 293 LYS   A O     1 
ATOM   2310 C CB    . LYS   A 1 303 ? 49.814 -0.154  64.129 1.00 64.24  ? 293 LYS   A CB    1 
ATOM   2311 C CG    . LYS   A 1 303 ? 48.488 -0.606  64.740 1.00 68.82  ? 293 LYS   A CG    1 
ATOM   2312 C CD    . LYS   A 1 303 ? 48.162 0.023   66.091 1.00 73.34  ? 293 LYS   A CD    1 
ATOM   2313 C CE    . LYS   A 1 303 ? 48.817 -0.649  67.259 1.00 75.67  ? 293 LYS   A CE    1 
ATOM   2314 N NZ    . LYS   A 1 303 ? 48.061 -1.827  67.693 1.00 76.23  ? 293 LYS   A NZ    1 
ATOM   2315 N N     . VAL   A 1 304 ? 47.965 -0.624  61.394 1.00 55.52  ? 294 VAL   A N     1 
ATOM   2316 C CA    . VAL   A 1 304 ? 46.916 -0.101  60.533 1.00 55.04  ? 294 VAL   A CA    1 
ATOM   2317 C C     . VAL   A 1 304 ? 45.575 -0.352  61.210 1.00 53.94  ? 294 VAL   A C     1 
ATOM   2318 O O     . VAL   A 1 304 ? 45.261 -1.489  61.550 1.00 56.20  ? 294 VAL   A O     1 
ATOM   2319 C CB    . VAL   A 1 304 ? 46.937 -0.716  59.121 1.00 54.35  ? 294 VAL   A CB    1 
ATOM   2320 C CG1   . VAL   A 1 304 ? 45.736 -0.275  58.292 1.00 53.13  ? 294 VAL   A CG1   1 
ATOM   2321 C CG2   . VAL   A 1 304 ? 48.233 -0.389  58.394 1.00 55.05  ? 294 VAL   A CG2   1 
ATOM   2322 N N     . GLU   A 1 305 ? 44.791 0.718   61.378 1.00 52.80  ? 295 GLU   A N     1 
ATOM   2323 C CA    . GLU   A 1 305 ? 43.496 0.643   62.031 1.00 53.60  ? 295 GLU   A CA    1 
ATOM   2324 C C     . GLU   A 1 305 ? 42.424 1.021   61.019 1.00 51.69  ? 295 GLU   A C     1 
ATOM   2325 O O     . GLU   A 1 305 ? 42.510 2.072   60.395 1.00 52.52  ? 295 GLU   A O     1 
ATOM   2326 C CB    . GLU   A 1 305 ? 43.456 1.589   63.230 1.00 56.45  ? 295 GLU   A CB    1 
ATOM   2327 C CG    . GLU   A 1 305 ? 42.153 1.544   64.022 1.00 58.51  ? 295 GLU   A CG    1 
ATOM   2328 C CD    . GLU   A 1 305 ? 42.048 2.588   65.122 1.00 60.23  ? 295 GLU   A CD    1 
ATOM   2329 O OE1   . GLU   A 1 305 ? 42.903 3.497   65.196 1.00 58.81  ? 295 GLU   A OE1   1 
ATOM   2330 O OE2   . GLU   A 1 305 ? 41.094 2.479   65.919 1.00 64.40  ? 295 GLU   A OE2   1 
ATOM   2331 N N     . ILE   A 1 306 ? 41.420 0.155   60.872 1.00 51.20  ? 296 ILE   A N     1 
ATOM   2332 C CA    . ILE   A 1 306 ? 40.372 0.343   59.882 1.00 51.36  ? 296 ILE   A CA    1 
ATOM   2333 C C     . ILE   A 1 306 ? 39.032 0.274   60.602 1.00 52.13  ? 296 ILE   A C     1 
ATOM   2334 O O     . ILE   A 1 306 ? 38.644 -0.792  61.073 1.00 54.53  ? 296 ILE   A O     1 
ATOM   2335 C CB    . ILE   A 1 306 ? 40.484 -0.705  58.754 1.00 49.68  ? 296 ILE   A CB    1 
ATOM   2336 C CG1   . ILE   A 1 306 ? 41.831 -0.593  58.033 1.00 49.24  ? 296 ILE   A CG1   1 
ATOM   2337 C CG2   . ILE   A 1 306 ? 39.311 -0.599  57.776 1.00 48.64  ? 296 ILE   A CG2   1 
ATOM   2338 C CD1   . ILE   A 1 306 ? 42.035 -1.611  56.926 1.00 50.08  ? 296 ILE   A CD1   1 
ATOM   2339 N N     . ILE   A 1 307 ? 38.336 1.415   60.664 1.00 52.31  ? 297 ILE   A N     1 
ATOM   2340 C CA    . ILE   A 1 307 ? 37.096 1.533   61.413 1.00 52.91  ? 297 ILE   A CA    1 
ATOM   2341 C C     . ILE   A 1 307 ? 35.939 1.592   60.419 1.00 52.58  ? 297 ILE   A C     1 
ATOM   2342 O O     . ILE   A 1 307 ? 35.742 2.601   59.750 1.00 52.43  ? 297 ILE   A O     1 
ATOM   2343 C CB    . ILE   A 1 307 ? 37.138 2.758   62.345 1.00 52.88  ? 297 ILE   A CB    1 
ATOM   2344 C CG1   . ILE   A 1 307 ? 38.422 2.774   63.179 1.00 52.98  ? 297 ILE   A CG1   1 
ATOM   2345 C CG2   . ILE   A 1 307 ? 35.892 2.819   63.232 1.00 54.06  ? 297 ILE   A CG2   1 
ATOM   2346 C CD1   . ILE   A 1 307 ? 38.589 4.009   64.044 1.00 53.75  ? 297 ILE   A CD1   1 
ATOM   2347 N N     . VAL   A 1 308 ? 35.191 0.487   60.337 1.00 53.48  ? 298 VAL   A N     1 
ATOM   2348 C CA    . VAL   A 1 308 ? 34.081 0.342   59.411 1.00 53.62  ? 298 VAL   A CA    1 
ATOM   2349 C C     . VAL   A 1 308 ? 32.821 0.046   60.212 1.00 52.83  ? 298 VAL   A C     1 
ATOM   2350 O O     . VAL   A 1 308 ? 32.893 -0.401  61.353 1.00 52.20  ? 298 VAL   A O     1 
ATOM   2351 C CB    . VAL   A 1 308 ? 34.328 -0.763  58.367 1.00 54.72  ? 298 VAL   A CB    1 
ATOM   2352 C CG1   . VAL   A 1 308 ? 35.297 -0.314  57.282 1.00 56.03  ? 298 VAL   A CG1   1 
ATOM   2353 C CG2   . VAL   A 1 308 ? 34.812 -2.058  59.010 1.00 55.10  ? 298 VAL   A CG2   1 
ATOM   2354 N N     . GLY   A 1 309 ? 31.668 0.293   59.587 1.00 53.08  ? 299 GLY   A N     1 
ATOM   2355 C CA    . GLY   A 1 309 ? 30.386 0.012   60.202 1.00 53.20  ? 299 GLY   A CA    1 
ATOM   2356 C C     . GLY   A 1 309 ? 30.019 -1.456  60.026 1.00 53.98  ? 299 GLY   A C     1 
ATOM   2357 O O     . GLY   A 1 309 ? 30.374 -2.073  59.025 1.00 53.96  ? 299 GLY   A O     1 
ATOM   2358 N N     . ASP   A 1 310 ? 29.310 -2.005  61.016 1.00 54.19  ? 300 ASP   A N     1 
ATOM   2359 C CA    . ASP   A 1 310 ? 28.613 -3.266  60.841 1.00 54.26  ? 300 ASP   A CA    1 
ATOM   2360 C C     . ASP   A 1 310 ? 27.622 -3.094  59.697 1.00 53.95  ? 300 ASP   A C     1 
ATOM   2361 O O     . ASP   A 1 310 ? 27.163 -1.985  59.436 1.00 56.48  ? 300 ASP   A O     1 
ATOM   2362 C CB    . ASP   A 1 310 ? 27.919 -3.706  62.120 1.00 53.82  ? 300 ASP   A CB    1 
ATOM   2363 C CG    . ASP   A 1 310 ? 27.297 -5.093  62.066 1.00 53.81  ? 300 ASP   A CG    1 
ATOM   2364 O OD1   . ASP   A 1 310 ? 28.060 -6.068  61.918 1.00 52.21  ? 300 ASP   A OD1   1 
ATOM   2365 O OD2   . ASP   A 1 310 ? 26.055 -5.184  62.150 1.00 55.33  ? 300 ASP   A OD2   1 
ATOM   2366 N N     . LYS   A 1 311 ? 27.292 -4.193  59.019 1.00 53.32  ? 301 LYS   A N     1 
ATOM   2367 C CA    . LYS   A 1 311 ? 26.360 -4.131  57.908 1.00 55.57  ? 301 LYS   A CA    1 
ATOM   2368 C C     . LYS   A 1 311 ? 25.006 -3.592  58.374 1.00 54.34  ? 301 LYS   A C     1 
ATOM   2369 O O     . LYS   A 1 311 ? 24.320 -2.936  57.593 1.00 50.56  ? 301 LYS   A O     1 
ATOM   2370 C CB    . LYS   A 1 311 ? 26.222 -5.506  57.249 1.00 58.28  ? 301 LYS   A CB    1 
ATOM   2371 C CG    . LYS   A 1 311 ? 25.617 -6.567  58.143 1.00 60.62  ? 301 LYS   A CG    1 
ATOM   2372 C CD    . LYS   A 1 311 ? 25.718 -7.966  57.554 1.00 62.60  ? 301 LYS   A CD    1 
ATOM   2373 C CE    . LYS   A 1 311 ? 25.652 -8.994  58.625 1.00 62.12  ? 301 LYS   A CE    1 
ATOM   2374 N NZ    . LYS   A 1 311 ? 25.977 -10.296 58.057 1.00 62.73  ? 301 LYS   A NZ    1 
ATOM   2375 N N     . THR   A 1 312 ? 24.641 -3.861  59.642 1.00 54.98  ? 302 THR   A N     1 
ATOM   2376 C CA    . THR   A 1 312 ? 23.383 -3.399  60.223 1.00 54.08  ? 302 THR   A CA    1 
ATOM   2377 C C     . THR   A 1 312 ? 23.413 -1.888  60.471 1.00 53.21  ? 302 THR   A C     1 
ATOM   2378 O O     . THR   A 1 312 ? 22.365 -1.281  60.695 1.00 52.50  ? 302 THR   A O     1 
ATOM   2379 C CB    . THR   A 1 312 ? 23.066 -4.157  61.516 1.00 54.66  ? 302 THR   A CB    1 
ATOM   2380 O OG1   . THR   A 1 312 ? 24.085 -3.840  62.459 1.00 54.12  ? 302 THR   A OG1   1 
ATOM   2381 C CG2   . THR   A 1 312 ? 22.981 -5.663  61.327 1.00 54.53  ? 302 THR   A CG2   1 
ATOM   2382 N N     . ALA   A 1 313 ? 24.612 -1.288  60.427 1.00 52.69  ? 303 ALA   A N     1 
ATOM   2383 C CA    . ALA   A 1 313 ? 24.782 0.148   60.584 1.00 53.66  ? 303 ALA   A CA    1 
ATOM   2384 C C     . ALA   A 1 313 ? 25.018 0.833   59.234 1.00 55.39  ? 303 ALA   A C     1 
ATOM   2385 O O     . ALA   A 1 313 ? 25.395 2.002   59.195 1.00 57.18  ? 303 ALA   A O     1 
ATOM   2386 C CB    . ALA   A 1 313 ? 25.925 0.410   61.539 1.00 53.50  ? 303 ALA   A CB    1 
ATOM   2387 N N     . ASN   A 1 314 ? 24.797 0.103   58.133 1.00 55.26  ? 304 ASN   A N     1 
ATOM   2388 C CA    . ASN   A 1 314 ? 24.843 0.663   56.792 1.00 56.06  ? 304 ASN   A CA    1 
ATOM   2389 C C     . ASN   A 1 314 ? 23.451 1.178   56.442 1.00 57.90  ? 304 ASN   A C     1 
ATOM   2390 O O     . ASN   A 1 314 ? 22.462 0.506   56.725 1.00 59.10  ? 304 ASN   A O     1 
ATOM   2391 C CB    . ASN   A 1 314 ? 25.329 -0.384  55.795 1.00 57.26  ? 304 ASN   A CB    1 
ATOM   2392 C CG    . ASN   A 1 314 ? 25.602 0.198   54.429 1.00 58.00  ? 304 ASN   A CG    1 
ATOM   2393 O OD1   . ASN   A 1 314 ? 24.671 0.596   53.717 1.00 57.04  ? 304 ASN   A OD1   1 
ATOM   2394 N ND2   . ASN   A 1 314 ? 26.870 0.244   54.047 1.00 58.64  ? 304 ASN   A ND2   1 
ATOM   2395 N N     . ASP   A 1 315 ? 23.364 2.354   55.807 1.00 61.20  ? 305 ASP   A N     1 
ATOM   2396 C CA    . ASP   A 1 315 ? 22.069 3.003   55.654 1.00 65.11  ? 305 ASP   A CA    1 
ATOM   2397 C C     . ASP   A 1 315 ? 21.264 2.348   54.532 1.00 63.20  ? 305 ASP   A C     1 
ATOM   2398 O O     . ASP   A 1 315 ? 20.107 2.709   54.339 1.00 63.53  ? 305 ASP   A O     1 
ATOM   2399 C CB    . ASP   A 1 315 ? 22.179 4.520   55.550 1.00 68.55  ? 305 ASP   A CB    1 
ATOM   2400 C CG    . ASP   A 1 315 ? 22.203 5.110   54.149 1.00 72.55  ? 305 ASP   A CG    1 
ATOM   2401 O OD1   . ASP   A 1 315 ? 23.095 4.701   53.367 1.00 76.91  ? 305 ASP   A OD1   1 
ATOM   2402 O OD2   . ASP   A 1 315 ? 21.331 5.973   53.862 1.00 68.98  ? 305 ASP   A OD2   1 
ATOM   2403 N N     . PHE   A 1 316 ? 21.862 1.378   53.822 1.00 62.94  ? 306 PHE   A N     1 
ATOM   2404 C CA    . PHE   A 1 316 ? 21.155 0.594   52.818 1.00 62.73  ? 306 PHE   A CA    1 
ATOM   2405 C C     . PHE   A 1 316 ? 20.559 -0.673  53.430 1.00 63.07  ? 306 PHE   A C     1 
ATOM   2406 O O     . PHE   A 1 316 ? 19.819 -1.387  52.755 1.00 63.27  ? 306 PHE   A O     1 
ATOM   2407 C CB    . PHE   A 1 316 ? 22.073 0.200   51.656 1.00 62.56  ? 306 PHE   A CB    1 
ATOM   2408 C CG    . PHE   A 1 316 ? 22.454 1.349   50.732 1.00 61.87  ? 306 PHE   A CG    1 
ATOM   2409 C CD1   . PHE   A 1 316 ? 21.579 1.786   49.744 1.00 61.88  ? 306 PHE   A CD1   1 
ATOM   2410 C CD2   . PHE   A 1 316 ? 23.687 1.980   50.846 1.00 61.45  ? 306 PHE   A CD2   1 
ATOM   2411 C CE1   . PHE   A 1 316 ? 21.922 2.836   48.906 1.00 61.31  ? 306 PHE   A CE1   1 
ATOM   2412 C CE2   . PHE   A 1 316 ? 24.026 3.023   50.000 1.00 62.44  ? 306 PHE   A CE2   1 
ATOM   2413 C CZ    . PHE   A 1 316 ? 23.143 3.450   49.032 1.00 61.28  ? 306 PHE   A CZ    1 
ATOM   2414 N N     . TYR   A 1 317 ? 20.880 -0.950  54.700 1.00 63.39  ? 307 TYR   A N     1 
ATOM   2415 C CA    . TYR   A 1 317 ? 20.469 -2.188  55.342 1.00 63.64  ? 307 TYR   A CA    1 
ATOM   2416 C C     . TYR   A 1 317 ? 18.952 -2.199  55.514 1.00 64.19  ? 307 TYR   A C     1 
ATOM   2417 O O     . TYR   A 1 317 ? 18.357 -1.204  55.915 1.00 64.91  ? 307 TYR   A O     1 
ATOM   2418 C CB    . TYR   A 1 317 ? 21.202 -2.343  56.677 1.00 64.01  ? 307 TYR   A CB    1 
ATOM   2419 C CG    . TYR   A 1 317 ? 20.876 -3.622  57.434 1.00 64.98  ? 307 TYR   A CG    1 
ATOM   2420 C CD1   . TYR   A 1 317 ? 21.380 -4.851  57.021 1.00 65.30  ? 307 TYR   A CD1   1 
ATOM   2421 C CD2   . TYR   A 1 317 ? 20.076 -3.599  58.571 1.00 66.22  ? 307 TYR   A CD2   1 
ATOM   2422 C CE1   . TYR   A 1 317 ? 21.080 -6.020  57.705 1.00 65.53  ? 307 TYR   A CE1   1 
ATOM   2423 C CE2   . TYR   A 1 317 ? 19.773 -4.760  59.266 1.00 65.53  ? 307 TYR   A CE2   1 
ATOM   2424 C CZ    . TYR   A 1 317 ? 20.275 -5.973  58.831 1.00 65.13  ? 307 TYR   A CZ    1 
ATOM   2425 O OH    . TYR   A 1 317 ? 19.981 -7.112  59.522 1.00 65.33  ? 307 TYR   A OH    1 
ATOM   2426 N N     . ILE   A 1 318 ? 18.343 -3.343  55.191 1.00 65.66  ? 308 ILE   A N     1 
ATOM   2427 C CA    . ILE   A 1 318 ? 16.945 -3.601  55.493 1.00 65.29  ? 308 ILE   A CA    1 
ATOM   2428 C C     . ILE   A 1 318 ? 16.898 -4.800  56.440 1.00 65.80  ? 308 ILE   A C     1 
ATOM   2429 O O     . ILE   A 1 318 ? 17.452 -5.849  56.115 1.00 63.81  ? 308 ILE   A O     1 
ATOM   2430 C CB    . ILE   A 1 318 ? 16.144 -3.843  54.198 1.00 66.16  ? 308 ILE   A CB    1 
ATOM   2431 C CG1   . ILE   A 1 318 ? 16.458 -2.786  53.129 1.00 66.83  ? 308 ILE   A CG1   1 
ATOM   2432 C CG2   . ILE   A 1 318 ? 14.644 -3.924  54.484 1.00 66.71  ? 308 ILE   A CG2   1 
ATOM   2433 C CD1   . ILE   A 1 318 ? 15.746 -3.002  51.805 1.00 67.26  ? 308 ILE   A CD1   1 
ATOM   2434 N N     . PRO   A 1 319 ? 16.274 -4.681  57.641 1.00 69.79  ? 309 PRO   A N     1 
ATOM   2435 C CA    . PRO   A 1 319 ? 16.136 -5.817  58.563 1.00 70.87  ? 309 PRO   A CA    1 
ATOM   2436 C C     . PRO   A 1 319 ? 15.396 -7.008  57.954 1.00 75.32  ? 309 PRO   A C     1 
ATOM   2437 O O     . PRO   A 1 319 ? 14.697 -6.855  56.953 1.00 77.69  ? 309 PRO   A O     1 
ATOM   2438 C CB    . PRO   A 1 319 ? 15.364 -5.239  59.770 1.00 69.69  ? 309 PRO   A CB    1 
ATOM   2439 C CG    . PRO   A 1 319 ? 15.517 -3.735  59.658 1.00 69.04  ? 309 PRO   A CG    1 
ATOM   2440 C CD    . PRO   A 1 319 ? 15.689 -3.439  58.179 1.00 69.33  ? 309 PRO   A CD    1 
ATOM   2441 N N     . GLU   A 1 320 ? 15.553 -8.192  58.567 1.00 80.13  ? 310 GLU   A N     1 
ATOM   2442 C CA    . GLU   A 1 320 ? 14.798 -9.377  58.179 1.00 83.83  ? 310 GLU   A CA    1 
ATOM   2443 C C     . GLU   A 1 320 ? 13.298 -9.073  58.217 1.00 86.92  ? 310 GLU   A C     1 
ATOM   2444 O O     . GLU   A 1 320 ? 12.583 -9.409  57.277 1.00 89.21  ? 310 GLU   A O     1 
ATOM   2445 C CB    . GLU   A 1 320 ? 15.055 -10.590 59.078 1.00 85.97  ? 310 GLU   A CB    1 
ATOM   2446 C CG    . GLU   A 1 320 ? 16.263 -11.444 58.695 1.00 85.88  ? 310 GLU   A CG    1 
ATOM   2447 C CD    . GLU   A 1 320 ? 17.613 -10.905 59.137 1.00 84.72  ? 310 GLU   A CD    1 
ATOM   2448 O OE1   . GLU   A 1 320 ? 17.708 -9.682  59.372 1.00 85.82  ? 310 GLU   A OE1   1 
ATOM   2449 O OE2   . GLU   A 1 320 ? 18.564 -11.709 59.274 1.00 80.40  ? 310 GLU   A OE2   1 
ATOM   2450 N N     . ASP   A 1 321 ? 12.843 -8.452  59.317 1.00 89.27  ? 311 ASP   A N     1 
ATOM   2451 C CA    . ASP   A 1 321 ? 11.462 -8.022  59.500 1.00 90.14  ? 311 ASP   A CA    1 
ATOM   2452 C C     . ASP   A 1 321 ? 10.839 -7.554  58.186 1.00 92.53  ? 311 ASP   A C     1 
ATOM   2453 O O     . ASP   A 1 321 ? 9.892  -8.163  57.693 1.00 98.38  ? 311 ASP   A O     1 
ATOM   2454 C CB    . ASP   A 1 321 ? 11.361 -6.859  60.477 1.00 89.36  ? 311 ASP   A CB    1 
ATOM   2455 C CG    . ASP   A 1 321 ? 11.490 -7.193  61.955 1.00 89.29  ? 311 ASP   A CG    1 
ATOM   2456 O OD1   . ASP   A 1 321 ? 11.437 -8.391  62.300 1.00 88.12  ? 311 ASP   A OD1   1 
ATOM   2457 O OD2   . ASP   A 1 321 ? 11.648 -6.242  62.746 1.00 89.71  ? 311 ASP   A OD2   1 
ATOM   2458 N N     . GLU   A 1 322 ? 11.381 -6.459  57.639 1.00 91.73  ? 312 GLU   A N     1 
ATOM   2459 C CA    . GLU   A 1 322 ? 10.749 -5.714  56.562 1.00 89.82  ? 312 GLU   A CA    1 
ATOM   2460 C C     . GLU   A 1 322 ? 10.942 -6.442  55.233 1.00 88.12  ? 312 GLU   A C     1 
ATOM   2461 O O     . GLU   A 1 322 ? 11.850 -7.262  55.096 1.00 84.86  ? 312 GLU   A O     1 
ATOM   2462 C CB    . GLU   A 1 322 ? 11.335 -4.301  56.566 1.00 89.90  ? 312 GLU   A CB    1 
ATOM   2463 C CG    . GLU   A 1 322 ? 10.869 -3.476  57.763 1.00 90.06  ? 312 GLU   A CG    1 
ATOM   2464 C CD    . GLU   A 1 322 ? 11.940 -2.616  58.407 1.00 90.65  ? 312 GLU   A CD    1 
ATOM   2465 O OE1   . GLU   A 1 322 ? 12.235 -2.866  59.595 1.00 89.67  ? 312 GLU   A OE1   1 
ATOM   2466 O OE2   . GLU   A 1 322 ? 12.479 -1.710  57.736 1.00 92.28  ? 312 GLU   A OE2   1 
ATOM   2467 N N     . PRO   A 1 323 ? 10.096 -6.170  54.212 1.00 89.12  ? 313 PRO   A N     1 
ATOM   2468 C CA    . PRO   A 1 323 ? 10.227 -6.838  52.918 1.00 89.15  ? 313 PRO   A CA    1 
ATOM   2469 C C     . PRO   A 1 323 ? 11.629 -6.595  52.371 1.00 88.27  ? 313 PRO   A C     1 
ATOM   2470 O O     . PRO   A 1 323 ? 12.167 -5.498  52.518 1.00 88.12  ? 313 PRO   A O     1 
ATOM   2471 C CB    . PRO   A 1 323 ? 9.125  -6.200  52.047 1.00 90.51  ? 313 PRO   A CB    1 
ATOM   2472 C CG    . PRO   A 1 323 ? 8.808  -4.889  52.744 1.00 90.52  ? 313 PRO   A CG    1 
ATOM   2473 C CD    . PRO   A 1 323 ? 9.000  -5.187  54.225 1.00 89.79  ? 313 PRO   A CD    1 
ATOM   2474 N N     . PHE   A 1 324 ? 12.215 -7.629  51.762 1.00 86.77  ? 314 PHE   A N     1 
ATOM   2475 C CA    . PHE   A 1 324 ? 13.534 -7.502  51.168 1.00 85.63  ? 314 PHE   A CA    1 
ATOM   2476 C C     . PHE   A 1 324 ? 13.426 -6.704  49.871 1.00 86.44  ? 314 PHE   A C     1 
ATOM   2477 O O     . PHE   A 1 324 ? 12.465 -6.861  49.122 1.00 91.46  ? 314 PHE   A O     1 
ATOM   2478 C CB    . PHE   A 1 324 ? 14.179 -8.865  50.911 1.00 84.44  ? 314 PHE   A CB    1 
ATOM   2479 C CG    . PHE   A 1 324 ? 15.514 -8.729  50.198 1.00 85.49  ? 314 PHE   A CG    1 
ATOM   2480 C CD1   . PHE   A 1 324 ? 16.596 -8.127  50.835 1.00 85.61  ? 314 PHE   A CD1   1 
ATOM   2481 C CD2   . PHE   A 1 324 ? 15.678 -9.175  48.890 1.00 85.08  ? 314 PHE   A CD2   1 
ATOM   2482 C CE1   . PHE   A 1 324 ? 17.810 -7.982  50.182 1.00 85.51  ? 314 PHE   A CE1   1 
ATOM   2483 C CE2   . PHE   A 1 324 ? 16.898 -9.036  48.244 1.00 85.36  ? 314 PHE   A CE2   1 
ATOM   2484 C CZ    . PHE   A 1 324 ? 17.962 -8.442  48.891 1.00 85.68  ? 314 PHE   A CZ    1 
ATOM   2485 N N     . LYS   A 1 325 ? 14.417 -5.833  49.639 1.00 84.73  ? 315 LYS   A N     1 
ATOM   2486 C CA    . LYS   A 1 325 ? 14.573 -5.110  48.387 1.00 82.78  ? 315 LYS   A CA    1 
ATOM   2487 C C     . LYS   A 1 325 ? 16.010 -5.314  47.919 1.00 79.26  ? 315 LYS   A C     1 
ATOM   2488 O O     . LYS   A 1 325 ? 16.906 -5.491  48.738 1.00 79.32  ? 315 LYS   A O     1 
ATOM   2489 C CB    . LYS   A 1 325 ? 14.246 -3.618  48.542 1.00 84.91  ? 315 LYS   A CB    1 
ATOM   2490 C CG    . LYS   A 1 325 ? 12.806 -3.282  48.934 1.00 87.99  ? 315 LYS   A CG    1 
ATOM   2491 C CD    . LYS   A 1 325 ? 11.784 -3.406  47.806 1.00 90.78  ? 315 LYS   A CD    1 
ATOM   2492 C CE    . LYS   A 1 325 ? 10.359 -3.508  48.281 1.00 91.29  ? 315 LYS   A CE    1 
ATOM   2493 N NZ    . LYS   A 1 325 ? 9.922  -2.350  49.065 1.00 91.62  ? 315 LYS   A NZ    1 
