data_9JRL
# 
_entry.id   9JRL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JRL         pdb_00009jrl 10.2210/pdb9jrl/pdb 
WWPDB D_1300051899 ?            ?                   
EMDB  EMD-61759    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'EM metadata'     1 0 2025-02-26 ? 
3 FSC               1 0 2025-02-26 ? 
4 'Half map'        1 0 2025-02-26 1 
5 'Half map'        1 0 2025-02-26 2 
6 Image             1 0 2025-02-26 ? 
7 'Primary map'     1 0 2025-02-26 ? 
8 'Structure model' 1 1 2025-04-23 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 'Primary map'     repository 'Initial release' ? ? 
# 
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 8 'Structure model' 'Data collection'     
2 8 '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 8 'Structure model' citation        
2 8 'Structure model' citation_author 
3 8 'Structure model' em_admin        
# 
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  8 'Structure model' '_citation.country'                 
2  8 'Structure model' '_citation.journal_abbrev'          
3  8 'Structure model' '_citation.journal_id_CSD'          
4  8 'Structure model' '_citation.journal_id_ISSN'         
5  8 'Structure model' '_citation.journal_volume'          
6  8 'Structure model' '_citation.page_first'              
7  8 'Structure model' '_citation.page_last'               
8  8 'Structure model' '_citation.pdbx_database_id_DOI'    
9  8 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 8 'Structure model' '_citation.title'                   
11 8 'Structure model' '_citation.year'                    
12 8 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JRL 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'outward-open hSLC19A1 + PT523' 
_pdbx_database_related.db_id          EMD-61759 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              18222089765@163.com 
_pdbx_contact_author.name_first         Qixiang 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7879-171X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, Q.X.' 1 ? 
'Liu, K.X.'   2 ? 
'Gao, P.'     3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3146 
_citation.page_last                 3146 
_citation.title                     'Molecular basis of SLC19A1-mediated folate and cyclic dinucleotide transport.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58378-1 
_citation.pdbx_database_id_PubMed   40175380 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, Q.' 1  0000-0001-7879-171X 
primary 'Zhang, X.' 2  0000-0002-6305-1556 
primary 'Liu, K.'   3  ?                   
primary 'Zhu, Y.'   4  ?                   
primary 'Nie, X.'   5  ?                   
primary 'Ma, J.'    6  ?                   
primary 'Sun, P.'   7  ?                   
primary 'Li, Z.'    8  ?                   
primary 'Gao, Y.'   9  ?                   
primary 'Liu, S.'   10 ?                   
primary 'Gao, A.'   11 0000-0001-8834-9781 
primary 'Zhang, L.' 12 0000-0002-9795-0314 
primary 'Gao, P.'   13 0000-0002-5328-9755 
# 
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 'Soluble cytochrome b562,Reduced folate transporter,fusion protein'                                77480.914 1 ? 
? ? ? 
2 non-polymer syn 'N-(4-CARBOXY-4-{4-[(2,4-DIAMINO-PTERIDIN-6-YLMETHYL)-AMINO]-BENZOYLAMINO}-BUTYL)-PHTHALAMIC ACID' 573.560   1 ? 
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Cytochrome b-562,FOLT,Cyclic dinucleotide:anion antiporter SLC19A1,Folate:anion antiporter SLC19A1,Intestinal folate carrier 1,IFC-1,Placental folate transporter,Reduced folate carrier protein,RFC,hRFC,Reduced folate transporter 1,RFT-1,Solute carrier family 19 member 1,hSLC19A1
;
# 
_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       
;MADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLA
NEGKVKEAQAAAEQLKTTRNAYIQKYLSWRHLVCYLCFYGFMAQIRPGESFITPYLLGPDKQFTREQVTNEITPVLSYSY
LAVLVPVFLLTDYLRYTPVLLLQGLSFVSVWLLLLLGHSVAHMQLMELFYSVTMAARIAYSSYIFSLVRPARYQRVAGYS
RAAVLLGVFTSSVLGQLLVTVGRVSFSTLNYISLAFLTFSVVLALFLKRPKRSLFFNRDDRGRCETSASELERMNPGPGG
KLGHALRVACGDSVLARMLRELGDSLRRPQLRLWSLWWVFNSAGYYLVVYYVHILWNEVDPTTNSARVYNFAADAASTLL
GAITSFAAGFVKIRWARWSKLLIAGVTATQAGLVFLLAHTRHPSSIWLCYAAFVLFRGSYQFLVPIATFQIASSLSKELC
ALVFGVNTFFATIVKTIITFIVSDVRGLGLPVRKQFQLYSVYFLILSIIYFLGAMLDGLRHAEEEKRKAEEEKRKGSGSQ
VQLQESGGGLVQPGGSLRLSCAASGRTISRYAMSWFRQAPGKEREFVAVARRSGDGAFYADSVQGRFTVSRDDAKNTVYL
QMNSLKPEDTAVYYCAIDSDTFYSGSYDYWGQGTQVTVSSHHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLA
NEGKVKEAQAAAEQLKTTRNAYIQKYLSWRHLVCYLCFYGFMAQIRPGESFITPYLLGPDKQFTREQVTNEITPVLSYSY
LAVLVPVFLLTDYLRYTPVLLLQGLSFVSVWLLLLLGHSVAHMQLMELFYSVTMAARIAYSSYIFSLVRPARYQRVAGYS
RAAVLLGVFTSSVLGQLLVTVGRVSFSTLNYISLAFLTFSVVLALFLKRPKRSLFFNRDDRGRCETSASELERMNPGPGG
KLGHALRVACGDSVLARMLRELGDSLRRPQLRLWSLWWVFNSAGYYLVVYYVHILWNEVDPTTNSARVYNFAADAASTLL
GAITSFAAGFVKIRWARWSKLLIAGVTATQAGLVFLLAHTRHPSSIWLCYAAFVLFRGSYQFLVPIATFQIASSLSKELC
ALVFGVNTFFATIVKTIITFIVSDVRGLGLPVRKQFQLYSVYFLILSIIYFLGAMLDGLRHAEEEKRKAEEEKRKGSGSQ
VQLQESGGGLVQPGGSLRLSCAASGRTISRYAMSWFRQAPGKEREFVAVARRSGDGAFYADSVQGRFTVSRDDAKNTVYL
QMNSLKPEDTAVYYCAIDSDTFYSGSYDYWGQGTQVTVSSHHHHHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'N-(4-CARBOXY-4-{4-[(2,4-DIAMINO-PTERIDIN-6-YLMETHYL)-AMINO]-BENZOYLAMINO}-BUTYL)-PHTHALAMIC ACID' 
_pdbx_entity_nonpoly.comp_id     COP 
# 
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   ALA n 
1 3   ASP n 
1 4   LEU n 
1 5   GLU n 
1 6   ASP n 
1 7   ASN n 
1 8   TRP n 
1 9   GLU n 
1 10  THR n 
1 11  LEU n 
1 12  ASN n 
1 13  ASP n 
1 14  ASN n 
1 15  LEU n 
1 16  LYS n 
1 17  VAL n 
1 18  ILE n 
1 19  GLU n 
1 20  LYS n 
1 21  ALA n 
1 22  ASP n 
1 23  ASN n 
1 24  ALA n 
1 25  ALA n 
1 26  GLN n 
1 27  VAL n 
1 28  LYS n 
1 29  ASP n 
1 30  ALA n 
1 31  LEU n 
1 32  THR n 
1 33  LYS n 
1 34  MET n 
1 35  ARG n 
1 36  ALA n 
1 37  ALA n 
1 38  ALA n 
1 39  LEU n 
1 40  ASP n 
1 41  ALA n 
1 42  GLN n 
1 43  LYS n 
1 44  ALA n 
1 45  THR n 
1 46  PRO n 
1 47  PRO n 
1 48  LYS n 
1 49  LEU n 
1 50  GLU n 
1 51  ASP n 
1 52  LYS n 
1 53  SER n 
1 54  PRO n 
1 55  ASP n 
1 56  SER n 
1 57  PRO n 
1 58  GLU n 
1 59  MET n 
1 60  LYS n 
1 61  ASP n 
1 62  PHE n 
1 63  ARG n 
1 64  HIS n 
1 65  GLY n 
1 66  PHE n 
1 67  ASP n 
1 68  ILE n 
1 69  LEU n 
1 70  VAL n 
1 71  GLY n 
1 72  GLN n 
1 73  ILE n 
1 74  ASP n 
1 75  ASP n 
1 76  ALA n 
1 77  LEU n 
1 78  LYS n 
1 79  LEU n 
1 80  ALA n 
1 81  ASN n 
1 82  GLU n 
1 83  GLY n 
1 84  LYS n 
1 85  VAL n 
1 86  LYS n 
1 87  GLU n 
1 88  ALA n 
1 89  GLN n 
1 90  ALA n 
1 91  ALA n 
1 92  ALA n 
1 93  GLU n 
1 94  GLN n 
1 95  LEU n 
1 96  LYS n 
1 97  THR n 
1 98  THR n 
1 99  ARG n 
1 100 ASN n 
1 101 ALA n 
1 102 TYR n 
1 103 ILE n 
1 104 GLN n 
1 105 LYS n 
1 106 TYR n 
1 107 LEU n 
1 108 SER n 
1 109 TRP n 
1 110 ARG n 
1 111 HIS n 
1 112 LEU n 
1 113 VAL n 
1 114 CYS n 
1 115 TYR n 
1 116 LEU n 
1 117 CYS n 
1 118 PHE n 
1 119 TYR n 
1 120 GLY n 
1 121 PHE n 
1 122 MET n 
1 123 ALA n 
1 124 GLN n 
1 125 ILE n 
1 126 ARG n 
1 127 PRO n 
1 128 GLY n 
1 129 GLU n 
1 130 SER n 
1 131 PHE n 
1 132 ILE n 
1 133 THR n 
1 134 PRO n 
1 135 TYR n 
1 136 LEU n 
1 137 LEU n 
1 138 GLY n 
1 139 PRO n 
1 140 ASP n 
1 141 LYS n 
1 142 GLN n 
1 143 PHE n 
1 144 THR n 
1 145 ARG n 
1 146 GLU n 
1 147 GLN n 
1 148 VAL n 
1 149 THR n 
1 150 ASN n 
1 151 GLU n 
1 152 ILE n 
1 153 THR n 
1 154 PRO n 
1 155 VAL n 
1 156 LEU n 
1 157 SER n 
1 158 TYR n 
1 159 SER n 
1 160 TYR n 
1 161 LEU n 
1 162 ALA n 
1 163 VAL n 
1 164 LEU n 
1 165 VAL n 
1 166 PRO n 
1 167 VAL n 
1 168 PHE n 
1 169 LEU n 
1 170 LEU n 
1 171 THR n 
1 172 ASP n 
1 173 TYR n 
1 174 LEU n 
1 175 ARG n 
1 176 TYR n 
1 177 THR n 
1 178 PRO n 
1 179 VAL n 
1 180 LEU n 
1 181 LEU n 
1 182 LEU n 
1 183 GLN n 
1 184 GLY n 
1 185 LEU n 
1 186 SER n 
1 187 PHE n 
1 188 VAL n 
1 189 SER n 
1 190 VAL n 
1 191 TRP n 
1 192 LEU n 
1 193 LEU n 
1 194 LEU n 
1 195 LEU n 
1 196 LEU n 
1 197 GLY n 
1 198 HIS n 
1 199 SER n 
1 200 VAL n 
1 201 ALA n 
1 202 HIS n 
1 203 MET n 
1 204 GLN n 
1 205 LEU n 
1 206 MET n 
1 207 GLU n 
1 208 LEU n 
1 209 PHE n 
1 210 TYR n 
1 211 SER n 
1 212 VAL n 
1 213 THR n 
1 214 MET n 
1 215 ALA n 
1 216 ALA n 
1 217 ARG n 
1 218 ILE n 
1 219 ALA n 
1 220 TYR n 
1 221 SER n 
1 222 SER n 
1 223 TYR n 
1 224 ILE n 
1 225 PHE n 
1 226 SER n 
1 227 LEU n 
1 228 VAL n 
1 229 ARG n 
1 230 PRO n 
1 231 ALA n 
1 232 ARG n 
1 233 TYR n 
1 234 GLN n 
1 235 ARG n 
1 236 VAL n 
1 237 ALA n 
1 238 GLY n 
1 239 TYR n 
1 240 SER n 
1 241 ARG n 
1 242 ALA n 
1 243 ALA n 
1 244 VAL n 
1 245 LEU n 
1 246 LEU n 
1 247 GLY n 
1 248 VAL n 
1 249 PHE n 
1 250 THR n 
1 251 SER n 
1 252 SER n 
1 253 VAL n 
1 254 LEU n 
1 255 GLY n 
1 256 GLN n 
1 257 LEU n 
1 258 LEU n 
1 259 VAL n 
1 260 THR n 
1 261 VAL n 
1 262 GLY n 
1 263 ARG n 
1 264 VAL n 
1 265 SER n 
1 266 PHE n 
1 267 SER n 
1 268 THR n 
1 269 LEU n 
1 270 ASN n 
1 271 TYR n 
1 272 ILE n 
1 273 SER n 
1 274 LEU n 
1 275 ALA n 
1 276 PHE n 
1 277 LEU n 
1 278 THR n 
1 279 PHE n 
1 280 SER n 
1 281 VAL n 
1 282 VAL n 
1 283 LEU n 
1 284 ALA n 
1 285 LEU n 
1 286 PHE n 
1 287 LEU n 
1 288 LYS n 
1 289 ARG n 
1 290 PRO n 
1 291 LYS n 
1 292 ARG n 
1 293 SER n 
1 294 LEU n 
1 295 PHE n 
1 296 PHE n 
1 297 ASN n 
1 298 ARG n 
1 299 ASP n 
1 300 ASP n 
1 301 ARG n 
1 302 GLY n 
1 303 ARG n 
1 304 CYS n 
1 305 GLU n 
1 306 THR n 
1 307 SER n 
1 308 ALA n 
1 309 SER n 
1 310 GLU n 
1 311 LEU n 
1 312 GLU n 
1 313 ARG n 
1 314 MET n 
1 315 ASN n 
1 316 PRO n 
1 317 GLY n 
1 318 PRO n 
1 319 GLY n 
1 320 GLY n 
1 321 LYS n 
1 322 LEU n 
1 323 GLY n 
1 324 HIS n 
1 325 ALA n 
1 326 LEU n 
1 327 ARG n 
1 328 VAL n 
1 329 ALA n 
1 330 CYS n 
1 331 GLY n 
1 332 ASP n 
1 333 SER n 
1 334 VAL n 
1 335 LEU n 
1 336 ALA n 
1 337 ARG n 
1 338 MET n 
1 339 LEU n 
1 340 ARG n 
1 341 GLU n 
1 342 LEU n 
1 343 GLY n 
1 344 ASP n 
1 345 SER n 
1 346 LEU n 
1 347 ARG n 
1 348 ARG n 
1 349 PRO n 
1 350 GLN n 
1 351 LEU n 
1 352 ARG n 
1 353 LEU n 
1 354 TRP n 
1 355 SER n 
1 356 LEU n 
1 357 TRP n 
1 358 TRP n 
1 359 VAL n 
1 360 PHE n 
1 361 ASN n 
1 362 SER n 
1 363 ALA n 
1 364 GLY n 
1 365 TYR n 
1 366 TYR n 
1 367 LEU n 
1 368 VAL n 
1 369 VAL n 
1 370 TYR n 
1 371 TYR n 
1 372 VAL n 
1 373 HIS n 
1 374 ILE n 
1 375 LEU n 
1 376 TRP n 
1 377 ASN n 
1 378 GLU n 
1 379 VAL n 
1 380 ASP n 
1 381 PRO n 
1 382 THR n 
1 383 THR n 
1 384 ASN n 
1 385 SER n 
1 386 ALA n 
1 387 ARG n 
1 388 VAL n 
1 389 TYR n 
1 390 ASN n 
1 391 PHE n 
1 392 ALA n 
1 393 ALA n 
1 394 ASP n 
1 395 ALA n 
1 396 ALA n 
1 397 SER n 
1 398 THR n 
1 399 LEU n 
1 400 LEU n 
1 401 GLY n 
1 402 ALA n 
1 403 ILE n 
1 404 THR n 
1 405 SER n 
1 406 PHE n 
1 407 ALA n 
1 408 ALA n 
1 409 GLY n 
1 410 PHE n 
1 411 VAL n 
1 412 LYS n 
1 413 ILE n 
1 414 ARG n 
1 415 TRP n 
1 416 ALA n 
1 417 ARG n 
1 418 TRP n 
1 419 SER n 
1 420 LYS n 
1 421 LEU n 
1 422 LEU n 
1 423 ILE n 
1 424 ALA n 
1 425 GLY n 
1 426 VAL n 
1 427 THR n 
1 428 ALA n 
1 429 THR n 
1 430 GLN n 
1 431 ALA n 
1 432 GLY n 
1 433 LEU n 
1 434 VAL n 
1 435 PHE n 
1 436 LEU n 
1 437 LEU n 
1 438 ALA n 
1 439 HIS n 
1 440 THR n 
1 441 ARG n 
1 442 HIS n 
1 443 PRO n 
1 444 SER n 
1 445 SER n 
1 446 ILE n 
1 447 TRP n 
1 448 LEU n 
1 449 CYS n 
1 450 TYR n 
1 451 ALA n 
1 452 ALA n 
1 453 PHE n 
1 454 VAL n 
1 455 LEU n 
1 456 PHE n 
1 457 ARG n 
1 458 GLY n 
1 459 SER n 
1 460 TYR n 
1 461 GLN n 
1 462 PHE n 
1 463 LEU n 
1 464 VAL n 
1 465 PRO n 
1 466 ILE n 
1 467 ALA n 
1 468 THR n 
1 469 PHE n 
1 470 GLN n 
1 471 ILE n 
1 472 ALA n 
1 473 SER n 
1 474 SER n 
1 475 LEU n 
1 476 SER n 
1 477 LYS n 
1 478 GLU n 
1 479 LEU n 
1 480 CYS n 
1 481 ALA n 
1 482 LEU n 
1 483 VAL n 
1 484 PHE n 
1 485 GLY n 
1 486 VAL n 
1 487 ASN n 
1 488 THR n 
1 489 PHE n 
1 490 PHE n 
1 491 ALA n 
1 492 THR n 
1 493 ILE n 
1 494 VAL n 
1 495 LYS n 
1 496 THR n 
1 497 ILE n 
1 498 ILE n 
1 499 THR n 
1 500 PHE n 
1 501 ILE n 
1 502 VAL n 
1 503 SER n 
1 504 ASP n 
1 505 VAL n 
1 506 ARG n 
1 507 GLY n 
1 508 LEU n 
1 509 GLY n 
1 510 LEU n 
1 511 PRO n 
1 512 VAL n 
1 513 ARG n 
1 514 LYS n 
1 515 GLN n 
1 516 PHE n 
1 517 GLN n 
1 518 LEU n 
1 519 TYR n 
1 520 SER n 
1 521 VAL n 
1 522 TYR n 
1 523 PHE n 
1 524 LEU n 
1 525 ILE n 
1 526 LEU n 
1 527 SER n 
1 528 ILE n 
1 529 ILE n 
1 530 TYR n 
1 531 PHE n 
1 532 LEU n 
1 533 GLY n 
1 534 ALA n 
1 535 MET n 
1 536 LEU n 
1 537 ASP n 
1 538 GLY n 
1 539 LEU n 
1 540 ARG n 
1 541 HIS n 
1 542 ALA n 
1 543 GLU n 
1 544 GLU n 
1 545 GLU n 
1 546 LYS n 
1 547 ARG n 
1 548 LYS n 
1 549 ALA n 
1 550 GLU n 
1 551 GLU n 
1 552 GLU n 
1 553 LYS n 
1 554 ARG n 
1 555 LYS n 
1 556 GLY n 
1 557 SER n 
1 558 GLY n 
1 559 SER n 
1 560 GLN n 
1 561 VAL n 
1 562 GLN n 
1 563 LEU n 
1 564 GLN n 
1 565 GLU n 
1 566 SER n 
1 567 GLY n 
1 568 GLY n 
1 569 GLY n 
1 570 LEU n 
1 571 VAL n 
1 572 GLN n 
1 573 PRO n 
1 574 GLY n 
1 575 GLY n 
1 576 SER n 
1 577 LEU n 
1 578 ARG n 
1 579 LEU n 
1 580 SER n 
1 581 CYS n 
1 582 ALA n 
1 583 ALA n 
1 584 SER n 
1 585 GLY n 
1 586 ARG n 
1 587 THR n 
1 588 ILE n 
1 589 SER n 
1 590 ARG n 
1 591 TYR n 
1 592 ALA n 
1 593 MET n 
1 594 SER n 
1 595 TRP n 
1 596 PHE n 
1 597 ARG n 
1 598 GLN n 
1 599 ALA n 
1 600 PRO n 
1 601 GLY n 
1 602 LYS n 
1 603 GLU n 
1 604 ARG n 
1 605 GLU n 
1 606 PHE n 
1 607 VAL n 
1 608 ALA n 
1 609 VAL n 
1 610 ALA n 
1 611 ARG n 
1 612 ARG n 
1 613 SER n 
1 614 GLY n 
1 615 ASP n 
1 616 GLY n 
1 617 ALA n 
1 618 PHE n 
1 619 TYR n 
1 620 ALA n 
1 621 ASP n 
1 622 SER n 
1 623 VAL n 
1 624 GLN n 
1 625 GLY n 
1 626 ARG n 
1 627 PHE n 
1 628 THR n 
1 629 VAL n 
1 630 SER n 
1 631 ARG n 
1 632 ASP n 
1 633 ASP n 
1 634 ALA n 
1 635 LYS n 
1 636 ASN n 
1 637 THR n 
1 638 VAL n 
1 639 TYR n 
1 640 LEU n 
1 641 GLN n 
1 642 MET n 
1 643 ASN n 
1 644 SER n 
1 645 LEU n 
1 646 LYS n 
1 647 PRO n 
1 648 GLU n 
1 649 ASP n 
1 650 THR n 
1 651 ALA n 
1 652 VAL n 
1 653 TYR n 
1 654 TYR n 
1 655 CYS n 
1 656 ALA n 
1 657 ILE n 
1 658 ASP n 
1 659 SER n 
1 660 ASP n 
1 661 THR n 
1 662 PHE n 
1 663 TYR n 
1 664 SER n 
1 665 GLY n 
1 666 SER n 
1 667 TYR n 
1 668 ASP n 
1 669 TYR n 
1 670 TRP n 
1 671 GLY n 
1 672 GLN n 
1 673 GLY n 
1 674 THR n 
1 675 GLN n 
1 676 VAL n 
1 677 THR n 
1 678 VAL n 
1 679 SER n 
1 680 SER n 
1 681 HIS n 
1 682 HIS n 
1 683 HIS n 
1 684 HIS n 
1 685 HIS n 
1 686 HIS n 
1 687 HIS n 
1 688 HIS n 
1 689 HIS n 
1 690 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   107 ?     ? cybC                   ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 108 541 human ? 'SLC19A1, FLOT1, RFC1' ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 542 690 human ? ?                      ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                            ?     
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                                                           ?     
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                         ?     
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                    ?     
'C4 H7 N O4'     133.103 
COP non-polymer         . 'N-(4-CARBOXY-4-{4-[(2,4-DIAMINO-PTERIDIN-6-YLMETHYL)-AMINO]-BENZOYLAMINO}-BUTYL)-PHTHALAMIC ACID' PT523 
'C27 H27 N9 O6'  573.560 
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 
ILE 'L-peptide linking' y ISOLEUCINE                                                                                         ?     
'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                            ?     
'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                                                             ?     
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                                         ?     
'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                      ?     
'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                                                            ?     
'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                                                             ?     
'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                                                          ?     
'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                         ?     
'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                           ?     
'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                                                             ?     
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -83 ?   ?   ?   A . n 
A 1 2   ALA 2   -82 ?   ?   ?   A . n 
A 1 3   ASP 3   -81 ?   ?   ?   A . n 
A 1 4   LEU 4   -80 ?   ?   ?   A . n 
A 1 5   GLU 5   -79 ?   ?   ?   A . n 
A 1 6   ASP 6   -78 ?   ?   ?   A . n 
A 1 7   ASN 7   -77 ?   ?   ?   A . n 
A 1 8   TRP 8   -76 ?   ?   ?   A . n 
A 1 9   GLU 9   -75 ?   ?   ?   A . n 
A 1 10  THR 10  -74 ?   ?   ?   A . n 
A 1 11  LEU 11  -73 ?   ?   ?   A . n 
A 1 12  ASN 12  -72 ?   ?   ?   A . n 
A 1 13  ASP 13  -71 ?   ?   ?   A . n 
A 1 14  ASN 14  -70 ?   ?   ?   A . n 
A 1 15  LEU 15  -69 ?   ?   ?   A . n 
A 1 16  LYS 16  -68 ?   ?   ?   A . n 
A 1 17  VAL 17  -67 ?   ?   ?   A . n 
A 1 18  ILE 18  -66 ?   ?   ?   A . n 
A 1 19  GLU 19  -65 ?   ?   ?   A . n 
A 1 20  LYS 20  -64 ?   ?   ?   A . n 
A 1 21  ALA 21  -63 ?   ?   ?   A . n 
A 1 22  ASP 22  -62 ?   ?   ?   A . n 
A 1 23  ASN 23  -61 ?   ?   ?   A . n 
A 1 24  ALA 24  -60 ?   ?   ?   A . n 
A 1 25  ALA 25  -59 ?   ?   ?   A . n 
A 1 26  GLN 26  -58 ?   ?   ?   A . n 
A 1 27  VAL 27  -57 ?   ?   ?   A . n 
A 1 28  LYS 28  -56 ?   ?   ?   A . n 
A 1 29  ASP 29  -55 ?   ?   ?   A . n 
A 1 30  ALA 30  -54 ?   ?   ?   A . n 
A 1 31  LEU 31  -53 ?   ?   ?   A . n 
A 1 32  THR 32  -52 ?   ?   ?   A . n 
A 1 33  LYS 33  -51 ?   ?   ?   A . n 
A 1 34  MET 34  -50 ?   ?   ?   A . n 
A 1 35  ARG 35  -49 ?   ?   ?   A . n 
A 1 36  ALA 36  -48 ?   ?   ?   A . n 
A 1 37  ALA 37  -47 ?   ?   ?   A . n 
A 1 38  ALA 38  -46 ?   ?   ?   A . n 
A 1 39  LEU 39  -45 ?   ?   ?   A . n 
A 1 40  ASP 40  -44 ?   ?   ?   A . n 
A 1 41  ALA 41  -43 ?   ?   ?   A . n 
A 1 42  GLN 42  -42 ?   ?   ?   A . n 
A 1 43  LYS 43  -41 ?   ?   ?   A . n 
A 1 44  ALA 44  -40 ?   ?   ?   A . n 
A 1 45  THR 45  -39 ?   ?   ?   A . n 
A 1 46  PRO 46  -38 ?   ?   ?   A . n 
A 1 47  PRO 47  -37 ?   ?   ?   A . n 
A 1 48  LYS 48  -36 ?   ?   ?   A . n 
A 1 49  LEU 49  -35 ?   ?   ?   A . n 
A 1 50  GLU 50  -34 ?   ?   ?   A . n 
A 1 51  ASP 51  -33 ?   ?   ?   A . n 
A 1 52  LYS 52  -32 ?   ?   ?   A . n 
A 1 53  SER 53  -31 ?   ?   ?   A . n 
A 1 54  PRO 54  -30 ?   ?   ?   A . n 
A 1 55  ASP 55  -29 ?   ?   ?   A . n 
A 1 56  SER 56  -28 ?   ?   ?   A . n 
A 1 57  PRO 57  -27 ?   ?   ?   A . n 
A 1 58  GLU 58  -26 ?   ?   ?   A . n 
A 1 59  MET 59  -25 ?   ?   ?   A . n 
A 1 60  LYS 60  -24 ?   ?   ?   A . n 
A 1 61  ASP 61  -23 ?   ?   ?   A . n 
A 1 62  PHE 62  -22 ?   ?   ?   A . n 
A 1 63  ARG 63  -21 ?   ?   ?   A . n 
A 1 64  HIS 64  -20 ?   ?   ?   A . n 
A 1 65  GLY 65  -19 ?   ?   ?   A . n 
A 1 66  PHE 66  -18 ?   ?   ?   A . n 
A 1 67  ASP 67  -17 ?   ?   ?   A . n 
A 1 68  ILE 68  -16 ?   ?   ?   A . n 
A 1 69  LEU 69  -15 ?   ?   ?   A . n 
A 1 70  VAL 70  -14 ?   ?   ?   A . n 
A 1 71  GLY 71  -13 ?   ?   ?   A . n 
A 1 72  GLN 72  -12 ?   ?   ?   A . n 
A 1 73  ILE 73  -11 ?   ?   ?   A . n 
A 1 74  ASP 74  -10 ?   ?   ?   A . n 
A 1 75  ASP 75  -9  ?   ?   ?   A . n 
A 1 76  ALA 76  -8  ?   ?   ?   A . n 
A 1 77  LEU 77  -7  ?   ?   ?   A . n 
A 1 78  LYS 78  -6  ?   ?   ?   A . n 
A 1 79  LEU 79  -5  ?   ?   ?   A . n 
A 1 80  ALA 80  -4  ?   ?   ?   A . n 
A 1 81  ASN 81  -3  ?   ?   ?   A . n 
A 1 82  GLU 82  -2  ?   ?   ?   A . n 
A 1 83  GLY 83  -1  ?   ?   ?   A . n 
A 1 84  LYS 84  0   ?   ?   ?   A . n 
A 1 85  VAL 85  1   ?   ?   ?   A . n 
A 1 86  LYS 86  2   ?   ?   ?   A . n 
A 1 87  GLU 87  3   ?   ?   ?   A . n 
A 1 88  ALA 88  4   ?   ?   ?   A . n 
A 1 89  GLN 89  5   ?   ?   ?   A . n 
A 1 90  ALA 90  6   ?   ?   ?   A . n 
A 1 91  ALA 91  7   ?   ?   ?   A . n 
A 1 92  ALA 92  8   ?   ?   ?   A . n 
A 1 93  GLU 93  9   ?   ?   ?   A . n 
A 1 94  GLN 94  10  ?   ?   ?   A . n 
A 1 95  LEU 95  11  ?   ?   ?   A . n 
A 1 96  LYS 96  12  ?   ?   ?   A . n 
A 1 97  THR 97  13  ?   ?   ?   A . n 
A 1 98  THR 98  14  ?   ?   ?   A . n 
A 1 99  ARG 99  15  ?   ?   ?   A . n 
A 1 100 ASN 100 16  ?   ?   ?   A . n 
A 1 101 ALA 101 17  ?   ?   ?   A . n 
A 1 102 TYR 102 18  ?   ?   ?   A . n 
A 1 103 ILE 103 19  ?   ?   ?   A . n 
A 1 104 GLN 104 20  ?   ?   ?   A . n 
A 1 105 LYS 105 21  ?   ?   ?   A . n 
A 1 106 TYR 106 22  ?   ?   ?   A . n 
A 1 107 LEU 107 23  ?   ?   ?   A . n 
A 1 108 SER 108 24  24  SER SER A . n 
A 1 109 TRP 109 25  25  TRP TRP A . n 
A 1 110 ARG 110 26  26  ARG ARG A . n 
A 1 111 HIS 111 27  27  HIS HIS A . n 
A 1 112 LEU 112 28  28  LEU LEU A . n 
A 1 113 VAL 113 29  29  VAL VAL A . n 
A 1 114 CYS 114 30  30  CYS CYS A . n 
A 1 115 TYR 115 31  31  TYR TYR A . n 
A 1 116 LEU 116 32  32  LEU LEU A . n 
A 1 117 CYS 117 33  33  CYS CYS A . n 
A 1 118 PHE 118 34  34  PHE PHE A . n 
A 1 119 TYR 119 35  35  TYR TYR A . n 
A 1 120 GLY 120 36  36  GLY GLY A . n 
A 1 121 PHE 121 37  37  PHE PHE A . n 
A 1 122 MET 122 38  38  MET MET A . n 
A 1 123 ALA 123 39  39  ALA ALA A . n 
A 1 124 GLN 124 40  40  GLN GLN A . n 
A 1 125 ILE 125 41  41  ILE ILE A . n 
A 1 126 ARG 126 42  42  ARG ARG A . n 
A 1 127 PRO 127 43  43  PRO PRO A . n 
A 1 128 GLY 128 44  44  GLY GLY A . n 
A 1 129 GLU 129 45  45  GLU GLU A . n 
A 1 130 SER 130 46  46  SER SER A . n 
A 1 131 PHE 131 47  47  PHE PHE A . n 
A 1 132 ILE 132 48  48  ILE ILE A . n 
A 1 133 THR 133 49  49  THR THR A . n 
A 1 134 PRO 134 50  50  PRO PRO A . n 
A 1 135 TYR 135 51  51  TYR TYR A . n 
A 1 136 LEU 136 52  52  LEU LEU A . n 
A 1 137 LEU 137 53  53  LEU LEU A . n 
A 1 138 GLY 138 54  54  GLY GLY A . n 
A 1 139 PRO 139 55  55  PRO PRO A . n 
A 1 140 ASP 140 56  56  ASP ASP A . n 
A 1 141 LYS 141 57  57  LYS LYS A . n 
A 1 142 GLN 142 58  58  GLN GLN A . n 
A 1 143 PHE 143 59  59  PHE PHE A . n 
A 1 144 THR 144 60  60  THR THR A . n 
A 1 145 ARG 145 61  61  ARG ARG A . n 
A 1 146 GLU 146 62  62  GLU GLU A . n 
A 1 147 GLN 147 63  63  GLN GLN A . n 
A 1 148 VAL 148 64  64  VAL VAL A . n 
A 1 149 THR 149 65  65  THR THR A . n 
A 1 150 ASN 150 66  66  ASN ASN A . n 
A 1 151 GLU 151 67  67  GLU GLU A . n 
A 1 152 ILE 152 68  68  ILE ILE A . n 
A 1 153 THR 153 69  69  THR THR A . n 
A 1 154 PRO 154 70  70  PRO PRO A . n 
A 1 155 VAL 155 71  71  VAL VAL A . n 
A 1 156 LEU 156 72  72  LEU LEU A . n 
A 1 157 SER 157 73  73  SER SER A . n 
A 1 158 TYR 158 74  74  TYR TYR A . n 
A 1 159 SER 159 75  75  SER SER A . n 
A 1 160 TYR 160 76  76  TYR TYR A . n 
A 1 161 LEU 161 77  77  LEU LEU A . n 
A 1 162 ALA 162 78  78  ALA ALA A . n 
A 1 163 VAL 163 79  79  VAL VAL A . n 
A 1 164 LEU 164 80  80  LEU LEU A . n 
A 1 165 VAL 165 81  81  VAL VAL A . n 
A 1 166 PRO 166 82  82  PRO PRO A . n 
A 1 167 VAL 167 83  83  VAL VAL A . n 
A 1 168 PHE 168 84  84  PHE PHE A . n 
A 1 169 LEU 169 85  85  LEU LEU A . n 
A 1 170 LEU 170 86  86  LEU LEU A . n 
A 1 171 THR 171 87  87  THR THR A . n 
A 1 172 ASP 172 88  88  ASP ASP A . n 
A 1 173 TYR 173 89  89  TYR TYR A . n 
A 1 174 LEU 174 90  90  LEU LEU A . n 
A 1 175 ARG 175 91  91  ARG ARG A . n 
A 1 176 TYR 176 92  92  TYR TYR A . n 
A 1 177 THR 177 93  93  THR THR A . n 
A 1 178 PRO 178 94  94  PRO PRO A . n 
A 1 179 VAL 179 95  95  VAL VAL A . n 
A 1 180 LEU 180 96  96  LEU LEU A . n 
A 1 181 LEU 181 97  97  LEU LEU A . n 
A 1 182 LEU 182 98  98  LEU LEU A . n 
A 1 183 GLN 183 99  99  GLN GLN A . n 
A 1 184 GLY 184 100 100 GLY GLY A . n 
A 1 185 LEU 185 101 101 LEU LEU A . n 
A 1 186 SER 186 102 102 SER SER A . n 
A 1 187 PHE 187 103 103 PHE PHE A . n 
A 1 188 VAL 188 104 104 VAL VAL A . n 
A 1 189 SER 189 105 105 SER SER A . n 
A 1 190 VAL 190 106 106 VAL VAL A . n 
A 1 191 TRP 191 107 107 TRP TRP A . n 
A 1 192 LEU 192 108 108 LEU LEU A . n 
A 1 193 LEU 193 109 109 LEU LEU A . n 
A 1 194 LEU 194 110 110 LEU LEU A . n 
A 1 195 LEU 195 111 111 LEU LEU A . n 
A 1 196 LEU 196 112 112 LEU LEU A . n 
A 1 197 GLY 197 113 113 GLY GLY A . n 
A 1 198 HIS 198 114 114 HIS HIS A . n 
A 1 199 SER 199 115 115 SER SER A . n 
A 1 200 VAL 200 116 116 VAL VAL A . n 
A 1 201 ALA 201 117 117 ALA ALA A . n 
A 1 202 HIS 202 118 118 HIS HIS A . n 
A 1 203 MET 203 119 119 MET MET A . n 
A 1 204 GLN 204 120 120 GLN GLN A . n 
A 1 205 LEU 205 121 121 LEU LEU A . n 
A 1 206 MET 206 122 122 MET MET A . n 
A 1 207 GLU 207 123 123 GLU GLU A . n 
A 1 208 LEU 208 124 124 LEU LEU A . n 
A 1 209 PHE 209 125 125 PHE PHE A . n 
A 1 210 TYR 210 126 126 TYR TYR A . n 
A 1 211 SER 211 127 127 SER SER A . n 
A 1 212 VAL 212 128 128 VAL VAL A . n 
A 1 213 THR 213 129 129 THR THR A . n 
A 1 214 MET 214 130 130 MET MET A . n 
A 1 215 ALA 215 131 131 ALA ALA A . n 
A 1 216 ALA 216 132 132 ALA ALA A . n 
A 1 217 ARG 217 133 133 ARG ARG A . n 
A 1 218 ILE 218 134 134 ILE ILE A . n 
A 1 219 ALA 219 135 135 ALA ALA A . n 
A 1 220 TYR 220 136 136 TYR TYR A . n 
A 1 221 SER 221 137 137 SER SER A . n 
A 1 222 SER 222 138 138 SER SER A . n 
A 1 223 TYR 223 139 139 TYR TYR A . n 
A 1 224 ILE 224 140 140 ILE ILE A . n 
A 1 225 PHE 225 141 141 PHE PHE A . n 
A 1 226 SER 226 142 142 SER SER A . n 
A 1 227 LEU 227 143 143 LEU LEU A . n 
A 1 228 VAL 228 144 144 VAL VAL A . n 
A 1 229 ARG 229 145 145 ARG ARG A . n 
A 1 230 PRO 230 146 146 PRO PRO A . n 
A 1 231 ALA 231 147 147 ALA ALA A . n 
A 1 232 ARG 232 148 148 ARG ARG A . n 
A 1 233 TYR 233 149 149 TYR TYR A . n 
A 1 234 GLN 234 150 150 GLN GLN A . n 
A 1 235 ARG 235 151 151 ARG ARG A . n 
A 1 236 VAL 236 152 152 VAL VAL A . n 
A 1 237 ALA 237 153 153 ALA ALA A . n 
A 1 238 GLY 238 154 154 GLY GLY A . n 
A 1 239 TYR 239 155 155 TYR TYR A . n 
A 1 240 SER 240 156 156 SER SER A . n 
A 1 241 ARG 241 157 157 ARG ARG A . n 
A 1 242 ALA 242 158 158 ALA ALA A . n 
A 1 243 ALA 243 159 159 ALA ALA A . n 
A 1 244 VAL 244 160 160 VAL VAL A . n 
A 1 245 LEU 245 161 161 LEU LEU A . n 
A 1 246 LEU 246 162 162 LEU LEU A . n 
A 1 247 GLY 247 163 163 GLY GLY A . n 
A 1 248 VAL 248 164 164 VAL VAL A . n 
A 1 249 PHE 249 165 165 PHE PHE A . n 
A 1 250 THR 250 166 166 THR THR A . n 
A 1 251 SER 251 167 167 SER SER A . n 
A 1 252 SER 252 168 168 SER SER A . n 
A 1 253 VAL 253 169 169 VAL VAL A . n 
A 1 254 LEU 254 170 170 LEU LEU A . n 
A 1 255 GLY 255 171 171 GLY GLY A . n 
A 1 256 GLN 256 172 172 GLN GLN A . n 
A 1 257 LEU 257 173 173 LEU LEU A . n 
A 1 258 LEU 258 174 174 LEU LEU A . n 
A 1 259 VAL 259 175 175 VAL VAL A . n 
A 1 260 THR 260 176 176 THR THR A . n 
A 1 261 VAL 261 177 177 VAL VAL A . n 
A 1 262 GLY 262 178 178 GLY GLY A . n 
A 1 263 ARG 263 179 179 ARG ARG A . n 
A 1 264 VAL 264 180 180 VAL VAL A . n 
A 1 265 SER 265 181 181 SER SER A . n 
A 1 266 PHE 266 182 182 PHE PHE A . n 
A 1 267 SER 267 183 183 SER SER A . n 
A 1 268 THR 268 184 184 THR THR A . n 
A 1 269 LEU 269 185 185 LEU LEU A . n 
A 1 270 ASN 270 186 186 ASN ASN A . n 
A 1 271 TYR 271 187 187 TYR TYR A . n 
A 1 272 ILE 272 188 188 ILE ILE A . n 
A 1 273 SER 273 189 189 SER SER A . n 
A 1 274 LEU 274 190 190 LEU LEU A . n 
A 1 275 ALA 275 191 191 ALA ALA A . n 
A 1 276 PHE 276 192 192 PHE PHE A . n 
A 1 277 LEU 277 193 193 LEU LEU A . n 
A 1 278 THR 278 194 194 THR THR A . n 
A 1 279 PHE 279 195 195 PHE PHE A . n 
A 1 280 SER 280 196 196 SER SER A . n 
A 1 281 VAL 281 197 197 VAL VAL A . n 
A 1 282 VAL 282 198 198 VAL VAL A . n 
A 1 283 LEU 283 199 199 LEU LEU A . n 
A 1 284 ALA 284 200 200 ALA ALA A . n 
A 1 285 LEU 285 201 201 LEU LEU A . n 
A 1 286 PHE 286 202 202 PHE PHE A . n 
A 1 287 LEU 287 203 203 LEU LEU A . n 
A 1 288 LYS 288 204 204 LYS LYS A . n 
A 1 289 ARG 289 205 205 ARG ARG A . n 
A 1 290 PRO 290 206 206 PRO PRO A . n 
A 1 291 LYS 291 207 207 LYS LYS A . n 
A 1 292 ARG 292 208 ?   ?   ?   A . n 
A 1 293 SER 293 209 ?   ?   ?   A . n 
A 1 294 LEU 294 210 ?   ?   ?   A . n 
A 1 295 PHE 295 211 ?   ?   ?   A . n 
A 1 296 PHE 296 212 ?   ?   ?   A . n 
A 1 297 ASN 297 213 ?   ?   ?   A . n 
A 1 298 ARG 298 214 ?   ?   ?   A . n 
A 1 299 ASP 299 215 ?   ?   ?   A . n 
A 1 300 ASP 300 216 ?   ?   ?   A . n 
A 1 301 ARG 301 217 ?   ?   ?   A . n 
A 1 302 GLY 302 218 ?   ?   ?   A . n 
A 1 303 ARG 303 219 ?   ?   ?   A . n 
A 1 304 CYS 304 220 ?   ?   ?   A . n 
A 1 305 GLU 305 221 ?   ?   ?   A . n 
A 1 306 THR 306 222 ?   ?   ?   A . n 
A 1 307 SER 307 223 ?   ?   ?   A . n 
A 1 308 ALA 308 224 ?   ?   ?   A . n 
A 1 309 SER 309 225 ?   ?   ?   A . n 
A 1 310 GLU 310 226 ?   ?   ?   A . n 
A 1 311 LEU 311 227 ?   ?   ?   A . n 
A 1 312 GLU 312 228 ?   ?   ?   A . n 
A 1 313 ARG 313 229 ?   ?   ?   A . n 
A 1 314 MET 314 230 ?   ?   ?   A . n 
A 1 315 ASN 315 231 ?   ?   ?   A . n 
A 1 316 PRO 316 232 ?   ?   ?   A . n 
A 1 317 GLY 317 233 ?   ?   ?   A . n 
A 1 318 PRO 318 234 ?   ?   ?   A . n 
A 1 319 GLY 319 235 ?   ?   ?   A . n 
A 1 320 GLY 320 236 ?   ?   ?   A . n 
A 1 321 LYS 321 237 ?   ?   ?   A . n 
A 1 322 LEU 322 238 ?   ?   ?   A . n 
A 1 323 GLY 323 239 ?   ?   ?   A . n 
A 1 324 HIS 324 240 ?   ?   ?   A . n 
A 1 325 ALA 325 241 ?   ?   ?   A . n 
A 1 326 LEU 326 242 ?   ?   ?   A . n 
A 1 327 ARG 327 243 ?   ?   ?   A . n 
A 1 328 VAL 328 244 ?   ?   ?   A . n 
A 1 329 ALA 329 245 ?   ?   ?   A . n 
A 1 330 CYS 330 246 ?   ?   ?   A . n 
A 1 331 GLY 331 247 ?   ?   ?   A . n 
A 1 332 ASP 332 248 ?   ?   ?   A . n 
A 1 333 SER 333 249 249 SER SER A . n 
A 1 334 VAL 334 250 250 VAL VAL A . n 
A 1 335 LEU 335 251 251 LEU LEU A . n 
A 1 336 ALA 336 252 252 ALA ALA A . n 
A 1 337 ARG 337 253 253 ARG ARG A . n 
A 1 338 MET 338 254 254 MET MET A . n 
A 1 339 LEU 339 255 255 LEU LEU A . n 
A 1 340 ARG 340 256 256 ARG ARG A . n 
A 1 341 GLU 341 257 257 GLU GLU A . n 
A 1 342 LEU 342 258 258 LEU LEU A . n 
A 1 343 GLY 343 259 259 GLY GLY A . n 
A 1 344 ASP 344 260 260 ASP ASP A . n 
A 1 345 SER 345 261 261 SER SER A . n 
A 1 346 LEU 346 262 262 LEU LEU A . n 
A 1 347 ARG 347 263 263 ARG ARG A . n 
A 1 348 ARG 348 264 264 ARG ARG A . n 
A 1 349 PRO 349 265 265 PRO PRO A . n 
A 1 350 GLN 350 266 266 GLN GLN A . n 
A 1 351 LEU 351 267 267 LEU LEU A . n 
A 1 352 ARG 352 268 268 ARG ARG A . n 
A 1 353 LEU 353 269 269 LEU LEU A . n 
A 1 354 TRP 354 270 270 TRP TRP A . n 
A 1 355 SER 355 271 271 SER SER A . n 
A 1 356 LEU 356 272 272 LEU LEU A . n 
A 1 357 TRP 357 273 273 TRP TRP A . n 
A 1 358 TRP 358 274 274 TRP TRP A . n 
A 1 359 VAL 359 275 275 VAL VAL A . n 
A 1 360 PHE 360 276 276 PHE PHE A . n 
A 1 361 ASN 361 277 277 ASN ASN A . n 
A 1 362 SER 362 278 278 SER SER A . n 
A 1 363 ALA 363 279 279 ALA ALA A . n 
A 1 364 GLY 364 280 280 GLY GLY A . n 
A 1 365 TYR 365 281 281 TYR TYR A . n 
A 1 366 TYR 366 282 282 TYR TYR A . n 
A 1 367 LEU 367 283 283 LEU LEU A . n 
A 1 368 VAL 368 284 284 VAL VAL A . n 
A 1 369 VAL 369 285 285 VAL VAL A . n 
A 1 370 TYR 370 286 286 TYR TYR A . n 
A 1 371 TYR 371 287 287 TYR TYR A . n 
A 1 372 VAL 372 288 288 VAL VAL A . n 
A 1 373 HIS 373 289 289 HIS HIS A . n 
A 1 374 ILE 374 290 290 ILE ILE A . n 
A 1 375 LEU 375 291 291 LEU LEU A . n 
A 1 376 TRP 376 292 292 TRP TRP A . n 
A 1 377 ASN 377 293 293 ASN ASN A . n 
A 1 378 GLU 378 294 294 GLU GLU A . n 
A 1 379 VAL 379 295 295 VAL VAL A . n 
A 1 380 ASP 380 296 ?   ?   ?   A . n 
A 1 381 PRO 381 297 ?   ?   ?   A . n 
A 1 382 THR 382 298 ?   ?   ?   A . n 
A 1 383 THR 383 299 ?   ?   ?   A . n 
A 1 384 ASN 384 300 ?   ?   ?   A . n 
A 1 385 SER 385 301 ?   ?   ?   A . n 
A 1 386 ALA 386 302 ?   ?   ?   A . n 
A 1 387 ARG 387 303 303 ARG ARG A . n 
A 1 388 VAL 388 304 304 VAL VAL A . n 
A 1 389 TYR 389 305 305 TYR TYR A . n 
A 1 390 ASN 390 306 306 ASN ASN A . n 
A 1 391 PHE 391 307 307 PHE PHE A . n 
A 1 392 ALA 392 308 308 ALA ALA A . n 
A 1 393 ALA 393 309 309 ALA ALA A . n 
A 1 394 ASP 394 310 310 ASP ASP A . n 
A 1 395 ALA 395 311 311 ALA ALA A . n 
A 1 396 ALA 396 312 312 ALA ALA A . n 
A 1 397 SER 397 313 313 SER SER A . n 
A 1 398 THR 398 314 314 THR THR A . n 
A 1 399 LEU 399 315 315 LEU LEU A . n 
A 1 400 LEU 400 316 316 LEU LEU A . n 
A 1 401 GLY 401 317 317 GLY GLY A . n 
A 1 402 ALA 402 318 318 ALA ALA A . n 
A 1 403 ILE 403 319 319 ILE ILE A . n 
A 1 404 THR 404 320 320 THR THR A . n 
A 1 405 SER 405 321 321 SER SER A . n 
A 1 406 PHE 406 322 322 PHE PHE A . n 
A 1 407 ALA 407 323 323 ALA ALA A . n 
A 1 408 ALA 408 324 324 ALA ALA A . n 
A 1 409 GLY 409 325 325 GLY GLY A . n 
A 1 410 PHE 410 326 326 PHE PHE A . n 
A 1 411 VAL 411 327 327 VAL VAL A . n 
A 1 412 LYS 412 328 328 LYS LYS A . n 
A 1 413 ILE 413 329 329 ILE ILE A . n 
A 1 414 ARG 414 330 330 ARG ARG A . n 
A 1 415 TRP 415 331 331 TRP TRP A . n 
A 1 416 ALA 416 332 332 ALA ALA A . n 
A 1 417 ARG 417 333 333 ARG ARG A . n 
A 1 418 TRP 418 334 334 TRP TRP A . n 
A 1 419 SER 419 335 335 SER SER A . n 
A 1 420 LYS 420 336 336 LYS LYS A . n 
A 1 421 LEU 421 337 337 LEU LEU A . n 
A 1 422 LEU 422 338 338 LEU LEU A . n 
A 1 423 ILE 423 339 339 ILE ILE A . n 
A 1 424 ALA 424 340 340 ALA ALA A . n 
A 1 425 GLY 425 341 341 GLY GLY A . n 
A 1 426 VAL 426 342 342 VAL VAL A . n 
A 1 427 THR 427 343 343 THR THR A . n 
A 1 428 ALA 428 344 344 ALA ALA A . n 
A 1 429 THR 429 345 345 THR THR A . n 
A 1 430 GLN 430 346 346 GLN GLN A . n 
A 1 431 ALA 431 347 347 ALA ALA A . n 
A 1 432 GLY 432 348 348 GLY GLY A . n 
A 1 433 LEU 433 349 349 LEU LEU A . n 
A 1 434 VAL 434 350 350 VAL VAL A . n 
A 1 435 PHE 435 351 351 PHE PHE A . n 
A 1 436 LEU 436 352 352 LEU LEU A . n 
A 1 437 LEU 437 353 353 LEU LEU A . n 
A 1 438 ALA 438 354 354 ALA ALA A . n 
A 1 439 HIS 439 355 355 HIS HIS A . n 
A 1 440 THR 440 356 356 THR THR A . n 
A 1 441 ARG 441 357 357 ARG ARG A . n 
A 1 442 HIS 442 358 358 HIS HIS A . n 
A 1 443 PRO 443 359 359 PRO PRO A . n 
A 1 444 SER 444 360 360 SER SER A . n 
A 1 445 SER 445 361 361 SER SER A . n 
A 1 446 ILE 446 362 362 ILE ILE A . n 
A 1 447 TRP 447 363 363 TRP TRP A . n 
A 1 448 LEU 448 364 364 LEU LEU A . n 
A 1 449 CYS 449 365 365 CYS CYS A . n 
A 1 450 TYR 450 366 366 TYR TYR A . n 
A 1 451 ALA 451 367 367 ALA ALA A . n 
A 1 452 ALA 452 368 368 ALA ALA A . n 
A 1 453 PHE 453 369 369 PHE PHE A . n 
A 1 454 VAL 454 370 370 VAL VAL A . n 
A 1 455 LEU 455 371 371 LEU LEU A . n 
A 1 456 PHE 456 372 372 PHE PHE A . n 
A 1 457 ARG 457 373 373 ARG ARG A . n 
A 1 458 GLY 458 374 374 GLY GLY A . n 
A 1 459 SER 459 375 375 SER SER A . n 
A 1 460 TYR 460 376 376 TYR TYR A . n 
A 1 461 GLN 461 377 377 GLN GLN A . n 
A 1 462 PHE 462 378 378 PHE PHE A . n 
A 1 463 LEU 463 379 379 LEU LEU A . n 
A 1 464 VAL 464 380 380 VAL VAL A . n 
A 1 465 PRO 465 381 381 PRO PRO A . n 
A 1 466 ILE 466 382 382 ILE ILE A . n 
A 1 467 ALA 467 383 383 ALA ALA A . n 
A 1 468 THR 468 384 384 THR THR A . n 
A 1 469 PHE 469 385 385 PHE PHE A . n 
A 1 470 GLN 470 386 386 GLN GLN A . n 
A 1 471 ILE 471 387 387 ILE ILE A . n 
A 1 472 ALA 472 388 388 ALA ALA A . n 
A 1 473 SER 473 389 389 SER SER A . n 
A 1 474 SER 474 390 390 SER SER A . n 
A 1 475 LEU 475 391 391 LEU LEU A . n 
A 1 476 SER 476 392 392 SER SER A . n 
A 1 477 LYS 477 393 393 LYS LYS A . n 
A 1 478 GLU 478 394 394 GLU GLU A . n 
A 1 479 LEU 479 395 395 LEU LEU A . n 
A 1 480 CYS 480 396 396 CYS CYS A . n 
A 1 481 ALA 481 397 397 ALA ALA A . n 
A 1 482 LEU 482 398 398 LEU LEU A . n 
A 1 483 VAL 483 399 399 VAL VAL A . n 
A 1 484 PHE 484 400 400 PHE PHE A . n 
A 1 485 GLY 485 401 401 GLY GLY A . n 
A 1 486 VAL 486 402 402 VAL VAL A . n 
A 1 487 ASN 487 403 403 ASN ASN A . n 
A 1 488 THR 488 404 404 THR THR A . n 
A 1 489 PHE 489 405 405 PHE PHE A . n 
A 1 490 PHE 490 406 406 PHE PHE A . n 
A 1 491 ALA 491 407 407 ALA ALA A . n 
A 1 492 THR 492 408 408 THR THR A . n 
A 1 493 ILE 493 409 409 ILE ILE A . n 
A 1 494 VAL 494 410 410 VAL VAL A . n 
A 1 495 LYS 495 411 411 LYS LYS A . n 
A 1 496 THR 496 412 412 THR THR A . n 
A 1 497 ILE 497 413 413 ILE ILE A . n 
A 1 498 ILE 498 414 414 ILE ILE A . n 
A 1 499 THR 499 415 415 THR THR A . n 
A 1 500 PHE 500 416 416 PHE PHE A . n 
A 1 501 ILE 501 417 417 ILE ILE A . n 
A 1 502 VAL 502 418 418 VAL VAL A . n 
A 1 503 SER 503 419 419 SER SER A . n 
A 1 504 ASP 504 420 420 ASP ASP A . n 
A 1 505 VAL 505 421 421 VAL VAL A . n 
A 1 506 ARG 506 422 422 ARG ARG A . n 
A 1 507 GLY 507 423 423 GLY GLY A . n 
A 1 508 LEU 508 424 424 LEU LEU A . n 
A 1 509 GLY 509 425 425 GLY GLY A . n 
A 1 510 LEU 510 426 426 LEU LEU A . n 
A 1 511 PRO 511 427 427 PRO PRO A . n 
A 1 512 VAL 512 428 428 VAL VAL A . n 
A 1 513 ARG 513 429 429 ARG ARG A . n 
A 1 514 LYS 514 430 430 LYS LYS A . n 
A 1 515 GLN 515 431 431 GLN GLN A . n 
A 1 516 PHE 516 432 432 PHE PHE A . n 
A 1 517 GLN 517 433 433 GLN GLN A . n 
A 1 518 LEU 518 434 434 LEU LEU A . n 
A 1 519 TYR 519 435 435 TYR TYR A . n 
A 1 520 SER 520 436 436 SER SER A . n 
A 1 521 VAL 521 437 437 VAL VAL A . n 
A 1 522 TYR 522 438 438 TYR TYR A . n 
A 1 523 PHE 523 439 439 PHE PHE A . n 
A 1 524 LEU 524 440 440 LEU LEU A . n 
A 1 525 ILE 525 441 441 ILE ILE A . n 
A 1 526 LEU 526 442 442 LEU LEU A . n 
A 1 527 SER 527 443 443 SER SER A . n 
A 1 528 ILE 528 444 444 ILE ILE A . n 
A 1 529 ILE 529 445 445 ILE ILE A . n 
A 1 530 TYR 530 446 446 TYR TYR A . n 
A 1 531 PHE 531 447 447 PHE PHE A . n 
A 1 532 LEU 532 448 448 LEU LEU A . n 
A 1 533 GLY 533 449 449 GLY GLY A . n 
A 1 534 ALA 534 450 450 ALA ALA A . n 
A 1 535 MET 535 451 451 MET MET A . n 
A 1 536 LEU 536 452 452 LEU LEU A . n 
A 1 537 ASP 537 453 453 ASP ASP A . n 
A 1 538 GLY 538 454 454 GLY GLY A . n 
A 1 539 LEU 539 455 455 LEU LEU A . n 
A 1 540 ARG 540 456 456 ARG ARG A . n 
A 1 541 HIS 541 457 457 HIS HIS A . n 
A 1 542 ALA 542 458 ?   ?   ?   A . n 
A 1 543 GLU 543 459 ?   ?   ?   A . n 
A 1 544 GLU 544 460 ?   ?   ?   A . n 
A 1 545 GLU 545 461 ?   ?   ?   A . n 
A 1 546 LYS 546 462 ?   ?   ?   A . n 
A 1 547 ARG 547 463 ?   ?   ?   A . n 
A 1 548 LYS 548 464 ?   ?   ?   A . n 
A 1 549 ALA 549 465 ?   ?   ?   A . n 
A 1 550 GLU 550 466 ?   ?   ?   A . n 
A 1 551 GLU 551 467 ?   ?   ?   A . n 
A 1 552 GLU 552 468 ?   ?   ?   A . n 
A 1 553 LYS 553 469 ?   ?   ?   A . n 
A 1 554 ARG 554 470 ?   ?   ?   A . n 
A 1 555 LYS 555 471 ?   ?   ?   A . n 
A 1 556 GLY 556 472 ?   ?   ?   A . n 
A 1 557 SER 557 473 ?   ?   ?   A . n 
A 1 558 GLY 558 474 ?   ?   ?   A . n 
A 1 559 SER 559 475 ?   ?   ?   A . n 
A 1 560 GLN 560 476 ?   ?   ?   A . n 
A 1 561 VAL 561 477 ?   ?   ?   A . n 
A 1 562 GLN 562 478 ?   ?   ?   A . n 
A 1 563 LEU 563 479 ?   ?   ?   A . n 
A 1 564 GLN 564 480 ?   ?   ?   A . n 
A 1 565 GLU 565 481 ?   ?   ?   A . n 
A 1 566 SER 566 482 ?   ?   ?   A . n 
A 1 567 GLY 567 483 ?   ?   ?   A . n 
A 1 568 GLY 568 484 ?   ?   ?   A . n 
A 1 569 GLY 569 485 ?   ?   ?   A . n 
A 1 570 LEU 570 486 ?   ?   ?   A . n 
A 1 571 VAL 571 487 ?   ?   ?   A . n 
A 1 572 GLN 572 488 ?   ?   ?   A . n 
A 1 573 PRO 573 489 ?   ?   ?   A . n 
A 1 574 GLY 574 490 ?   ?   ?   A . n 
A 1 575 GLY 575 491 ?   ?   ?   A . n 
A 1 576 SER 576 492 ?   ?   ?   A . n 
A 1 577 LEU 577 493 ?   ?   ?   A . n 
A 1 578 ARG 578 494 ?   ?   ?   A . n 
A 1 579 LEU 579 495 ?   ?   ?   A . n 
A 1 580 SER 580 496 ?   ?   ?   A . n 
A 1 581 CYS 581 497 ?   ?   ?   A . n 
A 1 582 ALA 582 498 ?   ?   ?   A . n 
A 1 583 ALA 583 499 ?   ?   ?   A . n 
A 1 584 SER 584 500 ?   ?   ?   A . n 
A 1 585 GLY 585 501 ?   ?   ?   A . n 
A 1 586 ARG 586 502 ?   ?   ?   A . n 
A 1 587 THR 587 503 ?   ?   ?   A . n 
A 1 588 ILE 588 504 ?   ?   ?   A . n 
A 1 589 SER 589 505 ?   ?   ?   A . n 
A 1 590 ARG 590 506 ?   ?   ?   A . n 
A 1 591 TYR 591 507 ?   ?   ?   A . n 
A 1 592 ALA 592 508 ?   ?   ?   A . n 
A 1 593 MET 593 509 ?   ?   ?   A . n 
A 1 594 SER 594 510 ?   ?   ?   A . n 
A 1 595 TRP 595 511 ?   ?   ?   A . n 
A 1 596 PHE 596 512 ?   ?   ?   A . n 
A 1 597 ARG 597 513 ?   ?   ?   A . n 
A 1 598 GLN 598 514 ?   ?   ?   A . n 
A 1 599 ALA 599 515 ?   ?   ?   A . n 
A 1 600 PRO 600 516 ?   ?   ?   A . n 
A 1 601 GLY 601 517 ?   ?   ?   A . n 
A 1 602 LYS 602 518 ?   ?   ?   A . n 
A 1 603 GLU 603 519 ?   ?   ?   A . n 
A 1 604 ARG 604 520 ?   ?   ?   A . n 
A 1 605 GLU 605 521 ?   ?   ?   A . n 
A 1 606 PHE 606 522 ?   ?   ?   A . n 
A 1 607 VAL 607 523 ?   ?   ?   A . n 
A 1 608 ALA 608 524 ?   ?   ?   A . n 
A 1 609 VAL 609 525 ?   ?   ?   A . n 
A 1 610 ALA 610 526 ?   ?   ?   A . n 
A 1 611 ARG 611 527 ?   ?   ?   A . n 
A 1 612 ARG 612 528 ?   ?   ?   A . n 
A 1 613 SER 613 529 ?   ?   ?   A . n 
A 1 614 GLY 614 530 ?   ?   ?   A . n 
A 1 615 ASP 615 531 ?   ?   ?   A . n 
A 1 616 GLY 616 532 ?   ?   ?   A . n 
A 1 617 ALA 617 533 ?   ?   ?   A . n 
A 1 618 PHE 618 534 ?   ?   ?   A . n 
A 1 619 TYR 619 535 ?   ?   ?   A . n 
A 1 620 ALA 620 536 ?   ?   ?   A . n 
A 1 621 ASP 621 537 ?   ?   ?   A . n 
A 1 622 SER 622 538 ?   ?   ?   A . n 
A 1 623 VAL 623 539 ?   ?   ?   A . n 
A 1 624 GLN 624 540 ?   ?   ?   A . n 
A 1 625 GLY 625 541 ?   ?   ?   A . n 
A 1 626 ARG 626 542 ?   ?   ?   A . n 
A 1 627 PHE 627 543 ?   ?   ?   A . n 
A 1 628 THR 628 544 ?   ?   ?   A . n 
A 1 629 VAL 629 545 ?   ?   ?   A . n 
A 1 630 SER 630 546 ?   ?   ?   A . n 
A 1 631 ARG 631 547 ?   ?   ?   A . n 
A 1 632 ASP 632 548 ?   ?   ?   A . n 
A 1 633 ASP 633 549 ?   ?   ?   A . n 
A 1 634 ALA 634 550 ?   ?   ?   A . n 
A 1 635 LYS 635 551 ?   ?   ?   A . n 
A 1 636 ASN 636 552 ?   ?   ?   A . n 
A 1 637 THR 637 553 ?   ?   ?   A . n 
A 1 638 VAL 638 554 ?   ?   ?   A . n 
A 1 639 TYR 639 555 ?   ?   ?   A . n 
A 1 640 LEU 640 556 ?   ?   ?   A . n 
A 1 641 GLN 641 557 ?   ?   ?   A . n 
A 1 642 MET 642 558 ?   ?   ?   A . n 
A 1 643 ASN 643 559 ?   ?   ?   A . n 
A 1 644 SER 644 560 ?   ?   ?   A . n 
A 1 645 LEU 645 561 ?   ?   ?   A . n 
A 1 646 LYS 646 562 ?   ?   ?   A . n 
A 1 647 PRO 647 563 ?   ?   ?   A . n 
A 1 648 GLU 648 564 ?   ?   ?   A . n 
A 1 649 ASP 649 565 ?   ?   ?   A . n 
A 1 650 THR 650 566 ?   ?   ?   A . n 
A 1 651 ALA 651 567 ?   ?   ?   A . n 
A 1 652 VAL 652 568 ?   ?   ?   A . n 
A 1 653 TYR 653 569 ?   ?   ?   A . n 
A 1 654 TYR 654 570 ?   ?   ?   A . n 
A 1 655 CYS 655 571 ?   ?   ?   A . n 
A 1 656 ALA 656 572 ?   ?   ?   A . n 
A 1 657 ILE 657 573 ?   ?   ?   A . n 
A 1 658 ASP 658 574 ?   ?   ?   A . n 
A 1 659 SER 659 575 ?   ?   ?   A . n 
A 1 660 ASP 660 576 ?   ?   ?   A . n 
A 1 661 THR 661 577 ?   ?   ?   A . n 
A 1 662 PHE 662 578 ?   ?   ?   A . n 
A 1 663 TYR 663 579 ?   ?   ?   A . n 
A 1 664 SER 664 580 ?   ?   ?   A . n 
A 1 665 GLY 665 581 ?   ?   ?   A . n 
A 1 666 SER 666 582 ?   ?   ?   A . n 
A 1 667 TYR 667 583 ?   ?   ?   A . n 
A 1 668 ASP 668 584 ?   ?   ?   A . n 
A 1 669 TYR 669 585 ?   ?   ?   A . n 
A 1 670 TRP 670 586 ?   ?   ?   A . n 
A 1 671 GLY 671 587 ?   ?   ?   A . n 
A 1 672 GLN 672 588 ?   ?   ?   A . n 
A 1 673 GLY 673 589 ?   ?   ?   A . n 
A 1 674 THR 674 590 ?   ?   ?   A . n 
A 1 675 GLN 675 591 ?   ?   ?   A . n 
A 1 676 VAL 676 592 ?   ?   ?   A . n 
A 1 677 THR 677 593 ?   ?   ?   A . n 
A 1 678 VAL 678 594 ?   ?   ?   A . n 
A 1 679 SER 679 595 ?   ?   ?   A . n 
A 1 680 SER 680 596 ?   ?   ?   A . n 
A 1 681 HIS 681 597 ?   ?   ?   A . n 
A 1 682 HIS 682 598 ?   ?   ?   A . n 
A 1 683 HIS 683 599 ?   ?   ?   A . n 
A 1 684 HIS 684 600 ?   ?   ?   A . n 
A 1 685 HIS 685 601 ?   ?   ?   A . n 
A 1 686 HIS 686 602 ?   ?   ?   A . n 
A 1 687 HIS 687 603 ?   ?   ?   A . n 
A 1 688 HIS 688 604 ?   ?   ?   A . n 
A 1 689 HIS 689 605 ?   ?   ?   A . n 
A 1 690 HIS 690 606 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        COP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   COP 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          COP 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     701 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      COP 
_pdbx_nonpoly_scheme.auth_mon_id     COP 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_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                     9JRL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9JRL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JRL 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9JRL 
_struct.title                        'outward-open hSLC19A1 + PT523' 
_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        9JRL 
_struct_keywords.text            'outward-open hSLC19A1, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP C562_ECOLX  P0ABE7 ? 1 
;ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN
EGKVKEAQAAAEQLKTTRNAYHQKYR
;
23  
2 UNP S19A1_HUMAN P41440 ? 1 
;SWRHLVCYLCFYGFMAQIRPGESFITPYLLGPDKNFTREQVTNEITPVLSYSYLAVLVPVFLLTDYLRYTPVLLLQGLSF
VSVWLLLLLGHSVAHMQLMELFYSVTMAARIAYSSYIFSLVRPARYQRVAGYSRAAVLLGVFTSSVLGQLLVTVGRVSFS
TLNYISLAFLTFSVVLALFLKRPKRSLFFNRDDRGRCETSASELERMNPGPGGKLGHALRVACGDSVLARMLRELGDSLR
RPQLRLWSLWWVFNSAGYYLVVYYVHILWNEVDPTTNSARVYNGAADAASTLLGAITSFAAGFVKIRWARWSKLLIAGVT
ATQAGLVFLLAHTRHPSSIWLCYAAFVLFRGSYQFLVPIATFQIASSLSKELCALVFGVNTFFATIVKTIITFIVSDVRG
LGLPVRKQFQLYSVYFLILSIIYFLGAMLDGLRH
;
24  
3 PDB 9JRL        9JRL   ? 1 ? 542 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JRL A 2   ? 107 ? P0ABE7 23  ? 128 ? -82 23  
2 2 9JRL A 108 ? 541 ? P41440 24  ? 457 ? 24  457 
3 3 9JRL A 542 ? 690 ? 9JRL   458 ? 606 ? 458 606 
# 
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 9JRL MET A 1   ? UNP P0ABE7 ?   ?   'initiating methionine' -83 1 
1 9JRL TRP A 8   ? UNP P0ABE7 MET 29  conflict                -76 2 
1 9JRL ILE A 103 ? UNP P0ABE7 HIS 124 conflict                19  3 
1 9JRL LEU A 107 ? UNP P0ABE7 ARG 128 conflict                23  4 
2 9JRL GLN A 142 ? UNP P41440 ASN 58  conflict                58  5 
2 9JRL PHE A 391 ? UNP P41440 GLY 307 conflict                307 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 TRP A 109 ? GLN A 124 ? TRP A 25  GLN A 40  1 ? 16 
HELX_P HELX_P2  AA2 ILE A 125 ? SER A 130 ? ILE A 41  SER A 46  5 ? 6  
HELX_P HELX_P3  AA3 PHE A 131 ? GLY A 138 ? PHE A 47  GLY A 54  1 ? 8  
HELX_P HELX_P4  AA4 THR A 144 ? ILE A 152 ? THR A 60  ILE A 68  1 ? 9  
HELX_P HELX_P5  AA5 ILE A 152 ? THR A 171 ? ILE A 68  THR A 87  1 ? 20 
HELX_P HELX_P6  AA6 ARG A 175 ? LEU A 196 ? ARG A 91  LEU A 112 1 ? 22 
HELX_P HELX_P7  AA7 SER A 199 ? ALA A 215 ? SER A 115 ALA A 131 1 ? 17 
HELX_P HELX_P8  AA8 ALA A 216 ? LEU A 227 ? ALA A 132 LEU A 143 1 ? 12 
HELX_P HELX_P9  AA9 ARG A 229 ? ALA A 231 ? ARG A 145 ALA A 147 5 ? 3  
HELX_P HELX_P10 AB1 ARG A 232 ? VAL A 261 ? ARG A 148 VAL A 177 1 ? 30 
HELX_P HELX_P11 AB2 SER A 265 ? PHE A 286 ? SER A 181 PHE A 202 1 ? 22 
HELX_P HELX_P12 AB3 VAL A 334 ? ARG A 347 ? VAL A 250 ARG A 263 1 ? 14 
HELX_P HELX_P13 AB4 ARG A 348 ? VAL A 379 ? ARG A 264 VAL A 295 1 ? 32 
HELX_P HELX_P14 AB5 VAL A 388 ? VAL A 411 ? VAL A 304 VAL A 327 1 ? 24 
HELX_P HELX_P15 AB6 SER A 419 ? THR A 440 ? SER A 335 THR A 356 1 ? 22 
HELX_P HELX_P16 AB7 HIS A 442 ? SER A 444 ? HIS A 358 SER A 360 5 ? 3  
HELX_P HELX_P17 AB8 SER A 445 ? SER A 474 ? SER A 361 SER A 390 1 ? 30 
HELX_P HELX_P18 AB9 LEU A 475 ? GLU A 478 ? LEU A 391 GLU A 394 5 ? 4  
HELX_P HELX_P19 AC1 LEU A 479 ? VAL A 502 ? LEU A 395 VAL A 418 1 ? 24 
HELX_P HELX_P20 AC2 PRO A 511 ? ARG A 540 ? PRO A 427 ARG A 456 1 ? 30 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9JRL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 55  ? ? -83.39  40.37   
2 1 ILE A 68  ? ? -126.48 -55.60  
3 1 ARG A 91  ? ? 63.35   160.76  
4 1 SER A 360 ? ? -92.57  47.42   
5 1 SER A 361 ? ? -141.00 15.40   
6 1 GLU A 394 ? ? -95.60  58.25   
7 1 ARG A 422 ? ? 51.18   -98.97  
8 1 PRO A 427 ? ? -67.59  -179.66 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9JRL 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9JRL 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.25 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               94583 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'outward-open hSLC19A1 + PT523' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9JRL 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TALOS ARCTICA' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             500 
_em_imaging.nominal_defocus_max             1000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9JRL 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9JRL 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 -83 ? A MET 1   
2   1 Y 1 A ALA -82 ? A ALA 2   
3   1 Y 1 A ASP -81 ? A ASP 3   
4   1 Y 1 A LEU -80 ? A LEU 4   
5   1 Y 1 A GLU -79 ? A GLU 5   
6   1 Y 1 A ASP -78 ? A ASP 6   
7   1 Y 1 A ASN -77 ? A ASN 7   
8   1 Y 1 A TRP -76 ? A TRP 8   
9   1 Y 1 A GLU -75 ? A GLU 9   
10  1 Y 1 A THR -74 ? A THR 10  
11  1 Y 1 A LEU -73 ? A LEU 11  
12  1 Y 1 A ASN -72 ? A ASN 12  
13  1 Y 1 A ASP -71 ? A ASP 13  
14  1 Y 1 A ASN -70 ? A ASN 14  
15  1 Y 1 A LEU -69 ? A LEU 15  
16  1 Y 1 A LYS -68 ? A LYS 16  
17  1 Y 1 A VAL -67 ? A VAL 17  
18  1 Y 1 A ILE -66 ? A ILE 18  
19  1 Y 1 A GLU -65 ? A GLU 19  
20  1 Y 1 A LYS -64 ? A LYS 20  
21  1 Y 1 A ALA -63 ? A ALA 21  
22  1 Y 1 A ASP -62 ? A ASP 22  
23  1 Y 1 A ASN -61 ? A ASN 23  
24  1 Y 1 A ALA -60 ? A ALA 24  
25  1 Y 1 A ALA -59 ? A ALA 25  
26  1 Y 1 A GLN -58 ? A GLN 26  
27  1 Y 1 A VAL -57 ? A VAL 27  
28  1 Y 1 A LYS -56 ? A LYS 28  
29  1 Y 1 A ASP -55 ? A ASP 29  
30  1 Y 1 A ALA -54 ? A ALA 30  
31  1 Y 1 A LEU -53 ? A LEU 31  
32  1 Y 1 A THR -52 ? A THR 32  
33  1 Y 1 A LYS -51 ? A LYS 33  
34  1 Y 1 A MET -50 ? A MET 34  
35  1 Y 1 A ARG -49 ? A ARG 35  
36  1 Y 1 A ALA -48 ? A ALA 36  
37  1 Y 1 A ALA -47 ? A ALA 37  
38  1 Y 1 A ALA -46 ? A ALA 38  
39  1 Y 1 A LEU -45 ? A LEU 39  
40  1 Y 1 A ASP -44 ? A ASP 40  
41  1 Y 1 A ALA -43 ? A ALA 41  
42  1 Y 1 A GLN -42 ? A GLN 42  
43  1 Y 1 A LYS -41 ? A LYS 43  
44  1 Y 1 A ALA -40 ? A ALA 44  
45  1 Y 1 A THR -39 ? A THR 45  
46  1 Y 1 A PRO -38 ? A PRO 46  
47  1 Y 1 A PRO -37 ? A PRO 47  
48  1 Y 1 A LYS -36 ? A LYS 48  
49  1 Y 1 A LEU -35 ? A LEU 49  
50  1 Y 1 A GLU -34 ? A GLU 50  
51  1 Y 1 A ASP -33 ? A ASP 51  
52  1 Y 1 A LYS -32 ? A LYS 52  
53  1 Y 1 A SER -31 ? A SER 53  
54  1 Y 1 A PRO -30 ? A PRO 54  
55  1 Y 1 A ASP -29 ? A ASP 55  
56  1 Y 1 A SER -28 ? A SER 56  
57  1 Y 1 A PRO -27 ? A PRO 57  
58  1 Y 1 A GLU -26 ? A GLU 58  
59  1 Y 1 A MET -25 ? A MET 59  
60  1 Y 1 A LYS -24 ? A LYS 60  
61  1 Y 1 A ASP -23 ? A ASP 61  
62  1 Y 1 A PHE -22 ? A PHE 62  
63  1 Y 1 A ARG -21 ? A ARG 63  
64  1 Y 1 A HIS -20 ? A HIS 64  
65  1 Y 1 A GLY -19 ? A GLY 65  
66  1 Y 1 A PHE -18 ? A PHE 66  
67  1 Y 1 A ASP -17 ? A ASP 67  
68  1 Y 1 A ILE -16 ? A ILE 68  
69  1 Y 1 A LEU -15 ? A LEU 69  
70  1 Y 1 A VAL -14 ? A VAL 70  
71  1 Y 1 A GLY -13 ? A GLY 71  
72  1 Y 1 A GLN -12 ? A GLN 72  
73  1 Y 1 A ILE -11 ? A ILE 73  
74  1 Y 1 A ASP -10 ? A ASP 74  
75  1 Y 1 A ASP -9  ? A ASP 75  
76  1 Y 1 A ALA -8  ? A ALA 76  
77  1 Y 1 A LEU -7  ? A LEU 77  
78  1 Y 1 A LYS -6  ? A LYS 78  
79  1 Y 1 A LEU -5  ? A LEU 79  
80  1 Y 1 A ALA -4  ? A ALA 80  
81  1 Y 1 A ASN -3  ? A ASN 81  
82  1 Y 1 A GLU -2  ? A GLU 82  
83  1 Y 1 A GLY -1  ? A GLY 83  
84  1 Y 1 A LYS 0   ? A LYS 84  
85  1 Y 1 A VAL 1   ? A VAL 85  
86  1 Y 1 A LYS 2   ? A LYS 86  
87  1 Y 1 A GLU 3   ? A GLU 87  
88  1 Y 1 A ALA 4   ? A ALA 88  
89  1 Y 1 A GLN 5   ? A GLN 89  
90  1 Y 1 A ALA 6   ? A ALA 90  
91  1 Y 1 A ALA 7   ? A ALA 91  
92  1 Y 1 A ALA 8   ? A ALA 92  
93  1 Y 1 A GLU 9   ? A GLU 93  
94  1 Y 1 A GLN 10  ? A GLN 94  
95  1 Y 1 A LEU 11  ? A LEU 95  
96  1 Y 1 A LYS 12  ? A LYS 96  
97  1 Y 1 A THR 13  ? A THR 97  
98  1 Y 1 A THR 14  ? A THR 98  
99  1 Y 1 A ARG 15  ? A ARG 99  
100 1 Y 1 A ASN 16  ? A ASN 100 
101 1 Y 1 A ALA 17  ? A ALA 101 
102 1 Y 1 A TYR 18  ? A TYR 102 
103 1 Y 1 A ILE 19  ? A ILE 103 
104 1 Y 1 A GLN 20  ? A GLN 104 
105 1 Y 1 A LYS 21  ? A LYS 105 
106 1 Y 1 A TYR 22  ? A TYR 106 
107 1 Y 1 A LEU 23  ? A LEU 107 
108 1 Y 1 A ARG 208 ? A ARG 292 
109 1 Y 1 A SER 209 ? A SER 293 
110 1 Y 1 A LEU 210 ? A LEU 294 
111 1 Y 1 A PHE 211 ? A PHE 295 
112 1 Y 1 A PHE 212 ? A PHE 296 
113 1 Y 1 A ASN 213 ? A ASN 297 
114 1 Y 1 A ARG 214 ? A ARG 298 
115 1 Y 1 A ASP 215 ? A ASP 299 
116 1 Y 1 A ASP 216 ? A ASP 300 
117 1 Y 1 A ARG 217 ? A ARG 301 
118 1 Y 1 A GLY 218 ? A GLY 302 
119 1 Y 1 A ARG 219 ? A ARG 303 
120 1 Y 1 A CYS 220 ? A CYS 304 
121 1 Y 1 A GLU 221 ? A GLU 305 
122 1 Y 1 A THR 222 ? A THR 306 
123 1 Y 1 A SER 223 ? A SER 307 
124 1 Y 1 A ALA 224 ? A ALA 308 
125 1 Y 1 A SER 225 ? A SER 309 
126 1 Y 1 A GLU 226 ? A GLU 310 
127 1 Y 1 A LEU 227 ? A LEU 311 
128 1 Y 1 A GLU 228 ? A GLU 312 
129 1 Y 1 A ARG 229 ? A ARG 313 
130 1 Y 1 A MET 230 ? A MET 314 
131 1 Y 1 A ASN 231 ? A ASN 315 
132 1 Y 1 A PRO 232 ? A PRO 316 
133 1 Y 1 A GLY 233 ? A GLY 317 
134 1 Y 1 A PRO 234 ? A PRO 318 
135 1 Y 1 A GLY 235 ? A GLY 319 
136 1 Y 1 A GLY 236 ? A GLY 320 
137 1 Y 1 A LYS 237 ? A LYS 321 
138 1 Y 1 A LEU 238 ? A LEU 322 
139 1 Y 1 A GLY 239 ? A GLY 323 
140 1 Y 1 A HIS 240 ? A HIS 324 
141 1 Y 1 A ALA 241 ? A ALA 325 
142 1 Y 1 A LEU 242 ? A LEU 326 
143 1 Y 1 A ARG 243 ? A ARG 327 
144 1 Y 1 A VAL 244 ? A VAL 328 
145 1 Y 1 A ALA 245 ? A ALA 329 
146 1 Y 1 A CYS 246 ? A CYS 330 
147 1 Y 1 A GLY 247 ? A GLY 331 
148 1 Y 1 A ASP 248 ? A ASP 332 
149 1 Y 1 A ASP 296 ? A ASP 380 
150 1 Y 1 A PRO 297 ? A PRO 381 
151 1 Y 1 A THR 298 ? A THR 382 
152 1 Y 1 A THR 299 ? A THR 383 
153 1 Y 1 A ASN 300 ? A ASN 384 
154 1 Y 1 A SER 301 ? A SER 385 
155 1 Y 1 A ALA 302 ? A ALA 386 
156 1 Y 1 A ALA 458 ? A ALA 542 
157 1 Y 1 A GLU 459 ? A GLU 543 
158 1 Y 1 A GLU 460 ? A GLU 544 
159 1 Y 1 A GLU 461 ? A GLU 545 
160 1 Y 1 A LYS 462 ? A LYS 546 
161 1 Y 1 A ARG 463 ? A ARG 547 
162 1 Y 1 A LYS 464 ? A LYS 548 
163 1 Y 1 A ALA 465 ? A ALA 549 
164 1 Y 1 A GLU 466 ? A GLU 550 
165 1 Y 1 A GLU 467 ? A GLU 551 
166 1 Y 1 A GLU 468 ? A GLU 552 
167 1 Y 1 A LYS 469 ? A LYS 553 
168 1 Y 1 A ARG 470 ? A ARG 554 
169 1 Y 1 A LYS 471 ? A LYS 555 
170 1 Y 1 A GLY 472 ? A GLY 556 
171 1 Y 1 A SER 473 ? A SER 557 
172 1 Y 1 A GLY 474 ? A GLY 558 
173 1 Y 1 A SER 475 ? A SER 559 
174 1 Y 1 A GLN 476 ? A GLN 560 
175 1 Y 1 A VAL 477 ? A VAL 561 
176 1 Y 1 A GLN 478 ? A GLN 562 
177 1 Y 1 A LEU 479 ? A LEU 563 
178 1 Y 1 A GLN 480 ? A GLN 564 
179 1 Y 1 A GLU 481 ? A GLU 565 
180 1 Y 1 A SER 482 ? A SER 566 
181 1 Y 1 A GLY 483 ? A GLY 567 
182 1 Y 1 A GLY 484 ? A GLY 568 
183 1 Y 1 A GLY 485 ? A GLY 569 
184 1 Y 1 A LEU 486 ? A LEU 570 
185 1 Y 1 A VAL 487 ? A VAL 571 
186 1 Y 1 A GLN 488 ? A GLN 572 
187 1 Y 1 A PRO 489 ? A PRO 573 
188 1 Y 1 A GLY 490 ? A GLY 574 
189 1 Y 1 A GLY 491 ? A GLY 575 
190 1 Y 1 A SER 492 ? A SER 576 
191 1 Y 1 A LEU 493 ? A LEU 577 
192 1 Y 1 A ARG 494 ? A ARG 578 
193 1 Y 1 A LEU 495 ? A LEU 579 
194 1 Y 1 A SER 496 ? A SER 580 
195 1 Y 1 A CYS 497 ? A CYS 581 
196 1 Y 1 A ALA 498 ? A ALA 582 
197 1 Y 1 A ALA 499 ? A ALA 583 
198 1 Y 1 A SER 500 ? A SER 584 
199 1 Y 1 A GLY 501 ? A GLY 585 
200 1 Y 1 A ARG 502 ? A ARG 586 
201 1 Y 1 A THR 503 ? A THR 587 
202 1 Y 1 A ILE 504 ? A ILE 588 
203 1 Y 1 A SER 505 ? A SER 589 
204 1 Y 1 A ARG 506 ? A ARG 590 
205 1 Y 1 A TYR 507 ? A TYR 591 
206 1 Y 1 A ALA 508 ? A ALA 592 
207 1 Y 1 A MET 509 ? A MET 593 
208 1 Y 1 A SER 510 ? A SER 594 
209 1 Y 1 A TRP 511 ? A TRP 595 
210 1 Y 1 A PHE 512 ? A PHE 596 
211 1 Y 1 A ARG 513 ? A ARG 597 
212 1 Y 1 A GLN 514 ? A GLN 598 
213 1 Y 1 A ALA 515 ? A ALA 599 
214 1 Y 1 A PRO 516 ? A PRO 600 
215 1 Y 1 A GLY 517 ? A GLY 601 
216 1 Y 1 A LYS 518 ? A LYS 602 
217 1 Y 1 A GLU 519 ? A GLU 603 
218 1 Y 1 A ARG 520 ? A ARG 604 
219 1 Y 1 A GLU 521 ? A GLU 605 
220 1 Y 1 A PHE 522 ? A PHE 606 
221 1 Y 1 A VAL 523 ? A VAL 607 
222 1 Y 1 A ALA 524 ? A ALA 608 
223 1 Y 1 A VAL 525 ? A VAL 609 
224 1 Y 1 A ALA 526 ? A ALA 610 
225 1 Y 1 A ARG 527 ? A ARG 611 
226 1 Y 1 A ARG 528 ? A ARG 612 
227 1 Y 1 A SER 529 ? A SER 613 
228 1 Y 1 A GLY 530 ? A GLY 614 
229 1 Y 1 A ASP 531 ? A ASP 615 
230 1 Y 1 A GLY 532 ? A GLY 616 
231 1 Y 1 A ALA 533 ? A ALA 617 
232 1 Y 1 A PHE 534 ? A PHE 618 
233 1 Y 1 A TYR 535 ? A TYR 619 
234 1 Y 1 A ALA 536 ? A ALA 620 
235 1 Y 1 A ASP 537 ? A ASP 621 
236 1 Y 1 A SER 538 ? A SER 622 
237 1 Y 1 A VAL 539 ? A VAL 623 
238 1 Y 1 A GLN 540 ? A GLN 624 
239 1 Y 1 A GLY 541 ? A GLY 625 
240 1 Y 1 A ARG 542 ? A ARG 626 
241 1 Y 1 A PHE 543 ? A PHE 627 
242 1 Y 1 A THR 544 ? A THR 628 
243 1 Y 1 A VAL 545 ? A VAL 629 
244 1 Y 1 A SER 546 ? A SER 630 
245 1 Y 1 A ARG 547 ? A ARG 631 
246 1 Y 1 A ASP 548 ? A ASP 632 
247 1 Y 1 A ASP 549 ? A ASP 633 
248 1 Y 1 A ALA 550 ? A ALA 634 
249 1 Y 1 A LYS 551 ? A LYS 635 
250 1 Y 1 A ASN 552 ? A ASN 636 
251 1 Y 1 A THR 553 ? A THR 637 
252 1 Y 1 A VAL 554 ? A VAL 638 
253 1 Y 1 A TYR 555 ? A TYR 639 
254 1 Y 1 A LEU 556 ? A LEU 640 
255 1 Y 1 A GLN 557 ? A GLN 641 
256 1 Y 1 A MET 558 ? A MET 642 
257 1 Y 1 A ASN 559 ? A ASN 643 
258 1 Y 1 A SER 560 ? A SER 644 
259 1 Y 1 A LEU 561 ? A LEU 645 
260 1 Y 1 A LYS 562 ? A LYS 646 
261 1 Y 1 A PRO 563 ? A PRO 647 
262 1 Y 1 A GLU 564 ? A GLU 648 
263 1 Y 1 A ASP 565 ? A ASP 649 
264 1 Y 1 A THR 566 ? A THR 650 
265 1 Y 1 A ALA 567 ? A ALA 651 
266 1 Y 1 A VAL 568 ? A VAL 652 
267 1 Y 1 A TYR 569 ? A TYR 653 
268 1 Y 1 A TYR 570 ? A TYR 654 
269 1 Y 1 A CYS 571 ? A CYS 655 
270 1 Y 1 A ALA 572 ? A ALA 656 
271 1 Y 1 A ILE 573 ? A ILE 657 
272 1 Y 1 A ASP 574 ? A ASP 658 
273 1 Y 1 A SER 575 ? A SER 659 
274 1 Y 1 A ASP 576 ? A ASP 660 
275 1 Y 1 A THR 577 ? A THR 661 
276 1 Y 1 A PHE 578 ? A PHE 662 
277 1 Y 1 A TYR 579 ? A TYR 663 
278 1 Y 1 A SER 580 ? A SER 664 
279 1 Y 1 A GLY 581 ? A GLY 665 
280 1 Y 1 A SER 582 ? A SER 666 
281 1 Y 1 A TYR 583 ? A TYR 667 
282 1 Y 1 A ASP 584 ? A ASP 668 
283 1 Y 1 A TYR 585 ? A TYR 669 
284 1 Y 1 A TRP 586 ? A TRP 670 
285 1 Y 1 A GLY 587 ? A GLY 671 
286 1 Y 1 A GLN 588 ? A GLN 672 
287 1 Y 1 A GLY 589 ? A GLY 673 
288 1 Y 1 A THR 590 ? A THR 674 
289 1 Y 1 A GLN 591 ? A GLN 675 
290 1 Y 1 A VAL 592 ? A VAL 676 
291 1 Y 1 A THR 593 ? A THR 677 
292 1 Y 1 A VAL 594 ? A VAL 678 
293 1 Y 1 A SER 595 ? A SER 679 
294 1 Y 1 A SER 596 ? A SER 680 
295 1 Y 1 A HIS 597 ? A HIS 681 
296 1 Y 1 A HIS 598 ? A HIS 682 
297 1 Y 1 A HIS 599 ? A HIS 683 
298 1 Y 1 A HIS 600 ? A HIS 684 
299 1 Y 1 A HIS 601 ? A HIS 685 
300 1 Y 1 A HIS 602 ? A HIS 686 
301 1 Y 1 A HIS 603 ? A HIS 687 
302 1 Y 1 A HIS 604 ? A HIS 688 
303 1 Y 1 A HIS 605 ? A HIS 689 
304 1 Y 1 A HIS 606 ? A HIS 690 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
COP C3   C Y N 74  
COP C1   C Y N 75  
COP C10  C Y N 76  
COP C8   C Y N 77  
COP C7   C Y N 78  
COP C5   C Y N 79  
COP C11  C N N 80  
COP C13  C Y N 81  
COP C18  C Y N 82  
COP C17  C Y N 83  
COP C16  C Y N 84  
COP C15  C Y N 85  
COP C14  C Y N 86  
COP C19  C N N 87  
COP C21  C N S 88  
COP C24  C N N 89  
COP C27  C N N 90  
COP C28  C N N 91  
COP C29  C N N 92  
COP N4   N Y N 93  
COP N3   N N N 94  
COP N2   N Y N 95  
COP N1   N N N 96  
COP N9   N Y N 97  
COP N6   N Y N 98  
COP N12  N N N 99  
COP N20  N N N 100 
COP O19  O N N 101 
COP O24  O N N 102 
COP O25  O N N 103 
COP N30  N N N 104 
COP C31  C N N 105 
COP O32  O N N 106 
COP C33  C Y N 107 
COP C38  C Y N 108 
COP C37  C Y N 109 
COP C36  C Y N 110 
COP C35  C Y N 111 
COP C34  C Y N 112 
COP C39  C N N 113 
COP O40  O N N 114 
COP O41  O N N 115 
COP H7   H N N 116 
COP H111 H N N 117 
COP H112 H N N 118 
COP H18  H N N 119 
COP H17  H N N 120 
COP H15  H N N 121 
COP H14  H N N 122 
COP H21  H N N 123 
COP H271 H N N 124 
COP H272 H N N 125 
COP H281 H N N 126 
COP H282 H N N 127 
COP H291 H N N 128 
COP H292 H N N 129 
COP HN31 H N N 130 
COP HN32 H N N 131 
COP HN11 H N N 132 
COP HN12 H N N 133 
COP HN2  H N N 134 
COP HN0  H N N 135 
COP HO5  H N N 136 
COP HN3  H N N 137 
COP H37  H N N 138 
COP H36  H N N 139 
COP H35  H N N 140 
COP H34  H N N 141 
COP HO1  H N N 142 
CYS N    N N N 143 
CYS CA   C N R 144 
CYS C    C N N 145 
CYS O    O N N 146 
CYS CB   C N N 147 
CYS SG   S N N 148 
CYS OXT  O N N 149 
CYS H    H N N 150 
CYS H2   H N N 151 
CYS HA   H N N 152 
CYS HB2  H N N 153 
CYS HB3  H N N 154 
CYS HG   H N N 155 
CYS HXT  H N N 156 
GLN N    N N N 157 
GLN CA   C N S 158 
GLN C    C N N 159 
GLN O    O N N 160 
GLN CB   C N N 161 
GLN CG   C N N 162 
GLN CD   C N N 163 
GLN OE1  O N N 164 
GLN NE2  N N N 165 
GLN OXT  O N N 166 
GLN H    H N N 167 
GLN H2   H N N 168 
GLN HA   H N N 169 
GLN HB2  H N N 170 
GLN HB3  H N N 171 
GLN HG2  H N N 172 
GLN HG3  H N N 173 
GLN HE21 H N N 174 
GLN HE22 H N N 175 
GLN HXT  H N N 176 
GLU N    N N N 177 
GLU CA   C N S 178 
GLU C    C N N 179 
GLU O    O N N 180 
GLU CB   C N N 181 
GLU CG   C N N 182 
GLU CD   C N N 183 
GLU OE1  O N N 184 
GLU OE2  O N N 185 
GLU OXT  O N N 186 
GLU H    H N N 187 
GLU H2   H N N 188 
GLU HA   H N N 189 
GLU HB2  H N N 190 
GLU HB3  H N N 191 
GLU HG2  H N N 192 
GLU HG3  H N N 193 
GLU HE2  H N N 194 
GLU HXT  H N N 195 
GLY N    N N N 196 
GLY CA   C N N 197 
GLY C    C N N 198 
GLY O    O N N 199 
GLY OXT  O N N 200 
GLY H    H N N 201 
GLY H2   H N N 202 
GLY HA2  H N N 203 
GLY HA3  H N N 204 
GLY HXT  H N N 205 
HIS N    N N N 206 
HIS CA   C N S 207 
HIS C    C N N 208 
HIS O    O N N 209 
HIS CB   C N N 210 
HIS CG   C Y N 211 
HIS ND1  N Y N 212 
HIS CD2  C Y N 213 
HIS CE1  C Y N 214 
HIS NE2  N Y N 215 
HIS OXT  O N N 216 
HIS H    H N N 217 
HIS H2   H N N 218 
HIS HA   H N N 219 
HIS HB2  H N N 220 
HIS HB3  H N N 221 
HIS HD1  H N N 222 
HIS HD2  H N N 223 
HIS HE1  H N N 224 
HIS HE2  H N N 225 
HIS HXT  H N N 226 
ILE N    N N N 227 
ILE CA   C N S 228 
ILE C    C N N 229 
ILE O    O N N 230 
ILE CB   C N S 231 
ILE CG1  C N N 232 
ILE CG2  C N N 233 
ILE CD1  C N N 234 
ILE OXT  O N N 235 
ILE H    H N N 236 
ILE H2   H N N 237 
ILE HA   H N N 238 
ILE HB   H N N 239 
ILE HG12 H N N 240 
ILE HG13 H N N 241 
ILE HG21 H N N 242 
ILE HG22 H N N 243 
ILE HG23 H N N 244 
ILE HD11 H N N 245 
ILE HD12 H N N 246 
ILE HD13 H N N 247 
ILE HXT  H N N 248 
LEU N    N N N 249 
LEU CA   C N S 250 
LEU C    C N N 251 
LEU O    O N N 252 
LEU CB   C N N 253 
LEU CG   C N N 254 
LEU CD1  C N N 255 
LEU CD2  C N N 256 
LEU OXT  O N N 257 
LEU H    H N N 258 
LEU H2   H N N 259 
LEU HA   H N N 260 
LEU HB2  H N N 261 
LEU HB3  H N N 262 
LEU HG   H N N 263 
LEU HD11 H N N 264 
LEU HD12 H N N 265 
LEU HD13 H N N 266 
LEU HD21 H N N 267 
LEU HD22 H N N 268 
LEU HD23 H N N 269 
LEU HXT  H N N 270 
LYS N    N N N 271 
LYS CA   C N S 272 
LYS C    C N N 273 
LYS O    O N N 274 
LYS CB   C N N 275 
LYS CG   C N N 276 
LYS CD   C N N 277 
LYS CE   C N N 278 
LYS NZ   N N N 279 
LYS OXT  O N N 280 
LYS H    H N N 281 
LYS H2   H N N 282 
LYS HA   H N N 283 
LYS HB2  H N N 284 
LYS HB3  H N N 285 
LYS HG2  H N N 286 
LYS HG3  H N N 287 
LYS HD2  H N N 288 
LYS HD3  H N N 289 
LYS HE2  H N N 290 
LYS HE3  H N N 291 
LYS HZ1  H N N 292 
LYS HZ2  H N N 293 
LYS HZ3  H N N 294 
LYS HXT  H N N 295 
MET N    N N N 296 
MET CA   C N S 297 
MET C    C N N 298 
MET O    O N N 299 
MET CB   C N N 300 
MET CG   C N N 301 
MET SD   S N N 302 
MET CE   C N N 303 
MET OXT  O N N 304 
MET H    H N N 305 
MET H2   H N N 306 
MET HA   H N N 307 
MET HB2  H N N 308 
MET HB3  H N N 309 
MET HG2  H N N 310 
MET HG3  H N N 311 
MET HE1  H N N 312 
MET HE2  H N N 313 
MET HE3  H N N 314 
MET HXT  H N N 315 
PHE N    N N N 316 
PHE CA   C N S 317 
PHE C    C N N 318 
PHE O    O N N 319 
PHE CB   C N N 320 
PHE CG   C Y N 321 
PHE CD1  C Y N 322 
PHE CD2  C Y N 323 
PHE CE1  C Y N 324 
PHE CE2  C Y N 325 
PHE CZ   C Y N 326 
PHE OXT  O N N 327 
PHE H    H N N 328 
PHE H2   H N N 329 
PHE HA   H N N 330 
PHE HB2  H N N 331 
PHE HB3  H N N 332 
PHE HD1  H N N 333 
PHE HD2  H N N 334 
PHE HE1  H N N 335 
PHE HE2  H N N 336 
PHE HZ   H N N 337 
PHE HXT  H N N 338 
PRO N    N N N 339 
PRO CA   C N S 340 
PRO C    C N N 341 
PRO O    O N N 342 
PRO CB   C N N 343 
PRO CG   C N N 344 
PRO CD   C N N 345 
PRO OXT  O N N 346 
PRO H    H N N 347 
PRO HA   H N N 348 
PRO HB2  H N N 349 
PRO HB3  H N N 350 
PRO HG2  H N N 351 
PRO HG3  H N N 352 
PRO HD2  H N N 353 
PRO HD3  H N N 354 
PRO HXT  H N N 355 
SER N    N N N 356 
SER CA   C N S 357 
SER C    C N N 358 
SER O    O N N 359 
SER CB   C N N 360 
SER OG   O N N 361 
SER OXT  O N N 362 
SER H    H N N 363 
SER H2   H N N 364 
SER HA   H N N 365 
SER HB2  H N N 366 
SER HB3  H N N 367 
SER HG   H N N 368 
SER HXT  H N N 369 
THR N    N N N 370 
THR CA   C N S 371 
THR C    C N N 372 
THR O    O N N 373 
THR CB   C N R 374 
THR OG1  O N N 375 
THR CG2  C N N 376 
THR OXT  O N N 377 
THR H    H N N 378 
THR H2   H N N 379 
THR HA   H N N 380 
THR HB   H N N 381 
THR HG1  H N N 382 
THR HG21 H N N 383 
THR HG22 H N N 384 
THR HG23 H N N 385 
THR HXT  H N N 386 
TRP N    N N N 387 
TRP CA   C N S 388 
TRP C    C N N 389 
TRP O    O N N 390 
TRP CB   C N N 391 
TRP CG   C Y N 392 
TRP CD1  C Y N 393 
TRP CD2  C Y N 394 
TRP NE1  N Y N 395 
TRP CE2  C Y N 396 
TRP CE3  C Y N 397 
TRP CZ2  C Y N 398 
TRP CZ3  C Y N 399 
TRP CH2  C Y N 400 
TRP OXT  O N N 401 
TRP H    H N N 402 
TRP H2   H N N 403 
TRP HA   H N N 404 
TRP HB2  H N N 405 
TRP HB3  H N N 406 
TRP HD1  H N N 407 
TRP HE1  H N N 408 
TRP HE3  H N N 409 
TRP HZ2  H N N 410 
TRP HZ3  H N N 411 
TRP HH2  H N N 412 
TRP HXT  H N N 413 
TYR N    N N N 414 
TYR CA   C N S 415 
TYR C    C N N 416 
TYR O    O N N 417 
TYR CB   C N N 418 
TYR CG   C Y N 419 
TYR CD1  C Y N 420 
TYR CD2  C Y N 421 
TYR CE1  C Y N 422 
TYR CE2  C Y N 423 
TYR CZ   C Y N 424 
TYR OH   O N N 425 
TYR OXT  O N N 426 
TYR H    H N N 427 
TYR H2   H N N 428 
TYR HA   H N N 429 
TYR HB2  H N N 430 
TYR HB3  H N N 431 
TYR HD1  H N N 432 
TYR HD2  H N N 433 
TYR HE1  H N N 434 
TYR HE2  H N N 435 
TYR HH   H N N 436 
TYR HXT  H N N 437 
VAL N    N N N 438 
VAL CA   C N S 439 
VAL C    C N N 440 
VAL O    O N N 441 
VAL CB   C N N 442 
VAL CG1  C N N 443 
VAL CG2  C N N 444 
VAL OXT  O N N 445 
VAL H    H N N 446 
VAL H2   H N N 447 
VAL HA   H N N 448 
VAL HB   H N N 449 
VAL HG11 H N N 450 
VAL HG12 H N N 451 
VAL HG13 H N N 452 
VAL HG21 H N N 453 
VAL HG22 H N N 454 
VAL HG23 H N N 455 
VAL HXT  H N N 456 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
COP C3  N4   doub Y N 70  
COP C3  N3   sing N N 71  
COP C3  N2   sing Y N 72  
COP C1  C10  sing Y N 73  
COP C1  N2   doub Y N 74  
COP C1  N1   sing N N 75  
COP C10 C5   doub Y N 76  
COP C10 N9   sing Y N 77  
COP C8  C7   sing Y N 78  
COP C8  C11  sing N N 79  
COP C8  N9   doub Y N 80  
COP C7  N6   doub Y N 81  
COP C7  H7   sing N N 82  
COP C5  N4   sing Y N 83  
COP C5  N6   sing Y N 84  
COP C11 N12  sing N N 85  
COP C11 H111 sing N N 86  
COP C11 H112 sing N N 87  
COP C13 C18  doub Y N 88  
COP C13 C14  sing Y N 89  
COP C13 N12  sing N N 90  
COP C18 C17  sing Y N 91  
COP C18 H18  sing N N 92  
COP C17 C16  doub Y N 93  
COP C17 H17  sing N N 94  
COP C16 C15  sing Y N 95  
COP C16 C19  sing N N 96  
COP C15 C14  doub Y N 97  
COP C15 H15  sing N N 98  
COP C14 H14  sing N N 99  
COP C19 N20  sing N N 100 
COP C19 O19  doub N N 101 
COP C21 C24  sing N N 102 
COP C21 C27  sing N N 103 
COP C21 N20  sing N N 104 
COP C21 H21  sing N N 105 
COP C24 O24  doub N N 106 
COP C24 O25  sing N N 107 
COP C27 C28  sing N N 108 
COP C27 H271 sing N N 109 
COP C27 H272 sing N N 110 
COP C28 C29  sing N N 111 
COP C28 H281 sing N N 112 
COP C28 H282 sing N N 113 
COP C29 N30  sing N N 114 
COP C29 H291 sing N N 115 
COP C29 H292 sing N N 116 
COP N3  HN31 sing N N 117 
COP N3  HN32 sing N N 118 
COP N1  HN11 sing N N 119 
COP N1  HN12 sing N N 120 
COP N12 HN2  sing N N 121 
COP N20 HN0  sing N N 122 
COP O25 HO5  sing N N 123 
COP N30 C31  sing N N 124 
COP N30 HN3  sing N N 125 
COP C31 O32  doub N N 126 
COP C31 C33  sing N N 127 
COP C33 C38  doub Y N 128 
COP C33 C34  sing Y N 129 
COP C38 C37  sing Y N 130 
COP C38 C39  sing N N 131 
COP C37 C36  doub Y N 132 
COP C37 H37  sing N N 133 
COP C36 C35  sing Y N 134 
COP C36 H36  sing N N 135 
COP C35 C34  doub Y N 136 
COP C35 H35  sing N N 137 
COP C34 H34  sing N N 138 
COP C39 O40  doub N N 139 
COP C39 O41  sing N N 140 
COP O41 HO1  sing N N 141 
CYS N   CA   sing N N 142 
CYS N   H    sing N N 143 
CYS N   H2   sing N N 144 
CYS CA  C    sing N N 145 
CYS CA  CB   sing N N 146 
CYS CA  HA   sing N N 147 
CYS C   O    doub N N 148 
CYS C   OXT  sing N N 149 
CYS CB  SG   sing N N 150 
CYS CB  HB2  sing N N 151 
CYS CB  HB3  sing N N 152 
CYS SG  HG   sing N N 153 
CYS OXT HXT  sing N N 154 
GLN N   CA   sing N N 155 
GLN N   H    sing N N 156 
GLN N   H2   sing N N 157 
GLN CA  C    sing N N 158 
GLN CA  CB   sing N N 159 
GLN CA  HA   sing N N 160 
GLN C   O    doub N N 161 
GLN C   OXT  sing N N 162 
GLN CB  CG   sing N N 163 
GLN CB  HB2  sing N N 164 
GLN CB  HB3  sing N N 165 
GLN CG  CD   sing N N 166 
GLN CG  HG2  sing N N 167 
GLN CG  HG3  sing N N 168 
GLN CD  OE1  doub N N 169 
GLN CD  NE2  sing N N 170 
GLN NE2 HE21 sing N N 171 
GLN NE2 HE22 sing N N 172 
GLN OXT HXT  sing N N 173 
GLU N   CA   sing N N 174 
GLU N   H    sing N N 175 
GLU N   H2   sing N N 176 
GLU CA  C    sing N N 177 
GLU CA  CB   sing N N 178 
GLU CA  HA   sing N N 179 
GLU C   O    doub N N 180 
GLU C   OXT  sing N N 181 
GLU CB  CG   sing N N 182 
GLU CB  HB2  sing N N 183 
GLU CB  HB3  sing N N 184 
GLU CG  CD   sing N N 185 
GLU CG  HG2  sing N N 186 
GLU CG  HG3  sing N N 187 
GLU CD  OE1  doub N N 188 
GLU CD  OE2  sing N N 189 
GLU OE2 HE2  sing N N 190 
GLU OXT HXT  sing N N 191 
GLY N   CA   sing N N 192 
GLY N   H    sing N N 193 
GLY N   H2   sing N N 194 
GLY CA  C    sing N N 195 
GLY CA  HA2  sing N N 196 
GLY CA  HA3  sing N N 197 
GLY C   O    doub N N 198 
GLY C   OXT  sing N N 199 
GLY OXT HXT  sing N N 200 
HIS N   CA   sing N N 201 
HIS N   H    sing N N 202 
HIS N   H2   sing N N 203 
HIS CA  C    sing N N 204 
HIS CA  CB   sing N N 205 
HIS CA  HA   sing N N 206 
HIS C   O    doub N N 207 
HIS C   OXT  sing N N 208 
HIS CB  CG   sing N N 209 
HIS CB  HB2  sing N N 210 
HIS CB  HB3  sing N N 211 
HIS CG  ND1  sing Y N 212 
HIS CG  CD2  doub Y N 213 
HIS ND1 CE1  doub Y N 214 
HIS ND1 HD1  sing N N 215 
HIS CD2 NE2  sing Y N 216 
HIS CD2 HD2  sing N N 217 
HIS CE1 NE2  sing Y N 218 
HIS CE1 HE1  sing N N 219 
HIS NE2 HE2  sing N N 220 
HIS OXT HXT  sing N N 221 
ILE N   CA   sing N N 222 
ILE N   H    sing N N 223 
ILE N   H2   sing N N 224 
ILE CA  C    sing N N 225 
ILE CA  CB   sing N N 226 
ILE CA  HA   sing N N 227 
ILE C   O    doub N N 228 
ILE C   OXT  sing N N 229 
ILE CB  CG1  sing N N 230 
ILE CB  CG2  sing N N 231 
ILE CB  HB   sing N N 232 
ILE CG1 CD1  sing N N 233 
ILE CG1 HG12 sing N N 234 
ILE CG1 HG13 sing N N 235 
ILE CG2 HG21 sing N N 236 
ILE CG2 HG22 sing N N 237 
ILE CG2 HG23 sing N N 238 
ILE CD1 HD11 sing N N 239 
ILE CD1 HD12 sing N N 240 
ILE CD1 HD13 sing N N 241 
ILE OXT HXT  sing N N 242 
LEU N   CA   sing N N 243 
LEU N   H    sing N N 244 
LEU N   H2   sing N N 245 
LEU CA  C    sing N N 246 
LEU CA  CB   sing N N 247 
LEU CA  HA   sing N N 248 
LEU C   O    doub N N 249 
LEU C   OXT  sing N N 250 
LEU CB  CG   sing N N 251 
LEU CB  HB2  sing N N 252 
LEU CB  HB3  sing N N 253 
LEU CG  CD1  sing N N 254 
LEU CG  CD2  sing N N 255 
LEU CG  HG   sing N N 256 
LEU CD1 HD11 sing N N 257 
LEU CD1 HD12 sing N N 258 
LEU CD1 HD13 sing N N 259 
LEU CD2 HD21 sing N N 260 
LEU CD2 HD22 sing N N 261 
LEU CD2 HD23 sing N N 262 
LEU OXT HXT  sing N N 263 
LYS N   CA   sing N N 264 
LYS N   H    sing N N 265 
LYS N   H2   sing N N 266 
LYS CA  C    sing N N 267 
LYS CA  CB   sing N N 268 
LYS CA  HA   sing N N 269 
LYS C   O    doub N N 270 
LYS C   OXT  sing N N 271 
LYS CB  CG   sing N N 272 
LYS CB  HB2  sing N N 273 
LYS CB  HB3  sing N N 274 
LYS CG  CD   sing N N 275 
LYS CG  HG2  sing N N 276 
LYS CG  HG3  sing N N 277 
LYS CD  CE   sing N N 278 
LYS CD  HD2  sing N N 279 
LYS CD  HD3  sing N N 280 
LYS CE  NZ   sing N N 281 
LYS CE  HE2  sing N N 282 
LYS CE  HE3  sing N N 283 
LYS NZ  HZ1  sing N N 284 
LYS NZ  HZ2  sing N N 285 
LYS NZ  HZ3  sing N N 286 
LYS OXT HXT  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
PHE N   CA   sing N N 307 
PHE N   H    sing N N 308 
PHE N   H2   sing N N 309 
PHE CA  C    sing N N 310 
PHE CA  CB   sing N N 311 
PHE CA  HA   sing N N 312 
PHE C   O    doub N N 313 
PHE C   OXT  sing N N 314 
PHE CB  CG   sing N N 315 
PHE CB  HB2  sing N N 316 
PHE CB  HB3  sing N N 317 
PHE CG  CD1  doub Y N 318 
PHE CG  CD2  sing Y N 319 
PHE CD1 CE1  sing Y N 320 
PHE CD1 HD1  sing N N 321 
PHE CD2 CE2  doub Y N 322 
PHE CD2 HD2  sing N N 323 
PHE CE1 CZ   doub Y N 324 
PHE CE1 HE1  sing N N 325 
PHE CE2 CZ   sing Y N 326 
PHE CE2 HE2  sing N N 327 
PHE CZ  HZ   sing N N 328 
PHE OXT HXT  sing N N 329 
PRO N   CA   sing N N 330 
PRO N   CD   sing N N 331 
PRO N   H    sing N N 332 
PRO CA  C    sing N N 333 
PRO CA  CB   sing N N 334 
PRO CA  HA   sing N N 335 
PRO C   O    doub N N 336 
PRO C   OXT  sing N N 337 
PRO CB  CG   sing N N 338 
PRO CB  HB2  sing N N 339 
PRO CB  HB3  sing N N 340 
PRO CG  CD   sing N N 341 
PRO CG  HG2  sing N N 342 
PRO CG  HG3  sing N N 343 
PRO CD  HD2  sing N N 344 
PRO CD  HD3  sing N N 345 
PRO OXT HXT  sing N N 346 
SER N   CA   sing N N 347 
SER N   H    sing N N 348 
SER N   H2   sing N N 349 
SER CA  C    sing N N 350 
SER CA  CB   sing N N 351 
SER CA  HA   sing N N 352 
SER C   O    doub N N 353 
SER C   OXT  sing N N 354 
SER CB  OG   sing N N 355 
SER CB  HB2  sing N N 356 
SER CB  HB3  sing N N 357 
SER OG  HG   sing N N 358 
SER OXT HXT  sing N N 359 
THR N   CA   sing N N 360 
THR N   H    sing N N 361 
THR N   H2   sing N N 362 
THR CA  C    sing N N 363 
THR CA  CB   sing N N 364 
THR CA  HA   sing N N 365 
THR C   O    doub N N 366 
THR C   OXT  sing N N 367 
THR CB  OG1  sing N N 368 
THR CB  CG2  sing N N 369 
THR CB  HB   sing N N 370 
THR OG1 HG1  sing N N 371 
THR CG2 HG21 sing N N 372 
THR CG2 HG22 sing N N 373 
THR CG2 HG23 sing N N 374 
THR OXT HXT  sing N N 375 
TRP N   CA   sing N N 376 
TRP N   H    sing N N 377 
TRP N   H2   sing N N 378 
TRP CA  C    sing N N 379 
TRP CA  CB   sing N N 380 
TRP CA  HA   sing N N 381 
TRP C   O    doub N N 382 
TRP C   OXT  sing N N 383 
TRP CB  CG   sing N N 384 
TRP CB  HB2  sing N N 385 
TRP CB  HB3  sing N N 386 
TRP CG  CD1  doub Y N 387 
TRP CG  CD2  sing Y N 388 
TRP CD1 NE1  sing Y N 389 
TRP CD1 HD1  sing N N 390 
TRP CD2 CE2  doub Y N 391 
TRP CD2 CE3  sing Y N 392 
TRP NE1 CE2  sing Y N 393 
TRP NE1 HE1  sing N N 394 
TRP CE2 CZ2  sing Y N 395 
TRP CE3 CZ3  doub Y N 396 
TRP CE3 HE3  sing N N 397 
TRP CZ2 CH2  doub Y N 398 
TRP CZ2 HZ2  sing N N 399 
TRP CZ3 CH2  sing Y N 400 
TRP CZ3 HZ3  sing N N 401 
TRP CH2 HH2  sing N N 402 
TRP OXT HXT  sing N N 403 
TYR N   CA   sing N N 404 
TYR N   H    sing N N 405 
TYR N   H2   sing N N 406 
TYR CA  C    sing N N 407 
TYR CA  CB   sing N N 408 
TYR CA  HA   sing N N 409 
TYR C   O    doub N N 410 
TYR C   OXT  sing N N 411 
TYR CB  CG   sing N N 412 
TYR CB  HB2  sing N N 413 
TYR CB  HB3  sing N N 414 
TYR CG  CD1  doub Y N 415 
TYR CG  CD2  sing Y N 416 
TYR CD1 CE1  sing Y N 417 
TYR CD1 HD1  sing N N 418 
TYR CD2 CE2  doub Y N 419 
TYR CD2 HD2  sing N N 420 
TYR CE1 CZ   doub Y N 421 
TYR CE1 HE1  sing N N 422 
TYR CE2 CZ   sing Y N 423 
TYR CE2 HE2  sing N N 424 
TYR CZ  OH   sing N N 425 
TYR OH  HH   sing N N 426 
TYR OXT HXT  sing N N 427 
VAL N   CA   sing N N 428 
VAL N   H    sing N N 429 
VAL N   H2   sing N N 430 
VAL CA  C    sing N N 431 
VAL CA  CB   sing N N 432 
VAL CA  HA   sing N N 433 
VAL C   O    doub N N 434 
VAL C   OXT  sing N N 435 
VAL CB  CG1  sing N N 436 
VAL CB  CG2  sing N N 437 
VAL CB  HB   sing N N 438 
VAL CG1 HG11 sing N N 439 
VAL CG1 HG12 sing N N 440 
VAL CG1 HG13 sing N N 441 
VAL CG2 HG21 sing N N 442 
VAL CG2 HG22 sing N N 443 
VAL CG2 HG23 sing N N 444 
VAL OXT HXT  sing N N 445 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-29 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9JRL 
_em_admin.last_update        2025-04-23 
_em_admin.map_release_date   2025-02-26 
_em_admin.title              'outward-open hSLC19A1 + PT523' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K2 QUANTUM (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9JRL 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 108 ? 133.074 148.848 125.395 1.00 95.35  ?  24  SER A N   1 
ATOM   2    C CA  . SER A 1 108 ? 133.204 147.421 125.132 1.00 95.10  ?  24  SER A CA  1 
ATOM   3    C C   . SER A 1 108 ? 131.831 146.768 125.046 1.00 98.17  ?  24  SER A C   1 
ATOM   4    O O   . SER A 1 108 ? 131.719 145.566 124.810 1.00 103.40 ?  24  SER A O   1 
ATOM   5    C CB  . SER A 1 108 ? 134.045 146.749 126.220 1.00 94.42  ?  24  SER A CB  1 
ATOM   6    O OG  . SER A 1 108 ? 134.188 145.362 125.976 1.00 93.93  ?  24  SER A OG  1 
ATOM   7    N N   . TRP A 1 109 ? 130.785 147.572 125.237 1.00 101.41 ?  25  TRP A N   1 
ATOM   8    C CA  . TRP A 1 109 ? 129.430 147.033 125.288 1.00 103.35 ?  25  TRP A CA  1 
ATOM   9    C C   . TRP A 1 109 ? 128.849 146.846 123.889 1.00 105.00 ?  25  TRP A C   1 
ATOM   10   O O   . TRP A 1 109 ? 128.521 145.725 123.486 1.00 107.63 ?  25  TRP A O   1 
ATOM   11   C CB  . TRP A 1 109 ? 128.531 147.939 126.139 1.00 102.18 ?  25  TRP A CB  1 
ATOM   12   C CG  . TRP A 1 109 ? 128.422 149.362 125.659 1.00 105.79 ?  25  TRP A CG  1 
ATOM   13   C CD1 . TRP A 1 109 ? 129.445 150.237 125.434 1.00 106.92 ?  25  TRP A CD1 1 
ATOM   14   C CD2 . TRP A 1 109 ? 127.216 150.067 125.339 1.00 106.19 ?  25  TRP A CD2 1 
ATOM   15   N NE1 . TRP A 1 109 ? 128.951 151.442 124.997 1.00 110.51 ?  25  TRP A NE1 1 
ATOM   16   C CE2 . TRP A 1 109 ? 127.585 151.363 124.930 1.00 107.95 ?  25  TRP A CE2 1 
ATOM   17   C CE3 . TRP A 1 109 ? 125.859 149.727 125.360 1.00 102.55 ?  25  TRP A CE3 1 
ATOM   18   C CZ2 . TRP A 1 109 ? 126.648 152.320 124.546 1.00 103.80 ?  25  TRP A CZ2 1 
ATOM   19   C CZ3 . TRP A 1 109 ? 124.931 150.679 124.979 1.00 105.00 ?  25  TRP A CZ3 1 
ATOM   20   C CH2 . TRP A 1 109 ? 125.330 151.959 124.577 1.00 103.83 ?  25  TRP A CH2 1 
ATOM   21   N N   . ARG A 1 110 ? 128.723 147.933 123.130 1.00 87.92  ?  26  ARG A N   1 
ATOM   22   C CA  . ARG A 1 110 ? 128.094 147.855 121.817 1.00 84.40  ?  26  ARG A CA  1 
ATOM   23   C C   . ARG A 1 110 ? 129.071 147.356 120.762 1.00 84.13  ?  26  ARG A C   1 
ATOM   24   O O   . ARG A 1 110 ? 128.829 146.331 120.108 1.00 79.53  ?  26  ARG A O   1 
ATOM   25   C CB  . ARG A 1 110 ? 127.540 149.224 121.412 1.00 76.75  ?  26  ARG A CB  1 
ATOM   26   C CG  . ARG A 1 110 ? 126.655 149.178 120.177 1.00 81.98  ?  26  ARG A CG  1 
ATOM   27   C CD  . ARG A 1 110 ? 126.834 150.409 119.300 1.00 88.72  ?  26  ARG A CD  1 
ATOM   28   N NE  . ARG A 1 110 ? 126.707 150.081 117.884 1.00 90.61  ?  26  ARG A NE  1 
ATOM   29   C CZ  . ARG A 1 110 ? 127.325 150.723 116.902 1.00 83.57  ?  26  ARG A CZ  1 
ATOM   30   N NH1 . ARG A 1 110 ? 128.107 151.764 117.140 1.00 82.59  1  26  ARG A NH1 1 
ATOM   31   N NH2 . ARG A 1 110 ? 127.157 150.310 115.649 1.00 76.66  ?  26  ARG A NH2 1 
ATOM   32   N N   . HIS A 1 111 ? 130.199 148.058 120.611 1.00 89.88  ?  27  HIS A N   1 
ATOM   33   C CA  . HIS A 1 111 ? 131.009 147.895 119.410 1.00 85.15  ?  27  HIS A CA  1 
ATOM   34   C C   . HIS A 1 111 ? 131.518 146.470 119.263 1.00 88.11  ?  27  HIS A C   1 
ATOM   35   O O   . HIS A 1 111 ? 131.478 145.924 118.165 1.00 90.89  ?  27  HIS A O   1 
ATOM   36   C CB  . HIS A 1 111 ? 132.171 148.891 119.383 1.00 78.20  ?  27  HIS A CB  1 
ATOM   37   C CG  . HIS A 1 111 ? 132.719 149.237 120.730 1.00 88.77  ?  27  HIS A CG  1 
ATOM   38   N ND1 . HIS A 1 111 ? 132.307 150.345 121.437 1.00 86.69  ?  27  HIS A ND1 1 
ATOM   39   C CD2 . HIS A 1 111 ? 133.664 148.635 121.489 1.00 86.98  ?  27  HIS A CD2 1 
ATOM   40   C CE1 . HIS A 1 111 ? 132.967 150.404 122.580 1.00 86.07  ?  27  HIS A CE1 1 
ATOM   41   N NE2 . HIS A 1 111 ? 133.798 149.379 122.635 1.00 85.34  ?  27  HIS A NE2 1 
ATOM   42   N N   . LEU A 1 112 ? 131.951 145.832 120.351 1.00 78.01  ?  28  LEU A N   1 
ATOM   43   C CA  . LEU A 1 112 ? 132.515 144.490 120.220 1.00 65.64  ?  28  LEU A CA  1 
ATOM   44   C C   . LEU A 1 112 ? 131.597 143.553 119.443 1.00 69.27  ?  28  LEU A C   1 
ATOM   45   O O   . LEU A 1 112 ? 131.904 143.184 118.304 1.00 80.26  ?  28  LEU A O   1 
ATOM   46   C CB  . LEU A 1 112 ? 132.808 143.893 121.596 1.00 73.86  ?  28  LEU A CB  1 
ATOM   47   C CG  . LEU A 1 112 ? 134.192 144.162 122.184 1.00 82.38  ?  28  LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 112 ? 134.424 143.299 123.414 1.00 75.18  ?  28  LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 112 ? 135.267 143.916 121.142 1.00 80.67  ?  28  LEU A CD2 1 
ATOM   50   N N   . VAL A 1 113 ? 130.431 143.237 120.003 1.00 69.66  ?  29  VAL A N   1 
ATOM   51   C CA  . VAL A 1 113 ? 129.551 142.262 119.366 1.00 70.94  ?  29  VAL A CA  1 
ATOM   52   C C   . VAL A 1 113 ? 128.881 142.844 118.127 1.00 69.77  ?  29  VAL A C   1 
ATOM   53   O O   . VAL A 1 113 ? 128.775 142.169 117.095 1.00 60.24  ?  29  VAL A O   1 
ATOM   54   C CB  . VAL A 1 113 ? 128.517 141.737 120.376 1.00 71.56  ?  29  VAL A CB  1 
ATOM   55   C CG1 . VAL A 1 113 ? 127.664 140.655 119.740 1.00 65.54  ?  29  VAL A CG1 1 
ATOM   56   C CG2 . VAL A 1 113 ? 129.217 141.202 121.611 1.00 69.98  ?  29  VAL A CG2 1 
ATOM   57   N N   . CYS A 1 114 ? 128.404 144.091 118.200 1.00 72.49  ?  30  CYS A N   1 
ATOM   58   C CA  . CYS A 1 114 ? 127.685 144.657 117.062 1.00 62.44  ?  30  CYS A CA  1 
ATOM   59   C C   . CYS A 1 114 ? 128.597 144.786 115.849 1.00 62.62  ?  30  CYS A C   1 
ATOM   60   O O   . CYS A 1 114 ? 128.230 144.395 114.737 1.00 72.86  ?  30  CYS A O   1 
ATOM   61   C CB  . CYS A 1 114 ? 127.087 146.012 117.440 1.00 70.58  ?  30  CYS A CB  1 
ATOM   62   S SG  . CYS A 1 114 ? 125.856 145.938 118.761 1.00 75.38  ?  30  CYS A SG  1 
ATOM   63   N N   . TYR A 1 115 ? 129.799 145.326 116.049 1.00 52.39  ?  31  TYR A N   1 
ATOM   64   C CA  . TYR A 1 115 ? 130.791 145.459 114.997 1.00 52.56  ?  31  TYR A CA  1 
ATOM   65   C C   . TYR A 1 115 ? 131.296 144.106 114.523 1.00 52.61  ?  31  TYR A C   1 
ATOM   66   O O   . TYR A 1 115 ? 131.609 143.954 113.341 1.00 58.45  ?  31  TYR A O   1 
ATOM   67   C CB  . TYR A 1 115 ? 131.943 146.311 115.524 1.00 51.11  ?  31  TYR A CB  1 
ATOM   68   C CG  . TYR A 1 115 ? 132.979 146.719 114.515 1.00 42.88  ?  31  TYR A CG  1 
ATOM   69   C CD1 . TYR A 1 115 ? 134.070 145.909 114.245 1.00 46.86  ?  31  TYR A CD1 1 
ATOM   70   C CD2 . TYR A 1 115 ? 132.888 147.935 113.860 1.00 47.21  ?  31  TYR A CD2 1 
ATOM   71   C CE1 . TYR A 1 115 ? 135.027 146.288 113.337 1.00 49.72  ?  31  TYR A CE1 1 
ATOM   72   C CE2 . TYR A 1 115 ? 133.838 148.323 112.951 1.00 55.33  ?  31  TYR A CE2 1 
ATOM   73   C CZ  . TYR A 1 115 ? 134.905 147.496 112.693 1.00 56.90  ?  31  TYR A CZ  1 