ATOM   2494 N N     . ILE   A 1 326 ? 16.221 -5.263  46.601 1.00 77.82  ? 316 ILE   A N     1 
ATOM   2495 C CA    . ILE   A 1 326 ? 17.465 -5.717  46.000 1.00 77.76  ? 316 ILE   A CA    1 
ATOM   2496 C C     . ILE   A 1 326 ? 18.622 -4.816  46.441 1.00 77.36  ? 316 ILE   A C     1 
ATOM   2497 O O     . ILE   A 1 326 ? 19.741 -5.298  46.616 1.00 75.66  ? 316 ILE   A O     1 
ATOM   2498 C CB    . ILE   A 1 326 ? 17.329 -5.801  44.467 1.00 78.95  ? 316 ILE   A CB    1 
ATOM   2499 C CG1   . ILE   A 1 326 ? 16.176 -6.733  44.059 1.00 80.70  ? 316 ILE   A CG1   1 
ATOM   2500 C CG2   . ILE   A 1 326 ? 18.648 -6.230  43.824 1.00 78.32  ? 316 ILE   A CG2   1 
ATOM   2501 C CD1   . ILE   A 1 326 ? 15.869 -6.746  42.571 1.00 80.12  ? 316 ILE   A CD1   1 
ATOM   2502 N N     . ILE   A 1 327 ? 18.343 -3.519  46.643 1.00 76.31  ? 317 ILE   A N     1 
ATOM   2503 C CA    . ILE   A 1 327 ? 19.351 -2.559  47.075 1.00 74.42  ? 317 ILE   A CA    1 
ATOM   2504 C C     . ILE   A 1 327 ? 19.867 -2.936  48.467 1.00 71.53  ? 317 ILE   A C     1 
ATOM   2505 O O     . ILE   A 1 327 ? 20.995 -2.596  48.821 1.00 69.62  ? 317 ILE   A O     1 
ATOM   2506 C CB    . ILE   A 1 327 ? 18.797 -1.117  47.035 1.00 75.61  ? 317 ILE   A CB    1 
ATOM   2507 C CG1   . ILE   A 1 327 ? 19.913 -0.065  47.036 1.00 74.81  ? 317 ILE   A CG1   1 
ATOM   2508 C CG2   . ILE   A 1 327 ? 17.793 -0.863  48.163 1.00 75.84  ? 317 ILE   A CG2   1 
ATOM   2509 C CD1   . ILE   A 1 327 ? 20.716 -0.006  45.749 1.00 75.02  ? 317 ILE   A CD1   1 
ATOM   2510 N N     . GLY   A 1 328 ? 19.044 -3.655  49.241 1.00 68.82  ? 318 GLY   A N     1 
ATOM   2511 C CA    . GLY   A 1 328 ? 19.403 -4.079  50.584 1.00 67.14  ? 318 GLY   A CA    1 
ATOM   2512 C C     . GLY   A 1 328 ? 20.532 -5.109  50.617 1.00 66.17  ? 318 GLY   A C     1 
ATOM   2513 O O     . GLY   A 1 328 ? 20.927 -5.537  51.698 1.00 66.22  ? 318 GLY   A O     1 
ATOM   2514 N N     . ALA   A 1 329 ? 21.053 -5.498  49.445 1.00 65.34  ? 319 ALA   A N     1 
ATOM   2515 C CA    . ALA   A 1 329 ? 22.146 -6.457  49.363 1.00 65.31  ? 319 ALA   A CA    1 
ATOM   2516 C C     . ALA   A 1 329 ? 23.513 -5.784  49.493 1.00 64.71  ? 319 ALA   A C     1 
ATOM   2517 O O     . ALA   A 1 329 ? 24.515 -6.482  49.650 1.00 64.67  ? 319 ALA   A O     1 
ATOM   2518 C CB    . ALA   A 1 329 ? 22.054 -7.223  48.062 1.00 65.89  ? 319 ALA   A CB    1 
ATOM   2519 N N     . LEU   A 1 330 ? 23.558 -4.443  49.418 1.00 63.35  ? 320 LEU   A N     1 
ATOM   2520 C CA    . LEU   A 1 330 ? 24.818 -3.709  49.373 1.00 62.92  ? 320 LEU   A CA    1 
ATOM   2521 C C     . LEU   A 1 330 ? 25.645 -3.959  50.635 1.00 61.68  ? 320 LEU   A C     1 
ATOM   2522 O O     . LEU   A 1 330 ? 26.831 -4.259  50.523 1.00 62.55  ? 320 LEU   A O     1 
ATOM   2523 C CB    . LEU   A 1 330 ? 24.625 -2.206  49.155 1.00 64.05  ? 320 LEU   A CB    1 
ATOM   2524 C CG    . LEU   A 1 330 ? 24.171 -1.755  47.763 1.00 64.26  ? 320 LEU   A CG    1 
ATOM   2525 C CD1   . LEU   A 1 330 ? 24.297 -0.245  47.680 1.00 63.99  ? 320 LEU   A CD1   1 
ATOM   2526 C CD2   . LEU   A 1 330 ? 24.934 -2.422  46.629 1.00 64.18  ? 320 LEU   A CD2   1 
ATOM   2527 N N     . PRO   A 1 331 ? 25.085 -3.835  51.865 1.00 59.93  ? 321 PRO   A N     1 
ATOM   2528 C CA    . PRO   A 1 331 ? 25.879 -4.014  53.084 1.00 58.93  ? 321 PRO   A CA    1 
ATOM   2529 C C     . PRO   A 1 331 ? 26.526 -5.395  53.163 1.00 57.10  ? 321 PRO   A C     1 
ATOM   2530 O O     . PRO   A 1 331 ? 27.626 -5.557  53.700 1.00 56.98  ? 321 PRO   A O     1 
ATOM   2531 C CB    . PRO   A 1 331 ? 24.870 -3.772  54.221 1.00 59.41  ? 321 PRO   A CB    1 
ATOM   2532 C CG    . PRO   A 1 331 ? 23.768 -2.970  53.568 1.00 60.53  ? 321 PRO   A CG    1 
ATOM   2533 C CD    . PRO   A 1 331 ? 23.676 -3.525  52.157 1.00 60.24  ? 321 PRO   A CD    1 
ATOM   2534 N N     . TYR   A 1 332 ? 25.833 -6.389  52.605 1.00 56.07  ? 322 TYR   A N     1 
ATOM   2535 C CA    . TYR   A 1 332 ? 26.367 -7.738  52.553 1.00 56.55  ? 322 TYR   A CA    1 
ATOM   2536 C C     . TYR   A 1 332 ? 27.609 -7.742  51.663 1.00 55.38  ? 322 TYR   A C     1 
ATOM   2537 O O     . TYR   A 1 332 ? 28.625 -8.322  52.033 1.00 55.47  ? 322 TYR   A O     1 
ATOM   2538 C CB    . TYR   A 1 332 ? 25.240 -8.690  52.137 1.00 56.25  ? 322 TYR   A CB    1 
ATOM   2539 C CG    . TYR   A 1 332 ? 24.114 -8.809  53.158 1.00 55.78  ? 322 TYR   A CG    1 
ATOM   2540 C CD1   . TYR   A 1 332 ? 24.215 -9.670  54.243 1.00 56.24  ? 322 TYR   A CD1   1 
ATOM   2541 C CD2   . TYR   A 1 332 ? 22.950 -8.057  53.042 1.00 56.79  ? 322 TYR   A CD2   1 
ATOM   2542 C CE1   . TYR   A 1 332 ? 23.197 -9.786  55.176 1.00 55.34  ? 322 TYR   A CE1   1 
ATOM   2543 C CE2   . TYR   A 1 332 ? 21.925 -8.161  53.970 1.00 56.22  ? 322 TYR   A CE2   1 
ATOM   2544 C CZ    . TYR   A 1 332 ? 22.048 -9.031  55.037 1.00 54.87  ? 322 TYR   A CZ    1 
ATOM   2545 O OH    . TYR   A 1 332 ? 21.047 -9.137  55.956 1.00 54.46  ? 322 TYR   A OH    1 
ATOM   2546 N N     . LEU   A 1 333 ? 27.540 -7.064  50.511 1.00 56.14  ? 323 LEU   A N     1 
ATOM   2547 C CA    . LEU   A 1 333 ? 28.672 -6.995  49.596 1.00 57.34  ? 323 LEU   A CA    1 
ATOM   2548 C C     . LEU   A 1 333 ? 29.843 -6.271  50.258 1.00 57.17  ? 323 LEU   A C     1 
ATOM   2549 O O     . LEU   A 1 333 ? 30.992 -6.678  50.116 1.00 57.95  ? 323 LEU   A O     1 
ATOM   2550 C CB    . LEU   A 1 333 ? 28.295 -6.310  48.283 1.00 57.91  ? 323 LEU   A CB    1 
ATOM   2551 C CG    . LEU   A 1 333 ? 27.283 -7.033  47.389 1.00 57.88  ? 323 LEU   A CG    1 
ATOM   2552 C CD1   . LEU   A 1 333 ? 26.973 -6.122  46.212 1.00 58.22  ? 323 LEU   A CD1   1 
ATOM   2553 C CD2   . LEU   A 1 333 ? 27.759 -8.399  46.911 1.00 56.09  ? 323 LEU   A CD2   1 
ATOM   2554 N N     . TYR   A 1 334 ? 29.552 -5.183  50.975 1.00 56.17  ? 324 TYR   A N     1 
ATOM   2555 C CA    . TYR   A 1 334 ? 30.603 -4.439  51.647 1.00 56.98  ? 324 TYR   A CA    1 
ATOM   2556 C C     . TYR   A 1 334 ? 31.254 -5.296  52.733 1.00 57.21  ? 324 TYR   A C     1 
ATOM   2557 O O     . TYR   A 1 334 ? 32.441 -5.138  53.002 1.00 59.25  ? 324 TYR   A O     1 
ATOM   2558 C CB    . TYR   A 1 334 ? 30.055 -3.130  52.216 1.00 55.56  ? 324 TYR   A CB    1 
ATOM   2559 C CG    . TYR   A 1 334 ? 29.785 -2.061  51.171 1.00 53.89  ? 324 TYR   A CG    1 
ATOM   2560 C CD1   . TYR   A 1 334 ? 30.825 -1.492  50.450 1.00 55.31  ? 324 TYR   A CD1   1 
ATOM   2561 C CD2   . TYR   A 1 334 ? 28.504 -1.579  50.951 1.00 53.53  ? 324 TYR   A CD2   1 
ATOM   2562 C CE1   . TYR   A 1 334 ? 30.592 -0.505  49.508 1.00 55.05  ? 324 TYR   A CE1   1 
ATOM   2563 C CE2   . TYR   A 1 334 ? 28.257 -0.590  50.018 1.00 53.76  ? 324 TYR   A CE2   1 
ATOM   2564 C CZ    . TYR   A 1 334 ? 29.304 -0.048  49.296 1.00 54.98  ? 324 TYR   A CZ    1 
ATOM   2565 O OH    . TYR   A 1 334 ? 29.062 0.943   48.387 1.00 57.28  ? 324 TYR   A OH    1 
ATOM   2566 N N     . GLU   A 1 335 ? 30.483 -6.195  53.359 1.00 56.96  ? 325 GLU   A N     1 
ATOM   2567 C CA    . GLU   A 1 335 ? 31.028 -7.083  54.375 1.00 57.32  ? 325 GLU   A CA    1 
ATOM   2568 C C     . GLU   A 1 335 ? 31.875 -8.178  53.723 1.00 57.07  ? 325 GLU   A C     1 
ATOM   2569 O O     . GLU   A 1 335 ? 32.922 -8.553  54.255 1.00 58.03  ? 325 GLU   A O     1 
ATOM   2570 C CB    . GLU   A 1 335 ? 29.922 -7.682  55.246 1.00 57.50  ? 325 GLU   A CB    1 
ATOM   2571 C CG    . GLU   A 1 335 ? 30.462 -8.573  56.365 1.00 57.26  ? 325 GLU   A CG    1 
ATOM   2572 C CD    . GLU   A 1 335 ? 29.401 -9.254  57.209 1.00 57.33  ? 325 GLU   A CD    1 
ATOM   2573 O OE1   . GLU   A 1 335 ? 28.535 -9.923  56.612 1.00 55.33  ? 325 GLU   A OE1   1 
ATOM   2574 O OE2   . GLU   A 1 335 ? 29.450 -9.134  58.452 1.00 58.86  ? 325 GLU   A OE2   1 
ATOM   2575 N N     . ILE   A 1 336 ? 31.402 -8.706  52.586 1.00 55.27  ? 326 ILE   A N     1 
ATOM   2576 C CA    . ILE   A 1 336 ? 32.152 -9.691  51.820 1.00 56.33  ? 326 ILE   A CA    1 
ATOM   2577 C C     . ILE   A 1 336 ? 33.537 -9.124  51.518 1.00 56.12  ? 326 ILE   A C     1 
ATOM   2578 O O     . ILE   A 1 336 ? 34.538 -9.812  51.705 1.00 57.78  ? 326 ILE   A O     1 
ATOM   2579 C CB    . ILE   A 1 336 ? 31.390 -10.092 50.539 1.00 56.80  ? 326 ILE   A CB    1 
ATOM   2580 C CG1   . ILE   A 1 336 ? 30.161 -10.945 50.860 1.00 57.27  ? 326 ILE   A CG1   1 
ATOM   2581 C CG2   . ILE   A 1 336 ? 32.306 -10.797 49.538 1.00 56.60  ? 326 ILE   A CG2   1 
ATOM   2582 C CD1   . ILE   A 1 336 ? 29.142 -11.008 49.737 1.00 58.49  ? 326 ILE   A CD1   1 
ATOM   2583 N N     . ASN   A 1 337 ? 33.577 -7.865  51.061 1.00 55.94  ? 327 ASN   A N     1 
ATOM   2584 C CA    . ASN   A 1 337 ? 34.822 -7.171  50.763 1.00 56.42  ? 327 ASN   A CA    1 
ATOM   2585 C C     . ASN   A 1 337 ? 35.757 -7.198  51.970 1.00 57.62  ? 327 ASN   A C     1 
ATOM   2586 O O     . ASN   A 1 337 ? 36.956 -7.429  51.825 1.00 61.67  ? 327 ASN   A O     1 
ATOM   2587 C CB    . ASN   A 1 337 ? 34.589 -5.713  50.380 1.00 57.07  ? 327 ASN   A CB    1 
ATOM   2588 C CG    . ASN   A 1 337 ? 33.834 -5.540  49.083 1.00 56.55  ? 327 ASN   A CG    1 
ATOM   2589 O OD1   . ASN   A 1 337 ? 33.603 -6.506  48.345 1.00 55.57  ? 327 ASN   A OD1   1 
ATOM   2590 N ND2   . ASN   A 1 337 ? 33.465 -4.306  48.776 1.00 55.93  ? 327 ASN   A ND2   1 
ATOM   2591 N N     . LEU   A 1 338 ? 35.200 -6.924  53.155 1.00 57.07  ? 328 LEU   A N     1 
ATOM   2592 C CA    . LEU   A 1 338 ? 35.983 -6.805  54.373 1.00 56.18  ? 328 LEU   A CA    1 
ATOM   2593 C C     . LEU   A 1 338 ? 36.529 -8.173  54.770 1.00 55.22  ? 328 LEU   A C     1 
ATOM   2594 O O     . LEU   A 1 338 ? 37.692 -8.290  55.149 1.00 55.20  ? 328 LEU   A O     1 
ATOM   2595 C CB    . LEU   A 1 338 ? 35.121 -6.199  55.479 1.00 56.46  ? 328 LEU   A CB    1 
ATOM   2596 C CG    . LEU   A 1 338 ? 35.817 -5.938  56.820 1.00 55.34  ? 328 LEU   A CG    1 
ATOM   2597 C CD1   . LEU   A 1 338 ? 36.838 -4.833  56.685 1.00 54.56  ? 328 LEU   A CD1   1 
ATOM   2598 C CD2   . LEU   A 1 338 ? 34.802 -5.611  57.902 1.00 55.28  ? 328 LEU   A CD2   1 
ATOM   2599 N N     . ARG   A 1 339 ? 35.673 -9.195  54.694 1.00 56.48  ? 329 ARG   A N     1 
ATOM   2600 C CA    . ARG   A 1 339 ? 36.041 -10.544 55.102 1.00 57.88  ? 329 ARG   A CA    1 
ATOM   2601 C C     . ARG   A 1 339 ? 37.141 -11.082 54.186 1.00 58.74  ? 329 ARG   A C     1 
ATOM   2602 O O     . ARG   A 1 339 ? 38.092 -11.703 54.647 1.00 58.71  ? 329 ARG   A O     1 
ATOM   2603 C CB    . ARG   A 1 339 ? 34.795 -11.435 55.082 1.00 56.82  ? 329 ARG   A CB    1 
ATOM   2604 C CG    . ARG   A 1 339 ? 34.979 -12.796 55.733 1.00 56.54  ? 329 ARG   A CG    1 
ATOM   2605 C CD    . ARG   A 1 339 ? 33.646 -13.520 55.815 1.00 57.22  ? 329 ARG   A CD    1 
ATOM   2606 N NE    . ARG   A 1 339 ? 33.730 -14.765 56.585 1.00 59.27  ? 329 ARG   A NE    1 
ATOM   2607 C CZ    . ARG   A 1 339 ? 34.333 -15.886 56.198 1.00 60.26  ? 329 ARG   A CZ    1 
ATOM   2608 N NH1   . ARG   A 1 339 ? 34.888 -15.967 55.000 1.00 60.80  ? 329 ARG   A NH1   1 
ATOM   2609 N NH2   . ARG   A 1 339 ? 34.376 -16.928 57.014 1.00 60.26  ? 329 ARG   A NH2   1 
ATOM   2610 N N     . ARG   A 1 340 ? 37.005 -10.822 52.883 1.00 60.65  ? 330 ARG   A N     1 
ATOM   2611 C CA    . ARG   A 1 340 ? 38.019 -11.194 51.909 1.00 62.39  ? 330 ARG   A CA    1 
ATOM   2612 C C     . ARG   A 1 340 ? 39.335 -10.485 52.241 1.00 60.26  ? 330 ARG   A C     1 
ATOM   2613 O O     . ARG   A 1 340 ? 40.394 -11.104 52.213 1.00 59.71  ? 330 ARG   A O     1 
ATOM   2614 C CB    . ARG   A 1 340 ? 37.480 -10.869 50.508 1.00 65.55  ? 330 ARG   A CB    1 
ATOM   2615 C CG    . ARG   A 1 340 ? 38.203 -11.511 49.330 1.00 68.48  ? 330 ARG   A CG    1 
ATOM   2616 C CD    . ARG   A 1 340 ? 37.768 -10.891 48.002 1.00 70.22  ? 330 ARG   A CD    1 
ATOM   2617 N NE    . ARG   A 1 340 ? 38.064 -9.454  48.039 1.00 72.47  ? 330 ARG   A NE    1 
ATOM   2618 C CZ    . ARG   A 1 340 ? 37.179 -8.465  47.932 1.00 74.48  ? 330 ARG   A CZ    1 
ATOM   2619 N NH1   . ARG   A 1 340 ? 35.982 -8.695  47.418 1.00 75.05  ? 330 ARG   A NH1   1 
ATOM   2620 N NH2   . ARG   A 1 340 ? 37.517 -7.237  48.299 1.00 73.81  ? 330 ARG   A NH2   1 
ATOM   2621 N N     . PHE   A 1 341 ? 39.255 -9.188  52.568 1.00 59.22  ? 331 PHE   A N     1 
ATOM   2622 C CA    . PHE   A 1 341 ? 40.421 -8.392  52.916 1.00 59.20  ? 331 PHE   A CA    1 
ATOM   2623 C C     . PHE   A 1 341 ? 41.035 -8.901  54.218 1.00 59.88  ? 331 PHE   A C     1 
ATOM   2624 O O     . PHE   A 1 341 ? 42.256 -8.964  54.340 1.00 62.37  ? 331 PHE   A O     1 
ATOM   2625 C CB    . PHE   A 1 341 ? 40.025 -6.912  52.992 1.00 60.03  ? 331 PHE   A CB    1 
ATOM   2626 C CG    . PHE   A 1 341 ? 41.021 -5.988  53.686 1.00 59.42  ? 331 PHE   A CG    1 
ATOM   2627 C CD1   . PHE   A 1 341 ? 41.027 -5.863  55.074 1.00 59.49  ? 331 PHE   A CD1   1 
ATOM   2628 C CD2   . PHE   A 1 341 ? 41.923 -5.222  52.954 1.00 59.56  ? 331 PHE   A CD2   1 
ATOM   2629 C CE1   . PHE   A 1 341 ? 41.923 -5.012  55.708 1.00 59.71  ? 331 PHE   A CE1   1 
ATOM   2630 C CE2   . PHE   A 1 341 ? 42.819 -4.372  53.594 1.00 59.22  ? 331 PHE   A CE2   1 
ATOM   2631 C CZ    . PHE   A 1 341 ? 42.817 -4.270  54.968 1.00 59.65  ? 331 PHE   A CZ    1 
ATOM   2632 N N     . LEU   A 1 342 ? 40.190 -9.252  55.193 1.00 60.50  ? 332 LEU   A N     1 
ATOM   2633 C CA    . LEU   A 1 342 ? 40.675 -9.743  56.475 1.00 61.82  ? 332 LEU   A CA    1 
ATOM   2634 C C     . LEU   A 1 342 ? 41.296 -11.133 56.324 1.00 61.53  ? 332 LEU   A C     1 
ATOM   2635 O O     . LEU   A 1 342 ? 42.267 -11.442 57.009 1.00 63.11  ? 332 LEU   A O     1 
ATOM   2636 C CB    . LEU   A 1 342 ? 39.567 -9.736  57.528 1.00 62.65  ? 332 LEU   A CB    1 
ATOM   2637 C CG    . LEU   A 1 342 ? 39.536 -8.519  58.458 1.00 64.15  ? 332 LEU   A CG    1 
ATOM   2638 C CD1   . LEU   A 1 342 ? 38.215 -8.404  59.195 1.00 64.20  ? 332 LEU   A CD1   1 
ATOM   2639 C CD2   . LEU   A 1 342 ? 40.686 -8.599  59.447 1.00 64.19  ? 332 LEU   A CD2   1 
ATOM   2640 N N     . SER   A 1 343 ? 40.742 -11.967 55.436 1.00 60.07  ? 333 SER   A N     1 
ATOM   2641 C CA    . SER   A 1 343 ? 41.251 -13.318 55.263 1.00 61.25  ? 333 SER   A CA    1 
ATOM   2642 C C     . SER   A 1 343 ? 42.662 -13.268 54.685 1.00 62.63  ? 333 SER   A C     1 
ATOM   2643 O O     . SER   A 1 343 ? 43.532 -14.017 55.120 1.00 63.51  ? 333 SER   A O     1 
ATOM   2644 C CB    . SER   A 1 343 ? 40.327 -14.175 54.424 1.00 62.32  ? 333 SER   A CB    1 
ATOM   2645 O OG    . SER   A 1 343 ? 40.250 -13.723 53.081 1.00 64.60  ? 333 SER   A OG    1 
ATOM   2646 N N     . ARG   A 1 344 ? 42.883 -12.355 53.733 1.00 64.03  ? 334 ARG   A N     1 
ATOM   2647 C CA    . ARG   A 1 344 ? 44.189 -12.176 53.117 1.00 65.65  ? 334 ARG   A CA    1 
ATOM   2648 C C     . ARG   A 1 344 ? 45.238 -11.760 54.151 1.00 61.55  ? 334 ARG   A C     1 
ATOM   2649 O O     . ARG   A 1 344 ? 46.388 -12.175 54.042 1.00 62.01  ? 334 ARG   A O     1 
ATOM   2650 C CB    . ARG   A 1 344 ? 44.140 -11.153 51.973 1.00 69.49  ? 334 ARG   A CB    1 
ATOM   2651 C CG    . ARG   A 1 344 ? 43.570 -11.647 50.646 1.00 74.01  ? 334 ARG   A CG    1 
ATOM   2652 C CD    . ARG   A 1 344 ? 43.645 -10.590 49.533 1.00 77.61  ? 334 ARG   A CD    1 
ATOM   2653 N NE    . ARG   A 1 344 ? 45.000 -10.056 49.317 1.00 79.36  ? 334 ARG   A NE    1 
ATOM   2654 C CZ    . ARG   A 1 344 ? 45.305 -8.942  48.650 1.00 78.29  ? 334 ARG   A CZ    1 
ATOM   2655 N NH1   . ARG   A 1 344 ? 44.354 -8.195  48.120 1.00 79.54  ? 334 ARG   A NH1   1 
ATOM   2656 N NH2   . ARG   A 1 344 ? 46.564 -8.566  48.518 1.00 77.53  ? 334 ARG   A NH2   1 
ATOM   2657 N N     . LEU   A 1 345 ? 44.845 -10.955 55.148 1.00 57.36  ? 335 LEU   A N     1 
ATOM   2658 C CA    . LEU   A 1 345 ? 45.803 -10.319 56.040 1.00 55.04  ? 335 LEU   A CA    1 
ATOM   2659 C C     . LEU   A 1 345 ? 45.641 -10.797 57.482 1.00 53.01  ? 335 LEU   A C     1 
ATOM   2660 O O     . LEU   A 1 345 ? 46.006 -10.077 58.405 1.00 52.75  ? 335 LEU   A O     1 
ATOM   2661 C CB    . LEU   A 1 345 ? 45.606 -8.808  55.943 1.00 56.00  ? 335 LEU   A CB    1 
ATOM   2662 C CG    . LEU   A 1 345 ? 45.753 -8.188  54.549 1.00 56.18  ? 335 LEU   A CG    1 
ATOM   2663 C CD1   . LEU   A 1 345 ? 45.392 -6.718  54.579 1.00 56.21  ? 335 LEU   A CD1   1 
ATOM   2664 C CD2   . LEU   A 1 345 ? 47.161 -8.365  54.020 1.00 57.53  ? 335 LEU   A CD2   1 
ATOM   2665 N N     . GLN   A 1 346 ? 45.150 -12.027 57.672 1.00 51.85  ? 336 GLN   A N     1 
ATOM   2666 C CA    . GLN   A 1 346 ? 44.848 -12.541 58.999 1.00 53.08  ? 336 GLN   A CA    1 
ATOM   2667 C C     . GLN   A 1 346 ? 46.107 -12.603 59.869 1.00 54.16  ? 336 GLN   A C     1 
ATOM   2668 O O     . GLN   A 1 346 ? 46.015 -12.519 61.096 1.00 53.58  ? 336 GLN   A O     1 
ATOM   2669 C CB    . GLN   A 1 346 ? 44.173 -13.909 58.889 1.00 54.68  ? 336 GLN   A CB    1 
ATOM   2670 C CG    . GLN   A 1 346 ? 43.794 -14.545 60.226 1.00 56.22  ? 336 GLN   A CG    1 
ATOM   2671 C CD    . GLN   A 1 346 ? 42.867 -13.695 61.071 1.00 57.16  ? 336 GLN   A CD    1 
ATOM   2672 O OE1   . GLN   A 1 346 ? 41.821 -13.224 60.607 1.00 57.50  ? 336 GLN   A OE1   1 
ATOM   2673 N NE2   . GLN   A 1 346 ? 43.240 -13.493 62.327 1.00 57.54  ? 336 GLN   A NE2   1 
ATOM   2674 N N     . TYR   A 1 347 ? 47.281 -12.763 59.244 1.00 54.05  ? 337 TYR   A N     1 
ATOM   2675 C CA    . TYR   A 1 347 ? 48.529 -12.792 59.991 1.00 54.08  ? 337 TYR   A CA    1 
ATOM   2676 C C     . TYR   A 1 347 ? 48.673 -11.495 60.787 1.00 54.19  ? 337 TYR   A C     1 