ATOM   74   O OH  . TYR A 1 115 ? 135.857 147.886 111.786 1.00 63.50  ?  31  TYR A OH  1 
ATOM   75   N N   . LEU A 1 116 ? 131.388 143.113 115.412 1.00 51.09  ?  32  LEU A N   1 
ATOM   76   C CA  . LEU A 1 116 ? 131.781 141.782 114.965 1.00 50.26  ?  32  LEU A CA  1 
ATOM   77   C C   . LEU A 1 116 ? 130.741 141.189 114.024 1.00 58.93  ?  32  LEU A C   1 
ATOM   78   O O   . LEU A 1 116 ? 131.085 140.634 112.974 1.00 66.31  ?  32  LEU A O   1 
ATOM   79   C CB  . LEU A 1 116 ? 132.000 140.879 116.174 1.00 56.35  ?  32  LEU A CB  1 
ATOM   80   C CG  . LEU A 1 116 ? 132.932 139.688 115.992 1.00 54.63  ?  32  LEU A CG  1 
ATOM   81   C CD1 . LEU A 1 116 ? 134.021 140.011 114.991 1.00 54.13  ?  32  LEU A CD1 1 
ATOM   82   C CD2 . LEU A 1 116 ? 133.535 139.328 117.334 1.00 57.24  ?  32  LEU A CD2 1 
ATOM   83   N N   . CYS A 1 117 ? 129.459 141.312 114.376 1.00 57.74  ?  33  CYS A N   1 
ATOM   84   C CA  . CYS A 1 117 ? 128.402 140.836 113.488 1.00 49.96  ?  33  CYS A CA  1 
ATOM   85   C C   . CYS A 1 117 ? 128.368 141.637 112.191 1.00 56.16  ?  33  CYS A C   1 
ATOM   86   O O   . CYS A 1 117 ? 128.144 141.074 111.113 1.00 66.19  ?  33  CYS A O   1 
ATOM   87   C CB  . CYS A 1 117 ? 127.052 140.900 114.197 1.00 56.36  ?  33  CYS A CB  1 
ATOM   88   S SG  . CYS A 1 117 ? 126.953 139.884 115.686 1.00 78.83  ?  33  CYS A SG  1 
ATOM   89   N N   . PHE A 1 118 ? 128.586 142.950 112.276 1.00 44.67  ?  34  PHE A N   1 
ATOM   90   C CA  . PHE A 1 118 ? 128.611 143.785 111.080 1.00 39.65  ?  34  PHE A CA  1 
ATOM   91   C C   . PHE A 1 118 ? 129.752 143.388 110.153 1.00 46.06  ?  34  PHE A C   1 
ATOM   92   O O   . PHE A 1 118 ? 129.579 143.341 108.930 1.00 59.88  ?  34  PHE A O   1 
ATOM   93   C CB  . PHE A 1 118 ? 128.730 145.254 111.479 1.00 44.47  ?  34  PHE A CB  1 
ATOM   94   C CG  . PHE A 1 118 ? 128.721 146.200 110.320 1.00 43.11  ?  34  PHE A CG  1 
ATOM   95   C CD1 . PHE A 1 118 ? 127.714 146.148 109.376 1.00 48.40  ?  34  PHE A CD1 1 
ATOM   96   C CD2 . PHE A 1 118 ? 129.716 147.149 110.179 1.00 44.10  ?  34  PHE A CD2 1 
ATOM   97   C CE1 . PHE A 1 118 ? 127.700 147.023 108.311 1.00 52.26  ?  34  PHE A CE1 1 
ATOM   98   C CE2 . PHE A 1 118 ? 129.708 148.025 109.116 1.00 45.54  ?  34  PHE A CE2 1 
ATOM   99   C CZ  . PHE A 1 118 ? 128.700 147.961 108.180 1.00 49.19  ?  34  PHE A CZ  1 
ATOM   100  N N   . TYR A 1 119 ? 130.929 143.111 110.714 1.00 43.06  ?  35  TYR A N   1 
ATOM   101  C CA  . TYR A 1 119 ? 132.049 142.662 109.898 1.00 46.24  ?  35  TYR A CA  1 
ATOM   102  C C   . TYR A 1 119 ? 131.777 141.290 109.300 1.00 50.72  ?  35  TYR A C   1 
ATOM   103  O O   . TYR A 1 119 ? 132.139 141.029 108.149 1.00 50.86  ?  35  TYR A O   1 
ATOM   104  C CB  . TYR A 1 119 ? 133.335 142.632 110.719 1.00 39.45  ?  35  TYR A CB  1 
ATOM   105  C CG  . TYR A 1 119 ? 134.448 141.904 110.010 1.00 42.88  ?  35  TYR A CG  1 
ATOM   106  C CD1 . TYR A 1 119 ? 135.001 142.416 108.849 1.00 50.14  ?  35  TYR A CD1 1 
ATOM   107  C CD2 . TYR A 1 119 ? 134.928 140.694 110.486 1.00 51.14  ?  35  TYR A CD2 1 
ATOM   108  C CE1 . TYR A 1 119 ? 136.008 141.753 108.187 1.00 54.32  ?  35  TYR A CE1 1 
ATOM   109  C CE2 . TYR A 1 119 ? 135.938 140.023 109.830 1.00 54.70  ?  35  TYR A CE2 1 
ATOM   110  C CZ  . TYR A 1 119 ? 136.475 140.558 108.681 1.00 55.29  ?  35  TYR A CZ  1 
ATOM   111  O OH  . TYR A 1 119 ? 137.482 139.896 108.019 1.00 52.15  ?  35  TYR A OH  1 
ATOM   112  N N   . GLY A 1 120 ? 131.157 140.394 110.068 1.00 48.24  ?  36  GLY A N   1 
ATOM   113  C CA  . GLY A 1 120 ? 130.791 139.102 109.513 1.00 47.32  ?  36  GLY A CA  1 
ATOM   114  C C   . GLY A 1 120 ? 129.827 139.231 108.351 1.00 54.70  ?  36  GLY A C   1 
ATOM   115  O O   . GLY A 1 120 ? 129.921 138.495 107.367 1.00 64.83  ?  36  GLY A O   1 
ATOM   116  N N   . PHE A 1 121 ? 128.887 140.171 108.452 1.00 49.04  ?  37  PHE A N   1 
ATOM   117  C CA  . PHE A 1 121 ? 127.944 140.404 107.364 1.00 42.38  ?  37  PHE A CA  1 
ATOM   118  C C   . PHE A 1 121 ? 128.640 140.995 106.144 1.00 52.33  ?  37  PHE A C   1 
ATOM   119  O O   . PHE A 1 121 ? 128.455 140.517 105.020 1.00 64.50  ?  37  PHE A O   1 
ATOM   120  C CB  . PHE A 1 121 ? 126.821 141.325 107.842 1.00 46.08  ?  37  PHE A CB  1 
ATOM   121  C CG  . PHE A 1 121 ? 125.999 141.914 106.733 1.00 49.51  ?  37  PHE A CG  1 
ATOM   122  C CD1 . PHE A 1 121 ? 124.934 141.214 106.197 1.00 54.33  ?  37  PHE A CD1 1 
ATOM   123  C CD2 . PHE A 1 121 ? 126.280 143.175 106.236 1.00 48.48  ?  37  PHE A CD2 1 
ATOM   124  C CE1 . PHE A 1 121 ? 124.174 141.752 105.181 1.00 49.65  ?  37  PHE A CE1 1 
ATOM   125  C CE2 . PHE A 1 121 ? 125.523 143.717 105.220 1.00 53.55  ?  37  PHE A CE2 1 
ATOM   126  C CZ  . PHE A 1 121 ? 124.468 143.006 104.693 1.00 53.23  ?  37  PHE A CZ  1 
ATOM   127  N N   . MET A 1 122 ? 129.451 142.036 106.347 1.00 50.68  ?  38  MET A N   1 
ATOM   128  C CA  . MET A 1 122 ? 130.024 142.766 105.221 1.00 43.45  ?  38  MET A CA  1 
ATOM   129  C C   . MET A 1 122 ? 131.152 142.007 104.538 1.00 49.34  ?  38  MET A C   1 
ATOM   130  O O   . MET A 1 122 ? 131.300 142.103 103.316 1.00 62.69  ?  38  MET A O   1 
ATOM   131  C CB  . MET A 1 122 ? 130.522 144.135 105.677 1.00 43.33  ?  38  MET A CB  1 
ATOM   132  C CG  . MET A 1 122 ? 129.408 145.111 106.000 1.00 52.01  ?  38  MET A CG  1 
ATOM   133  S SD  . MET A 1 122 ? 128.565 145.758 104.543 1.00 64.05  ?  38  MET A SD  1 
ATOM   134  C CE  . MET A 1 122 ? 129.919 145.873 103.376 1.00 57.42  ?  38  MET A CE  1 
ATOM   135  N N   . ALA A 1 123 ? 131.958 141.260 105.294 1.00 42.86  ?  39  ALA A N   1 
ATOM   136  C CA  . ALA A 1 123 ? 133.023 140.474 104.686 1.00 48.20  ?  39  ALA A CA  1 
ATOM   137  C C   . ALA A 1 123 ? 132.483 139.379 103.782 1.00 53.62  ?  39  ALA A C   1 
ATOM   138  O O   . ALA A 1 123 ? 133.224 138.868 102.936 1.00 59.57  ?  39  ALA A O   1 
ATOM   139  C CB  . ALA A 1 123 ? 133.912 139.863 105.768 1.00 49.55  ?  39  ALA A CB  1 
ATOM   140  N N   . GLN A 1 124 ? 131.215 139.011 103.939 1.00 52.91  ?  40  GLN A N   1 
ATOM   141  C CA  . GLN A 1 124 ? 130.587 137.991 103.116 1.00 51.21  ?  40  GLN A CA  1 
ATOM   142  C C   . GLN A 1 124 ? 129.909 138.564 101.879 1.00 51.82  ?  40  GLN A C   1 
ATOM   143  O O   . GLN A 1 124 ? 129.331 137.801 101.100 1.00 60.76  ?  40  GLN A O   1 
ATOM   144  C CB  . GLN A 1 124 ? 129.566 137.207 103.944 1.00 52.76  ?  40  GLN A CB  1 
ATOM   145  C CG  . GLN A 1 124 ? 130.162 136.098 104.796 1.00 57.84  ?  40  GLN A CG  1 
ATOM   146  C CD  . GLN A 1 124 ? 131.197 135.276 104.057 1.00 65.13  ?  40  GLN A CD  1 
ATOM   147  O OE1 . GLN A 1 124 ? 130.860 134.344 103.329 1.00 62.06  ?  40  GLN A OE1 1 
ATOM   148  N NE2 . GLN A 1 124 ? 132.468 135.607 104.254 1.00 66.11  ?  40  GLN A NE2 1 
ATOM   149  N N   . ILE A 1 125 ? 129.966 139.878 101.677 1.00 38.55  ?  41  ILE A N   1 
ATOM   150  C CA  . ILE A 1 125 ? 129.310 140.507 100.535 1.00 44.71  ?  41  ILE A CA  1 
ATOM   151  C C   . ILE A 1 125 ? 130.292 140.522 99.368  1.00 54.12  ?  41  ILE A C   1 
ATOM   152  O O   . ILE A 1 125 ? 131.268 141.275 99.370  1.00 57.87  ?  41  ILE A O   1 
ATOM   153  C CB  . ILE A 1 125 ? 128.822 141.920 100.871 1.00 41.30  ?  41  ILE A CB  1 
ATOM   154  C CG1 . ILE A 1 125 ? 127.559 141.852 101.726 1.00 50.37  ?  41  ILE A CG1 1 
ATOM   155  C CG2 . ILE A 1 125 ? 128.520 142.697 99.604  1.00 50.13  ?  41  ILE A CG2 1 
ATOM   156  C CD1 . ILE A 1 125 ? 126.942 143.199 101.999 1.00 56.48  ?  41  ILE A CD1 1 
ATOM   157  N N   . ARG A 1 126 ? 130.039 139.673 98.373  1.00 60.62  ?  42  ARG A N   1 
ATOM   158  C CA  . ARG A 1 126 ? 130.826 139.632 97.142  1.00 55.25  ?  42  ARG A CA  1 
ATOM   159  C C   . ARG A 1 126 ? 129.864 139.327 96.006  1.00 59.52  ?  42  ARG A C   1 
ATOM   160  O O   . ARG A 1 126 ? 129.632 138.161 95.665  1.00 65.70  ?  42  ARG A O   1 
ATOM   161  C CB  . ARG A 1 126 ? 131.939 138.586 97.212  1.00 51.82  ?  42  ARG A CB  1 
ATOM   162  C CG  . ARG A 1 126 ? 133.054 138.923 98.176  1.00 51.97  ?  42  ARG A CG  1 
ATOM   163  C CD  . ARG A 1 126 ? 133.804 137.679 98.611  1.00 58.47  ?  42  ARG A CD  1 
ATOM   164  N NE  . ARG A 1 126 ? 132.915 136.541 98.805  1.00 61.49  ?  42  ARG A NE  1 
ATOM   165  C CZ  . ARG A 1 126 ? 132.659 135.983 99.980  1.00 63.62  ?  42  ARG A CZ  1 
ATOM   166  N NH1 . ARG A 1 126 ? 133.208 136.436 101.094 1.00 54.90  1  42  ARG A NH1 1 
ATOM   167  N NH2 . ARG A 1 126 ? 131.832 134.943 100.037 1.00 62.29  ?  42  ARG A NH2 1 
ATOM   168  N N   . PRO A 1 127 ? 129.268 140.359 95.405  1.00 53.95  ?  43  PRO A N   1 
ATOM   169  C CA  . PRO A 1 127 ? 128.263 140.113 94.359  1.00 55.05  ?  43  PRO A CA  1 
ATOM   170  C C   . PRO A 1 127 ? 128.791 139.316 93.183  1.00 57.95  ?  43  PRO A C   1 
ATOM   171  O O   . PRO A 1 127 ? 128.037 138.540 92.584  1.00 58.25  ?  43  PRO A O   1 
ATOM   172  C CB  . PRO A 1 127 ? 127.847 141.529 93.937  1.00 57.65  ?  43  PRO A CB  1 
ATOM   173  C CG  . PRO A 1 127 ? 128.204 142.395 95.091  1.00 53.60  ?  43  PRO A CG  1 
ATOM   174  C CD  . PRO A 1 127 ? 129.424 141.790 95.705  1.00 50.72  ?  43  PRO A CD  1 
ATOM   175  N N   . GLY A 1 128 ? 130.062 139.478 92.835  1.00 64.72  ?  44  GLY A N   1 
ATOM   176  C CA  . GLY A 1 128 ? 130.632 138.806 91.690  1.00 59.34  ?  44  GLY A CA  1 
ATOM   177  C C   . GLY A 1 128 ? 131.206 137.434 91.941  1.00 62.96  ?  44  GLY A C   1 
ATOM   178  O O   . GLY A 1 128 ? 131.749 136.831 91.011  1.00 73.38  ?  44  GLY A O   1 
ATOM   179  N N   . GLU A 1 129 ? 131.112 136.908 93.163  1.00 61.68  ?  45  GLU A N   1 
ATOM   180  C CA  . GLU A 1 129 ? 131.669 135.590 93.440  1.00 62.44  ?  45  GLU A CA  1 
ATOM   181  C C   . GLU A 1 129 ? 130.820 134.463 92.873  1.00 65.75  ?  45  GLU A C   1 
ATOM   182  O O   . GLU A 1 129 ? 131.335 133.357 92.678  1.00 69.73  ?  45  GLU A O   1 
ATOM   183  C CB  . GLU A 1 129 ? 131.854 135.392 94.946  1.00 60.51  ?  45  GLU A CB  1 
ATOM   184  C CG  . GLU A 1 129 ? 130.731 134.644 95.635  1.00 64.43  ?  45  GLU A CG  1 
ATOM   185  C CD  . GLU A 1 129 ? 131.168 134.041 96.953  1.00 72.77  ?  45  GLU A CD  1 
ATOM   186  O OE1 . GLU A 1 129 ? 132.389 133.996 97.208  1.00 72.02  ?  45  GLU A OE1 1 
ATOM   187  O OE2 . GLU A 1 129 ? 130.293 133.616 97.736  1.00 73.45  -1 45  GLU A OE2 1 
ATOM   188  N N   . SER A 1 130 ? 129.540 134.711 92.605  1.00 69.68  ?  46  SER A N   1 
ATOM   189  C CA  . SER A 1 130 ? 128.694 133.708 91.976  1.00 68.42  ?  46  SER A CA  1 
ATOM   190  C C   . SER A 1 130 ? 128.810 133.710 90.460  1.00 63.41  ?  46  SER A C   1 
ATOM   191  O O   . SER A 1 130 ? 128.298 132.791 89.814  1.00 66.30  ?  46  SER A O   1 
ATOM   192  C CB  . SER A 1 130 ? 127.233 133.924 92.375  1.00 67.11  ?  46  SER A CB  1 
ATOM   193  O OG  . SER A 1 130 ? 127.091 133.972 93.783  1.00 66.61  ?  46  SER A OG  1 
ATOM   194  N N   . PHE A 1 131 ? 129.470 134.712 89.881  1.00 65.07  ?  47  PHE A N   1 
ATOM   195  C CA  . PHE A 1 131 ? 129.593 134.853 88.437  1.00 69.55  ?  47  PHE A CA  1 
ATOM   196  C C   . PHE A 1 131 ? 131.052 134.851 87.998  1.00 70.62  ?  47  PHE A C   1 
ATOM   197  O O   . PHE A 1 131 ? 131.399 135.434 86.970  1.00 73.49  ?  47  PHE A O   1 
ATOM   198  C CB  . PHE A 1 131 ? 128.894 136.124 87.960  1.00 66.29  ?  47  PHE A CB  1 
ATOM   199  C CG  . PHE A 1 131 ? 127.465 136.227 88.399  1.00 71.11  ?  47  PHE A CG  1 
ATOM   200  C CD1 . PHE A 1 131 ? 126.456 135.643 87.657  1.00 70.92  ?  47  PHE A CD1 1 
ATOM   201  C CD2 . PHE A 1 131 ? 127.132 136.901 89.559  1.00 71.19  ?  47  PHE A CD2 1 
ATOM   202  C CE1 . PHE A 1 131 ? 125.141 135.734 88.061  1.00 71.88  ?  47  PHE A CE1 1 
ATOM   203  C CE2 . PHE A 1 131 ? 125.821 136.997 89.968  1.00 71.50  ?  47  PHE A CE2 1 
ATOM   204  C CZ  . PHE A 1 131 ? 124.824 136.411 89.219  1.00 73.00  ?  47  PHE A CZ  1 
ATOM   205  N N   . ILE A 1 132 ? 131.920 134.204 88.775  1.00 62.33  ?  48  ILE A N   1 
ATOM   206  C CA  . ILE A 1 132 ? 133.330 134.137 88.407  1.00 60.58  ?  48  ILE A CA  1 
ATOM   207  C C   . ILE A 1 132 ? 133.518 133.269 87.169  1.00 65.07  ?  48  ILE A C   1 
ATOM   208  O O   . ILE A 1 132 ? 134.229 133.647 86.231  1.00 70.50  ?  48  ILE A O   1 
ATOM   209  C CB  . ILE A 1 132 ? 134.170 133.625 89.589  1.00 63.64  ?  48  ILE A CB  1 
ATOM   210  C CG1 . ILE A 1 132 ? 134.151 134.640 90.733  1.00 61.48  ?  48  ILE A CG1 1 
ATOM   211  C CG2 . ILE A 1 132 ? 135.588 133.352 89.144  1.00 68.47  ?  48  ILE A CG2 1 
ATOM   212  C CD1 . ILE A 1 132 ? 135.043 134.266 91.892  1.00 62.02  ?  48  ILE A CD1 1 
ATOM   213  N N   . THR A 1 133 ? 132.883 132.093 87.184  1.00 64.17  ?  49  THR A N   1 
ATOM   214  C CA  . THR A 1 133 ? 133.001 131.151 86.039  1.00 70.60  ?  49  THR A CA  1 
ATOM   215  C C   . THR A 1 133 ? 132.535 131.840 84.748  1.00 73.92  ?  49  THR A C   1 
ATOM   216  O O   . THR A 1 133 ? 133.345 131.874 83.801  1.00 70.94  ?  49  THR A O   1 
ATOM   217  C CB  . THR A 1 133 ? 132.248 129.842 86.315  1.00 71.81  ?  49  THR A CB  1 
ATOM   218  O OG1 . THR A 1 133 ? 132.757 129.287 87.528  1.00 68.47  ?  49  THR A OG1 1 
ATOM   219  C CG2 . THR A 1 133 ? 132.384 128.837 85.193  1.00 70.82  ?  49  THR A CG2 1 
ATOM   220  N N   . PRO A 1 134 ? 131.307 132.400 84.634  1.00 69.49  ?  50  PRO A N   1 
ATOM   221  C CA  . PRO A 1 134 ? 130.917 133.069 83.380  1.00 62.49  ?  50  PRO A CA  1 
ATOM   222  C C   . PRO A 1 134 ? 131.860 134.190 82.990  1.00 68.06  ?  50  PRO A C   1 
ATOM   223  O O   . PRO A 1 134 ? 132.183 134.342 81.804  1.00 74.93  ?  50  PRO A O   1 
ATOM   224  C CB  . PRO A 1 134 ? 129.504 133.595 83.675  1.00 61.32  ?  50  PRO A CB  1 
ATOM   225  C CG  . PRO A 1 134 ? 129.036 132.857 84.858  1.00 67.60  ?  50  PRO A CG  1 
ATOM   226  C CD  . PRO A 1 134 ? 130.235 132.462 85.644  1.00 66.36  ?  50  PRO A CD  1 
ATOM   227  N N   . TYR A 1 135 ? 132.341 134.960 83.970  1.00 62.09  ?  51  TYR A N   1 
ATOM   228  C CA  . TYR A 1 135 ? 133.243 136.068 83.675  1.00 57.10  ?  51  TYR A CA  1 
ATOM   229  C C   . TYR A 1 135 ? 134.512 135.574 83.000  1.00 68.49  ?  51  TYR A C   1 
ATOM   230  O O   . TYR A 1 135 ? 135.014 136.205 82.063  1.00 73.71  ?  51  TYR A O   1 
ATOM   231  C CB  . TYR A 1 135 ? 133.582 136.821 84.958  1.00 52.86  ?  51  TYR A CB  1 
ATOM   232  C CG  . TYR A 1 135 ? 134.533 137.973 84.754  1.00 59.81  ?  51  TYR A CG  1 
ATOM   233  C CD1 . TYR A 1 135 ? 134.308 138.916 83.765  1.00 70.28  ?  51  TYR A CD1 1 
ATOM   234  C CD2 . TYR A 1 135 ? 135.661 138.113 85.545  1.00 61.44  ?  51  TYR A CD2 1 
ATOM   235  C CE1 . TYR A 1 135 ? 135.173 139.970 83.577  1.00 69.32  ?  51  TYR A CE1 1 
ATOM   236  C CE2 . TYR A 1 135 ? 136.535 139.162 85.361  1.00 62.99  ?  51  TYR A CE2 1 
ATOM   237  C CZ  . TYR A 1 135 ? 136.285 140.088 84.376  1.00 67.02  ?  51  TYR A CZ  1 
ATOM   238  O OH  . TYR A 1 135 ? 137.153 141.137 84.188  1.00 73.49  ?  51  TYR A OH  1 
ATOM   239  N N   . LEU A 1 136 ? 135.049 134.446 83.467  1.00 73.58  ?  52  LEU A N   1 
ATOM   240  C CA  . LEU A 1 136 ? 136.205 133.852 82.809  1.00 71.84  ?  52  LEU A CA  1 
ATOM   241  C C   . LEU A 1 136 ? 135.862 133.423 81.389  1.00 73.40  ?  52  LEU A C   1 
ATOM   242  O O   . LEU A 1 136 ? 136.680 133.569 80.473  1.00 80.17  ?  52  LEU A O   1 
ATOM   243  C CB  . LEU A 1 136 ? 136.719 132.666 83.624  1.00 68.27  ?  52  LEU A CB  1 
ATOM   244  C CG  . LEU A 1 136 ? 137.151 132.985 85.056  1.00 62.61  ?  52  LEU A CG  1 
ATOM   245  C CD1 . LEU A 1 136 ? 137.969 131.848 85.640  1.00 68.93  ?  52  LEU A CD1 1 
ATOM   246  C CD2 . LEU A 1 136 ? 137.930 134.284 85.101  1.00 68.71  ?  52  LEU A CD2 1 
ATOM   247  N N   . LEU A 1 137 ? 134.657 132.895 81.183  1.00 70.59  ?  53  LEU A N   1 
ATOM   248  C CA  . LEU A 1 137 ? 134.246 132.431 79.867  1.00 73.21  ?  53  LEU A CA  1 
ATOM   249  C C   . LEU A 1 137 ? 133.601 133.520 79.023  1.00 69.69  ?  53  LEU A C   1 
ATOM   250  O O   . LEU A 1 137 ? 133.323 133.284 77.843  1.00 70.15  ?  53  LEU A O   1 
ATOM   251  C CB  . LEU A 1 137 ? 133.283 131.248 80.003  1.00 74.68  ?  53  LEU A CB  1 
ATOM   252  C CG  . LEU A 1 137 ? 133.778 130.094 80.874  1.00 71.48  ?  53  LEU A CG  1 
ATOM   253  C CD1 . LEU A 1 137 ? 132.640 129.146 81.212  1.00 69.66  ?  53  LEU A CD1 1 
ATOM   254  C CD2 . LEU A 1 137 ? 134.907 129.359 80.181  1.00 74.13  ?  53  LEU A CD2 1 
ATOM   255  N N   . GLY A 1 138 ? 133.364 134.701 79.588  1.00 73.10  ?  54  GLY A N   1 
ATOM   256  C CA  . GLY A 1 138 ? 132.800 135.792 78.834  1.00 75.81  ?  54  GLY A CA  1 
ATOM   257  C C   . GLY A 1 138 ? 133.833 136.464 77.959  1.00 80.74  ?  54  GLY A C   1 
ATOM   258  O O   . GLY A 1 138 ? 134.997 136.052 77.875  1.00 81.86  ?  54  GLY A O   1 
ATOM   259  N N   . PRO A 1 139 ? 133.410 137.533 77.281  1.00 82.67  ?  55  PRO A N   1 
ATOM   260  C CA  . PRO A 1 139 ? 134.297 138.262 76.365  1.00 81.39  ?  55  PRO A CA  1 
ATOM   261  C C   . PRO A 1 139 ? 135.189 139.286 77.066  1.00 84.94  ?  55  PRO A C   1 
ATOM   262  O O   . PRO A 1 139 ? 135.406 140.393 76.570  1.00 84.13  ?  55  PRO A O   1 
ATOM   263  C CB  . PRO A 1 139 ? 133.315 138.933 75.400  1.00 78.79  ?  55  PRO A CB  1 
ATOM   264  C CG  . PRO A 1 139 ? 131.934 138.792 76.020  1.00 78.80  ?  55  PRO A CG  1 
ATOM   265  C CD  . PRO A 1 139 ? 132.076 138.146 77.357  1.00 82.76  ?  55  PRO A CD  1 
ATOM   266  N N   . ASP A 1 140 ? 135.709 138.912 78.234  1.00 85.55  ?  56  ASP A N   1 
ATOM   267  C CA  . ASP A 1 140 ? 136.693 139.727 78.933  1.00 85.07  ?  56  ASP A CA  1 
ATOM   268  C C   . ASP A 1 140 ? 137.985 138.942 79.115  1.00 85.44  ?  56  ASP A C   1 
ATOM   269  O O   . ASP A 1 140 ? 139.076 139.446 78.831  1.00 88.10  ?  56  ASP A O   1 
ATOM   270  C CB  . ASP A 1 140 ? 136.151 140.188 80.286  1.00 83.25  ?  56  ASP A CB  1 
ATOM   271  C CG  . ASP A 1 140 ? 134.707 140.643 80.211  1.00 86.58  ?  56  ASP A CG  1 
ATOM   272  O OD1 . ASP A 1 140 ? 134.459 141.764 79.720  1.00 90.07  ?  56  ASP A OD1 1 
ATOM   273  O OD2 . ASP A 1 140 ? 133.818 139.880 80.646  1.00 82.12  -1 56  ASP A OD2 1 
ATOM   274  N N   . LYS A 1 141 ? 137.864 137.703 79.590  1.00 77.51  ?  57  LYS A N   1 
ATOM   275  C CA  . LYS A 1 141 ? 139.017 136.834 79.779  1.00 79.12  ?  57  LYS A CA  1 
ATOM   276  C C   . LYS A 1 141 ? 139.243 135.902 78.598  1.00 81.19  ?  57  LYS A C   1 
ATOM   277  O O   . LYS A 1 141 ? 140.392 135.542 78.315  1.00 80.99  ?  57  LYS A O   1 
ATOM   278  C CB  . LYS A 1 141 ? 138.847 136.008 81.056  1.00 77.61  ?  57  LYS A CB  1 
ATOM   279  C CG  . LYS A 1 141 ? 138.856 136.824 82.335  1.00 80.08  ?  57  LYS A CG  1 
ATOM   280  C CD  . LYS A 1 141 ? 140.132 137.630 82.463  1.00 82.20  ?  57  LYS A CD  1 
ATOM   281  C CE  . LYS A 1 141 ? 139.889 138.950 83.174  1.00 79.91  ?  57  LYS A CE  1 
ATOM   282  N NZ  . LYS A 1 141 ? 138.873 139.785 82.479  1.00 76.23  1  57  LYS A NZ  1 
ATOM   283  N N   . GLN A 1 142 ? 138.170 135.503 77.913  1.00 85.63  ?  58  GLN A N   1 
ATOM   284  C CA  . GLN A 1 142 ? 138.240 134.656 76.722  1.00 83.81  ?  58  GLN A CA  1 
ATOM   285  C C   . GLN A 1 142 ? 138.871 133.298 77.018  1.00 84.60  ?  58  GLN A C   1 
ATOM   286  O O   . GLN A 1 142 ? 139.503 132.694 76.150  1.00 86.89  ?  58  GLN A O   1 
ATOM   287  C CB  . GLN A 1 142 ? 139.024 135.364 75.615  1.00 30.00  ?  58  GLN A CB  1 
ATOM   288  C CG  . GLN A 1 142 ? 138.339 136.603 75.064  1.00 30.00  ?  58  GLN A CG  1 
ATOM   289  C CD  . GLN A 1 142 ? 139.176 137.318 74.023  1.00 30.00  ?  58  GLN A CD  1 
ATOM   290  O OE1 . GLN A 1 142 ? 140.401 137.201 74.015  1.00 30.00  ?  58  GLN A OE1 1 
ATOM   291  N NE2 . GLN A 1 142 ? 138.516 138.060 73.139  1.00 30.00  ?  58  GLN A NE2 1 
ATOM   292  N N   . PHE A 1 143 ? 138.706 132.805 78.243  1.00 83.98  ?  59  PHE A N   1 
ATOM   293  C CA  . PHE A 1 143 ? 139.210 131.483 78.584  1.00 80.86  ?  59  PHE A CA  1 
ATOM   294  C C   . PHE A 1 143 ? 138.301 130.400 78.021  1.00 81.48  ?  59  PHE A C   1 
ATOM   295  O O   . PHE A 1 143 ? 137.077 130.547 77.986  1.00 77.52  ?  59  PHE A O   1 
ATOM   296  C CB  . PHE A 1 143 ? 139.325 131.324 80.098  1.00 80.41  ?  59  PHE A CB  1 
ATOM   297  C CG  . PHE A 1 143 ? 140.474 132.070 80.697  1.00 83.60  ?  59  PHE A CG  1 
ATOM   298  C CD1 . PHE A 1 143 ? 141.757 131.895 80.212  1.00 85.77  ?  59  PHE A CD1 1 
ATOM   299  C CD2 . PHE A 1 143 ? 140.273 132.946 81.745  1.00 80.68  ?  59  PHE A CD2 1 
ATOM   300  C CE1 . PHE A 1 143 ? 142.817 132.584 80.760  1.00 85.86  ?  59  PHE A CE1 1 
ATOM   301  C CE2 . PHE A 1 143 ? 141.327 133.639 82.293  1.00 80.04  ?  59  PHE A CE2 1 
ATOM   302  C CZ  . PHE A 1 143 ? 142.601 133.456 81.803  1.00 80.95  ?  59  PHE A CZ  1 
ATOM   303  N N   . THR A 1 144 ? 138.910 129.305 77.578  1.00 88.63  ?  60  THR A N   1 
ATOM   304  C CA  . THR A 1 144 ? 138.139 128.160 77.127  1.00 89.63  ?  60  THR A CA  1 
ATOM   305  C C   . THR A 1 144 ? 137.541 127.423 78.322  1.00 87.45  ?  60  THR A C   1 
ATOM   306  O O   . THR A 1 144 ? 138.000 127.551 79.460  1.00 89.99  ?  60  THR A O   1 
ATOM   307  C CB  . THR A 1 144 ? 139.013 127.212 76.308  1.00 91.32  ?  60  THR A CB  1 
ATOM   308  O OG1 . THR A 1 144 ? 139.796 126.404 77.193  1.00 91.21  ?  60  THR A OG1 1 
ATOM   309  C CG2 . THR A 1 144 ? 139.943 128.000 75.399  1.00 89.09  ?  60  THR A CG2 1 
ATOM   310  N N   . ARG A 1 145 ? 136.491 126.647 78.049  1.00 87.34  ?  61  ARG A N   1 
ATOM   311  C CA  . ARG A 1 145 ? 135.820 125.911 79.116  1.00 91.04  ?  61  ARG A CA  1 
ATOM   312  C C   . ARG A 1 145 ? 136.754 124.892 79.756  1.00 89.44  ?  61  ARG A C   1 
ATOM   313  O O   . ARG A 1 145 ? 136.764 124.731 80.983  1.00 91.05  ?  61  ARG A O   1 
ATOM   314  C CB  . ARG A 1 145 ? 134.568 125.225 78.570  1.00 89.62  ?  61  ARG A CB  1 
ATOM   315  C CG  . ARG A 1 145 ? 133.867 124.321 79.567  1.00 86.29  ?  61  ARG A CG  1 
ATOM   316  C CD  . ARG A 1 145 ? 132.647 125.002 80.161  1.00 86.85  ?  61  ARG A CD  1 
ATOM   317  N NE  . ARG A 1 145 ? 131.834 124.078 80.943  1.00 91.73  ?  61  ARG A NE  1 
ATOM   318  C CZ  . ARG A 1 145 ? 130.947 124.449 81.855  1.00 91.45  ?  61  ARG A CZ  1 
ATOM   319  N NH1 . ARG A 1 145 ? 130.730 125.725 82.129  1.00 89.38  1  61  ARG A NH1 1 
ATOM   320  N NH2 . ARG A 1 145 ? 130.259 123.517 82.508  1.00 89.81  ?  61  ARG A NH2 1 
ATOM   321  N N   . GLU A 1 146 ? 137.526 124.193 78.921  1.00 91.11  ?  62  GLU A N   1 
ATOM   322  C CA  . GLU A 1 146 ? 138.481 123.182 79.443  1.00 92.59  ?  62  GLU A CA  1 
ATOM   323  C C   . GLU A 1 146 ? 139.457 123.873 80.398  1.00 94.60  ?  62  GLU A C   1 
ATOM   324  O O   . GLU A 1 146 ? 139.666 123.349 81.507  1.00 95.84  ?  62  GLU A O   1 
ATOM   325  C CB  . GLU A 1 146 ? 139.230 122.514 78.289  1.00 92.22  ?  62  GLU A CB  1 
ATOM   326  C CG  . GLU A 1 146 ? 138.309 121.875 77.267  1.00 96.69  ?  62  GLU A CG  1 
ATOM   327  C CD  . GLU A 1 146 ? 139.024 121.231 76.092  1.00 100.45 ?  62  GLU A CD  1 
ATOM   328  O OE1 . GLU A 1 146 ? 140.269 121.278 76.062  1.00 99.38  ?  62  GLU A OE1 1 
ATOM   329  O OE2 . GLU A 1 146 ? 138.333 120.684 75.210  1.00 97.17  -1 62  GLU A OE2 1 
ATOM   330  N N   . GLN A 1 147 ? 140.014 125.014 79.984  1.00 84.68  ?  63  GLN A N   1 
ATOM   331  C CA  . GLN A 1 147 ? 141.002 125.704 80.809  1.00 82.61  ?  63  GLN A CA  1 
ATOM   332  C C   . GLN A 1 147 ? 140.457 125.967 82.206  1.00 87.02  ?  63  GLN A C   1 
ATOM   333  O O   . GLN A 1 147 ? 141.102 125.641 83.209  1.00 90.86  ?  63  GLN A O   1 
ATOM   334  C CB  . GLN A 1 147 ? 141.418 127.018 80.147  1.00 83.73  ?  63  GLN A CB  1 
ATOM   335  C CG  . GLN A 1 147 ? 142.414 126.868 79.014  1.00 87.89  ?  63  GLN A CG  1 
ATOM   336  C CD  . GLN A 1 147 ? 143.014 128.194 78.592  1.00 90.73  ?  63  GLN A CD  1 
ATOM   337  O OE1 . GLN A 1 147 ? 142.297 129.169 78.369  1.00 89.94  ?  63  GLN A OE1 1 
ATOM   338  N NE2 . GLN A 1 147 ? 144.335 128.236 78.477  1.00 89.48  ?  63  GLN A NE2 1 
ATOM   339  N N   . VAL A 1 148 ? 139.253 126.535 82.289  1.00 83.99  ?  64  VAL A N   1 
ATOM   340  C CA  . VAL A 1 148 ? 138.659 126.847 83.586  1.00 82.41  ?  64  VAL A CA  1 
ATOM   341  C C   . VAL A 1 148 ? 138.377 125.571 84.369  1.00 80.10  ?  64  VAL A C   1 
ATOM   342  O O   . VAL A 1 148 ? 138.628 125.500 85.578  1.00 80.11  ?  64  VAL A O   1 
ATOM   343  C CB  . VAL A 1 148 ? 137.385 127.692 83.398  1.00 81.07  ?  64  VAL A CB  1 
ATOM   344  C CG1 . VAL A 1 148 ? 136.725 127.968 84.738  1.00 78.72  ?  64  VAL A CG1 1 
ATOM   345  C CG2 . VAL A 1 148 ? 137.713 128.990 82.686  1.00 80.60  ?  64  VAL A CG2 1 
ATOM   346  N N   . THR A 1 149 ? 137.855 124.542 83.698  1.00 82.82  ?  65  THR A N   1 
ATOM   347  C CA  . THR A 1 149 ? 137.423 123.351 84.422  1.00 82.55  ?  65  THR A CA  1 
ATOM   348  C C   . THR A 1 149 ? 138.595 122.497 84.888  1.00 86.35  ?  65  THR A C   1 
ATOM   349  O O   . THR A 1 149 ? 138.465 121.769 85.878  1.00 92.73  ?  65  THR A O   1 
ATOM   350  C CB  . THR A 1 149 ? 136.479 122.516 83.559  1.00 84.59  ?  65  THR A CB  1 
ATOM   351  O OG1 . THR A 1 149 ? 137.032 122.369 82.246  1.00 91.29  ?  65  THR A OG1 1 
ATOM   352  C CG2 . THR A 1 149 ? 135.118 123.185 83.460  1.00 87.60  ?  65  THR A CG2 1 
ATOM   353  N N   . ASN A 1 150 ? 139.738 122.557 84.203  1.00 83.38  ?  66  ASN A N   1 
ATOM   354  C CA  . ASN A 1 150 ? 140.860 121.686 84.534  1.00 84.13  ?  66  ASN A CA  1 
ATOM   355  C C   . ASN A 1 150 ? 141.993 122.404 85.258  1.00 86.00  ?  66  ASN A C   1 
ATOM   356  O O   . ASN A 1 150 ? 142.502 121.896 86.260  1.00 86.20  ?  66  ASN A O   1 
ATOM   357  C CB  . ASN A 1 150 ? 141.403 121.020 83.263  1.00 83.67  ?  66  ASN A CB  1 
ATOM   358  C CG  . ASN A 1 150 ? 140.306 120.431 82.398  1.00 88.13  ?  66  ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 150 ? 139.140 120.400 82.788  1.00 88.29  ?  66  ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 150 ? 140.678 119.957 81.215  1.00 89.32  ?  66  ASN A ND2 1 
ATOM   361  N N   . GLU A 1 151 ? 142.413 123.569 84.773  1.00 86.05  ?  67  GLU A N   1 
ATOM   362  C CA  . GLU A 1 151 ? 143.601 124.223 85.300  1.00 81.72  ?  67  GLU A CA  1 
ATOM   363  C C   . GLU A 1 151 ? 143.301 125.265 86.368  1.00 81.28  ?  67  GLU A C   1 
ATOM   364  O O   . GLU A 1 151 ? 144.221 125.972 86.790  1.00 83.47  ?  67  GLU A O   1 
ATOM   365  C CB  . GLU A 1 151 ? 144.389 124.880 84.162  1.00 81.22  ?  67  GLU A CB  1 
ATOM   366  C CG  . GLU A 1 151 ? 144.145 124.266 82.796  1.00 85.26  ?  67  GLU A CG  1 
ATOM   367  C CD  . GLU A 1 151 ? 144.962 124.930 81.706  1.00 87.04  ?  67  GLU A CD  1 
ATOM   368  O OE1 . GLU A 1 151 ? 146.053 125.453 82.013  1.00 85.02  ?  67  GLU A OE1 1 
ATOM   369  O OE2 . GLU A 1 151 ? 144.515 124.927 80.540  1.00 86.07  -1 67  GLU A OE2 1 
ATOM   370  N N   . ILE A 1 152 ? 142.052 125.392 86.814  1.00 74.38  ?  68  ILE A N   1 
ATOM   371  C CA  . ILE A 1 152 ? 141.696 126.505 87.687  1.00 71.90  ?  68  ILE A CA  1 
ATOM   372  C C   . ILE A 1 152 ? 141.024 126.036 88.975  1.00 65.69  ?  68  ILE A C   1 
ATOM   373  O O   . ILE A 1 152 ? 141.486 126.361 90.072  1.00 74.96  ?  68  ILE A O   1 
ATOM   374  C CB  . ILE A 1 152 ? 140.821 127.517 86.925  1.00 75.65  ?  68  ILE A CB  1 
ATOM   375  C CG1 . ILE A 1 152 ? 141.621 128.133 85.773  1.00 73.66  ?  68  ILE A CG1 1 
ATOM   376  C CG2 . ILE A 1 152 ? 140.335 128.605 87.843  1.00 70.93  ?  68  ILE A CG2 1 
ATOM   377  C CD1 . ILE A 1 152 ? 140.945 129.305 85.103  1.00 71.79  ?  68  ILE A CD1 1 
ATOM   378  N N   . THR A 1 153 ? 139.938 125.274 88.869  1.00 65.64  ?  69  THR A N   1 
ATOM   379  C CA  . THR A 1 153 ? 139.212 124.882 90.078  1.00 76.00  ?  69  THR A CA  1 
ATOM   380  C C   . THR A 1 153 ? 139.911 123.761 90.855  1.00 79.43  ?  69  THR A C   1 
ATOM   381  O O   . THR A 1 153 ? 139.913 123.786 92.099  1.00 75.95  ?  69  THR A O   1 
ATOM   382  C CB  . THR A 1 153 ? 137.774 124.483 89.735  1.00 77.95  ?  69  THR A CB  1 
ATOM   383  O OG1 . THR A 1 153 ? 137.267 125.349 88.712  1.00 75.44  ?  69  THR A OG1 1 
ATOM   384  C CG2 . THR A 1 153 ? 136.886 124.593 90.965  1.00 74.99  ?  69  THR A CG2 1 
ATOM   385  N N   . PRO A 1 154 ? 140.501 122.757 90.190  1.00 78.42  ?  70  PRO A N   1 
ATOM   386  C CA  . PRO A 1 154 ? 141.359 121.825 90.938  1.00 75.57  ?  70  PRO A CA  1 
ATOM   387  C C   . PRO A 1 154 ? 142.469 122.530 91.690  1.00 74.11  ?  70  PRO A C   1 
ATOM   388  O O   . PRO A 1 154 ? 142.880 122.064 92.761  1.00 73.12  ?  70  PRO A O   1 
ATOM   389  C CB  . PRO A 1 154 ? 141.915 120.901 89.849  1.00 73.24  ?  70  PRO A CB  1 
ATOM   390  C CG  . PRO A 1 154 ? 140.920 120.937 88.770  1.00 74.98  ?  70  PRO A CG  1 
ATOM   391  C CD  . PRO A 1 154 ? 140.172 122.234 88.850  1.00 72.08  ?  70  PRO A CD  1 
ATOM   392  N N   . VAL A 1 155 ? 142.964 123.649 91.157  1.00 68.64  ?  71  VAL A N   1 
ATOM   393  C CA  . VAL A 1 155 ? 143.915 124.466 91.902  1.00 60.09  ?  71  VAL A CA  1 
ATOM   394  C C   . VAL A 1 155 ? 143.286 124.947 93.201  1.00 65.15  ?  71  VAL A C   1 
ATOM   395  O O   . VAL A 1 155 ? 143.923 124.920 94.260  1.00 71.23  ?  71  VAL A O   1 
ATOM   396  C CB  . VAL A 1 155 ? 144.406 125.642 91.038  1.00 58.43  ?  71  VAL A CB  1 
ATOM   397  C CG1 . VAL A 1 155 ? 145.151 126.651 91.891  1.00 62.38  ?  71  VAL A CG1 1 
ATOM   398  C CG2 . VAL A 1 155 ? 145.286 125.135 89.910  1.00 63.37  ?  71  VAL A CG2 1 
ATOM   399  N N   . LEU A 1 156 ? 142.023 125.376 93.146  1.00 65.32  ?  72  LEU A N   1 
ATOM   400  C CA  . LEU A 1 156 ? 141.334 125.804 94.360  1.00 63.51  ?  72  LEU A CA  1 
ATOM   401  C C   . LEU A 1 156 ? 141.281 124.671 95.374  1.00 63.08  ?  72  LEU A C   1 
ATOM   402  O O   . LEU A 1 156 ? 141.606 124.864 96.550  1.00 67.20  ?  72  LEU A O   1 
ATOM   403  C CB  . LEU A 1 156 ? 139.922 126.297 94.022  1.00 63.59  ?  72  LEU A CB  1 
ATOM   404  C CG  . LEU A 1 156 ? 139.010 127.050 95.011  1.00 65.12  ?  72  LEU A CG  1 
ATOM   405  C CD1 . LEU A 1 156 ? 137.656 127.285 94.364  1.00 67.73  ?  72  LEU A CD1 1 
ATOM   406  C CD2 . LEU A 1 156 ? 138.811 126.382 96.365  1.00 60.85  ?  72  LEU A CD2 1 
ATOM   407  N N   . SER A 1 157 ? 140.872 123.479 94.937  1.00 70.02  ?  73  SER A N   1 
ATOM   408  C CA  . SER A 1 157 ? 140.729 122.369 95.880  1.00 71.04  ?  73  SER A CA  1 
ATOM   409  C C   . SER A 1 157 ? 142.072 121.992 96.503  1.00 71.82  ?  73  SER A C   1 
ATOM   410  O O   . SER A 1 157 ? 142.189 121.849 97.730  1.00 73.13  ?  73  SER A O   1 
ATOM   411  C CB  . SER A 1 157 ? 140.099 121.164 95.183  1.00 72.21  ?  73  SER A CB  1 
ATOM   412  O OG  . SER A 1 157 ? 139.052 121.562 94.315  1.00 72.11  ?  73  SER A OG  1 
ATOM   413  N N   . TYR A 1 158 ? 143.100 121.831 95.666  1.00 75.22  ?  74  TYR A N   1 
ATOM   414  C CA  . TYR A 1 158 ? 144.410 121.427 96.168  1.00 72.07  ?  74  TYR A CA  1 
ATOM   415  C C   . TYR A 1 158 ? 144.991 122.481 97.100  1.00 69.12  ?  74  TYR A C   1 
ATOM   416  O O   . TYR A 1 158 ? 145.546 122.152 98.157  1.00 66.81  ?  74  TYR A O   1 
ATOM   417  C CB  . TYR A 1 158 ? 145.364 121.162 95.001  1.00 67.54  ?  74  TYR A CB  1 
ATOM   418  C CG  . TYR A 1 158 ? 144.878 120.148 93.982  1.00 70.58  ?  74  TYR A CG  1 
ATOM   419  C CD1 . TYR A 1 158 ? 143.773 119.342 94.232  1.00 69.73  ?  74  TYR A CD1 1 
ATOM   420  C CD2 . TYR A 1 158 ? 145.521 120.009 92.760  1.00 74.09  ?  74  TYR A CD2 1 
ATOM   421  C CE1 . TYR A 1 158 ? 143.330 118.425 93.300  1.00 73.97  ?  74  TYR A CE1 1 
ATOM   422  C CE2 . TYR A 1 158 ? 145.085 119.094 91.822  1.00 77.21  ?  74  TYR A CE2 1 
ATOM   423  C CZ  . TYR A 1 158 ? 143.990 118.305 92.097  1.00 80.74  ?  74  TYR A CZ  1 
ATOM   424  O OH  . TYR A 1 158 ? 143.552 117.391 91.166  1.00 79.68  ?  74  TYR A OH  1 
ATOM   425  N N   . SER A 1 159 ? 144.867 123.757 96.729  1.00 60.41  ?  75  SER A N   1 
ATOM   426  C CA  . SER A 1 159 ? 145.397 124.823 97.565  1.00 59.81  ?  75  SER A CA  1 
ATOM   427  C C   . SER A 1 159 ? 144.634 124.927 98.876  1.00 64.25  ?  75  SER A C   1 
ATOM   428  O O   . SER A 1 159 ? 145.228 125.225 99.912  1.00 71.34  ?  75  SER A O   1 
ATOM   429  C CB  . SER A 1 159 ? 145.360 126.147 96.806  1.00 64.85  ?  75  SER A CB  1 
ATOM   430  O OG  . SER A 1 159 ? 145.938 126.005 95.521  1.00 70.91  ?  75  SER A OG  1 
ATOM   431  N N   . TYR A 1 160 ? 143.323 124.680 98.863  1.00 62.54  ?  76  TYR A N   1 
ATOM   432  C CA  . TYR A 1 160 ? 142.574 124.671 100.115 1.00 57.27  ?  76  TYR A CA  1 
ATOM   433  C C   . TYR A 1 160 ? 143.078 123.570 101.034 1.00 58.78  ?  76  TYR A C   1 
ATOM   434  O O   . TYR A 1 160 ? 143.309 123.796 102.229 1.00 65.76  ?  76  TYR A O   1 
ATOM   435  C CB  . TYR A 1 160 ? 141.083 124.494 99.837  1.00 58.73  ?  76  TYR A CB  1 
ATOM   436  C CG  . TYR A 1 160 ? 140.226 124.513 101.081 1.00 60.77  ?  76  TYR A CG  1 
ATOM   437  C CD1 . TYR A 1 160 ? 140.536 125.342 102.148 1.00 61.21  ?  76  TYR A CD1 1 
ATOM   438  C CD2 . TYR A 1 160 ? 139.112 123.696 101.191 1.00 66.36  ?  76  TYR A CD2 1 
ATOM   439  C CE1 . TYR A 1 160 ? 139.757 125.361 103.286 1.00 58.35  ?  76  TYR A CE1 1 
ATOM   440  C CE2 . TYR A 1 160 ? 138.327 123.708 102.325 1.00 66.47  ?  76  TYR A CE2 1 
ATOM   441  C CZ  . TYR A 1 160 ? 138.655 124.542 103.369 1.00 61.14  ?  76  TYR A CZ  1 
ATOM   442  O OH  . TYR A 1 160 ? 137.875 124.559 104.501 1.00 62.70  ?  76  TYR A OH  1 
ATOM   443  N N   . LEU A 1 161 ? 143.275 122.371 100.481 1.00 66.05  ?  77  LEU A N   1 
ATOM   444  C CA  . LEU A 1 161 ? 143.758 121.264 101.302 1.00 69.60  ?  77  LEU A CA  1 
ATOM   445  C C   . LEU A 1 161 ? 145.147 121.553 101.861 1.00 70.16  ?  77  LEU A C   1 
ATOM   446  O O   . LEU A 1 161 ? 145.437 121.225 103.018 1.00 65.28  ?  77  LEU A O   1 
ATOM   447  C CB  . LEU A 1 161 ? 143.761 119.968 100.493 1.00 68.33  ?  77  LEU A CB  1 
ATOM   448  C CG  . LEU A 1 161 ? 142.681 118.957 100.883 1.00 71.29  ?  77  LEU A CG  1 
ATOM   449  C CD1 . LEU A 1 161 ? 142.851 117.660 100.107 1.00 67.91  ?  77  LEU A CD1 1 
ATOM   450  C CD2 . LEU A 1 161 ? 142.703 118.700 102.382 1.00 61.80  ?  77  LEU A CD2 1 
ATOM   451  N N   . ALA A 1 162 ? 146.019 122.168 101.059 1.00 67.03  ?  78  ALA A N   1 
ATOM   452  C CA  . ALA A 1 162 ? 147.382 122.436 101.507 1.00 62.23  ?  78  ALA A CA  1 
ATOM   453  C C   . ALA A 1 162 ? 147.509 123.707 102.341 1.00 58.39  ?  78  ALA A C   1 
ATOM   454  O O   . ALA A 1 162 ? 148.549 123.910 102.975 1.00 58.37  ?  78  ALA A O   1 
ATOM   455  C CB  . ALA A 1 162 ? 148.321 122.521 100.303 1.00 62.54  ?  78  ALA A CB  1 
ATOM   456  N N   . VAL A 1 163 ? 146.488 124.561 102.356 1.00 53.22  ?  79  VAL A N   1 
ATOM   457  C CA  . VAL A 1 163 ? 146.552 125.827 103.075 1.00 54.29  ?  79  VAL A CA  1 
ATOM   458  C C   . VAL A 1 163 ? 145.784 125.790 104.393 1.00 58.49  ?  79  VAL A C   1 
ATOM   459  O O   . VAL A 1 163 ? 146.112 126.561 105.308 1.00 57.48  ?  79  VAL A O   1 
ATOM   460  C CB  . VAL A 1 163 ? 146.051 126.973 102.164 1.00 56.54  ?  79  VAL A CB  1 
ATOM   461  C CG1 . VAL A 1 163 ? 145.638 128.202 102.956 1.00 59.47  ?  79  VAL A CG1 1 
ATOM   462  C CG2 . VAL A 1 163 ? 147.133 127.352 101.164 1.00 57.75  ?  79  VAL A CG2 1 
ATOM   463  N N   . LEU A 1 164 ? 144.810 124.888 104.539 1.00 61.93  ?  80  LEU A N   1 
ATOM   464  C CA  . LEU A 1 164 ? 144.104 124.782 105.812 1.00 57.91  ?  80  LEU A CA  1 
ATOM   465  C C   . LEU A 1 164 ? 145.064 124.522 106.969 1.00 60.00  ?  80  LEU A C   1 
ATOM   466  O O   . LEU A 1 164 ? 144.906 125.098 108.050 1.00 65.92  ?  80  LEU A O   1 
ATOM   467  C CB  . LEU A 1 164 ? 143.049 123.681 105.737 1.00 61.47  ?  80  LEU A CB  1 
ATOM   468  C CG  . LEU A 1 164 ? 141.860 123.798 106.691 1.00 58.17  ?  80  LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 164 ? 141.551 125.247 107.009 1.00 56.48  ?  80  LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 164 ? 140.648 123.116 106.089 1.00 63.29  ?  80  LEU A CD2 1 
ATOM   471  N N   . VAL A 1 165 ? 146.072 123.679 106.758 1.00 59.97  ?  81  VAL A N   1 
ATOM   472  C CA  . VAL A 1 165 ? 146.970 123.257 107.834 1.00 61.65  ?  81  VAL A CA  1 
ATOM   473  C C   . VAL A 1 165 ? 147.749 124.439 108.413 1.00 59.22  ?  81  VAL A C   1 
ATOM   474  O O   . VAL A 1 165 ? 147.661 124.675 109.630 1.00 62.34  ?  81  VAL A O   1 
ATOM   475  C CB  . VAL A 1 165 ? 147.914 122.137 107.363 1.00 64.25  ?  81  VAL A CB  1 
ATOM   476  C CG1 . VAL A 1 165 ? 149.097 122.007 108.308 1.00 65.34  ?  81  VAL A CG1 1 
ATOM   477  C CG2 . VAL A 1 165 ? 147.164 120.825 107.258 1.00 63.83  ?  81  VAL A CG2 1 
ATOM   478  N N   . PRO A 1 166 ? 148.511 125.212 107.624 1.00 59.46  ?  82  PRO A N   1 
ATOM   479  C CA  . PRO A 1 166 ? 149.193 126.368 108.230 1.00 59.99  ?  82  PRO A CA  1 
ATOM   480  C C   . PRO A 1 166 ? 148.227 127.370 108.822 1.00 57.99  ?  82  PRO A C   1 
ATOM   481  O O   . PRO A 1 166 ? 148.547 128.003 109.835 1.00 62.71  ?  82  PRO A O   1 
ATOM   482  C CB  . PRO A 1 166 ? 149.998 126.983 107.075 1.00 62.78  ?  82  PRO A CB  1 
ATOM   483  C CG  . PRO A 1 166 ? 149.676 126.234 105.870 1.00 62.47  ?  82  PRO A CG  1 
ATOM   484  C CD  . PRO A 1 166 ? 148.759 125.109 106.173 1.00 64.09  ?  82  PRO A CD  1 
ATOM   485  N N   . VAL A 1 167 ? 147.042 127.519 108.229 1.00 56.38  ?  83  VAL A N   1 
ATOM   486  C CA  . VAL A 1 167 ? 146.092 128.514 108.715 1.00 60.46  ?  83  VAL A CA  1 
ATOM   487  C C   . VAL A 1 167 ? 145.658 128.188 110.137 1.00 59.49  ?  83  VAL A C   1 
ATOM   488  O O   . VAL A 1 167 ? 145.703 129.047 111.022 1.00 65.01  ?  83  VAL A O   1 
ATOM   489  C CB  . VAL A 1 167 ? 144.887 128.625 107.766 1.00 63.56  ?  83  VAL A CB  1 
ATOM   490  C CG1 . VAL A 1 167 ? 143.708 129.241 108.494 1.00 56.06  ?  83  VAL A CG1 1 
ATOM   491  C CG2 . VAL A 1 167 ? 145.253 129.457 106.549 1.00 62.13  ?  83  VAL A CG2 1 
ATOM   492  N N   . PHE A 1 168 ? 145.239 126.944 110.388 1.00 56.69  ?  84  PHE A N   1 
ATOM   493  C CA  . PHE A 1 168 ? 144.818 126.622 111.747 1.00 57.26  ?  84  PHE A CA  1 
ATOM   494  C C   . PHE A 1 168 ? 145.994 126.402 112.686 1.00 60.96  ?  84  PHE A C   1 
ATOM   495  O O   . PHE A 1 168 ? 145.810 126.470 113.906 1.00 63.65  ?  84  PHE A O   1 
ATOM   496  C CB  . PHE A 1 168 ? 143.858 125.417 111.773 1.00 55.87  ?  84  PHE A CB  1 
ATOM   497  C CG  . PHE A 1 168 ? 144.479 124.079 111.424 1.00 58.77  ?  84  PHE A CG  1 
ATOM   498  C CD1 . PHE A 1 168 ? 145.432 123.483 112.234 1.00 57.46  ?  84  PHE A CD1 1 
ATOM   499  C CD2 . PHE A 1 168 ? 144.030 123.376 110.321 1.00 62.08  ?  84  PHE A CD2 1 
ATOM   500  C CE1 . PHE A 1 168 ? 145.969 122.253 111.916 1.00 60.27  ?  84  PHE A CE1 1 
ATOM   501  C CE2 . PHE A 1 168 ? 144.559 122.142 110.002 1.00 60.41  ?  84  PHE A CE2 1 
ATOM   502  C CZ  . PHE A 1 168 ? 145.530 121.581 110.800 1.00 59.37  ?  84  PHE A CZ  1 
ATOM   503  N N   . LEU A 1 169 ? 147.192 126.140 112.159 1.00 62.43  ?  85  LEU A N   1 
ATOM   504  C CA  . LEU A 1 169 ? 148.348 126.054 113.044 1.00 63.11  ?  85  LEU A CA  1 
ATOM   505  C C   . LEU A 1 169 ? 148.810 127.433 113.502 1.00 64.92  ?  85  LEU A C   1 
ATOM   506  O O   . LEU A 1 169 ? 149.390 127.560 114.585 1.00 64.27  ?  85  LEU A O   1 
ATOM   507  C CB  . LEU A 1 169 ? 149.490 125.309 112.355 1.00 62.33  ?  85  LEU A CB  1 
ATOM   508  C CG  . LEU A 1 169 ? 149.330 123.791 112.261 1.00 56.57  ?  85  LEU A CG  1 
ATOM   509  C CD1 . LEU A 1 169 ? 150.558 123.162 111.630 1.00 58.09  ?  85  LEU A CD1 1 
ATOM   510  C CD2 . LEU A 1 169 ? 149.064 123.195 113.630 1.00 55.75  ?  85  LEU A CD2 1 
ATOM   511  N N   . LEU A 1 170 ? 148.560 128.471 112.704 1.00 68.02  ?  86  LEU A N   1 
ATOM   512  C CA  . LEU A 1 170 ? 149.064 129.809 112.994 1.00 63.16  ?  86  LEU A CA  1 
ATOM   513  C C   . LEU A 1 170 ? 148.016 130.745 113.583 1.00 65.53  ?  86  LEU A C   1 
ATOM   514  O O   . LEU A 1 170 ? 148.366 131.626 114.374 1.00 71.91  ?  86  LEU A O   1 
ATOM   515  C CB  . LEU A 1 170 ? 149.642 130.435 111.721 1.00 58.51  ?  86  LEU A CB  1 
ATOM   516  C CG  . LEU A 1 170 ? 151.146 130.293 111.477 1.00 62.45  ?  86  LEU A CG  1 
ATOM   517  C CD1 . LEU A 1 170 ? 151.915 131.352 112.245 1.00 68.76  ?  86  LEU A CD1 1 
ATOM   518  C CD2 . LEU A 1 170 ? 151.641 128.905 111.847 1.00 62.47  ?  86  LEU A CD2 1 
ATOM   519  N N   . THR A 1 171 ? 146.740 130.588 113.217 1.00 60.08  ?  87  THR A N   1 
ATOM   520  C CA  . THR A 1 171 ? 145.711 131.507 113.697 1.00 58.59  ?  87  THR A CA  1 
ATOM   521  C C   . THR A 1 171 ? 145.570 131.449 115.210 1.00 59.24  ?  87  THR A C   1 
ATOM   522  O O   . THR A 1 171 ? 145.145 132.427 115.834 1.00 60.31  ?  87  THR A O   1 
ATOM   523  C CB  . THR A 1 171 ? 144.367 131.199 113.034 1.00 55.33  ?  87  THR A CB  1 
ATOM   524  O OG1 . THR A 1 171 ? 143.390 132.150 113.472 1.00 59.51  ?  87  THR A OG1 1 
ATOM   525  C CG2 . THR A 1 171 ? 143.891 129.811 113.403 1.00 58.78  ?  87  THR A CG2 1 
ATOM   526  N N   . ASP A 1 172 ? 145.913 130.313 115.811 1.00 72.63  ?  88  ASP A N   1 
ATOM   527  C CA  . ASP A 1 172 ? 145.861 130.190 117.259 1.00 75.23  ?  88  ASP A CA  1 
ATOM   528  C C   . ASP A 1 172 ? 146.955 131.016 117.923 1.00 75.53  ?  88  ASP A C   1 
ATOM   529  O O   . ASP A 1 172 ? 146.740 131.582 119.000 1.00 70.42  ?  88  ASP A O   1 
ATOM   530  C CB  . ASP A 1 172 ? 145.981 128.714 117.632 1.00 80.12  ?  88  ASP A CB  1 
ATOM   531  C CG  . ASP A 1 172 ? 145.087 128.326 118.781 1.00 84.24  ?  88  ASP A CG  1 