ATOM   2677 O O     . TYR   A 1 347 ? 49.015 -11.525 61.965 1.00 52.65  ? 337 TYR   A O     1 
ATOM   2678 C CB    . TYR   A 1 347 ? 49.735 -13.033 59.076 1.00 52.97  ? 337 TYR   A CB    1 
ATOM   2679 C CG    . TYR   A 1 347 ? 51.083 -12.831 59.758 1.00 52.18  ? 337 TYR   A CG    1 
ATOM   2680 C CD1   . TYR   A 1 347 ? 51.498 -13.678 60.777 1.00 51.63  ? 337 TYR   A CD1   1 
ATOM   2681 C CD2   . TYR   A 1 347 ? 51.939 -11.795 59.393 1.00 51.97  ? 337 TYR   A CD2   1 
ATOM   2682 C CE1   . TYR   A 1 347 ? 52.712 -13.497 61.419 1.00 51.78  ? 337 TYR   A CE1   1 
ATOM   2683 C CE2   . TYR   A 1 347 ? 53.164 -11.613 60.019 1.00 52.74  ? 337 TYR   A CE2   1 
ATOM   2684 C CZ    . TYR   A 1 347 ? 53.554 -12.471 61.034 1.00 52.76  ? 337 TYR   A CZ    1 
ATOM   2685 O OH    . TYR   A 1 347 ? 54.758 -12.333 61.671 1.00 54.32  ? 337 TYR   A OH    1 
ATOM   2686 N N     . TYR   A 1 348 ? 48.394 -10.358 60.141 1.00 56.22  ? 338 TYR   A N     1 
ATOM   2687 C CA    . TYR   A 1 348 ? 48.630 -9.057  60.750 1.00 56.32  ? 338 TYR   A CA    1 
ATOM   2688 C C     . TYR   A 1 348 ? 47.572 -8.760  61.812 1.00 56.66  ? 338 TYR   A C     1 
ATOM   2689 O O     . TYR   A 1 348 ? 47.797 -7.931  62.688 1.00 57.48  ? 338 TYR   A O     1 
ATOM   2690 C CB    . TYR   A 1 348 ? 48.752 -8.029  59.622 1.00 56.01  ? 338 TYR   A CB    1 
ATOM   2691 C CG    . TYR   A 1 348 ? 50.010 -8.272  58.798 1.00 56.61  ? 338 TYR   A CG    1 
ATOM   2692 C CD1   . TYR   A 1 348 ? 51.267 -8.049  59.353 1.00 57.04  ? 338 TYR   A CD1   1 
ATOM   2693 C CD2   . TYR   A 1 348 ? 49.951 -8.748  57.492 1.00 56.21  ? 338 TYR   A CD2   1 
ATOM   2694 C CE1   . TYR   A 1 348 ? 52.427 -8.288  58.638 1.00 57.04  ? 338 TYR   A CE1   1 
ATOM   2695 C CE2   . TYR   A 1 348 ? 51.106 -8.984  56.763 1.00 56.80  ? 338 TYR   A CE2   1 
ATOM   2696 C CZ    . TYR   A 1 348 ? 52.346 -8.754  57.338 1.00 57.39  ? 338 TYR   A CZ    1 
ATOM   2697 O OH    . TYR   A 1 348 ? 53.504 -8.974  56.652 1.00 58.17  ? 338 TYR   A OH    1 
ATOM   2698 N N     . VAL   A 1 349 ? 46.426 -9.443  61.746 1.00 56.87  ? 339 VAL   A N     1 
ATOM   2699 C CA    . VAL   A 1 349 ? 45.443 -9.372  62.815 1.00 56.82  ? 339 VAL   A CA    1 
ATOM   2700 C C     . VAL   A 1 349 ? 45.998 -10.127 64.022 1.00 57.55  ? 339 VAL   A C     1 
ATOM   2701 O O     . VAL   A 1 349 ? 45.822 -9.692  65.157 1.00 59.17  ? 339 VAL   A O     1 
ATOM   2702 C CB    . VAL   A 1 349 ? 44.068 -9.918  62.380 1.00 55.97  ? 339 VAL   A CB    1 
ATOM   2703 C CG1   . VAL   A 1 349 ? 43.060 -9.928  63.523 1.00 56.08  ? 339 VAL   A CG1   1 
ATOM   2704 C CG2   . VAL   A 1 349 ? 43.505 -9.155  61.189 1.00 54.23  ? 339 VAL   A CG2   1 
ATOM   2705 N N     . ASN   A 1 350 ? 46.689 -11.243 63.755 1.00 57.17  ? 340 ASN   A N     1 
ATOM   2706 C CA    . ASN   A 1 350 ? 47.288 -12.064 64.797 1.00 56.26  ? 340 ASN   A CA    1 
ATOM   2707 C C     . ASN   A 1 350 ? 48.399 -11.308 65.528 1.00 56.25  ? 340 ASN   A C     1 
ATOM   2708 O O     . ASN   A 1 350 ? 48.545 -11.468 66.735 1.00 56.92  ? 340 ASN   A O     1 
ATOM   2709 C CB    . ASN   A 1 350 ? 47.838 -13.381 64.249 1.00 56.19  ? 340 ASN   A CB    1 
ATOM   2710 C CG    . ASN   A 1 350 ? 46.770 -14.291 63.690 1.00 56.99  ? 340 ASN   A CG    1 
ATOM   2711 O OD1   . ASN   A 1 350 ? 45.570 -14.023 63.831 1.00 59.83  ? 340 ASN   A OD1   1 
ATOM   2712 N ND2   . ASN   A 1 350 ? 47.182 -15.379 63.058 1.00 56.92  ? 340 ASN   A ND2   1 
ATOM   2713 N N     . THR   A 1 351 ? 49.194 -10.512 64.798 1.00 57.72  ? 341 THR   A N     1 
ATOM   2714 C CA    . THR   A 1 351 ? 50.335 -9.814  65.381 1.00 59.07  ? 341 THR   A CA    1 
ATOM   2715 C C     . THR   A 1 351 ? 49.911 -8.486  66.011 1.00 60.77  ? 341 THR   A C     1 
ATOM   2716 O O     . THR   A 1 351 ? 50.763 -7.766  66.529 1.00 58.93  ? 341 THR   A O     1 
ATOM   2717 C CB    . THR   A 1 351 ? 51.412 -9.572  64.322 1.00 59.95  ? 341 THR   A CB    1 
ATOM   2718 O OG1   . THR   A 1 351 ? 50.832 -8.718  63.338 1.00 60.22  ? 341 THR   A OG1   1 
ATOM   2719 C CG2   . THR   A 1 351 ? 51.925 -10.859 63.701 1.00 60.04  ? 341 THR   A CG2   1 
ATOM   2720 N N     . ASP   A 1 352 ? 48.609 -8.156  65.923 1.00 62.54  ? 342 ASP   A N     1 
ATOM   2721 C CA    . ASP   A 1 352 ? 48.030 -6.965  66.533 1.00 62.67  ? 342 ASP   A CA    1 
ATOM   2722 C C     . ASP   A 1 352 ? 48.416 -5.699  65.766 1.00 61.76  ? 342 ASP   A C     1 
ATOM   2723 O O     . ASP   A 1 352 ? 48.206 -4.600  66.271 1.00 62.29  ? 342 ASP   A O     1 
ATOM   2724 C CB    . ASP   A 1 352 ? 48.338 -6.867  68.023 1.00 62.79  ? 342 ASP   A CB    1 
ATOM   2725 C CG    . ASP   A 1 352 ? 47.635 -7.902  68.887 1.00 62.66  ? 342 ASP   A CG    1 
ATOM   2726 O OD1   . ASP   A 1 352 ? 46.393 -7.890  68.897 1.00 65.19  ? 342 ASP   A OD1   1 
ATOM   2727 O OD2   . ASP   A 1 352 ? 48.330 -8.715  69.524 1.00 61.52  ? 342 ASP   A OD2   1 
ATOM   2728 N N     . GLN   A 1 353 ? 48.933 -5.846  64.539 1.00 61.23  ? 343 GLN   A N     1 
ATOM   2729 C CA    . GLN   A 1 353 ? 49.261 -4.698  63.708 1.00 60.56  ? 343 GLN   A CA    1 
ATOM   2730 C C     . GLN   A 1 353 ? 48.028 -4.224  62.947 1.00 60.49  ? 343 GLN   A C     1 
ATOM   2731 O O     . GLN   A 1 353 ? 47.852 -3.027  62.752 1.00 59.68  ? 343 GLN   A O     1 
ATOM   2732 C CB    . GLN   A 1 353 ? 50.308 -5.018  62.650 1.00 60.56  ? 343 GLN   A CB    1 
ATOM   2733 C CG    . GLN   A 1 353 ? 51.695 -5.312  63.200 1.00 60.43  ? 343 GLN   A CG    1 
ATOM   2734 C CD    . GLN   A 1 353 ? 52.617 -5.784  62.099 1.00 61.04  ? 343 GLN   A CD    1 
ATOM   2735 O OE1   . GLN   A 1 353 ? 53.010 -5.006  61.224 1.00 59.23  ? 343 GLN   A OE1   1 
ATOM   2736 N NE2   . GLN   A 1 353 ? 52.930 -7.073  62.105 1.00 61.12  ? 343 GLN   A NE2   1 
ATOM   2737 N N     . LEU   A 1 354 ? 47.205 -5.173  62.481 1.00 61.10  ? 344 LEU   A N     1 
ATOM   2738 C CA    . LEU   A 1 354 ? 45.988 -4.841  61.758 1.00 59.92  ? 344 LEU   A CA    1 
ATOM   2739 C C     . LEU   A 1 354 ? 44.807 -4.941  62.718 1.00 58.51  ? 344 LEU   A C     1 
ATOM   2740 O O     . LEU   A 1 354 ? 44.497 -6.018  63.220 1.00 58.00  ? 344 LEU   A O     1 
ATOM   2741 C CB    . LEU   A 1 354 ? 45.802 -5.749  60.544 1.00 60.36  ? 344 LEU   A CB    1 
ATOM   2742 C CG    . LEU   A 1 354 ? 44.531 -5.517  59.719 1.00 59.63  ? 344 LEU   A CG    1 
ATOM   2743 C CD1   . LEU   A 1 354 ? 44.460 -4.102  59.173 1.00 59.12  ? 344 LEU   A CD1   1 
ATOM   2744 C CD2   . LEU   A 1 354 ? 44.459 -6.525  58.590 1.00 59.30  ? 344 LEU   A CD2   1 
ATOM   2745 N N     . VAL   A 1 355 ? 44.162 -3.794  62.958 1.00 58.09  ? 345 VAL   A N     1 
ATOM   2746 C CA    . VAL   A 1 355 ? 43.031 -3.701  63.865 1.00 55.69  ? 345 VAL   A CA    1 
ATOM   2747 C C     . VAL   A 1 355 ? 41.828 -3.214  63.066 1.00 53.09  ? 345 VAL   A C     1 
ATOM   2748 O O     . VAL   A 1 355 ? 41.766 -2.050  62.687 1.00 53.88  ? 345 VAL   A O     1 
ATOM   2749 C CB    . VAL   A 1 355 ? 43.351 -2.766  65.048 1.00 56.05  ? 345 VAL   A CB    1 
ATOM   2750 C CG1   . VAL   A 1 355 ? 42.167 -2.614  65.994 1.00 55.60  ? 345 VAL   A CG1   1 
ATOM   2751 C CG2   . VAL   A 1 355 ? 44.586 -3.225  65.815 1.00 55.92  ? 345 VAL   A CG2   1 
ATOM   2752 N N     . VAL   A 1 356 ? 40.899 -4.132  62.795 1.00 52.38  ? 346 VAL   A N     1 
ATOM   2753 C CA    . VAL   A 1 356 ? 39.656 -3.816  62.118 1.00 53.13  ? 346 VAL   A CA    1 
ATOM   2754 C C     . VAL   A 1 356 ? 38.545 -3.755  63.163 1.00 53.68  ? 346 VAL   A C     1 
ATOM   2755 O O     . VAL   A 1 356 ? 38.299 -4.736  63.856 1.00 54.74  ? 346 VAL   A O     1 
ATOM   2756 C CB    . VAL   A 1 356 ? 39.362 -4.860  61.024 1.00 54.18  ? 346 VAL   A CB    1 
ATOM   2757 C CG1   . VAL   A 1 356 ? 37.974 -4.692  60.416 1.00 55.29  ? 346 VAL   A CG1   1 
ATOM   2758 C CG2   . VAL   A 1 356 ? 40.422 -4.832  59.930 1.00 54.85  ? 346 VAL   A CG2   1 
ATOM   2759 N N     . ARG   A 1 357 ? 37.886 -2.593  63.258 1.00 53.85  ? 347 ARG   A N     1 
ATOM   2760 C CA    . ARG   A 1 357 ? 36.839 -2.344  64.233 1.00 53.61  ? 347 ARG   A CA    1 
ATOM   2761 C C     . ARG   A 1 357 ? 35.494 -2.251  63.522 1.00 53.93  ? 347 ARG   A C     1 
ATOM   2762 O O     . ARG   A 1 357 ? 35.340 -1.442  62.612 1.00 53.40  ? 347 ARG   A O     1 
ATOM   2763 C CB    . ARG   A 1 357 ? 37.093 -1.012  64.948 1.00 54.64  ? 347 ARG   A CB    1 
ATOM   2764 C CG    . ARG   A 1 357 ? 38.436 -0.935  65.656 1.00 54.72  ? 347 ARG   A CG    1 
ATOM   2765 C CD    . ARG   A 1 357 ? 38.590 0.329   66.463 1.00 54.81  ? 347 ARG   A CD    1 
ATOM   2766 N NE    . ARG   A 1 357 ? 39.881 0.312   67.158 1.00 55.29  ? 347 ARG   A NE    1 
ATOM   2767 C CZ    . ARG   A 1 357 ? 40.053 0.000   68.438 1.00 55.92  ? 347 ARG   A CZ    1 
ATOM   2768 N NH1   . ARG   A 1 357 ? 39.015 -0.321  69.189 1.00 55.73  ? 347 ARG   A NH1   1 
ATOM   2769 N NH2   . ARG   A 1 357 ? 41.268 -0.010  68.961 1.00 55.95  ? 347 ARG   A NH2   1 
ATOM   2770 N N     . LEU   A 1 358 ? 34.542 -3.092  63.948 1.00 55.07  ? 348 LEU   A N     1 
ATOM   2771 C CA    . LEU   A 1 358 ? 33.158 -3.006  63.512 1.00 56.01  ? 348 LEU   A CA    1 
ATOM   2772 C C     . LEU   A 1 358 ? 32.425 -2.052  64.443 1.00 54.19  ? 348 LEU   A C     1 
ATOM   2773 O O     . LEU   A 1 358 ? 32.385 -2.295  65.642 1.00 55.80  ? 348 LEU   A O     1 
ATOM   2774 C CB    . LEU   A 1 358 ? 32.460 -4.368  63.512 1.00 58.60  ? 348 LEU   A CB    1 
ATOM   2775 C CG    . LEU   A 1 358 ? 32.461 -5.153  62.196 1.00 61.08  ? 348 LEU   A CG    1 
ATOM   2776 C CD1   . LEU   A 1 358 ? 32.019 -4.323  61.007 1.00 61.66  ? 348 LEU   A CD1   1 
ATOM   2777 C CD2   . LEU   A 1 358 ? 33.830 -5.737  61.942 1.00 64.51  ? 348 LEU   A CD2   1 
ATOM   2778 N N     . TRP   A 1 359 ? 31.832 -0.999  63.871 1.00 53.27  ? 349 TRP   A N     1 
ATOM   2779 C CA    . TRP   A 1 359 ? 31.026 -0.050  64.619 1.00 53.64  ? 349 TRP   A CA    1 
ATOM   2780 C C     . TRP   A 1 359 ? 29.565 -0.478  64.584 1.00 54.46  ? 349 TRP   A C     1 
ATOM   2781 O O     . TRP   A 1 359 ? 29.037 -0.783  63.515 1.00 52.89  ? 349 TRP   A O     1 
ATOM   2782 C CB    . TRP   A 1 359 ? 31.169 1.362   64.037 1.00 52.89  ? 349 TRP   A CB    1 
ATOM   2783 C CG    . TRP   A 1 359 ? 30.441 2.421   64.824 1.00 52.65  ? 349 TRP   A CG    1 
ATOM   2784 C CD1   . TRP   A 1 359 ? 30.968 3.221   65.794 1.00 53.06  ? 349 TRP   A CD1   1 
ATOM   2785 C CD2   . TRP   A 1 359 ? 29.054 2.806   64.701 1.00 52.42  ? 349 TRP   A CD2   1 
ATOM   2786 N NE1   . TRP   A 1 359 ? 30.015 4.072   66.284 1.00 52.67  ? 349 TRP   A NE1   1 
ATOM   2787 C CE2   . TRP   A 1 359 ? 28.833 3.842   65.635 1.00 52.15  ? 349 TRP   A CE2   1 
ATOM   2788 C CE3   . TRP   A 1 359 ? 27.987 2.384   63.901 1.00 52.53  ? 349 TRP   A CE3   1 
ATOM   2789 C CZ2   . TRP   A 1 359 ? 27.593 4.456   65.785 1.00 52.32  ? 349 TRP   A CZ2   1 
ATOM   2790 C CZ3   . TRP   A 1 359 ? 26.760 2.992   64.051 1.00 53.10  ? 349 TRP   A CZ3   1 
ATOM   2791 C CH2   . TRP   A 1 359 ? 26.569 4.016   64.979 1.00 53.27  ? 349 TRP   A CH2   1 
ATOM   2792 N N     . LYS   A 1 360 ? 28.916 -0.454  65.757 1.00 55.76  ? 350 LYS   A N     1 
ATOM   2793 C CA    . LYS   A 1 360 ? 27.502 -0.774  65.864 1.00 56.15  ? 350 LYS   A CA    1 
ATOM   2794 C C     . LYS   A 1 360 ? 26.942 -0.186  67.153 1.00 56.23  ? 350 LYS   A C     1 
ATOM   2795 O O     . LYS   A 1 360 ? 27.551 -0.312  68.213 1.00 53.93  ? 350 LYS   A O     1 
ATOM   2796 C CB    . LYS   A 1 360 ? 27.251 -2.285  65.833 1.00 56.48  ? 350 LYS   A CB    1 
ATOM   2797 C CG    . LYS   A 1 360 ? 25.780 -2.673  65.831 1.00 57.95  ? 350 LYS   A CG    1 
ATOM   2798 C CD    . LYS   A 1 360 ? 25.540 -4.178  65.785 1.00 59.85  ? 350 LYS   A CD    1 
ATOM   2799 C CE    . LYS   A 1 360 ? 24.144 -4.545  66.199 1.00 61.52  ? 350 LYS   A CE    1 
ATOM   2800 N NZ    . LYS   A 1 360 ? 23.139 -3.766  65.471 1.00 62.74  ? 350 LYS   A NZ    1 
ATOM   2801 N N     . ASP   A 1 361 ? 25.763 0.435   67.029 1.00 58.17  ? 351 ASP   A N     1 
ATOM   2802 C CA    . ASP   A 1 361 ? 25.058 1.048   68.142 1.00 59.52  ? 351 ASP   A CA    1 
ATOM   2803 C C     . ASP   A 1 361 ? 23.561 0.929   67.872 1.00 60.46  ? 351 ASP   A C     1 
ATOM   2804 O O     . ASP   A 1 361 ? 22.938 1.860   67.363 1.00 61.64  ? 351 ASP   A O     1 
ATOM   2805 C CB    . ASP   A 1 361 ? 25.510 2.485   68.346 1.00 59.74  ? 351 ASP   A CB    1 
ATOM   2806 C CG    . ASP   A 1 361 ? 24.763 3.277   69.409 1.00 59.29  ? 351 ASP   A CG    1 
ATOM   2807 O OD1   . ASP   A 1 361 ? 24.024 2.656   70.199 1.00 59.69  ? 351 ASP   A OD1   1 
ATOM   2808 O OD2   . ASP   A 1 361 ? 24.918 4.512   69.427 1.00 58.28  ? 351 ASP   A OD2   1 
ATOM   2809 N N     . ASP   A 1 362 ? 23.005 -0.237  68.216 1.00 62.34  ? 352 ASP   A N     1 
ATOM   2810 C CA    . ASP   A 1 362 ? 21.630 -0.582  67.892 1.00 64.78  ? 352 ASP   A CA    1 
ATOM   2811 C C     . ASP   A 1 362 ? 21.443 -0.371  66.391 1.00 62.76  ? 352 ASP   A C     1 
ATOM   2812 O O     . ASP   A 1 362 ? 22.220 -0.906  65.606 1.00 60.82  ? 352 ASP   A O     1 
ATOM   2813 C CB    . ASP   A 1 362 ? 20.647 0.118   68.822 1.00 68.02  ? 352 ASP   A CB    1 
ATOM   2814 C CG    . ASP   A 1 362 ? 20.851 -0.158  70.308 1.00 73.38  ? 352 ASP   A CG    1 
ATOM   2815 O OD1   . ASP   A 1 362 ? 20.829 -1.347  70.695 1.00 74.83  ? 352 ASP   A OD1   1 
ATOM   2816 O OD2   . ASP   A 1 362 ? 21.040 0.819   71.073 1.00 76.53  ? 352 ASP   A OD2   1 
ATOM   2817 N N     . ASP   A 1 363 ? 20.444 0.429   66.003 1.00 63.41  ? 353 ASP   A N     1 
ATOM   2818 C CA    . ASP   A 1 363 ? 20.083 0.581   64.602 1.00 65.48  ? 353 ASP   A CA    1 
ATOM   2819 C C     . ASP   A 1 363 ? 20.520 1.952   64.083 1.00 63.55  ? 353 ASP   A C     1 
ATOM   2820 O O     . ASP   A 1 363 ? 20.125 2.354   62.990 1.00 62.97  ? 353 ASP   A O     1 
ATOM   2821 C CB    . ASP   A 1 363 ? 18.601 0.305   64.390 1.00 66.69  ? 353 ASP   A CB    1 
ATOM   2822 C CG    . ASP   A 1 363 ? 17.649 1.152   65.222 1.00 69.97  ? 353 ASP   A CG    1 
ATOM   2823 O OD1   . ASP   A 1 363 ? 18.135 1.883   66.113 1.00 72.08  ? 353 ASP   A OD1   1 
ATOM   2824 O OD2   . ASP   A 1 363 ? 16.427 1.078   64.969 1.00 74.34  ? 353 ASP   A OD2   1 
ATOM   2825 N N     . ASN   A 1 364 ? 21.346 2.664   64.860 1.00 60.90  ? 354 ASN   A N     1 
ATOM   2826 C CA    . ASN   A 1 364 ? 21.986 3.875   64.369 1.00 60.32  ? 354 ASN   A CA    1 
ATOM   2827 C C     . ASN   A 1 364 ? 22.925 3.490   63.226 1.00 58.03  ? 354 ASN   A C     1 
ATOM   2828 O O     . ASN   A 1 364 ? 23.335 2.333   63.140 1.00 57.87  ? 354 ASN   A O     1 
ATOM   2829 C CB    . ASN   A 1 364 ? 22.682 4.626   65.497 1.00 60.14  ? 354 ASN   A CB    1 
ATOM   2830 C CG    . ASN   A 1 364 ? 21.737 4.936   66.632 1.00 59.96  ? 354 ASN   A CG    1 
ATOM   2831 O OD1   . ASN   A 1 364 ? 21.942 4.474   67.758 1.00 60.42  ? 354 ASN   A OD1   1 
ATOM   2832 N ND2   . ASN   A 1 364 ? 20.691 5.699   66.360 1.00 59.06  ? 354 ASN   A ND2   1 
ATOM   2833 N N     . THR   A 1 365 ? 23.251 4.448   62.346 1.00 54.85  ? 355 THR   A N     1 
ATOM   2834 C CA    . THR   A 1 365 ? 24.026 4.130   61.155 1.00 53.95  ? 355 THR   A CA    1 
ATOM   2835 C C     . THR   A 1 365 ? 25.380 4.836   61.178 1.00 52.78  ? 355 THR   A C     1 
ATOM   2836 O O     . THR   A 1 365 ? 25.595 5.784   61.931 1.00 52.26  ? 355 THR   A O     1 
ATOM   2837 C CB    . THR   A 1 365 ? 23.225 4.445   59.892 1.00 54.56  ? 355 THR   A CB    1 
ATOM   2838 O OG1   . THR   A 1 365 ? 22.889 5.830   59.864 1.00 53.97  ? 355 THR   A OG1   1 
ATOM   2839 C CG2   . THR   A 1 365 ? 21.956 3.617   59.800 1.00 54.74  ? 355 THR   A CG2   1 
ATOM   2840 N N     . TYR   A 1 366 ? 26.289 4.333   60.333 1.00 53.09  ? 356 TYR   A N     1 
ATOM   2841 C CA    . TYR   A 1 366 ? 27.694 4.712   60.339 1.00 52.36  ? 356 TYR   A CA    1 
ATOM   2842 C C     . TYR   A 1 366 ? 28.066 5.411   59.035 1.00 52.44  ? 356 TYR   A C     1 
ATOM   2843 O O     . TYR   A 1 366 ? 27.829 4.860   57.962 1.00 52.57  ? 356 TYR   A O     1 
ATOM   2844 C CB    . TYR   A 1 366 ? 28.516 3.431   60.491 1.00 50.65  ? 356 TYR   A CB    1 
ATOM   2845 C CG    . TYR   A 1 366 ? 30.018 3.651   60.576 1.00 49.27  ? 356 TYR   A CG    1 
ATOM   2846 C CD1   . TYR   A 1 366 ? 30.610 4.062   61.762 1.00 48.38  ? 356 TYR   A CD1   1 
ATOM   2847 C CD2   . TYR   A 1 366 ? 30.844 3.435   59.480 1.00 48.61  ? 356 TYR   A CD2   1 
ATOM   2848 C CE1   . TYR   A 1 366 ? 31.978 4.248   61.857 1.00 48.55  ? 356 TYR   A CE1   1 
ATOM   2849 C CE2   . TYR   A 1 366 ? 32.215 3.618   59.561 1.00 47.21  ? 356 TYR   A CE2   1 
ATOM   2850 C CZ    . TYR   A 1 366 ? 32.783 4.025   60.754 1.00 48.66  ? 356 TYR   A CZ    1 
ATOM   2851 O OH    . TYR   A 1 366 ? 34.131 4.227   60.853 1.00 50.37  ? 356 TYR   A OH    1 
ATOM   2852 N N     . ALA   A 1 367 ? 28.687 6.595   59.141 1.00 51.65  ? 357 ALA   A N     1 
ATOM   2853 C CA    . ALA   A 1 367 ? 29.076 7.365   57.968 1.00 51.58  ? 357 ALA   A CA    1 
ATOM   2854 C C     . ALA   A 1 367 ? 30.447 8.016   58.143 1.00 51.25  ? 357 ALA   A C     1 
ATOM   2855 O O     . ALA   A 1 367 ? 30.732 8.999   57.473 1.00 51.63  ? 357 ALA   A O     1 
ATOM   2856 C CB    . ALA   A 1 367 ? 28.024 8.418   57.677 1.00 51.48  ? 357 ALA   A CB    1 
ATOM   2857 N N     . LEU   A 1 368 ? 31.308 7.476   59.014 1.00 51.65  ? 358 LEU   A N     1 
ATOM   2858 C CA    . LEU   A 1 368 ? 32.562 8.150   59.325 1.00 52.47  ? 358 LEU   A CA    1 
ATOM   2859 C C     . LEU   A 1 368 ? 33.523 8.050   58.141 1.00 51.44  ? 358 LEU   A C     1 
ATOM   2860 O O     . LEU   A 1 368 ? 33.687 6.982   57.552 1.00 50.03  ? 358 LEU   A O     1 
ATOM   2861 C CB    . LEU   A 1 368 ? 33.236 7.590   60.576 1.00 54.44  ? 358 LEU   A CB    1 
ATOM   2862 C CG    . LEU   A 1 368 ? 32.411 7.562   61.866 1.00 56.31  ? 358 LEU   A CG    1 
ATOM   2863 C CD1   . LEU   A 1 368 ? 33.296 7.055   62.996 1.00 56.17  ? 358 LEU   A CD1   1 
ATOM   2864 C CD2   . LEU   A 1 368 ? 31.808 8.913   62.214 1.00 56.77  ? 358 LEU   A CD2   1 
ATOM   2865 N N     . LYS   A 1 369 ? 34.182 9.171   57.829 1.00 50.37  ? 359 LYS   A N     1 
ATOM   2866 C CA    . LYS   A 1 369 ? 35.308 9.167   56.912 1.00 50.64  ? 359 LYS   A CA    1 
ATOM   2867 C C     . LYS   A 1 369 ? 36.530 9.747   57.613 1.00 48.74  ? 359 LYS   A C     1 
ATOM   2868 O O     . LYS   A 1 369 ? 36.418 10.383  58.656 1.00 48.46  ? 359 LYS   A O     1 
ATOM   2869 C CB    . LYS   A 1 369 ? 35.049 9.993   55.649 1.00 52.29  ? 359 LYS   A CB    1 
ATOM   2870 C CG    . LYS   A 1 369 ? 33.714 9.755   54.962 1.00 53.90  ? 359 LYS   A CG    1 
ATOM   2871 C CD    . LYS   A 1 369 ? 32.600 10.702  55.394 1.00 54.45  ? 359 LYS   A CD    1 
ATOM   2872 C CE    . LYS   A 1 369 ? 31.393 10.617  54.505 1.00 55.34  ? 359 LYS   A CE    1 
ATOM   2873 N NZ    . LYS   A 1 369 ? 30.582 9.416   54.720 1.00 56.16  ? 359 LYS   A NZ    1 
ATOM   2874 N N     . GLY   A 1 370 ? 37.704 9.515   57.023 1.00 49.07  ? 360 GLY   A N     1 
ATOM   2875 C CA    . GLY   A 1 370 ? 38.910 10.203  57.447 1.00 48.46  ? 360 GLY   A CA    1 
ATOM   2876 C C     . GLY   A 1 370 ? 40.137 9.304   57.414 1.00 48.56  ? 360 GLY   A C     1 
ATOM   2877 O O     . GLY   A 1 370 ? 40.025 8.083   57.406 1.00 47.24  ? 360 GLY   A O     1 
ATOM   2878 N N     . MET   A 1 371 ? 41.303 9.950   57.368 1.00 52.29  ? 361 MET   A N     1 
ATOM   2879 C CA    . MET   A 1 371 ? 42.576 9.288   57.566 1.00 56.03  ? 361 MET   A CA    1 
ATOM   2880 C C     . MET   A 1 371 ? 43.321 10.016  58.680 1.00 56.34  ? 361 MET   A C     1 
ATOM   2881 O O     . MET   A 1 371 ? 43.213 11.234  58.802 1.00 59.26  ? 361 MET   A O     1 
ATOM   2882 C CB    . MET   A 1 371 ? 43.441 9.333   56.303 1.00 60.90  ? 361 MET   A CB    1 
ATOM   2883 C CG    . MET   A 1 371 ? 42.809 8.705   55.074 1.00 64.46  ? 361 MET   A CG    1 
ATOM   2884 S SD    . MET   A 1 371 ? 43.904 8.731   53.636 1.00 69.52  ? 361 MET   A SD    1 
ATOM   2885 C CE    . MET   A 1 371 ? 45.430 7.985   54.223 1.00 66.99  ? 361 MET   A CE    1 
ATOM   2886 N N     . TRP   A 1 372 ? 44.051 9.242   59.491 1.00 55.48  ? 362 TRP   A N     1 
ATOM   2887 C CA    . TRP   A 1 372 ? 45.004 9.754   60.462 1.00 53.34  ? 362 TRP   A CA    1 
ATOM   2888 C C     . TRP   A 1 372 ? 46.361 9.129   60.153 1.00 52.37  ? 362 TRP   A C     1 
ATOM   2889 O O     . TRP   A 1 372 ? 46.480 7.907   60.141 1.00 53.81  ? 362 TRP   A O     1 
ATOM   2890 C CB    . TRP   A 1 372 ? 44.600 9.378   61.898 1.00 52.93  ? 362 TRP   A CB    1 
ATOM   2891 C CG    . TRP   A 1 372 ? 43.309 9.944   62.433 1.00 52.04  ? 362 TRP   A CG    1 
ATOM   2892 C CD1   . TRP   A 1 372 ? 43.184 10.901  63.396 1.00 52.24  ? 362 TRP   A CD1   1 
ATOM   2893 C CD2   . TRP   A 1 372 ? 41.963 9.544   62.094 1.00 51.15  ? 362 TRP   A CD2   1 
ATOM   2894 N NE1   . TRP   A 1 372 ? 41.865 11.139  63.666 1.00 52.35  ? 362 TRP   A NE1   1 
ATOM   2895 C CE2   . TRP   A 1 372 ? 41.092 10.322  62.886 1.00 51.48  ? 362 TRP   A CE2   1 
ATOM   2896 C CE3   . TRP   A 1 372 ? 41.410 8.621   61.202 1.00 50.90  ? 362 TRP   A CE3   1 
ATOM   2897 C CZ2   . TRP   A 1 372 ? 39.707 10.199  62.810 1.00 51.28  ? 362 TRP   A CZ2   1 
ATOM   2898 C CZ3   . TRP   A 1 372 ? 40.041 8.500   61.128 1.00 51.50  ? 362 TRP   A CZ3   1 
ATOM   2899 C CH2   . TRP   A 1 372 ? 39.202 9.271   61.931 1.00 51.18  ? 362 TRP   A CH2   1 
ATOM   2900 N N     . VAL   A 1 373 ? 47.378 9.958   59.916 1.00 51.60  ? 363 VAL   A N     1 
ATOM   2901 C CA    . VAL   A 1 373 ? 48.727 9.462   59.702 1.00 51.43  ? 363 VAL   A CA    1 
ATOM   2902 C C     . VAL   A 1 373 ? 49.547 9.814   60.936 1.00 51.63  ? 363 VAL   A C     1 
ATOM   2903 O O     . VAL   A 1 373 ? 49.796 10.988  61.194 1.00 51.34  ? 363 VAL   A O     1 
ATOM   2904 C CB    . VAL   A 1 373 ? 49.351 10.025  58.409 1.00 51.16  ? 363 VAL   A CB    1 
ATOM   2905 C CG1   . VAL   A 1 373 ? 50.790 9.562   58.210 1.00 50.34  ? 363 VAL   A CG1   1 
ATOM   2906 C CG2   . VAL   A 1 373 ? 48.510 9.668   57.190 1.00 51.26  ? 363 VAL   A CG2   1 
ATOM   2907 N N     . ASP   A 1 374 ? 49.944 8.781   61.690 1.00 53.98  ? 364 ASP   A N     1 
ATOM   2908 C CA    . ASP   A 1 374 ? 50.594 8.947   62.981 1.00 56.24  ? 364 ASP   A CA    1 
ATOM   2909 C C     . ASP   A 1 374 ? 49.747 9.891   63.833 1.00 57.43  ? 364 ASP   A C     1 
ATOM   2910 O O     . ASP   A 1 374 ? 48.537 9.708   63.926 1.00 58.96  ? 364 ASP   A O     1 
ATOM   2911 C CB    . ASP   A 1 374 ? 52.048 9.359   62.807 1.00 57.39  ? 364 ASP   A CB    1 
ATOM   2912 C CG    . ASP   A 1 374 ? 52.942 8.331   62.132 1.00 59.20  ? 364 ASP   A CG    1 
ATOM   2913 O OD1   . ASP   A 1 374 ? 52.584 7.134   62.149 1.00 59.41  ? 364 ASP   A OD1   1 
ATOM   2914 O OD2   . ASP   A 1 374 ? 53.985 8.741   61.581 1.00 61.04  ? 364 ASP   A OD2   1 
ATOM   2915 N N     . ASP   A 1 375 ? 50.394 10.899  64.430 1.00 60.22  ? 365 ASP   A N     1 
ATOM   2916 C CA    . ASP   A 1 375 ? 49.728 11.926  65.215 1.00 61.59  ? 365 ASP   A CA    1 
ATOM   2917 C C     . ASP   A 1 375 ? 49.931 13.280  64.534 1.00 62.00  ? 365 ASP   A C     1 
ATOM   2918 O O     . ASP   A 1 375 ? 49.765 14.318  65.171 1.00 62.61  ? 365 ASP   A O     1 
ATOM   2919 C CB    . ASP   A 1 375 ? 50.245 11.920  66.649 1.00 62.52  ? 365 ASP   A CB    1 
ATOM   2920 C CG    . ASP   A 1 375 ? 51.754 12.071  66.822 1.00 63.18  ? 365 ASP   A CG    1 
ATOM   2921 O OD1   . ASP   A 1 375 ? 52.459 12.194  65.799 1.00 63.65  ? 365 ASP   A OD1   1 
ATOM   2922 O OD2   . ASP   A 1 375 ? 52.222 12.066  67.982 1.00 63.97  ? 365 ASP   A OD2   1 
ATOM   2923 N N     . LYS   A 1 376 ? 50.257 13.253  63.231 1.00 60.95  ? 366 LYS   A N     1 
ATOM   2924 C CA    . LYS   A 1 376 ? 50.797 14.410  62.532 1.00 61.68  ? 366 LYS   A CA    1 
ATOM   2925 C C     . LYS   A 1 376 ? 49.840 14.922  61.458 1.00 59.03  ? 366 LYS   A C     1 
ATOM   2926 O O     . LYS   A 1 376 ? 49.770 16.132  61.247 1.00 55.93  ? 366 LYS   A O     1 
ATOM   2927 C CB    . LYS   A 1 376 ? 52.151 14.089  61.887 1.00 64.66  ? 366 LYS   A CB    1 
ATOM   2928 C CG    . LYS   A 1 376 ? 53.299 13.894  62.867 1.00 65.78  ? 366 LYS   A CG    1 
ATOM   2929 C CD    . LYS   A 1 376 ? 53.695 15.170  63.600 1.00 67.53  ? 366 LYS   A CD    1 
ATOM   2930 C CE    . LYS   A 1 376 ? 54.502 14.906  64.830 1.00 69.50  ? 366 LYS   A CE    1 
ATOM   2931 N NZ    . LYS   A 1 376 ? 55.827 14.375  64.518 1.00 70.22  ? 366 LYS   A NZ    1 
ATOM   2932 N N     . TRP   A 1 377 ? 49.152 14.010  60.754 1.00 56.48  ? 367 TRP   A N     1 
ATOM   2933 C CA    . TRP   A 1 377 ? 48.190 14.399  59.734 1.00 55.19  ? 367 TRP   A CA    1 
ATOM   2934 C C     . TRP   A 1 377 ? 46.793 13.939  60.125 1.00 54.43  ? 367 TRP   A C     1 
ATOM   2935 O O     . TRP   A 1 377 ? 46.630 12.861  60.688 1.00 55.04  ? 367 TRP   A O     1 
ATOM   2936 C CB    . TRP   A 1 377 ? 48.557 13.805  58.368 1.00 55.40  ? 367 TRP   A CB    1 
ATOM   2937 C CG    . TRP   A 1 377 ? 49.946 14.153  57.925 1.00 57.19  ? 367 TRP   A CG    1 
ATOM   2938 C CD1   . TRP   A 1 377 ? 51.094 13.490  58.242 1.00 56.86  ? 367 TRP   A CD1   1 
ATOM   2939 C CD2   . TRP   A 1 377 ? 50.333 15.273  57.102 1.00 58.01  ? 367 TRP   A CD2   1 
ATOM   2940 N NE1   . TRP   A 1 377 ? 52.167 14.112  57.669 1.00 58.37  ? 367 TRP   A NE1   1 
ATOM   2941 C CE2   . TRP   A 1 377 ? 51.736 15.210  56.971 1.00 58.77  ? 367 TRP   A CE2   1 
ATOM   2942 C CE3   . TRP   A 1 377 ? 49.640 16.313  56.474 1.00 58.70  ? 367 TRP   A CE3   1 
ATOM   2943 C CZ2   . TRP   A 1 377 ? 52.454 16.149  56.233 1.00 59.94  ? 367 TRP   A CZ2   1 
ATOM   2944 C CZ3   . TRP   A 1 377 ? 50.350 17.239  55.742 1.00 59.01  ? 367 TRP   A CZ3   1 
ATOM   2945 C CH2   . TRP   A 1 377 ? 51.738 17.159  55.631 1.00 60.61  ? 367 TRP   A CH2   1 
ATOM   2946 N N     . MET   A 1 378 ? 45.795 14.756  59.779 1.00 52.86  ? 368 MET   A N     1 
ATOM   2947 C CA    . MET   A 1 378 ? 44.411 14.324  59.801 1.00 52.83  ? 368 MET   A CA    1 
ATOM   2948 C C     . MET   A 1 378 ? 43.750 14.762  58.502 1.00 51.96  ? 368 MET   A C     1 
ATOM   2949 O O     . MET   A 1 378 ? 43.758 15.944  58.172 1.00 52.75  ? 368 MET   A O     1 
ATOM   2950 C CB    . MET   A 1 378 ? 43.654 14.925  60.988 1.00 53.23  ? 368 MET   A CB    1 
ATOM   2951 C CG    . MET   A 1 378 ? 44.154 14.441  62.330 1.00 54.60  ? 368 MET   A CG    1 
ATOM   2952 S SD    . MET   A 1 378 ? 43.390 15.329  63.700 1.00 55.52  ? 368 MET   A SD    1 
ATOM   2953 C CE    . MET   A 1 378 ? 41.709 14.743  63.450 1.00 56.22  ? 368 MET   A CE    1 
ATOM   2954 N N     . LEU   A 1 379 ? 43.212 13.791  57.760 1.00 51.31  ? 369 LEU   A N     1 
ATOM   2955 C CA    . LEU   A 1 379 ? 42.410 14.082  56.588 1.00 52.57  ? 369 LEU   A CA    1 
ATOM   2956 C C     . LEU   A 1 379 ? 40.941 13.988  56.986 1.00 52.49  ? 369 LEU   A C     1 
ATOM   2957 O O     . LEU   A 1 379 ? 40.471 12.919  57.363 1.00 51.39  ? 369 LEU   A O     1 
ATOM   2958 C CB    . LEU   A 1 379 ? 42.738 13.119  55.449 1.00 52.74  ? 369 LEU   A CB    1 
ATOM   2959 C CG    . LEU   A 1 379 ? 42.037 13.409  54.119 1.00 54.16  ? 369 LEU   A CG    1 
ATOM   2960 C CD1   . LEU   A 1 379 ? 42.628 14.640  53.456 1.00 55.09  ? 369 LEU   A CD1   1 
ATOM   2961 C CD2   . LEU   A 1 379 ? 42.108 12.209  53.195 1.00 55.43  ? 369 LEU   A CD2   1 
ATOM   2962 N N     . ILE   A 1 380 ? 40.242 15.128  56.937 1.00 53.20  ? 370 ILE   A N     1 
ATOM   2963 C CA    . ILE   A 1 380 ? 38.795 15.153  57.061 1.00 52.83  ? 370 ILE   A CA    1 
ATOM   2964 C C     . ILE   A 1 380 ? 38.240 15.343  55.654 1.00 50.90  ? 370 ILE   A C     1 
ATOM   2965 O O     . ILE   A 1 380 ? 38.708 16.212  54.921 1.00 51.72  ? 370 ILE   A O     1 
ATOM   2966 C CB    . ILE   A 1 380 ? 38.330 16.225  58.070 1.00 53.94  ? 370 ILE   A CB    1 
ATOM   2967 C CG1   . ILE   A 1 380 ? 38.438 17.654  57.547 1.00 53.98  ? 370 ILE   A CG1   1 
ATOM   2968 C CG2   . ILE   A 1 380 ? 39.087 16.075  59.389 1.00 55.66  ? 370 ILE   A CG2   1 
ATOM   2969 C CD1   . ILE   A 1 380 ? 37.960 18.697  58.540 1.00 54.56  ? 370 ILE   A CD1   1 
ATOM   2970 N N     . THR   A 1 381 ? 37.290 14.483  55.270 1.00 49.85  ? 371 THR   A N     1 
ATOM   2971 C CA    . THR   A 1 381 ? 36.886 14.351  53.881 1.00 49.40  ? 371 THR   A CA    1 
ATOM   2972 C C     . THR   A 1 381 ? 35.500 13.719  53.810 1.00 48.82  ? 371 THR   A C     1 
ATOM   2973 O O     . THR   A 1 381 ? 35.024 13.150  54.786 1.00 50.98  ? 371 THR   A O     1 
ATOM   2974 C CB    . THR   A 1 381 ? 37.931 13.516  53.137 1.00 50.18  ? 371 THR   A CB    1 
ATOM   2975 O OG1   . THR   A 1 381 ? 37.585 13.552  51.754 1.00 50.01  ? 371 THR   A OG1   1 
ATOM   2976 C CG2   . THR   A 1 381 ? 37.999 12.081  53.629 1.00 49.45  ? 371 THR   A CG2   1 
ATOM   2977 N N     . GLY   A 1 382 ? 34.856 13.848  52.648 1.00 48.91  ? 372 GLY   A N     1 
ATOM   2978 C CA    . GLY   A 1 382 ? 33.696 13.037  52.314 1.00 50.05  ? 372 GLY   A CA    1 
ATOM   2979 C C     . GLY   A 1 382 ? 34.101 11.758  51.580 1.00 50.45  ? 372 GLY   A C     1 
ATOM   2980 O O     . GLY   A 1 382 ? 33.262 10.897  51.340 1.00 51.96  ? 372 GLY   A O     1 
ATOM   2981 N N     . ASN   A 1 383 ? 35.393 11.640  51.239 1.00 50.71  ? 373 ASN   A N     1 
ATOM   2982 C CA    . ASN   A 1 383 ? 35.909 10.550  50.426 1.00 51.12  ? 373 ASN   A CA    1 
ATOM   2983 C C     . ASN   A 1 383 ? 35.798 9.245   51.212 1.00 51.37  ? 373 ASN   A C     1 
ATOM   2984 O O     . ASN   A 1 383 ? 36.345 9.137   52.305 1.00 52.33  ? 373 ASN   A O     1 
ATOM   2985 C CB    . ASN   A 1 383 ? 37.344 10.846  49.998 1.00 52.66  ? 373 ASN   A CB    1 
ATOM   2986 C CG    . ASN   A 1 383 ? 37.842 9.964   48.874 1.00 52.75  ? 373 ASN   A CG    1 
ATOM   2987 O OD1   . ASN   A 1 383 ? 37.672 8.741   48.903 1.00 53.86  ? 373 ASN   A OD1   1 
ATOM   2988 N ND2   . ASN   A 1 383 ? 38.478 10.562  47.879 1.00 52.59  ? 373 ASN   A ND2   1 
ATOM   2989 N N     . ASN   A 1 384 ? 35.100 8.260   50.630 1.00 51.67  ? 374 ASN   A N     1 
ATOM   2990 C CA    . ASN   A 1 384 ? 34.830 6.986   51.276 1.00 50.92  ? 374 ASN   A CA    1 
ATOM   2991 C C     . ASN   A 1 384 ? 35.860 5.926   50.880 1.00 51.08  ? 374 ASN   A C     1 
ATOM   2992 O O     . ASN   A 1 384 ? 35.655 4.747   51.162 1.00 49.70  ? 374 ASN   A O     1 
ATOM   2993 C CB    . ASN   A 1 384 ? 33.424 6.495   50.942 1.00 51.44  ? 374 ASN   A CB    1 
ATOM   2994 C CG    . ASN   A 1 384 ? 32.344 7.391   51.501 1.00 52.57  ? 374 ASN   A CG    1 
ATOM   2995 O OD1   . ASN   A 1 384 ? 31.361 7.697   50.819 1.00 53.56  ? 374 ASN   A OD1   1 
ATOM   2996 N ND2   . ASN   A 1 384 ? 32.474 7.788   52.755 1.00 54.72  ? 374 ASN   A ND2   1 
ATOM   2997 N N     . LEU   A 1 385 ? 36.947 6.350   50.216 1.00 52.99  ? 375 LEU   A N     1 
ATOM   2998 C CA    . LEU   A 1 385 ? 38.034 5.475   49.789 1.00 54.39  ? 375 LEU   A CA    1 
ATOM   2999 C C     . LEU   A 1 385 ? 37.517 4.259   49.015 1.00 56.85  ? 375 LEU   A C     1 
ATOM   3000 O O     . LEU   A 1 385 ? 37.990 3.144   49.226 1.00 57.06  ? 375 LEU   A O     1 
ATOM   3001 C CB    . LEU   A 1 385 ? 38.840 5.054   51.014 1.00 53.20  ? 375 LEU   A CB    1 
ATOM   3002 C CG    . LEU   A 1 385 ? 39.331 6.191   51.911 1.00 52.58  ? 375 LEU   A CG    1 
ATOM   3003 C CD1   . LEU   A 1 385 ? 40.067 5.597   53.088 1.00 52.90  ? 375 LEU   A CD1   1 
ATOM   3004 C CD2   . LEU   A 1 385 ? 40.210 7.173   51.168 1.00 52.01  ? 375 LEU   A CD2   1 
ATOM   3005 N N     . ASN   A 1 386 ? 36.565 4.482   48.099 1.00 58.82  ? 376 ASN   A N     1 
ATOM   3006 C CA    . ASN   A 1 386 ? 36.000 3.416   47.284 1.00 58.63  ? 376 ASN   A CA    1 
ATOM   3007 C C     . ASN   A 1 386 ? 36.091 3.804   45.805 1.00 58.82  ? 376 ASN   A C     1 
ATOM   3008 O O     . ASN   A 1 386 ? 36.463 4.933   45.481 1.00 56.85  ? 376 ASN   A O     1 
ATOM   3009 C CB    . ASN   A 1 386 ? 34.580 3.083   47.734 1.00 57.51  ? 376 ASN   A CB    1 
ATOM   3010 C CG    . ASN   A 1 386 ? 33.663 4.279   47.685 1.00 56.73  ? 376 ASN   A CG    1 
ATOM   3011 O OD1   . ASN   A 1 386 ? 34.119 5.405   47.464 1.00 58.03  ? 376 ASN   A OD1   1 
ATOM   3012 N ND2   . ASN   A 1 386 ? 32.376 4.064   47.907 1.00 57.18  ? 376 ASN   A ND2   1 
ATOM   3013 N N     . PRO   A 1 387 ? 35.813 2.872   44.861 1.00 60.16  ? 377 PRO   A N     1 
ATOM   3014 C CA    . PRO   A 1 387 ? 35.768 3.203   43.432 1.00 60.77  ? 377 PRO   A CA    1 
ATOM   3015 C C     . PRO   A 1 387 ? 34.938 4.427   43.052 1.00 61.45  ? 377 PRO   A C     1 
ATOM   3016 O O     . PRO   A 1 387 ? 35.318 5.160   42.144 1.00 62.07  ? 377 PRO   A O     1 
ATOM   3017 C CB    . PRO   A 1 387 ? 35.211 1.918   42.819 1.00 59.14  ? 377 PRO   A CB    1 
ATOM   3018 C CG    . PRO   A 1 387 ? 35.787 0.843   43.702 1.00 60.31  ? 377 PRO   A CG    1 
ATOM   3019 C CD    . PRO   A 1 387 ? 35.662 1.428   45.099 1.00 60.09  ? 377 PRO   A CD    1 
ATOM   3020 N N     . ARG   A 1 388 ? 33.816 4.642   43.747 1.00 62.42  ? 378 ARG   A N     1 
ATOM   3021 C CA    . ARG   A 1 388 ? 33.006 5.832   43.539 1.00 65.52  ? 378 ARG   A CA    1 
ATOM   3022 C C     . ARG   A 1 388 ? 33.857 7.096   43.661 1.00 66.33  ? 378 ARG   A C     1 
ATOM   3023 O O     . ARG   A 1 388 ? 33.847 7.940   42.769 1.00 67.23  ? 378 ARG   A O     1 
ATOM   3024 C CB    . ARG   A 1 388 ? 31.866 5.939   44.555 1.00 65.08  ? 378 ARG   A CB    1 
ATOM   3025 C CG    . ARG   A 1 388 ? 30.718 4.973   44.309 1.00 65.46  ? 378 ARG   A CG    1 
ATOM   3026 C CD    . ARG   A 1 388 ? 29.439 5.526   44.898 1.00 64.79  ? 378 ARG   A CD    1 
ATOM   3027 N NE    . ARG   A 1 388 ? 28.990 6.671   44.100 1.00 64.23  ? 378 ARG   A NE    1 
ATOM   3028 C CZ    . ARG   A 1 388 ? 28.404 6.598   42.911 1.00 63.45  ? 378 ARG   A CZ    1 
ATOM   3029 N NH1   . ARG   A 1 388 ? 28.070 5.428   42.393 1.00 62.87  ? 378 ARG   A NH1   1 
ATOM   3030 N NH2   . ARG   A 1 388 ? 28.125 7.707   42.249 1.00 62.86  ? 378 ARG   A NH2   1 
ATOM   3031 N N     . ALA   A 1 389 ? 34.580 7.228   44.777 1.00 66.26  ? 379 ALA   A N     1 
ATOM   3032 C CA    . ALA   A 1 389 ? 35.346 8.432   45.052 1.00 68.16  ? 379 ALA   A CA    1 
ATOM   3033 C C     . ALA   A 1 389 ? 36.566 8.510   44.141 1.00 69.34  ? 379 ALA   A C     1 
ATOM   3034 O O     . ALA   A 1 389 ? 37.073 9.595   43.874 1.00 72.14  ? 379 ALA   A O     1 
ATOM   3035 C CB    . ALA   A 1 389 ? 35.760 8.465   46.505 1.00 70.45  ? 379 ALA   A CB    1 
ATOM   3036 N N     . TRP   A 1 390 ? 37.043 7.352   43.682 1.00 71.72  ? 380 TRP   A N     1 
ATOM   3037 C CA    . TRP   A 1 390 ? 38.272 7.299   42.911 1.00 72.60  ? 380 TRP   A CA    1 
ATOM   3038 C C     . TRP   A 1 390 ? 38.021 7.760   41.476 1.00 73.78  ? 380 TRP   A C     1 
ATOM   3039 O O     . TRP   A 1 390 ? 38.882 8.406   40.879 1.00 76.73  ? 380 TRP   A O     1 
ATOM   3040 C CB    . TRP   A 1 390 ? 38.868 5.885   42.958 1.00 72.64  ? 380 TRP   A CB    1 
ATOM   3041 C CG    . TRP   A 1 390 ? 40.330 5.885   43.310 1.00 74.24  ? 380 TRP   A CG    1 
ATOM   3042 C CD1   . TRP   A 1 390 ? 41.384 5.472   42.548 1.00 76.14  ? 380 TRP   A CD1   1 
ATOM   3043 C CD2   . TRP   A 1 390 ? 40.892 6.385   44.541 1.00 74.06  ? 380 TRP   A CD2   1 
ATOM   3044 N NE1   . TRP   A 1 390 ? 42.559 5.655   43.228 1.00 76.44  ? 380 TRP   A NE1   1 