ATOM   532  O OD1 . ASP A 1 172 ? 144.149 129.086 119.100 1.00 80.45  ?  88  ASP A OD1 1 
ATOM   533  O OD2 . ASP A 1 172 ? 145.302 127.230 119.336 1.00 84.22  -1 88  ASP A OD2 1 
ATOM   534  N N   . TYR A 1 173 ? 148.120 131.113 117.281 1.00 78.13  ?  89  TYR A N   1 
ATOM   535  C CA  . TYR A 1 173 ? 149.263 131.822 117.846 1.00 70.55  ?  89  TYR A CA  1 
ATOM   536  C C   . TYR A 1 173 ? 149.160 133.325 117.612 1.00 72.27  ?  89  TYR A C   1 
ATOM   537  O O   . TYR A 1 173 ? 149.192 134.117 118.560 1.00 71.49  ?  89  TYR A O   1 
ATOM   538  C CB  . TYR A 1 173 ? 150.556 131.275 117.236 1.00 70.09  ?  89  TYR A CB  1 
ATOM   539  C CG  . TYR A 1 173 ? 151.819 131.744 117.916 1.00 72.95  ?  89  TYR A CG  1 
ATOM   540  C CD1 . TYR A 1 173 ? 151.844 132.000 119.279 1.00 74.66  ?  89  TYR A CD1 1 
ATOM   541  C CD2 . TYR A 1 173 ? 152.988 131.926 117.193 1.00 71.48  ?  89  TYR A CD2 1 
ATOM   542  C CE1 . TYR A 1 173 ? 153.000 132.426 119.903 1.00 73.56  ?  89  TYR A CE1 1 
ATOM   543  C CE2 . TYR A 1 173 ? 154.148 132.351 117.807 1.00 73.58  ?  89  TYR A CE2 1 
ATOM   544  C CZ  . TYR A 1 173 ? 154.149 132.600 119.162 1.00 74.34  ?  89  TYR A CZ  1 
ATOM   545  O OH  . TYR A 1 173 ? 155.304 133.025 119.777 1.00 70.74  ?  89  TYR A OH  1 
ATOM   546  N N   . LEU A 1 174 ? 149.030 133.732 116.349 1.00 72.14  ?  90  LEU A N   1 
ATOM   547  C CA  . LEU A 1 174 ? 149.043 135.139 115.964 1.00 65.99  ?  90  LEU A CA  1 
ATOM   548  C C   . LEU A 1 174 ? 147.796 135.894 116.388 1.00 59.99  ?  90  LEU A C   1 
ATOM   549  O O   . LEU A 1 174 ? 147.676 137.072 116.037 1.00 61.03  ?  90  LEU A O   1 
ATOM   550  C CB  . LEU A 1 174 ? 149.198 135.267 114.448 1.00 55.46  ?  90  LEU A CB  1 
ATOM   551  C CG  . LEU A 1 174 ? 150.384 134.582 113.780 1.00 61.05  ?  90  LEU A CG  1 
ATOM   552  C CD1 . LEU A 1 174 ? 150.177 134.569 112.280 1.00 60.74  ?  90  LEU A CD1 1 
ATOM   553  C CD2 . LEU A 1 174 ? 151.678 135.284 114.140 1.00 64.31  ?  90  LEU A CD2 1 
ATOM   554  N N   . ARG A 1 175 ? 146.875 135.250 117.107 1.00 62.53  ?  91  ARG A N   1 
ATOM   555  C CA  . ARG A 1 175 ? 145.538 135.776 117.365 1.00 64.71  ?  91  ARG A CA  1 
ATOM   556  C C   . ARG A 1 175 ? 144.772 135.919 116.054 1.00 63.91  ?  91  ARG A C   1 
ATOM   557  O O   . ARG A 1 175 ? 145.365 135.940 114.972 1.00 72.47  ?  91  ARG A O   1 
ATOM   558  C CB  . ARG A 1 175 ? 145.596 137.101 118.128 1.00 66.03  ?  91  ARG A CB  1 
ATOM   559  C CG  . ARG A 1 175 ? 145.878 136.932 119.611 1.00 67.71  ?  91  ARG A CG  1 
ATOM   560  C CD  . ARG A 1 175 ? 147.342 137.168 119.930 1.00 62.62  ?  91  ARG A CD  1 
ATOM   561  N NE  . ARG A 1 175 ? 147.619 138.571 120.210 1.00 65.93  ?  91  ARG A NE  1 
ATOM   562  C CZ  . ARG A 1 175 ? 148.834 139.076 120.372 1.00 67.98  ?  91  ARG A CZ  1 
ATOM   563  N NH1 . ARG A 1 175 ? 149.914 138.319 120.281 1.00 68.36  1  91  ARG A NH1 1 
ATOM   564  N NH2 . ARG A 1 175 ? 148.968 140.373 120.630 1.00 68.71  ?  91  ARG A NH2 1 
ATOM   565  N N   . TYR A 1 176 ? 143.451 136.002 116.138 1.00 43.40  ?  92  TYR A N   1 
ATOM   566  C CA  . TYR A 1 176 ? 142.611 135.814 114.966 1.00 51.00  ?  92  TYR A CA  1 
ATOM   567  C C   . TYR A 1 176 ? 142.434 137.072 114.128 1.00 58.90  ?  92  TYR A C   1 
ATOM   568  O O   . TYR A 1 176 ? 142.007 136.972 112.971 1.00 61.51  ?  92  TYR A O   1 
ATOM   569  C CB  . TYR A 1 176 ? 141.252 135.276 115.410 1.00 55.91  ?  92  TYR A CB  1 
ATOM   570  C CG  . TYR A 1 176 ? 141.364 134.390 116.628 1.00 54.50  ?  92  TYR A CG  1 
ATOM   571  C CD1 . TYR A 1 176 ? 141.679 133.046 116.503 1.00 52.13  ?  92  TYR A CD1 1 
ATOM   572  C CD2 . TYR A 1 176 ? 141.171 134.900 117.904 1.00 58.58  ?  92  TYR A CD2 1 
ATOM   573  C CE1 . TYR A 1 176 ? 141.792 132.233 117.612 1.00 57.31  ?  92  TYR A CE1 1 
ATOM   574  C CE2 . TYR A 1 176 ? 141.283 134.095 119.018 1.00 59.61  ?  92  TYR A CE2 1 
ATOM   575  C CZ  . TYR A 1 176 ? 141.591 132.762 118.866 1.00 60.74  ?  92  TYR A CZ  1 
ATOM   576  O OH  . TYR A 1 176 ? 141.702 131.955 119.973 1.00 61.13  ?  92  TYR A OH  1 
ATOM   577  N N   . THR A 1 177 ? 142.747 138.246 114.672 1.00 58.90  ?  93  THR A N   1 
ATOM   578  C CA  . THR A 1 177 ? 142.641 139.472 113.884 1.00 48.68  ?  93  THR A CA  1 
ATOM   579  C C   . THR A 1 177 ? 143.608 139.502 112.705 1.00 51.74  ?  93  THR A C   1 
ATOM   580  O O   . THR A 1 177 ? 143.182 139.884 111.600 1.00 61.71  ?  93  THR A O   1 
ATOM   581  C CB  . THR A 1 177 ? 142.816 140.688 114.801 1.00 55.36  ?  93  THR A CB  1 
ATOM   582  O OG1 . THR A 1 177 ? 141.614 140.896 115.550 1.00 61.61  ?  93  THR A OG1 1 
ATOM   583  C CG2 . THR A 1 177 ? 143.123 141.937 113.990 1.00 55.31  ?  93  THR A CG2 1 
ATOM   584  N N   . PRO A 1 178 ? 144.896 139.155 112.852 1.00 51.20  ?  94  PRO A N   1 
ATOM   585  C CA  . PRO A 1 178 ? 145.757 139.103 111.658 1.00 51.25  ?  94  PRO A CA  1 
ATOM   586  C C   . PRO A 1 178 ? 145.265 138.135 110.599 1.00 50.43  ?  94  PRO A C   1 
ATOM   587  O O   . PRO A 1 178 ? 145.382 138.424 109.405 1.00 55.19  ?  94  PRO A O   1 
ATOM   588  C CB  . PRO A 1 178 ? 147.117 138.679 112.226 1.00 53.69  ?  94  PRO A CB  1 
ATOM   589  C CG  . PRO A 1 178 ? 147.095 139.136 113.621 1.00 54.55  ?  94  PRO A CG  1 
ATOM   590  C CD  . PRO A 1 178 ? 145.682 138.973 114.085 1.00 54.87  ?  94  PRO A CD  1 
ATOM   591  N N   . VAL A 1 179 ? 144.703 136.994 110.998 1.00 51.82  ?  95  VAL A N   1 
ATOM   592  C CA  . VAL A 1 179 ? 144.224 136.029 110.013 1.00 48.13  ?  95  VAL A CA  1 
ATOM   593  C C   . VAL A 1 179 ? 142.961 136.537 109.329 1.00 52.19  ?  95  VAL A C   1 
ATOM   594  O O   . VAL A 1 179 ? 142.754 136.303 108.135 1.00 57.04  ?  95  VAL A O   1 
ATOM   595  C CB  . VAL A 1 179 ? 144.012 134.657 110.671 1.00 49.23  ?  95  VAL A CB  1 
ATOM   596  C CG1 . VAL A 1 179 ? 143.567 133.640 109.639 1.00 53.90  ?  95  VAL A CG1 1 
ATOM   597  C CG2 . VAL A 1 179 ? 145.296 134.209 111.333 1.00 50.43  ?  95  VAL A CG2 1 
ATOM   598  N N   . LEU A 1 180 ? 142.091 137.229 110.068 1.00 55.09  ?  96  LEU A N   1 
ATOM   599  C CA  . LEU A 1 180 ? 140.926 137.845 109.437 1.00 53.78  ?  96  LEU A CA  1 
ATOM   600  C C   . LEU A 1 180 ? 141.345 138.919 108.438 1.00 52.43  ?  96  LEU A C   1 
ATOM   601  O O   . LEU A 1 180 ? 140.787 139.013 107.336 1.00 51.86  ?  96  LEU A O   1 
ATOM   602  C CB  . LEU A 1 180 ? 140.002 138.427 110.504 1.00 50.20  ?  96  LEU A CB  1 
ATOM   603  C CG  . LEU A 1 180 ? 139.134 137.414 111.248 1.00 52.06  ?  96  LEU A CG  1 
ATOM   604  C CD1 . LEU A 1 180 ? 138.134 138.117 112.145 1.00 52.79  ?  96  LEU A CD1 1 
ATOM   605  C CD2 . LEU A 1 180 ? 138.422 136.512 110.259 1.00 52.22  ?  96  LEU A CD2 1 
ATOM   606  N N   . LEU A 1 181 ? 142.335 139.733 108.806 1.00 49.60  ?  97  LEU A N   1 
ATOM   607  C CA  . LEU A 1 181 ? 142.862 140.725 107.876 1.00 49.11  ?  97  LEU A CA  1 
ATOM   608  C C   . LEU A 1 181 ? 143.482 140.056 106.659 1.00 53.23  ?  97  LEU A C   1 
ATOM   609  O O   . LEU A 1 181 ? 143.359 140.554 105.535 1.00 57.68  ?  97  LEU A O   1 
ATOM   610  C CB  . LEU A 1 181 ? 143.887 141.610 108.583 1.00 43.94  ?  97  LEU A CB  1 
ATOM   611  C CG  . LEU A 1 181 ? 144.083 143.021 108.031 1.00 47.28  ?  97  LEU A CG  1 
ATOM   612  C CD1 . LEU A 1 181 ? 142.745 143.704 107.812 1.00 49.82  ?  97  LEU A CD1 1 
ATOM   613  C CD2 . LEU A 1 181 ? 144.960 143.832 108.967 1.00 52.76  ?  97  LEU A CD2 1 
ATOM   614  N N   . LEU A 1 182 ? 144.162 138.927 106.866 1.00 53.74  ?  98  LEU A N   1 
ATOM   615  C CA  . LEU A 1 182 ? 144.743 138.184 105.753 1.00 48.43  ?  98  LEU A CA  1 
ATOM   616  C C   . LEU A 1 182 ? 143.662 137.625 104.835 1.00 55.56  ?  98  LEU A C   1 
ATOM   617  O O   . LEU A 1 182 ? 143.824 137.620 103.612 1.00 62.66  ?  98  LEU A O   1 
ATOM   618  C CB  . LEU A 1 182 ? 145.653 137.079 106.298 1.00 52.90  ?  98  LEU A CB  1 
ATOM   619  C CG  . LEU A 1 182 ? 146.193 135.918 105.458 1.00 54.57  ?  98  LEU A CG  1 
ATOM   620  C CD1 . LEU A 1 182 ? 147.408 135.341 106.148 1.00 56.23  ?  98  LEU A CD1 1 
ATOM   621  C CD2 . LEU A 1 182 ? 145.158 134.821 105.319 1.00 56.03  ?  98  LEU A CD2 1 
ATOM   622  N N   . GLN A 1 183 ? 142.556 137.146 105.406 1.00 54.88  ?  99  GLN A N   1 
ATOM   623  C CA  . GLN A 1 183 ? 141.436 136.681 104.591 1.00 54.69  ?  99  GLN A CA  1 
ATOM   624  C C   . GLN A 1 183 ? 140.857 137.815 103.756 1.00 50.22  ?  99  GLN A C   1 
ATOM   625  O O   . GLN A 1 183 ? 140.591 137.653 102.557 1.00 56.82  ?  99  GLN A O   1 
ATOM   626  C CB  . GLN A 1 183 ? 140.354 136.073 105.482 1.00 50.54  ?  99  GLN A CB  1 
ATOM   627  C CG  . GLN A 1 183 ? 138.992 135.987 104.816 1.00 51.91  ?  99  GLN A CG  1 
ATOM   628  C CD  . GLN A 1 183 ? 137.972 135.247 105.654 1.00 61.47  ?  99  GLN A CD  1 
ATOM   629  O OE1 . GLN A 1 183 ? 138.135 135.101 106.865 1.00 63.50  ?  99  GLN A OE1 1 
ATOM   630  N NE2 . GLN A 1 183 ? 136.911 134.772 105.013 1.00 61.49  ?  99  GLN A NE2 1 
ATOM   631  N N   . GLY A 1 184 ? 140.654 138.978 104.375 1.00 46.52  ?  100 GLY A N   1 
ATOM   632  C CA  . GLY A 1 184 ? 140.145 140.116 103.626 1.00 50.12  ?  100 GLY A CA  1 
ATOM   633  C C   . GLY A 1 184 ? 141.088 140.552 102.520 1.00 52.58  ?  100 GLY A C   1 
ATOM   634  O O   . GLY A 1 184 ? 140.663 140.817 101.390 1.00 60.19  ?  100 GLY A O   1 
ATOM   635  N N   . LEU A 1 185 ? 142.384 140.624 102.826 1.00 47.06  ?  101 LEU A N   1 
ATOM   636  C CA  . LEU A 1 185 ? 143.364 141.016 101.823 1.00 46.88  ?  101 LEU A CA  1 
ATOM   637  C C   . LEU A 1 185 ? 143.477 139.977 100.718 1.00 53.25  ?  101 LEU A C   1 
ATOM   638  O O   . LEU A 1 185 ? 143.731 140.330 99.564  1.00 58.84  ?  101 LEU A O   1 
ATOM   639  C CB  . LEU A 1 185 ? 144.723 141.248 102.480 1.00 49.76  ?  101 LEU A CB  1 
ATOM   640  C CG  . LEU A 1 185 ? 144.855 142.546 103.276 1.00 52.54  ?  101 LEU A CG  1 
ATOM   641  C CD1 . LEU A 1 185 ? 146.257 142.688 103.839 1.00 58.03  ?  101 LEU A CD1 1 
ATOM   642  C CD2 . LEU A 1 185 ? 144.497 143.741 102.412 1.00 55.47  ?  101 LEU A CD2 1 
ATOM   643  N N   . SER A 1 186 ? 143.273 138.699 101.039 1.00 52.78  ?  102 SER A N   1 
ATOM   644  C CA  . SER A 1 186 ? 143.314 137.668 100.012 1.00 55.90  ?  102 SER A CA  1 
ATOM   645  C C   . SER A 1 186 ? 142.089 137.742 99.111  1.00 58.75  ?  102 SER A C   1 
ATOM   646  O O   . SER A 1 186 ? 142.185 137.479 97.911  1.00 63.39  ?  102 SER A O   1 
ATOM   647  C CB  . SER A 1 186 ? 143.436 136.290 100.657 1.00 53.44  ?  102 SER A CB  1 
ATOM   648  O OG  . SER A 1 186 ? 144.703 136.124 101.267 1.00 65.22  ?  102 SER A OG  1 
ATOM   649  N N   . PHE A 1 187 ? 140.947 138.147 99.674  1.00 58.70  ?  103 PHE A N   1 
ATOM   650  C CA  . PHE A 1 187 ? 139.751 138.346 98.815  1.00 49.94  ?  103 PHE A CA  1 
ATOM   651  C C   . PHE A 1 187 ? 140.012 139.543 97.895  1.00 51.66  ?  103 PHE A C   1 
ATOM   652  O O   . PHE A 1 187 ? 139.685 139.459 96.696  1.00 63.52  ?  103 PHE A O   1 
ATOM   653  C CB  . PHE A 1 187 ? 138.487 138.537 99.656  1.00 55.88  ?  103 PHE A CB  1 
ATOM   654  C CG  . PHE A 1 187 ? 137.651 137.292 99.808  1.00 58.88  ?  103 PHE A CG  1 
ATOM   655  C CD1 . PHE A 1 187 ? 137.266 136.561 98.696  1.00 59.45  ?  103 PHE A CD1 1 
ATOM   656  C CD2 . PHE A 1 187 ? 137.232 136.862 101.056 1.00 55.88  ?  103 PHE A CD2 1 
ATOM   657  C CE1 . PHE A 1 187 ? 136.496 135.417 98.830  1.00 58.50  ?  103 PHE A CE1 1 
ATOM   658  C CE2 . PHE A 1 187 ? 136.458 135.720 101.189 1.00 56.22  ?  103 PHE A CE2 1 
ATOM   659  C CZ  . PHE A 1 187 ? 136.092 134.999 100.076 1.00 61.00  ?  103 PHE A CZ  1 
ATOM   660  N N   . VAL A 1 188 ? 140.590 140.617 98.442  1.00 53.37  ?  104 VAL A N   1 
ATOM   661  C CA  . VAL A 1 188 ? 140.922 141.779 97.623  1.00 51.38  ?  104 VAL A CA  1 
ATOM   662  C C   . VAL A 1 188 ? 141.894 141.387 96.518  1.00 59.06  ?  104 VAL A C   1 
ATOM   663  O O   . VAL A 1 188 ? 141.764 141.831 95.372  1.00 67.12  ?  104 VAL A O   1 
ATOM   664  C CB  . VAL A 1 188 ? 141.485 142.911 98.501  1.00 58.30  ?  104 VAL A CB  1 
ATOM   665  C CG1 . VAL A 1 188 ? 142.165 143.963 97.645  1.00 56.41  ?  104 VAL A CG1 1 
ATOM   666  C CG2 . VAL A 1 188 ? 140.375 143.536 99.322  1.00 58.60  ?  104 VAL A CG2 1 
ATOM   667  N N   . SER A 1 189 ? 142.876 140.543 96.841  1.00 54.61  ?  105 SER A N   1 
ATOM   668  C CA  . SER A 1 189 ? 143.825 140.076 95.836  1.00 55.70  ?  105 SER A CA  1 
ATOM   669  C C   . SER A 1 189 ? 143.147 139.195 94.795  1.00 56.19  ?  105 SER A C   1 
ATOM   670  O O   . SER A 1 189 ? 143.492 139.252 93.610  1.00 61.84  ?  105 SER A O   1 
ATOM   671  C CB  . SER A 1 189 ? 144.970 139.324 96.507  1.00 53.46  ?  105 SER A CB  1 
ATOM   672  O OG  . SER A 1 189 ? 145.861 138.799 95.540  1.00 60.17  ?  105 SER A OG  1 
ATOM   673  N N   . VAL A 1 190 ? 142.187 138.370 95.217  1.00 52.92  ?  106 VAL A N   1 
ATOM   674  C CA  . VAL A 1 190 ? 141.436 137.547 94.272  1.00 53.76  ?  106 VAL A CA  1 
ATOM   675  C C   . VAL A 1 190 ? 140.742 138.432 93.251  1.00 55.56  ?  106 VAL A C   1 
ATOM   676  O O   . VAL A 1 190 ? 140.823 138.200 92.039  1.00 63.75  ?  106 VAL A O   1 
ATOM   677  C CB  . VAL A 1 190 ? 140.420 136.661 95.015  1.00 51.19  ?  106 VAL A CB  1 
ATOM   678  C CG1 . VAL A 1 190 ? 139.314 136.221 94.072  1.00 48.94  ?  106 VAL A CG1 1 
ATOM   679  C CG2 . VAL A 1 190 ? 141.097 135.459 95.616  1.00 57.49  ?  106 VAL A CG2 1 
ATOM   680  N N   . TRP A 1 191 ? 140.064 139.479 93.726  1.00 52.23  ?  107 TRP A N   1 
ATOM   681  C CA  . TRP A 1 191 ? 139.302 140.327 92.770  1.00 51.40  ?  107 TRP A CA  1 
ATOM   682  C C   . TRP A 1 191 ? 140.268 141.186 91.948  1.00 59.44  ?  107 TRP A C   1 
ATOM   683  O O   . TRP A 1 191 ? 139.958 141.443 90.769  1.00 70.07  ?  107 TRP A O   1 
ATOM   684  C CB  . TRP A 1 191 ? 138.223 141.160 93.474  1.00 53.45  ?  107 TRP A CB  1 
ATOM   685  C CG  . TRP A 1 191 ? 136.865 140.556 93.300  1.00 61.35  ?  107 TRP A CG  1 
ATOM   686  C CD1 . TRP A 1 191 ? 135.877 140.984 92.462  1.00 63.07  ?  107 TRP A CD1 1 
ATOM   687  C CD2 . TRP A 1 191 ? 136.345 139.396 93.973  1.00 61.68  ?  107 TRP A CD2 1 
ATOM   688  N NE1 . TRP A 1 191 ? 134.782 140.168 92.562  1.00 66.26  ?  107 TRP A NE1 1 
ATOM   689  C CE2 . TRP A 1 191 ? 135.036 139.191 93.487  1.00 63.61  ?  107 TRP A CE2 1 
ATOM   690  C CE3 . TRP A 1 191 ? 136.851 138.516 94.936  1.00 61.03  ?  107 TRP A CE3 1 
ATOM   691  C CZ2 . TRP A 1 191 ? 134.233 138.144 93.936  1.00 60.90  ?  107 TRP A CZ2 1 
ATOM   692  C CZ3 . TRP A 1 191 ? 136.057 137.483 95.379  1.00 61.62  ?  107 TRP A CZ3 1 
ATOM   693  C CH2 . TRP A 1 191 ? 134.766 137.301 94.883  1.00 64.10  ?  107 TRP A CH2 1 
ATOM   694  N N   . LEU A 1 192 ? 141.396 141.601 92.533  1.00 54.95  ?  108 LEU A N   1 
ATOM   695  C CA  . LEU A 1 192 ? 142.379 142.342 91.752  1.00 56.87  ?  108 LEU A CA  1 
ATOM   696  C C   . LEU A 1 192 ? 142.943 141.486 90.626  1.00 63.78  ?  108 LEU A C   1 
ATOM   697  O O   . LEU A 1 192 ? 143.155 141.977 89.512  1.00 65.59  ?  108 LEU A O   1 
ATOM   698  C CB  . LEU A 1 192 ? 143.499 142.846 92.658  1.00 50.94  ?  108 LEU A CB  1 
ATOM   699  C CG  . LEU A 1 192 ? 143.419 144.321 93.044  1.00 54.68  ?  108 LEU A CG  1 
ATOM   700  C CD1 . LEU A 1 192 ? 144.668 144.742 93.794  1.00 62.07  ?  108 LEU A CD1 1 
ATOM   701  C CD2 . LEU A 1 192 ? 143.216 145.180 91.810  1.00 57.04  ?  108 LEU A CD2 1 
ATOM   702  N N   . LEU A 1 193 ? 143.202 140.206 90.901  1.00 58.99  ?  109 LEU A N   1 
ATOM   703  C CA  . LEU A 1 193 ? 143.652 139.300 89.852  1.00 56.55  ?  109 LEU A CA  1 
ATOM   704  C C   . LEU A 1 193 ? 142.550 139.052 88.832  1.00 57.24  ?  109 LEU A C   1 
ATOM   705  O O   . LEU A 1 193 ? 142.824 138.899 87.637  1.00 67.22  ?  109 LEU A O   1 
ATOM   706  C CB  . LEU A 1 193 ? 144.125 137.984 90.464  1.00 48.02  ?  109 LEU A CB  1 
ATOM   707  C CG  . LEU A 1 193 ? 145.589 137.969 90.898  1.00 53.54  ?  109 LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 193 ? 145.828 136.892 91.936  1.00 57.71  ?  109 LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 193 ? 146.492 137.770 89.697  1.00 56.36  ?  109 LEU A CD2 1 
ATOM   710  N N   . LEU A 1 194 ? 141.297 139.000 89.287  1.00 53.02  ?  110 LEU A N   1 
ATOM   711  C CA  . LEU A 1 194 ? 140.182 138.854 88.358  1.00 60.18  ?  110 LEU A CA  1 
ATOM   712  C C   . LEU A 1 194 ? 140.093 140.046 87.416  1.00 60.37  ?  110 LEU A C   1 
ATOM   713  O O   . LEU A 1 194 ? 139.879 139.879 86.210  1.00 59.08  ?  110 LEU A O   1 
ATOM   714  C CB  . LEU A 1 194 ? 138.873 138.687 89.128  1.00 59.42  ?  110 LEU A CB  1 
ATOM   715  C CG  . LEU A 1 194 ? 138.309 137.271 89.215  1.00 55.30  ?  110 LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 194 ? 137.089 137.234 90.116  1.00 59.14  ?  110 LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 194 ? 137.971 136.748 87.834  1.00 59.13  ?  110 LEU A CD2 1 
ATOM   718  N N   . LEU A 1 195 ? 140.256 141.258 87.945  1.00 63.30  ?  111 LEU A N   1 
ATOM   719  C CA  . LEU A 1 195 ? 140.123 142.461 87.135  1.00 64.93  ?  111 LEU A CA  1 
ATOM   720  C C   . LEU A 1 195 ? 141.401 142.845 86.403  1.00 67.74  ?  111 LEU A C   1 
ATOM   721  O O   . LEU A 1 195 ? 141.345 143.688 85.502  1.00 66.62  ?  111 LEU A O   1 
ATOM   722  C CB  . LEU A 1 195 ? 139.670 143.630 88.011  1.00 60.73  ?  111 LEU A CB  1 
ATOM   723  C CG  . LEU A 1 195 ? 138.252 143.520 88.563  1.00 63.31  ?  111 LEU A CG  1 
ATOM   724  C CD1 . LEU A 1 195 ? 138.155 144.198 89.916  1.00 64.73  ?  111 LEU A CD1 1 
ATOM   725  C CD2 . LEU A 1 195 ? 137.263 144.122 87.582  1.00 67.43  ?  111 LEU A CD2 1 
ATOM   726  N N   . LEU A 1 196 ? 142.543 142.261 86.759  1.00 65.18  ?  112 LEU A N   1 
ATOM   727  C CA  . LEU A 1 196 ? 143.818 142.620 86.145  1.00 61.10  ?  112 LEU A CA  1 
ATOM   728  C C   . LEU A 1 196 ? 144.637 141.374 85.843  1.00 69.67  ?  112 LEU A C   1 
ATOM   729  O O   . LEU A 1 196 ? 145.861 141.360 86.008  1.00 77.12  ?  112 LEU A O   1 
ATOM   730  C CB  . LEU A 1 196 ? 144.609 143.577 87.034  1.00 64.11  ?  112 LEU A CB  1 
ATOM   731  C CG  . LEU A 1 196 ? 144.004 144.963 87.251  1.00 70.16  ?  112 LEU A CG  1 
ATOM   732  C CD1 . LEU A 1 196 ? 144.758 145.711 88.335  1.00 68.92  ?  112 LEU A CD1 1 
ATOM   733  C CD2 . LEU A 1 196 ? 144.004 145.750 85.952  1.00 67.68  ?  112 LEU A CD2 1 
ATOM   734  N N   . GLY A 1 197 ? 143.976 140.312 85.395  1.00 73.41  ?  113 GLY A N   1 
ATOM   735  C CA  . GLY A 1 197 ? 144.671 139.085 85.066  1.00 72.91  ?  113 GLY A CA  1 
ATOM   736  C C   . GLY A 1 197 ? 144.249 138.511 83.732  1.00 75.60  ?  113 GLY A C   1 
ATOM   737  O O   . GLY A 1 197 ? 143.061 138.274 83.499  1.00 79.91  ?  113 GLY A O   1 
ATOM   738  N N   . HIS A 1 198 ? 145.214 138.284 82.844  1.00 86.17  ?  114 HIS A N   1 
ATOM   739  C CA  . HIS A 1 198 ? 144.943 137.752 81.515  1.00 84.47  ?  114 HIS A CA  1 
ATOM   740  C C   . HIS A 1 198 ? 145.383 136.305 81.351  1.00 86.22  ?  114 HIS A C   1 
ATOM   741  O O   . HIS A 1 198 ? 144.683 135.521 80.703  1.00 90.56  ?  114 HIS A O   1 
ATOM   742  C CB  . HIS A 1 198 ? 145.632 138.613 80.452  1.00 85.54  ?  114 HIS A CB  1 
ATOM   743  C CG  . HIS A 1 198 ? 147.027 139.017 80.815  1.00 93.30  ?  114 HIS A CG  1 
ATOM   744  N ND1 . HIS A 1 198 ? 147.301 140.057 81.678  1.00 93.12  ?  114 HIS A ND1 1 
ATOM   745  C CD2 . HIS A 1 198 ? 148.227 138.519 80.433  1.00 90.47  ?  114 HIS A CD2 1 
ATOM   746  C CE1 . HIS A 1 198 ? 148.609 140.183 81.811  1.00 89.38  ?  114 HIS A CE1 1 
ATOM   747  N NE2 . HIS A 1 198 ? 149.194 139.262 81.066  1.00 90.74  ?  114 HIS A NE2 1 
ATOM   748  N N   . SER A 1 199 ? 146.524 135.930 81.922  1.00 80.79  ?  115 SER A N   1 
ATOM   749  C CA  . SER A 1 199 ? 147.053 134.588 81.753  1.00 79.94  ?  115 SER A CA  1 
ATOM   750  C C   . SER A 1 199 ? 146.365 133.610 82.702  1.00 79.62  ?  115 SER A C   1 
ATOM   751  O O   . SER A 1 199 ? 145.699 133.993 83.666  1.00 81.53  ?  115 SER A O   1 
ATOM   752  C CB  . SER A 1 199 ? 148.563 134.576 81.983  1.00 81.38  ?  115 SER A CB  1 
ATOM   753  O OG  . SER A 1 199 ? 148.888 135.143 83.239  1.00 83.00  ?  115 SER A OG  1 
ATOM   754  N N   . VAL A 1 200 ? 146.535 132.319 82.409  1.00 75.77  ?  116 VAL A N   1 
ATOM   755  C CA  . VAL A 1 200 ? 145.972 131.281 83.265  1.00 74.34  ?  116 VAL A CA  1 
ATOM   756  C C   . VAL A 1 200 ? 146.701 131.228 84.601  1.00 75.86  ?  116 VAL A C   1 
ATOM   757  O O   . VAL A 1 200 ? 146.102 130.888 85.629  1.00 79.20  ?  116 VAL A O   1 
ATOM   758  C CB  . VAL A 1 200 ? 146.008 129.921 82.544  1.00 72.42  ?  116 VAL A CB  1 
ATOM   759  C CG1 . VAL A 1 200 ? 145.259 128.871 83.346  1.00 72.14  ?  116 VAL A CG1 1 
ATOM   760  C CG2 . VAL A 1 200 ? 145.421 130.047 81.151  1.00 73.83  ?  116 VAL A CG2 1 
ATOM   761  N N   . ALA A 1 201 ? 147.996 131.554 84.616  1.00 74.61  ?  117 ALA A N   1 
ATOM   762  C CA  . ALA A 1 201 ? 148.751 131.538 85.866  1.00 77.60  ?  117 ALA A CA  1 
ATOM   763  C C   . ALA A 1 201 ? 148.195 132.550 86.860  1.00 75.41  ?  117 ALA A C   1 
ATOM   764  O O   . ALA A 1 201 ? 148.147 132.285 88.068  1.00 77.59  ?  117 ALA A O   1 
ATOM   765  C CB  . ALA A 1 201 ? 150.229 131.811 85.589  1.00 76.88  ?  117 ALA A CB  1 
ATOM   766  N N   . HIS A 1 202 ? 147.777 133.719 86.372  1.00 71.98  ?  118 HIS A N   1 
ATOM   767  C CA  . HIS A 1 202 ? 147.150 134.699 87.251  1.00 72.04  ?  118 HIS A CA  1 
ATOM   768  C C   . HIS A 1 202 ? 145.875 134.142 87.871  1.00 72.94  ?  118 HIS A C   1 
ATOM   769  O O   . HIS A 1 202 ? 145.611 134.352 89.058  1.00 83.36  ?  118 HIS A O   1 
ATOM   770  C CB  . HIS A 1 202 ? 146.852 135.984 86.480  1.00 72.47  ?  118 HIS A CB  1 
ATOM   771  C CG  . HIS A 1 202 ? 148.076 136.693 85.993  1.00 76.61  ?  118 HIS A CG  1 
ATOM   772  N ND1 . HIS A 1 202 ? 148.149 137.283 84.750  1.00 76.48  ?  118 HIS A ND1 1 
ATOM   773  C CD2 . HIS A 1 202 ? 149.276 136.906 86.582  1.00 78.94  ?  118 HIS A CD2 1 
ATOM   774  C CE1 . HIS A 1 202 ? 149.340 137.831 84.595  1.00 77.26  ?  118 HIS A CE1 1 
ATOM   775  N NE2 . HIS A 1 202 ? 150.044 137.616 85.691  1.00 80.09  ?  118 HIS A NE2 1 
ATOM   776  N N   . MET A 1 203 ? 145.075 133.421 87.084  1.00 67.80  ?  119 MET A N   1 
ATOM   777  C CA  . MET A 1 203 ? 143.848 132.844 87.619  1.00 65.98  ?  119 MET A CA  1 
ATOM   778  C C   . MET A 1 203 ? 144.140 131.729 88.615  1.00 75.31  ?  119 MET A C   1 
ATOM   779  O O   . MET A 1 203 ? 143.412 131.570 89.600  1.00 84.48  ?  119 MET A O   1 
ATOM   780  C CB  . MET A 1 203 ? 142.976 132.328 86.479  1.00 69.85  ?  119 MET A CB  1 
ATOM   781  C CG  . MET A 1 203 ? 142.896 133.276 85.296  1.00 77.35  ?  119 MET A CG  1 
ATOM   782  S SD  . MET A 1 203 ? 142.638 135.016 85.696  1.00 90.31  ?  119 MET A SD  1 
ATOM   783  C CE  . MET A 1 203 ? 141.144 134.944 86.676  1.00 72.38  ?  119 MET A CE  1 
ATOM   784  N N   . GLN A 1 204 ? 145.195 130.950 88.380  1.00 66.61  ?  120 GLN A N   1 
ATOM   785  C CA  . GLN A 1 204 ? 145.585 129.936 89.355  1.00 63.67  ?  120 GLN A CA  1 
ATOM   786  C C   . GLN A 1 204 ? 146.040 130.575 90.663  1.00 67.97  ?  120 GLN A C   1 
ATOM   787  O O   . GLN A 1 204 ? 145.711 130.083 91.749  1.00 72.52  ?  120 GLN A O   1 
ATOM   788  C CB  . GLN A 1 204 ? 146.677 129.043 88.770  1.00 62.95  ?  120 GLN A CB  1 
ATOM   789  C CG  . GLN A 1 204 ? 146.254 128.337 87.495  1.00 68.01  ?  120 GLN A CG  1 
ATOM   790  C CD  . GLN A 1 204 ? 147.251 127.294 87.040  1.00 69.24  ?  120 GLN A CD  1 
ATOM   791  O OE1 . GLN A 1 204 ? 147.540 126.340 87.760  1.00 72.01  ?  120 GLN A OE1 1 
ATOM   792  N NE2 . GLN A 1 204 ? 147.778 127.468 85.835  1.00 65.50  ?  120 GLN A NE2 1 
ATOM   793  N N   . LEU A 1 205 ? 146.791 131.675 90.581  1.00 64.13  ?  121 LEU A N   1 
ATOM   794  C CA  . LEU A 1 205 ? 147.155 132.410 91.789  1.00 58.81  ?  121 LEU A CA  1 
ATOM   795  C C   . LEU A 1 205 ? 145.916 132.959 92.487  1.00 62.30  ?  121 LEU A C   1 
ATOM   796  O O   . LEU A 1 205 ? 145.832 132.961 93.723  1.00 65.35  ?  121 LEU A O   1 
ATOM   797  C CB  . LEU A 1 205 ? 148.126 133.537 91.442  1.00 58.19  ?  121 LEU A CB  1 
ATOM   798  C CG  . LEU A 1 205 ? 148.659 134.368 92.608  1.00 60.87  ?  121 LEU A CG  1 
ATOM   799  C CD1 . LEU A 1 205 ? 149.648 133.561 93.427  1.00 63.39  ?  121 LEU A CD1 1 
ATOM   800  C CD2 . LEU A 1 205 ? 149.300 135.646 92.098  1.00 65.69  ?  121 LEU A CD2 1 
ATOM   801  N N   . MET A 1 206 ? 144.943 133.431 91.706  1.00 66.11  ?  122 MET A N   1 
ATOM   802  C CA  . MET A 1 206 ? 143.675 133.864 92.279  1.00 62.48  ?  122 MET A CA  1 
ATOM   803  C C   . MET A 1 206 ? 142.995 132.722 93.018  1.00 69.43  ?  122 MET A C   1 
ATOM   804  O O   . MET A 1 206 ? 142.391 132.929 94.073  1.00 79.28  ?  122 MET A O   1 
ATOM   805  C CB  . MET A 1 206 ? 142.755 134.405 91.187  1.00 59.04  ?  122 MET A CB  1 
ATOM   806  C CG  . MET A 1 206 ? 141.297 134.045 91.404  1.00 59.70  ?  122 MET A CG  1 
ATOM   807  S SD  . MET A 1 206 ? 140.231 134.377 90.000  1.00 72.26  ?  122 MET A SD  1 
ATOM   808  C CE  . MET A 1 206 ? 139.000 133.100 90.231  1.00 69.98  ?  122 MET A CE  1 
ATOM   809  N N   . GLU A 1 207 ? 143.073 131.509 92.473  1.00 64.10  ?  123 GLU A N   1 
ATOM   810  C CA  . GLU A 1 207 ? 142.458 130.368 93.144  1.00 61.80  ?  123 GLU A CA  1 
ATOM   811  C C   . GLU A 1 207 ? 143.202 130.000 94.421  1.00 70.54  ?  123 GLU A C   1 
ATOM   812  O O   . GLU A 1 207 ? 142.580 129.596 95.409  1.00 78.41  ?  123 GLU A O   1 
ATOM   813  C CB  . GLU A 1 207 ? 142.379 129.175 92.199  1.00 59.39  ?  123 GLU A CB  1 
ATOM   814  C CG  . GLU A 1 207 ? 141.361 129.350 91.092  1.00 66.36  ?  123 GLU A CG  1 
ATOM   815  C CD  . GLU A 1 207 ? 139.938 129.072 91.546  1.00 74.99  ?  123 GLU A CD  1 
ATOM   816  O OE1 . GLU A 1 207 ? 139.644 129.220 92.748  1.00 70.99  ?  123 GLU A OE1 1 
ATOM   817  O OE2 . GLU A 1 207 ? 139.106 128.692 90.699  1.00 80.67  -1 123 GLU A OE2 1 
ATOM   818  N N   . LEU A 1 208 ? 144.531 130.122 94.423  1.00 62.78  ?  124 LEU A N   1 
ATOM   819  C CA  . LEU A 1 208 ? 145.271 129.955 95.672  1.00 56.79  ?  124 LEU A CA  1 
ATOM   820  C C   . LEU A 1 208 ? 144.798 130.955 96.720  1.00 62.02  ?  124 LEU A C   1 
ATOM   821  O O   . LEU A 1 208 ? 144.566 130.597 97.881  1.00 69.17  ?  124 LEU A O   1 
ATOM   822  C CB  . LEU A 1 208 ? 146.777 130.100 95.445  1.00 58.41  ?  124 LEU A CB  1 
ATOM   823  C CG  . LEU A 1 208 ? 147.608 128.876 95.051  1.00 65.73  ?  124 LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 208 ? 147.771 128.734 93.554  1.00 67.50  ?  124 LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 208 ? 148.967 128.944 95.729  1.00 61.69  ?  124 LEU A CD2 1 
ATOM   826  N N   . PHE A 1 209 ? 144.634 132.217 96.321  1.00 56.11  ?  125 PHE A N   1 
ATOM   827  C CA  . PHE A 1 209 ? 144.174 133.226 97.270  1.00 56.36  ?  125 PHE A CA  1 
ATOM   828  C C   . PHE A 1 209 ? 142.740 132.958 97.718  1.00 58.77  ?  125 PHE A C   1 
ATOM   829  O O   . PHE A 1 209 ? 142.390 133.207 98.877  1.00 69.63  ?  125 PHE A O   1 
ATOM   830  C CB  . PHE A 1 209 ? 144.305 134.619 96.662  1.00 56.25  ?  125 PHE A CB  1 
ATOM   831  C CG  . PHE A 1 209 ? 145.703 135.156 96.681  1.00 59.11  ?  125 PHE A CG  1 
ATOM   832  C CD1 . PHE A 1 209 ? 146.443 135.149 97.849  1.00 58.53  ?  125 PHE A CD1 1 
ATOM   833  C CD2 . PHE A 1 209 ? 146.279 135.667 95.534  1.00 59.18  ?  125 PHE A CD2 1 
ATOM   834  C CE1 . PHE A 1 209 ? 147.729 135.640 97.873  1.00 59.42  ?  125 PHE A CE1 1 
ATOM   835  C CE2 . PHE A 1 209 ? 147.566 136.161 95.551  1.00 60.39  ?  125 PHE A CE2 1 
ATOM   836  C CZ  . PHE A 1 209 ? 148.292 136.147 96.722  1.00 63.86  ?  125 PHE A CZ  1 
ATOM   837  N N   . TYR A 1 210 ? 141.897 132.451 96.819  1.00 45.21  ?  126 TYR A N   1 
ATOM   838  C CA  . TYR A 1 210 ? 140.528 132.108 97.194  1.00 53.31  ?  126 TYR A CA  1 
ATOM   839  C C   . TYR A 1 210 ? 140.501 130.958 98.191  1.00 60.36  ?  126 TYR A C   1 
ATOM   840  O O   . TYR A 1 210 ? 139.695 130.959 99.127  1.00 71.23  ?  126 TYR A O   1 
ATOM   841  C CB  . TYR A 1 210 ? 139.710 131.760 95.952  1.00 54.49  ?  126 TYR A CB  1 
ATOM   842  C CG  . TYR A 1 210 ? 138.229 131.999 96.123  1.00 55.79  ?  126 TYR A CG  1 
ATOM   843  C CD1 . TYR A 1 210 ? 137.452 131.137 96.882  1.00 56.96  ?  126 TYR A CD1 1 
ATOM   844  C CD2 . TYR A 1 210 ? 137.609 133.088 95.530  1.00 59.32  ?  126 TYR A CD2 1 
ATOM   845  C CE1 . TYR A 1 210 ? 136.101 131.352 97.046  1.00 57.87  ?  126 TYR A CE1 1 
ATOM   846  C CE2 . TYR A 1 210 ? 136.257 133.310 95.687  1.00 66.53  ?  126 TYR A CE2 1 
ATOM   847  C CZ  . TYR A 1 210 ? 135.509 132.439 96.447  1.00 67.64  ?  126 TYR A CZ  1 
ATOM   848  O OH  . TYR A 1 210 ? 134.160 132.656 96.607  1.00 70.07  ?  126 TYR A OH  1 
ATOM   849  N N   . SER A 1 211 ? 141.366 129.963 98.000  1.00 54.05  ?  127 SER A N   1 
ATOM   850  C CA  . SER A 1 211 ? 141.484 128.889 98.978  1.00 49.83  ?  127 SER A CA  1 
ATOM   851  C C   . SER A 1 211 ? 141.965 129.425 100.319 1.00 54.18  ?  127 SER A C   1 
ATOM   852  O O   . SER A 1 211 ? 141.506 128.981 101.378 1.00 62.52  ?  127 SER A O   1 
ATOM   853  C CB  . SER A 1 211 ? 142.437 127.819 98.460  1.00 56.98  ?  127 SER A CB  1 
ATOM   854  O OG  . SER A 1 211 ? 143.766 128.306 98.446  1.00 64.05  ?  127 SER A OG  1 
ATOM   855  N N   . VAL A 1 212 ? 142.895 130.381 100.289 1.00 54.42  ?  128 VAL A N   1 
ATOM   856  C CA  . VAL A 1 212 ? 143.348 131.022 101.521 1.00 58.23  ?  128 VAL A CA  1 
ATOM   857  C C   . VAL A 1 212 ? 142.185 131.715 102.222 1.00 64.44  ?  128 VAL A C   1 
ATOM   858  O O   . VAL A 1 212 ? 142.050 131.646 103.450 1.00 65.78  ?  128 VAL A O   1 
ATOM   859  C CB  . VAL A 1 212 ? 144.497 132.001 101.218 1.00 55.21  ?  128 VAL A CB  1 
ATOM   860  C CG1 . VAL A 1 212 ? 144.796 132.858 102.425 1.00 56.61  ?  128 VAL A CG1 1 
ATOM   861  C CG2 . VAL A 1 212 ? 145.738 131.241 100.794 1.00 53.06  ?  128 VAL A CG2 1 
ATOM   862  N N   . THR A 1 213 ? 141.332 132.401 101.457 1.00 58.70  ?  129 THR A N   1 
ATOM   863  C CA  . THR A 1 213 ? 140.146 133.022 102.045 1.00 54.89  ?  129 THR A CA  1 
ATOM   864  C C   . THR A 1 213 ? 139.213 131.978 102.641 1.00 54.87  ?  129 THR A C   1 
ATOM   865  O O   . THR A 1 213 ? 138.673 132.169 103.737 1.00 63.39  ?  129 THR A O   1 
ATOM   866  C CB  . THR A 1 213 ? 139.392 133.847 101.003 1.00 51.17  ?  129 THR A CB  1 
ATOM   867  O OG1 . THR A 1 213 ? 138.960 132.995 99.938  1.00 59.11  ?  129 THR A OG1 1 
ATOM   868  C CG2 . THR A 1 213 ? 140.263 134.942 100.448 1.00 53.05  ?  129 THR A CG2 1 
ATOM   869  N N   . MET A 1 214 ? 139.001 130.872 101.928 1.00 55.88  ?  130 MET A N   1 
ATOM   870  C CA  . MET A 1 214 ? 138.100 129.829 102.403 1.00 57.63  ?  130 MET A CA  1 
ATOM   871  C C   . MET A 1 214 ? 138.641 129.106 103.627 1.00 62.24  ?  130 MET A C   1 
ATOM   872  O O   . MET A 1 214 ? 137.858 128.513 104.376 1.00 70.23  ?  130 MET A O   1 
ATOM   873  C CB  . MET A 1 214 ? 137.830 128.815 101.292 1.00 58.37  ?  130 MET A CB  1 
ATOM   874  C CG  . MET A 1 214 ? 136.997 129.350 100.145 1.00 61.07  ?  130 MET A CG  1 
ATOM   875  S SD  . MET A 1 214 ? 136.409 128.057 99.034  1.00 65.92  ?  130 MET A SD  1 
ATOM   876  C CE  . MET A 1 214 ? 136.997 126.584 99.865  1.00 63.23  ?  130 MET A CE  1 
ATOM   877  N N   . ALA A 1 215 ? 139.953 129.136 103.846 1.00 56.41  ?  131 ALA A N   1 
ATOM   878  C CA  . ALA A 1 215 ? 140.539 128.451 104.988 1.00 52.93  ?  131 ALA A CA  1 
ATOM   879  C C   . ALA A 1 215 ? 140.502 129.272 106.270 1.00 57.16  ?  131 ALA A C   1 
ATOM   880  O O   . ALA A 1 215 ? 140.821 128.734 107.334 1.00 65.49  ?  131 ALA A O   1 
ATOM   881  C CB  . ALA A 1 215 ? 141.985 128.059 104.679 1.00 54.05  ?  131 ALA A CB  1 
ATOM   882  N N   . ALA A 1 216 ? 140.112 130.544 106.206 1.00 58.69  ?  132 ALA A N   1 
ATOM   883  C CA  . ALA A 1 216 ? 140.211 131.448 107.344 1.00 60.98  ?  132 ALA A CA  1 
ATOM   884  C C   . ALA A 1 216 ? 138.872 131.726 108.018 1.00 63.41  ?  132 ALA A C   1 
ATOM   885  O O   . ALA A 1 216 ? 138.761 132.704 108.763 1.00 69.07  ?  132 ALA A O   1 
ATOM   886  C CB  . ALA A 1 216 ? 140.859 132.764 106.913 1.00 52.67  ?  132 ALA A CB  1 
ATOM   887  N N   . ARG A 1 217 ? 137.852 130.902 107.773 1.00 57.89  ?  133 ARG A N   1 
ATOM   888  C CA  . ARG A 1 217 ? 136.587 131.063 108.485 1.00 62.71  ?  133 ARG A CA  1 
ATOM   889  C C   . ARG A 1 217 ? 136.712 130.651 109.948 1.00 65.78  ?  133 ARG A C   1 
ATOM   890  O O   . ARG A 1 217 ? 136.039 131.222 110.822 1.00 66.49  ?  133 ARG A O   1 
ATOM   891  C CB  . ARG A 1 217 ? 135.496 130.252 107.790 1.00 64.47  ?  133 ARG A CB  1 
ATOM   892  C CG  . ARG A 1 217 ? 135.716 130.082 106.294 1.00 61.69  ?  133 ARG A CG  1 
ATOM   893  C CD  . ARG A 1 217 ? 134.553 129.347 105.646 1.00 68.23  ?  133 ARG A CD  1 
ATOM   894  N NE  . ARG A 1 217 ? 134.617 129.373 104.190 1.00 72.21  ?  133 ARG A NE  1 
ATOM   895  C CZ  . ARG A 1 217 ? 134.325 130.430 103.443 1.00 66.67  ?  133 ARG A CZ  1 
ATOM   896  N NH1 . ARG A 1 217 ? 133.958 131.579 103.983 1.00 64.29  1  133 ARG A NH1 1 
ATOM   897  N NH2 . ARG A 1 217 ? 134.403 130.330 102.119 1.00 67.13  ?  133 ARG A NH2 1 
ATOM   898  N N   . ILE A 1 218 ? 137.564 129.662 110.226 1.00 60.34  ?  134 ILE A N   1 
ATOM   899  C CA  . ILE A 1 218 ? 137.829 129.253 111.600 1.00 65.15  ?  134 ILE A CA  1 
ATOM   900  C C   . ILE A 1 218 ? 138.368 130.423 112.407 1.00 64.55  ?  134 ILE A C   1 
ATOM   901  O O   . ILE A 1 218 ? 138.103 130.533 113.612 1.00 68.28  ?  134 ILE A O   1 
ATOM   902  C CB  . ILE A 1 218 ? 138.798 128.055 111.610 1.00 67.63  ?  134 ILE A CB  1 
ATOM   903  C CG1 . ILE A 1 218 ? 140.149 128.459 111.014 1.00 62.01  ?  134 ILE A CG1 1 
ATOM   904  C CG2 . ILE A 1 218 ? 138.201 126.893 110.835 1.00 64.33  ?  134 ILE A CG2 1 
ATOM   905  C CD1 . ILE A 1 218 ? 141.002 127.303 110.562 1.00 64.12  ?  134 ILE A CD1 1 
ATOM   906  N N   . ALA A 1 219 ? 139.120 131.317 111.761 1.00 52.44  ?  135 ALA A N   1 
ATOM   907  C CA  . ALA A 1 219 ? 139.593 132.514 112.442 1.00 50.53  ?  135 ALA A CA  1 
ATOM   908  C C   . ALA A 1 219 ? 138.428 133.371 112.906 1.00 53.27  ?  135 ALA A C   1 
ATOM   909  O O   . ALA A 1 219 ? 138.415 133.841 114.046 1.00 57.58  ?  135 ALA A O   1 
ATOM   910  C CB  . ALA A 1 219 ? 140.514 133.313 111.524 1.00 48.89  ?  135 ALA A CB  1 
ATOM   911  N N   . TYR A 1 220 ? 137.427 133.567 112.045 1.00 52.78  ?  136 TYR A N   1 
ATOM   912  C CA  . TYR A 1 220 ? 136.264 134.356 112.438 1.00 55.96  ?  136 TYR A CA  1 
ATOM   913  C C   . TYR A 1 220 ? 135.502 133.696 113.578 1.00 56.78  ?  136 TYR A C   1 
ATOM   914  O O   . TYR A 1 220 ? 135.095 134.369 114.534 1.00 62.50  ?  136 TYR A O   1 
ATOM   915  C CB  . TYR A 1 220 ? 135.343 134.572 111.240 1.00 55.57  ?  136 TYR A CB  1 
ATOM   916  C CG  . TYR A 1 220 ? 134.111 135.384 111.563 1.00 57.34  ?  136 TYR A CG  1 
ATOM   917  C CD1 . TYR A 1 220 ? 134.181 136.764 111.696 1.00 59.03  ?  136 TYR A CD1 1 
ATOM   918  C CD2 . TYR A 1 220 ? 132.879 134.772 111.739 1.00 53.09  ?  136 TYR A CD2 1 
ATOM   919  C CE1 . TYR A 1 220 ? 133.059 137.508 111.993 1.00 60.61  ?  136 TYR A CE1 1 
ATOM   920  C CE2 . TYR A 1 220 ? 131.753 135.509 112.035 1.00 56.05  ?  136 TYR A CE2 1 
ATOM   921  C CZ  . TYR A 1 220 ? 131.848 136.876 112.160 1.00 59.81  ?  136 TYR A CZ  1 
ATOM   922  O OH  . TYR A 1 220 ? 130.727 137.613 112.455 1.00 57.59  ?  136 TYR A OH  1 
ATOM   923  N N   . SER A 1 221 ? 135.291 132.380 113.496 1.00 56.37  ?  137 SER A N   1 
ATOM   924  C CA  . SER A 1 221 ? 134.544 131.699 114.552 1.00 56.62  ?  137 SER A CA  1 
ATOM   925  C C   . SER A 1 221 ? 135.268 131.798 115.892 1.00 58.20  ?  137 SER A C   1 
ATOM   926  O O   . SER A 1 221 ? 134.694 132.240 116.899 1.00 66.90  ?  137 SER A O   1 
ATOM   927  C CB  . SER A 1 221 ? 134.314 130.238 114.168 1.00 63.07  ?  137 SER A CB  1 
ATOM   928  O OG  . SER A 1 221 ? 133.860 130.132 112.831 1.00 68.97  ?  137 SER A OG  1 
ATOM   929  N N   . SER A 1 222 ? 136.545 131.415 115.921 1.00 47.99  ?  138 SER A N   1 
ATOM   930  C CA  . SER A 1 222 ? 137.309 131.511 117.156 1.00 45.72  ?  138 SER A CA  1 
ATOM   931  C C   . SER A 1 222 ? 137.470 132.949 117.626 1.00 55.02  ?  138 SER A C   1 
ATOM   932  O O   . SER A 1 222 ? 137.630 133.180 118.827 1.00 61.53  ?  138 SER A O   1 
ATOM   933  C CB  . SER A 1 222 ? 138.675 130.864 116.968 1.00 55.35  ?  138 SER A CB  1 
ATOM   934  O OG  . SER A 1 222 ? 139.217 131.199 115.704 1.00 64.92  ?  138 SER A OG  1 
ATOM   935  N N   . TYR A 1 223 ? 137.423 133.924 116.714 1.00 52.80  ?  139 TYR A N   1 
ATOM   936  C CA  . TYR A 1 223 ? 137.540 135.317 117.121 1.00 46.79  ?  139 TYR A CA  1 
ATOM   937  C C   . TYR A 1 223 ? 136.279 135.796 117.819 1.00 52.21  ?  139 TYR A C   1 
ATOM   938  O O   . TYR A 1 223 ? 136.357 136.471 118.852 1.00 65.16  ?  139 TYR A O   1 
ATOM   939  C CB  . TYR A 1 223 ? 137.839 136.196 115.913 1.00 42.51  ?  139 TYR A CB  1 
ATOM   940  C CG  . TYR A 1 223 ? 138.024 137.643 116.277 1.00 51.71  ?  139 TYR A CG  1 
ATOM   941  C CD1 . TYR A 1 223 ? 138.964 138.022 117.219 1.00 54.74  ?  139 TYR A CD1 1 
ATOM   942  C CD2 . TYR A 1 223 ? 137.253 138.630 115.688 1.00 59.10  ?  139 TYR A CD2 1 
ATOM   943  C CE1 . TYR A 1 223 ? 139.137 139.340 117.558 1.00 50.11  ?  139 TYR A CE1 1 
ATOM   944  C CE2 . TYR A 1 223 ? 137.419 139.953 116.022 1.00 59.13  ?  139 TYR A CE2 1 
ATOM   945  C CZ  . TYR A 1 223 ? 138.363 140.302 116.958 1.00 52.01  ?  139 TYR A CZ  1 
ATOM   946  O OH  . TYR A 1 223 ? 138.532 141.623 117.296 1.00 58.28  ?  139 TYR A OH  1 
ATOM   947  N N   . ILE A 1 224 ? 135.106 135.471 117.269 1.00 52.35  ?  140 ILE A N   1 
ATOM   948  C CA  . ILE A 1 224 ? 133.876 135.826 117.971 1.00 51.54  ?  140 ILE A CA  1 
ATOM   949  C C   . ILE A 1 224 ? 133.804 135.086 119.294 1.00 52.68  ?  140 ILE A C   1 
ATOM   950  O O   . ILE A 1 224 ? 133.168 135.554 120.245 1.00 62.89  ?  140 ILE A O   1 
ATOM   951  C CB  . ILE A 1 224 ? 132.626 135.557 117.106 1.00 49.55  ?  140 ILE A CB  1 
ATOM   952  C CG1 . ILE A 1 224 ? 132.279 134.067 117.094 1.00 54.35  ?  140 ILE A CG1 1 
ATOM   953  C CG2 . ILE A 1 224 ? 132.814 136.098 115.703 1.00 56.37  ?  140 ILE A CG2 1 
ATOM   954  C CD1 . ILE A 1 224 ? 131.280 133.666 116.039 1.00 62.41  ?  140 ILE A CD1 1 
ATOM   955  N N   . PHE A 1 225 ? 134.456 133.927 119.386 1.00 54.18  ?  141 PHE A N   1 
ATOM   956  C CA  . PHE A 1 225 ? 134.400 133.167 120.629 1.00 46.88  ?  141 PHE A CA  1 
ATOM   957  C C   . PHE A 1 225 ? 135.371 133.700 121.677 1.00 45.65  ?  141 PHE A C   1 
ATOM   958  O O   . PHE A 1 225 ? 135.107 133.595 122.878 1.00 59.50  ?  141 PHE A O   1 
ATOM   959  C CB  . PHE A 1 225 ? 134.666 131.699 120.326 1.00 50.65  ?  141 PHE A CB  1 
ATOM   960  C CG  . PHE A 1 225 ? 133.438 130.952 119.934 1.00 49.61  ?  141 PHE A CG  1 
ATOM   961  C CD1 . PHE A 1 225 ? 133.450 129.585 119.822 1.00 56.11  ?  141 PHE A CD1 1 
ATOM   962  C CD2 . PHE A 1 225 ? 132.258 131.628 119.689 1.00 49.05  ?  141 PHE A CD2 1 
ATOM   963  C CE1 . PHE A 1 225 ? 132.316 128.904 119.463 1.00 63.33  ?  141 PHE A CE1 1 
ATOM   964  C CE2 . PHE A 1 225 ? 131.123 130.954 119.330 1.00 51.26  ?  141 PHE A CE2 1 
ATOM   965  C CZ  . PHE A 1 225 ? 131.150 129.588 119.217 1.00 63.53  ?  141 PHE A CZ  1 
ATOM   966  N N   . SER A 1 226 ? 136.497 134.269 121.249 1.00 55.71  ?  142 SER A N   1 
ATOM   967  C CA  . SER A 1 226 ? 137.529 134.711 122.179 1.00 62.39  ?  142 SER A CA  1 
ATOM   968  C C   . SER A 1 226 ? 137.247 136.072 122.802 1.00 64.57  ?  142 SER A C   1 
ATOM   969  O O   . SER A 1 226 ? 137.925 136.441 123.767 1.00 65.49  ?  142 SER A O   1 
ATOM   970  C CB  . SER A 1 226 ? 138.884 134.755 121.471 1.00 61.04  ?  142 SER A CB  1 
ATOM   971  O OG  . SER A 1 226 ? 139.929 135.015 122.390 1.00 69.30  ?  142 SER A OG  1 
ATOM   972  N N   . LEU A 1 227 ? 136.282 136.825 122.283 1.00 66.99  ?  143 LEU A N   1 
ATOM   973  C CA  . LEU A 1 227 ? 136.022 138.176 122.762 1.00 60.16  ?  143 LEU A CA  1 
ATOM   974  C C   . LEU A 1 227 ? 134.927 138.250 123.815 1.00 60.62  ?  143 LEU A C   1 
ATOM   975  O O   . LEU A 1 227 ? 134.645 139.345 124.311 1.00 62.00  ?  143 LEU A O   1 
ATOM   976  C CB  . LEU A 1 227 ? 135.644 139.087 121.590 1.00 61.49  ?  143 LEU A CB  1 
ATOM   977  C CG  . LEU A 1 227 ? 136.730 140.026 121.068 1.00 66.70  ?  143 LEU A CG  1 
ATOM   978  C CD1 . LEU A 1 227 ? 138.059 139.301 120.951 1.00 64.37  ?  143 LEU A CD1 1 
ATOM   979  C CD2 . LEU A 1 227 ? 136.315 140.613 119.731 1.00 64.46  ?  143 LEU A CD2 1 
ATOM   980  N N   . VAL A 1 228 ? 134.289 137.111 124.095 1.00 65.41  ?  144 VAL A N   1 
ATOM   981  C CA  . VAL A 1 228 ? 133.114 137.153 125.012 1.00 65.51  ?  144 VAL A CA  1 
ATOM   982  C C   . VAL A 1 228 ? 133.263 136.148 126.153 1.00 64.85  ?  144 VAL A C   1 
ATOM   983  O O   . VAL A 1 228 ? 133.980 135.141 125.977 1.00 66.14  ?  144 VAL A O   1 
ATOM   984  C CB  . VAL A 1 228 ? 131.804 136.904 124.237 1.00 63.65  ?  144 VAL A CB  1 
ATOM   985  C CG1 . VAL A 1 228 ? 131.575 137.962 123.169 1.00 60.73  ?  144 VAL A CG1 1 
ATOM   986  C CG2 . VAL A 1 228 ? 131.761 135.510 123.629 1.00 58.66  ?  144 VAL A CG2 1 
ATOM   987  N N   . ARG A 1 229 ? 132.615 136.431 127.281 1.00 68.52  ?  145 ARG A N   1 
ATOM   988  C CA  . ARG A 1 229 ? 132.595 135.525 128.414 1.00 68.35  ?  145 ARG A CA  1 
ATOM   989  C C   . ARG A 1 229 ? 131.957 134.202 127.993 1.00 72.08  ?  145 ARG A C   1 
ATOM   990  O O   . ARG A 1 229 ? 131.057 134.183 127.150 1.00 76.09  ?  145 ARG A O   1 
ATOM   991  C CB  . ARG A 1 229 ? 131.814 136.154 129.568 1.00 67.85  ?  145 ARG A CB  1 
ATOM   992  C CG  . ARG A 1 229 ? 131.998 135.496 130.925 1.00 66.65  ?  145 ARG A CG  1 
ATOM   993  C CD  . ARG A 1 229 ? 131.197 136.216 132.000 1.00 69.33  ?  145 ARG A CD  1 
ATOM   994  N NE  . ARG A 1 229 ? 131.932 136.318 133.255 1.00 76.04  ?  145 ARG A NE  1 
ATOM   995  C CZ  . ARG A 1 229 ? 131.797 137.310 134.125 1.00 75.55  ?  145 ARG A CZ  1 
ATOM   996  N NH1 . ARG A 1 229 ? 130.955 138.308 133.911 1.00 73.20  1  145 ARG A NH1 1 
ATOM   997  N NH2 . ARG A 1 229 ? 132.526 137.302 135.237 1.00 67.87  ?  145 ARG A NH2 1 
ATOM   998  N N   . PRO A 1 230 ? 132.415 133.077 128.551 1.00 66.21  ?  146 PRO A N   1 
ATOM   999  C CA  . PRO A 1 230 ? 131.839 131.783 128.149 1.00 60.04  ?  146 PRO A CA  1 
ATOM   1000 C C   . PRO A 1 230 ? 130.335 131.697 128.333 1.00 62.07  ?  146 PRO A C   1 
ATOM   1001 O O   . PRO A 1 230 ? 129.667 131.001 127.559 1.00 65.17  ?  146 PRO A O   1 
ATOM   1002 C CB  . PRO A 1 230 ? 132.578 130.785 129.048 1.00 60.90  ?  146 PRO A CB  1 
ATOM   1003 C CG  . PRO A 1 230 ? 133.897 131.424 129.284 1.00 65.32  ?  146 PRO A CG  1 
ATOM   1004 C CD  . PRO A 1 230 ? 133.640 132.907 129.352 1.00 65.74  ?  146 PRO A CD  1 
ATOM   1005 N N   . ALA A 1 231 ? 129.777 132.391 129.328 1.00 66.63  ?  147 ALA A N   1 
ATOM   1006 C CA  . ALA A 1 231 ? 128.330 132.397 129.509 1.00 63.39  ?  147 ALA A CA  1 
ATOM   1007 C C   . ALA A 1 231 ? 127.601 132.974 128.304 1.00 61.98  ?  147 ALA A C   1 
ATOM   1008 O O   . ALA A 1 231 ? 126.418 132.676 128.108 1.00 64.90  ?  147 ALA A O   1 
ATOM   1009 C CB  . ALA A 1 231 ? 127.960 133.183 130.767 1.00 60.92  ?  147 ALA A CB  1 
ATOM   1010 N N   . ARG A 1 232 ? 128.276 133.792 127.496 1.00 60.32  ?  148 ARG A N   1 
ATOM   1011 C CA  . ARG A 1 232 ? 127.710 134.337 126.271 1.00 62.10  ?  148 ARG A CA  1 
ATOM   1012 C C   . ARG A 1 232 ? 128.238 133.635 125.027 1.00 62.55  ?  148 ARG A C   1 
ATOM   1013 O O   . ARG A 1 232 ? 128.181 134.204 123.933 1.00 70.42  ?  148 ARG A O   1 
ATOM   1014 C CB  . ARG A 1 232 ? 127.986 135.838 126.183 1.00 59.28  ?  148 ARG A CB  1 
ATOM   1015 C CG  . ARG A 1 232 ? 126.790 136.657 125.730 1.00 60.62  ?  148 ARG A CG  1 
ATOM   1016 C CD  . ARG A 1 232 ? 126.939 138.118 126.117 1.00 65.85  ?  148 ARG A CD  1 
ATOM   1017 N NE  . ARG A 1 232 ? 127.886 138.818 125.258 1.00 65.60  ?  148 ARG A NE  1 
ATOM   1018 C CZ  . ARG A 1 232 ? 128.777 139.700 125.689 1.00 71.36  ?  148 ARG A CZ  1 
ATOM   1019 N NH1 . ARG A 1 232 ? 128.880 140.008 126.971 1.00 70.03  1  148 ARG A NH1 1 
ATOM   1020 N NH2 . ARG A 1 232 ? 129.586 140.287 124.812 1.00 67.71  ?  148 ARG A NH2 1 
ATOM   1021 N N   . TYR A 1 233 ? 128.763 132.416 125.175 1.00 55.17  ?  149 TYR A N   1 
ATOM   1022 C CA  . TYR A 1 233 ? 129.297 131.698 124.021 1.00 57.69  ?  149 TYR A CA  1 
ATOM   1023 C C   . TYR A 1 233 ? 128.204 131.372 123.013 1.00 58.17  ?  149 TYR A C   1 
ATOM   1024 O O   . TYR A 1 233 ? 128.404 131.515 121.802 1.00 62.29  ?  149 TYR A O   1 
ATOM   1025 C CB  . TYR A 1 233 ? 129.991 130.415 124.474 1.00 61.69  ?  149 TYR A CB  1 
ATOM   1026 C CG  . TYR A 1 233 ? 131.475 130.556 124.694 1.00 60.10  ?  149 TYR A CG  1 
ATOM   1027 C CD1 . TYR A 1 233 ? 132.095 131.791 124.601 1.00 59.71  ?  149 TYR A CD1 1 
ATOM   1028 C CD2 . TYR A 1 233 ? 132.256 129.452 124.994 1.00 60.22  ?  149 TYR A CD2 1 
ATOM   1029 C CE1 . TYR A 1 233 ? 133.450 131.922 124.806 1.00 60.78  ?  149 TYR A CE1 1 
ATOM   1030 C CE2 . TYR A 1 233 ? 133.612 129.574 125.197 1.00 64.88  ?  149 TYR A CE2 1 
ATOM   1031 C CZ  . TYR A 1 233 ? 134.205 130.811 125.101 1.00 63.58  ?  149 TYR A CZ  1 
ATOM   1032 O OH  . TYR A 1 233 ? 135.559 130.938 125.304 1.00 65.05  ?  149 TYR A OH  1 
ATOM   1033 N N   . GLN A 1 234 ? 127.045 130.919 123.492 1.00 53.59  ?  150 GLN A N   1 
ATOM   1034 C CA  . GLN A 1 234 ? 126.006 130.447 122.584 1.00 52.11  ?  150 GLN A CA  1 
ATOM   1035 C C   . GLN A 1 234 ? 125.435 131.585 121.749 1.00 59.57  ?  150 GLN A C   1 
ATOM   1036 O O   . GLN A 1 234 ? 125.384 131.496 120.517 1.00 67.01  ?  150 GLN A O   1 
ATOM   1037 C CB  . GLN A 1 234 ? 124.896 129.755 123.373 1.00 57.07  ?  150 GLN A CB  1 
ATOM   1038 C CG  . GLN A 1 234 ? 123.980 128.902 122.520 1.00 56.55  ?  150 GLN A CG  1 
ATOM   1039 C CD  . GLN A 1 234 ? 122.997 128.108 123.347 1.00 57.39  ?  150 GLN A CD  1 
ATOM   1040 O OE1 . GLN A 1 234 ? 122.859 128.328 124.549 1.00 56.86  ?  150 GLN A OE1 1 
ATOM   1041 N NE2 . GLN A 1 234 ? 122.306 127.174 122.707 1.00 60.40  ?  150 GLN A NE2 1 
ATOM   1042 N N   . ARG A 1 235 ? 125.021 132.674 122.403 1.00 58.78  ?  151 ARG A N   1 
ATOM   1043 C CA  . ARG A 1 235 ? 124.366 133.765 121.689 1.00 53.21  ?  151 ARG A CA  1 
ATOM   1044 C C   . ARG A 1 235 ? 125.278 134.337 120.614 1.00 51.88  ?  151 ARG A C   1 
ATOM   1045 O O   . ARG A 1 235 ? 124.866 134.513 119.461 1.00 62.04  ?  151 ARG A O   1 
ATOM   1046 C CB  . ARG A 1 235 ? 123.943 134.855 122.672 1.00 55.89  ?  151 ARG A CB  1 
ATOM   1047 C CG  . ARG A 1 235 ? 122.787 134.459 123.572 1.00 62.62  ?  151 ARG A CG  1 
ATOM   1048 C CD  . ARG A 1 235 ? 121.456 134.606 122.856 1.00 62.03  ?  151 ARG A CD  1 
ATOM   1049 N NE  . ARG A 1 235 ? 120.815 135.882 123.147 1.00 64.40  ?  151 ARG A NE  1 
ATOM   1050 C CZ  . ARG A 1 235 ? 119.840 136.044 124.031 1.00 63.34  ?  151 ARG A CZ  1 
ATOM   1051 N NH1 . ARG A 1 235 ? 119.368 135.027 124.732 1.00 58.14  1  151 ARG A NH1 1 
ATOM   1052 N NH2 . ARG A 1 235 ? 119.326 137.256 124.216 1.00 64.62  ?  151 ARG A NH2 1 
ATOM   1053 N N   . VAL A 1 236 ? 126.527 134.603 120.989 1.00 43.81  ?  152 VAL A N   1 
ATOM   1054 C CA  . VAL A 1 236 ? 127.504 135.105 119.982 1.00 44.97  ?  152 VAL A CA  1 
ATOM   1055 C C   . VAL A 1 236 ? 127.599 134.073 118.852 1.00 57.28  ?  152 VAL A C   1 
ATOM   1056 O O   . VAL A 1 236 ? 127.574 134.489 117.675 1.00 68.08  ?  152 VAL A O   1 
ATOM   1057 C CB  . VAL A 1 236 ? 128.868 135.397 120.632 1.00 49.78  ?  152 VAL A CB  1 
ATOM   1058 C CG1 . VAL A 1 236 ? 129.913 135.779 119.598 1.00 53.67  ?  152 VAL A CG1 1 
ATOM   1059 C CG2 . VAL A 1 236 ? 128.734 136.492 121.678 1.00 56.70  ?  152 VAL A CG2 1 
ATOM   1060 N N   . ALA A 1 237 ? 127.660 132.780 119.189 1.00 54.27  ?  153 ALA A N   1 
ATOM   1061 C CA  . ALA A 1 237 ? 127.678 131.776 118.132 1.00 49.33  ?  153 ALA A CA  1 
ATOM   1062 C C   . ALA A 1 237 ? 126.445 131.891 117.249 1.00 54.10  ?  153 ALA A C   1 
ATOM   1063 O O   . ALA A 1 237 ? 126.542 131.794 116.021 1.00 56.76  ?  153 ALA A O   1 
ATOM   1064 C CB  . ALA A 1 237 ? 127.768 130.377 118.737 1.00 48.10  ?  153 ALA A CB  1 
ATOM   1065 N N   . GLY A 1 238 ? 125.277 132.096 117.859 1.00 56.20  ?  154 GLY A N   1 
ATOM   1066 C CA  . GLY A 1 238 ? 124.058 132.204 117.077 1.00 47.03  ?  154 GLY A CA  1 
ATOM   1067 C C   . GLY A 1 238 ? 123.999 133.470 116.247 1.00 42.11  ?  154 GLY A C   1 
ATOM   1068 O O   . GLY A 1 238 ? 123.575 133.442 115.090 1.00 56.05  ?  154 GLY A O   1 
ATOM   1069 N N   . TYR A 1 239 ? 124.424 134.595 116.821 1.00 50.25  ?  155 TYR A N   1 
ATOM   1070 C CA  . TYR A 1 239 ? 124.301 135.873 116.128 1.00 53.25  ?  155 TYR A CA  1 
ATOM   1071 C C   . TYR A 1 239 ? 125.246 135.945 114.937 1.00 57.28  ?  155 TYR A C   1 
ATOM   1072 O O   . TYR A 1 239 ? 124.807 136.010 113.782 1.00 58.71  ?  155 TYR A O   1 
ATOM   1073 C CB  . TYR A 1 239 ? 124.584 137.026 117.093 1.00 51.30  ?  155 TYR A CB  1 
ATOM   1074 C CG  . TYR A 1 239 ? 123.605 137.156 118.234 1.00 59.48  ?  155 TYR A CG  1 
ATOM   1075 C CD1 . TYR A 1 239 ? 122.377 136.514 118.200 1.00 57.47  ?  155 TYR A CD1 1 
ATOM   1076 C CD2 . TYR A 1 239 ? 123.911 137.925 119.345 1.00 60.23  ?  155 TYR A CD2 1 
ATOM   1077 C CE1 . TYR A 1 239 ? 121.483 136.633 119.243 1.00 56.60  ?  155 TYR A CE1 1 
ATOM   1078 C CE2 . TYR A 1 239 ? 123.024 138.050 120.392 1.00 56.88  ?  155 TYR A CE2 1 
ATOM   1079 C CZ  . TYR A 1 239 ? 121.811 137.402 120.336 1.00 58.53  ?  155 TYR A CZ  1 
ATOM   1080 O OH  . TYR A 1 239 ? 120.924 137.524 121.380 1.00 66.94  ?  155 TYR A OH  1 
ATOM   1081 N N   . SER A 1 240 ? 126.555 135.895 115.204 1.00 54.93  ?  156 SER A N   1 
ATOM   1082 C CA  . SER A 1 240 ? 127.549 136.154 114.167 1.00 60.98  ?  156 SER A CA  1 
ATOM   1083 C C   . SER A 1 240 ? 127.354 135.233 112.972 1.00 62.33  ?  156 SER A C   1 
ATOM   1084 O O   . SER A 1 240 ? 127.237 135.696 111.831 1.00 68.77  ?  156 SER A O   1 
ATOM   1085 C CB  . SER A 1 240 ? 128.954 135.997 114.744 1.00 53.09  ?  156 SER A CB  1 
ATOM   1086 O OG  . SER A 1 240 ? 129.252 137.043 115.651 1.00 65.54  ?  156 SER A OG  1 
ATOM   1087 N N   . ARG A 1 241 ? 127.276 133.923 113.225 1.00 51.91  ?  157 ARG A N   1 
ATOM   1088 C CA  . ARG A 1 241 ? 127.031 132.969 112.149 1.00 50.84  ?  157 ARG A CA  1 
ATOM   1089 C C   . ARG A 1 241 ? 125.821 133.382 111.328 1.00 55.97  ?  157 ARG A C   1 
ATOM   1090 O O   . ARG A 1 241 ? 125.903 133.501 110.099 1.00 66.35  ?  157 ARG A O   1 
ATOM   1091 C CB  . ARG A 1 241 ? 126.836 131.568 112.729 1.00 51.92  ?  157 ARG A CB  1 
ATOM   1092 C CG  . ARG A 1 241 ? 126.468 130.515 111.701 1.00 47.34  ?  157 ARG A CG  1 
ATOM   1093 C CD  . ARG A 1 241 ? 127.697 129.977 110.996 1.00 52.35  ?  157 ARG A CD  1 
ATOM   1094 N NE  . ARG A 1 241 ? 127.362 128.915 110.057 1.00 60.67  ?  157 ARG A NE  1 
ATOM   1095 C CZ  . ARG A 1 241 ? 128.135 128.538 109.049 1.00 62.96  ?  157 ARG A CZ  1 
ATOM   1096 N NH1 . ARG A 1 241 ? 129.294 129.127 108.809 1.00 57.65  1  157 ARG A NH1 1 
ATOM   1097 N NH2 . ARG A 1 241 ? 127.735 127.544 108.260 1.00 64.57  ?  157 ARG A NH2 1 
ATOM   1098 N N   . ALA A 1 242 ? 124.704 133.668 112.002 1.00 51.81  ?  158 ALA A N   1 
ATOM   1099 C CA  . ALA A 1 242 ? 123.513 134.121 111.295 1.00 43.51  ?  158 ALA A CA  1 
ATOM   1100 C C   . ALA A 1 242 ? 123.842 135.313 110.414 1.00 54.48  ?  158 ALA A C   1 
ATOM   1101 O O   . ALA A 1 242 ? 123.595 135.290 109.202 1.00 66.32  ?  158 ALA A O   1 
ATOM   1102 C CB  . ALA A 1 242 ? 122.410 134.478 112.291 1.00 43.71  ?  158 ALA A CB  1 
ATOM   1103 N N   . ALA A 1 243 ? 124.472 136.335 111.000 1.00 51.11  ?  159 ALA A N   1 
ATOM   1104 C CA  . ALA A 1 243 ? 124.863 137.505 110.226 1.00 48.07  ?  159 ALA A CA  1 
ATOM   1105 C C   . ALA A 1 243 ? 125.670 137.087 109.009 1.00 50.52  ?  159 ALA A C   1 
ATOM   1106 O O   . ALA A 1 243 ? 125.349 137.466 107.876 1.00 58.62  ?  159 ALA A O   1 
ATOM   1107 C CB  . ALA A 1 243 ? 125.660 138.473 111.100 1.00 44.87  ?  159 ALA A CB  1 
ATOM   1108 N N   . VAL A 1 244 ? 126.675 136.233 109.221 1.00 45.81  ?  160 VAL A N   1 
ATOM   1109 C CA  . VAL A 1 244 ? 127.507 135.785 108.110 1.00 44.83  ?  160 VAL A CA  1 
ATOM   1110 C C   . VAL A 1 244 ? 126.636 135.162 107.032 1.00 51.01  ?  160 VAL A C   1 
ATOM   1111 O O   . VAL A 1 244 ? 126.697 135.551 105.859 1.00 62.88  ?  160 VAL A O   1 
ATOM   1112 C CB  . VAL A 1 244 ? 128.585 134.806 108.607 1.00 45.42  ?  160 VAL A CB  1 
ATOM   1113 C CG1 . VAL A 1 244 ? 129.000 133.863 107.497 1.00 49.23  ?  160 VAL A CG1 1 
ATOM   1114 C CG2 . VAL A 1 244 ? 129.783 135.570 109.124 1.00 51.37  ?  160 VAL A CG2 1 
ATOM   1115 N N   . LEU A 1 245 ? 125.752 134.243 107.429 1.00 46.22  ?  161 LEU A N   1 
ATOM   1116 C CA  . LEU A 1 245 ? 124.876 133.622 106.446 1.00 46.89  ?  161 LEU A CA  1 
ATOM   1117 C C   . LEU A 1 245 ? 124.007 134.669 105.775 1.00 49.41  ?  161 LEU A C   1 
ATOM   1118 O O   . LEU A 1 245 ? 123.892 134.693 104.543 1.00 46.82  ?  161 LEU A O   1 
ATOM   1119 C CB  . LEU A 1 245 ? 124.024 132.543 107.105 1.00 45.01  ?  161 LEU A CB  1 
ATOM   1120 C CG  . LEU A 1 245 ? 124.764 131.230 107.345 1.00 48.30  ?  161 LEU A CG  1 
ATOM   1121 C CD1 . LEU A 1 245 ? 123.990 130.362 108.312 1.00 51.95  ?  161 LEU A CD1 1 
ATOM   1122 C CD2 . LEU A 1 245 ? 124.996 130.505 106.033 1.00 56.96  ?  161 LEU A CD2 1 
ATOM   1123 N N   . LEU A 1 246 ? 123.444 135.587 106.566 1.00 51.49  ?  162 LEU A N   1 
ATOM   1124 C CA  . LEU A 1 246 ? 122.673 136.678 105.988 1.00 45.79  ?  162 LEU A CA  1 
ATOM   1125 C C   . LEU A 1 246 ? 123.506 137.412 104.953 1.00 49.27  ?  162 LEU A C   1 
ATOM   1126 O O   . LEU A 1 246 ? 123.059 137.631 103.819 1.00 62.30  ?  162 LEU A O   1 
ATOM   1127 C CB  . LEU A 1 246 ? 122.201 137.633 107.085 1.00 50.46  ?  162 LEU A CB  1 
ATOM   1128 C CG  . LEU A 1 246 ? 120.884 138.359 106.818 1.00 53.34  ?  162 LEU A CG  1 
ATOM   1129 C CD1 . LEU A 1 246 ? 119.710 137.414 106.989 1.00 53.74  ?  162 LEU A CD1 1 
ATOM   1130 C CD2 . LEU A 1 246 ? 120.745 139.557 107.738 1.00 55.73  ?  162 LEU A CD2 1 
ATOM   1131 N N   . GLY A 1 247 ? 124.756 137.726 105.304 1.00 45.89  ?  163 GLY A N   1 
ATOM   1132 C CA  . GLY A 1 247 ? 125.634 138.374 104.348 1.00 45.26  ?  163 GLY A CA  1 
ATOM   1133 C C   . GLY A 1 247 ? 125.711 137.605 103.050 1.00 52.79  ?  163 GLY A C   1 
ATOM   1134 O O   . GLY A 1 247 ? 125.444 138.150 101.974 1.00 61.77  ?  163 GLY A O   1 
ATOM   1135 N N   . VAL A 1 248 ? 125.975 136.298 103.145 1.00 49.49  ?  164 VAL A N   1 
ATOM   1136 C CA  . VAL A 1 248 ? 126.043 135.475 101.943 1.00 50.30  ?  164 VAL A CA  1 
ATOM   1137 C C   . VAL A 1 248 ? 124.755 135.622 101.152 1.00 57.28  ?  164 VAL A C   1 
ATOM   1138 O O   . VAL A 1 248 ? 124.774 135.953 99.959  1.00 60.48  ?  164 VAL A O   1 
ATOM   1139 C CB  . VAL A 1 248 ? 126.316 134.006 102.308 1.00 53.04  ?  164 VAL A CB  1 
ATOM   1140 C CG1 . VAL A 1 248 ? 126.363 133.151 101.056 1.00 51.03  ?  164 VAL A CG1 1 
ATOM   1141 C CG2 . VAL A 1 248 ? 127.613 133.887 103.085 1.00 57.73  ?  164 VAL A CG2 1 
ATOM   1142 N N   . PHE A 1 249 ? 123.616 135.471 101.837 1.00 57.71  ?  165 PHE A N   1 
ATOM   1143 C CA  . PHE A 1 249 ? 122.324 135.677 101.197 1.00 46.74  ?  165 PHE A CA  1 
ATOM   1144 C C   . PHE A 1 249 ? 122.324 136.989 100.434 1.00 48.18  ?  165 PHE A C   1 
ATOM   1145 O O   . PHE A 1 249 ? 122.214 137.007 99.200  1.00 59.14  ?  165 PHE A O   1 
ATOM   1146 C CB  . PHE A 1 249 ? 121.212 135.656 102.246 1.00 53.13  ?  165 PHE A CB  1 
ATOM   1147 C CG  . PHE A 1 249 ? 119.883 136.127 101.732 1.00 54.24  ?  165 PHE A CG  1 
ATOM   1148 C CD1 . PHE A 1 249 ? 119.172 135.372 100.818 1.00 55.71  ?  165 PHE A CD1 1 
ATOM   1149 C CD2 . PHE A 1 249 ? 119.344 137.325 102.167 1.00 58.24  ?  165 PHE A CD2 1 
ATOM   1150 C CE1 . PHE A 1 249 ? 117.948 135.802 100.348 1.00 54.15  ?  165 PHE A CE1 1 
ATOM   1151 C CE2 . PHE A 1 249 ? 118.121 137.760 101.699 1.00 57.04  ?  165 PHE A CE2 1 
ATOM   1152 C CZ  . PHE A 1 249 ? 117.423 136.997 100.788 1.00 53.47  ?  165 PHE A CZ  1 
ATOM   1153 N N   . THR A 1 250 ? 122.555 138.092 101.154 1.00 39.54  ?  166 THR A N   1 
ATOM   1154 C CA  . THR A 1 250 ? 122.559 139.400 100.514 1.00 44.79  ?  166 THR A CA  1 
ATOM   1155 C C   . THR A 1 250 ? 123.482 139.387 99.312  1.00 53.18  ?  166 THR A C   1 
ATOM   1156 O O   . THR A 1 250 ? 123.059 139.692 98.188  1.00 60.17  ?  166 THR A O   1 
ATOM   1157 C CB  . THR A 1 250 ? 122.989 140.477 101.508 1.00 49.59  ?  166 THR A CB  1 
ATOM   1158 O OG1 . THR A 1 250 ? 122.079 140.500 102.615 1.00 58.37  ?  166 THR A OG1 1 
ATOM   1159 C CG2 . THR A 1 250 ? 122.999 141.838 100.839 1.00 54.13  ?  166 THR A CG2 1 
ATOM   1160 N N   . SER A 1 251 ? 124.720 138.926 99.517  1.00 47.47  ?  167 SER A N   1 
ATOM   1161 C CA  . SER A 1 251 ? 125.684 138.864 98.429  1.00 46.86  ?  167 SER A CA  1 
ATOM   1162 C C   . SER A 1 251 ? 125.056 138.208 97.214  1.00 53.50  ?  167 SER A C   1 
ATOM   1163 O O   . SER A 1 251 ? 124.867 138.851 96.172  1.00 60.32  ?  167 SER A O   1 
ATOM   1164 C CB  . SER A 1 251 ? 126.932 138.102 98.876  1.00 50.23  ?  167 SER A CB  1 
ATOM   1165 O OG  . SER A 1 251 ? 127.585 137.507 97.770  1.00 51.05  ?  167 SER A OG  1 
ATOM   1166 N N   . SER A 1 252 ? 124.619 136.956 97.376  1.00 52.26  ?  168 SER A N   1 
ATOM   1167 C CA  . SER A 1 252 ? 124.049 136.231 96.250  1.00 45.96  ?  168 SER A CA  1 
ATOM   1168 C C   . SER A 1 252 ? 122.932 137.043 95.624  1.00 52.28  ?  168 SER A C   1 
ATOM   1169 O O   . SER A 1 252 ? 122.986 137.383 94.434  1.00 60.11  ?  168 SER A O   1 
ATOM   1170 C CB  . SER A 1 252 ? 123.539 134.864 96.706  1.00 51.25  ?  168 SER A CB  1 
ATOM   1171 O OG  . SER A 1 252 ? 124.479 134.225 97.550  1.00 59.07  ?  168 SER A OG  1 
ATOM   1172 N N   . VAL A 1 253 ? 121.975 137.471 96.451  1.00 53.57  ?  169 VAL A N   1 
ATOM   1173 C CA  . VAL A 1 253 ? 120.825 138.194 95.925  1.00 47.66  ?  169 VAL A CA  1 
ATOM   1174 C C   . VAL A 1 253 ? 121.300 139.409 95.153  1.00 55.86  ?  169 VAL A C   1 
ATOM   1175 O O   . VAL A 1 253 ? 120.954 139.592 93.977  1.00 62.39  ?  169 VAL A O   1 
ATOM   1176 C CB  . VAL A 1 253 ? 119.863 138.582 97.062  1.00 47.07  ?  169 VAL A CB  1 
ATOM   1177 C CG1 . VAL A 1 253 ? 119.065 139.816 96.685  1.00 50.59  ?  169 VAL A CG1 1 
ATOM   1178 C CG2 . VAL A 1 253 ? 118.937 137.425 97.375  1.00 52.57  ?  169 VAL A CG2 1 
ATOM   1179 N N   . LEU A 1 254 ? 122.196 140.190 95.765  1.00 52.68  ?  170 LEU A N   1 
ATOM   1180 C CA  . LEU A 1 254 ? 122.672 141.400 95.113  1.00 54.02  ?  170 LEU A CA  1 
ATOM   1181 C C   . LEU A 1 254 ? 123.191 141.067 93.729  1.00 54.38  ?  170 LEU A C   1 
ATOM   1182 O O   . LEU A 1 254 ? 122.706 141.605 92.725  1.00 58.90  ?  170 LEU A O   1 
ATOM   1183 C CB  . LEU A 1 254 ? 123.755 142.066 95.962  1.00 49.88  ?  170 LEU A CB  1 
ATOM   1184 C CG  . LEU A 1 254 ? 124.034 143.535 95.650  1.00 50.00  ?  170 LEU A CG  1 
ATOM   1185 C CD1 . LEU A 1 254 ? 122.824 144.383 95.995  1.00 52.61  ?  170 LEU A CD1 1 
ATOM   1186 C CD2 . LEU A 1 254 ? 125.255 144.013 96.410  1.00 53.27  ?  170 LEU A CD2 1 
ATOM   1187 N N   . GLY A 1 255 ? 124.090 140.083 93.652  1.00 52.14  ?  171 GLY A N   1 
ATOM   1188 C CA  . GLY A 1 255 ? 124.657 139.735 92.364  1.00 53.13  ?  171 GLY A CA  1 
ATOM   1189 C C   . GLY A 1 255 ? 123.578 139.431 91.352  1.00 55.64  ?  171 GLY A C   1 
ATOM   1190 O O   . GLY A 1 255 ? 123.508 140.060 90.291  1.00 62.54  ?  171 GLY A O   1 
ATOM   1191 N N   . GLN A 1 256 ? 122.649 138.544 91.718  1.00 54.46  ?  172 GLN A N   1 
ATOM   1192 C CA  . GLN A 1 256 ? 121.622 138.158 90.763  1.00 58.47  ?  172 GLN A CA  1 
ATOM   1193 C C   . GLN A 1 256 ? 120.795 139.363 90.358  1.00 63.66  ?  172 GLN A C   1 
ATOM   1194 O O   . GLN A 1 256 ? 120.543 139.578 89.166  1.00 66.83  ?  172 GLN A O   1 
ATOM   1195 C CB  . GLN A 1 256 ? 120.734 137.061 91.339  1.00 56.91  ?  172 GLN A CB  1 
ATOM   1196 C CG  . GLN A 1 256 ? 119.937 136.325 90.278  1.00 61.29  ?  172 GLN A CG  1 
ATOM   1197 C CD  . GLN A 1 256 ? 120.821 135.647 89.252  1.00 67.49  ?  172 GLN A CD  1 
ATOM   1198 O OE1 . GLN A 1 256 ? 120.510 135.631 88.061  1.00 66.95  ?  172 GLN A OE1 1 
ATOM   1199 N NE2 . GLN A 1 256 ? 121.926 135.071 89.710  1.00 65.56  ?  172 GLN A NE2 1 
ATOM   1200 N N   . LEU A 1 257 ? 120.424 140.201 91.327  1.00 58.75  ?  173 LEU A N   1 
ATOM   1201 C CA  . LEU A 1 257 ? 119.643 141.378 90.984  1.00 50.50  ?  173 LEU A CA  1 
ATOM   1202 C C   . LEU A 1 257 ? 120.420 142.247 90.010  1.00 58.67  ?  173 LEU A C   1 
ATOM   1203 O O   . LEU A 1 257 ? 119.901 142.640 88.958  1.00 66.67  ?  173 LEU A O   1 
ATOM   1204 C CB  . LEU A 1 257 ? 119.268 142.156 92.245  1.00 56.77  ?  173 LEU A CB  1 
ATOM   1205 C CG  . LEU A 1 257 ? 117.946 141.793 92.932  1.00 62.16  ?  173 LEU A CG  1 
ATOM   1206 C CD1 . LEU A 1 257 ? 116.762 142.211 92.083  1.00 60.51  ?  173 LEU A CD1 1 
ATOM   1207 C CD2 . LEU A 1 257 ? 117.857 140.311 93.261  1.00 63.34  ?  173 LEU A CD2 1 
ATOM   1208 N N   . LEU A 1 258 ? 121.707 142.461 90.292  1.00 58.73  ?  174 LEU A N   1 
ATOM   1209 C CA  . LEU A 1 258 ? 122.496 143.341 89.445  1.00 55.52  ?  174 LEU A CA  1 
ATOM   1210 C C   . LEU A 1 258 ? 122.694 142.764 88.053  1.00 64.60  ?  174 LEU A C   1 
ATOM   1211 O O   . LEU A 1 258 ? 123.089 143.501 87.145  1.00 72.19  ?  174 LEU A O   1 
ATOM   1212 C CB  . LEU A 1 258 ? 123.844 143.635 90.102  1.00 52.68  ?  174 LEU A CB  1 
ATOM   1213 C CG  . LEU A 1 258 ? 123.751 144.551 91.324  1.00 51.44  ?  174 LEU A CG  1 
ATOM   1214 C CD1 . LEU A 1 258 ? 125.127 144.963 91.811  1.00 57.71  ?  174 LEU A CD1 1 
ATOM   1215 C CD2 . LEU A 1 258 ? 122.906 145.771 91.009  1.00 58.11  ?  174 LEU A CD2 1 
ATOM   1216 N N   . VAL A 1 259 ? 122.419 141.475 87.858  1.00 60.08  ?  175 VAL A N   1 
ATOM   1217 C CA  . VAL A 1 259 ? 122.500 140.877 86.530  1.00 59.59  ?  175 VAL A CA  1 
ATOM   1218 C C   . VAL A 1 259 ? 121.142 140.484 85.976  1.00 64.27  ?  175 VAL A C   1 
ATOM   1219 O O   . VAL A 1 259 ? 121.082 139.968 84.848  1.00 70.41  ?  175 VAL A O   1 
ATOM   1220 C CB  . VAL A 1 259 ? 123.452 139.662 86.510  1.00 60.62  ?  175 VAL A CB  1 
ATOM   1221 C CG1 . VAL A 1 259 ? 124.761 140.002 87.198  1.00 55.92  ?  175 VAL A CG1 1 
ATOM   1222 C CG2 . VAL A 1 259 ? 122.797 138.459 87.158  1.00 66.10  ?  175 VAL A CG2 1 
ATOM   1223 N N   . THR A 1 260 ? 120.052 140.710 86.712  1.00 62.66  ?  176 THR A N   1 
ATOM   1224 C CA  . THR A 1 260 ? 118.725 140.367 86.216  1.00 64.93  ?  176 THR A CA  1 
ATOM   1225 C C   . THR A 1 260 ? 117.851 141.597 86.007  1.00 62.55  ?  176 THR A C   1 
ATOM   1226 O O   . THR A 1 260 ? 117.339 141.808 84.905  1.00 72.46  ?  176 THR A O   1 
ATOM   1227 C CB  . THR A 1 260 ? 118.036 139.374 87.162  1.00 71.66  ?  176 THR A CB  1 
ATOM   1228 O OG1 . THR A 1 260 ? 118.264 139.765 88.520  1.00 82.63  ?  176 THR A OG1 1 
ATOM   1229 C CG2 . THR A 1 260 ? 118.578 137.972 86.943  1.00 63.28  ?  176 THR A CG2 1 
ATOM   1230 N N   . VAL A 1 261 ? 117.662 142.422 87.037  1.00 59.16  ?  177 VAL A N   1 
ATOM   1231 C CA  . VAL A 1 261 ? 116.896 143.648 86.846  1.00 62.30  ?  177 VAL A CA  1 
ATOM   1232 C C   . VAL A 1 261 ? 117.787 144.751 86.291  1.00 68.21  ?  177 VAL A C   1 
ATOM   1233 O O   . VAL A 1 261 ? 117.368 145.526 85.424  1.00 68.54  ?  177 VAL A O   1 
ATOM   1234 C CB  . VAL A 1 261 ? 116.203 144.065 88.157  1.00 63.40  ?  177 VAL A CB  1 
ATOM   1235 C CG1 . VAL A 1 261 ? 117.217 144.306 89.258  1.00 63.29  ?  177 VAL A CG1 1 
ATOM   1236 C CG2 . VAL A 1 261 ? 115.348 145.303 87.936  1.00 70.69  ?  177 VAL A CG2 1 
ATOM   1237 N N   . GLY A 1 262 ? 119.028 144.837 86.771  1.00 72.48  ?  178 GLY A N   1 
ATOM   1238 C CA  . GLY A 1 262 ? 119.989 145.748 86.194  1.00 70.39  ?  178 GLY A CA  1 
ATOM   1239 C C   . GLY A 1 262 ? 120.614 145.176 84.941  1.00 76.10  ?  178 GLY A C   1 
ATOM   1240 O O   . GLY A 1 262 ? 120.443 144.006 84.600  1.00 76.94  ?  178 GLY A O   1 
ATOM   1241 N N   . ARG A 1 263 ? 121.355 146.029 84.237  1.00 88.13  ?  179 ARG A N   1 
ATOM   1242 C CA  . ARG A 1 263 ? 122.019 145.629 83.003  1.00 86.96  ?  179 ARG A CA  1 
ATOM   1243 C C   . ARG A 1 263 ? 123.534 145.765 83.103  1.00 87.29  ?  179 ARG A C   1 
ATOM   1244 O O   . ARG A 1 263 ? 124.210 145.885 82.077  1.00 86.10  ?  179 ARG A O   1 
ATOM   1245 C CB  . ARG A 1 263 ? 121.489 146.441 81.820  1.00 85.98  ?  179 ARG A CB  1 
ATOM   1246 C CG  . ARG A 1 263 ? 120.123 145.992 81.322  1.00 86.76  ?  179 ARG A CG  1 
ATOM   1247 C CD  . ARG A 1 263 ? 120.224 144.740 80.466  1.00 88.11  ?  179 ARG A CD  1 
ATOM   1248 N NE  . ARG A 1 263 ? 120.060 143.528 81.259  1.00 87.90  ?  179 ARG A NE  1 
ATOM   1249 C CZ  . ARG A 1 263 ? 120.535 142.337 80.919  1.00 88.42  ?  179 ARG A CZ  1 
ATOM   1250 N NH1 . ARG A 1 263 ? 121.217 142.160 79.799  1.00 87.40  1  179 ARG A NH1 1 
ATOM   1251 N NH2 . ARG A 1 263 ? 120.322 141.300 81.723  1.00 86.14  ?  179 ARG A NH2 1 
ATOM   1252 N N   . VAL A 1 264 ? 124.081 145.749 84.319  1.00 76.69  ?  180 VAL A N   1 
ATOM   1253 C CA  . VAL A 1 264 ? 125.520 145.897 84.480  1.00 77.31  ?  180 VAL A CA  1 
ATOM   1254 C C   . VAL A 1 264 ? 126.222 144.644 83.971  1.00 79.74  ?  180 VAL A C   1 
ATOM   1255 O O   . VAL A 1 264 ? 125.681 143.531 84.019  1.00 76.47  ?  180 VAL A O   1 
ATOM   1256 C CB  . VAL A 1 264 ? 125.887 146.189 85.948  1.00 74.11  ?  180 VAL A CB  1 
ATOM   1257 C CG1 . VAL A 1 264 ? 124.931 147.210 86.542  1.00 72.87  ?  180 VAL A CG1 1 
ATOM   1258 C CG2 . VAL A 1 264 ? 125.902 144.915 86.774  1.00 73.29  ?  180 VAL A CG2 1 
ATOM   1259 N N   . SER A 1 265 ? 127.431 144.831 83.450  1.00 80.02  ?  181 SER A N   1 
ATOM   1260 C CA  . SER A 1 265 ? 128.229 143.716 82.970  1.00 76.51  ?  181 SER A CA  1 
ATOM   1261 C C   . SER A 1 265 ? 128.978 143.076 84.135  1.00 76.93  ?  181 SER A C   1 
ATOM   1262 O O   . SER A 1 265 ? 128.900 143.523 85.282  1.00 77.39  ?  181 SER A O   1 
ATOM   1263 C CB  . SER A 1 265 ? 129.191 144.184 81.881  1.00 78.36  ?  181 SER A CB  1 
ATOM   1264 O OG  . SER A 1 265 ? 129.809 145.406 82.241  1.00 77.40  ?  181 SER A OG  1 
ATOM   1265 N N   . PHE A 1 266 ? 129.716 142.005 83.838  1.00 68.13  ?  182 PHE A N   1 
ATOM   1266 C CA  . PHE A 1 266 ? 130.489 141.341 84.880  1.00 67.42  ?  182 PHE A CA  1 
ATOM   1267 C C   . PHE A 1 266 ? 131.615 142.226 85.396  1.00 70.13  ?  182 PHE A C   1 
ATOM   1268 O O   . PHE A 1 266 ? 132.018 142.095 86.556  1.00 71.05  ?  182 PHE A O   1 
ATOM   1269 C CB  . PHE A 1 266 ? 131.050 140.020 84.359  1.00 68.68  ?  182 PHE A CB  1 
ATOM   1270 C CG  . PHE A 1 266 ? 129.999 138.998 84.045  1.00 64.70  ?  182 PHE A CG  1 
ATOM   1271 C CD1 . PHE A 1 266 ? 129.137 138.549 85.028  1.00 62.07  ?  182 PHE A CD1 1 
ATOM   1272 C CD2 . PHE A 1 266 ? 129.873 138.486 82.766  1.00 66.31  ?  182 PHE A CD2 1 
ATOM   1273 C CE1 . PHE A 1 266 ? 128.170 137.609 84.743  1.00 66.24  ?  182 PHE A CE1 1 
ATOM   1274 C CE2 . PHE A 1 266 ? 128.909 137.546 82.475  1.00 66.54  ?  182 PHE A CE2 1 
ATOM   1275 C CZ  . PHE A 1 266 ? 128.056 137.107 83.465  1.00 70.23  ?  182 PHE A CZ  1 
ATOM   1276 N N   . SER A 1 267 ? 132.138 143.123 84.558  1.00 69.25  ?  183 SER A N   1 
ATOM   1277 C CA  . SER A 1 267 ? 133.199 144.020 85.004  1.00 72.35  ?  183 SER A CA  1 
ATOM   1278 C C   . SER A 1 267 ? 132.698 144.974 86.082  1.00 75.20  ?  183 SER A C   1 
ATOM   1279 O O   . SER A 1 267 ? 133.367 145.181 87.101  1.00 74.18  ?  183 SER A O   1 
ATOM   1280 C CB  . SER A 1 267 ? 133.765 144.794 83.815  1.00 73.36  ?  183 SER A CB  1 
ATOM   1281 O OG  . SER A 1 267 ? 134.650 143.988 83.058  1.00 75.23  ?  183 SER A OG  1 
ATOM   1282 N N   . THR A 1 268 ? 131.519 145.565 85.875  1.00 73.24  ?  184 THR A N   1 
ATOM   1283 C CA  . THR A 1 268 ? 130.950 146.446 86.890  1.00 68.30  ?  184 THR A CA  1 
ATOM   1284 C C   . THR A 1 268 ? 130.655 145.682 88.173  1.00 63.76  ?  184 THR A C   1 
ATOM   1285 O O   . THR A 1 268 ? 130.886 146.189 89.277  1.00 68.54  ?  184 THR A O   1 
ATOM   1286 C CB  . THR A 1 268 ? 129.679 147.110 86.361  1.00 67.04  ?  184 THR A CB  1 
ATOM   1287 O OG1 . THR A 1 268 ? 129.946 147.713 85.089  1.00 71.24  ?  184 THR A OG1 1 
ATOM   1288 C CG2 . THR A 1 268 ? 129.194 148.176 87.327  1.00 65.14  ?  184 THR A CG2 1 
ATOM   1289 N N   . LEU A 1 269 ? 130.145 144.456 88.045  1.00 58.39  ?  185 LEU A N   1 
ATOM   1290 C CA  . LEU A 1 269 ? 129.872 143.637 89.220  1.00 62.19  ?  185 LEU A CA  1 
ATOM   1291 C C   . LEU A 1 269 ? 131.151 143.333 89.988  1.00 61.78  ?  185 LEU A C   1 
ATOM   1292 O O   . LEU A 1 269 ? 131.167 143.371 91.223  1.00 68.46  ?  185 LEU A O   1 
ATOM   1293 C CB  . LEU A 1 269 ? 129.176 142.346 88.799  1.00 63.81  ?  185 LEU A CB  1 
ATOM   1294 C CG  . LEU A 1 269 ? 128.437 141.590 89.896  1.00 60.96  ?  185 LEU A CG  1 
ATOM   1295 C CD1 . LEU A 1 269 ? 127.274 142.411 90.398  1.00 63.14  ?  185 LEU A CD1 1 
ATOM   1296 C CD2 . LEU A 1 269 ? 127.955 140.263 89.358  1.00 66.01  ?  185 LEU A CD2 1 
ATOM   1297 N N   . ASN A 1 270 ? 132.237 143.035 89.275  1.00 63.01  ?  186 ASN A N   1 
ATOM   1298 C CA  . ASN A 1 270 ? 133.502 142.767 89.946  1.00 62.66  ?  186 ASN A CA  1 
ATOM   1299 C C   . ASN A 1 270 ? 134.080 144.022 90.585  1.00 68.26  ?  186 ASN A C   1 
ATOM   1300 O O   . ASN A 1 270 ? 134.705 143.938 91.644  1.00 73.39  ?  186 ASN A O   1 
ATOM   1301 C CB  . ASN A 1 270 ? 134.499 142.156 88.968  1.00 63.12  ?  186 ASN A CB  1 
ATOM   1302 C CG  . ASN A 1 270 ? 134.193 140.707 88.664  1.00 69.34  ?  186 ASN A CG  1 
ATOM   1303 O OD1 . ASN A 1 270 ? 133.127 140.199 89.012  1.00 67.10  ?  186 ASN A OD1 1 
ATOM   1304 N ND2 . ASN A 1 270 ? 135.131 140.029 88.024  1.00 72.21  ?  186 ASN A ND2 1 
ATOM   1305 N N   . TYR A 1 271 ? 133.892 145.189 89.965  1.00 65.81  ?  187 TYR A N   1 
ATOM   1306 C CA  . TYR A 1 271 ? 134.329 146.428 90.602  1.00 53.83  ?  187 TYR A CA  1 
ATOM   1307 C C   . TYR A 1 271 ? 133.545 146.696 91.882  1.00 50.37  ?  187 TYR A C   1 
ATOM   1308 O O   . TYR A 1 271 ? 134.115 147.134 92.888  1.00 60.08  ?  187 TYR A O   1 
ATOM   1309 C CB  . TYR A 1 271 ? 134.199 147.600 89.632  1.00 53.56  ?  187 TYR A CB  1 
ATOM   1310 C CG  . TYR A 1 271 ? 135.297 147.651 88.597  1.00 56.78  ?  187 TYR A CG  1 
ATOM   1311 C CD1 . TYR A 1 271 ? 136.631 147.646 88.975  1.00 57.47  ?  187 TYR A CD1 1 
ATOM   1312 C CD2 . TYR A 1 271 ? 135.001 147.709 87.243  1.00 61.87  ?  187 TYR A CD2 1 
ATOM   1313 C CE1 . TYR A 1 271 ? 137.640 147.691 88.034  1.00 61.60  ?  187 TYR A CE1 1 
ATOM   1314 C CE2 . TYR A 1 271 ? 136.003 147.753 86.294  1.00 63.92  ?  187 TYR A CE2 1 
ATOM   1315 C CZ  . TYR A 1 271 ? 137.320 147.745 86.695  1.00 66.37  ?  187 TYR A CZ  1 
ATOM   1316 O OH  . TYR A 1 271 ? 138.322 147.791 85.754  1.00 68.84  ?  187 TYR A OH  1 
ATOM   1317 N N   . ILE A 1 272 ? 132.236 146.436 91.863  1.00 50.33  ?  188 ILE A N   1 
ATOM   1318 C CA  . ILE A 1 272 ? 131.432 146.578 93.076  1.00 52.03  ?  188 ILE A CA  1 
ATOM   1319 C C   . ILE A 1 272 ? 131.906 145.602 94.146  1.00 57.08  ?  188 ILE A C   1 
ATOM   1320 O O   . ILE A 1 272 ? 132.001 145.950 95.331  1.00 59.63  ?  188 ILE A O   1 
ATOM   1321 C CB  . ILE A 1 272 ? 129.939 146.386 92.756  1.00 45.63  ?  188 ILE A CB  1 
ATOM   1322 C CG1 . ILE A 1 272 ? 129.468 147.446 91.763  1.00 52.44  ?  188 ILE A CG1 1 
ATOM   1323 C CG2 . ILE A 1 272 ? 129.111 146.449 94.023  1.00 49.23  ?  188 ILE A CG2 1 
ATOM   1324 C CD1 . ILE A 1 272 ? 128.088 147.189 91.210  1.00 53.10  ?  188 ILE A CD1 1 
ATOM   1325 N N   . SER A 1 273 ? 132.201 144.364 93.747  1.00 50.08  ?  189 SER A N   1 
ATOM   1326 C CA  . SER A 1 273 ? 132.700 143.376 94.697  1.00 42.02  ?  189 SER A CA  1 
ATOM   1327 C C   . SER A 1 273 ? 134.038 143.804 95.284  1.00 54.12  ?  189 SER A C   1 
ATOM   1328 O O   . SER A 1 273 ? 134.288 143.614 96.477  1.00 66.41  ?  189 SER A O   1 
ATOM   1329 C CB  . SER A 1 273 ? 132.828 142.015 94.019  1.00 45.85  ?  189 SER A CB  1 
ATOM   1330 O OG  . SER A 1 273 ? 131.636 141.674 93.336  1.00 63.10  ?  189 SER A OG  1 
ATOM   1331 N N   . LEU A 1 274 ? 134.913 144.377 94.458  1.00 48.77  ?  190 LEU A N   1 
ATOM   1332 C CA  . LEU A 1 274 ? 136.199 144.860 94.948  1.00 46.45  ?  190 LEU A CA  1 
ATOM   1333 C C   . LEU A 1 274 ? 136.021 146.014 95.926  1.00 51.15  ?  190 LEU A C   1 
ATOM   1334 O O   . LEU A 1 274 ? 136.727 146.091 96.937  1.00 56.34  ?  190 LEU A O   1 
ATOM   1335 C CB  . LEU A 1 274 ? 137.080 145.275 93.772  1.00 42.38  ?  190 LEU A CB  1 
ATOM   1336 C CG  . LEU A 1 274 ? 138.347 146.065 94.094  1.00 47.73  ?  190 LEU A CG  1 
ATOM   1337 C CD1 . LEU A 1 274 ? 139.444 145.135 94.573  1.00 60.03  ?  190 LEU A CD1 1 
ATOM   1338 C CD2 . LEU A 1 274 ? 138.802 146.848 92.877  1.00 47.04  ?  190 LEU A CD2 1 
ATOM   1339 N N   . ALA A 1 275 ? 135.086 146.924 95.643  1.00 48.35  ?  191 ALA A N   1 
ATOM   1340 C CA  . ALA A 1 275 ? 134.816 148.013 96.577  1.00 40.10  ?  191 ALA A CA  1 
ATOM   1341 C C   . ALA A 1 275 ? 134.292 147.483 97.907  1.00 44.68  ?  191 ALA A C   1 
ATOM   1342 O O   . ALA A 1 275 ? 134.714 147.937 98.980  1.00 60.06  ?  191 ALA A O   1 
ATOM   1343 C CB  . ALA A 1 275 ? 133.825 148.999 95.963  1.00 41.52  ?  191 ALA A CB  1 
ATOM   1344 N N   . PHE A 1 276 ? 133.375 146.515 97.858  1.00 44.19  ?  192 PHE A N   1 
ATOM   1345 C CA  . PHE A 1 276 ? 132.854 145.934 99.092  1.00 47.75  ?  192 PHE A CA  1 
ATOM   1346 C C   . PHE A 1 276 ? 133.942 145.191 99.857  1.00 51.77  ?  192 PHE A C   1 
ATOM   1347 O O   . PHE A 1 276 ? 133.973 145.223 101.091 1.00 60.56  ?  192 PHE A O   1 
ATOM   1348 C CB  . PHE A 1 276 ? 131.682 145.007 98.782  1.00 44.14  ?  192 PHE A CB  1 
ATOM   1349 C CG  . PHE A 1 276 ? 130.363 145.713 98.706  1.00 51.96  ?  192 PHE A CG  1 
ATOM   1350 C CD1 . PHE A 1 276 ? 129.974 146.585 99.705  1.00 47.83  ?  192 PHE A CD1 1 
ATOM   1351 C CD2 . PHE A 1 276 ? 129.516 145.511 97.632  1.00 57.91  ?  192 PHE A CD2 1 
ATOM   1352 C CE1 . PHE A 1 276 ? 128.764 147.238 99.638  1.00 51.32  ?  192 PHE A CE1 1 
ATOM   1353 C CE2 . PHE A 1 276 ? 128.303 146.162 97.559  1.00 51.17  ?  192 PHE A CE2 1 
ATOM   1354 C CZ  . PHE A 1 276 ? 127.926 147.026 98.563  1.00 51.78  ?  192 PHE A CZ  1 
ATOM   1355 N N   . LEU A 1 277 ? 134.845 144.518 99.142  1.00 47.74  ?  193 LEU A N   1 
ATOM   1356 C CA  . LEU A 1 277 ? 135.950 143.830 99.799  1.00 54.43  ?  193 LEU A CA  1 
ATOM   1357 C C   . LEU A 1 277 ? 136.911 144.817 100.448 1.00 55.19  ?  193 LEU A C   1 
ATOM   1358 O O   . LEU A 1 277 ? 137.432 144.558 101.537 1.00 59.99  ?  193 LEU A O   1 
ATOM   1359 C CB  . LEU A 1 277 ? 136.681 142.947 98.795  1.00 55.73  ?  193 LEU A CB  1 
ATOM   1360 C CG  . LEU A 1 277 ? 135.924 141.674 98.432  1.00 56.90  ?  193 LEU A CG  1 
ATOM   1361 C CD1 . LEU A 1 277 ? 136.692 140.880 97.399  1.00 51.30  ?  193 LEU A CD1 1 
ATOM   1362 C CD2 . LEU A 1 277 ? 135.674 140.847 99.680  1.00 59.82  ?  193 LEU A CD2 1 
ATOM   1363 N N   . THR A 1 278 ? 137.167 145.948 99.790  1.00 49.35  ?  194 THR A N   1 
ATOM   1364 C CA  . THR A 1 278 ? 137.996 146.982 100.400 1.00 48.90  ?  194 THR A CA  1 
ATOM   1365 C C   . THR A 1 278 ? 137.343 147.530 101.662 1.00 53.51  ?  194 THR A C   1 
ATOM   1366 O O   . THR A 1 278 ? 138.017 147.752 102.677 1.00 60.46  ?  194 THR A O   1 
ATOM   1367 C CB  . THR A 1 278 ? 138.257 148.103 99.395  1.00 48.76  ?  194 THR A CB  1 
ATOM   1368 O OG1 . THR A 1 278 ? 139.079 147.609 98.332  1.00 57.05  ?  194 THR A OG1 1 
ATOM   1369 C CG2 . THR A 1 278 ? 138.958 149.272 100.065 1.00 51.01  ?  194 THR A CG2 1 
ATOM   1370 N N   . PHE A 1 279 ? 136.026 147.744 101.624 1.00 48.03  ?  195 PHE A N   1 
ATOM   1371 C CA  . PHE A 1 279 ? 135.328 148.195 102.824 1.00 43.84  ?  195 PHE A CA  1 
ATOM   1372 C C   . PHE A 1 279 ? 135.404 147.154 103.933 1.00 49.15  ?  195 PHE A C   1 
ATOM   1373 O O   . PHE A 1 279 ? 135.569 147.499 105.108 1.00 61.99  ?  195 PHE A O   1 
ATOM   1374 C CB  . PHE A 1 279 ? 133.873 148.525 102.503 1.00 47.46  ?  195 PHE A CB  1 
ATOM   1375 C CG  . PHE A 1 279 ? 133.137 149.159 103.646 1.00 52.48  ?  195 PHE A CG  1 
ATOM   1376 C CD1 . PHE A 1 279 ? 133.591 150.339 104.206 1.00 56.98  ?  195 PHE A CD1 1 
ATOM   1377 C CD2 . PHE A 1 279 ? 132.000 148.570 104.167 1.00 50.96  ?  195 PHE A CD2 1 
ATOM   1378 C CE1 . PHE A 1 279 ? 132.920 150.924 105.260 1.00 59.65  ?  195 PHE A CE1 1 
ATOM   1379 C CE2 . PHE A 1 279 ? 131.325 149.150 105.221 1.00 57.79  ?  195 PHE A CE2 1 
ATOM   1380 C CZ  . PHE A 1 279 ? 131.786 150.329 105.768 1.00 59.75  ?  195 PHE A CZ  1 
ATOM   1381 N N   . SER A 1 280 ? 135.283 145.873 103.581 1.00 38.40  ?  196 SER A N   1 
ATOM   1382 C CA  . SER A 1 280 ? 135.397 144.815 104.581 1.00 44.32  ?  196 SER A CA  1 
ATOM   1383 C C   . SER A 1 280 ? 136.795 144.770 105.186 1.00 46.47  ?  196 SER A C   1 
ATOM   1384 O O   . SER A 1 280 ? 136.952 144.518 106.385 1.00 48.70  ?  196 SER A O   1 
ATOM   1385 C CB  . SER A 1 280 ? 135.042 143.467 103.961 1.00 51.81  ?  196 SER A CB  1 
ATOM   1386 O OG  . SER A 1 280 ? 135.715 142.416 104.629 1.00 56.33  ?  196 SER A OG  1 
ATOM   1387 N N   . VAL A 1 281 ? 137.824 144.993 104.368 1.00 41.09  ?  197 VAL A N   1 
ATOM   1388 C CA  . VAL A 1 281 ? 139.189 145.039 104.883 1.00 37.61  ?  197 VAL A CA  1 
ATOM   1389 C C   . VAL A 1 281 ? 139.362 146.214 105.836 1.00 44.76  ?  197 VAL A C   1 
ATOM   1390 O O   . VAL A 1 281 ? 139.996 146.089 106.891 1.00 50.39  ?  197 VAL A O   1 
ATOM   1391 C CB  . VAL A 1 281 ? 140.197 145.101 103.723 1.00 42.72  ?  197 VAL A CB  1 
ATOM   1392 C CG1 . VAL A 1 281 ? 141.588 145.393 104.246 1.00 44.68  ?  197 VAL A CG1 1 
ATOM   1393 C CG2 . VAL A 1 281 ? 140.186 143.801 102.957 1.00 45.97  ?  197 VAL A CG2 1 
ATOM   1394 N N   . VAL A 1 282 ? 138.811 147.376 105.479 1.00 47.86  ?  198 VAL A N   1 
ATOM   1395 C CA  . VAL A 1 282 ? 138.874 148.528 106.375 1.00 43.75  ?  198 VAL A CA  1 
ATOM   1396 C C   . VAL A 1 282 ? 138.155 148.223 107.683 1.00 43.16  ?  198 VAL A C   1 
ATOM   1397 O O   . VAL A 1 282 ? 138.605 148.619 108.765 1.00 46.22  ?  198 VAL A O   1 
ATOM   1398 C CB  . VAL A 1 282 ? 138.300 149.778 105.684 1.00 46.47  ?  198 VAL A CB  1 
ATOM   1399 C CG1 . VAL A 1 282 ? 138.176 150.924 106.671 1.00 43.25  ?  198 VAL A CG1 1 
ATOM   1400 C CG2 . VAL A 1 282 ? 139.183 150.181 104.519 1.00 47.18  ?  198 VAL A CG2 1 
ATOM   1401 N N   . LEU A 1 283 ? 137.029 147.510 107.607 1.00 46.44  ?  199 LEU A N   1 
ATOM   1402 C CA  . LEU A 1 283 ? 136.323 147.107 108.819 1.00 43.56  ?  199 LEU A CA  1 
ATOM   1403 C C   . LEU A 1 283 ? 137.173 146.174 109.673 1.00 49.75  ?  199 LEU A C   1 
ATOM   1404 O O   . LEU A 1 283 ? 137.218 146.312 110.901 1.00 52.85  ?  199 LEU A O   1 
ATOM   1405 C CB  . LEU A 1 283 ? 134.999 146.433 108.462 1.00 39.45  ?  199 LEU A CB  1 
ATOM   1406 C CG  . LEU A 1 283 ? 133.870 147.336 107.976 1.00 39.71  ?  199 LEU A CG  1 
ATOM   1407 C CD1 . LEU A 1 283 ? 132.620 146.516 107.732 1.00 46.07  ?  199 LEU A CD1 1 
ATOM   1408 C CD2 . LEU A 1 283 ? 133.603 148.443 108.977 1.00 45.47  ?  199 LEU A CD2 1 
ATOM   1409 N N   . ALA A 1 284 ? 137.846 145.212 109.042 1.00 48.04  ?  200 ALA A N   1 
ATOM   1410 C CA  . ALA A 1 284 ? 138.676 144.272 109.788 1.00 39.98  ?  200 ALA A CA  1 
ATOM   1411 C C   . ALA A 1 284 ? 139.903 144.948 110.380 1.00 46.96  ?  200 ALA A C   1 
ATOM   1412 O O   . ALA A 1 284 ? 140.462 144.457 111.368 1.00 52.82  ?  200 ALA A O   1 
ATOM   1413 C CB  . ALA A 1 284 ? 139.100 143.113 108.889 1.00 39.60  ?  200 ALA A CB  1 
ATOM   1414 N N   . LEU A 1 285 ? 140.344 146.059 109.786 1.00 46.27  ?  201 LEU A N   1 
ATOM   1415 C CA  . LEU A 1 285 ? 141.511 146.766 110.306 1.00 43.75  ?  201 LEU A CA  1 
ATOM   1416 C C   . LEU A 1 285 ? 141.290 147.261 111.729 1.00 51.52  ?  201 LEU A C   1 
ATOM   1417 O O   . LEU A 1 285 ? 142.254 147.407 112.489 1.00 54.57  ?  201 LEU A O   1 
ATOM   1418 C CB  . LEU A 1 285 ? 141.864 147.941 109.396 1.00 44.07  ?  201 LEU A CB  1 
ATOM   1419 C CG  . LEU A 1 285 ? 142.962 147.717 108.358 1.00 53.03  ?  201 LEU A CG  1 
ATOM   1420 C CD1 . LEU A 1 285 ? 143.044 148.901 107.412 1.00 53.00  ?  201 LEU A CD1 1 
ATOM   1421 C CD2 . LEU A 1 285 ? 144.296 147.484 109.042 1.00 46.99  ?  201 LEU A CD2 1 
ATOM   1422 N N   . PHE A 1 286 ? 140.040 147.521 112.110 1.00 57.83  ?  202 PHE A N   1 
ATOM   1423 C CA  . PHE A 1 286 ? 139.718 148.083 113.414 1.00 57.87  ?  202 PHE A CA  1 
ATOM   1424 C C   . PHE A 1 286 ? 139.173 147.043 114.387 1.00 56.30  ?  202 PHE A C   1 
ATOM   1425 O O   . PHE A 1 286 ? 138.469 147.401 115.336 1.00 53.62  ?  202 PHE A O   1 
ATOM   1426 C CB  . PHE A 1 286 ? 138.724 149.233 113.257 1.00 47.79  ?  202 PHE A CB  1 
ATOM   1427 C CG  . PHE A 1 286 ? 139.279 150.410 112.511 1.00 50.82  ?  202 PHE A CG  1 
ATOM   1428 C CD1 . PHE A 1 286 ? 140.255 151.208 113.080 1.00 55.76  ?  202 PHE A CD1 1 
ATOM   1429 C CD2 . PHE A 1 286 ? 138.832 150.714 111.238 1.00 50.29  ?  202 PHE A CD2 1 
ATOM   1430 C CE1 . PHE A 1 286 ? 140.770 152.289 112.397 1.00 57.75  ?  202 PHE A CE1 1 
ATOM   1431 C CE2 . PHE A 1 286 ? 139.344 151.793 110.551 1.00 52.20  ?  202 PHE A CE2 1 
ATOM   1432 C CZ  . PHE A 1 286 ? 140.314 152.581 111.131 1.00 55.82  ?  202 PHE A CZ  1 
ATOM   1433 N N   . LEU A 1 287 ? 139.481 145.768 114.171 1.00 57.60  ?  203 LEU A N   1 
ATOM   1434 C CA  . LEU A 1 287 ? 139.043 144.720 115.080 1.00 54.10  ?  203 LEU A CA  1 
ATOM   1435 C C   . LEU A 1 287 ? 140.012 144.593 116.248 1.00 58.54  ?  203 LEU A C   1 
ATOM   1436 O O   . LEU A 1 287 ? 141.232 144.637 116.070 1.00 60.38  ?  203 LEU A O   1 
ATOM   1437 C CB  . LEU A 1 287 ? 138.932 143.385 114.345 1.00 49.51  ?  203 LEU A CB  1 
ATOM   1438 C CG  . LEU A 1 287 ? 137.663 143.147 113.525 1.00 52.12  ?  203 LEU A CG  1 
ATOM   1439 C CD1 . LEU A 1 287 ? 137.794 141.878 112.705 1.00 50.95  ?  203 LEU A CD1 1 
ATOM   1440 C CD2 . LEU A 1 287 ? 136.446 143.077 114.425 1.00 53.61  ?  203 LEU A CD2 1 
ATOM   1441 N N   . LYS A 1 288 ? 139.459 144.438 117.448 1.00 62.45  ?  204 LYS A N   1 
ATOM   1442 C CA  . LYS A 1 288 ? 140.281 144.310 118.644 1.00 58.12  ?  204 LYS A CA  1 
ATOM   1443 C C   . LYS A 1 288 ? 141.065 143.004 118.617 1.00 60.12  ?  204 LYS A C   1 
ATOM   1444 O O   . LYS A 1 288 ? 140.503 141.933 118.380 1.00 65.30  ?  204 LYS A O   1 
ATOM   1445 C CB  . LYS A 1 288 ? 139.398 144.372 119.890 1.00 56.86  ?  204 LYS A CB  1 
ATOM   1446 C CG  . LYS A 1 288 ? 140.143 144.208 121.203 1.00 61.69  ?  204 LYS A CG  1 
ATOM   1447 C CD  . LYS A 1 288 ? 139.221 144.461 122.386 1.00 59.65  ?  204 LYS A CD  1 