ATOM   3045 C CE2   . TRP   A 1 390 ? 42.292 6.219   44.449 1.00 75.77  ? 380 TRP   A CE2   1 
ATOM   3046 C CE3   . TRP   A 1 390 ? 40.349 6.944   45.703 1.00 72.99  ? 380 TRP   A CE3   1 
ATOM   3047 C CZ2   . TRP   A 1 390 ? 43.151 6.596   45.479 1.00 75.87  ? 380 TRP   A CZ2   1 
ATOM   3048 C CZ3   . TRP   A 1 390 ? 41.199 7.318   46.719 1.00 74.44  ? 380 TRP   A CZ3   1 
ATOM   3049 C CH2   . TRP   A 1 390 ? 42.581 7.151   46.603 1.00 76.43  ? 380 TRP   A CH2   1 
ATOM   3050 N N     . ARG   A 1 391 ? 36.837 7.440   40.937 1.00 72.28  ? 381 ARG   A N     1 
ATOM   3051 C CA    . ARG   A 1 391 ? 36.564 7.635   39.523 1.00 73.41  ? 381 ARG   A CA    1 
ATOM   3052 C C     . ARG   A 1 391 ? 35.343 8.523   39.280 1.00 71.39  ? 381 ARG   A C     1 
ATOM   3053 O O     . ARG   A 1 391 ? 35.354 9.305   38.334 1.00 73.11  ? 381 ARG   A O     1 
ATOM   3054 C CB    . ARG   A 1 391 ? 36.404 6.269   38.843 1.00 77.76  ? 381 ARG   A CB    1 
ATOM   3055 C CG    . ARG   A 1 391 ? 37.718 5.527   38.641 1.00 82.46  ? 381 ARG   A CG    1 
ATOM   3056 C CD    . ARG   A 1 391 ? 38.595 6.193   37.581 1.00 88.34  ? 381 ARG   A CD    1 
ATOM   3057 N NE    . ARG   A 1 391 ? 39.941 5.613   37.486 1.00 93.22  ? 381 ARG   A NE    1 
ATOM   3058 C CZ    . ARG   A 1 391 ? 41.059 6.106   38.029 1.00 98.03  ? 381 ARG   A CZ    1 
ATOM   3059 N NH1   . ARG   A 1 391 ? 41.021 7.119   38.884 1.00 99.27  ? 381 ARG   A NH1   1 
ATOM   3060 N NH2   . ARG   A 1 391 ? 42.225 5.546   37.744 1.00 97.93  ? 381 ARG   A NH2   1 
ATOM   3061 N N     . LEU   A 1 392 ? 34.298 8.413   40.110 1.00 67.38  ? 382 LEU   A N     1 
ATOM   3062 C CA    . LEU   A 1 392 ? 32.979 8.886   39.718 1.00 65.65  ? 382 LEU   A CA    1 
ATOM   3063 C C     . LEU   A 1 392 ? 32.645 10.259  40.300 1.00 64.82  ? 382 LEU   A C     1 
ATOM   3064 O O     . LEU   A 1 392 ? 32.243 11.149  39.557 1.00 63.10  ? 382 LEU   A O     1 
ATOM   3065 C CB    . LEU   A 1 392 ? 31.932 7.855   40.129 1.00 65.41  ? 382 LEU   A CB    1 
ATOM   3066 C CG    . LEU   A 1 392 ? 32.126 6.446   39.566 1.00 66.29  ? 382 LEU   A CG    1 
ATOM   3067 C CD1   . LEU   A 1 392 ? 30.960 5.556   39.955 1.00 66.65  ? 382 LEU   A CD1   1 
ATOM   3068 C CD2   . LEU   A 1 392 ? 32.300 6.480   38.059 1.00 66.52  ? 382 LEU   A CD2   1 
ATOM   3069 N N     . ASP   A 1 393 ? 32.757 10.416  41.626 1.00 65.67  ? 383 ASP   A N     1 
ATOM   3070 C CA    . ASP   A 1 393 ? 32.074 11.496  42.325 1.00 63.26  ? 383 ASP   A CA    1 
ATOM   3071 C C     . ASP   A 1 393 ? 33.021 12.662  42.590 1.00 60.94  ? 383 ASP   A C     1 
ATOM   3072 O O     . ASP   A 1 393 ? 34.232 12.485  42.681 1.00 59.58  ? 383 ASP   A O     1 
ATOM   3073 C CB    . ASP   A 1 393 ? 31.432 10.993  43.605 1.00 64.02  ? 383 ASP   A CB    1 
ATOM   3074 C CG    . ASP   A 1 393 ? 30.499 9.809   43.415 1.00 65.74  ? 383 ASP   A CG    1 
ATOM   3075 O OD1   . ASP   A 1 393 ? 29.750 9.815   42.418 1.00 66.00  ? 383 ASP   A OD1   1 
ATOM   3076 O OD2   . ASP   A 1 393 ? 30.515 8.902   44.270 1.00 66.94  ? 383 ASP   A OD2   1 
ATOM   3077 N N     . LEU   A 1 394 ? 32.437 13.860  42.697 1.00 60.65  ? 384 LEU   A N     1 
ATOM   3078 C CA    . LEU   A 1 394 ? 33.189 15.065  43.008 1.00 60.06  ? 384 LEU   A CA    1 
ATOM   3079 C C     . LEU   A 1 394 ? 33.494 15.048  44.500 1.00 59.15  ? 384 LEU   A C     1 
ATOM   3080 O O     . LEU   A 1 394 ? 32.583 15.166  45.312 1.00 58.34  ? 384 LEU   A O     1 
ATOM   3081 C CB    . LEU   A 1 394 ? 32.382 16.303  42.611 1.00 60.17  ? 384 LEU   A CB    1 
ATOM   3082 C CG    . LEU   A 1 394 ? 33.005 17.662  42.945 1.00 60.14  ? 384 LEU   A CG    1 
ATOM   3083 C CD1   . LEU   A 1 394 ? 34.419 17.807  42.401 1.00 59.99  ? 384 LEU   A CD1   1 
ATOM   3084 C CD2   . LEU   A 1 394 ? 32.117 18.768  42.412 1.00 59.60  ? 384 LEU   A CD2   1 
ATOM   3085 N N     . GLU   A 1 395 ? 34.773 14.870  44.839 1.00 58.95  ? 385 GLU   A N     1 
ATOM   3086 C CA    . GLU   A 1 395 ? 35.197 14.710  46.217 1.00 59.14  ? 385 GLU   A CA    1 
ATOM   3087 C C     . GLU   A 1 395 ? 36.014 15.922  46.650 1.00 58.72  ? 385 GLU   A C     1 
ATOM   3088 O O     . GLU   A 1 395 ? 36.649 16.581  45.827 1.00 58.44  ? 385 GLU   A O     1 
ATOM   3089 C CB    . GLU   A 1 395 ? 36.044 13.447  46.372 1.00 60.72  ? 385 GLU   A CB    1 
ATOM   3090 C CG    . GLU   A 1 395 ? 35.296 12.160  46.034 1.00 62.19  ? 385 GLU   A CG    1 
ATOM   3091 C CD    . GLU   A 1 395 ? 34.188 11.752  46.996 1.00 63.50  ? 385 GLU   A CD    1 
ATOM   3092 O OE1   . GLU   A 1 395 ? 33.985 12.419  48.036 1.00 62.83  ? 385 GLU   A OE1   1 
ATOM   3093 O OE2   . GLU   A 1 395 ? 33.514 10.745  46.691 1.00 63.93  ? 385 GLU   A OE2   1 
ATOM   3094 N N     . ASN   A 1 396 ? 35.998 16.197  47.959 1.00 57.72  ? 386 ASN   A N     1 
ATOM   3095 C CA    . ASN   A 1 396 ? 36.875 17.204  48.528 1.00 56.76  ? 386 ASN   A CA    1 
ATOM   3096 C C     . ASN   A 1 396 ? 37.301 16.775  49.929 1.00 57.22  ? 386 ASN   A C     1 
ATOM   3097 O O     . ASN   A 1 396 ? 36.856 15.744  50.435 1.00 58.10  ? 386 ASN   A O     1 
ATOM   3098 C CB    . ASN   A 1 396 ? 36.234 18.587  48.488 1.00 56.04  ? 386 ASN   A CB    1 
ATOM   3099 C CG    . ASN   A 1 396 ? 35.246 18.813  49.605 1.00 54.94  ? 386 ASN   A CG    1 
ATOM   3100 O OD1   . ASN   A 1 396 ? 34.778 17.857  50.236 1.00 55.63  ? 386 ASN   A OD1   1 
ATOM   3101 N ND2   . ASN   A 1 396 ? 34.901 20.070  49.845 1.00 52.87  ? 386 ASN   A ND2   1 
ATOM   3102 N N     . ALA   A 1 397 ? 38.176 17.587  50.535 1.00 55.78  ? 387 ALA   A N     1 
ATOM   3103 C CA    . ALA   A 1 397 ? 38.730 17.304  51.846 1.00 55.03  ? 387 ALA   A CA    1 
ATOM   3104 C C     . ALA   A 1 397 ? 39.405 18.552  52.400 1.00 55.23  ? 387 ALA   A C     1 
ATOM   3105 O O     . ALA   A 1 397 ? 39.601 19.532  51.687 1.00 55.92  ? 387 ALA   A O     1 
ATOM   3106 C CB    . ALA   A 1 397 ? 39.726 16.168  51.763 1.00 55.15  ? 387 ALA   A CB    1 
ATOM   3107 N N     . ILE   A 1 398 ? 39.752 18.484  53.687 1.00 55.61  ? 388 ILE   A N     1 
ATOM   3108 C CA    . ILE   A 1 398 ? 40.684 19.412  54.298 1.00 54.18  ? 388 ILE   A CA    1 
ATOM   3109 C C     . ILE   A 1 398 ? 41.754 18.566  54.974 1.00 54.07  ? 388 ILE   A C     1 
ATOM   3110 O O     . ILE   A 1 398 ? 41.422 17.683  55.759 1.00 56.54  ? 388 ILE   A O     1 
ATOM   3111 C CB    . ILE   A 1 398 ? 39.965 20.355  55.282 1.00 54.88  ? 388 ILE   A CB    1 
ATOM   3112 C CG1   . ILE   A 1 398 ? 38.811 21.101  54.612 1.00 54.31  ? 388 ILE   A CG1   1 
ATOM   3113 C CG2   . ILE   A 1 398 ? 40.954 21.329  55.926 1.00 55.22  ? 388 ILE   A CG2   1 
ATOM   3114 C CD1   . ILE   A 1 398 ? 37.821 21.703  55.587 1.00 54.66  ? 388 ILE   A CD1   1 
ATOM   3115 N N     . LEU   A 1 399 ? 43.024 18.803  54.624 1.00 54.74  ? 389 LEU   A N     1 
ATOM   3116 C CA    . LEU   A 1 399 ? 44.129 18.063  55.207 1.00 55.16  ? 389 LEU   A CA    1 
ATOM   3117 C C     . LEU   A 1 399 ? 44.789 18.932  56.271 1.00 55.63  ? 389 LEU   A C     1 
ATOM   3118 O O     . LEU   A 1 399 ? 45.384 19.959  55.950 1.00 55.92  ? 389 LEU   A O     1 
ATOM   3119 C CB    . LEU   A 1 399 ? 45.138 17.631  54.146 1.00 56.09  ? 389 LEU   A CB    1 
ATOM   3120 C CG    . LEU   A 1 399 ? 46.406 16.950  54.675 1.00 56.41  ? 389 LEU   A CG    1 
ATOM   3121 C CD1   . LEU   A 1 399 ? 46.080 15.638  55.365 1.00 55.87  ? 389 LEU   A CD1   1 
ATOM   3122 C CD2   . LEU   A 1 399 ? 47.410 16.733  53.557 1.00 57.34  ? 389 LEU   A CD2   1 
ATOM   3123 N N     . ILE   A 1 400 ? 44.686 18.483  57.529 1.00 56.09  ? 390 ILE   A N     1 
ATOM   3124 C CA    . ILE   A 1 400 ? 45.228 19.198  58.672 1.00 55.63  ? 390 ILE   A CA    1 
ATOM   3125 C C     . ILE   A 1 400 ? 46.621 18.640  58.961 1.00 55.34  ? 390 ILE   A C     1 
ATOM   3126 O O     . ILE   A 1 400 ? 46.771 17.441  59.168 1.00 57.43  ? 390 ILE   A O     1 
ATOM   3127 C CB    . ILE   A 1 400 ? 44.295 19.065  59.895 1.00 56.03  ? 390 ILE   A CB    1 
ATOM   3128 C CG1   . ILE   A 1 400 ? 42.835 19.365  59.547 1.00 56.50  ? 390 ILE   A CG1   1 
ATOM   3129 C CG2   . ILE   A 1 400 ? 44.780 19.937  61.057 1.00 55.88  ? 390 ILE   A CG2   1 
ATOM   3130 C CD1   . ILE   A 1 400 ? 41.846 18.995  60.641 1.00 56.66  ? 390 ILE   A CD1   1 
ATOM   3131 N N     . HIS   A 1 401 ? 47.633 19.514  58.972 1.00 55.49  ? 391 HIS   A N     1 
ATOM   3132 C CA    . HIS   A 1 401 ? 48.968 19.144  59.413 1.00 56.10  ? 391 HIS   A CA    1 
ATOM   3133 C C     . HIS   A 1 401 ? 49.209 19.757  60.787 1.00 55.61  ? 391 HIS   A C     1 
ATOM   3134 O O     . HIS   A 1 401 ? 49.197 20.973  60.921 1.00 57.14  ? 391 HIS   A O     1 
ATOM   3135 C CB    . HIS   A 1 401 ? 50.026 19.613  58.407 1.00 57.55  ? 391 HIS   A CB    1 
ATOM   3136 C CG    . HIS   A 1 401 ? 51.391 19.045  58.643 1.00 58.47  ? 391 HIS   A CG    1 
ATOM   3137 N ND1   . HIS   A 1 401 ? 52.546 19.687  58.255 1.00 59.10  ? 391 HIS   A ND1   1 
ATOM   3138 C CD2   . HIS   A 1 401 ? 51.784 17.893  59.201 1.00 59.58  ? 391 HIS   A CD2   1 
ATOM   3139 C CE1   . HIS   A 1 401 ? 53.592 18.940  58.580 1.00 59.43  ? 391 HIS   A CE1   1 
ATOM   3140 N NE2   . HIS   A 1 401 ? 53.151 17.848  59.157 1.00 59.71  ? 391 HIS   A NE2   1 
ATOM   3141 N N     . ASP   A 1 402 ? 49.459 18.906  61.789 1.00 56.49  ? 392 ASP   A N     1 
ATOM   3142 C CA    . ASP   A 1 402 ? 49.561 19.323  63.178 1.00 56.23  ? 392 ASP   A CA    1 
ATOM   3143 C C     . ASP   A 1 402 ? 50.917 18.895  63.741 1.00 57.48  ? 392 ASP   A C     1 
ATOM   3144 O O     . ASP   A 1 402 ? 50.975 18.121  64.695 1.00 57.42  ? 392 ASP   A O     1 
ATOM   3145 C CB    . ASP   A 1 402 ? 48.395 18.751  63.971 1.00 55.78  ? 392 ASP   A CB    1 
ATOM   3146 C CG    . ASP   A 1 402 ? 48.334 19.138  65.442 1.00 57.26  ? 392 ASP   A CG    1 
ATOM   3147 O OD1   . ASP   A 1 402 ? 48.957 20.158  65.811 1.00 57.02  ? 392 ASP   A OD1   1 
ATOM   3148 O OD2   . ASP   A 1 402 ? 47.687 18.397  66.215 1.00 57.21  ? 392 ASP   A OD2   1 
ATOM   3149 N N     . PRO   A 1 403 ? 52.052 19.417  63.213 1.00 60.59  ? 393 PRO   A N     1 
ATOM   3150 C CA    . PRO   A 1 403 ? 53.380 18.918  63.586 1.00 61.95  ? 393 PRO   A CA    1 
ATOM   3151 C C     . PRO   A 1 403 ? 53.740 19.117  65.057 1.00 61.04  ? 393 PRO   A C     1 
ATOM   3152 O O     . PRO   A 1 403 ? 54.541 18.361  65.598 1.00 60.36  ? 393 PRO   A O     1 
ATOM   3153 C CB    . PRO   A 1 403 ? 54.386 19.655  62.677 1.00 61.79  ? 393 PRO   A CB    1 
ATOM   3154 C CG    . PRO   A 1 403 ? 53.564 20.595  61.823 1.00 62.06  ? 393 PRO   A CG    1 
ATOM   3155 C CD    . PRO   A 1 403 ? 52.116 20.538  62.265 1.00 61.33  ? 393 PRO   A CD    1 
ATOM   3156 N N     . GLN   A 1 404 ? 53.164 20.148  65.687 1.00 61.00  ? 394 GLN   A N     1 
ATOM   3157 C CA    . GLN   A 1 404 ? 53.465 20.465  67.075 1.00 62.28  ? 394 GLN   A CA    1 
ATOM   3158 C C     . GLN   A 1 404 ? 52.441 19.827  68.018 1.00 62.13  ? 394 GLN   A C     1 
ATOM   3159 O O     . GLN   A 1 404 ? 52.506 20.041  69.227 1.00 62.55  ? 394 GLN   A O     1 
ATOM   3160 C CB    . GLN   A 1 404 ? 53.525 21.982  67.258 1.00 63.37  ? 394 GLN   A CB    1 
ATOM   3161 C CG    . GLN   A 1 404 ? 54.500 22.689  66.319 1.00 66.05  ? 394 GLN   A CG    1 
ATOM   3162 C CD    . GLN   A 1 404 ? 55.893 22.093  66.338 1.00 69.29  ? 394 GLN   A CD    1 
ATOM   3163 O OE1   . GLN   A 1 404 ? 56.426 21.734  67.395 1.00 72.67  ? 394 GLN   A OE1   1 
ATOM   3164 N NE2   . GLN   A 1 404 ? 56.496 21.964  65.164 1.00 68.56  ? 394 GLN   A NE2   1 
ATOM   3165 N N     . LEU   A 1 405 ? 51.505 19.043  67.466 1.00 60.45  ? 395 LEU   A N     1 
ATOM   3166 C CA    . LEU   A 1 405 ? 50.566 18.260  68.255 1.00 60.09  ? 395 LEU   A CA    1 
ATOM   3167 C C     . LEU   A 1 405 ? 49.634 19.179  69.044 1.00 58.59  ? 395 LEU   A C     1 
ATOM   3168 O O     . LEU   A 1 405 ? 49.270 18.868  70.174 1.00 58.40  ? 395 LEU   A O     1 
ATOM   3169 C CB    . LEU   A 1 405 ? 51.310 17.298  69.183 1.00 59.96  ? 395 LEU   A CB    1 
ATOM   3170 C CG    . LEU   A 1 405 ? 52.340 16.368  68.531 1.00 60.19  ? 395 LEU   A CG    1 
ATOM   3171 C CD1   . LEU   A 1 405 ? 52.904 15.398  69.555 1.00 59.77  ? 395 LEU   A CD1   1 
ATOM   3172 C CD2   . LEU   A 1 405 ? 51.748 15.609  67.361 1.00 60.91  ? 395 LEU   A CD2   1 
ATOM   3173 N N     . GLU   A 1 406 ? 49.221 20.291  68.427 1.00 58.51  ? 396 GLU   A N     1 
ATOM   3174 C CA    . GLU   A 1 406 ? 48.402 21.292  69.096 1.00 58.09  ? 396 GLU   A CA    1 
ATOM   3175 C C     . GLU   A 1 406 ? 46.955 20.815  69.235 1.00 57.85  ? 396 GLU   A C     1 
ATOM   3176 O O     . GLU   A 1 406 ? 46.231 21.321  70.092 1.00 58.45  ? 396 GLU   A O     1 
ATOM   3177 C CB    . GLU   A 1 406 ? 48.462 22.624  68.343 1.00 57.58  ? 396 GLU   A CB    1 
ATOM   3178 C CG    . GLU   A 1 406 ? 49.854 23.250  68.301 1.00 57.22  ? 396 GLU   A CG    1 
ATOM   3179 C CD    . GLU   A 1 406 ? 49.927 24.532  67.490 1.00 57.51  ? 396 GLU   A CD    1 
ATOM   3180 O OE1   . GLU   A 1 406 ? 49.241 25.503  67.878 1.00 58.73  ? 396 GLU   A OE1   1 
ATOM   3181 O OE2   . GLU   A 1 406 ? 50.643 24.559  66.463 1.00 56.88  ? 396 GLU   A OE2   1 
ATOM   3182 N N     . LEU   A 1 407 ? 46.536 19.849  68.402 1.00 56.91  ? 397 LEU   A N     1 
ATOM   3183 C CA    . LEU   A 1 407 ? 45.169 19.345  68.422 1.00 57.31  ? 397 LEU   A CA    1 
ATOM   3184 C C     . LEU   A 1 407 ? 45.099 17.957  69.057 1.00 56.13  ? 397 LEU   A C     1 
ATOM   3185 O O     . LEU   A 1 407 ? 44.109 17.258  68.867 1.00 56.34  ? 397 LEU   A O     1 
ATOM   3186 C CB    . LEU   A 1 407 ? 44.598 19.303  67.004 1.00 57.42  ? 397 LEU   A CB    1 
ATOM   3187 C CG    . LEU   A 1 407 ? 44.405 20.646  66.296 1.00 56.80  ? 397 LEU   A CG    1 
ATOM   3188 C CD1   . LEU   A 1 407 ? 44.035 20.406  64.839 1.00 56.75  ? 397 LEU   A CD1   1 
ATOM   3189 C CD2   . LEU   A 1 407 ? 43.352 21.492  66.990 1.00 55.92  ? 397 LEU   A CD2   1 
ATOM   3190 N N     . ALA   A 1 408 ? 46.124 17.573  69.828 1.00 57.73  ? 398 ALA   A N     1 
ATOM   3191 C CA    . ALA   A 1 408 ? 46.214 16.232  70.394 1.00 58.16  ? 398 ALA   A CA    1 
ATOM   3192 C C     . ALA   A 1 408 ? 45.019 15.924  71.294 1.00 57.34  ? 398 ALA   A C     1 
ATOM   3193 O O     . ALA   A 1 408 ? 44.462 14.834  71.212 1.00 58.12  ? 398 ALA   A O     1 
ATOM   3194 C CB    . ALA   A 1 408 ? 47.519 16.051  71.142 1.00 58.72  ? 398 ALA   A CB    1 
ATOM   3195 N N     . PRO   A 1 409 ? 44.581 16.841  72.188 1.00 58.19  ? 399 PRO   A N     1 
ATOM   3196 C CA    . PRO   A 1 409 ? 43.424 16.565  73.041 1.00 58.32  ? 399 PRO   A CA    1 
ATOM   3197 C C     . PRO   A 1 409 ? 42.178 16.232  72.223 1.00 56.95  ? 399 PRO   A C     1 
ATOM   3198 O O     . PRO   A 1 409 ? 41.462 15.291  72.550 1.00 58.09  ? 399 PRO   A O     1 
ATOM   3199 C CB    . PRO   A 1 409 ? 43.248 17.851  73.872 1.00 58.17  ? 399 PRO   A CB    1 
ATOM   3200 C CG    . PRO   A 1 409 ? 44.599 18.527  73.807 1.00 58.30  ? 399 PRO   A CG    1 
ATOM   3201 C CD    . PRO   A 1 409 ? 45.157 18.173  72.436 1.00 58.78  ? 399 PRO   A CD    1 
ATOM   3202 N N     . GLN   A 1 410 ? 41.942 16.995  71.149 1.00 56.13  ? 400 GLN   A N     1 
ATOM   3203 C CA    . GLN   A 1 410 ? 40.741 16.838  70.343 1.00 57.93  ? 400 GLN   A CA    1 
ATOM   3204 C C     . GLN   A 1 410 ? 40.822 15.570  69.488 1.00 55.75  ? 400 GLN   A C     1 
ATOM   3205 O O     . GLN   A 1 410 ? 39.838 14.838  69.362 1.00 52.04  ? 400 GLN   A O     1 
ATOM   3206 C CB    . GLN   A 1 410 ? 40.493 18.087  69.497 1.00 60.43  ? 400 GLN   A CB    1 
ATOM   3207 C CG    . GLN   A 1 410 ? 40.191 19.344  70.310 1.00 63.19  ? 400 GLN   A CG    1 
ATOM   3208 C CD    . GLN   A 1 410 ? 41.378 20.271  70.466 1.00 66.71  ? 400 GLN   A CD    1 
ATOM   3209 O OE1   . GLN   A 1 410 ? 42.404 19.926  71.064 1.00 67.55  ? 400 GLN   A OE1   1 
ATOM   3210 N NE2   . GLN   A 1 410 ? 41.250 21.472  69.916 1.00 69.53  ? 400 GLN   A NE2   1 
ATOM   3211 N N     . ARG   A 1 411 ? 41.997 15.317  68.903 1.00 54.93  ? 401 ARG   A N     1 
ATOM   3212 C CA    . ARG   A 1 411 ? 42.209 14.132  68.091 1.00 56.30  ? 401 ARG   A CA    1 
ATOM   3213 C C     . ARG   A 1 411 ? 41.953 12.888  68.938 1.00 57.74  ? 401 ARG   A C     1 
ATOM   3214 O O     . ARG   A 1 411 ? 41.177 12.021  68.543 1.00 60.47  ? 401 ARG   A O     1 
ATOM   3215 C CB    . ARG   A 1 411 ? 43.622 14.133  67.494 1.00 56.46  ? 401 ARG   A CB    1 
ATOM   3216 C CG    . ARG   A 1 411 ? 43.958 12.893  66.675 1.00 56.43  ? 401 ARG   A CG    1 
ATOM   3217 C CD    . ARG   A 1 411 ? 45.277 13.005  65.922 1.00 55.61  ? 401 ARG   A CD    1 
ATOM   3218 N NE    . ARG   A 1 411 ? 46.344 13.575  66.751 1.00 55.66  ? 401 ARG   A NE    1 
ATOM   3219 C CZ    . ARG   A 1 411 ? 46.830 13.048  67.870 1.00 56.04  ? 401 ARG   A CZ    1 
ATOM   3220 N NH1   . ARG   A 1 411 ? 46.485 11.829  68.250 1.00 56.80  ? 401 ARG   A NH1   1 
ATOM   3221 N NH2   . ARG   A 1 411 ? 47.685 13.742  68.601 1.00 55.76  ? 401 ARG   A NH2   1 
ATOM   3222 N N     . GLU   A 1 412 ? 42.597 12.824  70.110 1.00 58.63  ? 402 GLU   A N     1 
ATOM   3223 C CA    . GLU   A 1 412 ? 42.505 11.669  70.991 1.00 60.07  ? 402 GLU   A CA    1 
ATOM   3224 C C     . GLU   A 1 412 ? 41.073 11.467  71.475 1.00 57.68  ? 402 GLU   A C     1 
ATOM   3225 O O     . GLU   A 1 412 ? 40.596 10.336  71.542 1.00 56.85  ? 402 GLU   A O     1 
ATOM   3226 C CB    . GLU   A 1 412 ? 43.414 11.824  72.208 1.00 62.58  ? 402 GLU   A CB    1 
ATOM   3227 C CG    . GLU   A 1 412 ? 44.892 11.636  71.888 1.00 64.67  ? 402 GLU   A CG    1 
ATOM   3228 C CD    . GLU   A 1 412 ? 45.802 12.086  73.015 1.00 69.30  ? 402 GLU   A CD    1 