ATOM   1448 C CE  . LYS A 1 288 ? 138.665 143.163 122.947 1.00 59.31  ?  204 LYS A CE  1 
ATOM   1449 N NZ  . LYS A 1 288 ? 139.671 142.428 123.760 1.00 63.98  1  204 LYS A NZ  1 
ATOM   1450 N N   . ARG A 1 289 ? 142.369 143.095 118.866 1.00 59.54  ?  205 ARG A N   1 
ATOM   1451 C CA  . ARG A 1 289 ? 143.219 141.913 118.900 1.00 63.84  ?  205 ARG A CA  1 
ATOM   1452 C C   . ARG A 1 289 ? 143.288 141.377 120.322 1.00 68.13  ?  205 ARG A C   1 
ATOM   1453 O O   . ARG A 1 289 ? 143.707 142.112 121.226 1.00 68.47  ?  205 ARG A O   1 
ATOM   1454 C CB  . ARG A 1 289 ? 144.615 142.236 118.398 1.00 70.09  ?  205 ARG A CB  1 
ATOM   1455 C CG  . ARG A 1 289 ? 145.492 141.014 118.181 1.00 66.72  ?  205 ARG A CG  1 
ATOM   1456 C CD  . ARG A 1 289 ? 146.423 141.205 116.997 1.00 69.32  ?  205 ARG A CD  1 
ATOM   1457 N NE  . ARG A 1 289 ? 147.410 140.136 116.899 1.00 69.74  ?  205 ARG A NE  1 
ATOM   1458 C CZ  . ARG A 1 289 ? 148.722 140.324 116.918 1.00 66.69  ?  205 ARG A CZ  1 
ATOM   1459 N NH1 . ARG A 1 289 ? 149.246 141.533 117.028 1.00 69.21  1  205 ARG A NH1 1 
ATOM   1460 N NH2 . ARG A 1 289 ? 149.529 139.271 116.823 1.00 63.36  ?  205 ARG A NH2 1 
ATOM   1461 N N   . PRO A 1 290 ? 142.890 140.130 120.569 1.00 65.38  ?  206 PRO A N   1 
ATOM   1462 C CA  . PRO A 1 290 ? 142.921 139.605 121.939 1.00 66.23  ?  206 PRO A CA  1 
ATOM   1463 C C   . PRO A 1 290 ? 144.338 139.549 122.487 1.00 72.44  ?  206 PRO A C   1 
ATOM   1464 O O   . PRO A 1 290 ? 145.310 139.371 121.750 1.00 75.32  ?  206 PRO A O   1 
ATOM   1465 C CB  . PRO A 1 290 ? 142.321 138.200 121.797 1.00 64.71  ?  206 PRO A CB  1 
ATOM   1466 C CG  . PRO A 1 290 ? 141.601 138.211 120.489 1.00 65.84  ?  206 PRO A CG  1 
ATOM   1467 C CD  . PRO A 1 290 ? 142.361 139.148 119.612 1.00 61.96  ?  206 PRO A CD  1 
ATOM   1468 N N   . LYS A 1 291 ? 144.460 139.705 123.808 1.00 73.45  ?  207 LYS A N   1 
ATOM   1469 C CA  . LYS A 1 291 ? 145.802 139.675 124.451 1.00 72.35  ?  207 LYS A CA  1 
ATOM   1470 C C   . LYS A 1 291 ? 146.007 138.315 125.128 1.00 71.26  ?  207 LYS A C   1 
ATOM   1471 O O   . LYS A 1 291 ? 146.109 137.321 124.383 1.00 70.28  ?  207 LYS A O   1 
ATOM   1472 C CB  . LYS A 1 291 ? 145.933 140.824 125.455 1.00 75.63  ?  207 LYS A CB  1 
ATOM   1473 C CG  . LYS A 1 291 ? 145.730 142.217 124.874 1.00 73.43  ?  207 LYS A CG  1 
ATOM   1474 C CD  . LYS A 1 291 ? 145.857 143.319 125.902 1.00 73.35  ?  207 LYS A CD  1 
ATOM   1475 C CE  . LYS A 1 291 ? 145.646 144.700 125.319 1.00 69.45  ?  207 LYS A CE  1 
ATOM   1476 N NZ  . LYS A 1 291 ? 145.783 145.757 126.350 1.00 69.79  1  207 LYS A NZ  1 
ATOM   1477 N N   . SER A 1 333 ? 158.259 121.423 122.761 1.00 121.57 ?  249 SER A N   1 
ATOM   1478 C CA  . SER A 1 333 ? 157.997 122.514 121.830 1.00 122.70 ?  249 SER A CA  1 
ATOM   1479 C C   . SER A 1 333 ? 156.589 123.067 122.017 1.00 123.72 ?  249 SER A C   1 
ATOM   1480 O O   . SER A 1 333 ? 155.760 122.461 122.697 1.00 123.92 ?  249 SER A O   1 
ATOM   1481 C CB  . SER A 1 333 ? 158.190 122.047 120.386 1.00 121.89 ?  249 SER A CB  1 
ATOM   1482 O OG  . SER A 1 333 ? 159.501 121.550 120.181 1.00 122.93 ?  249 SER A OG  1 
ATOM   1483 N N   . VAL A 1 334 ? 156.327 124.228 121.413 1.00 118.66 ?  250 VAL A N   1 
ATOM   1484 C CA  . VAL A 1 334 ? 154.993 124.818 121.481 1.00 117.55 ?  250 VAL A CA  1 
ATOM   1485 C C   . VAL A 1 334 ? 153.985 123.930 120.764 1.00 116.43 ?  250 VAL A C   1 
ATOM   1486 O O   . VAL A 1 334 ? 152.854 123.743 121.231 1.00 114.79 ?  250 VAL A O   1 
ATOM   1487 C CB  . VAL A 1 334 ? 155.008 126.244 120.900 1.00 115.91 ?  250 VAL A CB  1 
ATOM   1488 C CG1 . VAL A 1 334 ? 153.690 126.947 121.182 1.00 114.40 ?  250 VAL A CG1 1 
ATOM   1489 C CG2 . VAL A 1 334 ? 156.175 127.034 121.471 1.00 115.34 ?  250 VAL A CG2 1 
ATOM   1490 N N   . LEU A 1 335 ? 154.376 123.373 119.614 1.00 113.98 ?  251 LEU A N   1 
ATOM   1491 C CA  . LEU A 1 335 ? 153.498 122.454 118.898 1.00 113.60 ?  251 LEU A CA  1 
ATOM   1492 C C   . LEU A 1 335 ? 153.207 121.205 119.719 1.00 114.84 ?  251 LEU A C   1 
ATOM   1493 O O   . LEU A 1 335 ? 152.079 120.701 119.697 1.00 116.52 ?  251 LEU A O   1 
ATOM   1494 C CB  . LEU A 1 335 ? 154.117 122.069 117.554 1.00 114.10 ?  251 LEU A CB  1 
ATOM   1495 C CG  . LEU A 1 335 ? 153.619 122.809 116.310 1.00 114.90 ?  251 LEU A CG  1 
ATOM   1496 C CD1 . LEU A 1 335 ? 153.514 124.303 116.565 1.00 114.53 ?  251 LEU A CD1 1 
ATOM   1497 C CD2 . LEU A 1 335 ? 154.526 122.528 115.122 1.00 113.25 ?  251 LEU A CD2 1 
ATOM   1498 N N   . ALA A 1 336 ? 154.206 120.690 120.439 1.00 115.05 ?  252 ALA A N   1 
ATOM   1499 C CA  . ALA A 1 336 ? 153.974 119.540 121.305 1.00 114.10 ?  252 ALA A CA  1 
ATOM   1500 C C   . ALA A 1 336 ? 152.978 119.875 122.407 1.00 116.18 ?  252 ALA A C   1 
ATOM   1501 O O   . ALA A 1 336 ? 152.091 119.070 122.718 1.00 120.31 ?  252 ALA A O   1 
ATOM   1502 C CB  . ALA A 1 336 ? 155.295 119.056 121.903 1.00 113.17 ?  252 ALA A CB  1 
ATOM   1503 N N   . ARG A 1 337 ? 153.123 121.066 122.995 1.00 112.34 ?  253 ARG A N   1 
ATOM   1504 C CA  . ARG A 1 337 ? 152.166 121.507 124.043 1.00 113.47 ?  253 ARG A CA  1 
ATOM   1505 C C   . ARG A 1 337 ? 150.763 121.554 123.433 1.00 113.63 ?  253 ARG A C   1 
ATOM   1506 O O   . ARG A 1 337 ? 149.830 121.012 124.058 1.00 109.39 ?  253 ARG A O   1 
ATOM   1507 C CB  . ARG A 1 337 ? 152.561 122.885 124.580 1.00 110.67 ?  253 ARG A CB  1 
ATOM   1508 C CG  . ARG A 1 337 ? 153.968 122.946 125.155 1.00 110.08 ?  253 ARG A CG  1 
ATOM   1509 C CD  . ARG A 1 337 ? 154.473 124.370 125.279 1.00 114.20 ?  253 ARG A CD  1 
ATOM   1510 N NE  . ARG A 1 337 ? 155.913 124.419 125.485 1.00 114.25 ?  253 ARG A NE  1 
ATOM   1511 C CZ  . ARG A 1 337 ? 156.504 124.952 126.548 1.00 110.44 ?  253 ARG A CZ  1 
ATOM   1512 N NH1 . ARG A 1 337 ? 155.774 125.472 127.518 1.00 108.90 1  253 ARG A NH1 1 
ATOM   1513 N NH2 . ARG A 1 337 ? 157.823 124.963 126.636 1.00 108.23 ?  253 ARG A NH2 1 
ATOM   1514 N N   . MET A 1 338 ? 150.628 122.171 122.255 1.00 113.53 ?  254 MET A N   1 
ATOM   1515 C CA  . MET A 1 338 ? 149.317 122.300 121.630 1.00 112.51 ?  254 MET A CA  1 
ATOM   1516 C C   . MET A 1 338 ? 148.710 120.935 121.334 1.00 113.55 ?  254 MET A C   1 
ATOM   1517 O O   . MET A 1 338 ? 147.513 120.726 121.543 1.00 114.20 ?  254 MET A O   1 
ATOM   1518 C CB  . MET A 1 338 ? 149.410 123.128 120.349 1.00 110.56 ?  254 MET A CB  1 
ATOM   1519 C CG  . MET A 1 338 ? 149.052 124.592 120.533 1.00 111.22 ?  254 MET A CG  1 
ATOM   1520 S SD  . MET A 1 338 ? 149.019 125.513 118.982 1.00 117.11 ?  254 MET A SD  1 
ATOM   1521 C CE  . MET A 1 338 ? 150.219 124.605 118.013 1.00 110.52 ?  254 MET A CE  1 
ATOM   1522 N N   . LEU A 1 339 ? 149.520 119.992 120.848 1.00 109.83 ?  255 LEU A N   1 
ATOM   1523 C CA  . LEU A 1 339 ? 149.003 118.658 120.555 1.00 108.76 ?  255 LEU A CA  1 
ATOM   1524 C C   . LEU A 1 339 ? 148.577 117.932 121.826 1.00 109.68 ?  255 LEU A C   1 
ATOM   1525 O O   . LEU A 1 339 ? 147.537 117.260 121.846 1.00 113.26 ?  255 LEU A O   1 
ATOM   1526 C CB  . LEU A 1 339 ? 150.050 117.844 119.796 1.00 109.28 ?  255 LEU A CB  1 
ATOM   1527 C CG  . LEU A 1 339 ? 150.304 118.233 118.338 1.00 109.81 ?  255 LEU A CG  1 
ATOM   1528 C CD1 . LEU A 1 339 ? 150.786 117.028 117.545 1.00 109.73 ?  255 LEU A CD1 1 
ATOM   1529 C CD2 . LEU A 1 339 ? 149.060 118.834 117.700 1.00 107.97 ?  255 LEU A CD2 1 
ATOM   1530 N N   . ARG A 1 340 ? 149.366 118.050 122.897 1.00 107.07 ?  256 ARG A N   1 
ATOM   1531 C CA  . ARG A 1 340 ? 148.991 117.415 124.156 1.00 110.15 ?  256 ARG A CA  1 
ATOM   1532 C C   . ARG A 1 340 ? 147.701 118.008 124.709 1.00 111.05 ?  256 ARG A C   1 
ATOM   1533 O O   . ARG A 1 340 ? 146.820 117.274 125.179 1.00 108.99 ?  256 ARG A O   1 
ATOM   1534 C CB  . ARG A 1 340 ? 150.127 117.547 125.170 1.00 109.49 ?  256 ARG A CB  1 
ATOM   1535 C CG  . ARG A 1 340 ? 151.363 116.734 124.815 1.00 108.00 ?  256 ARG A CG  1 
ATOM   1536 C CD  . ARG A 1 340 ? 152.554 117.126 125.673 1.00 107.50 ?  256 ARG A CD  1 
ATOM   1537 N NE  . ARG A 1 340 ? 152.558 116.429 126.954 1.00 111.75 ?  256 ARG A NE  1 
ATOM   1538 C CZ  . ARG A 1 340 ? 153.595 115.759 127.438 1.00 110.67 ?  256 ARG A CZ  1 
ATOM   1539 N NH1 . ARG A 1 340 ? 154.737 115.677 126.774 1.00 111.16 1  256 ARG A NH1 1 
ATOM   1540 N NH2 . ARG A 1 340 ? 153.485 115.157 128.619 1.00 107.14 ?  256 ARG A NH2 1 
ATOM   1541 N N   . GLU A 1 341 ? 147.565 119.336 124.654 1.00 109.46 ?  257 GLU A N   1 
ATOM   1542 C CA  . GLU A 1 341 ? 146.338 119.969 125.124 1.00 110.11 ?  257 GLU A CA  1 
ATOM   1543 C C   . GLU A 1 341 ? 145.154 119.594 124.242 1.00 109.35 ?  257 GLU A C   1 
ATOM   1544 O O   . GLU A 1 341 ? 144.035 119.423 124.737 1.00 108.85 ?  257 GLU A O   1 
ATOM   1545 C CB  . GLU A 1 341 ? 146.512 121.485 125.178 1.00 108.76 ?  257 GLU A CB  1 
ATOM   1546 C CG  . GLU A 1 341 ? 145.599 122.169 126.182 1.00 109.19 ?  257 GLU A CG  1 
ATOM   1547 C CD  . GLU A 1 341 ? 145.309 121.299 127.391 1.00 111.27 ?  257 GLU A CD  1 
ATOM   1548 O OE1 . GLU A 1 341 ? 146.243 121.045 128.182 1.00 109.77 ?  257 GLU A OE1 1 
ATOM   1549 O OE2 . GLU A 1 341 ? 144.148 120.867 127.549 1.00 109.44 -1 257 GLU A OE2 1 
ATOM   1550 N N   . LEU A 1 342 ? 145.384 119.457 122.935 1.00 103.02 ?  258 LEU A N   1 
ATOM   1551 C CA  . LEU A 1 342 ? 144.330 119.023 122.027 1.00 98.48  ?  258 LEU A CA  1 
ATOM   1552 C C   . LEU A 1 342 ? 143.849 117.624 122.382 1.00 101.37 ?  258 LEU A C   1 
ATOM   1553 O O   . LEU A 1 342 ? 142.642 117.364 122.415 1.00 100.63 ?  258 LEU A O   1 
ATOM   1554 C CB  . LEU A 1 342 ? 144.842 119.068 120.587 1.00 97.35  ?  258 LEU A CB  1 
ATOM   1555 C CG  . LEU A 1 342 ? 143.889 118.661 119.464 1.00 100.02 ?  258 LEU A CG  1 
ATOM   1556 C CD1 . LEU A 1 342 ? 142.558 119.360 119.628 1.00 101.59 ?  258 LEU A CD1 1 
ATOM   1557 C CD2 . LEU A 1 342 ? 144.495 118.968 118.104 1.00 100.62 ?  258 LEU A CD2 1 
ATOM   1558 N N   . GLY A 1 343 ? 144.781 116.711 122.660 1.00 103.28 ?  259 GLY A N   1 
ATOM   1559 C CA  . GLY A 1 343 ? 144.389 115.370 123.065 1.00 100.13 ?  259 GLY A CA  1 
ATOM   1560 C C   . GLY A 1 343 ? 143.643 115.355 124.387 1.00 102.28 ?  259 GLY A C   1 
ATOM   1561 O O   . GLY A 1 343 ? 142.634 114.656 124.537 1.00 104.34 ?  259 GLY A O   1 
ATOM   1562 N N   . ASP A 1 344 ? 144.124 116.131 125.361 1.00 101.49 ?  260 ASP A N   1 
ATOM   1563 C CA  . ASP A 1 344 ? 143.447 116.195 126.653 1.00 102.70 ?  260 ASP A CA  1 
ATOM   1564 C C   . ASP A 1 344 ? 142.035 116.747 126.504 1.00 102.14 ?  260 ASP A C   1 
ATOM   1565 O O   . ASP A 1 344 ? 141.097 116.259 127.145 1.00 101.90 ?  260 ASP A O   1 
ATOM   1566 C CB  . ASP A 1 344 ? 144.259 117.044 127.631 1.00 105.71 ?  260 ASP A CB  1 
ATOM   1567 C CG  . ASP A 1 344 ? 143.918 116.753 129.082 1.00 105.22 ?  260 ASP A CG  1 
ATOM   1568 O OD1 . ASP A 1 344 ? 142.717 116.694 129.420 1.00 101.78 ?  260 ASP A OD1 1 
ATOM   1569 O OD2 . ASP A 1 344 ? 144.856 116.580 129.889 1.00 104.76 -1 260 ASP A OD2 1 
ATOM   1570 N N   . SER A 1 345 ? 141.863 117.771 125.665 1.00 95.73  ?  261 SER A N   1 
ATOM   1571 C CA  . SER A 1 345 ? 140.532 118.312 125.415 1.00 94.64  ?  261 SER A CA  1 
ATOM   1572 C C   . SER A 1 345 ? 139.649 117.297 124.700 1.00 92.83  ?  261 SER A C   1 
ATOM   1573 O O   . SER A 1 345 ? 138.456 117.183 125.002 1.00 91.53  ?  261 SER A O   1 
ATOM   1574 C CB  . SER A 1 345 ? 140.636 119.605 124.608 1.00 96.01  ?  261 SER A CB  1 
ATOM   1575 O OG  . SER A 1 345 ? 141.409 120.575 125.293 1.00 95.22  ?  261 SER A OG  1 
ATOM   1576 N N   . LEU A 1 346 ? 140.215 116.554 123.747 1.00 89.20  ?  262 LEU A N   1 
ATOM   1577 C CA  . LEU A 1 346 ? 139.463 115.501 123.077 1.00 85.30  ?  262 LEU A CA  1 
ATOM   1578 C C   . LEU A 1 346 ? 139.102 114.357 124.011 1.00 86.96  ?  262 LEU A C   1 
ATOM   1579 O O   . LEU A 1 346 ? 138.205 113.578 123.687 1.00 87.62  ?  262 LEU A O   1 
ATOM   1580 C CB  . LEU A 1 346 ? 140.241 114.965 121.873 1.00 85.83  ?  262 LEU A CB  1 
ATOM   1581 C CG  . LEU A 1 346 ? 139.999 115.629 120.516 1.00 90.35  ?  262 LEU A CG  1 
ATOM   1582 C CD1 . LEU A 1 346 ? 138.691 115.133 119.924 1.00 89.90  ?  262 LEU A CD1 1 
ATOM   1583 C CD2 . LEU A 1 346 ? 139.973 117.140 120.625 1.00 92.27  ?  262 LEU A CD2 1 
ATOM   1584 N N   . ARG A 1 347 ? 139.782 114.218 125.147 1.00 97.35  ?  263 ARG A N   1 
ATOM   1585 C CA  . ARG A 1 347 ? 139.325 113.231 126.120 1.00 97.10  ?  263 ARG A CA  1 
ATOM   1586 C C   . ARG A 1 347 ? 137.941 113.569 126.670 1.00 97.43  ?  263 ARG A C   1 
ATOM   1587 O O   . ARG A 1 347 ? 137.237 112.670 127.142 1.00 97.18  ?  263 ARG A O   1 
ATOM   1588 C CB  . ARG A 1 347 ? 140.340 113.098 127.256 1.00 97.72  ?  263 ARG A CB  1 
ATOM   1589 C CG  . ARG A 1 347 ? 140.129 111.873 128.132 1.00 96.71  ?  263 ARG A CG  1 
ATOM   1590 C CD  . ARG A 1 347 ? 141.434 111.138 128.381 1.00 94.92  ?  263 ARG A CD  1 
ATOM   1591 N NE  . ARG A 1 347 ? 141.858 110.377 127.211 1.00 100.09 ?  263 ARG A NE  1 
ATOM   1592 C CZ  . ARG A 1 347 ? 142.816 110.755 126.376 1.00 102.88 ?  263 ARG A CZ  1 
ATOM   1593 N NH1 . ARG A 1 347 ? 143.477 111.889 126.549 1.00 102.09 1  263 ARG A NH1 1 
ATOM   1594 N NH2 . ARG A 1 347 ? 143.119 109.978 125.340 1.00 98.83  ?  263 ARG A NH2 1 
ATOM   1595 N N   . ARG A 1 348 ? 137.535 114.836 126.611 1.00 86.13  ?  264 ARG A N   1 
ATOM   1596 C CA  . ARG A 1 348 ? 136.201 115.226 127.041 1.00 83.69  ?  264 ARG A CA  1 
ATOM   1597 C C   . ARG A 1 348 ? 135.148 114.661 126.086 1.00 82.31  ?  264 ARG A C   1 
ATOM   1598 O O   . ARG A 1 348 ? 135.389 114.546 124.882 1.00 83.53  ?  264 ARG A O   1 
ATOM   1599 C CB  . ARG A 1 348 ? 136.089 116.748 127.104 1.00 81.28  ?  264 ARG A CB  1 
ATOM   1600 C CG  . ARG A 1 348 ? 135.383 117.283 128.340 1.00 83.38  ?  264 ARG A CG  1 
ATOM   1601 C CD  . ARG A 1 348 ? 135.916 118.646 128.758 1.00 83.40  ?  264 ARG A CD  1 
ATOM   1602 N NE  . ARG A 1 348 ? 137.350 118.626 129.018 1.00 86.02  ?  264 ARG A NE  1 
ATOM   1603 C CZ  . ARG A 1 348 ? 138.271 119.080 128.180 1.00 86.95  ?  264 ARG A CZ  1 
ATOM   1604 N NH1 . ARG A 1 348 ? 137.943 119.598 127.008 1.00 84.93  1  264 ARG A NH1 1 
ATOM   1605 N NH2 . ARG A 1 348 ? 139.553 119.013 128.527 1.00 86.07  ?  264 ARG A NH2 1 
ATOM   1606 N N   . PRO A 1 349 ? 133.966 114.296 126.600 1.00 78.14  ?  265 PRO A N   1 
ATOM   1607 C CA  . PRO A 1 349 ? 132.955 113.658 125.743 1.00 77.25  ?  265 PRO A CA  1 
ATOM   1608 C C   . PRO A 1 349 ? 132.274 114.611 124.771 1.00 73.95  ?  265 PRO A C   1 
ATOM   1609 O O   . PRO A 1 349 ? 132.039 114.253 123.613 1.00 76.85  ?  265 PRO A O   1 
ATOM   1610 C CB  . PRO A 1 349 ? 131.945 113.088 126.751 1.00 78.07  ?  265 PRO A CB  1 
ATOM   1611 C CG  . PRO A 1 349 ? 132.601 113.196 128.098 1.00 77.62  ?  265 PRO A CG  1 
ATOM   1612 C CD  . PRO A 1 349 ? 133.538 114.345 128.005 1.00 76.51  ?  265 PRO A CD  1 
ATOM   1613 N N   . GLN A 1 350 ? 131.934 115.816 125.235 1.00 64.30  ?  266 GLN A N   1 
ATOM   1614 C CA  . GLN A 1 350 ? 131.222 116.763 124.381 1.00 65.24  ?  266 GLN A CA  1 
ATOM   1615 C C   . GLN A 1 350 ? 132.064 117.165 123.177 1.00 63.19  ?  266 GLN A C   1 
ATOM   1616 O O   . GLN A 1 350 ? 131.550 117.275 122.056 1.00 66.00  ?  266 GLN A O   1 
ATOM   1617 C CB  . GLN A 1 350 ? 130.819 117.996 125.187 1.00 67.33  ?  266 GLN A CB  1 
ATOM   1618 C CG  . GLN A 1 350 ? 129.455 118.550 124.829 1.00 71.10  ?  266 GLN A CG  1 
ATOM   1619 C CD  . GLN A 1 350 ? 128.320 117.741 125.420 1.00 72.52  ?  266 GLN A CD  1 
ATOM   1620 O OE1 . GLN A 1 350 ? 128.478 117.091 126.453 1.00 74.09  ?  266 GLN A OE1 1 
ATOM   1621 N NE2 . GLN A 1 350 ? 127.164 117.780 124.769 1.00 67.50  ?  266 GLN A NE2 1 
ATOM   1622 N N   . LEU A 1 351 ? 133.358 117.401 123.394 1.00 60.71  ?  267 LEU A N   1 
ATOM   1623 C CA  . LEU A 1 351 ? 134.237 117.741 122.282 1.00 61.58  ?  267 LEU A CA  1 
ATOM   1624 C C   . LEU A 1 351 ? 134.331 116.591 121.290 1.00 60.77  ?  267 LEU A C   1 
ATOM   1625 O O   . LEU A 1 351 ? 134.292 116.813 120.077 1.00 67.56  ?  267 LEU A O   1 
ATOM   1626 C CB  . LEU A 1 351 ? 135.620 118.128 122.804 1.00 68.39  ?  267 LEU A CB  1 
ATOM   1627 C CG  . LEU A 1 351 ? 136.638 118.660 121.793 1.00 61.63  ?  267 LEU A CG  1 
ATOM   1628 C CD1 . LEU A 1 351 ? 135.971 119.496 120.722 1.00 59.53  ?  267 LEU A CD1 1 
ATOM   1629 C CD2 . LEU A 1 351 ? 137.695 119.476 122.507 1.00 63.21  ?  267 LEU A CD2 1 
ATOM   1630 N N   . ARG A 1 352 ? 134.446 115.353 121.782 1.00 58.09  ?  268 ARG A N   1 
ATOM   1631 C CA  . ARG A 1 352 ? 134.431 114.200 120.885 1.00 56.27  ?  268 ARG A CA  1 
ATOM   1632 C C   . ARG A 1 352 ? 133.168 114.180 120.044 1.00 57.79  ?  268 ARG A C   1 
ATOM   1633 O O   . ARG A 1 352 ? 133.226 114.063 118.815 1.00 65.22  ?  268 ARG A O   1 
ATOM   1634 C CB  . ARG A 1 352 ? 134.529 112.896 121.675 1.00 58.99  ?  268 ARG A CB  1 
ATOM   1635 C CG  . ARG A 1 352 ? 135.891 112.562 122.199 1.00 64.68  ?  268 ARG A CG  1 
ATOM   1636 C CD  . ARG A 1 352 ? 135.908 111.234 122.953 1.00 63.34  ?  268 ARG A CD  1 
ATOM   1637 N NE  . ARG A 1 352 ? 134.636 110.915 123.593 1.00 67.39  ?  268 ARG A NE  1 
ATOM   1638 C CZ  . ARG A 1 352 ? 133.739 110.068 123.104 1.00 70.65  ?  268 ARG A CZ  1 
ATOM   1639 N NH1 . ARG A 1 352 ? 133.940 109.433 121.961 1.00 65.50  1  268 ARG A NH1 1 
ATOM   1640 N NH2 . ARG A 1 352 ? 132.613 109.854 123.779 1.00 70.68  ?  268 ARG A NH2 1 
ATOM   1641 N N   . LEU A 1 353 ? 132.011 114.290 120.697 1.00 53.47  ?  269 LEU A N   1 
ATOM   1642 C CA  . LEU A 1 353 ? 130.743 114.172 119.988 1.00 53.61  ?  269 LEU A CA  1 
ATOM   1643 C C   . LEU A 1 353 ? 130.612 115.249 118.921 1.00 55.35  ?  269 LEU A C   1 
ATOM   1644 O O   . LEU A 1 353 ? 130.286 114.960 117.763 1.00 63.22  ?  269 LEU A O   1 
ATOM   1645 C CB  . LEU A 1 353 ? 129.587 114.252 120.983 1.00 54.05  ?  269 LEU A CB  1 
ATOM   1646 C CG  . LEU A 1 353 ? 128.218 114.599 120.411 1.00 54.09  ?  269 LEU A CG  1 
ATOM   1647 C CD1 . LEU A 1 353 ? 127.721 113.466 119.543 1.00 55.65  ?  269 LEU A CD1 1 
ATOM   1648 C CD2 . LEU A 1 353 ? 127.243 114.880 121.532 1.00 55.89  ?  269 LEU A CD2 1 
ATOM   1649 N N   . TRP A 1 354 ? 130.893 116.499 119.283 1.00 50.72  ?  270 TRP A N   1 
ATOM   1650 C CA  . TRP A 1 354 ? 130.662 117.577 118.333 1.00 45.01  ?  270 TRP A CA  1 
ATOM   1651 C C   . TRP A 1 354 ? 131.743 117.651 117.262 1.00 43.91  ?  270 TRP A C   1 
ATOM   1652 O O   . TRP A 1 354 ? 131.450 118.048 116.132 1.00 57.57  ?  270 TRP A O   1 
ATOM   1653 C CB  . TRP A 1 354 ? 130.519 118.900 119.076 1.00 53.95  ?  270 TRP A CB  1 
ATOM   1654 C CG  . TRP A 1 354 ? 129.178 119.015 119.728 1.00 56.96  ?  270 TRP A CG  1 
ATOM   1655 C CD1 . TRP A 1 354 ? 128.912 118.994 121.063 1.00 55.11  ?  270 TRP A CD1 1 
ATOM   1656 C CD2 . TRP A 1 354 ? 127.912 119.132 119.069 1.00 55.16  ?  270 TRP A CD2 1 
ATOM   1657 N NE1 . TRP A 1 354 ? 127.561 119.109 121.279 1.00 59.42  ?  270 TRP A NE1 1 
ATOM   1658 C CE2 . TRP A 1 354 ? 126.925 119.194 120.069 1.00 59.81  ?  270 TRP A CE2 1 
ATOM   1659 C CE3 . TRP A 1 354 ? 127.519 119.199 117.731 1.00 47.24  ?  270 TRP A CE3 1 
ATOM   1660 C CZ2 . TRP A 1 354 ? 125.571 119.322 119.772 1.00 52.47  ?  270 TRP A CZ2 1 
ATOM   1661 C CZ3 . TRP A 1 354 ? 126.176 119.329 117.439 1.00 42.90  ?  270 TRP A CZ3 1 
ATOM   1662 C CH2 . TRP A 1 354 ? 125.219 119.388 118.454 1.00 45.30  ?  270 TRP A CH2 1 
ATOM   1663 N N   . SER A 1 355 ? 132.979 117.246 117.566 1.00 40.95  ?  271 SER A N   1 
ATOM   1664 C CA  . SER A 1 355 ? 133.996 117.164 116.524 1.00 45.78  ?  271 SER A CA  1 
ATOM   1665 C C   . SER A 1 355 ? 133.685 116.046 115.539 1.00 50.19  ?  271 SER A C   1 
ATOM   1666 O O   . SER A 1 355 ? 133.897 116.202 114.331 1.00 54.07  ?  271 SER A O   1 
ATOM   1667 C CB  . SER A 1 355 ? 135.375 116.964 117.147 1.00 50.19  ?  271 SER A CB  1 
ATOM   1668 O OG  . SER A 1 355 ? 135.939 118.202 117.538 1.00 56.12  ?  271 SER A OG  1 
ATOM   1669 N N   . LEU A 1 356 ? 133.190 114.906 116.030 1.00 51.94  ?  272 LEU A N   1 
ATOM   1670 C CA  . LEU A 1 356 ? 132.760 113.850 115.123 1.00 48.73  ?  272 LEU A CA  1 
ATOM   1671 C C   . LEU A 1 356 ? 131.603 114.319 114.256 1.00 51.39  ?  272 LEU A C   1 
ATOM   1672 O O   . LEU A 1 356 ? 131.575 114.050 113.047 1.00 60.45  ?  272 LEU A O   1 
ATOM   1673 C CB  . LEU A 1 356 ? 132.369 112.601 115.910 1.00 51.33  ?  272 LEU A CB  1 
ATOM   1674 C CG  . LEU A 1 356 ? 133.506 111.831 116.581 1.00 53.75  ?  272 LEU A CG  1 
ATOM   1675 C CD1 . LEU A 1 356 ? 133.022 110.469 117.047 1.00 52.10  ?  272 LEU A CD1 1 
ATOM   1676 C CD2 . LEU A 1 356 ? 134.693 111.694 115.642 1.00 51.62  ?  272 LEU A CD2 1 
ATOM   1677 N N   . TRP A 1 357 ? 130.641 115.030 114.852 1.00 42.53  ?  273 TRP A N   1 
ATOM   1678 C CA  . TRP A 1 357 ? 129.551 115.587 114.061 1.00 48.51  ?  273 TRP A CA  1 
ATOM   1679 C C   . TRP A 1 357 ? 130.085 116.521 112.987 1.00 55.69  ?  273 TRP A C   1 
ATOM   1680 O O   . TRP A 1 357 ? 129.679 116.439 111.826 1.00 63.35  ?  273 TRP A O   1 
ATOM   1681 C CB  . TRP A 1 357 ? 128.553 116.330 114.947 1.00 50.86  ?  273 TRP A CB  1 
ATOM   1682 C CG  . TRP A 1 357 ? 127.503 117.032 114.134 1.00 50.11  ?  273 TRP A CG  1 
ATOM   1683 C CD1 . TRP A 1 357 ? 126.306 116.523 113.737 1.00 51.28  ?  273 TRP A CD1 1 
ATOM   1684 C CD2 . TRP A 1 357 ? 127.569 118.361 113.597 1.00 50.49  ?  273 TRP A CD2 1 
ATOM   1685 N NE1 . TRP A 1 357 ? 125.615 117.450 113.000 1.00 53.86  ?  273 TRP A NE1 1 
ATOM   1686 C CE2 . TRP A 1 357 ? 126.371 118.586 112.896 1.00 50.27  ?  273 TRP A CE2 1 
ATOM   1687 C CE3 . TRP A 1 357 ? 128.521 119.382 113.645 1.00 51.22  ?  273 TRP A CE3 1 
ATOM   1688 C CZ2 . TRP A 1 357 ? 126.101 119.786 112.247 1.00 47.71  ?  273 TRP A CZ2 1 
ATOM   1689 C CZ3 . TRP A 1 357 ? 128.252 120.571 112.999 1.00 52.84  ?  273 TRP A CZ3 1 
ATOM   1690 C CH2 . TRP A 1 357 ? 127.051 120.765 112.313 1.00 46.73  ?  273 TRP A CH2 1 
ATOM   1691 N N   . TRP A 1 358 ? 131.002 117.414 113.356 1.00 47.98  ?  274 TRP A N   1 
ATOM   1692 C CA  . TRP A 1 358 ? 131.579 118.331 112.380 1.00 39.95  ?  274 TRP A CA  1 
ATOM   1693 C C   . TRP A 1 358 ? 132.224 117.564 111.237 1.00 50.54  ?  274 TRP A C   1 
ATOM   1694 O O   . TRP A 1 358 ? 131.850 117.730 110.072 1.00 58.75  ?  274 TRP A O   1 
ATOM   1695 C CB  . TRP A 1 358 ? 132.601 119.237 113.065 1.00 45.32  ?  274 TRP A CB  1 
ATOM   1696 C CG  . TRP A 1 358 ? 132.863 120.513 112.342 1.00 51.16  ?  274 TRP A CG  1 
ATOM   1697 C CD1 . TRP A 1 358 ? 133.033 120.676 111.001 1.00 57.38  ?  274 TRP A CD1 1 
ATOM   1698 C CD2 . TRP A 1 358 ? 133.004 121.812 112.926 1.00 57.17  ?  274 TRP A CD2 1 
ATOM   1699 N NE1 . TRP A 1 358 ? 133.263 121.998 110.710 1.00 58.29  ?  274 TRP A NE1 1 
ATOM   1700 C CE2 . TRP A 1 358 ? 133.250 122.716 111.876 1.00 54.26  ?  274 TRP A CE2 1 
ATOM   1701 C CE3 . TRP A 1 358 ? 132.942 122.298 114.234 1.00 57.67  ?  274 TRP A CE3 1 
ATOM   1702 C CZ2 . TRP A 1 358 ? 133.434 124.076 112.094 1.00 54.47  ?  274 TRP A CZ2 1 
ATOM   1703 C CZ3 . TRP A 1 358 ? 133.125 123.647 114.447 1.00 57.08  ?  274 TRP A CZ3 1 
ATOM   1704 C CH2 . TRP A 1 358 ? 133.368 124.522 113.384 1.00 59.75  ?  274 TRP A CH2 1 
ATOM   1705 N N   . VAL A 1 359 ? 133.140 116.653 111.569 1.00 50.22  ?  275 VAL A N   1 
ATOM   1706 C CA  . VAL A 1 359 ? 133.928 115.968 110.549 1.00 44.14  ?  275 VAL A CA  1 
ATOM   1707 C C   . VAL A 1 359 ? 133.030 115.169 109.617 1.00 52.05  ?  275 VAL A C   1 
ATOM   1708 O O   . VAL A 1 359 ? 133.197 115.207 108.392 1.00 62.61  ?  275 VAL A O   1 
ATOM   1709 C CB  . VAL A 1 359 ? 134.992 115.075 111.210 1.00 41.88  ?  275 VAL A CB  1 
ATOM   1710 C CG1 . VAL A 1 359 ? 135.667 114.201 110.170 1.00 49.76  ?  275 VAL A CG1 1 
ATOM   1711 C CG2 . VAL A 1 359 ? 136.013 115.925 111.938 1.00 51.20  ?  275 VAL A CG2 1 
ATOM   1712 N N   . PHE A 1 360 ? 132.059 114.442 110.168 1.00 47.69  ?  276 PHE A N   1 
ATOM   1713 C CA  . PHE A 1 360 ? 131.283 113.518 109.357 1.00 47.78  ?  276 PHE A CA  1 
ATOM   1714 C C   . PHE A 1 360 ? 129.950 114.081 108.881 1.00 49.12  ?  276 PHE A C   1 
ATOM   1715 O O   . PHE A 1 360 ? 129.217 113.373 108.186 1.00 55.46  ?  276 PHE A O   1 
ATOM   1716 C CB  . PHE A 1 360 ? 131.053 112.219 110.132 1.00 54.14  ?  276 PHE A CB  1 
ATOM   1717 C CG  . PHE A 1 360 ? 132.286 111.378 110.266 1.00 53.43  ?  276 PHE A CG  1 
ATOM   1718 C CD1 . PHE A 1 360 ? 132.803 110.707 109.174 1.00 48.22  ?  276 PHE A CD1 1 
ATOM   1719 C CD2 . PHE A 1 360 ? 132.939 111.273 111.480 1.00 54.21  ?  276 PHE A CD2 1 
ATOM   1720 C CE1 . PHE A 1 360 ? 133.940 109.939 109.292 1.00 50.57  ?  276 PHE A CE1 1 
ATOM   1721 C CE2 . PHE A 1 360 ? 134.076 110.506 111.604 1.00 52.51  ?  276 PHE A CE2 1 
ATOM   1722 C CZ  . PHE A 1 360 ? 134.578 109.838 110.508 1.00 51.15  ?  276 PHE A CZ  1 
ATOM   1723 N N   . ASN A 1 361 ? 129.623 115.331 109.208 1.00 49.32  ?  277 ASN A N   1 
ATOM   1724 C CA  . ASN A 1 361 ? 128.407 115.952 108.709 1.00 49.80  ?  277 ASN A CA  1 
ATOM   1725 C C   . ASN A 1 361 ? 128.658 117.172 107.844 1.00 52.34  ?  277 ASN A C   1 
ATOM   1726 O O   . ASN A 1 361 ? 127.895 117.405 106.907 1.00 64.21  ?  277 ASN A O   1 
ATOM   1727 C CB  . ASN A 1 361 ? 127.491 116.353 109.870 1.00 51.53  ?  277 ASN A CB  1 
ATOM   1728 C CG  . ASN A 1 361 ? 126.319 115.411 110.032 1.00 59.47  ?  277 ASN A CG  1 
ATOM   1729 O OD1 . ASN A 1 361 ? 126.382 114.254 109.627 1.00 66.58  ?  277 ASN A OD1 1 
ATOM   1730 N ND2 . ASN A 1 361 ? 125.236 115.906 110.616 1.00 53.78  ?  277 ASN A ND2 1 
ATOM   1731 N N   . SER A 1 362 ? 129.696 117.963 108.130 1.00 43.84  ?  278 SER A N   1 
ATOM   1732 C CA  . SER A 1 362 ? 130.055 119.037 107.216 1.00 46.37  ?  278 SER A CA  1 
ATOM   1733 C C   . SER A 1 362 ? 130.443 118.476 105.858 1.00 56.45  ?  278 SER A C   1 
ATOM   1734 O O   . SER A 1 362 ? 130.121 119.066 104.823 1.00 63.37  ?  278 SER A O   1 
ATOM   1735 C CB  . SER A 1 362 ? 131.194 119.868 107.801 1.00 54.89  ?  278 SER A CB  1 
ATOM   1736 O OG  . SER A 1 362 ? 130.732 120.671 108.873 1.00 58.18  ?  278 SER A OG  1 
ATOM   1737 N N   . ALA A 1 363 ? 131.124 117.330 105.840 1.00 51.84  ?  279 ALA A N   1 
ATOM   1738 C CA  . ALA A 1 363 ? 131.483 116.704 104.573 1.00 52.55  ?  279 ALA A CA  1 
ATOM   1739 C C   . ALA A 1 363 ? 130.239 116.341 103.771 1.00 58.00  ?  279 ALA A C   1 
ATOM   1740 O O   . ALA A 1 363 ? 130.150 116.637 102.574 1.00 64.79  ?  279 ALA A O   1 
ATOM   1741 C CB  . ALA A 1 363 ? 132.344 115.468 104.825 1.00 49.14  ?  279 ALA A CB  1 
ATOM   1742 N N   . GLY A 1 364 ? 129.259 115.712 104.421 1.00 53.55  ?  280 GLY A N   1 
ATOM   1743 C CA  . GLY A 1 364 ? 128.034 115.359 103.724 1.00 51.98  ?  280 GLY A CA  1 
ATOM   1744 C C   . GLY A 1 364 ? 127.249 116.574 103.269 1.00 51.40  ?  280 GLY A C   1 
ATOM   1745 O O   . GLY A 1 364 ? 126.704 116.594 102.160 1.00 66.72  ?  280 GLY A O   1 
ATOM   1746 N N   . TYR A 1 365 ? 127.182 117.604 104.115 1.00 47.39  ?  281 TYR A N   1 
ATOM   1747 C CA  . TYR A 1 365 ? 126.480 118.826 103.744 1.00 55.54  ?  281 TYR A CA  1 
ATOM   1748 C C   . TYR A 1 365 ? 127.135 119.497 102.546 1.00 61.72  ?  281 TYR A C   1 
ATOM   1749 O O   . TYR A 1 365 ? 126.445 119.951 101.628 1.00 67.16  ?  281 TYR A O   1 
ATOM   1750 C CB  . TYR A 1 365 ? 126.431 119.782 104.934 1.00 55.48  ?  281 TYR A CB  1 
ATOM   1751 C CG  . TYR A 1 365 ? 126.091 121.209 104.571 1.00 54.60  ?  281 TYR A CG  1 
ATOM   1752 C CD1 . TYR A 1 365 ? 124.774 121.610 104.416 1.00 50.25  ?  281 TYR A CD1 1 
ATOM   1753 C CD2 . TYR A 1 365 ? 127.087 122.156 104.392 1.00 60.25  ?  281 TYR A CD2 1 
ATOM   1754 C CE1 . TYR A 1 365 ? 124.460 122.911 104.090 1.00 57.64  ?  281 TYR A CE1 1 
ATOM   1755 C CE2 . TYR A 1 365 ? 126.782 123.459 104.067 1.00 59.31  ?  281 TYR A CE2 1 
ATOM   1756 C CZ  . TYR A 1 365 ? 125.468 123.831 103.917 1.00 61.87  ?  281 TYR A CZ  1 
ATOM   1757 O OH  . TYR A 1 365 ? 125.162 125.131 103.592 1.00 64.44  ?  281 TYR A OH  1 
ATOM   1758 N N   . TYR A 1 366 ? 128.467 119.578 102.540 1.00 58.94  ?  282 TYR A N   1 
ATOM   1759 C CA  . TYR A 1 366 ? 129.162 120.186 101.412 1.00 57.36  ?  282 TYR A CA  1 
ATOM   1760 C C   . TYR A 1 366 ? 128.995 119.354 100.151 1.00 59.37  ?  282 TYR A C   1 
ATOM   1761 O O   . TYR A 1 366 ? 128.836 119.909 99.059  1.00 62.08  ?  282 TYR A O   1 
ATOM   1762 C CB  . TYR A 1 366 ? 130.641 120.388 101.738 1.00 57.28  ?  282 TYR A CB  1 
ATOM   1763 C CG  . TYR A 1 366 ? 130.889 121.404 102.830 1.00 59.09  ?  282 TYR A CG  1 
ATOM   1764 C CD1 . TYR A 1 366 ? 131.870 121.198 103.790 1.00 60.47  ?  282 TYR A CD1 1 
ATOM   1765 C CD2 . TYR A 1 366 ? 130.133 122.564 102.906 1.00 58.38  ?  282 TYR A CD2 1 
ATOM   1766 C CE1 . TYR A 1 366 ? 132.093 122.123 104.790 1.00 63.48  ?  282 TYR A CE1 1 
ATOM   1767 C CE2 . TYR A 1 366 ? 130.348 123.494 103.901 1.00 61.18  ?  282 TYR A CE2 1 
ATOM   1768 C CZ  . TYR A 1 366 ? 131.329 123.269 104.840 1.00 64.73  ?  282 TYR A CZ  1 
ATOM   1769 O OH  . TYR A 1 366 ? 131.547 124.194 105.833 1.00 65.90  ?  282 TYR A OH  1 
ATOM   1770 N N   . LEU A 1 367 ? 129.019 118.025 100.276 1.00 56.13  ?  283 LEU A N   1 
ATOM   1771 C CA  . LEU A 1 367 ? 128.762 117.173 99.120  1.00 58.78  ?  283 LEU A CA  1 
ATOM   1772 C C   . LEU A 1 367 ? 127.386 117.456 98.534  1.00 62.57  ?  283 LEU A C   1 
ATOM   1773 O O   . LEU A 1 367 ? 127.243 117.665 97.323  1.00 68.67  ?  283 LEU A O   1 
ATOM   1774 C CB  . LEU A 1 367 ? 128.875 115.703 99.516  1.00 53.68  ?  283 LEU A CB  1 
ATOM   1775 C CG  . LEU A 1 367 ? 130.272 115.112 99.674  1.00 58.31  ?  283 LEU A CG  1 
ATOM   1776 C CD1 . LEU A 1 367 ? 130.207 113.874 100.545 1.00 59.50  ?  283 LEU A CD1 1 
ATOM   1777 C CD2 . LEU A 1 367 ? 130.867 114.787 98.318  1.00 60.64  ?  283 LEU A CD2 1 
ATOM   1778 N N   . VAL A 1 368 ? 126.361 117.478 99.387  1.00 51.98  ?  284 VAL A N   1 
ATOM   1779 C CA  . VAL A 1 368 ? 124.998 117.696 98.909  1.00 48.12  ?  284 VAL A CA  1 
ATOM   1780 C C   . VAL A 1 368 ? 124.871 119.076 98.277  1.00 61.34  ?  284 VAL A C   1 
ATOM   1781 O O   . VAL A 1 368 ? 124.303 119.230 97.190  1.00 72.92  ?  284 VAL A O   1 
ATOM   1782 C CB  . VAL A 1 368 ? 123.991 117.503 100.055 1.00 45.17  ?  284 VAL A CB  1 
ATOM   1783 C CG1 . VAL A 1 368 ? 122.622 118.009 99.648  1.00 60.16  ?  284 VAL A CG1 1 
ATOM   1784 C CG2 . VAL A 1 368 ? 123.923 116.043 100.452 1.00 55.97  ?  284 VAL A CG2 1 
ATOM   1785 N N   . VAL A 1 369 ? 125.413 120.099 98.941  1.00 58.30  ?  285 VAL A N   1 
ATOM   1786 C CA  . VAL A 1 369 ? 125.296 121.464 98.438  1.00 60.28  ?  285 VAL A CA  1 
ATOM   1787 C C   . VAL A 1 369 ? 126.000 121.604 97.094  1.00 68.01  ?  285 VAL A C   1 
ATOM   1788 O O   . VAL A 1 369 ? 125.463 122.206 96.156  1.00 70.69  ?  285 VAL A O   1 
ATOM   1789 C CB  . VAL A 1 369 ? 125.846 122.458 99.477  1.00 54.74  ?  285 VAL A CB  1 
ATOM   1790 C CG1 . VAL A 1 369 ? 126.341 123.724 98.803  1.00 63.52  ?  285 VAL A CG1 1 
ATOM   1791 C CG2 . VAL A 1 369 ? 124.780 122.785 100.502 1.00 52.70  ?  285 VAL A CG2 1 
ATOM   1792 N N   . TYR A 1 370 ? 127.205 121.045 96.973  1.00 78.11  ?  286 TYR A N   1 
ATOM   1793 C CA  . TYR A 1 370 ? 127.963 121.178 95.736  1.00 75.73  ?  286 TYR A CA  1 
ATOM   1794 C C   . TYR A 1 370 ? 127.312 120.403 94.597  1.00 71.25  ?  286 TYR A C   1 
ATOM   1795 O O   . TYR A 1 370 ? 127.277 120.881 93.458  1.00 73.50  ?  286 TYR A O   1 
ATOM   1796 C CB  . TYR A 1 370 ? 129.402 120.711 95.957  1.00 74.87  ?  286 TYR A CB  1 
ATOM   1797 C CG  . TYR A 1 370 ? 130.171 120.434 94.687  1.00 75.37  ?  286 TYR A CG  1 
ATOM   1798 C CD1 . TYR A 1 370 ? 130.383 121.435 93.747  1.00 76.85  ?  286 TYR A CD1 1 
ATOM   1799 C CD2 . TYR A 1 370 ? 130.687 119.173 94.427  1.00 74.24  ?  286 TYR A CD2 1 
ATOM   1800 C CE1 . TYR A 1 370 ? 131.086 121.187 92.585  1.00 77.55  ?  286 TYR A CE1 1 
ATOM   1801 C CE2 . TYR A 1 370 ? 131.391 118.915 93.267  1.00 77.04  ?  286 TYR A CE2 1 
ATOM   1802 C CZ  . TYR A 1 370 ? 131.588 119.925 92.350  1.00 78.13  ?  286 TYR A CZ  1 
ATOM   1803 O OH  . TYR A 1 370 ? 132.289 119.672 91.194  1.00 73.57  ?  286 TYR A OH  1 
ATOM   1804 N N   . TYR A 1 371 ? 126.788 119.211 94.877  1.00 68.90  ?  287 TYR A N   1 
ATOM   1805 C CA  . TYR A 1 371 ? 126.262 118.368 93.814  1.00 75.99  ?  287 TYR A CA  1 
ATOM   1806 C C   . TYR A 1 371 ? 124.805 118.653 93.471  1.00 80.18  ?  287 TYR A C   1 
ATOM   1807 O O   . TYR A 1 371 ? 124.338 118.200 92.420  1.00 83.56  ?  287 TYR A O   1 
ATOM   1808 C CB  . TYR A 1 371 ? 126.425 116.891 94.191  1.00 74.60  ?  287 TYR A CB  1 
ATOM   1809 C CG  . TYR A 1 371 ? 127.842 116.386 94.033  1.00 75.52  ?  287 TYR A CG  1 
ATOM   1810 C CD1 . TYR A 1 371 ? 128.456 116.367 92.790  1.00 76.55  ?  287 TYR A CD1 1 
ATOM   1811 C CD2 . TYR A 1 371 ? 128.569 115.943 95.127  1.00 76.22  ?  287 TYR A CD2 1 
ATOM   1812 C CE1 . TYR A 1 371 ? 129.750 115.914 92.638  1.00 78.52  ?  287 TYR A CE1 1 
ATOM   1813 C CE2 . TYR A 1 371 ? 129.866 115.488 94.986  1.00 79.29  ?  287 TYR A CE2 1 
ATOM   1814 C CZ  . TYR A 1 371 ? 130.451 115.476 93.739  1.00 82.93  ?  287 TYR A CZ  1 
ATOM   1815 O OH  . TYR A 1 371 ? 131.742 115.023 93.593  1.00 82.88  ?  287 TYR A OH  1 
ATOM   1816 N N   . VAL A 1 372 ? 124.080 119.401 94.305  1.00 74.17  ?  288 VAL A N   1 
ATOM   1817 C CA  . VAL A 1 372 ? 122.676 119.660 94.001  1.00 71.80  ?  288 VAL A CA  1 
ATOM   1818 C C   . VAL A 1 372 ? 122.536 120.577 92.792  1.00 77.03  ?  288 VAL A C   1 
ATOM   1819 O O   . VAL A 1 372 ? 121.548 120.489 92.053  1.00 80.55  ?  288 VAL A O   1 
ATOM   1820 C CB  . VAL A 1 372 ? 121.956 120.221 95.241  1.00 64.39  ?  288 VAL A CB  1 
ATOM   1821 C CG1 . VAL A 1 372 ? 122.234 121.704 95.415  1.00 65.66  ?  288 VAL A CG1 1 
ATOM   1822 C CG2 . VAL A 1 372 ? 120.468 119.960 95.146  1.00 70.22  ?  288 VAL A CG2 1 
ATOM   1823 N N   . HIS A 1 373 ? 123.538 121.418 92.543  1.00 85.00  ?  289 HIS A N   1 
ATOM   1824 C CA  . HIS A 1 373 ? 123.472 122.339 91.375  1.00 83.92  ?  289 HIS A CA  1 
ATOM   1825 C C   . HIS A 1 373 ? 123.441 121.514 90.090  1.00 86.25  ?  289 HIS A C   1 
ATOM   1826 O O   . HIS A 1 373 ? 122.547 121.719 89.240  1.00 81.99  ?  289 HIS A O   1 
ATOM   1827 C CB  . HIS A 1 373 ? 124.622 123.344 91.433  1.00 82.43  ?  289 HIS A CB  1 
ATOM   1828 C CG  . HIS A 1 373 ? 124.528 124.034 92.737  1.00 86.77  ?  289 HIS A CG  1 
ATOM   1829 N ND1 . HIS A 1 373 ? 125.529 124.205 93.666  1.00 87.55  ?  289 HIS A ND1 1 
ATOM   1830 C CD2 . HIS A 1 373 ? 123.425 124.568 93.255  1.00 87.27  ?  289 HIS A CD2 1 
ATOM   1831 C CE1 . HIS A 1 373 ? 125.028 124.847 94.709  1.00 87.82  ?  289 HIS A CE1 1 
ATOM   1832 N NE2 . HIS A 1 373 ? 123.749 125.059 94.480  1.00 89.28  ?  289 HIS A NE2 1 
ATOM   1833 N N   . ILE A 1 374 ? 124.396 120.590 89.956  1.00 88.99  ?  290 ILE A N   1 
ATOM   1834 C CA  . ILE A 1 374 ? 124.450 119.724 88.741  1.00 88.57  ?  290 ILE A CA  1 
ATOM   1835 C C   . ILE A 1 374 ? 123.261 118.757 88.768  1.00 86.54  ?  290 ILE A C   1 
ATOM   1836 O O   . ILE A 1 374 ? 122.786 118.393 87.676  1.00 89.06  ?  290 ILE A O   1 
ATOM   1837 C CB  . ILE A 1 374 ? 125.802 118.988 88.628  1.00 88.45  ?  290 ILE A CB  1 
ATOM   1838 C CG1 . ILE A 1 374 ? 126.299 118.480 89.983  1.00 85.40  ?  290 ILE A CG1 1 
ATOM   1839 C CG2 . ILE A 1 374 ? 126.836 119.876 87.954  1.00 89.35  ?  290 ILE A CG2 1 
ATOM   1840 C CD1 . ILE A 1 374 ? 127.494 119.235 90.518  1.00 87.51  ?  290 ILE A CD1 1 
ATOM   1841 N N   . LEU A 1 375 ? 122.790 118.366 89.958  1.00 81.24  ?  291 LEU A N   1 
ATOM   1842 C CA  . LEU A 1 375 ? 121.607 117.513 90.001  1.00 82.70  ?  291 LEU A CA  1 
ATOM   1843 C C   . LEU A 1 375 ? 120.412 118.207 89.364  1.00 86.98  ?  291 LEU A C   1 
ATOM   1844 O O   . LEU A 1 375 ? 119.661 117.593 88.596  1.00 90.71  ?  291 LEU A O   1 
ATOM   1845 C CB  . LEU A 1 375 ? 121.291 117.128 91.445  1.00 81.70  ?  291 LEU A CB  1 
ATOM   1846 C CG  . LEU A 1 375 ? 119.855 116.685 91.722  1.00 83.54  ?  291 LEU A CG  1 
ATOM   1847 C CD1 . LEU A 1 375 ? 119.608 115.302 91.150  1.00 86.90  ?  291 LEU A CD1 1 
ATOM   1848 C CD2 . LEU A 1 375 ? 119.559 116.714 93.209  1.00 85.73  ?  291 LEU A CD2 1 
ATOM   1849 N N   . TRP A 1 376 ? 120.220 119.490 89.672  1.00 85.02  ?  292 TRP A N   1 
ATOM   1850 C CA  . TRP A 1 376 ? 119.115 120.236 89.080  1.00 88.43  ?  292 TRP A CA  1 
ATOM   1851 C C   . TRP A 1 376 ? 119.389 120.587 87.623  1.00 89.89  ?  292 TRP A C   1 
ATOM   1852 O O   . TRP A 1 376 ? 118.453 120.648 86.817  1.00 84.55  ?  292 TRP A O   1 
ATOM   1853 C CB  . TRP A 1 376 ? 118.839 121.498 89.896  1.00 82.72  ?  292 TRP A CB  1 
ATOM   1854 C CG  . TRP A 1 376 ? 118.225 121.217 91.234  1.00 85.60  ?  292 TRP A CG  1 
ATOM   1855 C CD1 . TRP A 1 376 ? 117.447 120.149 91.570  1.00 83.56  ?  292 TRP A CD1 1 
ATOM   1856 C CD2 . TRP A 1 376 ? 118.342 122.015 92.418  1.00 89.52  ?  292 TRP A CD2 1 
ATOM   1857 N NE1 . TRP A 1 376 ? 117.071 120.232 92.888  1.00 82.84  ?  292 TRP A NE1 1 
ATOM   1858 C CE2 . TRP A 1 376 ? 117.609 121.369 93.431  1.00 83.46  ?  292 TRP A CE2 1 
ATOM   1859 C CE3 . TRP A 1 376 ? 118.996 123.213 92.719  1.00 87.62  ?  292 TRP A CE3 1 
ATOM   1860 C CZ2 . TRP A 1 376 ? 117.509 121.881 94.721  1.00 79.75  ?  292 TRP A CZ2 1 
ATOM   1861 C CZ3 . TRP A 1 376 ? 118.896 123.719 94.000  1.00 80.00  ?  292 TRP A CZ3 1 
ATOM   1862 C CH2 . TRP A 1 376 ? 118.159 123.054 94.985  1.00 77.41  ?  292 TRP A CH2 1 
ATOM   1863 N N   . ASN A 1 377 ? 120.654 120.823 87.266  1.00 96.65  ?  293 ASN A N   1 
ATOM   1864 C CA  . ASN A 1 377 ? 120.985 121.118 85.874  1.00 97.69  ?  293 ASN A CA  1 
ATOM   1865 C C   . ASN A 1 377 ? 120.803 119.894 84.985  1.00 97.12  ?  293 ASN A C   1 
ATOM   1866 O O   . ASN A 1 377 ? 120.426 120.022 83.814  1.00 98.74  ?  293 ASN A O   1 
ATOM   1867 C CB  . ASN A 1 377 ? 122.417 121.644 85.774  1.00 97.92  ?  293 ASN A CB  1 
ATOM   1868 C CG  . ASN A 1 377 ? 122.547 123.075 86.253  1.00 98.74  ?  293 ASN A CG  1 
ATOM   1869 O OD1 . ASN A 1 377 ? 121.572 123.687 86.688  1.00 98.64  ?  293 ASN A OD1 1 
ATOM   1870 N ND2 . ASN A 1 377 ? 123.757 123.618 86.175  1.00 97.32  ?  293 ASN A ND2 1 
ATOM   1871 N N   . GLU A 1 378 ? 121.076 118.699 85.517  1.00 100.33 ?  294 GLU A N   1 
ATOM   1872 C CA  . GLU A 1 378 ? 120.966 117.483 84.717  1.00 101.70 ?  294 GLU A CA  1 
ATOM   1873 C C   . GLU A 1 378 ? 119.529 117.239 84.271  1.00 106.85 ?  294 GLU A C   1 
ATOM   1874 O O   . GLU A 1 378 ? 119.285 116.844 83.125  1.00 107.89 ?  294 GLU A O   1 
ATOM   1875 C CB  . GLU A 1 378 ? 121.497 116.288 85.510  1.00 102.18 ?  294 GLU A CB  1 
ATOM   1876 C CG  . GLU A 1 378 ? 121.022 114.935 85.006  1.00 103.33 ?  294 GLU A CG  1 
ATOM   1877 C CD  . GLU A 1 378 ? 121.622 113.780 85.783  1.00 104.88 ?  294 GLU A CD  1 
ATOM   1878 O OE1 . GLU A 1 378 ? 121.186 113.542 86.928  1.00 103.69 ?  294 GLU A OE1 1 
ATOM   1879 O OE2 . GLU A 1 378 ? 122.530 113.109 85.249  1.00 106.31 -1 294 GLU A OE2 1 
ATOM   1880 N N   . VAL A 1 379 ? 118.568 117.470 85.159  1.00 104.21 ?  295 VAL A N   1 
ATOM   1881 C CA  . VAL A 1 379 ? 117.159 117.286 84.831  1.00 105.29 ?  295 VAL A CA  1 
ATOM   1882 C C   . VAL A 1 379 ? 116.720 118.295 83.774  1.00 102.72 ?  295 VAL A C   1 
ATOM   1883 O O   . VAL A 1 379 ? 116.362 117.922 82.657  1.00 98.07  ?  295 VAL A O   1 
ATOM   1884 C CB  . VAL A 1 379 ? 116.278 117.400 86.085  1.00 101.74 ?  295 VAL A CB  1 
ATOM   1885 C CG1 . VAL A 1 379 ? 114.828 117.645 85.694  1.00 101.94 ?  295 VAL A CG1 1 
ATOM   1886 C CG2 . VAL A 1 379 ? 116.403 116.147 86.930  1.00 97.93  ?  295 VAL A CG2 1 
ATOM   1887 N N   . ARG A 1 387 ? 116.930 127.962 85.864  1.00 101.49 ?  303 ARG A N   1 
ATOM   1888 C CA  . ARG A 1 387 ? 118.084 128.841 86.193  1.00 105.41 ?  303 ARG A CA  1 
ATOM   1889 C C   . ARG A 1 387 ? 117.679 129.806 87.312  1.00 106.42 ?  303 ARG A C   1 
ATOM   1890 O O   . ARG A 1 387 ? 118.316 129.769 88.382  1.00 106.18 ?  303 ARG A O   1 
ATOM   1891 C CB  . ARG A 1 387 ? 118.542 129.610 84.950  1.00 103.95 ?  303 ARG A CB  1 
ATOM   1892 C CG  . ARG A 1 387 ? 119.018 128.720 83.811  1.00 104.00 ?  303 ARG A CG  1 
ATOM   1893 C CD  . ARG A 1 387 ? 119.490 129.523 82.614  1.00 104.05 ?  303 ARG A CD  1 
ATOM   1894 N NE  . ARG A 1 387 ? 119.971 128.672 81.535  1.00 106.27 ?  303 ARG A NE  1 
ATOM   1895 C CZ  . ARG A 1 387 ? 120.444 129.120 80.378  1.00 108.12 ?  303 ARG A CZ  1 
ATOM   1896 N NH1 . ARG A 1 387 ? 120.497 130.419 80.144  1.00 108.25 1  303 ARG A NH1 1 
ATOM   1897 N NH2 . ARG A 1 387 ? 120.864 128.267 79.459  1.00 106.30 ?  303 ARG A NH2 1 
ATOM   1898 N N   . VAL A 1 388 ? 116.664 130.639 87.067  1.00 99.35  ?  304 VAL A N   1 
ATOM   1899 C CA  . VAL A 1 388 ? 116.197 131.566 88.095  1.00 99.74  ?  304 VAL A CA  1 
ATOM   1900 C C   . VAL A 1 388 ? 115.763 130.801 89.339  1.00 99.80  ?  304 VAL A C   1 
ATOM   1901 O O   . VAL A 1 388 ? 116.015 131.229 90.473  1.00 98.08  ?  304 VAL A O   1 
ATOM   1902 C CB  . VAL A 1 388 ? 115.063 132.448 87.541  1.00 96.88  ?  304 VAL A CB  1 
ATOM   1903 C CG1 . VAL A 1 388 ? 114.211 133.011 88.670  1.00 95.52  ?  304 VAL A CG1 1 
ATOM   1904 C CG2 . VAL A 1 388 ? 115.635 133.571 86.689  1.00 95.32  ?  304 VAL A CG2 1 
ATOM   1905 N N   . TYR A 1 389 ? 115.113 129.652 89.146  1.00 96.92  ?  305 TYR A N   1 
ATOM   1906 C CA  . TYR A 1 389 ? 114.683 128.845 90.281  1.00 95.09  ?  305 TYR A CA  1 
ATOM   1907 C C   . TYR A 1 389 ? 115.868 128.317 91.079  1.00 94.49  ?  305 TYR A C   1 
ATOM   1908 O O   . TYR A 1 389 ? 115.766 128.154 92.300  1.00 94.26  ?  305 TYR A O   1 
ATOM   1909 C CB  . TYR A 1 389 ? 113.803 127.692 89.799  1.00 96.13  ?  305 TYR A CB  1 
ATOM   1910 C CG  . TYR A 1 389 ? 112.430 128.125 89.339  1.00 96.96  ?  305 TYR A CG  1 
ATOM   1911 C CD1 . TYR A 1 389 ? 112.228 128.612 88.055  1.00 95.06  ?  305 TYR A CD1 1 
ATOM   1912 C CD2 . TYR A 1 389 ? 111.336 128.051 90.190  1.00 94.95  ?  305 TYR A CD2 1 
ATOM   1913 C CE1 . TYR A 1 389 ? 110.975 129.010 87.631  1.00 96.54  ?  305 TYR A CE1 1 
ATOM   1914 C CE2 . TYR A 1 389 ? 110.080 128.448 89.775  1.00 95.07  ?  305 TYR A CE2 1 
ATOM   1915 C CZ  . TYR A 1 389 ? 109.905 128.926 88.495  1.00 97.02  ?  305 TYR A CZ  1 
ATOM   1916 O OH  . TYR A 1 389 ? 108.656 129.322 88.076  1.00 95.43  ?  305 TYR A OH  1 
ATOM   1917 N N   . ASN A 1 390 ? 116.996 128.048 90.417  1.00 91.23  ?  306 ASN A N   1 
ATOM   1918 C CA  . ASN A 1 390 ? 118.198 127.636 91.137  1.00 92.05  ?  306 ASN A CA  1 
ATOM   1919 C C   . ASN A 1 390 ? 118.662 128.724 92.098  1.00 90.88  ?  306 ASN A C   1 
ATOM   1920 O O   . ASN A 1 390 ? 118.951 128.456 93.272  1.00 89.39  ?  306 ASN A O   1 
ATOM   1921 C CB  . ASN A 1 390 ? 119.307 127.287 90.145  1.00 91.02  ?  306 ASN A CB  1 
ATOM   1922 C CG  . ASN A 1 390 ? 120.348 126.358 90.735  1.00 95.79  ?  306 ASN A CG  1 
ATOM   1923 O OD1 . ASN A 1 390 ? 120.249 125.952 91.893  1.00 93.83  ?  306 ASN A OD1 1 
ATOM   1924 N ND2 . ASN A 1 390 ? 121.358 126.020 89.942  1.00 94.59  ?  306 ASN A ND2 1 
ATOM   1925 N N   . PHE A 1 391 ? 118.731 129.967 91.616  1.00 76.33  ?  307 PHE A N   1 
ATOM   1926 C CA  . PHE A 1 391 ? 119.106 131.076 92.486  1.00 76.48  ?  307 PHE A CA  1 
ATOM   1927 C C   . PHE A 1 391 ? 118.081 131.278 93.592  1.00 77.31  ?  307 PHE A C   1 
ATOM   1928 O O   . PHE A 1 391 ? 118.442 131.594 94.730  1.00 78.78  ?  307 PHE A O   1 
ATOM   1929 C CB  . PHE A 1 391 ? 119.266 132.361 91.678  1.00 74.55  ?  307 PHE A CB  1 
ATOM   1930 C CG  . PHE A 1 391 ? 119.070 133.607 92.492  1.00 74.37  ?  307 PHE A CG  1 
ATOM   1931 C CD1 . PHE A 1 391 ? 120.011 133.988 93.434  1.00 72.47  ?  307 PHE A CD1 1 
ATOM   1932 C CD2 . PHE A 1 391 ? 117.935 134.384 92.333  1.00 74.05  ?  307 PHE A CD2 1 
ATOM   1933 C CE1 . PHE A 1 391 ? 119.829 135.126 94.191  1.00 72.36  ?  307 PHE A CE1 1 
ATOM   1934 C CE2 . PHE A 1 391 ? 117.749 135.525 93.087  1.00 75.95  ?  307 PHE A CE2 1 
ATOM   1935 C CZ  . PHE A 1 391 ? 118.697 135.896 94.017  1.00 76.25  ?  307 PHE A CZ  1 
ATOM   1936 N N   . ALA A 1 392 ? 116.795 131.130 93.271  1.00 73.74  ?  308 ALA A N   1 
ATOM   1937 C CA  . ALA A 1 392 ? 115.760 131.291 94.286  1.00 70.95  ?  308 ALA A CA  1 
ATOM   1938 C C   . ALA A 1 392 ? 115.924 130.261 95.396  1.00 76.21  ?  308 ALA A C   1 
ATOM   1939 O O   . ALA A 1 392 ? 115.838 130.593 96.584  1.00 80.58  ?  308 ALA A O   1 
ATOM   1940 C CB  . ALA A 1 392 ? 114.376 131.184 93.649  1.00 74.91  ?  308 ALA A CB  1 
ATOM   1941 N N   . ALA A 1 393 ? 116.172 129.003 95.024  1.00 74.24  ?  309 ALA A N   1 
ATOM   1942 C CA  . ALA A 1 393 ? 116.390 127.961 96.021  1.00 69.47  ?  309 ALA A CA  1 
ATOM   1943 C C   . ALA A 1 393 ? 117.639 128.236 96.846  1.00 69.52  ?  309 ALA A C   1 
ATOM   1944 O O   . ALA A 1 393 ? 117.630 128.068 98.070  1.00 72.01  ?  309 ALA A O   1 
ATOM   1945 C CB  . ALA A 1 393 ? 116.488 126.596 95.341  1.00 70.14  ?  309 ALA A CB  1 
ATOM   1946 N N   . ASP A 1 394 ? 118.723 128.665 96.194  1.00 67.99  ?  310 ASP A N   1 
ATOM   1947 C CA  . ASP A 1 394 ? 119.955 128.959 96.921  1.00 70.71  ?  310 ASP A CA  1 
ATOM   1948 C C   . ASP A 1 394 ? 119.747 130.086 97.927  1.00 70.48  ?  310 ASP A C   1 
ATOM   1949 O O   . ASP A 1 394 ? 120.161 129.985 99.089  1.00 71.52  ?  310 ASP A O   1 
ATOM   1950 C CB  . ASP A 1 394 ? 121.068 129.314 95.937  1.00 73.87  ?  310 ASP A CB  1 
ATOM   1951 C CG  . ASP A 1 394 ? 122.385 128.653 96.283  1.00 79.29  ?  310 ASP A CG  1 
ATOM   1952 O OD1 . ASP A 1 394 ? 122.383 127.719 97.111  1.00 80.97  ?  310 ASP A OD1 1 
ATOM   1953 O OD2 . ASP A 1 394 ? 123.424 129.069 95.728  1.00 75.79  -1 310 ASP A OD2 1 
ATOM   1954 N N   . ALA A 1 395 ? 119.094 131.168 97.498  1.00 60.68  ?  311 ALA A N   1 
ATOM   1955 C CA  . ALA A 1 395 ? 118.868 132.303 98.384  1.00 56.76  ?  311 ALA A CA  1 
ATOM   1956 C C   . ALA A 1 395 ? 117.925 131.942 99.522  1.00 59.83  ?  311 ALA A C   1 
ATOM   1957 O O   . ALA A 1 395 ? 118.143 132.353 100.667 1.00 67.12  ?  311 ALA A O   1 
ATOM   1958 C CB  . ALA A 1 395 ? 118.323 133.488 97.589  1.00 56.73  ?  311 ALA A CB  1 
ATOM   1959 N N   . ALA A 1 396 ? 116.867 131.181 99.231  1.00 59.95  ?  312 ALA A N   1 
ATOM   1960 C CA  . ALA A 1 396 ? 115.952 130.764 100.287 1.00 58.44  ?  312 ALA A CA  1 
ATOM   1961 C C   . ALA A 1 396 ? 116.657 129.877 101.302 1.00 62.71  ?  312 ALA A C   1 
ATOM   1962 O O   . ALA A 1 396 ? 116.445 130.016 102.511 1.00 68.95  ?  312 ALA A O   1 
ATOM   1963 C CB  . ALA A 1 396 ? 114.748 130.042 99.685  1.00 59.29  ?  312 ALA A CB  1 
ATOM   1964 N N   . SER A 1 397 ? 117.506 128.960 100.829 1.00 64.20  ?  313 SER A N   1 
ATOM   1965 C CA  . SER A 1 397 ? 118.243 128.099 101.745 1.00 58.13  ?  313 SER A CA  1 
ATOM   1966 C C   . SER A 1 397 ? 119.210 128.905 102.602 1.00 61.79  ?  313 SER A C   1 
ATOM   1967 O O   . SER A 1 397 ? 119.345 128.645 103.801 1.00 64.92  ?  313 SER A O   1 
ATOM   1968 C CB  . SER A 1 397 ? 118.986 127.018 100.964 1.00 58.89  ?  313 SER A CB  1 
ATOM   1969 O OG  . SER A 1 397 ? 119.626 127.561 99.824  1.00 66.59  ?  313 SER A OG  1 
ATOM   1970 N N   . THR A 1 398 ? 119.891 129.890 102.010 1.00 58.98  ?  314 THR A N   1 
ATOM   1971 C CA  . THR A 1 398 ? 120.806 130.720 102.790 1.00 52.85  ?  314 THR A CA  1 
ATOM   1972 C C   . THR A 1 398 ? 120.060 131.544 103.834 1.00 57.50  ?  314 THR A C   1 
ATOM   1973 O O   . THR A 1 398 ? 120.512 131.669 104.981 1.00 67.57  ?  314 THR A O   1 
ATOM   1974 C CB  . THR A 1 398 ? 121.608 131.634 101.867 1.00 58.38  ?  314 THR A CB  1 
ATOM   1975 O OG1 . THR A 1 398 ? 122.028 130.899 100.711 1.00 67.39  ?  314 THR A OG1 1 
ATOM   1976 C CG2 . THR A 1 398 ? 122.830 132.169 102.588 1.00 59.80  ?  314 THR A CG2 1 
ATOM   1977 N N   . LEU A 1 399 ? 118.917 132.120 103.457 1.00 54.52  ?  315 LEU A N   1 
ATOM   1978 C CA  . LEU A 1 399 ? 118.136 132.903 104.408 1.00 53.13  ?  315 LEU A CA  1 
ATOM   1979 C C   . LEU A 1 399 ? 117.609 132.029 105.540 1.00 55.38  ?  315 LEU A C   1 
ATOM   1980 O O   . LEU A 1 399 ? 117.651 132.426 106.712 1.00 62.16  ?  315 LEU A O   1 
ATOM   1981 C CB  . LEU A 1 399 ? 116.988 133.607 103.688 1.00 54.76  ?  315 LEU A CB  1 
ATOM   1982 C CG  . LEU A 1 399 ? 115.908 134.233 104.569 1.00 60.27  ?  315 LEU A CG  1 
ATOM   1983 C CD1 . LEU A 1 399 ? 116.410 135.526 105.185 1.00 58.24  ?  315 LEU A CD1 1 
ATOM   1984 C CD2 . LEU A 1 399 ? 114.642 134.475 103.768 1.00 61.75  ?  315 LEU A CD2 1 
ATOM   1985 N N   . LEU A 1 400 ? 117.113 130.831 105.215 1.00 50.53  ?  316 LEU A N   1 
ATOM   1986 C CA  . LEU A 1 400 ? 116.667 129.925 106.266 1.00 50.40  ?  316 LEU A CA  1 
ATOM   1987 C C   . LEU A 1 400 ? 117.828 129.476 107.140 1.00 61.05  ?  316 LEU A C   1 
ATOM   1988 O O   . LEU A 1 400 ? 117.649 129.279 108.343 1.00 74.19  ?  316 LEU A O   1 
ATOM   1989 C CB  . LEU A 1 400 ? 115.959 128.707 105.676 1.00 51.95  ?  316 LEU A CB  1 
ATOM   1990 C CG  . LEU A 1 400 ? 115.390 127.782 106.757 1.00 55.79  ?  316 LEU A CG  1 
ATOM   1991 C CD1 . LEU A 1 400 ? 114.213 128.443 107.454 1.00 57.34  ?  316 LEU A CD1 1 
ATOM   1992 C CD2 . LEU A 1 400 ? 114.996 126.428 106.209 1.00 58.70  ?  316 LEU A CD2 1 
ATOM   1993 N N   . GLY A 1 401 ? 119.016 129.305 106.561 1.00 49.25  ?  317 GLY A N   1 
ATOM   1994 C CA  . GLY A 1 401 ? 120.176 128.980 107.371 1.00 46.26  ?  317 GLY A CA  1 
ATOM   1995 C C   . GLY A 1 401 ? 120.516 130.079 108.356 1.00 50.54  ?  317 GLY A C   1 
ATOM   1996 O O   . GLY A 1 401 ? 120.828 129.810 109.519 1.00 56.84  ?  317 GLY A O   1 
ATOM   1997 N N   . ALA A 1 402 ? 120.455 131.334 107.906 1.00 48.22  ?  318 ALA A N   1 
ATOM   1998 C CA  . ALA A 1 402 ? 120.681 132.452 108.817 1.00 49.98  ?  318 ALA A CA  1 
ATOM   1999 C C   . ALA A 1 402 ? 119.630 132.485 109.920 1.00 54.30  ?  318 ALA A C   1 
ATOM   2000 O O   . ALA A 1 402 ? 119.956 132.684 111.098 1.00 67.70  ?  318 ALA A O   1 
ATOM   2001 C CB  . ALA A 1 402 ? 120.685 133.769 108.043 1.00 52.38  ?  318 ALA A CB  1 
ATOM   2002 N N   . ILE A 1 403 ? 118.363 132.273 109.558 1.00 50.53  ?  319 ILE A N   1 
ATOM   2003 C CA  . ILE A 1 403 ? 117.290 132.285 110.551 1.00 52.56  ?  319 ILE A CA  1 
ATOM   2004 C C   . ILE A 1 403 ? 117.482 131.162 111.563 1.00 54.63  ?  319 ILE A C   1 
ATOM   2005 O O   . ILE A 1 403 ? 117.296 131.355 112.771 1.00 67.13  ?  319 ILE A O   1 
ATOM   2006 C CB  . ILE A 1 403 ? 115.919 132.196 109.857 1.00 55.02  ?  319 ILE A CB  1 
ATOM   2007 C CG1 . ILE A 1 403 ? 115.665 133.451 109.023 1.00 57.79  ?  319 ILE A CG1 1 
ATOM   2008 C CG2 . ILE A 1 403 ? 114.813 132.012 110.878 1.00 53.82  ?  319 ILE A CG2 1 
ATOM   2009 C CD1 . ILE A 1 403 ? 114.421 133.373 108.173 1.00 58.28  ?  319 ILE A CD1 1 
ATOM   2010 N N   . THR A 1 404 ? 117.857 129.972 111.091 1.00 38.51  ?  320 THR A N   1 
ATOM   2011 C CA  . THR A 1 404 ? 118.032 128.841 111.992 1.00 47.52  ?  320 THR A CA  1 
ATOM   2012 C C   . THR A 1 404 ? 119.257 129.007 112.880 1.00 57.11  ?  320 THR A C   1 
ATOM   2013 O O   . THR A 1 404 ? 119.240 128.567 114.031 1.00 62.63  ?  320 THR A O   1 
ATOM   2014 C CB  . THR A 1 404 ? 118.127 127.540 111.200 1.00 48.94  ?  320 THR A CB  1 
ATOM   2015 O OG1 . THR A 1 404 ? 118.958 127.737 110.052 1.00 60.52  ?  320 THR A OG1 1 
ATOM   2016 C CG2 . THR A 1 404 ? 116.747 127.092 110.754 1.00 56.09  ?  320 THR A CG2 1 
ATOM   2017 N N   . SER A 1 405 ? 120.327 129.627 112.376 1.00 50.60  ?  321 SER A N   1 
ATOM   2018 C CA  . SER A 1 405 ? 121.459 129.940 113.244 1.00 45.81  ?  321 SER A CA  1 
ATOM   2019 C C   . SER A 1 405 ? 121.058 130.938 114.324 1.00 47.24  ?  321 SER A C   1 
ATOM   2020 O O   . SER A 1 405 ? 121.414 130.776 115.501 1.00 57.89  ?  321 SER A O   1 
ATOM   2021 C CB  . SER A 1 405 ? 122.623 130.480 112.416 1.00 48.47  ?  321 SER A CB  1 
ATOM   2022 O OG  . SER A 1 405 ? 123.000 129.559 111.411 1.00 53.65  ?  321 SER A OG  1 
ATOM   2023 N N   . PHE A 1 406 ? 120.299 131.968 113.943 1.00 42.47  ?  322 PHE A N   1 
ATOM   2024 C CA  . PHE A 1 406 ? 119.780 132.911 114.927 1.00 46.19  ?  322 PHE A CA  1 
ATOM   2025 C C   . PHE A 1 406 ? 118.958 132.193 115.989 1.00 57.57  ?  322 PHE A C   1 
ATOM   2026 O O   . PHE A 1 406 ? 119.104 132.454 117.188 1.00 60.76  ?  322 PHE A O   1 
ATOM   2027 C CB  . PHE A 1 406 ? 118.940 133.977 114.228 1.00 43.65  ?  322 PHE A CB  1 
ATOM   2028 C CG  . PHE A 1 406 ? 118.768 135.231 115.025 1.00 50.20  ?  322 PHE A CG  1 
ATOM   2029 C CD1 . PHE A 1 406 ? 119.863 135.990 115.391 1.00 54.74  ?  322 PHE A CD1 1 
ATOM   2030 C CD2 . PHE A 1 406 ? 117.508 135.649 115.413 1.00 52.11  ?  322 PHE A CD2 1 
ATOM   2031 C CE1 . PHE A 1 406 ? 119.705 137.145 116.126 1.00 61.20  ?  322 PHE A CE1 1 
ATOM   2032 C CE2 . PHE A 1 406 ? 117.343 136.801 116.149 1.00 57.77  ?  322 PHE A CE2 1 
ATOM   2033 C CZ  . PHE A 1 406 ? 118.443 137.551 116.506 1.00 62.76  ?  322 PHE A CZ  1 
ATOM   2034 N N   . ALA A 1 407 ? 118.088 131.275 115.563 1.00 53.79  ?  323 ALA A N   1 
ATOM   2035 C CA  . ALA A 1 407 ? 117.280 130.517 116.513 1.00 53.66  ?  323 ALA A CA  1 
ATOM   2036 C C   . ALA A 1 407 ? 118.150 129.637 117.401 1.00 55.16  ?  323 ALA A C   1 
ATOM   2037 O O   . ALA A 1 407 ? 117.880 129.492 118.599 1.00 60.19  ?  323 ALA A O   1 
ATOM   2038 C CB  . ALA A 1 407 ? 116.247 129.675 115.768 1.00 46.95  ?  323 ALA A CB  1 
ATOM   2039 N N   . ALA A 1 408 ? 119.193 129.032 116.829 1.00 52.79  ?  324 ALA A N   1 
ATOM   2040 C CA  . ALA A 1 408 ? 120.119 128.223 117.612 1.00 53.06  ?  324 ALA A CA  1 
ATOM   2041 C C   . ALA A 1 408 ? 120.815 129.051 118.676 1.00 57.13  ?  324 ALA A C   1 
ATOM   2042 O O   . ALA A 1 408 ? 121.204 128.519 119.721 1.00 57.00  ?  324 ALA A O   1 
ATOM   2043 C CB  . ALA A 1 408 ? 121.154 127.570 116.698 1.00 50.31  ?  324 ALA A CB  1 
ATOM   2044 N N   . GLY A 1 409 ? 120.993 130.347 118.425 1.00 61.41  ?  325 GLY A N   1 
ATOM   2045 C CA  . GLY A 1 409 ? 121.543 131.210 119.455 1.00 55.20  ?  325 GLY A CA  1 
ATOM   2046 C C   . GLY A 1 409 ? 120.661 131.318 120.685 1.00 61.74  ?  325 GLY A C   1 
ATOM   2047 O O   . GLY A 1 409 ? 121.150 131.605 121.780 1.00 58.49  ?  325 GLY A O   1 
ATOM   2048 N N   . PHE A 1 410 ? 119.358 131.083 120.530 1.00 67.17  ?  326 PHE A N   1 
ATOM   2049 C CA  . PHE A 1 410 ? 118.391 131.304 121.599 1.00 64.33  ?  326 PHE A CA  1 
ATOM   2050 C C   . PHE A 1 410 ? 117.920 130.025 122.279 1.00 63.20  ?  326 PHE A C   1 
ATOM   2051 O O   . PHE A 1 410 ? 117.184 130.108 123.266 1.00 68.28  ?  326 PHE A O   1 
ATOM   2052 C CB  . PHE A 1 410 ? 117.173 132.059 121.058 1.00 63.04  ?  326 PHE A CB  1 
ATOM   2053 C CG  . PHE A 1 410 ? 117.416 133.520 120.835 1.00 66.19  ?  326 PHE A CG  1 
ATOM   2054 C CD1 . PHE A 1 410 ? 118.061 133.962 119.695 1.00 59.12  ?  326 PHE A CD1 1 
ATOM   2055 C CD2 . PHE A 1 410 ? 117.000 134.454 121.766 1.00 68.69  ?  326 PHE A CD2 1 
ATOM   2056 C CE1 . PHE A 1 410 ? 118.286 135.305 119.486 1.00 62.63  ?  326 PHE A CE1 1 
ATOM   2057 C CE2 . PHE A 1 410 ? 117.223 135.799 121.564 1.00 63.04  ?  326 PHE A CE2 1 
ATOM   2058 C CZ  . PHE A 1 410 ? 117.867 136.225 120.422 1.00 64.12  ?  326 PHE A CZ  1 
ATOM   2059 N N   . VAL A 1 411 ? 118.314 128.851 121.785 1.00 64.10  ?  327 VAL A N   1 
ATOM   2060 C CA  . VAL A 1 411 ? 117.803 127.607 122.349 1.00 64.45  ?  327 VAL A CA  1 
ATOM   2061 C C   . VAL A 1 411 ? 118.425 127.364 123.721 1.00 67.19  ?  327 VAL A C   1 
ATOM   2062 O O   . VAL A 1 411 ? 119.519 127.854 124.034 1.00 69.36  ?  327 VAL A O   1 
ATOM   2063 C CB  . VAL A 1 411 ? 118.063 126.429 121.392 1.00 62.82  ?  327 VAL A CB  1 
ATOM   2064 C CG1 . VAL A 1 411 ? 119.450 125.860 121.602 1.00 63.98  ?  327 VAL A CG1 1 
ATOM   2065 C CG2 . VAL A 1 411 ? 117.007 125.353 121.574 1.00 66.65  ?  327 VAL A CG2 1 
ATOM   2066 N N   . LYS A 1 412 ? 117.713 126.611 124.556 1.00 78.34  ?  328 LYS A N   1 
ATOM   2067 C CA  . LYS A 1 412 ? 118.104 126.356 125.941 1.00 81.78  ?  328 LYS A CA  1 
ATOM   2068 C C   . LYS A 1 412 ? 118.012 124.868 126.259 1.00 85.14  ?  328 LYS A C   1 
ATOM   2069 O O   . LYS A 1 412 ? 117.467 124.454 127.284 1.00 77.67  ?  328 LYS A O   1 
ATOM   2070 C CB  . LYS A 1 412 ? 117.242 127.167 126.903 1.00 77.37  ?  328 LYS A CB  1 
ATOM   2071 C CG  . LYS A 1 412 ? 117.750 128.577 127.154 1.00 78.78  ?  328 LYS A CG  1 
ATOM   2072 C CD  . LYS A 1 412 ? 117.426 129.034 128.566 1.00 81.84  ?  328 LYS A CD  1 
ATOM   2073 C CE  . LYS A 1 412 ? 115.929 129.005 128.825 1.00 80.77  ?  328 LYS A CE  1 
ATOM   2074 N NZ  . LYS A 1 412 ? 115.616 129.045 130.280 1.00 78.70  1  328 LYS A NZ  1 
ATOM   2075 N N   . ILE A 1 413 ? 118.553 124.041 125.373 1.00 82.99  ?  329 ILE A N   1 
ATOM   2076 C CA  . ILE A 1 413 ? 118.519 122.594 125.547 1.00 72.78  ?  329 ILE A CA  1 
ATOM   2077 C C   . ILE A 1 413 ? 119.623 122.173 126.506 1.00 75.37  ?  329 ILE A C   1 
ATOM   2078 O O   . ILE A 1 413 ? 120.755 122.664 126.429 1.00 78.32  ?  329 ILE A O   1 
ATOM   2079 C CB  . ILE A 1 413 ? 118.656 121.889 124.185 1.00 66.85  ?  329 ILE A CB  1 
ATOM   2080 C CG1 . ILE A 1 413 ? 117.284 121.688 123.548 1.00 73.23  ?  329 ILE A CG1 1 
ATOM   2081 C CG2 . ILE A 1 413 ? 119.369 120.555 124.323 1.00 68.73  ?  329 ILE A CG2 1 
ATOM   2082 C CD1 . ILE A 1 413 ? 117.336 120.959 122.225 1.00 73.19  ?  329 ILE A CD1 1 
ATOM   2083 N N   . ARG A 1 414 ? 119.293 121.267 127.425 1.00 75.25  ?  330 ARG A N   1 
ATOM   2084 C CA  . ARG A 1 414 ? 120.293 120.678 128.311 1.00 74.04  ?  330 ARG A CA  1 
ATOM   2085 C C   . ARG A 1 414 ? 121.230 119.805 127.487 1.00 75.75  ?  330 ARG A C   1 
ATOM   2086 O O   . ARG A 1 414 ? 120.855 118.709 127.062 1.00 77.28  ?  330 ARG A O   1 
ATOM   2087 C CB  . ARG A 1 414 ? 119.616 119.869 129.411 1.00 70.95  ?  330 ARG A CB  1 
ATOM   2088 C CG  . ARG A 1 414 ? 120.577 119.291 130.434 1.00 71.57  ?  330 ARG A CG  1 
ATOM   2089 C CD  . ARG A 1 414 ? 119.965 119.283 131.826 1.00 74.17  ?  330 ARG A CD  1 
ATOM   2090 N NE  . ARG A 1 414 ? 120.428 118.155 132.626 1.00 75.01  ?  330 ARG A NE  1 
ATOM   2091 C CZ  . ARG A 1 414 ? 121.641 118.055 133.154 1.00 77.27  ?  330 ARG A CZ  1 
ATOM   2092 N NH1 . ARG A 1 414 ? 122.546 119.006 132.995 1.00 77.15  1  330 ARG A NH1 1 
ATOM   2093 N NH2 . ARG A 1 414 ? 121.952 116.974 133.864 1.00 74.30  ?  330 ARG A NH2 1 
ATOM   2094 N N   . TRP A 1 415 ? 122.452 120.286 127.262 1.00 67.60  ?  331 TRP A N   1 
ATOM   2095 C CA  . TRP A 1 415 ? 123.372 119.636 126.338 1.00 62.64  ?  331 TRP A CA  1 
ATOM   2096 C C   . TRP A 1 415 ? 124.102 118.447 126.942 1.00 64.19  ?  331 TRP A C   1 
ATOM   2097 O O   . TRP A 1 415 ? 124.748 117.700 126.200 1.00 66.08  ?  331 TRP A O   1 
ATOM   2098 C CB  . TRP A 1 415 ? 124.395 120.649 125.827 1.00 63.34  ?  331 TRP A CB  1 
ATOM   2099 C CG  . TRP A 1 415 ? 123.771 121.862 125.229 1.00 64.14  ?  331 TRP A CG  1 
ATOM   2100 C CD1 . TRP A 1 415 ? 123.745 123.117 125.761 1.00 66.04  ?  331 TRP A CD1 1 
ATOM   2101 C CD2 . TRP A 1 415 ? 123.071 121.939 123.984 1.00 64.47  ?  331 TRP A CD2 1 
ATOM   2102 N NE1 . TRP A 1 415 ? 123.076 123.972 124.922 1.00 69.68  ?  331 TRP A NE1 1 
ATOM   2103 C CE2 . TRP A 1 415 ? 122.652 123.272 123.823 1.00 66.92  ?  331 TRP A CE2 1 
ATOM   2104 C CE3 . TRP A 1 415 ? 122.761 121.009 122.988 1.00 69.07  ?  331 TRP A CE3 1 
ATOM   2105 C CZ2 . TRP A 1 415 ? 121.939 123.699 122.709 1.00 65.22  ?  331 TRP A CZ2 1 
ATOM   2106 C CZ3 . TRP A 1 415 ? 122.052 121.434 121.884 1.00 68.93  ?  331 TRP A CZ3 1 
ATOM   2107 C CH2 . TRP A 1 415 ? 121.648 122.767 121.753 1.00 66.88  ?  331 TRP A CH2 1 
ATOM   2108 N N   . ALA A 1 416 ? 124.029 118.252 128.259 1.00 70.02  ?  332 ALA A N   1 
ATOM   2109 C CA  . ALA A 1 416 ? 124.734 117.130 128.867 1.00 72.34  ?  332 ALA A CA  1 
ATOM   2110 C C   . ALA A 1 416 ? 124.086 115.800 128.511 1.00 70.12  ?  332 ALA A C   1 
ATOM   2111 O O   . ALA A 1 416 ? 124.773 114.774 128.449 1.00 69.86  ?  332 ALA A O   1 
ATOM   2112 C CB  . ALA A 1 416 ? 124.794 117.304 130.384 1.00 74.30  ?  332 ALA A CB  1 
ATOM   2113 N N   . ARG A 1 417 ? 122.779 115.795 128.272 1.00 71.50  ?  333 ARG A N   1 
ATOM   2114 C CA  . ARG A 1 417 ? 122.040 114.573 127.995 1.00 72.56  ?  333 ARG A CA  1 
ATOM   2115 C C   . ARG A 1 417 ? 121.339 114.567 126.647 1.00 75.08  ?  333 ARG A C   1 
ATOM   2116 O O   . ARG A 1 417 ? 121.250 113.509 126.021 1.00 74.70  ?  333 ARG A O   1 
ATOM   2117 C CB  . ARG A 1 417 ? 120.992 114.329 129.092 1.00 71.61  ?  333 ARG A CB  1 
ATOM   2118 C CG  . ARG A 1 417 ? 120.446 115.606 129.707 1.00 69.30  ?  333 ARG A CG  1 
ATOM   2119 C CD  . ARG A 1 417 ? 119.586 115.324 130.927 1.00 71.77  ?  333 ARG A CD  1 
ATOM   2120 N NE  . ARG A 1 417 ? 118.538 114.349 130.650 1.00 74.81  ?  333 ARG A NE  1 
ATOM   2121 C CZ  . ARG A 1 417 ? 117.815 113.744 131.581 1.00 79.79  ?  333 ARG A CZ  1 
ATOM   2122 N NH1 . ARG A 1 417 ? 117.993 113.998 132.867 1.00 78.24  1  333 ARG A NH1 1 
ATOM   2123 N NH2 . ARG A 1 417 ? 116.889 112.864 131.214 1.00 77.23  ?  333 ARG A NH2 1 
ATOM   2124 N N   . TRP A 1 418 ? 120.845 115.712 126.182 1.00 66.32  ?  334 TRP A N   1 
ATOM   2125 C CA  . TRP A 1 418 ? 120.060 115.796 124.952 1.00 57.82  ?  334 TRP A CA  1 
ATOM   2126 C C   . TRP A 1 418 ? 120.865 116.373 123.799 1.00 59.84  ?  334 TRP A C   1 
ATOM   2127 O O   . TRP A 1 418 ? 120.339 117.136 122.987 1.00 68.92  ?  334 TRP A O   1 
ATOM   2128 C CB  . TRP A 1 418 ? 118.801 116.620 125.191 1.00 61.26  ?  334 TRP A CB  1 
ATOM   2129 C CG  . TRP A 1 418 ? 117.981 116.120 126.330 1.00 62.08  ?  334 TRP A CG  1 
ATOM   2130 C CD1 . TRP A 1 418 ? 117.830 116.709 127.548 1.00 66.51  ?  334 TRP A CD1 1 
ATOM   2131 C CD2 . TRP A 1 418 ? 117.200 114.921 126.363 1.00 67.11  ?  334 TRP A CD2 1 
ATOM   2132 N NE1 . TRP A 1 418 ? 117.002 115.954 128.340 1.00 70.31  ?  334 TRP A NE1 1 
ATOM   2133 C CE2 . TRP A 1 418 ? 116.601 114.850 127.634 1.00 69.59  ?  334 TRP A CE2 1 
ATOM   2134 C CE3 . TRP A 1 418 ? 116.948 113.902 125.441 1.00 64.34  ?  334 TRP A CE3 1 
ATOM   2135 C CZ2 . TRP A 1 418 ? 115.766 113.801 128.007 1.00 66.66  ?  334 TRP A CZ2 1 
ATOM   2136 C CZ3 . TRP A 1 418 ? 116.119 112.863 125.814 1.00 65.76  ?  334 TRP A CZ3 1 
ATOM   2137 C CH2 . TRP A 1 418 ? 115.538 112.820 127.084 1.00 67.63  ?  334 TRP A CH2 1 
ATOM   2138 N N   . SER A 1 419 ? 122.148 116.035 123.709 1.00 56.85  ?  335 SER A N   1 
ATOM   2139 C CA  . SER A 1 419 ? 122.987 116.466 122.599 1.00 57.06  ?  335 SER A CA  1 
ATOM   2140 C C   . SER A 1 419 ? 123.115 115.395 121.525 1.00 54.97  ?  335 SER A C   1 
ATOM   2141 O O   . SER A 1 419 ? 122.974 115.689 120.336 1.00 59.78  ?  335 SER A O   1 
ATOM   2142 C CB  . SER A 1 419 ? 124.376 116.862 123.112 1.00 63.25  ?  335 SER A CB  1 
ATOM   2143 O OG  . SER A 1 419 ? 125.209 117.281 122.048 1.00 63.63  ?  335 SER A OG  1 
ATOM   2144 N N   . LYS A 1 420 ? 123.385 114.151 121.924 1.00 58.26  ?  336 LYS A N   1 
ATOM   2145 C CA  . LYS A 1 420 ? 123.454 113.062 120.957 1.00 56.81  ?  336 LYS A CA  1 
ATOM   2146 C C   . LYS A 1 420 ? 122.101 112.819 120.304 1.00 60.11  ?  336 LYS A C   1 
ATOM   2147 O O   . LYS A 1 420 ? 122.023 112.547 119.101 1.00 68.77  ?  336 LYS A O   1 
ATOM   2148 C CB  . LYS A 1 420 ? 123.957 111.789 121.637 1.00 60.41  ?  336 LYS A CB  1 
ATOM   2149 C CG  . LYS A 1 420 ? 125.255 111.251 121.065 1.00 61.16  ?  336 LYS A CG  1 
ATOM   2150 C CD  . LYS A 1 420 ? 125.800 110.112 121.909 1.00 59.85  ?  336 LYS A CD  1 
ATOM   2151 C CE  . LYS A 1 420 ? 126.678 110.626 123.036 1.00 60.03  ?  336 LYS A CE  1 
ATOM   2152 N NZ  . LYS A 1 420 ? 127.576 109.565 123.569 1.00 55.67  1  336 LYS A NZ  1 
ATOM   2153 N N   . LEU A 1 421 ? 121.037 112.891 121.111 1.00 57.39  ?  337 LEU A N   1 
ATOM   2154 C CA  . LEU A 1 421 ? 119.660 112.714 120.577 1.00 56.51  ?  337 LEU A CA  1 
ATOM   2155 C C   . LEU A 1 421 ? 119.415 113.773 119.503 1.00 57.85  ?  337 LEU A C   1 
ATOM   2156 O O   . LEU A 1 421 ? 118.986 113.404 118.393 1.00 64.21  ?  337 LEU A O   1 
ATOM   2157 C CB  . LEU A 1 421 ? 118.659 112.898 121.721 1.00 57.08  ?  337 LEU A CB  1 
ATOM   2158 C CG  . LEU A 1 421 ? 118.321 111.649 122.533 1.00 59.49  ?  337 LEU A CG  1 
ATOM   2159 C CD1 . LEU A 1 421 ? 118.122 110.446 121.624 1.00 57.81  ?  337 LEU A CD1 1 
ATOM   2160 C CD2 . LEU A 1 421 ? 119.385 111.372 123.584 1.00 61.43  ?  337 LEU A CD2 1 
ATOM   2161 N N   . LEU A 1 422 ? 119.679 115.039 119.832 1.00 54.61  ?  338 LEU A N   1 
ATOM   2162 C CA  . LEU A 1 422 ? 119.420 116.129 118.896 1.00 53.02  ?  338 LEU A CA  1 
ATOM   2163 C C   . LEU A 1 422 ? 120.156 115.907 117.583 1.00 55.44  ?  338 LEU A C   1 
ATOM   2164 O O   . LEU A 1 422 ? 119.588 116.086 116.498 1.00 60.75  ?  338 LEU A O   1 
ATOM   2165 C CB  . LEU A 1 422 ? 119.834 117.460 119.520 1.00 49.95  ?  338 LEU A CB  1 
ATOM   2166 C CG  . LEU A 1 422 ? 119.364 118.721 118.798 1.00 50.82  ?  338 LEU A CG  1 
ATOM   2167 C CD1 . LEU A 1 422 ? 117.890 118.966 119.053 1.00 61.35  ?  338 LEU A CD1 1 
ATOM   2168 C CD2 . LEU A 1 422 ? 120.194 119.916 119.226 1.00 56.41  ?  338 LEU A CD2 1 
ATOM   2169 N N   . ILE A 1 423 ? 121.428 115.515 117.666 1.00 49.42  ?  339 ILE A N   1 
ATOM   2170 C CA  . ILE A 1 423 ? 122.210 115.252 116.462 1.00 46.31  ?  339 ILE A CA  1 
ATOM   2171 C C   . ILE A 1 423 ? 121.601 114.107 115.672 1.00 50.80  ?  339 ILE A C   1 
ATOM   2172 O O   . ILE A 1 423 ? 121.493 114.174 114.444 1.00 58.96  ?  339 ILE A O   1 
ATOM   2173 C CB  . ILE A 1 423 ? 123.675 114.961 116.828 1.00 46.52  ?  339 ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 423 ? 124.341 116.206 117.399 1.00 49.68  ?  339 ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 423 ? 124.431 114.470 115.620 1.00 48.94  ?  339 ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 423 ? 125.724 115.945 117.921 1.00 54.47  ?  339 ILE A CD1 1 
ATOM   2177 N N   . ALA A 1 424 ? 121.196 113.038 116.359 1.00 51.20  ?  340 ALA A N   1 
ATOM   2178 C CA  . ALA A 1 424 ? 120.598 111.901 115.670 1.00 51.97  ?  340 ALA A CA  1 
ATOM   2179 C C   . ALA A 1 424 ? 119.323 112.309 114.945 1.00 56.54  ?  340 ALA A C   1 
ATOM   2180 O O   . ALA A 1 424 ? 119.117 111.958 113.777 1.00 61.28  ?  340 ALA A O   1 
ATOM   2181 C CB  . ALA A 1 424 ? 120.315 110.777 116.665 1.00 52.03  ?  340 ALA A CB  1 
ATOM   2182 N N   . GLY A 1 425 ? 118.462 113.074 115.618 1.00 56.59  ?  341 GLY A N   1 
ATOM   2183 C CA  . GLY A 1 425 ? 117.218 113.490 114.993 1.00 56.44  ?  341 GLY A CA  1 
ATOM   2184 C C   . GLY A 1 425 ? 117.441 114.391 113.795 1.00 55.80  ?  341 GLY A C   1 
ATOM   2185 O O   . GLY A 1 425 ? 116.835 114.202 112.736 1.00 61.93  ?  341 GLY A O   1 
ATOM   2186 N N   . VAL A 1 426 ? 118.328 115.377 113.940 1.00 46.29  ?  342 VAL A N   1 
ATOM   2187 C CA  . VAL A 1 426 ? 118.566 116.307 112.841 1.00 52.58  ?  342 VAL A CA  1 
ATOM   2188 C C   . VAL A 1 426 ? 119.243 115.598 111.675 1.00 53.05  ?  342 VAL A C   1 
ATOM   2189 O O   . VAL A 1 426 ? 118.950 115.883 110.509 1.00 58.39  ?  342 VAL A O   1 
ATOM   2190 C CB  . VAL A 1 426 ? 119.378 117.520 113.324 1.00 47.49  ?  342 VAL A CB  1 
ATOM   2191 C CG1 . VAL A 1 426 ? 119.670 118.449 112.164 1.00 52.66  ?  342 VAL A CG1 1 
ATOM   2192 C CG2 . VAL A 1 426 ? 118.616 118.263 114.403 1.00 50.85  ?  342 VAL A CG2 1 
ATOM   2193 N N   . THR A 1 427 ? 120.146 114.656 111.958 1.00 51.06  ?  343 THR A N   1 
ATOM   2194 C CA  . THR A 1 427 ? 120.801 113.922 110.881 1.00 51.61  ?  343 THR A CA  1 
ATOM   2195 C C   . THR A 1 427 ? 119.819 113.006 110.160 1.00 58.84  ?  343 THR A C   1 
ATOM   2196 O O   . THR A 1 427 ? 119.893 112.854 108.937 1.00 61.48  ?  343 THR A O   1 
ATOM   2197 C CB  . THR A 1 427 ? 121.984 113.126 111.428 1.00 51.43  ?  343 THR A CB  1 
ATOM   2198 O OG1 . THR A 1 427 ? 122.879 114.013 112.108 1.00 57.41  ?  343 THR A OG1 1 
ATOM   2199 C CG2 . THR A 1 427 ? 122.735 112.451 110.299 1.00 50.53  ?  343 THR A CG2 1 
ATOM   2200 N N   . ALA A 1 428 ? 118.889 112.389 110.894 1.00 60.27  ?  344 ALA A N   1 
ATOM   2201 C CA  . ALA A 1 428 ? 117.847 111.604 110.238 1.00 58.67  ?  344 ALA A CA  1 
ATOM   2202 C C   . ALA A 1 428 ? 116.971 112.486 109.359 1.00 63.86  ?  344 ALA A C   1 
ATOM   2203 O O   . ALA A 1 428 ? 116.603 112.099 108.241 1.00 67.35  ?  344 ALA A O   1 
ATOM   2204 C CB  . ALA A 1 428 ? 117.001 110.876 111.280 1.00 55.40  ?  344 ALA A CB  1 
ATOM   2205 N N   . THR A 1 429 ? 116.627 113.680 109.847 1.00 54.34  ?  345 THR A N   1 
ATOM   2206 C CA  . THR A 1 429 ? 115.853 114.613 109.034 1.00 53.02  ?  345 THR A CA  1 
ATOM   2207 C C   . THR A 1 429 ? 116.615 115.009 107.776 1.00 58.25  ?  345 THR A C   1 
ATOM   2208 O O   . THR A 1 429 ? 116.033 115.100 106.690 1.00 63.89  ?  345 THR A O   1 
ATOM   2209 C CB  . THR A 1 429 ? 115.496 115.851 109.854 1.00 52.95  ?  345 THR A CB  1 
ATOM   2210 O OG1 . THR A 1 429 ? 114.883 115.449 111.085 1.00 59.39  ?  345 THR A OG1 1 
ATOM   2211 C CG2 . THR A 1 429 ? 114.537 116.740 109.083 1.00 58.19  ?  345 THR A CG2 1 
ATOM   2212 N N   . GLN A 1 430 ? 117.921 115.249 107.904 1.00 57.03  ?  346 GLN A N   1 
ATOM   2213 C CA  . GLN A 1 430 ? 118.732 115.602 106.743 1.00 55.76  ?  346 GLN A CA  1 
ATOM   2214 C C   . GLN A 1 430 ? 118.825 114.443 105.759 1.00 59.94  ?  346 GLN A C   1 
ATOM   2215 O O   . GLN A 1 430 ? 118.828 114.657 104.543 1.00 69.12  ?  346 GLN A O   1 
ATOM   2216 C CB  . GLN A 1 430 ? 120.121 116.048 107.191 1.00 47.60  ?  346 GLN A CB  1 
ATOM   2217 C CG  . GLN A 1 430 ? 120.121 117.366 107.942 1.00 51.91  ?  346 GLN A CG  1 
ATOM   2218 C CD  . GLN A 1 430 ? 121.515 117.875 108.229 1.00 56.25  ?  346 GLN A CD  1 
ATOM   2219 O OE1 . GLN A 1 430 ? 121.820 119.044 107.998 1.00 55.39  ?  346 GLN A OE1 1 
ATOM   2220 N NE2 . GLN A 1 430 ? 122.371 117.000 108.739 1.00 62.58  ?  346 GLN A NE2 1 
ATOM   2221 N N   . ALA A 1 431 ? 118.909 113.210 106.262 1.00 56.97  ?  347 ALA A N   1 
ATOM   2222 C CA  . ALA A 1 431 ? 118.881 112.048 105.380 1.00 58.52  ?  347 ALA A CA  1 
ATOM   2223 C C   . ALA A 1 431 ? 117.569 111.976 104.613 1.00 62.30  ?  347 ALA A C   1 
ATOM   2224 O O   . ALA A 1 431 ? 117.558 111.718 103.402 1.00 65.60  ?  347 ALA A O   1 
ATOM   2225 C CB  . ALA A 1 431 ? 119.094 110.769 106.187 1.00 54.48  ?  347 ALA A CB  1 
ATOM   2226 N N   . GLY A 1 432 ? 116.451 112.202 105.303 1.00 56.35  ?  348 GLY A N   1 
ATOM   2227 C CA  . GLY A 1 432 ? 115.166 112.219 104.622 1.00 58.64  ?  348 GLY A CA  1 
ATOM   2228 C C   . GLY A 1 432 ? 115.080 113.311 103.572 1.00 58.08  ?  348 GLY A C   1 
ATOM   2229 O O   . GLY A 1 432 ? 114.552 113.097 102.479 1.00 65.46  ?  348 GLY A O   1 
ATOM   2230 N N   . LEU A 1 433 ? 115.608 114.494 103.887 1.00 55.21  ?  349 LEU A N   1 
ATOM   2231 C CA  . LEU A 1 433 ? 115.573 115.597 102.932 1.00 55.53  ?  349 LEU A CA  1 
ATOM   2232 C C   . LEU A 1 433 ? 116.457 115.316 101.721 1.00 60.75  ?  349 LEU A C   1 
ATOM   2233 O O   . LEU A 1 433 ? 116.100 115.666 100.590 1.00 68.13  ?  349 LEU A O   1 
ATOM   2234 C CB  . LEU A 1 433 ? 115.986 116.895 103.622 1.00 58.44  ?  349 LEU A CB  1 
ATOM   2235 C CG  . LEU A 1 433 ? 115.000 117.368 104.694 1.00 61.69  ?  349 LEU A CG  1 
ATOM   2236 C CD1 . LEU A 1 433 ? 115.661 118.328 105.666 1.00 57.02  ?  349 LEU A CD1 1 
ATOM   2237 C CD2 . LEU A 1 433 ? 113.774 118.000 104.063 1.00 65.69  ?  349 LEU A CD2 1 
ATOM   2238 N N   . VAL A 1 434 ? 117.611 114.682 101.929 1.00 60.77  ?  350 VAL A N   1 
ATOM   2239 C CA  . VAL A 1 434 ? 118.463 114.322 100.800 1.00 59.45  ?  350 VAL A CA  1 
ATOM   2240 C C   . VAL A 1 434 ? 117.787 113.262 99.938  1.00 63.62  ?  350 VAL A C   1 
ATOM   2241 O O   . VAL A 1 434 ? 117.867 113.301 98.704  1.00 70.28  ?  350 VAL A O   1 
ATOM   2242 C CB  . VAL A 1 434 ? 119.848 113.864 101.293 1.00 58.72  ?  350 VAL A CB  1 
ATOM   2243 C CG1 . VAL A 1 434 ? 120.654 113.276 100.150 1.00 62.31  ?  350 VAL A CG1 1 
ATOM   2244 C CG2 . VAL A 1 434 ? 120.595 115.027 101.913 1.00 62.87  ?  350 VAL A CG2 1 
ATOM   2245 N N   . PHE A 1 435 ? 117.102 112.304 100.565 1.00 61.37  ?  351 PHE A N   1 
ATOM   2246 C CA  . PHE A 1 435 ? 116.352 111.331 99.778  1.00 63.22  ?  351 PHE A CA  1 
ATOM   2247 C C   . PHE A 1 435 ? 115.236 112.003 98.990  1.00 70.58  ?  351 PHE A C   1 
ATOM   2248 O O   . PHE A 1 435 ? 114.927 111.594 97.866  1.00 78.66  ?  351 PHE A O   1 
ATOM   2249 C CB  . PHE A 1 435 ? 115.778 110.233 100.666 1.00 66.30  ?  351 PHE A CB  1 
ATOM   2250 C CG  . PHE A 1 435 ? 115.118 109.132 99.892  1.00 68.05  ?  351 PHE A CG  1 
ATOM   2251 C CD1 . PHE A 1 435 ? 115.780 108.521 98.841  1.00 70.85  ?  351 PHE A CD1 1 
ATOM   2252 C CD2 . PHE A 1 435 ? 113.830 108.726 100.194 1.00 69.56  ?  351 PHE A CD2 1 
ATOM   2253 C CE1 . PHE A 1 435 ? 115.177 107.513 98.116  1.00 73.16  ?  351 PHE A CE1 1 
ATOM   2254 C CE2 . PHE A 1 435 ? 113.221 107.718 99.471  1.00 73.74  ?  351 PHE A CE2 1 
ATOM   2255 C CZ  . PHE A 1 435 ? 113.896 107.111 98.431  1.00 74.63  ?  351 PHE A CZ  1 
ATOM   2256 N N   . LEU A 1 436 ? 114.599 113.019 99.575  1.00 71.93  ?  352 LEU A N   1 
ATOM   2257 C CA  . LEU A 1 436 ? 113.609 113.790 98.829  1.00 66.81  ?  352 LEU A CA  1 
ATOM   2258 C C   . LEU A 1 436 ? 114.249 114.486 97.636  1.00 67.51  ?  352 LEU A C   1 
ATOM   2259 O O   . LEU A 1 436 ? 113.672 114.522 96.545  1.00 73.80  ?  352 LEU A O   1 
ATOM   2260 C CB  . LEU A 1 436 ? 112.935 114.813 99.741  1.00 69.17  ?  352 LEU A CB  1 
ATOM   2261 C CG  . LEU A 1 436 ? 111.611 114.397 100.377 1.00 68.93  ?  352 LEU A CG  1 
ATOM   2262 C CD1 . LEU A 1 436 ? 110.961 115.585 101.065 1.00 66.90  ?  352 LEU A CD1 1 
ATOM   2263 C CD2 . LEU A 1 436 ? 110.685 113.797 99.335  1.00 67.10  ?  352 LEU A CD2 1 
ATOM   2264 N N   . LEU A 1 437 ? 115.443 115.048 97.830  1.00 66.40  ?  353 LEU A N   1 
ATOM   2265 C CA  . LEU A 1 437 ? 116.162 115.670 96.723  1.00 65.95  ?  353 LEU A CA  1 
ATOM   2266 C C   . LEU A 1 437 ? 116.485 114.662 95.629  1.00 70.24  ?  353 LEU A C   1 
ATOM   2267 O O   . LEU A 1 437 ? 116.497 115.012 94.444  1.00 72.16  ?  353 LEU A O   1 
ATOM   2268 C CB  . LEU A 1 437 ? 117.452 116.314 97.230  1.00 67.63  ?  353 LEU A CB  1 
ATOM   2269 C CG  . LEU A 1 437 ? 117.385 117.738 97.775  1.00 65.71  ?  353 LEU A CG  1 
ATOM   2270 C CD1 . LEU A 1 437 ? 118.725 118.130 98.367  1.00 63.60  ?  353 LEU A CD1 1 
ATOM   2271 C CD2 . LEU A 1 437 ? 116.986 118.699 96.677  1.00 72.74  ?  353 LEU A CD2 1 
ATOM   2272 N N   . ALA A 1 438 ? 116.754 113.414 96.007  1.00 79.46  ?  354 ALA A N   1 
ATOM   2273 C CA  . ALA A 1 438 ? 117.196 112.415 95.038  1.00 84.34  ?  354 ALA A CA  1 
ATOM   2274 C C   . ALA A 1 438 ? 116.025 111.785 94.290  1.00 83.38  ?  354 ALA A C   1 
ATOM   2275 O O   . ALA A 1 438 ? 115.937 111.876 93.061  1.00 84.42  ?  354 ALA A O   1 
ATOM   2276 C CB  . ALA A 1 438 ? 118.017 111.333 95.743  1.00 82.82  ?  354 ALA A CB  1 
ATOM   2277 N N   . HIS A 1 439 ? 115.113 111.145 95.020  1.00 93.56  ?  355 HIS A N   1 
ATOM   2278 C CA  . HIS A 1 439 ? 114.095 110.297 94.412  1.00 94.40  ?  355 HIS A CA  1 
ATOM   2279 C C   . HIS A 1 439 ? 112.939 111.073 93.797  1.00 96.81  ?  355 HIS A C   1 
ATOM   2280 O O   . HIS A 1 439 ? 112.104 110.464 93.120  1.00 96.32  ?  355 HIS A O   1 
ATOM   2281 C CB  . HIS A 1 439 ? 113.545 109.314 95.449  1.00 94.64  ?  355 HIS A CB  1 
ATOM   2282 C CG  . HIS A 1 439 ? 113.169 107.982 94.878  1.00 100.22 ?  355 HIS A CG  1 
ATOM   2283 N ND1 . HIS A 1 439 ? 111.958 107.751 94.261  1.00 102.89 ?  355 HIS A ND1 1 
ATOM   2284 C CD2 . HIS A 1 439 ? 113.844 106.809 94.831  1.00 97.84  ?  355 HIS A CD2 1 
ATOM   2285 C CE1 . HIS A 1 439 ? 111.904 106.494 93.859  1.00 100.01 ?  355 HIS A CE1 1 
ATOM   2286 N NE2 . HIS A 1 439 ? 113.036 105.900 94.192  1.00 100.78 ?  355 HIS A NE2 1 
ATOM   2287 N N   . THR A 1 440 ? 112.859 112.386 94.010  1.00 100.39 ?  356 THR A N   1 
ATOM   2288 C CA  . THR A 1 440 ? 111.768 113.185 93.454  1.00 102.42 ?  356 THR A CA  1 
ATOM   2289 C C   . THR A 1 440 ? 112.087 113.495 91.994  1.00 102.98 ?  356 THR A C   1 
ATOM   2290 O O   . THR A 1 440 ? 112.560 114.576 91.635  1.00 98.88  ?  356 THR A O   1 
ATOM   2291 C CB  . THR A 1 440 ? 111.556 114.456 94.263  1.00 99.46  ?  356 THR A CB  1 
ATOM   2292 O OG1 . THR A 1 440 ? 111.564 114.138 95.660  1.00 103.51 ?  356 THR A OG1 1 
ATOM   2293 C CG2 . THR A 1 440 ? 110.230 115.094 93.908  1.00 97.89  ?  356 THR A CG2 1 
ATOM   2294 N N   . ARG A 1 441 ? 111.819 112.511 91.139  1.00 118.33 ?  357 ARG A N   1 
ATOM   2295 C CA  . ARG A 1 441 ? 112.072 112.625 89.710  1.00 116.43 ?  357 ARG A CA  1 
ATOM   2296 C C   . ARG A 1 441 ? 110.876 113.159 88.933  1.00 115.56 ?  357 ARG A C   1 
ATOM   2297 O O   . ARG A 1 441 ? 110.975 113.321 87.712  1.00 114.11 ?  357 ARG A O   1 
ATOM   2298 C CB  . ARG A 1 441 ? 112.490 111.264 89.138  1.00 115.74 ?  357 ARG A CB  1 
ATOM   2299 C CG  . ARG A 1 441 ? 111.335 110.304 88.890  1.00 117.24 ?  357 ARG A CG  1 
ATOM   2300 C CD  . ARG A 1 441 ? 110.962 109.536 90.148  1.00 117.73 ?  357 ARG A CD  1 
ATOM   2301 N NE  . ARG A 1 441 ? 109.612 108.990 90.075  1.00 119.22 ?  357 ARG A NE  1 
ATOM   2302 C CZ  . ARG A 1 441 ? 109.000 108.369 91.073  1.00 115.72 ?  357 ARG A CZ  1 
ATOM   2303 N NH1 . ARG A 1 441 ? 109.588 108.199 92.246  1.00 113.50 1  357 ARG A NH1 1 
ATOM   2304 N NH2 . ARG A 1 441 ? 107.766 107.908 90.891  1.00 113.64 ?  357 ARG A NH2 1 
ATOM   2305 N N   . HIS A 1 442 ? 109.762 113.436 89.598  1.00 122.85 ?  358 HIS A N   1 
ATOM   2306 C CA  . HIS A 1 442 ? 108.591 113.974 88.913  1.00 126.06 ?  358 HIS A CA  1 
ATOM   2307 C C   . HIS A 1 442 ? 108.889 115.381 88.413  1.00 125.07 ?  358 HIS A C   1 
ATOM   2308 O O   . HIS A 1 442 ? 109.272 116.244 89.215  1.00 122.87 ?  358 HIS A O   1 
ATOM   2309 C CB  . HIS A 1 442 ? 107.383 113.986 89.847  1.00 126.01 ?  358 HIS A CB  1 
ATOM   2310 C CG  . HIS A 1 442 ? 106.750 112.643 90.036  1.00 126.23 ?  358 HIS A CG  1 
ATOM   2311 N ND1 . HIS A 1 442 ? 106.266 111.893 88.986  1.00 126.61 ?  358 HIS A ND1 1 
ATOM   2312 C CD2 . HIS A 1 442 ? 106.516 111.917 91.155  1.00 123.83 ?  358 HIS A CD2 1 
ATOM   2313 C CE1 . HIS A 1 442 ? 105.765 110.762 89.449  1.00 124.84 ?  358 HIS A CE1 1 
ATOM   2314 N NE2 . HIS A 1 442 ? 105.904 110.752 90.762  1.00 125.50 ?  358 HIS A NE2 1 
ATOM   2315 N N   . PRO A 1 443 ? 108.746 115.656 87.113  1.00 127.83 ?  359 PRO A N   1 
ATOM   2316 C CA  . PRO A 1 443 ? 109.062 117.007 86.616  1.00 127.96 ?  359 PRO A CA  1 
ATOM   2317 C C   . PRO A 1 443 ? 108.206 118.099 87.235  1.00 127.98 ?  359 PRO A C   1 
ATOM   2318 O O   . PRO A 1 443 ? 108.704 119.206 87.476  1.00 127.74 ?  359 PRO A O   1 
ATOM   2319 C CB  . PRO A 1 443 ? 108.829 116.888 85.101  1.00 127.95 ?  359 PRO A CB  1 
ATOM   2320 C CG  . PRO A 1 443 ? 108.842 115.415 84.812  1.00 127.73 ?  359 PRO A CG  1 
ATOM   2321 C CD  . PRO A 1 443 ? 108.304 114.755 86.037  1.00 126.85 ?  359 PRO A CD  1 
ATOM   2322 N N   . SER A 1 444 ? 106.932 117.825 87.500  1.00 123.81 ?  360 SER A N   1 
ATOM   2323 C CA  . SER A 1 444 ? 106.050 118.815 88.119  1.00 122.99 ?  360 SER A CA  1 
ATOM   2324 C C   . SER A 1 444 ? 106.037 118.674 89.638  1.00 124.38 ?  360 SER A C   1 
ATOM   2325 O O   . SER A 1 444 ? 104.987 118.660 90.279  1.00 125.43 ?  360 SER A O   1 
ATOM   2326 C CB  . SER A 1 444 ? 104.645 118.686 87.545  1.00 121.11 ?  360 SER A CB  1 
ATOM   2327 O OG  . SER A 1 444 ? 103.896 117.706 88.246  1.00 120.64 ?  360 SER A OG  1 
ATOM   2328 N N   . SER A 1 445 ? 107.229 118.567 90.224  1.00 109.28 ?  361 SER A N   1 
ATOM   2329 C CA  . SER A 1 445 ? 107.338 118.478 91.675  1.00 107.31 ?  361 SER A CA  1 
ATOM   2330 C C   . SER A 1 445 ? 108.524 119.261 92.227  1.00 105.56 ?  361 SER A C   1 
ATOM   2331 O O   . SER A 1 445 ? 108.895 119.037 93.386  1.00 102.81 ?  361 SER A O   1 
ATOM   2332 C CB  . SER A 1 445 ? 107.442 117.012 92.106  1.00 107.02 ?  361 SER A CB  1 
ATOM   2333 O OG  . SER A 1 445 ? 108.607 116.417 91.566  1.00 107.78 ?  361 SER A OG  1 
ATOM   2334 N N   . ILE A 1 446 ? 109.130 120.164 91.452  1.00 94.62  ?  362 ILE A N   1 
ATOM   2335 C CA  . ILE A 1 446 ? 110.391 120.777 91.850  1.00 91.74  ?  362 ILE A CA  1 
ATOM   2336 C C   . ILE A 1 446 ? 110.241 121.643 93.091  1.00 89.21  ?  362 ILE A C   1 
ATOM   2337 O O   . ILE A 1 446 ? 111.237 121.934 93.763  1.00 93.35  ?  362 ILE A O   1 
ATOM   2338 C CB  . ILE A 1 446 ? 110.980 121.585 90.674  1.00 89.35  ?  362 ILE A CB  1 
ATOM   2339 C CG1 . ILE A 1 446 ? 112.485 121.777 90.864  1.00 90.75  ?  362 ILE A CG1 1 
ATOM   2340 C CG2 . ILE A 1 446 ? 110.279 122.925 90.534  1.00 90.71  ?  362 ILE A CG2 1 
ATOM   2341 C CD1 . ILE A 1 446 ? 113.281 120.496 90.733  1.00 92.28  ?  362 ILE A CD1 1 
ATOM   2342 N N   . TRP A 1 447 ? 109.018 122.063 93.422  1.00 92.70  ?  363 TRP A N   1 
ATOM   2343 C CA  . TRP A 1 447 ? 108.821 122.808 94.660  1.00 95.00  ?  363 TRP A CA  1 
ATOM   2344 C C   . TRP A 1 447 ? 109.173 121.950 95.866  1.00 95.92  ?  363 TRP A C   1 
ATOM   2345 O O   . TRP A 1 447 ? 109.752 122.442 96.841  1.00 94.30  ?  363 TRP A O   1 
ATOM   2346 C CB  . TRP A 1 447 ? 107.381 123.322 94.750  1.00 95.57  ?  363 TRP A CB  1 
ATOM   2347 C CG  . TRP A 1 447 ? 106.375 122.298 95.189  1.00 99.18  ?  363 TRP A CG  1 
ATOM   2348 C CD1 . TRP A 1 447 ? 105.934 121.222 94.475  1.00 97.27  ?  363 TRP A CD1 1 
ATOM   2349 C CD2 . TRP A 1 447 ? 105.676 122.261 96.440  1.00 100.32 ?  363 TRP A CD2 1 
ATOM   2350 N NE1 . TRP A 1 447 ? 105.009 120.515 95.204  1.00 97.97  ?  363 TRP A NE1 1 
ATOM   2351 C CE2 . TRP A 1 447 ? 104.833 121.132 96.415  1.00 100.42 ?  363 TRP A CE2 1 
ATOM   2352 C CE3 . TRP A 1 447 ? 105.683 123.071 97.579  1.00 96.30  ?  363 TRP A CE3 1 
ATOM   2353 C CZ2 . TRP A 1 447 ? 104.006 120.794 97.484  1.00 97.92  ?  363 TRP A CZ2 1 
ATOM   2354 C CZ3 . TRP A 1 447 ? 104.861 122.733 98.641  1.00 95.43  ?  363 TRP A CZ3 1 
ATOM   2355 C CH2 . TRP A 1 447 ? 104.034 121.605 98.585  1.00 96.91  ?  363 TRP A CH2 1 
ATOM   2356 N N   . LEU A 1 448 ? 108.853 120.655 95.808  1.00 92.58  ?  364 LEU A N   1 
ATOM   2357 C CA  . LEU A 1 448 ? 109.213 119.753 96.895  1.00 91.93  ?  364 LEU A CA  1 
ATOM   2358 C C   . LEU A 1 448 ? 110.725 119.595 97.010  1.00 90.79  ?  364 LEU A C   1 
ATOM   2359 O O   . LEU A 1 448 ? 111.265 119.574 98.120  1.00 90.02  ?  364 LEU A O   1 
ATOM   2360 C CB  . LEU A 1 448 ? 108.538 118.397 96.695  1.00 90.00  ?  364 LEU A CB  1 
ATOM   2361 C CG  . LEU A 1 448 ? 108.849 117.324 97.736  1.00 88.02  ?  364 LEU A CG  1 
ATOM   2362 C CD1 . LEU A 1 448 ? 107.920 117.463 98.929  1.00 86.38  ?  364 LEU A CD1 1 
ATOM   2363 C CD2 . LEU A 1 448 ? 108.721 115.945 97.121  1.00 89.93  ?  364 LEU A CD2 1 
ATOM   2364 N N   . CYS A 1 449 ? 111.425 119.483 95.877  1.00 83.85  ?  365 CYS A N   1 