ATOM   3229 O OE1   . GLU   A 1 412 ? 45.272 12.472  74.087 1.00 71.04  ? 402 GLU   A OE1   1 
ATOM   3230 O OE2   . GLU   A 1 412 ? 47.038 12.064  72.813 1.00 72.49  ? 402 GLU   A OE2   1 
ATOM   3231 N N     . LYS   A 1 413 ? 40.404 12.570  71.822 1.00 56.00  ? 403 LYS   A N     1 
ATOM   3232 C CA    . LYS   A 1 413 ? 39.046 12.509  72.334 1.00 55.48  ? 403 LYS   A CA    1 
ATOM   3233 C C     . LYS   A 1 413 ? 38.111 11.986  71.248 1.00 55.76  ? 403 LYS   A C     1 
ATOM   3234 O O     . LYS   A 1 413 ? 37.251 11.146  71.522 1.00 56.81  ? 403 LYS   A O     1 
ATOM   3235 C CB    . LYS   A 1 413 ? 38.566 13.877  72.828 1.00 55.89  ? 403 LYS   A CB    1 
ATOM   3236 C CG    . LYS   A 1 413 ? 37.194 13.829  73.476 1.00 58.01  ? 403 LYS   A CG    1 
ATOM   3237 C CD    . LYS   A 1 413 ? 36.634 15.180  73.892 1.00 60.70  ? 403 LYS   A CD    1 
ATOM   3238 C CE    . LYS   A 1 413 ? 35.239 15.017  74.410 1.00 62.14  ? 403 LYS   A CE    1 
ATOM   3239 N NZ    . LYS   A 1 413 ? 34.616 16.318  74.660 1.00 63.75  ? 403 LYS   A NZ    1 
ATOM   3240 N N     . GLU   A 1 414 ? 38.292 12.496  70.021 1.00 52.99  ? 404 GLU   A N     1 
ATOM   3241 C CA    . GLU   A 1 414 ? 37.440 12.128  68.903 1.00 50.51  ? 404 GLU   A CA    1 
ATOM   3242 C C     . GLU   A 1 414 ? 37.584 10.637  68.593 1.00 50.90  ? 404 GLU   A C     1 
ATOM   3243 O O     . GLU   A 1 414 ? 36.593 9.950   68.377 1.00 49.30  ? 404 GLU   A O     1 
ATOM   3244 C CB    . GLU   A 1 414 ? 37.770 12.986  67.684 1.00 49.59  ? 404 GLU   A CB    1 
ATOM   3245 C CG    . GLU   A 1 414 ? 36.840 12.716  66.504 1.00 49.49  ? 404 GLU   A CG    1 
ATOM   3246 C CD    . GLU   A 1 414 ? 37.256 13.379  65.209 1.00 48.28  ? 404 GLU   A CD    1 
ATOM   3247 O OE1   . GLU   A 1 414 ? 38.480 13.514  65.007 1.00 47.31  ? 404 GLU   A OE1   1 
ATOM   3248 O OE2   . GLU   A 1 414 ? 36.363 13.712  64.398 1.00 45.36  ? 404 GLU   A OE2   1 
ATOM   3249 N N     . LEU   A 1 415 ? 38.822 10.138  68.566 1.00 53.37  ? 405 LEU   A N     1 
ATOM   3250 C CA    . LEU   A 1 415 ? 39.069 8.733   68.278 1.00 54.84  ? 405 LEU   A CA    1 
ATOM   3251 C C     . LEU   A 1 415 ? 38.546 7.841   69.406 1.00 56.22  ? 405 LEU   A C     1 
ATOM   3252 O O     . LEU   A 1 415 ? 38.039 6.749   69.148 1.00 54.71  ? 405 LEU   A O     1 
ATOM   3253 C CB    . LEU   A 1 415 ? 40.559 8.528   68.024 1.00 55.48  ? 405 LEU   A CB    1 
ATOM   3254 C CG    . LEU   A 1 415 ? 41.040 8.895   66.617 1.00 56.15  ? 405 LEU   A CG    1 
ATOM   3255 C CD1   . LEU   A 1 415 ? 42.552 8.971   66.546 1.00 56.78  ? 405 LEU   A CD1   1 
ATOM   3256 C CD2   . LEU   A 1 415 ? 40.519 7.884   65.617 1.00 56.29  ? 405 LEU   A CD2   1 
ATOM   3257 N N     . GLU   A 1 416 ? 38.670 8.311   70.652 1.00 58.78  ? 406 GLU   A N     1 
ATOM   3258 C CA    . GLU   A 1 416 ? 38.164 7.587   71.807 1.00 60.69  ? 406 GLU   A CA    1 
ATOM   3259 C C     . GLU   A 1 416 ? 36.658 7.376   71.647 1.00 57.76  ? 406 GLU   A C     1 
ATOM   3260 O O     . GLU   A 1 416 ? 36.157 6.272   71.847 1.00 54.72  ? 406 GLU   A O     1 
ATOM   3261 C CB    . GLU   A 1 416 ? 38.553 8.396   73.044 1.00 65.63  ? 406 GLU   A CB    1 
ATOM   3262 C CG    . GLU   A 1 416 ? 38.220 7.740   74.379 1.00 70.56  ? 406 GLU   A CG    1 
ATOM   3263 C CD    . GLU   A 1 416 ? 38.547 8.647   75.557 1.00 74.96  ? 406 GLU   A CD    1 
ATOM   3264 O OE1   . GLU   A 1 416 ? 39.703 9.125   75.637 1.00 76.93  ? 406 GLU   A OE1   1 
ATOM   3265 O OE2   . GLU   A 1 416 ? 37.644 8.887   76.389 1.00 76.82  ? 406 GLU   A OE2   1 
ATOM   3266 N N     . LEU   A 1 417 ? 35.952 8.438   71.241 1.00 55.99  ? 407 LEU   A N     1 
ATOM   3267 C CA    . LEU   A 1 417 ? 34.508 8.385   71.047 1.00 57.84  ? 407 LEU   A CA    1 
ATOM   3268 C C     . LEU   A 1 417 ? 34.137 7.564   69.807 1.00 56.36  ? 407 LEU   A C     1 
ATOM   3269 O O     . LEU   A 1 417 ? 33.117 6.880   69.805 1.00 56.90  ? 407 LEU   A O     1 
ATOM   3270 C CB    . LEU   A 1 417 ? 33.940 9.805   70.969 1.00 58.64  ? 407 LEU   A CB    1 
ATOM   3271 C CG    . LEU   A 1 417 ? 33.951 10.609  72.277 1.00 59.07  ? 407 LEU   A CG    1 
ATOM   3272 C CD1   . LEU   A 1 417 ? 33.519 12.044  72.021 1.00 58.90  ? 407 LEU   A CD1   1 
ATOM   3273 C CD2   . LEU   A 1 417 ? 33.070 9.980   73.349 1.00 57.48  ? 407 LEU   A CD2   1 
ATOM   3274 N N     . ILE   A 1 418 ? 34.946 7.646   68.744 1.00 55.64  ? 408 ILE   A N     1 
ATOM   3275 C CA    . ILE   A 1 418 ? 34.699 6.874   67.535 1.00 56.22  ? 408 ILE   A CA    1 
ATOM   3276 C C     . ILE   A 1 418 ? 34.787 5.384   67.873 1.00 55.68  ? 408 ILE   A C     1 
ATOM   3277 O O     . ILE   A 1 418 ? 33.970 4.594   67.405 1.00 56.40  ? 408 ILE   A O     1 
ATOM   3278 C CB    . ILE   A 1 418 ? 35.659 7.294   66.397 1.00 55.42  ? 408 ILE   A CB    1 
ATOM   3279 C CG1   . ILE   A 1 418 ? 35.280 8.661   65.824 1.00 54.58  ? 408 ILE   A CG1   1 
ATOM   3280 C CG2   . ILE   A 1 418 ? 35.720 6.236   65.293 1.00 56.22  ? 408 ILE   A CG2   1 
ATOM   3281 C CD1   . ILE   A 1 418 ? 36.341 9.297   64.944 1.00 54.46  ? 408 ILE   A CD1   1 
ATOM   3282 N N     . ARG   A 1 419 ? 35.764 5.018   68.710 1.00 54.88  ? 409 ARG   A N     1 
ATOM   3283 C CA    . ARG   A 1 419 ? 36.078 3.626   68.983 1.00 55.55  ? 409 ARG   A CA    1 
ATOM   3284 C C     . ARG   A 1 419 ? 35.117 3.012   70.001 1.00 55.97  ? 409 ARG   A C     1 
ATOM   3285 O O     . ARG   A 1 419 ? 35.093 1.794   70.159 1.00 54.77  ? 409 ARG   A O     1 
ATOM   3286 C CB    . ARG   A 1 419 ? 37.517 3.527   69.502 1.00 55.94  ? 409 ARG   A CB    1 
ATOM   3287 C CG    . ARG   A 1 419 ? 38.598 3.815   68.469 1.00 56.65  ? 409 ARG   A CG    1 
ATOM   3288 C CD    . ARG   A 1 419 ? 39.976 3.817   69.117 1.00 56.83  ? 409 ARG   A CD    1 
ATOM   3289 N NE    . ARG   A 1 419 ? 41.065 4.112   68.179 1.00 56.41  ? 409 ARG   A NE    1 
ATOM   3290 C CZ    . ARG   A 1 419 ? 42.042 4.984   68.399 1.00 57.22  ? 409 ARG   A CZ    1 
ATOM   3291 N NH1   . ARG   A 1 419 ? 42.091 5.636   69.548 1.00 57.84  ? 409 ARG   A NH1   1 
ATOM   3292 N NH2   . ARG   A 1 419 ? 42.975 5.194   67.483 1.00 56.06  ? 409 ARG   A NH2   1 
ATOM   3293 N N     . GLU   A 1 420 ? 34.329 3.850   70.686 1.00 58.31  ? 410 GLU   A N     1 
ATOM   3294 C CA    . GLU   A 1 420 ? 33.544 3.423   71.836 1.00 60.48  ? 410 GLU   A CA    1 
ATOM   3295 C C     . GLU   A 1 420 ? 32.595 2.280   71.468 1.00 58.77  ? 410 GLU   A C     1 
ATOM   3296 O O     . GLU   A 1 420 ? 32.541 1.278   72.174 1.00 57.54  ? 410 GLU   A O     1 
ATOM   3297 C CB    . GLU   A 1 420 ? 32.785 4.624   72.404 1.00 66.47  ? 410 GLU   A CB    1 
ATOM   3298 C CG    . GLU   A 1 420 ? 32.032 4.314   73.695 1.00 72.33  ? 410 GLU   A CG    1 
ATOM   3299 C CD    . GLU   A 1 420 ? 31.205 5.454   74.260 1.00 76.34  ? 410 GLU   A CD    1 
ATOM   3300 O OE1   . GLU   A 1 420 ? 31.373 6.615   73.819 1.00 78.12  ? 410 GLU   A OE1   1 
ATOM   3301 O OE2   . GLU   A 1 420 ? 30.366 5.154   75.137 1.00 78.46  ? 410 GLU   A OE2   1 
ATOM   3302 N N     . HIS   A 1 421 ? 31.854 2.432   70.362 1.00 57.47  ? 411 HIS   A N     1 
ATOM   3303 C CA    . HIS   A 1 421 ? 30.842 1.469   69.955 1.00 55.44  ? 411 HIS   A CA    1 
ATOM   3304 C C     . HIS   A 1 421 ? 31.393 0.501   68.906 1.00 54.47  ? 411 HIS   A C     1 
ATOM   3305 O O     . HIS   A 1 421 ? 30.653 0.048   68.034 1.00 52.26  ? 411 HIS   A O     1 
ATOM   3306 C CB    . HIS   A 1 421 ? 29.616 2.207   69.406 1.00 57.14  ? 411 HIS   A CB    1 
ATOM   3307 C CG    . HIS   A 1 421 ? 28.900 3.047   70.411 1.00 59.02  ? 411 HIS   A CG    1 
ATOM   3308 N ND1   . HIS   A 1 421 ? 28.364 2.539   71.577 1.00 58.47  ? 411 HIS   A ND1   1 
ATOM   3309 C CD2   . HIS   A 1 421 ? 28.593 4.352   70.396 1.00 59.58  ? 411 HIS   A CD2   1 
ATOM   3310 C CE1   . HIS   A 1 421 ? 27.777 3.519   72.247 1.00 59.89  ? 411 HIS   A CE1   1 
ATOM   3311 N NE2   . HIS   A 1 421 ? 27.909 4.630   71.551 1.00 60.14  ? 411 HIS   A NE2   1 
ATOM   3312 N N     . THR   A 1 422 ? 32.689 0.173   68.994 1.00 53.07  ? 412 THR   A N     1 
ATOM   3313 C CA    . THR   A 1 422 ? 33.297 -0.756  68.057 1.00 53.81  ? 412 THR   A CA    1 
ATOM   3314 C C     . THR   A 1 422 ? 33.744 -2.008  68.808 1.00 54.63  ? 412 THR   A C     1 
ATOM   3315 O O     . THR   A 1 422 ? 33.960 -1.968  70.015 1.00 54.59  ? 412 THR   A O     1 
ATOM   3316 C CB    . THR   A 1 422 ? 34.471 -0.099  67.330 1.00 54.53  ? 412 THR   A CB    1 
ATOM   3317 O OG1   . THR   A 1 422 ? 35.519 0.107   68.275 1.00 54.99  ? 412 THR   A OG1   1 
ATOM   3318 C CG2   . THR   A 1 422 ? 34.099 1.215   66.669 1.00 54.44  ? 412 THR   A CG2   1 
ATOM   3319 N N     . THR   A 1 423 ? 33.880 -3.119  68.078 1.00 55.83  ? 413 THR   A N     1 
ATOM   3320 C CA    . THR   A 1 423 ? 34.541 -4.301  68.608 1.00 57.36  ? 413 THR   A CA    1 
ATOM   3321 C C     . THR   A 1 423 ? 35.610 -4.735  67.611 1.00 56.14  ? 413 THR   A C     1 
ATOM   3322 O O     . THR   A 1 423 ? 35.402 -4.670  66.404 1.00 54.70  ? 413 THR   A O     1 
ATOM   3323 C CB    . THR   A 1 423 ? 33.525 -5.405  68.910 1.00 58.70  ? 413 THR   A CB    1 
ATOM   3324 O OG1   . THR   A 1 423 ? 32.897 -5.773  67.687 1.00 61.08  ? 413 THR   A OG1   1 
ATOM   3325 C CG2   . THR   A 1 423 ? 32.453 -4.957  69.889 1.00 58.86  ? 413 THR   A CG2   1 
ATOM   3326 N N     . ILE   A 1 424 ? 36.764 -5.150  68.135 1.00 57.62  ? 414 ILE   A N     1 
ATOM   3327 C CA    . ILE   A 1 424 ? 37.888 -5.554  67.307 1.00 58.69  ? 414 ILE   A CA    1 
ATOM   3328 C C     . ILE   A 1 424 ? 37.626 -6.955  66.761 1.00 58.66  ? 414 ILE   A C     1 
ATOM   3329 O O     . ILE   A 1 424 ? 37.315 -7.869  67.518 1.00 58.28  ? 414 ILE   A O     1 
ATOM   3330 C CB    . ILE   A 1 424 ? 39.202 -5.482  68.107 1.00 60.11  ? 414 ILE   A CB    1 
ATOM   3331 C CG1   . ILE   A 1 424 ? 39.473 -4.053  68.594 1.00 60.21  ? 414 ILE   A CG1   1 
ATOM   3332 C CG2   . ILE   A 1 424 ? 40.374 -6.039  67.294 1.00 61.16  ? 414 ILE   A CG2   1 
ATOM   3333 C CD1   . ILE   A 1 424 ? 40.767 -3.888  69.372 1.00 60.79  ? 414 ILE   A CD1   1 
ATOM   3334 N N     . VAL   A 1 425 ? 37.767 -7.106  65.440 1.00 59.83  ? 415 VAL   A N     1 
ATOM   3335 C CA    . VAL   A 1 425 ? 37.715 -8.408  64.796 1.00 61.21  ? 415 VAL   A CA    1 
ATOM   3336 C C     . VAL   A 1 425 ? 39.029 -9.133  65.064 1.00 62.39  ? 415 VAL   A C     1 
ATOM   3337 O O     . VAL   A 1 425 ? 40.095 -8.621  64.737 1.00 62.78  ? 415 VAL   A O     1 
ATOM   3338 C CB    . VAL   A 1 425 ? 37.460 -8.285  63.284 1.00 61.56  ? 415 VAL   A CB    1 
ATOM   3339 C CG1   . VAL   A 1 425 ? 37.490 -9.644  62.600 1.00 62.35  ? 415 VAL   A CG1   1 
ATOM   3340 C CG2   . VAL   A 1 425 ? 36.147 -7.572  62.997 1.00 62.63  ? 415 VAL   A CG2   1 
ATOM   3341 N N     . LYS   A 1 426 ? 38.935 -10.325 65.661 1.00 65.38  ? 416 LYS   A N     1 
ATOM   3342 C CA    . LYS   A 1 426 ? 40.105 -11.083 66.077 1.00 66.91  ? 416 LYS   A CA    1 
ATOM   3343 C C     . LYS   A 1 426 ? 40.413 -12.167 65.043 1.00 64.03  ? 416 LYS   A C     1 
ATOM   3344 O O     . LYS   A 1 426 ? 41.552 -12.616 64.946 1.00 64.15  ? 416 LYS   A O     1 
ATOM   3345 C CB    . LYS   A 1 426 ? 39.852 -11.591 67.501 1.00 71.17  ? 416 LYS   A CB    1 
ATOM   3346 C CG    . LYS   A 1 426 ? 39.632 -10.474 68.530 1.00 75.87  ? 416 LYS   A CG    1 
ATOM   3347 C CD    . LYS   A 1 426 ? 38.875 -10.864 69.799 1.00 79.29  ? 416 LYS   A CD    1 
ATOM   3348 C CE    . LYS   A 1 426 ? 39.735 -11.425 70.895 1.00 81.94  ? 416 LYS   A CE    1 
ATOM   3349 N NZ    . LYS   A 1 426 ? 40.391 -12.687 70.531 1.00 83.59  ? 416 LYS   A NZ    1 
ATOM   3350 N N     . HIS   A 1 427 ? 39.399 -12.573 64.269 1.00 61.86  ? 417 HIS   A N     1 
ATOM   3351 C CA    . HIS   A 1 427 ? 39.601 -13.475 63.147 1.00 62.61  ? 417 HIS   A CA    1 
ATOM   3352 C C     . HIS   A 1 427 ? 38.508 -13.250 62.107 1.00 62.39  ? 417 HIS   A C     1 
ATOM   3353 O O     . HIS   A 1 427 ? 37.375 -12.936 62.458 1.00 64.16  ? 417 HIS   A O     1 
ATOM   3354 C CB    . HIS   A 1 427 ? 39.615 -14.936 63.609 1.00 62.88  ? 417 HIS   A CB    1 
ATOM   3355 C CG    . HIS   A 1 427 ? 40.191 -15.860 62.584 1.00 64.18  ? 417 HIS   A CG    1 
ATOM   3356 N ND1   . HIS   A 1 427 ? 39.459 -16.389 61.541 1.00 63.33  ? 417 HIS   A ND1   1 
ATOM   3357 C CD2   . HIS   A 1 427 ? 41.442 -16.324 62.432 1.00 63.37  ? 417 HIS   A CD2   1 
ATOM   3358 C CE1   . HIS   A 1 427 ? 40.246 -17.157 60.801 1.00 63.98  ? 417 HIS   A CE1   1 
ATOM   3359 N NE2   . HIS   A 1 427 ? 41.455 -17.129 61.323 1.00 63.45  ? 417 HIS   A NE2   1 
ATOM   3360 N N     . TYR   A 1 428 ? 38.849 -13.452 60.830 1.00 60.31  ? 418 TYR   A N     1 
ATOM   3361 C CA    . TYR   A 1 428 ? 37.961 -13.105 59.731 1.00 61.43  ? 418 TYR   A CA    1 
ATOM   3362 C C     . TYR   A 1 428 ? 36.705 -13.977 59.734 1.00 60.81  ? 418 TYR   A C     1 
ATOM   3363 O O     . TYR   A 1 428 ? 35.667 -13.549 59.234 1.00 60.24  ? 418 TYR   A O     1 
ATOM   3364 C CB    . TYR   A 1 428 ? 38.698 -13.161 58.385 1.00 63.32  ? 418 TYR   A CB    1 
ATOM   3365 C CG    . TYR   A 1 428 ? 39.086 -14.527 57.827 1.00 64.70  ? 418 TYR   A CG    1 
ATOM   3366 C CD1   . TYR   A 1 428 ? 40.276 -15.150 58.194 1.00 66.18  ? 418 TYR   A CD1   1 
ATOM   3367 C CD2   . TYR   A 1 428 ? 38.290 -15.166 56.883 1.00 66.54  ? 418 TYR   A CD2   1 
ATOM   3368 C CE1   . TYR   A 1 428 ? 40.644 -16.378 57.666 1.00 66.79  ? 418 TYR   A CE1   1 
ATOM   3369 C CE2   . TYR   A 1 428 ? 38.648 -16.393 56.347 1.00 68.34  ? 418 TYR   A CE2   1 
ATOM   3370 C CZ    . TYR   A 1 428 ? 39.827 -17.001 56.740 1.00 67.17  ? 418 TYR   A CZ    1 
ATOM   3371 O OH    . TYR   A 1 428 ? 40.167 -18.211 56.211 1.00 67.86  ? 418 TYR   A OH    1 
ATOM   3372 N N     . ARG   A 1 429 ? 36.789 -15.190 60.295 1.00 62.76  ? 419 ARG   A N     1 
ATOM   3373 C CA    . ARG   A 1 429 ? 35.652 -16.100 60.321 1.00 65.58  ? 419 ARG   A CA    1 
ATOM   3374 C C     . ARG   A 1 429 ? 34.640 -15.667 61.385 1.00 65.27  ? 419 ARG   A C     1 
ATOM   3375 O O     . ARG   A 1 429 ? 33.537 -16.201 61.430 1.00 67.17  ? 419 ARG   A O     1 
ATOM   3376 C CB    . ARG   A 1 429 ? 36.083 -17.557 60.533 1.00 67.93  ? 419 ARG   A CB    1 
ATOM   3377 C CG    . ARG   A 1 429 ? 36.969 -18.123 59.431 1.00 70.79  ? 419 ARG   A CG    1 
ATOM   3378 C CD    . ARG   A 1 429 ? 37.191 -19.627 59.563 1.00 72.01  ? 419 ARG   A CD    1 
ATOM   3379 N NE    . ARG   A 1 429 ? 36.045 -20.406 59.075 1.00 74.44  ? 419 ARG   A NE    1 
ATOM   3380 C CZ    . ARG   A 1 429 ? 35.936 -21.736 59.087 1.00 74.94  ? 419 ARG   A CZ    1 
ATOM   3381 N NH1   . ARG   A 1 429 ? 36.875 -22.489 59.633 1.00 75.51  ? 419 ARG   A NH1   1 
ATOM   3382 N NH2   . ARG   A 1 429 ? 34.871 -22.316 58.565 1.00 75.22  ? 419 ARG   A NH2   1 
ATOM   3383 N N     . ASP   A 1 430 ? 35.006 -14.695 62.230 1.00 64.06  ? 420 ASP   A N     1 
ATOM   3384 C CA    . ASP   A 1 430 ? 34.057 -14.070 63.136 1.00 63.11  ? 420 ASP   A CA    1 
ATOM   3385 C C     . ASP   A 1 430 ? 33.083 -13.181 62.365 1.00 62.56  ? 420 ASP   A C     1 
ATOM   3386 O O     . ASP   A 1 430 ? 32.037 -12.820 62.898 1.00 63.80  ? 420 ASP   A O     1 
ATOM   3387 C CB    . ASP   A 1 430 ? 34.762 -13.280 64.226 1.00 63.76  ? 420 ASP   A CB    1 
ATOM   3388 C CG    . ASP   A 1 430 ? 35.681 -14.102 65.115 1.00 65.19  ? 420 ASP   A CG    1 
ATOM   3389 O OD1   . ASP   A 1 430 ? 35.530 -15.345 65.108 1.00 66.78  ? 420 ASP   A OD1   1 
ATOM   3390 O OD2   . ASP   A 1 430 ? 36.554 -13.497 65.778 1.00 63.63  ? 420 ASP   A OD2   1 
ATOM   3391 N N     . LEU   A 1 431 ? 33.442 -12.797 61.133 1.00 61.73  ? 421 LEU   A N     1 
ATOM   3392 C CA    . LEU   A 1 431 ? 32.496 -12.169 60.222 1.00 61.92  ? 421 LEU   A CA    1 
ATOM   3393 C C     . LEU   A 1 431 ? 31.700 -13.267 59.522 1.00 61.85  ? 421 LEU   A C     1 
ATOM   3394 O O     . LEU   A 1 431 ? 32.257 -14.295 59.144 1.00 64.10  ? 421 LEU   A O     1 
ATOM   3395 C CB    . LEU   A 1 431 ? 33.215 -11.284 59.204 1.00 62.81  ? 421 LEU   A CB    1 
ATOM   3396 C CG    . LEU   A 1 431 ? 34.073 -10.148 59.764 1.00 62.24  ? 421 LEU   A CG    1 
ATOM   3397 C CD1   . LEU   A 1 431 ? 34.847 -9.487  58.638 1.00 62.86  ? 421 LEU   A CD1   1 
ATOM   3398 C CD2   . LEU   A 1 431 ? 33.231 -9.125  60.500 1.00 61.85  ? 421 LEU   A CD2   1 
ATOM   3399 N N     . GLN   A 1 432 ? 30.396 -13.035 59.341 1.00 61.48  ? 422 GLN   A N     1 
ATOM   3400 C CA    . GLN   A 1 432 ? 29.528 -13.998 58.686 1.00 61.05  ? 422 GLN   A CA    1 
ATOM   3401 C C     . GLN   A 1 432 ? 29.943 -14.192 57.230 1.00 61.33  ? 422 GLN   A C     1 
ATOM   3402 O O     . GLN   A 1 432 ? 30.393 -13.259 56.574 1.00 61.81  ? 422 GLN   A O     1 
ATOM   3403 C CB    . GLN   A 1 432 ? 28.080 -13.518 58.695 1.00 60.95  ? 422 GLN   A CB    1 
ATOM   3404 C CG    . GLN   A 1 432 ? 27.392 -13.630 60.047 1.00 60.82  ? 422 GLN   A CG    1 
ATOM   3405 C CD    . GLN   A 1 432 ? 25.925 -13.269 59.972 1.00 61.24  ? 422 GLN   A CD    1 
ATOM   3406 O OE1   . GLN   A 1 432 ? 25.487 -12.548 59.069 1.00 60.01  ? 422 GLN   A OE1   1 
ATOM   3407 N NE2   . GLN   A 1 432 ? 25.149 -13.762 60.924 1.00 61.46  ? 422 GLN   A NE2   1 
ATOM   3408 N N     . SER   A 1 433 ? 29.762 -15.419 56.736 1.00 62.87  ? 423 SER   A N     1 
ATOM   3409 C CA    . SER   A 1 433 ? 29.980 -15.740 55.337 1.00 62.74  ? 423 SER   A CA    1 
ATOM   3410 C C     . SER   A 1 433 ? 28.648 -15.652 54.600 1.00 63.21  ? 423 SER   A C     1 
ATOM   3411 O O     . SER   A 1 433 ? 27.601 -15.471 55.222 1.00 62.80  ? 423 SER   A O     1 
ATOM   3412 C CB    . SER   A 1 433 ? 30.600 -17.103 55.187 1.00 62.09  ? 423 SER   A CB    1 
ATOM   3413 O OG    . SER   A 1 433 ? 29.686 -18.107 55.600 1.00 62.50  ? 423 SER   A OG    1 
ATOM   3414 N N     . ILE   A 1 434 ? 28.704 -15.792 53.272 1.00 62.99  ? 424 ILE   A N     1 
ATOM   3415 C CA    . ILE   A 1 434 ? 27.525 -15.674 52.433 1.00 64.24  ? 424 ILE   A CA    1 
ATOM   3416 C C     . ILE   A 1 434 ? 26.467 -16.674 52.901 1.00 64.34  ? 424 ILE   A C     1 
ATOM   3417 O O     . ILE   A 1 434 ? 25.284 -16.337 52.940 1.00 64.98  ? 424 ILE   A O     1 
ATOM   3418 C CB    . ILE   A 1 434 ? 27.897 -15.849 50.948 1.00 65.86  ? 424 ILE   A CB    1 
ATOM   3419 C CG1   . ILE   A 1 434 ? 28.835 -14.727 50.476 1.00 66.07  ? 424 ILE   A CG1   1 
ATOM   3420 C CG2   . ILE   A 1 434 ? 26.646 -15.936 50.072 1.00 66.34  ? 424 ILE   A CG2   1 
ATOM   3421 C CD1   . ILE   A 1 434 ? 29.541 -15.006 49.162 1.00 65.44  ? 424 ILE   A CD1   1 
ATOM   3422 N N     . ALA   A 1 435 ? 26.917 -17.877 53.290 1.00 63.44  ? 425 ALA   A N     1 
ATOM   3423 C CA    . ALA   A 1 435 ? 26.050 -18.971 53.709 1.00 63.93  ? 425 ALA   A CA    1 
ATOM   3424 C C     . ALA   A 1 435 ? 25.076 -18.553 54.812 1.00 65.29  ? 425 ALA   A C     1 
ATOM   3425 O O     . ALA   A 1 435 ? 23.950 -19.043 54.850 1.00 66.69  ? 425 ALA   A O     1 
ATOM   3426 C CB    . ALA   A 1 435 ? 26.901 -20.140 54.161 1.00 63.84  ? 425 ALA   A CB    1 
ATOM   3427 N N     . ASP   A 1 436 ? 25.514 -17.655 55.706 1.00 65.23  ? 426 ASP   A N     1 
ATOM   3428 C CA    . ASP   A 1 436 ? 24.754 -17.286 56.891 1.00 64.50  ? 426 ASP   A CA    1 
ATOM   3429 C C     . ASP   A 1 436 ? 23.730 -16.187 56.604 1.00 64.09  ? 426 ASP   A C     1 
ATOM   3430 O O     . ASP   A 1 436 ? 22.927 -15.860 57.477 1.00 65.31  ? 426 ASP   A O     1 
ATOM   3431 C CB    . ASP   A 1 436 ? 25.672 -16.808 58.005 1.00 64.40  ? 426 ASP   A CB    1 
ATOM   3432 C CG    . ASP   A 1 436 ? 26.884 -17.691 58.263 1.00 63.93  ? 426 ASP   A CG    1 
ATOM   3433 O OD1   . ASP   A 1 436 ? 26.711 -18.925 58.273 1.00 65.32  ? 426 ASP   A OD1   1 
ATOM   3434 O OD2   . ASP   A 1 436 ? 27.984 -17.137 58.453 1.00 62.85  ? 426 ASP   A OD2   1 
ATOM   3435 N N     . TYR   A 1 437 ? 23.764 -15.600 55.402 1.00 63.32  ? 427 TYR   A N     1 
ATOM   3436 C CA    . TYR   A 1 437 ? 22.904 -14.468 55.090 1.00 62.59  ? 427 TYR   A CA    1 
ATOM   3437 C C     . TYR   A 1 437 ? 21.471 -14.955 54.874 1.00 61.84  ? 427 TYR   A C     1 
ATOM   3438 O O     . TYR   A 1 437 ? 21.249 -16.126 54.584 1.00 60.62  ? 427 TYR   A O     1 
ATOM   3439 C CB    . TYR   A 1 437 ? 23.442 -13.712 53.870 1.00 62.58  ? 427 TYR   A CB    1 
ATOM   3440 C CG    . TYR   A 1 437 ? 24.803 -13.035 54.015 1.00 62.00  ? 427 TYR   A CG    1 
ATOM   3441 C CD1   . TYR   A 1 437 ? 25.386 -12.799 55.257 1.00 61.53  ? 427 TYR   A CD1   1 
ATOM   3442 C CD2   . TYR   A 1 437 ? 25.496 -12.600 52.889 1.00 62.12  ? 427 TYR   A CD2   1 
ATOM   3443 C CE1   . TYR   A 1 437 ? 26.619 -12.174 55.370 1.00 61.13  ? 427 TYR   A CE1   1 
ATOM   3444 C CE2   . TYR   A 1 437 ? 26.730 -11.977 52.989 1.00 61.26  ? 427 TYR   A CE2   1 
ATOM   3445 C CZ    . TYR   A 1 437 ? 27.289 -11.757 54.234 1.00 60.84  ? 427 TYR   A CZ    1 
ATOM   3446 O OH    . TYR   A 1 437 ? 28.495 -11.128 54.323 1.00 62.16  ? 427 TYR   A OH    1 
ATOM   3447 N N     . PRO   A 1 438 ? 20.447 -14.079 55.015 1.00 64.05  ? 428 PRO   A N     1 
ATOM   3448 C CA    . PRO   A 1 438 ? 19.059 -14.467 54.746 1.00 66.62  ? 428 PRO   A CA    1 
ATOM   3449 C C     . PRO   A 1 438 ? 18.872 -14.990 53.322 1.00 69.98  ? 428 PRO   A C     1 
ATOM   3450 O O     . PRO   A 1 438 ? 19.583 -14.575 52.407 1.00 71.31  ? 428 PRO   A O     1 
ATOM   3451 C CB    . PRO   A 1 438 ? 18.247 -13.188 55.010 1.00 65.95  ? 428 PRO   A CB    1 
ATOM   3452 C CG    . PRO   A 1 438 ? 19.149 -12.338 55.878 1.00 65.08  ? 428 PRO   A CG    1 
ATOM   3453 C CD    . PRO   A 1 438 ? 20.566 -12.680 55.452 1.00 64.74  ? 428 PRO   A CD    1 
ATOM   3454 N N     . VAL   A 1 439 ? 17.884 -15.881 53.158 1.00 72.00  ? 429 VAL   A N     1 
ATOM   3455 C CA    . VAL   A 1 439 ? 17.775 -16.760 51.999 1.00 72.83  ? 429 VAL   A CA    1 
ATOM   3456 C C     . VAL   A 1 439 ? 17.728 -15.942 50.708 1.00 71.95  ? 429 VAL   A C     1 
ATOM   3457 O O     . VAL   A 1 439 ? 18.388 -16.300 49.734 1.00 74.07  ? 429 VAL   A O     1 
ATOM   3458 C CB    . VAL   A 1 439 ? 16.587 -17.748 52.086 1.00 73.46  ? 429 VAL   A CB    1 
ATOM   3459 C CG1   . VAL   A 1 439 ? 17.003 -19.102 52.654 1.00 72.54  ? 429 VAL   A CG1   1 
ATOM   3460 C CG2   . VAL   A 1 439 ? 15.399 -17.193 52.868 1.00 74.57  ? 429 VAL   A CG2   1 
ATOM   3461 N N     . LYS   A 1 440 ? 16.963 -14.844 50.703 1.00 71.05  ? 430 LYS   A N     1 
ATOM   3462 C CA    . LYS   A 1 440 ? 16.792 -14.037 49.503 1.00 71.09  ? 430 LYS   A CA    1 
ATOM   3463 C C     . LYS   A 1 440 ? 18.085 -13.309 49.143 1.00 71.91  ? 430 LYS   A C     1 
ATOM   3464 O O     . LYS   A 1 440 ? 18.438 -13.228 47.968 1.00 71.71  ? 430 LYS   A O     1 
ATOM   3465 C CB    . LYS   A 1 440 ? 15.636 -13.048 49.677 1.00 72.26  ? 430 LYS   A CB    1 
ATOM   3466 C CG    . LYS   A 1 440 ? 14.270 -13.709 49.703 1.00 73.95  ? 430 LYS   A CG    1 
ATOM   3467 C CD    . LYS   A 1 440 ? 13.111 -12.726 49.649 1.00 75.56  ? 430 LYS   A CD    1 
ATOM   3468 C CE    . LYS   A 1 440 ? 11.798 -13.422 49.525 1.00 77.25  ? 430 LYS   A CE    1 
ATOM   3469 N NZ    . LYS   A 1 440 ? 10.694 -12.460 49.507 1.00 79.19  ? 430 LYS   A NZ    1 
ATOM   3470 N N     . VAL   A 1 441 ? 18.780 -12.775 50.157 1.00 72.58  ? 431 VAL   A N     1 
ATOM   3471 C CA    . VAL   A 1 441 ? 20.032 -12.064 49.947 1.00 71.78  ? 431 VAL   A CA    1 
ATOM   3472 C C     . VAL   A 1 441 ? 21.084 -13.062 49.473 1.00 69.44  ? 431 VAL   A C     1 
ATOM   3473 O O     . VAL   A 1 441 ? 21.751 -12.831 48.470 1.00 68.27  ? 431 VAL   A O     1 
ATOM   3474 C CB    . VAL   A 1 441 ? 20.528 -11.329 51.208 1.00 74.39  ? 431 VAL   A CB    1 
ATOM   3475 C CG1   . VAL   A 1 441 ? 21.802 -10.540 50.936 1.00 73.49  ? 431 VAL   A CG1   1 
ATOM   3476 C CG2   . VAL   A 1 441 ? 19.463 -10.414 51.799 1.00 76.84  ? 431 VAL   A CG2   1 
ATOM   3477 N N     . ARG   A 1 442 ? 21.227 -14.154 50.233 1.00 69.04  ? 432 ARG   A N     1 
ATOM   3478 C CA    . ARG   A 1 442 ? 22.190 -15.206 49.953 1.00 70.58  ? 432 ARG   A CA    1 
ATOM   3479 C C     . ARG   A 1 442 ? 22.065 -15.665 48.500 1.00 71.58  ? 432 ARG   A C     1 
ATOM   3480 O O     . ARG   A 1 442 ? 23.056 -15.735 47.776 1.00 69.64  ? 432 ARG   A O     1 
ATOM   3481 C CB    . ARG   A 1 442 ? 21.929 -16.353 50.937 1.00 70.90  ? 432 ARG   A CB    1 
ATOM   3482 C CG    . ARG   A 1 442 ? 22.901 -17.521 50.849 1.00 72.06  ? 432 ARG   A CG    1 
ATOM   3483 C CD    . ARG   A 1 442 ? 22.288 -18.778 51.435 1.00 72.84  ? 432 ARG   A CD    1 
ATOM   3484 N NE    . ARG   A 1 442 ? 21.927 -18.619 52.846 1.00 73.92  ? 432 ARG   A NE    1 
ATOM   3485 C CZ    . ARG   A 1 442 ? 21.063 -19.381 53.513 1.00 76.55  ? 432 ARG   A CZ    1 
ATOM   3486 N NH1   . ARG   A 1 442 ? 20.326 -20.277 52.883 1.00 76.03  ? 432 ARG   A NH1   1 
ATOM   3487 N NH2   . ARG   A 1 442 ? 20.912 -19.222 54.816 1.00 79.62  ? 432 ARG   A NH2   1 
ATOM   3488 N N     . LYS   A 1 443 ? 20.833 -15.983 48.091 1.00 73.61  ? 433 LYS   A N     1 
ATOM   3489 C CA    . LYS   A 1 443 ? 20.549 -16.459 46.747 1.00 76.09  ? 433 LYS   A CA    1 
ATOM   3490 C C     . LYS   A 1 443 ? 20.987 -15.415 45.720 1.00 74.35  ? 433 LYS   A C     1 
ATOM   3491 O O     . LYS   A 1 443 ? 21.724 -15.728 44.787 1.00 74.71  ? 433 LYS   A O     1 
ATOM   3492 C CB    . LYS   A 1 443 ? 19.053 -16.788 46.655 1.00 79.30  ? 433 LYS   A CB    1 
ATOM   3493 C CG    . LYS   A 1 443 ? 18.520 -17.173 45.277 1.00 82.96  ? 433 LYS   A CG    1 
ATOM   3494 C CD    . LYS   A 1 443 ? 17.090 -17.704 45.298 1.00 86.12  ? 433 LYS   A CD    1 
ATOM   3495 C CE    . LYS   A 1 443 ? 16.083 -16.717 45.814 1.00 87.93  ? 433 LYS   A CE    1 
ATOM   3496 N NZ    . LYS   A 1 443 ? 14.736 -17.288 45.850 1.00 89.24  ? 433 LYS   A NZ    1 
ATOM   3497 N N     . LEU   A 1 444 ? 20.526 -14.173 45.904 1.00 71.12  ? 434 LEU   A N     1 
ATOM   3498 C CA    . LEU   A 1 444 ? 20.837 -13.095 44.982 1.00 70.72  ? 434 LEU   A CA    1 
ATOM   3499 C C     . LEU   A 1 444 ? 22.349 -12.968 44.819 1.00 70.80  ? 434 LEU   A C     1 
ATOM   3500 O O     . LEU   A 1 444 ? 22.836 -12.857 43.697 1.00 72.94  ? 434 LEU   A O     1 
ATOM   3501 C CB    . LEU   A 1 444 ? 20.219 -11.788 45.475 1.00 72.36  ? 434 LEU   A CB    1 
ATOM   3502 C CG    . LEU   A 1 444 ? 20.760 -10.505 44.834 1.00 74.29  ? 434 LEU   A CG    1 
ATOM   3503 C CD1   . LEU   A 1 444 ? 20.520 -10.470 43.333 1.00 74.60  ? 434 LEU   A CD1   1 
ATOM   3504 C CD2   . LEU   A 1 444 ? 20.143 -9.293  45.505 1.00 75.67  ? 434 LEU   A CD2   1 
ATOM   3505 N N     . ILE   A 1 445 ? 23.079 -12.975 45.942 1.00 68.87  ? 435 ILE   A N     1 
ATOM   3506 C CA    . ILE   A 1 445 ? 24.506 -12.692 45.936 1.00 68.48  ? 435 ILE   A CA    1 
ATOM   3507 C C     . ILE   A 1 445 ? 25.259 -13.836 45.262 1.00 68.80  ? 435 ILE   A C     1 
ATOM   3508 O O     . ILE   A 1 445 ? 26.254 -13.597 44.586 1.00 69.28  ? 435 ILE   A O     1 
ATOM   3509 C CB    . ILE   A 1 445 ? 25.028 -12.401 47.358 1.00 67.32  ? 435 ILE   A CB    1 
ATOM   3510 C CG1   . ILE   A 1 445 ? 24.540 -11.026 47.834 1.00 67.39  ? 435 ILE   A CG1   1 
ATOM   3511 C CG2   . ILE   A 1 445 ? 26.554 -12.519 47.430 1.00 66.08  ? 435 ILE   A CG2   1 
ATOM   3512 C CD1   . ILE   A 1 445 ? 24.968 -10.645 49.240 1.00 66.78  ? 435 ILE   A CD1   1 
ATOM   3513 N N     . ARG   A 1 446 ? 24.782 -15.070 45.450 1.00 69.16  ? 436 ARG   A N     1 
ATOM   3514 C CA    . ARG   A 1 446 ? 25.440 -16.233 44.877 1.00 69.33  ? 436 ARG   A CA    1 
ATOM   3515 C C     . ARG   A 1 446 ? 25.359 -16.183 43.355 1.00 69.85  ? 436 ARG   A C     1 
ATOM   3516 O O     . ARG   A 1 446 ? 26.335 -16.509 42.683 1.00 70.11  ? 436 ARG   A O     1 
ATOM   3517 C CB    . ARG   A 1 446 ? 24.849 -17.534 45.429 1.00 69.33  ? 436 ARG   A CB    1 
ATOM   3518 C CG    . ARG   A 1 446 ? 25.493 -17.920 46.751 1.00 68.51  ? 436 ARG   A CG    1 
ATOM   3519 C CD    . ARG   A 1 446 ? 24.790 -19.075 47.419 1.00 67.87  ? 436 ARG   A CD    1 
ATOM   3520 N NE    . ARG   A 1 446 ? 25.559 -19.532 48.581 1.00 67.96  ? 436 ARG   A NE    1 
ATOM   3521 C CZ    . ARG   A 1 446 ? 25.117 -20.379 49.503 1.00 66.17  ? 436 ARG   A CZ    1 
ATOM   3522 N NH1   . ARG   A 1 446 ? 23.897 -20.880 49.414 1.00 67.11  ? 436 ARG   A NH1   1 
ATOM   3523 N NH2   . ARG   A 1 446 ? 25.900 -20.722 50.511 1.00 64.37  ? 436 ARG   A NH2   1 
ATOM   3524 N N     . ARG   A 1 447 ? 24.194 -15.772 42.837 1.00 71.92  ? 437 ARG   A N     1 
ATOM   3525 C CA    . ARG   A 1 447 ? 23.960 -15.657 41.405 1.00 74.18  ? 437 ARG   A CA    1 
ATOM   3526 C C     . ARG   A 1 447 ? 24.852 -14.575 40.795 1.00 75.17  ? 437 ARG   A C     1 
ATOM   3527 O O     . ARG   A 1 447 ? 25.389 -14.762 39.708 1.00 76.65  ? 437 ARG   A O     1 
ATOM   3528 C CB    . ARG   A 1 447 ? 22.486 -15.343 41.129 1.00 75.42  ? 437 ARG   A CB    1 
ATOM   3529 C CG    . ARG   A 1 447 ? 21.543 -16.481 41.488 1.00 77.58  ? 437 ARG   A CG    1 
ATOM   3530 C CD    . ARG   A 1 447 ? 20.080 -16.094 41.328 1.00 79.33  ? 437 ARG   A CD    1 
ATOM   3531 N NE    . ARG   A 1 447 ? 19.199 -17.225 41.644 1.00 82.31  ? 437 ARG   A NE    1 
ATOM   3532 C CZ    . ARG   A 1 447 ? 17.869 -17.205 41.630 1.00 83.22  ? 437 ARG   A CZ    1 
ATOM   3533 N NH1   . ARG   A 1 447 ? 17.212 -16.103 41.311 1.00 84.20  ? 437 ARG   A NH1   1 
ATOM   3534 N NH2   . ARG   A 1 447 ? 17.194 -18.298 41.937 1.00 83.23  ? 437 ARG   A NH2   1 
ATOM   3535 N N     . LEU   A 1 448 ? 25.003 -13.445 41.495 1.00 75.15  ? 438 LEU   A N     1 
ATOM   3536 C CA    . LEU   A 1 448 ? 25.851 -12.359 41.031 1.00 75.84  ? 438 LEU   A CA    1 
ATOM   3537 C C     . LEU   A 1 448 ? 27.310 -12.812 40.962 1.00 76.84  ? 438 LEU   A C     1 
ATOM   3538 O O     . LEU   A 1 448 ? 28.054 -12.343 40.105 1.00 79.79  ? 438 LEU   A O     1 
ATOM   3539 C CB    . LEU   A 1 448 ? 25.699 -11.136 41.935 1.00 76.85  ? 438 LEU   A CB    1 
ATOM   3540 C CG    . LEU   A 1 448 ? 24.371 -10.376 41.842 1.00 76.63  ? 438 LEU   A CG    1 
ATOM   3541 C CD1   . LEU   A 1 448 ? 24.284 -9.352  42.957 1.00 77.04  ? 438 LEU   A CD1   1 
ATOM   3542 C CD2   . LEU   A 1 448 ? 24.197 -9.694  40.497 1.00 77.01  ? 438 LEU   A CD2   1 
ATOM   3543 N N     . ARG   A 1 449 ? 27.722 -13.710 41.864 1.00 75.86  ? 439 ARG   A N     1 
ATOM   3544 C CA    . ARG   A 1 449 ? 29.112 -14.138 41.929 1.00 75.85  ? 439 ARG   A CA    1 
ATOM   3545 C C     . ARG   A 1 449 ? 29.380 -15.230 40.896 1.00 77.68  ? 439 ARG   A C     1 
ATOM   3546 O O     . ARG   A 1 449 ? 30.499 -15.330 40.396 1.00 76.71  ? 439 ARG   A O     1 
ATOM   3547 C CB    . ARG   A 1 449 ? 29.485 -14.598 43.343 1.00 75.36  ? 439 ARG   A CB    1 
ATOM   3548 C CG    . ARG   A 1 449 ? 29.294 -13.517 44.398 1.00 74.29  ? 439 ARG   A CG    1 
ATOM   3549 C CD    . ARG   A 1 449 ? 29.596 -13.993 45.807 1.00 73.33  ? 439 ARG   A CD    1 
ATOM   3550 N NE    . ARG   A 1 449 ? 30.997 -13.725 46.150 1.00 72.54  ? 439 ARG   A NE    1 
ATOM   3551 C CZ    . ARG   A 1 449 ? 31.903 -14.592 46.578 1.00 71.78  ? 439 ARG   A CZ    1 
ATOM   3552 N NH1   . ARG   A 1 449 ? 31.600 -15.864 46.757 1.00 72.42  ? 439 ARG   A NH1   1 
ATOM   3553 N NH2   . ARG   A 1 449 ? 33.128 -14.174 46.842 1.00 73.15  ? 439 ARG   A NH2   1 
ATOM   3554 N N     . ARG   A 1 450 ? 28.358 -16.046 40.595 1.00 82.14  ? 440 ARG   A N     1 
ATOM   3555 C CA    . ARG   A 1 450 ? 28.452 -17.049 39.543 1.00 84.95  ? 440 ARG   A CA    1 
ATOM   3556 C C     . ARG   A 1 450 ? 28.813 -16.371 38.224 1.00 83.42  ? 440 ARG   A C     1 
ATOM   3557 O O     . ARG   A 1 450 ? 29.771 -16.779 37.571 1.00 82.11  ? 440 ARG   A O     1 
ATOM   3558 C CB    . ARG   A 1 450 ? 27.157 -17.853 39.368 1.00 88.72  ? 440 ARG   A CB    1 
ATOM   3559 C CG    . ARG   A 1 450 ? 26.988 -19.014 40.338 1.00 93.02  ? 440 ARG   A CG    1 
ATOM   3560 C CD    . ARG   A 1 450 ? 25.557 -19.538 40.355 1.00 95.88  ? 440 ARG   A CD    1 
ATOM   3561 N NE    . ARG   A 1 450 ? 25.285 -20.397 41.515 1.00 98.83  ? 440 ARG   A NE    1 
ATOM   3562 C CZ    . ARG   A 1 450 ? 24.075 -20.663 42.010 1.00 99.57  ? 440 ARG   A CZ    1 
ATOM   3563 N NH1   . ARG   A 1 450 ? 23.000 -20.088 41.497 1.00 98.96  ? 440 ARG   A NH1   1 
ATOM   3564 N NH2   . ARG   A 1 450 ? 23.941 -21.493 43.031 1.00 99.85  ? 440 ARG   A NH2   1 
ATOM   3565 N N     . ILE   A 1 451 ? 28.066 -15.317 37.866 1.00 82.27  ? 441 ILE   A N     1 
ATOM   3566 C CA    . ILE   A 1 451 ? 28.233 -14.645 36.585 1.00 84.51  ? 441 ILE   A CA    1 
ATOM   3567 C C     . ILE   A 1 451 ? 29.049 -13.355 36.741 1.00 86.26  ? 441 ILE   A C     1 
ATOM   3568 O O     . ILE   A 1 451 ? 28.980 -12.476 35.885 1.00 86.57  ? 441 ILE   A O     1 
ATOM   3569 C CB    . ILE   A 1 451 ? 26.861 -14.410 35.918 1.00 83.55  ? 441 ILE   A CB    1 
ATOM   3570 C CG1   . ILE   A 1 451 ? 25.931 -13.546 36.767 1.00 82.80  ? 441 ILE   A CG1   1 
ATOM   3571 C CG2   . ILE   A 1 451 ? 26.204 -15.745 35.569 1.00 83.66  ? 441 ILE   A CG2   1 
ATOM   3572 C CD1   . ILE   A 1 451 ? 24.666 -13.110 36.049 1.00 82.60  ? 441 ILE   A CD1   1 
ATOM   3573 N N     . ARG   A 1 452 ? 29.832 -13.254 37.828 1.00 87.79  ? 442 ARG   A N     1 
ATOM   3574 C CA    . ARG   A 1 452 ? 30.852 -12.227 38.014 1.00 87.67  ? 442 ARG   A CA    1 
ATOM   3575 C C     . ARG   A 1 452 ? 30.297 -10.801 37.918 1.00 84.86  ? 442 ARG   A C     1 
ATOM   3576 O O     . ARG   A 1 452 ? 31.052 -9.879  37.622 1.00 83.11  ? 442 ARG   A O     1 
ATOM   3577 C CB    . ARG   A 1 452 ? 32.007 -12.402 37.017 1.00 90.81  ? 442 ARG   A CB    1 
ATOM   3578 C CG    . ARG   A 1 452 ? 33.149 -13.316 37.443 1.00 93.76  ? 442 ARG   A CG    1 
ATOM   3579 C CD    . ARG   A 1 452 ? 32.799 -14.800 37.431 1.00 98.12  ? 442 ARG   A CD    1 
ATOM   3580 N NE    . ARG   A 1 452 ? 33.974 -15.637 37.147 1.00 103.12 ? 442 ARG   A NE    1 
ATOM   3581 C CZ    . ARG   A 1 452 ? 33.990 -16.968 37.045 1.00 104.42 ? 442 ARG   A CZ    1 
ATOM   3582 N NH1   . ARG   A 1 452 ? 32.913 -17.680 37.331 1.00 104.34 ? 442 ARG   A NH1   1 
ATOM   3583 N NH2   . ARG   A 1 452 ? 35.098 -17.589 36.676 1.00 104.07 ? 442 ARG   A NH2   1 
ATOM   3584 N N     . ILE   A 1 453 ? 29.005 -10.600 38.215 1.00 84.24  ? 443 ILE   A N     1 
ATOM   3585 C CA    . ILE   A 1 453 ? 28.401 -9.276  38.149 1.00 84.67  ? 443 ILE   A CA    1 
ATOM   3586 C C     . ILE   A 1 453 ? 28.818 -8.464  39.377 1.00 83.84  ? 443 ILE   A C     1 
ATOM   3587 O O     . ILE   A 1 453 ? 28.839 -7.236  39.330 1.00 82.11  ? 443 ILE   A O     1 
ATOM   3588 C CB    . ILE   A 1 453 ? 26.867 -9.362  38.006 1.00 86.96  ? 443 ILE   A CB    1 
ATOM   3589 C CG1   . ILE   A 1 453 ? 26.446 -10.054 36.700 1.00 87.72  ? 443 ILE   A CG1   1 
ATOM   3590 C CG2   . ILE   A 1 453 ? 26.222 -7.980  38.128 1.00 87.70  ? 443 ILE   A CG2   1 
ATOM   3591 C CD1   . ILE   A 1 453 ? 26.547 -9.185  35.458 1.00 86.71  ? 443 ILE   A CD1   1 
ATOM   3592 N N     . ASP   A 1 454 ? 29.155 -9.155  40.474 1.00 84.10  ? 444 ASP   A N     1 
ATOM   3593 C CA    . ASP   A 1 454 ? 29.594 -8.506  41.700 1.00 82.90  ? 444 ASP   A CA    1 
ATOM   3594 C C     . ASP   A 1 454 ? 30.890 -7.728  41.458 1.00 82.84  ? 444 ASP   A C     1 
ATOM   3595 O O     . ASP   A 1 454 ? 31.105 -6.679  42.058 1.00 82.65  ? 444 ASP   A O     1 
ATOM   3596 C CB    . ASP   A 1 454 ? 29.754 -9.513  42.828 1.00 80.40  ? 444 ASP   A CB    1 
ATOM   3597 C CG    . ASP   A 1 454 ? 30.897 -10.498 42.643 1.00 79.77  ? 444 ASP   A CG    1 
ATOM   3598 O OD1   . ASP   A 1 454 ? 30.928 -11.159 41.588 1.00 82.03  ? 444 ASP   A OD1   1 
ATOM   3599 O OD2   . ASP   A 1 454 ? 31.749 -10.589 43.548 1.00 78.64  ? 444 ASP   A OD2   1 
ATOM   3600 N N     . ARG   A 1 455 ? 31.752 -8.256  40.582 1.00 84.49  ? 445 ARG   A N     1 
ATOM   3601 C CA    . ARG   A 1 455 ? 33.010 -7.610  40.235 1.00 85.55  ? 445 ARG   A CA    1 
ATOM   3602 C C     . ARG   A 1 455 ? 32.736 -6.308  39.478 1.00 82.16  ? 445 ARG   A C     1 
ATOM   3603 O O     . ARG   A 1 455 ? 33.479 -5.340  39.613 1.00 80.19  ? 445 ARG   A O     1 
ATOM   3604 C CB    . ARG   A 1 455 ? 33.860 -8.570  39.392 1.00 90.72  ? 445 ARG   A CB    1 
ATOM   3605 C CG    . ARG   A 1 455 ? 34.212 -9.906  40.037 1.00 93.98  ? 445 ARG   A CG    1 
ATOM   3606 C CD    . ARG   A 1 455 ? 35.532 -9.894  40.801 1.00 98.13  ? 445 ARG   A CD    1 
ATOM   3607 N NE    . ARG   A 1 455 ? 35.761 -11.150 41.528 1.00 101.87 ? 445 ARG   A NE    1 
ATOM   3608 C CZ    . ARG   A 1 455 ? 35.210 -11.511 42.692 1.00 102.79 ? 445 ARG   A CZ    1 
ATOM   3609 N NH1   . ARG   A 1 455 ? 34.490 -10.653 43.396 1.00 102.25 ? 445 ARG   A NH1   1 
ATOM   3610 N NH2   . ARG   A 1 455 ? 35.407 -12.730 43.169 1.00 101.32 ? 445 ARG   A NH2   1 
ATOM   3611 N N     . LEU   A 1 456 ? 31.656 -6.297  38.687 1.00 80.40  ? 446 LEU   A N     1 
ATOM   3612 C CA    . LEU   A 1 456 ? 31.279 -5.146  37.879 1.00 81.66  ? 446 LEU   A CA    1 
ATOM   3613 C C     . LEU   A 1 456 ? 30.676 -4.057  38.767 1.00 81.06  ? 446 LEU   A C     1 
ATOM   3614 O O     . LEU   A 1 456 ? 31.097 -2.904  38.708 1.00 83.35  ? 446 LEU   A O     1 
ATOM   3615 C CB    . LEU   A 1 456 ? 30.281 -5.581  36.805 1.00 82.98  ? 446 LEU   A CB    1 
ATOM   3616 C CG    . LEU   A 1 456 ? 30.294 -4.779  35.500 1.00 82.99  ? 446 LEU   A CG    1 
ATOM   3617 C CD1   . LEU   A 1 456 ? 31.184 -5.479  34.477 1.00 83.42  ? 446 LEU   A CD1   1 
ATOM   3618 C CD2   . LEU   A 1 456 ? 28.892 -4.556  34.952 1.00 81.93  ? 446 LEU   A CD2   1 
ATOM   3619 N N     . ILE   A 1 457 ? 29.673 -4.439  39.572 1.00 78.49  ? 447 ILE   A N     1 
ATOM   3620 C CA    . ILE   A 1 457 ? 28.933 -3.513  40.416 1.00 76.24  ? 447 ILE   A CA    1 
ATOM   3621 C C     . ILE   A 1 457 ? 29.887 -2.827  41.394 1.00 73.07  ? 447 ILE   A C     1 
ATOM   3622 O O     . ILE   A 1 457 ? 29.706 -1.657  41.718 1.00 70.51  ? 447 ILE   A O     1 
ATOM   3623 C CB    . ILE   A 1 457 ? 27.778 -4.233  41.142 1.00 78.22  ? 447 ILE   A CB    1 
ATOM   3624 C CG1   . ILE   A 1 457 ? 26.793 -3.245  41.763 1.00 81.36  ? 447 ILE   A CG1   1 
ATOM   3625 C CG2   . ILE   A 1 457 ? 28.298 -5.222  42.183 1.00 78.78  ? 447 ILE   A CG2   1 
ATOM   3626 C CD1   . ILE   A 1 457 ? 25.702 -3.896  42.595 1.00 82.89  ? 447 ILE   A CD1   1 
ATOM   3627 N N     . SER   A 1 458 ? 30.917 -3.559  41.835 1.00 73.01  ? 448 SER   A N     1 
ATOM   3628 C CA    . SER   A 1 458 ? 31.928 -3.049  42.749 1.00 72.36  ? 448 SER   A CA    1 
ATOM   3629 C C     . SER   A 1 458 ? 32.410 -1.651  42.352 1.00 73.44  ? 448 SER   A C     1 
ATOM   3630 O O     . SER   A 1 458 ? 32.739 -0.849  43.224 1.00 73.00  ? 448 SER   A O     1 
ATOM   3631 C CB    . SER   A 1 458 ? 33.080 -4.019  42.834 1.00 70.77  ? 448 SER   A CB    1 
ATOM   3632 O OG    . SER   A 1 458 ? 34.022 -3.624  43.820 1.00 71.56  ? 448 SER   A OG    1 
ATOM   3633 N N     . ARG   A 1 459 ? 32.447 -1.362  41.042 1.00 74.34  ? 449 ARG   A N     1 
ATOM   3634 C CA    . ARG   A 1 459 ? 33.015 -0.126  40.519 1.00 74.37  ? 449 ARG   A CA    1 
ATOM   3635 C C     . ARG   A 1 459 ? 32.141 1.092   40.825 1.00 69.88  ? 449 ARG   A C     1 
ATOM   3636 O O     . ARG   A 1 459 ? 32.642 2.210   40.782 1.00 67.26  ? 449 ARG   A O     1 
ATOM   3637 C CB    . ARG   A 1 459 ? 33.216 -0.200  39.002 1.00 79.19  ? 449 ARG   A CB    1 
ATOM   3638 C CG    . ARG   A 1 459 ? 34.171 -1.287  38.532 1.00 84.70  ? 449 ARG   A CG    1 
ATOM   3639 C CD    . ARG   A 1 459 ? 34.329 -1.259  37.021 1.00 89.93  ? 449 ARG   A CD    1 
ATOM   3640 N NE    . ARG   A 1 459 ? 35.179 -2.349  36.528 1.00 96.29  ? 449 ARG   A NE    1 
ATOM   3641 C CZ    . ARG   A 1 459 ? 35.476 -2.582  35.249 1.00 101.03 ? 449 ARG   A CZ    1 
ATOM   3642 N NH1   . ARG   A 1 459 ? 34.989 -1.807  34.292 1.00 101.34 ? 449 ARG   A NH1   1 
ATOM   3643 N NH2   . ARG   A 1 459 ? 36.262 -3.599  34.928 1.00 102.52 ? 449 ARG   A NH2   1 
ATOM   3644 N N     . ILE   A 1 460 ? 30.845 0.888   41.106 1.00 68.72  ? 450 ILE   A N     1 
ATOM   3645 C CA    . ILE   A 1 460 ? 29.968 1.981   41.507 1.00 69.57  ? 450 ILE   A CA    1 
ATOM   3646 C C     . ILE   A 1 460 ? 29.674 1.937   43.012 1.00 69.68  ? 450 ILE   A C     1 
ATOM   3647 O O     . ILE   A 1 460 ? 28.756 2.619   43.473 1.00 67.43  ? 450 ILE   A O     1 
ATOM   3648 C CB    . ILE   A 1 460 ? 28.665 1.976   40.686 1.00 70.02  ? 450 ILE   A CB    1 
ATOM   3649 C CG1   . ILE   A 1 460 ? 27.902 0.664   40.831 1.00 70.30  ? 450 ILE   A CG1   1 
ATOM   3650 C CG2   . ILE   A 1 460 ? 28.944 2.307   39.221 1.00 71.50  ? 450 ILE   A CG2   1 
ATOM   3651 C CD1   . ILE   A 1 460 ? 26.445 0.758   40.425 1.00 71.12  ? 450 ILE   A CD1   1 
ATOM   3652 N N     . LEU   A 1 461 ? 30.457 1.150   43.770 1.00 67.77  ? 451 LEU   A N     1 
ATOM   3653 C CA    . LEU   A 1 461 ? 30.289 1.009   45.211 1.00 66.24  ? 451 LEU   A CA    1 
ATOM   3654 C C     . LEU   A 1 461 ? 31.467 1.678   45.945 1.00 65.07  ? 451 LEU   A C     1 
ATOM   3655 O O     . LEU   A 1 461 ? 32.473 2.011   45.273 1.00 62.89  ? 451 LEU   A O     1 
ATOM   3656 C CB    . LEU   A 1 461 ? 30.186 -0.465  45.609 1.00 65.13  ? 451 LEU   A CB    1 
ATOM   3657 C CG    . LEU   A 1 461 ? 28.979 -1.248  45.084 1.00 63.72  ? 451 LEU   A CG    1 
ATOM   3658 C CD1   . LEU   A 1 461 ? 28.919 -2.604  45.770 1.00 62.74  ? 451 LEU   A CD1   1 
ATOM   3659 C CD2   . LEU   A 1 461 ? 27.669 -0.497  45.255 1.00 64.31  ? 451 LEU   A CD2   1 
ATOM   3660 O OXT   . LEU   A 1 461 ? 31.344 1.813   47.178 1.00 66.13  ? 451 LEU   A OXT   1 
HETATM 3661 O OCL   . A1LZV B 2 .   ? 25.008 8.647   46.541 1.00 69.46  ? 501 A1LZV A OCL   1 
HETATM 3662 C CBE   . A1LZV B 2 .   ? 25.741 7.969   45.864 1.00 71.54  ? 501 A1LZV A CBE   1 
HETATM 3663 C CBF   . A1LZV B 2 .   ? 25.333 7.213   44.624 1.00 75.35  ? 501 A1LZV A CBF   1 
HETATM 3664 C CBG   . A1LZV B 2 .   ? 23.862 6.930   44.535 1.00 79.21  ? 501 A1LZV A CBG   1 
HETATM 3665 C CBH   . A1LZV B 2 .   ? 23.469 6.310   43.200 1.00 84.52  ? 501 A1LZV A CBH   1 
HETATM 3666 C CBI   . A1LZV B 2 .   ? 22.023 5.875   43.111 1.00 88.80  ? 501 A1LZV A CBI   1 
HETATM 3667 C CBJ   . A1LZV B 2 .   ? 21.645 5.220   41.800 1.00 92.46  ? 501 A1LZV A CBJ   1 
HETATM 3668 C CBK   . A1LZV B 2 .   ? 20.155 5.189   41.528 1.00 96.00  ? 501 A1LZV A CBK   1 
HETATM 3669 C CBL   . A1LZV B 2 .   ? 19.746 4.358   40.332 1.00 99.47  ? 501 A1LZV A CBL   1 
HETATM 3670 C CBM   . A1LZV B 2 .   ? 19.929 2.862   40.510 1.00 103.42 ? 501 A1LZV A CBM   1 
HETATM 3671 C CBN   . A1LZV B 2 .   ? 18.819 1.865   40.787 1.00 106.44 ? 501 A1LZV A CBN   1 
HETATM 3672 C CBO   . A1LZV B 2 .   ? 18.933 0.372   40.518 1.00 108.24 ? 501 A1LZV A CBO   1 
HETATM 3673 C CBP   . A1LZV B 2 .   ? 18.274 -0.525  41.554 1.00 108.96 ? 501 A1LZV A CBP   1 
HETATM 3674 C CBQ   . A1LZV B 2 .   ? 16.945 -1.116  41.126 1.00 109.54 ? 501 A1LZV A CBQ   1 
HETATM 3675 C CBR   . A1LZV B 2 .   ? 16.244 -1.929  42.197 1.00 111.11 ? 501 A1LZV A CBR   1 
HETATM 3676 C CBS   . A1LZV B 2 .   ? 14.942 -1.333  42.700 1.00 110.43 ? 501 A1LZV A CBS   1 
HETATM 3677 C CBT   . A1LZV B 2 .   ? 14.325 -2.065  43.876 1.00 108.28 ? 501 A1LZV A CBT   1 
HETATM 3678 O OBD   . A1LZV B 2 .   ? 27.036 7.796   46.123 1.00 67.88  ? 501 A1LZV A OBD   1 
HETATM 3679 C CBC   . A1LZV B 2 .   ? 27.582 8.459   47.287 1.00 68.48  ? 501 A1LZV A CBC   1 
HETATM 3680 C CBA   . A1LZV B 2 .   ? 27.294 7.616   48.511 1.00 67.70  ? 501 A1LZV A CBA   1 
HETATM 3681 C CAZ   . A1LZV B 2 .   ? 27.959 8.120   49.768 1.00 68.48  ? 501 A1LZV A CAZ   1 
HETATM 3682 O OAY   . A1LZV B 2 .   ? 27.642 9.517   50.010 1.00 70.47  ? 501 A1LZV A OAY   1 
HETATM 3683 P PAV   . A1LZV B 2 .   ? 27.902 10.138  51.470 1.00 71.64  ? 501 A1LZV A PAV   1 
HETATM 3684 O OAW   . A1LZV B 2 .   ? 28.947 9.331   52.174 1.00 68.20  ? 501 A1LZV A OAW   1 
HETATM 3685 O OAX   . A1LZV B 2 .   ? 28.099 11.610  51.330 1.00 71.19  ? 501 A1LZV A OAX   1 
HETATM 3686 O OAU   . A1LZV B 2 .   ? 26.463 9.914   52.151 1.00 78.17  ? 501 A1LZV A OAU   1 
HETATM 3687 P PAR   . A1LZV B 2 .   ? 25.447 8.685   52.331 1.00 82.54  ? 501 A1LZV A PAR   1 
HETATM 3688 O OAS   . A1LZV B 2 .   ? 24.335 9.118   53.232 1.00 84.95  ? 501 A1LZV A OAS   1 
HETATM 3689 O OAT   . A1LZV B 2 .   ? 26.254 7.484   52.708 1.00 81.98  ? 501 A1LZV A OAT   1 
HETATM 3690 O "O5'" . A1LZV B 2 .   ? 24.864 8.499   50.845 1.00 85.02  ? 501 A1LZV A "O5'" 1 
HETATM 3691 C "C5'" . A1LZV B 2 .   ? 23.842 7.491   50.608 1.00 83.71  ? 501 A1LZV A "C5'" 1 
HETATM 3692 C "C4'" . A1LZV B 2 .   ? 22.926 7.952   49.499 1.00 82.38  ? 501 A1LZV A "C4'" 1 
HETATM 3693 C "C3'" . A1LZV B 2 .   ? 21.913 9.045   49.881 1.00 80.78  ? 501 A1LZV A "C3'" 1 
HETATM 3694 O "O3'" . A1LZV B 2 .   ? 21.627 9.892   48.775 1.00 76.74  ? 501 A1LZV A "O3'" 1 
HETATM 3695 C "C2'" . A1LZV B 2 .   ? 20.702 8.206   50.303 1.00 82.43  ? 501 A1LZV A "C2'" 1 
HETATM 3696 O "O2'" . A1LZV B 2 .   ? 19.469 8.895   50.264 1.00 81.07  ? 501 A1LZV A "O2'" 1 
HETATM 3697 O "O4'" . A1LZV B 2 .   ? 22.118 6.836   49.030 1.00 79.81  ? 501 A1LZV A "O4'" 1 
HETATM 3698 C "C1'" . A1LZV B 2 .   ? 20.752 7.145   49.201 1.00 81.63  ? 501 A1LZV A "C1'" 1 
HETATM 3699 N NAH   . A1LZV B 2 .   ? 19.997 5.904   49.528 1.00 80.12  ? 501 A1LZV A NAH   1 
HETATM 3700 C CAG   . A1LZV B 2 .   ? 20.294 5.160   50.633 1.00 80.46  ? 501 A1LZV A CAG   1 
HETATM 3701 C CAF   . A1LZV B 2 .   ? 19.612 4.039   50.921 1.00 80.98  ? 501 A1LZV A CAF   1 
HETATM 3702 C CAD   . A1LZV B 2 .   ? 18.568 3.649   50.032 1.00 81.46  ? 501 A1LZV A CAD   1 
HETATM 3703 N NAE   . A1LZV B 2 .   ? 17.857 2.552   50.249 1.00 80.91  ? 501 A1LZV A NAE   1 
HETATM 3704 N NAC   . A1LZV B 2 .   ? 18.274 4.378   48.947 1.00 83.22  ? 501 A1LZV A NAC   1 
HETATM 3705 C CAB   . A1LZV B 2 .   ? 18.967 5.510   48.667 1.00 81.30  ? 501 A1LZV A CAB   1 
HETATM 3706 O OAA   . A1LZV B 2 .   ? 18.712 6.206   47.671 1.00 81.76  ? 501 A1LZV A OAA   1 
HETATM 3707 O OBB   . A1LZV B 2 .   ? 27.785 6.265   48.283 1.00 66.56  ? 501 A1LZV A OBB   1 
HETATM 3708 C CBU   . A1LZV B 2 .   ? 26.914 5.248   48.350 1.00 67.23  ? 501 A1LZV A CBU   1 
HETATM 3709 O OCK   . A1LZV B 2 .   ? 25.759 5.422   48.623 1.00 67.72  ? 501 A1LZV A OCK   1 
HETATM 3710 C CBV   . A1LZV B 2 .   ? 27.523 3.910   48.027 1.00 68.97  ? 501 A1LZV A CBV   1 
HETATM 3711 C CBW   . A1LZV B 2 .   ? 26.574 2.970   47.338 1.00 71.05  ? 501 A1LZV A CBW   1 
HETATM 3712 C CBX   . A1LZV B 2 .   ? 26.210 3.423   45.934 1.00 72.87  ? 501 A1LZV A CBX   1 
HETATM 3713 C CBY   . A1LZV B 2 .   ? 25.037 2.691   45.315 1.00 75.16  ? 501 A1LZV A CBY   1 
HETATM 3714 C CBZ   . A1LZV B 2 .   ? 25.295 2.163   43.916 1.00 78.90  ? 501 A1LZV A CBZ   1 
HETATM 3715 C CCA   . A1LZV B 2 .   ? 24.121 2.279   42.966 1.00 81.73  ? 501 A1LZV A CCA   1 
HETATM 3716 C CCB   . A1LZV B 2 .   ? 22.912 1.463   43.345 1.00 84.85  ? 501 A1LZV A CCB   1 
HETATM 3717 C CCC   . A1LZV B 2 .   ? 23.149 -0.027  43.396 1.00 88.49  ? 501 A1LZV A CCC   1 
HETATM 3718 C CCD   . A1LZV B 2 .   ? 23.250 -0.938  42.200 1.00 90.79  ? 501 A1LZV A CCD   1 
HETATM 3719 C CCE   . A1LZV B 2 .   ? 22.079 -1.588  41.505 1.00 92.04  ? 501 A1LZV A CCE   1 
HETATM 3720 C CCF   . A1LZV B 2 .   ? 21.990 -3.083  41.701 1.00 91.59  ? 501 A1LZV A CCF   1 
HETATM 3721 C CCG   . A1LZV B 2 .   ? 21.319 -3.508  42.987 1.00 90.84  ? 501 A1LZV A CCG   1 
HETATM 3722 C CCH   . A1LZV B 2 .   ? 22.224 -4.232  43.957 1.00 88.62  ? 501 A1LZV A CCH   1 
HETATM 3723 C CCI   . A1LZV B 2 .   ? 22.531 -5.660  43.576 1.00 86.96  ? 501 A1LZV A CCI   1 
HETATM 3724 C CCJ   . A1LZV B 2 .   ? 23.654 -6.284  44.369 1.00 85.81  ? 501 A1LZV A CCJ   1 
HETATM 3725 S S     . SO4   C 3 .   ? 25.569 45.169  60.769 1.00 89.96  ? 502 SO4   A S     1 
HETATM 3726 O O1    . SO4   C 3 .   ? 26.013 44.569  59.540 1.00 91.48  ? 502 SO4   A O1    1 
HETATM 3727 O O2    . SO4   C 3 .   ? 24.469 46.062  60.504 1.00 85.28  ? 502 SO4   A O2    1 
HETATM 3728 O O3    . SO4   C 3 .   ? 25.144 44.135  61.673 1.00 91.69  ? 502 SO4   A O3    1 
HETATM 3729 O O4    . SO4   C 3 .   ? 26.656 45.902  61.359 1.00 91.43  ? 502 SO4   A O4    1 
HETATM 3730 O O     . HOH   D 4 .   ? 8.754  35.416  45.984 1.00 64.10  ? 601 HOH   A O     1 
HETATM 3731 O O     . HOH   D 4 .   ? 18.601 9.309   52.440 1.00 59.66  ? 602 HOH   A O     1 
HETATM 3732 O O     . HOH   D 4 .   ? 21.297 -21.643 42.249 1.00 65.57  ? 603 HOH   A O     1 
HETATM 3733 O O     . HOH   D 4 .   ? 6.961  18.507  53.713 1.00 73.84  ? 604 HOH   A O     1 
HETATM 3734 O O     . HOH   D 4 .   ? 32.466 11.479  67.910 1.00 44.60  ? 605 HOH   A O     1 
HETATM 3735 O O     . HOH   D 4 .   ? 48.311 15.816  66.522 1.00 54.93  ? 606 HOH   A O     1 
HETATM 3736 O O     . HOH   D 4 .   ? 25.829 13.144  61.584 1.00 43.58  ? 607 HOH   A O     1 
HETATM 3737 O O     . HOH   D 4 .   ? 7.160  26.795  54.818 1.00 72.36  ? 608 HOH   A O     1 
HETATM 3738 O O     . HOH   D 4 .   ? 40.602 12.396  65.782 1.00 49.78  ? 609 HOH   A O     1 
HETATM 3739 O O     . HOH   D 4 .   ? 34.191 14.455  49.572 1.00 50.10  ? 610 HOH   A O     1 
HETATM 3740 O O     . HOH   D 4 .   ? 21.890 8.692   54.009 1.00 60.89  ? 611 HOH   A O     1 
HETATM 3741 O O     . HOH   D 4 .   ? 55.669 10.376  62.635 1.00 54.19  ? 612 HOH   A O     1 
HETATM 3742 O O     . HOH   D 4 .   ? 28.397 18.581  52.767 1.00 50.05  ? 613 HOH   A O     1 
HETATM 3743 O O     . HOH   D 4 .   ? 8.434  20.779  41.593 1.00 74.41  ? 614 HOH   A O     1 
HETATM 3744 O O     . HOH   D 4 .   ? 52.268 22.447  58.121 1.00 60.89  ? 615 HOH   A O     1 
HETATM 3745 O O     . HOH   D 4 .   ? 16.803 11.387  40.043 1.00 51.89  ? 616 HOH   A O     1 
HETATM 3746 O O     . HOH   D 4 .   ? 24.298 5.427   71.786 1.00 64.79  ? 617 HOH   A O     1 
HETATM 3747 O O     . HOH   D 4 .   ? 29.588 -6.641  59.223 1.00 46.75  ? 618 HOH   A O     1 
HETATM 3748 O O     . HOH   D 4 .   ? 24.492 0.480   64.615 1.00 51.97  ? 619 HOH   A O     1 
HETATM 3749 O O     . HOH   D 4 .   ? 11.130 14.725  49.555 1.00 62.17  ? 620 HOH   A O     1 
HETATM 3750 O O     . HOH   D 4 .   ? 7.715  17.690  48.259 1.00 78.35  ? 621 HOH   A O     1 
HETATM 3751 O O     . HOH   D 4 .   ? 55.811 -8.965  58.011 1.00 45.09  ? 622 HOH   A O     1 
HETATM 3752 O O     . HOH   D 4 .   ? 25.282 13.967  40.009 1.00 59.77  ? 623 HOH   A O     1 
HETATM 3753 O O     . HOH   D 4 .   ? 20.067 16.268  46.752 1.00 50.29  ? 624 HOH   A O     1 
HETATM 3754 O O     . HOH   D 4 .   ? 13.657 13.899  47.173 1.00 65.13  ? 625 HOH   A O     1 
HETATM 3755 O O     . HOH   D 4 .   ? 18.145 17.014  48.072 1.00 55.41  ? 626 HOH   A O     1 
HETATM 3756 O O     . HOH   D 4 .   ? 28.259 11.068  55.039 1.00 40.23  ? 627 HOH   A O     1 
HETATM 3757 O O     . HOH   D 4 .   ? 47.818 21.208  55.844 1.00 53.23  ? 628 HOH   A O     1 
HETATM 3758 O O     . HOH   D 4 .   ? 28.172 16.131  49.073 1.00 57.08  ? 629 HOH   A O     1 
HETATM 3759 O O     . HOH   D 4 .   ? 11.016 14.406  60.360 1.00 62.17  ? 630 HOH   A O     1 
HETATM 3760 O O     . HOH   D 4 .   ? 31.629 -1.068  54.732 1.00 45.66  ? 631 HOH   A O     1 
HETATM 3761 O O     . HOH   D 4 .   ? 36.972 -4.796  70.859 1.00 50.70  ? 632 HOH   A O     1 
HETATM 3762 O O     . HOH   D 4 .   ? 32.271 -3.611  55.294 1.00 45.40  ? 633 HOH   A O     1 
HETATM 3763 O O     . HOH   D 4 .   ? 50.249 28.079  61.758 1.00 61.00  ? 634 HOH   A O     1 
HETATM 3764 O O     . HOH   D 4 .   ? 36.623 1.673   51.196 1.00 51.60  ? 635 HOH   A O     1 
HETATM 3765 O O     . HOH   D 4 .   ? 44.428 21.473  46.616 1.00 56.94  ? 636 HOH   A O     1 
HETATM 3766 O O     . HOH   D 4 .   ? 52.872 25.967  52.013 1.00 56.04  ? 637 HOH   A O     1 
HETATM 3767 O O     . HOH   D 4 .   ? 45.680 6.025   67.384 1.00 44.23  ? 638 HOH   A O     1 
HETATM 3768 O O     . HOH   D 4 .   ? 43.980 0.807   67.071 1.00 52.84  ? 639 HOH   A O     1 
HETATM 3769 O O     . HOH   D 4 .   ? 36.178 -14.264 53.088 1.00 51.91  ? 640 HOH   A O     1 
HETATM 3770 O O     . HOH   D 4 .   ? 35.442 -13.231 48.419 1.00 51.53  ? 641 HOH   A O     1 
HETATM 3771 O O     . HOH   D 4 .   ? 25.286 30.877  38.011 1.00 56.79  ? 642 HOH   A O     1 
HETATM 3772 O O     . HOH   D 4 .   ? 49.801 27.816  64.311 1.00 57.30  ? 643 HOH   A O     1 
HETATM 3773 O O     . HOH   D 4 .   ? 31.480 -16.046 52.017 1.00 48.77  ? 644 HOH   A O     1 
HETATM 3774 O O     . HOH   D 4 .   ? 28.966 -1.271  55.704 1.00 54.20  ? 645 HOH   A O     1 
HETATM 3775 O O     . HOH   D 4 .   ? 41.126 5.775   72.483 1.00 54.23  ? 646 HOH   A O     1 
HETATM 3776 O O     . HOH   D 4 .   ? 42.935 20.221  44.990 1.00 52.69  ? 647 HOH   A O     1 
HETATM 3777 O O     . HOH   D 4 .   ? 37.941 -6.069  33.681 1.00 69.35  ? 648 HOH   A O     1 
HETATM 3778 O O     . HOH   D 4 .   ? 34.112 14.386  57.665 1.00 49.57  ? 649 HOH   A O     1 
HETATM 3779 O O     . HOH   D 4 .   ? 37.277 -6.529  36.161 1.00 72.64  ? 650 HOH   A O     1 
# 