ATOM   2365 C CA  . CYS A 1 449 ? 112.882 119.389 95.917  1.00 81.46  ?  365 CYS A CA  1 
ATOM   2366 C C   . CYS A 1 449 ? 113.503 120.652 96.497  1.00 84.57  ?  365 CYS A C   1 
ATOM   2367 O O   . CYS A 1 449 ? 114.431 120.583 97.315  1.00 90.62  ?  365 CYS A O   1 
ATOM   2368 C CB  . CYS A 1 449 ? 113.433 119.127 94.516  1.00 82.03  ?  365 CYS A CB  1 
ATOM   2369 S SG  . CYS A 1 449 ? 113.520 117.389 94.048  1.00 96.76  ?  365 CYS A SG  1 
ATOM   2370 N N   . TYR A 1 450 ? 113.009 121.819 96.079  1.00 78.67  ?  366 TYR A N   1 
ATOM   2371 C CA  . TYR A 1 450 ? 113.536 123.070 96.610  1.00 74.59  ?  366 TYR A CA  1 
ATOM   2372 C C   . TYR A 1 450 ? 113.271 123.186 98.105  1.00 77.64  ?  366 TYR A C   1 
ATOM   2373 O O   . TYR A 1 450 ? 114.147 123.613 98.864  1.00 77.70  ?  366 TYR A O   1 
ATOM   2374 C CB  . TYR A 1 450 ? 112.930 124.254 95.859  1.00 76.76  ?  366 TYR A CB  1 
ATOM   2375 C CG  . TYR A 1 450 ? 113.415 124.371 94.434  1.00 76.83  ?  366 TYR A CG  1 
ATOM   2376 C CD1 . TYR A 1 450 ? 114.492 123.623 93.985  1.00 81.73  ?  366 TYR A CD1 1 
ATOM   2377 C CD2 . TYR A 1 450 ? 112.792 125.225 93.537  1.00 76.72  ?  366 TYR A CD2 1 
ATOM   2378 C CE1 . TYR A 1 450 ? 114.939 123.722 92.685  1.00 83.43  ?  366 TYR A CE1 1 
ATOM   2379 C CE2 . TYR A 1 450 ? 113.232 125.331 92.235  1.00 78.59  ?  366 TYR A CE2 1 
ATOM   2380 C CZ  . TYR A 1 450 ? 114.307 124.577 91.814  1.00 80.47  ?  366 TYR A CZ  1 
ATOM   2381 O OH  . TYR A 1 450 ? 114.753 124.675 90.517  1.00 81.54  ?  366 TYR A OH  1 
ATOM   2382 N N   . ALA A 1 451 ? 112.071 122.800 98.547  1.00 69.72  ?  367 ALA A N   1 
ATOM   2383 C CA  . ALA A 1 451 ? 111.768 122.826 99.973  1.00 69.85  ?  367 ALA A CA  1 
ATOM   2384 C C   . ALA A 1 451 ? 112.672 121.874 100.744 1.00 70.79  ?  367 ALA A C   1 
ATOM   2385 O O   . ALA A 1 451 ? 113.137 122.201 101.841 1.00 69.23  ?  367 ALA A O   1 
ATOM   2386 C CB  . ALA A 1 451 ? 110.299 122.475 100.203 1.00 69.87  ?  367 ALA A CB  1 
ATOM   2387 N N   . ALA A 1 452 ? 112.929 120.690 100.185 1.00 72.52  ?  368 ALA A N   1 
ATOM   2388 C CA  . ALA A 1 452 ? 113.804 119.730 100.847 1.00 69.97  ?  368 ALA A CA  1 
ATOM   2389 C C   . ALA A 1 452 ? 115.211 120.290 101.000 1.00 67.59  ?  368 ALA A C   1 
ATOM   2390 O O   . ALA A 1 452 ? 115.819 120.186 102.071 1.00 76.91  ?  368 ALA A O   1 
ATOM   2391 C CB  . ALA A 1 452 ? 113.827 118.417 100.066 1.00 66.21  ?  368 ALA A CB  1 
ATOM   2392 N N   . PHE A 1 453 ? 115.743 120.897 99.938  1.00 59.16  ?  369 PHE A N   1 
ATOM   2393 C CA  . PHE A 1 453 ? 117.081 121.476 100.025 1.00 58.26  ?  369 PHE A CA  1 
ATOM   2394 C C   . PHE A 1 453 ? 117.124 122.627 101.022 1.00 61.77  ?  369 PHE A C   1 
ATOM   2395 O O   . PHE A 1 453 ? 118.088 122.760 101.790 1.00 67.06  ?  369 PHE A O   1 
ATOM   2396 C CB  . PHE A 1 453 ? 117.547 121.950 98.652  1.00 58.70  ?  369 PHE A CB  1 
ATOM   2397 C CG  . PHE A 1 453 ? 118.962 122.438 98.637  1.00 57.30  ?  369 PHE A CG  1 
ATOM   2398 C CD1 . PHE A 1 453 ? 119.998 121.600 99.000  1.00 62.09  ?  369 PHE A CD1 1 
ATOM   2399 C CD2 . PHE A 1 453 ? 119.257 123.736 98.265  1.00 63.27  ?  369 PHE A CD2 1 
ATOM   2400 C CE1 . PHE A 1 453 ? 121.302 122.046 98.989  1.00 63.38  ?  369 PHE A CE1 1 
ATOM   2401 C CE2 . PHE A 1 453 ? 120.559 124.186 98.251  1.00 66.41  ?  369 PHE A CE2 1 
ATOM   2402 C CZ  . PHE A 1 453 ? 121.582 123.340 98.613  1.00 65.31  ?  369 PHE A CZ  1 
ATOM   2403 N N   . VAL A 1 454 ? 116.092 123.473 101.019 1.00 64.11  ?  370 VAL A N   1 
ATOM   2404 C CA  . VAL A 1 454 ? 116.056 124.610 101.934 1.00 62.24  ?  370 VAL A CA  1 
ATOM   2405 C C   . VAL A 1 454 ? 116.032 124.126 103.378 1.00 60.03  ?  370 VAL A C   1 
ATOM   2406 O O   . VAL A 1 454 ? 116.772 124.627 104.230 1.00 65.13  ?  370 VAL A O   1 
ATOM   2407 C CB  . VAL A 1 454 ? 114.855 125.517 101.612 1.00 59.83  ?  370 VAL A CB  1 
ATOM   2408 C CG1 . VAL A 1 454 ? 114.644 126.531 102.710 1.00 63.49  ?  370 VAL A CG1 1 
ATOM   2409 C CG2 . VAL A 1 454 ? 115.072 126.226 100.290 1.00 56.93  ?  370 VAL A CG2 1 
ATOM   2410 N N   . LEU A 1 455 ? 115.199 123.122 103.669 1.00 58.13  ?  371 LEU A N   1 
ATOM   2411 C CA  . LEU A 1 455 ? 115.142 122.585 105.025 1.00 60.74  ?  371 LEU A CA  1 
ATOM   2412 C C   . LEU A 1 455 ? 116.437 121.881 105.413 1.00 64.17  ?  371 LEU A C   1 
ATOM   2413 O O   . LEU A 1 455 ? 116.848 121.948 106.575 1.00 68.24  ?  371 LEU A O   1 
ATOM   2414 C CB  . LEU A 1 455 ? 113.957 121.631 105.167 1.00 64.73  ?  371 LEU A CB  1 
ATOM   2415 C CG  . LEU A 1 455 ? 112.567 122.248 105.012 1.00 66.00  ?  371 LEU A CG  1 
ATOM   2416 C CD1 . LEU A 1 455 ? 111.506 121.163 104.934 1.00 66.29  ?  371 LEU A CD1 1 
ATOM   2417 C CD2 . LEU A 1 455 ? 112.276 123.203 106.155 1.00 63.55  ?  371 LEU A CD2 1 
ATOM   2418 N N   . PHE A 1 456 ? 117.090 121.203 104.467 1.00 57.49  ?  372 PHE A N   1 
ATOM   2419 C CA  . PHE A 1 456 ? 118.361 120.548 104.758 1.00 47.26  ?  372 PHE A CA  1 
ATOM   2420 C C   . PHE A 1 456 ? 119.424 121.568 105.151 1.00 57.66  ?  372 PHE A C   1 
ATOM   2421 O O   . PHE A 1 456 ? 120.113 121.414 106.173 1.00 69.23  ?  372 PHE A O   1 
ATOM   2422 C CB  . PHE A 1 456 ? 118.797 119.733 103.538 1.00 47.03  ?  372 PHE A CB  1 
ATOM   2423 C CG  . PHE A 1 456 ? 120.221 119.267 103.584 1.00 53.32  ?  372 PHE A CG  1 
ATOM   2424 C CD1 . PHE A 1 456 ? 120.566 118.122 104.276 1.00 63.05  ?  372 PHE A CD1 1 
ATOM   2425 C CD2 . PHE A 1 456 ? 121.211 119.959 102.911 1.00 55.40  ?  372 PHE A CD2 1 
ATOM   2426 C CE1 . PHE A 1 456 ? 121.873 117.687 104.313 1.00 58.86  ?  372 PHE A CE1 1 
ATOM   2427 C CE2 . PHE A 1 456 ? 122.518 119.527 102.945 1.00 58.16  ?  372 PHE A CE2 1 
ATOM   2428 C CZ  . PHE A 1 456 ? 122.849 118.390 103.648 1.00 57.23  ?  372 PHE A CZ  1 
ATOM   2429 N N   . ARG A 1 457 ? 119.558 122.632 104.357 1.00 54.93  ?  373 ARG A N   1 
ATOM   2430 C CA  . ARG A 1 457 ? 120.526 123.671 104.690 1.00 45.16  ?  373 ARG A CA  1 
ATOM   2431 C C   . ARG A 1 457 ? 120.151 124.373 105.988 1.00 53.61  ?  373 ARG A C   1 
ATOM   2432 O O   . ARG A 1 457 ? 121.028 124.735 106.781 1.00 67.13  ?  373 ARG A O   1 
ATOM   2433 C CB  . ARG A 1 457 ? 120.649 124.671 103.544 1.00 53.06  ?  373 ARG A CB  1 
ATOM   2434 C CG  . ARG A 1 457 ? 121.470 124.147 102.381 1.00 67.72  ?  373 ARG A CG  1 
ATOM   2435 C CD  . ARG A 1 457 ? 122.013 125.269 101.517 1.00 66.26  ?  373 ARG A CD  1 
ATOM   2436 N NE  . ARG A 1 457 ? 123.014 126.067 102.213 1.00 64.67  ?  373 ARG A NE  1 
ATOM   2437 C CZ  . ARG A 1 457 ? 123.757 127.000 101.635 1.00 65.80  ?  373 ARG A CZ  1 
ATOM   2438 N NH1 . ARG A 1 457 ? 123.641 127.275 100.347 1.00 57.32  1  373 ARG A NH1 1 
ATOM   2439 N NH2 . ARG A 1 457 ? 124.639 127.672 102.368 1.00 70.12  ?  373 ARG A NH2 1 
ATOM   2440 N N   . GLY A 1 458 ? 118.853 124.566 106.230 1.00 53.69  ?  374 GLY A N   1 
ATOM   2441 C CA  . GLY A 1 458 ? 118.427 125.162 107.484 1.00 48.03  ?  374 GLY A CA  1 
ATOM   2442 C C   . GLY A 1 458 ? 118.804 124.321 108.687 1.00 51.38  ?  374 GLY A C   1 
ATOM   2443 O O   . GLY A 1 458 ? 119.271 124.845 109.697 1.00 54.91  ?  374 GLY A O   1 
ATOM   2444 N N   . SER A 1 459 ? 118.618 123.003 108.592 1.00 50.37  ?  375 SER A N   1 
ATOM   2445 C CA  . SER A 1 459 ? 119.003 122.120 109.688 1.00 48.27  ?  375 SER A CA  1 
ATOM   2446 C C   . SER A 1 459 ? 120.507 122.156 109.928 1.00 53.01  ?  375 SER A C   1 
ATOM   2447 O O   . SER A 1 459 ? 120.961 122.226 111.079 1.00 59.85  ?  375 SER A O   1 
ATOM   2448 C CB  . SER A 1 459 ? 118.546 120.692 109.398 1.00 48.44  ?  375 SER A CB  1 
ATOM   2449 O OG  . SER A 1 459 ? 117.245 120.675 108.841 1.00 60.00  ?  375 SER A OG  1 
ATOM   2450 N N   . TYR A 1 460 ? 121.301 122.112 108.854 1.00 47.65  ?  376 TYR A N   1 
ATOM   2451 C CA  . TYR A 1 460 ? 122.750 122.127 109.035 1.00 44.60  ?  376 TYR A CA  1 
ATOM   2452 C C   . TYR A 1 460 ? 123.216 123.435 109.666 1.00 45.70  ?  376 TYR A C   1 
ATOM   2453 O O   . TYR A 1 460 ? 124.025 123.434 110.604 1.00 61.67  ?  376 TYR A O   1 
ATOM   2454 C CB  . TYR A 1 460 ? 123.463 121.893 107.707 1.00 53.21  ?  376 TYR A CB  1 
ATOM   2455 C CG  . TYR A 1 460 ? 124.966 121.963 107.843 1.00 57.85  ?  376 TYR A CG  1 
ATOM   2456 C CD1 . TYR A 1 460 ? 125.681 120.911 108.395 1.00 51.68  ?  376 TYR A CD1 1 
ATOM   2457 C CD2 . TYR A 1 460 ? 125.666 123.090 107.441 1.00 59.38  ?  376 TYR A CD2 1 
ATOM   2458 C CE1 . TYR A 1 460 ? 127.051 120.975 108.529 1.00 51.74  ?  376 TYR A CE1 1 
ATOM   2459 C CE2 . TYR A 1 460 ? 127.034 123.163 107.572 1.00 55.40  ?  376 TYR A CE2 1 
ATOM   2460 C CZ  . TYR A 1 460 ? 127.722 122.104 108.115 1.00 56.10  ?  376 TYR A CZ  1 
ATOM   2461 O OH  . TYR A 1 460 ? 129.088 122.179 108.245 1.00 61.67  ?  376 TYR A OH  1 
ATOM   2462 N N   . GLN A 1 461 ? 122.726 124.567 109.156 1.00 43.95  ?  377 GLN A N   1 
ATOM   2463 C CA  . GLN A 1 461 ? 123.116 125.853 109.717 1.00 46.93  ?  377 GLN A CA  1 
ATOM   2464 C C   . GLN A 1 461 ? 122.486 126.112 111.076 1.00 51.07  ?  377 GLN A C   1 
ATOM   2465 O O   . GLN A 1 461 ? 122.907 127.046 111.764 1.00 58.32  ?  377 GLN A O   1 
ATOM   2466 C CB  . GLN A 1 461 ? 122.754 126.984 108.756 1.00 47.78  ?  377 GLN A CB  1 
ATOM   2467 C CG  . GLN A 1 461 ? 123.270 126.797 107.340 1.00 47.53  ?  377 GLN A CG  1 
ATOM   2468 C CD  . GLN A 1 461 ? 124.777 126.838 107.257 1.00 49.67  ?  377 GLN A CD  1 
ATOM   2469 O OE1 . GLN A 1 461 ? 125.441 127.427 108.107 1.00 51.43  ?  377 GLN A OE1 1 
ATOM   2470 N NE2 . GLN A 1 461 ? 125.329 126.213 106.226 1.00 55.35  ?  377 GLN A NE2 1 
ATOM   2471 N N   . PHE A 1 462 ? 121.470 125.340 111.460 1.00 44.52  ?  378 PHE A N   1 
ATOM   2472 C CA  . PHE A 1 462 ? 120.992 125.373 112.836 1.00 46.18  ?  378 PHE A CA  1 
ATOM   2473 C C   . PHE A 1 462 ? 121.953 124.642 113.758 1.00 51.02  ?  378 PHE A C   1 
ATOM   2474 O O   . PHE A 1 462 ? 122.248 125.114 114.861 1.00 59.90  ?  378 PHE A O   1 
ATOM   2475 C CB  . PHE A 1 462 ? 119.598 124.752 112.917 1.00 50.61  ?  378 PHE A CB  1 
ATOM   2476 C CG  . PHE A 1 462 ? 119.201 124.323 114.298 1.00 50.70  ?  378 PHE A CG  1 
ATOM   2477 C CD1 . PHE A 1 462 ? 118.977 125.258 115.291 1.00 54.10  ?  378 PHE A CD1 1 
ATOM   2478 C CD2 . PHE A 1 462 ? 119.050 122.983 114.603 1.00 48.57  ?  378 PHE A CD2 1 
ATOM   2479 C CE1 . PHE A 1 462 ? 118.612 124.866 116.562 1.00 50.90  ?  378 PHE A CE1 1 
ATOM   2480 C CE2 . PHE A 1 462 ? 118.686 122.585 115.873 1.00 49.81  ?  378 PHE A CE2 1 
ATOM   2481 C CZ  . PHE A 1 462 ? 118.466 123.528 116.853 1.00 48.59  ?  378 PHE A CZ  1 
ATOM   2482 N N   . LEU A 1 463 ? 122.452 123.488 113.319 1.00 50.81  ?  379 LEU A N   1 
ATOM   2483 C CA  . LEU A 1 463 ? 123.316 122.692 114.182 1.00 49.15  ?  379 LEU A CA  1 
ATOM   2484 C C   . LEU A 1 463 ? 124.731 123.252 114.284 1.00 48.41  ?  379 LEU A C   1 
ATOM   2485 O O   . LEU A 1 463 ? 125.416 122.992 115.278 1.00 53.26  ?  379 LEU A O   1 
ATOM   2486 C CB  . LEU A 1 463 ? 123.365 121.247 113.692 1.00 43.86  ?  379 LEU A CB  1 
ATOM   2487 C CG  . LEU A 1 463 ? 122.424 120.272 114.394 1.00 41.28  ?  379 LEU A CG  1 
ATOM   2488 C CD1 . LEU A 1 463 ? 122.729 118.858 113.957 1.00 48.91  ?  379 LEU A CD1 1 
ATOM   2489 C CD2 . LEU A 1 463 ? 122.547 120.407 115.898 1.00 49.85  ?  379 LEU A CD2 1 
ATOM   2490 N N   . VAL A 1 464 ? 125.193 124.002 113.280 1.00 46.89  ?  380 VAL A N   1 
ATOM   2491 C CA  . VAL A 1 464 ? 126.581 124.480 113.295 1.00 46.12  ?  380 VAL A CA  1 
ATOM   2492 C C   . VAL A 1 464 ? 126.891 125.389 114.485 1.00 56.54  ?  380 VAL A C   1 
ATOM   2493 O O   . VAL A 1 464 ? 127.904 125.151 115.163 1.00 64.20  ?  380 VAL A O   1 
ATOM   2494 C CB  . VAL A 1 464 ? 126.932 125.132 111.944 1.00 46.13  ?  380 VAL A CB  1 
ATOM   2495 C CG1 . VAL A 1 464 ? 128.171 125.995 112.082 1.00 48.83  ?  380 VAL A CG1 1 
ATOM   2496 C CG2 . VAL A 1 464 ? 127.155 124.069 110.901 1.00 52.72  ?  380 VAL A CG2 1 
ATOM   2497 N N   . PRO A 1 465 ? 126.107 126.441 114.777 1.00 52.74  ?  381 PRO A N   1 
ATOM   2498 C CA  . PRO A 1 465 ? 126.452 127.278 115.943 1.00 42.88  ?  381 PRO A CA  1 
ATOM   2499 C C   . PRO A 1 465 ? 126.484 126.505 117.246 1.00 53.65  ?  381 PRO A C   1 
ATOM   2500 O O   . PRO A 1 465 ? 127.336 126.771 118.102 1.00 60.86  ?  381 PRO A O   1 
ATOM   2501 C CB  . PRO A 1 465 ? 125.359 128.356 115.966 1.00 46.25  ?  381 PRO A CB  1 
ATOM   2502 C CG  . PRO A 1 465 ? 124.510 128.142 114.807 1.00 53.68  ?  381 PRO A CG  1 
ATOM   2503 C CD  . PRO A 1 465 ? 124.990 126.999 113.998 1.00 55.86  ?  381 PRO A CD  1 
ATOM   2504 N N   . ILE A 1 466 ? 125.572 125.546 117.416 1.00 52.51  ?  382 ILE A N   1 
ATOM   2505 C CA  . ILE A 1 466 ? 125.586 124.707 118.609 1.00 50.62  ?  382 ILE A CA  1 
ATOM   2506 C C   . ILE A 1 466 ? 126.877 123.907 118.672 1.00 50.93  ?  382 ILE A C   1 
ATOM   2507 O O   . ILE A 1 466 ? 127.492 123.773 119.736 1.00 62.90  ?  382 ILE A O   1 
ATOM   2508 C CB  . ILE A 1 466 ? 124.352 123.790 118.630 1.00 51.00  ?  382 ILE A CB  1 
ATOM   2509 C CG1 . ILE A 1 466 ? 123.081 124.606 118.856 1.00 55.39  ?  382 ILE A CG1 1 
ATOM   2510 C CG2 . ILE A 1 466 ? 124.501 122.726 119.696 1.00 58.01  ?  382 ILE A CG2 1 
ATOM   2511 C CD1 . ILE A 1 466 ? 121.914 124.146 118.017 1.00 56.68  ?  382 ILE A CD1 1 
ATOM   2512 N N   . ALA A 1 467 ? 127.307 123.363 117.533 1.00 33.49  ?  383 ALA A N   1 
ATOM   2513 C CA  . ALA A 1 467 ? 128.547 122.598 117.500 1.00 38.13  ?  383 ALA A CA  1 
ATOM   2514 C C   . ALA A 1 467 ? 129.733 123.459 117.908 1.00 49.19  ?  383 ALA A C   1 
ATOM   2515 O O   . ALA A 1 467 ? 130.546 123.055 118.744 1.00 60.36  ?  383 ALA A O   1 
ATOM   2516 C CB  . ALA A 1 467 ? 128.766 122.015 116.106 1.00 47.69  ?  383 ALA A CB  1 
ATOM   2517 N N   . THR A 1 468 ? 129.841 124.660 117.333 1.00 52.27  ?  384 THR A N   1 
ATOM   2518 C CA  . THR A 1 468 ? 130.966 125.529 117.667 1.00 44.41  ?  384 THR A CA  1 
ATOM   2519 C C   . THR A 1 468 ? 130.937 125.935 119.135 1.00 45.17  ?  384 THR A C   1 
ATOM   2520 O O   . THR A 1 468 ? 131.972 125.918 119.813 1.00 49.81  ?  384 THR A O   1 
ATOM   2521 C CB  . THR A 1 468 ? 130.965 126.768 116.773 1.00 41.91  ?  384 THR A CB  1 
ATOM   2522 O OG1 . THR A 1 468 ? 129.799 127.553 117.045 1.00 50.25  ?  384 THR A OG1 1 
ATOM   2523 C CG2 . THR A 1 468 ? 130.967 126.369 115.311 1.00 50.40  ?  384 THR A CG2 1 
ATOM   2524 N N   . PHE A 1 469 ? 129.758 126.299 119.647 1.00 48.82  ?  385 PHE A N   1 
ATOM   2525 C CA  . PHE A 1 469 ? 129.654 126.735 121.034 1.00 44.20  ?  385 PHE A CA  1 
ATOM   2526 C C   . PHE A 1 469 ? 129.999 125.608 121.998 1.00 53.89  ?  385 PHE A C   1 
ATOM   2527 O O   . PHE A 1 469 ? 130.714 125.824 122.984 1.00 66.64  ?  385 PHE A O   1 
ATOM   2528 C CB  . PHE A 1 469 ? 128.248 127.278 121.295 1.00 46.03  ?  385 PHE A CB  1 
ATOM   2529 C CG  . PHE A 1 469 ? 127.676 126.897 122.629 1.00 59.02  ?  385 PHE A CG  1 
ATOM   2530 C CD1 . PHE A 1 469 ? 128.155 127.464 123.799 1.00 62.84  ?  385 PHE A CD1 1 
ATOM   2531 C CD2 . PHE A 1 469 ? 126.636 125.989 122.710 1.00 58.68  ?  385 PHE A CD2 1 
ATOM   2532 C CE1 . PHE A 1 469 ? 127.622 127.116 125.024 1.00 57.53  ?  385 PHE A CE1 1 
ATOM   2533 C CE2 . PHE A 1 469 ? 126.097 125.640 123.930 1.00 61.78  ?  385 PHE A CE2 1 
ATOM   2534 C CZ  . PHE A 1 469 ? 126.590 126.203 125.089 1.00 61.23  ?  385 PHE A CZ  1 
ATOM   2535 N N   . GLN A 1 470 ? 129.513 124.394 121.730 1.00 52.06  ?  386 GLN A N   1 
ATOM   2536 C CA  . GLN A 1 470 ? 129.808 123.280 122.622 1.00 47.88  ?  386 GLN A CA  1 
ATOM   2537 C C   . GLN A 1 470 ? 131.253 122.823 122.495 1.00 51.60  ?  386 GLN A C   1 
ATOM   2538 O O   . GLN A 1 470 ? 131.823 122.307 123.462 1.00 61.90  ?  386 GLN A O   1 
ATOM   2539 C CB  . GLN A 1 470 ? 128.853 122.120 122.351 1.00 50.36  ?  386 GLN A CB  1 
ATOM   2540 C CG  . GLN A 1 470 ? 127.541 122.227 123.101 1.00 52.03  ?  386 GLN A CG  1 
ATOM   2541 C CD  . GLN A 1 470 ? 127.731 122.201 124.604 1.00 64.10  ?  386 GLN A CD  1 
ATOM   2542 O OE1 . GLN A 1 470 ? 128.688 121.619 125.112 1.00 62.52  ?  386 GLN A OE1 1 
ATOM   2543 N NE2 . GLN A 1 470 ? 126.822 122.844 125.324 1.00 69.05  ?  386 GLN A NE2 1 
ATOM   2544 N N   . ILE A 1 471 ? 131.861 122.991 121.321 1.00 43.99  ?  387 ILE A N   1 
ATOM   2545 C CA  . ILE A 1 471 ? 133.278 122.683 121.183 1.00 47.27  ?  387 ILE A CA  1 
ATOM   2546 C C   . ILE A 1 471 ? 134.116 123.665 121.987 1.00 60.54  ?  387 ILE A C   1 
ATOM   2547 O O   . ILE A 1 471 ? 135.037 123.269 122.710 1.00 70.55  ?  387 ILE A O   1 
ATOM   2548 C CB  . ILE A 1 471 ? 133.679 122.678 119.697 1.00 44.00  ?  387 ILE A CB  1 
ATOM   2549 C CG1 . ILE A 1 471 ? 133.235 121.380 119.027 1.00 52.06  ?  387 ILE A CG1 1 
ATOM   2550 C CG2 . ILE A 1 471 ? 135.174 122.870 119.542 1.00 44.84  ?  387 ILE A CG2 1 
ATOM   2551 C CD1 . ILE A 1 471 ? 133.663 121.271 117.589 1.00 55.05  ?  387 ILE A CD1 1 
ATOM   2552 N N   . ALA A 1 472 ? 133.807 124.959 121.885 1.00 55.80  ?  388 ALA A N   1 
ATOM   2553 C CA  . ALA A 1 472 ? 134.600 125.961 122.590 1.00 48.00  ?  388 ALA A CA  1 
ATOM   2554 C C   . ALA A 1 472 ? 134.402 125.884 124.096 1.00 56.90  ?  388 ALA A C   1 
ATOM   2555 O O   . ALA A 1 472 ? 135.364 126.022 124.859 1.00 68.00  ?  388 ALA A O   1 
ATOM   2556 C CB  . ALA A 1 472 ? 134.255 127.354 122.089 1.00 48.85  ?  388 ALA A CB  1 
ATOM   2557 N N   . SER A 1 473 ? 133.164 125.673 124.548 1.00 54.35  ?  389 SER A N   1 
ATOM   2558 C CA  . SER A 1 473 ? 132.903 125.643 125.982 1.00 52.41  ?  389 SER A CA  1 
ATOM   2559 C C   . SER A 1 473 ? 133.605 124.484 126.675 1.00 58.42  ?  389 SER A C   1 
ATOM   2560 O O   . SER A 1 473 ? 133.751 124.509 127.901 1.00 59.18  ?  389 SER A O   1 
ATOM   2561 C CB  . SER A 1 473 ? 131.399 125.575 126.241 1.00 53.40  ?  389 SER A CB  1 
ATOM   2562 O OG  . SER A 1 473 ? 130.960 124.233 126.304 1.00 61.49  ?  389 SER A OG  1 
ATOM   2563 N N   . SER A 1 474 ? 134.042 123.475 125.925 1.00 62.20  ?  390 SER A N   1 
ATOM   2564 C CA  . SER A 1 474 ? 134.781 122.336 126.456 1.00 67.85  ?  390 SER A CA  1 
ATOM   2565 C C   . SER A 1 474 ? 136.231 122.346 125.980 1.00 67.13  ?  390 SER A C   1 
ATOM   2566 O O   . SER A 1 474 ? 136.798 121.305 125.647 1.00 75.24  ?  390 SER A O   1 
ATOM   2567 C CB  . SER A 1 474 ? 134.106 121.024 126.065 1.00 64.40  ?  390 SER A CB  1 
ATOM   2568 O OG  . SER A 1 474 ? 132.710 121.077 126.298 1.00 60.33  ?  390 SER A OG  1 
ATOM   2569 N N   . LEU A 1 475 ? 136.849 123.524 125.942 1.00 59.11  ?  391 LEU A N   1 
ATOM   2570 C CA  . LEU A 1 475 ? 138.174 123.676 125.354 1.00 61.66  ?  391 LEU A CA  1 
ATOM   2571 C C   . LEU A 1 475 ? 139.023 124.563 126.258 1.00 72.16  ?  391 LEU A C   1 
ATOM   2572 O O   . LEU A 1 475 ? 138.640 124.889 127.386 1.00 75.22  ?  391 LEU A O   1 
ATOM   2573 C CB  . LEU A 1 475 ? 138.069 124.250 123.936 1.00 58.29  ?  391 LEU A CB  1 
ATOM   2574 C CG  . LEU A 1 475 ? 138.279 123.267 122.790 1.00 60.26  ?  391 LEU A CG  1 
ATOM   2575 C CD1 . LEU A 1 475 ? 138.044 123.966 121.470 1.00 62.82  ?  391 LEU A CD1 1 
ATOM   2576 C CD2 . LEU A 1 475 ? 139.675 122.681 122.848 1.00 64.05  ?  391 LEU A CD2 1 
ATOM   2577 N N   . SER A 1 476 ? 140.191 124.947 125.749 1.00 89.26  ?  392 SER A N   1 
ATOM   2578 C CA  . SER A 1 476 ? 141.104 125.849 126.429 1.00 85.97  ?  392 SER A CA  1 
ATOM   2579 C C   . SER A 1 476 ? 141.038 127.231 125.782 1.00 83.57  ?  392 SER A C   1 
ATOM   2580 O O   . SER A 1 476 ? 140.238 127.488 124.879 1.00 80.98  ?  392 SER A O   1 
ATOM   2581 C CB  . SER A 1 476 ? 142.528 125.292 126.400 1.00 81.90  ?  392 SER A CB  1 
ATOM   2582 O OG  . SER A 1 476 ? 142.552 123.931 126.792 1.00 86.23  ?  392 SER A OG  1 
ATOM   2583 N N   . LYS A 1 477 ? 141.897 128.135 126.253 1.00 95.11  ?  393 LYS A N   1 
ATOM   2584 C CA  . LYS A 1 477 ? 141.892 129.498 125.731 1.00 97.02  ?  393 LYS A CA  1 
ATOM   2585 C C   . LYS A 1 477 ? 142.459 129.546 124.317 1.00 96.23  ?  393 LYS A C   1 
ATOM   2586 O O   . LYS A 1 477 ? 141.757 129.903 123.364 1.00 92.84  ?  393 LYS A O   1 
ATOM   2587 C CB  . LYS A 1 477 ? 142.682 130.419 126.665 1.00 93.60  ?  393 LYS A CB  1 
ATOM   2588 C CG  . LYS A 1 477 ? 142.083 130.565 128.058 1.00 95.75  ?  393 LYS A CG  1 
ATOM   2589 C CD  . LYS A 1 477 ? 140.577 130.780 128.006 1.00 96.33  ?  393 LYS A CD  1 
ATOM   2590 C CE  . LYS A 1 477 ? 140.225 132.152 127.456 1.00 93.19  ?  393 LYS A CE  1 
ATOM   2591 N NZ  . LYS A 1 477 ? 138.820 132.200 126.968 1.00 93.53  1  393 LYS A NZ  1 
ATOM   2592 N N   . GLU A 1 478 ? 143.729 129.188 124.163 1.00 95.31  ?  394 GLU A N   1 
ATOM   2593 C CA  . GLU A 1 478 ? 144.390 129.207 122.859 1.00 93.57  ?  394 GLU A CA  1 
ATOM   2594 C C   . GLU A 1 478 ? 144.338 127.818 122.223 1.00 93.04  ?  394 GLU A C   1 
ATOM   2595 O O   . GLU A 1 478 ? 145.355 127.191 121.937 1.00 93.05  ?  394 GLU A O   1 
ATOM   2596 C CB  . GLU A 1 478 ? 145.827 129.707 123.010 1.00 93.90  ?  394 GLU A CB  1 
ATOM   2597 C CG  . GLU A 1 478 ? 146.604 129.872 121.707 1.00 95.13  ?  394 GLU A CG  1 
ATOM   2598 C CD  . GLU A 1 478 ? 148.076 130.171 121.933 1.00 96.23  ?  394 GLU A CD  1 
ATOM   2599 O OE1 . GLU A 1 478 ? 148.416 130.751 122.985 1.00 96.78  ?  394 GLU A OE1 1 
ATOM   2600 O OE2 . GLU A 1 478 ? 148.895 129.826 121.057 1.00 89.97  -1 394 GLU A OE2 1 
ATOM   2601 N N   . LEU A 1 479 ? 143.113 127.315 122.042 1.00 82.16  ?  395 LEU A N   1 
ATOM   2602 C CA  . LEU A 1 479 ? 142.892 126.067 121.314 1.00 80.15  ?  395 LEU A CA  1 
ATOM   2603 C C   . LEU A 1 479 ? 141.760 126.120 120.297 1.00 77.86  ?  395 LEU A C   1 
ATOM   2604 O O   . LEU A 1 479 ? 141.827 125.382 119.307 1.00 81.45  ?  395 LEU A O   1 
ATOM   2605 C CB  . LEU A 1 479 ? 142.601 124.912 122.288 1.00 84.32  ?  395 LEU A CB  1 
ATOM   2606 C CG  . LEU A 1 479 ? 143.654 123.882 122.719 1.00 87.21  ?  395 LEU A CG  1 
ATOM   2607 C CD1 . LEU A 1 479 ? 143.925 122.885 121.598 1.00 83.90  ?  395 LEU A CD1 1 
ATOM   2608 C CD2 . LEU A 1 479 ? 144.948 124.498 123.218 1.00 86.32  ?  395 LEU A CD2 1 
ATOM   2609 N N   . CYS A 1 480 ? 140.758 126.990 120.468 1.00 69.36  ?  396 CYS A N   1 
ATOM   2610 C CA  . CYS A 1 480 ? 139.497 126.833 119.744 1.00 68.25  ?  396 CYS A CA  1 
ATOM   2611 C C   . CYS A 1 480 ? 139.723 126.796 118.242 1.00 66.76  ?  396 CYS A C   1 
ATOM   2612 O O   . CYS A 1 480 ? 139.339 125.829 117.570 1.00 72.37  ?  396 CYS A O   1 
ATOM   2613 C CB  . CYS A 1 480 ? 138.535 127.963 120.111 1.00 72.23  ?  396 CYS A CB  1 
ATOM   2614 S SG  . CYS A 1 480 ? 138.710 128.581 121.797 1.00 101.70 ?  396 CYS A SG  1 
ATOM   2615 N N   . ALA A 1 481 ? 140.405 127.812 117.709 1.00 63.97  ?  397 ALA A N   1 
ATOM   2616 C CA  . ALA A 1 481 ? 140.667 127.870 116.277 1.00 61.69  ?  397 ALA A CA  1 
ATOM   2617 C C   . ALA A 1 481 ? 141.282 126.571 115.790 1.00 63.51  ?  397 ALA A C   1 
ATOM   2618 O O   . ALA A 1 481 ? 140.781 125.948 114.844 1.00 69.10  ?  397 ALA A O   1 
ATOM   2619 C CB  . ALA A 1 481 ? 141.587 129.047 115.963 1.00 63.02  ?  397 ALA A CB  1 
ATOM   2620 N N   . LEU A 1 482 ? 142.326 126.108 116.483 1.00 60.68  ?  398 LEU A N   1 
ATOM   2621 C CA  . LEU A 1 482 ? 143.001 124.879 116.091 1.00 60.67  ?  398 LEU A CA  1 
ATOM   2622 C C   . LEU A 1 482 ? 141.993 123.757 115.909 1.00 65.94  ?  398 LEU A C   1 
ATOM   2623 O O   . LEU A 1 482 ? 141.900 123.155 114.830 1.00 68.13  ?  398 LEU A O   1 
ATOM   2624 C CB  . LEU A 1 482 ? 144.046 124.508 117.146 1.00 63.08  ?  398 LEU A CB  1 
ATOM   2625 C CG  . LEU A 1 482 ? 144.779 123.173 117.010 1.00 65.35  ?  398 LEU A CG  1 
ATOM   2626 C CD1 . LEU A 1 482 ? 145.465 123.064 115.666 1.00 65.75  ?  398 LEU A CD1 1 
ATOM   2627 C CD2 . LEU A 1 482 ? 145.783 123.001 118.136 1.00 67.98  ?  398 LEU A CD2 1 
ATOM   2628 N N   . VAL A 1 483 ? 141.148 123.546 116.921 1.00 65.60  ?  399 VAL A N   1 
ATOM   2629 C CA  . VAL A 1 483 ? 140.175 122.461 116.849 1.00 54.04  ?  399 VAL A CA  1 
ATOM   2630 C C   . VAL A 1 483 ? 139.309 122.629 115.615 1.00 54.74  ?  399 VAL A C   1 
ATOM   2631 O O   . VAL A 1 483 ? 139.206 121.720 114.780 1.00 65.79  ?  399 VAL A O   1 
ATOM   2632 C CB  . VAL A 1 483 ? 139.327 122.409 118.129 1.00 51.99  ?  399 VAL A CB  1 
ATOM   2633 C CG1 . VAL A 1 483 ? 138.208 121.402 117.971 1.00 52.47  ?  399 VAL A CG1 1 
ATOM   2634 C CG2 . VAL A 1 483 ? 140.197 122.055 119.312 1.00 63.28  ?  399 VAL A CG2 1 
ATOM   2635 N N   . PHE A 1 484 ? 138.751 123.830 115.436 1.00 54.20  ?  400 PHE A N   1 
ATOM   2636 C CA  . PHE A 1 484 ? 137.909 124.080 114.275 1.00 54.37  ?  400 PHE A CA  1 
ATOM   2637 C C   . PHE A 1 484 ? 138.648 123.689 113.010 1.00 54.34  ?  400 PHE A C   1 
ATOM   2638 O O   . PHE A 1 484 ? 138.168 122.859 112.226 1.00 62.12  ?  400 PHE A O   1 
ATOM   2639 C CB  . PHE A 1 484 ? 137.494 125.551 114.226 1.00 58.71  ?  400 PHE A CB  1 
ATOM   2640 C CG  . PHE A 1 484 ? 136.555 125.957 115.326 1.00 62.92  ?  400 PHE A CG  1 
ATOM   2641 C CD1 . PHE A 1 484 ? 135.861 125.008 116.054 1.00 62.02  ?  400 PHE A CD1 1 
ATOM   2642 C CD2 . PHE A 1 484 ? 136.365 127.292 115.630 1.00 63.82  ?  400 PHE A CD2 1 
ATOM   2643 C CE1 . PHE A 1 484 ? 135.000 125.384 117.062 1.00 60.42  ?  400 PHE A CE1 1 
ATOM   2644 C CE2 . PHE A 1 484 ? 135.505 127.671 116.638 1.00 63.12  ?  400 PHE A CE2 1 
ATOM   2645 C CZ  . PHE A 1 484 ? 134.822 126.717 117.354 1.00 59.03  ?  400 PHE A CZ  1 
ATOM   2646 N N   . GLY A 1 485 ? 139.876 124.191 112.861 1.00 53.86  ?  401 GLY A N   1 
ATOM   2647 C CA  . GLY A 1 485 ? 140.635 123.886 111.664 1.00 56.41  ?  401 GLY A CA  1 
ATOM   2648 C C   . GLY A 1 485 ? 140.753 122.397 111.450 1.00 59.42  ?  401 GLY A C   1 
ATOM   2649 O O   . GLY A 1 485 ? 140.392 121.879 110.388 1.00 65.80  ?  401 GLY A O   1 
ATOM   2650 N N   . VAL A 1 486 ? 141.161 121.673 112.497 1.00 52.17  ?  402 VAL A N   1 
ATOM   2651 C CA  . VAL A 1 486 ? 141.331 120.232 112.362 1.00 48.07  ?  402 VAL A CA  1 
ATOM   2652 C C   . VAL A 1 486 ? 140.034 119.610 111.877 1.00 52.63  ?  402 VAL A C   1 
ATOM   2653 O O   . VAL A 1 486 ? 140.010 118.900 110.863 1.00 62.78  ?  402 VAL A O   1 
ATOM   2654 C CB  . VAL A 1 486 ? 141.797 119.612 113.690 1.00 53.35  ?  402 VAL A CB  1 
ATOM   2655 C CG1 . VAL A 1 486 ? 141.914 118.108 113.550 1.00 49.51  ?  402 VAL A CG1 1 
ATOM   2656 C CG2 . VAL A 1 486 ? 143.127 120.207 114.109 1.00 57.53  ?  402 VAL A CG2 1 
ATOM   2657 N N   . ASN A 1 487 ? 138.922 119.955 112.532 1.00 47.26  ?  403 ASN A N   1 
ATOM   2658 C CA  . ASN A 1 487 ? 137.638 119.414 112.108 1.00 41.97  ?  403 ASN A CA  1 
ATOM   2659 C C   . ASN A 1 487 ? 137.401 119.727 110.642 1.00 39.71  ?  403 ASN A C   1 
ATOM   2660 O O   . ASN A 1 487 ? 137.212 118.816 109.825 1.00 50.16  ?  403 ASN A O   1 
ATOM   2661 C CB  . ASN A 1 487 ? 136.515 119.975 112.978 1.00 54.77  ?  403 ASN A CB  1 
ATOM   2662 C CG  . ASN A 1 487 ? 136.582 119.476 114.403 1.00 54.26  ?  403 ASN A CG  1 
ATOM   2663 O OD1 . ASN A 1 487 ? 137.217 118.462 114.686 1.00 49.30  ?  403 ASN A OD1 1 
ATOM   2664 N ND2 . ASN A 1 487 ? 135.926 120.185 115.310 1.00 50.99  ?  403 ASN A ND2 1 
ATOM   2665 N N   . THR A 1 488 ? 137.520 121.006 110.276 1.00 48.34  ?  404 THR A N   1 
ATOM   2666 C CA  . THR A 1 488 ? 137.337 121.387 108.884 1.00 47.51  ?  404 THR A CA  1 
ATOM   2667 C C   . THR A 1 488 ? 138.267 120.577 108.000 1.00 51.17  ?  404 THR A C   1 
ATOM   2668 O O   . THR A 1 488 ? 137.828 119.942 107.033 1.00 59.21  ?  404 THR A O   1 
ATOM   2669 C CB  . THR A 1 488 ? 137.588 122.884 108.706 1.00 44.49  ?  404 THR A CB  1 
ATOM   2670 O OG1 . THR A 1 488 ? 136.977 123.603 109.784 1.00 53.45  ?  404 THR A OG1 1 
ATOM   2671 C CG2 . THR A 1 488 ? 137.002 123.363 107.394 1.00 45.75  ?  404 THR A CG2 1 
ATOM   2672 N N   . PHE A 1 489 ? 139.546 120.514 108.382 1.00 49.84  ?  405 PHE A N   1 
ATOM   2673 C CA  . PHE A 1 489 ? 140.508 119.746 107.606 1.00 43.74  ?  405 PHE A CA  1 
ATOM   2674 C C   . PHE A 1 489 ? 140.009 118.325 107.419 1.00 54.38  ?  405 PHE A C   1 
ATOM   2675 O O   . PHE A 1 489 ? 139.818 117.863 106.286 1.00 63.20  ?  405 PHE A O   1 
ATOM   2676 C CB  . PHE A 1 489 ? 141.868 119.770 108.305 1.00 46.14  ?  405 PHE A CB  1 
ATOM   2677 C CG  . PHE A 1 489 ? 142.934 118.987 107.599 1.00 45.78  ?  405 PHE A CG  1 
ATOM   2678 C CD1 . PHE A 1 489 ? 143.640 119.543 106.549 1.00 56.37  ?  405 PHE A CD1 1 
ATOM   2679 C CD2 . PHE A 1 489 ? 143.246 117.700 107.999 1.00 49.67  ?  405 PHE A CD2 1 
ATOM   2680 C CE1 . PHE A 1 489 ? 144.624 118.827 105.902 1.00 57.26  ?  405 PHE A CE1 1 
ATOM   2681 C CE2 . PHE A 1 489 ? 144.230 116.981 107.356 1.00 51.11  ?  405 PHE A CE2 1 
ATOM   2682 C CZ  . PHE A 1 489 ? 144.920 117.545 106.307 1.00 52.62  ?  405 PHE A CZ  1 
ATOM   2683 N N   . PHE A 1 490 ? 139.669 117.660 108.526 1.00 51.00  ?  406 PHE A N   1 
ATOM   2684 C CA  . PHE A 1 490 ? 139.210 116.284 108.422 1.00 43.61  ?  406 PHE A CA  1 
ATOM   2685 C C   . PHE A 1 490 ? 137.948 116.212 107.582 1.00 49.54  ?  406 PHE A C   1 
ATOM   2686 O O   . PHE A 1 490 ? 137.831 115.352 106.699 1.00 50.63  ?  406 PHE A O   1 
ATOM   2687 C CB  . PHE A 1 490 ? 138.982 115.693 109.811 1.00 41.68  ?  406 PHE A CB  1 
ATOM   2688 C CG  . PHE A 1 490 ? 140.240 115.223 110.476 1.00 51.88  ?  406 PHE A CG  1 
ATOM   2689 C CD1 . PHE A 1 490 ? 141.384 114.992 109.734 1.00 53.14  ?  406 PHE A CD1 1 
ATOM   2690 C CD2 . PHE A 1 490 ? 140.281 115.013 111.843 1.00 57.88  ?  406 PHE A CD2 1 
ATOM   2691 C CE1 . PHE A 1 490 ? 142.546 114.561 110.340 1.00 56.95  ?  406 PHE A CE1 1 
ATOM   2692 C CE2 . PHE A 1 490 ? 141.441 114.582 112.455 1.00 55.19  ?  406 PHE A CE2 1 
ATOM   2693 C CZ  . PHE A 1 490 ? 142.574 114.356 111.702 1.00 55.69  ?  406 PHE A CZ  1 
ATOM   2694 N N   . ALA A 1 491 ? 137.025 117.155 107.794 1.00 52.17  ?  407 ALA A N   1 
ATOM   2695 C CA  . ALA A 1 491 ? 135.805 117.175 107.000 1.00 45.37  ?  407 ALA A CA  1 
ATOM   2696 C C   . ALA A 1 491 ? 136.147 117.170 105.522 1.00 45.01  ?  407 ALA A C   1 
ATOM   2697 O O   . ALA A 1 491 ? 135.668 116.316 104.765 1.00 61.91  ?  407 ALA A O   1 
ATOM   2698 C CB  . ALA A 1 491 ? 134.958 118.394 107.361 1.00 48.83  ?  407 ALA A CB  1 
ATOM   2699 N N   . THR A 1 492 ? 137.053 118.065 105.114 1.00 45.33  ?  408 THR A N   1 
ATOM   2700 C CA  . THR A 1 492 ? 137.445 118.120 103.713 1.00 49.73  ?  408 THR A CA  1 
ATOM   2701 C C   . THR A 1 492 ? 137.912 116.753 103.248 1.00 55.00  ?  408 THR A C   1 
ATOM   2702 O O   . THR A 1 492 ? 137.394 116.205 102.266 1.00 59.16  ?  408 THR A O   1 
ATOM   2703 C CB  . THR A 1 492 ? 138.542 119.164 103.509 1.00 52.56  ?  408 THR A CB  1 
ATOM   2704 O OG1 . THR A 1 492 ? 138.161 120.390 104.144 1.00 62.24  ?  408 THR A OG1 1 
ATOM   2705 C CG2 . THR A 1 492 ? 138.766 119.414 102.030 1.00 51.47  ?  408 THR A CG2 1 
ATOM   2706 N N   . ILE A 1 493 ? 138.828 116.147 104.008 1.00 52.11  ?  409 ILE A N   1 
ATOM   2707 C CA  . ILE A 1 493 ? 139.355 114.842 103.629 1.00 51.78  ?  409 ILE A CA  1 
ATOM   2708 C C   . ILE A 1 493 ? 138.212 113.856 103.456 1.00 51.84  ?  409 ILE A C   1 
ATOM   2709 O O   . ILE A 1 493 ? 138.104 113.182 102.423 1.00 58.10  ?  409 ILE A O   1 
ATOM   2710 C CB  . ILE A 1 493 ? 140.379 114.352 104.667 1.00 51.85  ?  409 ILE A CB  1 
ATOM   2711 C CG1 . ILE A 1 493 ? 141.741 114.999 104.410 1.00 50.39  ?  409 ILE A CG1 1 
ATOM   2712 C CG2 . ILE A 1 493 ? 140.489 112.838 104.635 1.00 56.14  ?  409 ILE A CG2 1 
ATOM   2713 C CD1 . ILE A 1 493 ? 142.880 114.346 105.157 1.00 51.95  ?  409 ILE A CD1 1 
ATOM   2714 N N   . VAL A 1 494 ? 137.295 113.823 104.427 1.00 47.71  ?  410 VAL A N   1 
ATOM   2715 C CA  . VAL A 1 494 ? 136.183 112.883 104.347 1.00 43.45  ?  410 VAL A CA  1 
ATOM   2716 C C   . VAL A 1 494 ? 135.411 113.109 103.059 1.00 51.70  ?  410 VAL A C   1 
ATOM   2717 O O   . VAL A 1 494 ? 135.173 112.172 102.285 1.00 63.67  ?  410 VAL A O   1 
ATOM   2718 C CB  . VAL A 1 494 ? 135.275 113.005 105.582 1.00 42.16  ?  410 VAL A CB  1 
ATOM   2719 C CG1 . VAL A 1 494 ? 133.995 112.223 105.368 1.00 43.44  ?  410 VAL A CG1 1 
ATOM   2720 C CG2 . VAL A 1 494 ? 136.000 112.509 106.817 1.00 52.66  ?  410 VAL A CG2 1 
ATOM   2721 N N   . LYS A 1 495 ? 135.080 114.372 102.771 1.00 56.76  ?  411 LYS A N   1 
ATOM   2722 C CA  . LYS A 1 495 ? 134.363 114.671 101.538 1.00 51.19  ?  411 LYS A CA  1 
ATOM   2723 C C   . LYS A 1 495 ? 135.125 114.126 100.343 1.00 57.10  ?  411 LYS A C   1 
ATOM   2724 O O   . LYS A 1 495 ? 134.568 113.383 99.524  1.00 64.65  ?  411 LYS A O   1 
ATOM   2725 C CB  . LYS A 1 495 ? 134.142 116.178 101.404 1.00 50.43  ?  411 LYS A CB  1 
ATOM   2726 C CG  . LYS A 1 495 ? 133.649 116.604 100.033 1.00 54.98  ?  411 LYS A CG  1 
ATOM   2727 C CD  . LYS A 1 495 ? 133.258 118.072 100.005 1.00 60.49  ?  411 LYS A CD  1 
ATOM   2728 C CE  . LYS A 1 495 ? 134.478 118.975 100.040 1.00 61.13  ?  411 LYS A CE  1 
ATOM   2729 N NZ  . LYS A 1 495 ? 134.307 120.103 100.996 1.00 57.56  1  411 LYS A NZ  1 
ATOM   2730 N N   . THR A 1 496 ? 136.429 114.413 100.280 1.00 52.65  ?  412 THR A N   1 
ATOM   2731 C CA  . THR A 1 496 ? 137.235 113.920 99.171  1.00 53.22  ?  412 THR A CA  1 
ATOM   2732 C C   . THR A 1 496 ? 137.116 112.410 99.062  1.00 56.69  ?  412 THR A C   1 
ATOM   2733 O O   . THR A 1 496 ? 136.836 111.874 97.982  1.00 60.11  ?  412 THR A O   1 
ATOM   2734 C CB  . THR A 1 496 ? 138.694 114.336 99.350  1.00 57.04  ?  412 THR A CB  1 
ATOM   2735 O OG1 . THR A 1 496 ? 138.766 115.751 99.559  1.00 59.74  ?  412 THR A OG1 1 
ATOM   2736 C CG2 . THR A 1 496 ? 139.498 113.973 98.116  1.00 61.44  ?  412 THR A CG2 1 
ATOM   2737 N N   . ILE A 1 497 ? 137.247 111.711 100.192 1.00 57.83  ?  413 ILE A N   1 
ATOM   2738 C CA  . ILE A 1 497 ? 137.158 110.257 100.164 1.00 56.63  ?  413 ILE A CA  1 
ATOM   2739 C C   . ILE A 1 497 ? 135.842 109.835 99.532  1.00 56.27  ?  413 ILE A C   1 
ATOM   2740 O O   . ILE A 1 497 ? 135.815 109.034 98.588  1.00 63.95  ?  413 ILE A O   1 
ATOM   2741 C CB  . ILE A 1 497 ? 137.321 109.679 101.580 1.00 56.05  ?  413 ILE A CB  1 
ATOM   2742 C CG1 . ILE A 1 497 ? 138.791 109.711 101.996 1.00 57.54  ?  413 ILE A CG1 1 
ATOM   2743 C CG2 . ILE A 1 497 ? 136.774 108.262 101.645 1.00 54.40  ?  413 ILE A CG2 1 
ATOM   2744 C CD1 . ILE A 1 497 ? 139.004 109.630 103.488 1.00 57.49  ?  413 ILE A CD1 1 
ATOM   2745 N N   . ILE A 1 498 ? 134.739 110.435 99.982  1.00 48.90  ?  414 ILE A N   1 
ATOM   2746 C CA  . ILE A 1 498 ? 133.443 110.068 99.425  1.00 52.09  ?  414 ILE A CA  1 
ATOM   2747 C C   . ILE A 1 498 ? 133.397 110.406 97.944  1.00 66.76  ?  414 ILE A C   1 
ATOM   2748 O O   . ILE A 1 498 ? 132.986 109.580 97.119  1.00 75.66  ?  414 ILE A O   1 
ATOM   2749 C CB  . ILE A 1 498 ? 132.304 110.744 100.207 1.00 52.11  ?  414 ILE A CB  1 
ATOM   2750 C CG1 . ILE A 1 498 ? 132.321 110.273 101.661 1.00 54.22  ?  414 ILE A CG1 1 
ATOM   2751 C CG2 . ILE A 1 498 ? 130.968 110.420 99.571  1.00 59.69  ?  414 ILE A CG2 1 
ATOM   2752 C CD1 . ILE A 1 498 ? 131.478 111.114 102.587 1.00 61.91  ?  414 ILE A CD1 1 
ATOM   2753 N N   . THR A 1 499 ? 133.882 111.593 97.568  1.00 70.29  ?  415 THR A N   1 
ATOM   2754 C CA  . THR A 1 499 ? 133.805 111.955 96.160  1.00 66.16  ?  415 THR A CA  1 
ATOM   2755 C C   . THR A 1 499 ? 134.777 111.148 95.315  1.00 71.81  ?  415 THR A C   1 
ATOM   2756 O O   . THR A 1 499 ? 134.727 111.241 94.084  1.00 72.69  ?  415 THR A O   1 
ATOM   2757 C CB  . THR A 1 499 ? 134.045 113.454 95.958  1.00 66.52  ?  415 THR A CB  1 
ATOM   2758 O OG1 . THR A 1 499 ? 133.535 113.843 94.678  1.00 71.30  ?  415 THR A OG1 1 
ATOM   2759 C CG2 . THR A 1 499 ? 135.520 113.775 95.991  1.00 67.00  ?  415 THR A CG2 1 
ATOM   2760 N N   . PHE A 1 500 ? 135.659 110.367 95.942  1.00 77.76  ?  416 PHE A N   1 
ATOM   2761 C CA  . PHE A 1 500 ? 136.453 109.402 95.197  1.00 76.28  ?  416 PHE A CA  1 
ATOM   2762 C C   . PHE A 1 500 ? 135.700 108.093 95.000  1.00 78.10  ?  416 PHE A C   1 
ATOM   2763 O O   . PHE A 1 500 ? 135.803 107.476 93.935  1.00 82.96  ?  416 PHE A O   1 
ATOM   2764 C CB  . PHE A 1 500 ? 137.786 109.151 95.912  1.00 78.60  ?  416 PHE A CB  1 
ATOM   2765 C CG  . PHE A 1 500 ? 138.751 108.290 95.134  1.00 83.26  ?  416 PHE A CG  1 
ATOM   2766 C CD1 . PHE A 1 500 ? 139.838 108.859 94.494  1.00 85.93  ?  416 PHE A CD1 1 
ATOM   2767 C CD2 . PHE A 1 500 ? 138.597 106.912 95.079  1.00 79.50  ?  416 PHE A CD2 1 
ATOM   2768 C CE1 . PHE A 1 500 ? 140.734 108.077 93.788  1.00 84.02  ?  416 PHE A CE1 1 
ATOM   2769 C CE2 . PHE A 1 500 ? 139.487 106.127 94.374  1.00 79.66  ?  416 PHE A CE2 1 
ATOM   2770 C CZ  . PHE A 1 500 ? 140.557 106.710 93.729  1.00 82.18  ?  416 PHE A CZ  1 
ATOM   2771 N N   . ILE A 1 501 ? 134.927 107.661 96.001  1.00 73.06  ?  417 ILE A N   1 
ATOM   2772 C CA  . ILE A 1 501 ? 134.287 106.350 95.930  1.00 76.74  ?  417 ILE A CA  1 
ATOM   2773 C C   . ILE A 1 501 ? 132.912 106.391 95.284  1.00 74.20  ?  417 ILE A C   1 
ATOM   2774 O O   . ILE A 1 501 ? 132.341 105.325 95.006  1.00 74.19  ?  417 ILE A O   1 
ATOM   2775 C CB  . ILE A 1 501 ? 134.157 105.708 97.326  1.00 67.72  ?  417 ILE A CB  1 
ATOM   2776 C CG1 . ILE A 1 501 ? 132.952 106.282 98.070  1.00 69.21  ?  417 ILE A CG1 1 
ATOM   2777 C CG2 . ILE A 1 501 ? 135.434 105.902 98.125  1.00 69.16  ?  417 ILE A CG2 1 
ATOM   2778 C CD1 . ILE A 1 501 ? 132.473 105.418 99.214  1.00 70.77  ?  417 ILE A CD1 1 
ATOM   2779 N N   . VAL A 1 502 ? 132.372 107.584 95.002  1.00 71.04  ?  418 VAL A N   1 
ATOM   2780 C CA  . VAL A 1 502 ? 130.972 107.632 94.470  1.00 74.27  ?  418 VAL A CA  1 
ATOM   2781 C C   . VAL A 1 502 ? 130.916 108.275 93.079  1.00 82.90  ?  418 VAL A C   1 
ATOM   2782 O O   . VAL A 1 502 ? 130.001 107.909 92.314  1.00 85.80  ?  418 VAL A O   1 
ATOM   2783 C CB  . VAL A 1 502 ? 129.999 108.349 95.431  1.00 71.71  ?  418 VAL A CB  1 
ATOM   2784 C CG1 . VAL A 1 502 ? 129.983 107.732 96.820  1.00 74.64  ?  418 VAL A CG1 1 
ATOM   2785 C CG2 . VAL A 1 502 ? 130.244 109.848 95.501  1.00 75.66  ?  418 VAL A CG2 1 
ATOM   2786 N N   . SER A 1 503 ? 131.833 109.192 92.751  1.00 95.03  ?  419 SER A N   1 
ATOM   2787 C CA  . SER A 1 503 ? 131.712 109.896 91.478  1.00 95.62  ?  419 SER A CA  1 
ATOM   2788 C C   . SER A 1 503 ? 132.885 109.645 90.540  1.00 94.93  ?  419 SER A C   1 
ATOM   2789 O O   . SER A 1 503 ? 132.676 109.171 89.420  1.00 94.76  ?  419 SER A O   1 
ATOM   2790 C CB  . SER A 1 503 ? 131.551 111.400 91.734  1.00 92.98  ?  419 SER A CB  1 
ATOM   2791 O OG  . SER A 1 503 ? 132.788 112.075 91.592  1.00 91.65  ?  419 SER A OG  1 
ATOM   2792 N N   . ASP A 1 504 ? 134.111 109.936 90.960  1.00 106.92 ?  420 ASP A N   1 
ATOM   2793 C CA  . ASP A 1 504 ? 135.239 110.061 90.048  1.00 109.52 ?  420 ASP A CA  1 
ATOM   2794 C C   . ASP A 1 504 ? 136.199 108.885 90.199  1.00 108.75 ?  420 ASP A C   1 
ATOM   2795 O O   . ASP A 1 504 ? 136.028 108.012 91.054  1.00 108.87 ?  420 ASP A O   1 
ATOM   2796 C CB  . ASP A 1 504 ? 135.965 111.388 90.281  1.00 111.15 ?  420 ASP A CB  1 
ATOM   2797 C CG  . ASP A 1 504 ? 136.538 111.972 89.004  1.00 112.53 ?  420 ASP A CG  1 
ATOM   2798 O OD1 . ASP A 1 504 ? 135.774 112.139 88.029  1.00 110.75 ?  420 ASP A OD1 1 
ATOM   2799 O OD2 . ASP A 1 504 ? 137.752 112.265 88.975  1.00 110.15 -1 420 ASP A OD2 1 
ATOM   2800 N N   . VAL A 1 505 ? 137.228 108.891 89.346  1.00 110.20 ?  421 VAL A N   1 
ATOM   2801 C CA  . VAL A 1 505 ? 138.284 107.882 89.310  1.00 112.32 ?  421 VAL A CA  1 
ATOM   2802 C C   . VAL A 1 505 ? 137.669 106.489 89.289  1.00 112.54 ?  421 VAL A C   1 
ATOM   2803 O O   . VAL A 1 505 ? 137.988 105.644 90.134  1.00 112.50 ?  421 VAL A O   1 
ATOM   2804 C CB  . VAL A 1 505 ? 139.255 108.045 90.496  1.00 111.87 ?  421 VAL A CB  1 
ATOM   2805 C CG1 . VAL A 1 505 ? 140.593 107.387 90.182  1.00 110.17 ?  421 VAL A CG1 1 
ATOM   2806 C CG2 . VAL A 1 505 ? 139.453 109.519 90.823  1.00 106.69 ?  421 VAL A CG2 1 
ATOM   2807 N N   . ARG A 1 506 ? 136.791 106.244 88.314  1.00 110.94 ?  422 ARG A N   1 
ATOM   2808 C CA  . ARG A 1 506 ? 136.033 105.001 88.236  1.00 111.61 ?  422 ARG A CA  1 
ATOM   2809 C C   . ARG A 1 506 ? 135.351 104.713 89.566  1.00 114.36 ?  422 ARG A C   1 
ATOM   2810 O O   . ARG A 1 506 ? 134.297 105.284 89.866  1.00 114.19 ?  422 ARG A O   1 
ATOM   2811 C CB  . ARG A 1 506 ? 136.934 103.831 87.833  1.00 112.74 ?  422 ARG A CB  1 
ATOM   2812 C CG  . ARG A 1 506 ? 137.862 104.122 86.667  1.00 113.24 ?  422 ARG A CG  1 
ATOM   2813 C CD  . ARG A 1 506 ? 138.325 102.832 86.009  1.00 113.48 ?  422 ARG A CD  1 
ATOM   2814 N NE  . ARG A 1 506 ? 138.824 101.870 86.984  1.00 113.70 ?  422 ARG A NE  1 
ATOM   2815 C CZ  . ARG A 1 506 ? 138.603 100.564 86.930  1.00 113.04 ?  422 ARG A CZ  1 
ATOM   2816 N NH1 . ARG A 1 506 ? 137.891 100.023 85.956  1.00 111.30 1  422 ARG A NH1 1 
ATOM   2817 N NH2 . ARG A 1 506 ? 139.109 99.781  87.879  1.00 113.43 ?  422 ARG A NH2 1 
ATOM   2818 N N   . GLY A 1 507 ? 135.958 103.845 90.372  1.00 116.99 ?  423 GLY A N   1 
ATOM   2819 C CA  . GLY A 1 507 ? 135.387 103.507 91.662  1.00 114.27 ?  423 GLY A CA  1 
ATOM   2820 C C   . GLY A 1 507 ? 133.998 102.929 91.505  1.00 116.19 ?  423 GLY A C   1 
ATOM   2821 O O   . GLY A 1 507 ? 133.721 102.147 90.588  1.00 116.90 ?  423 GLY A O   1 
ATOM   2822 N N   . LEU A 1 508 ? 133.103 103.321 92.406  1.00 101.72 ?  424 LEU A N   1 
ATOM   2823 C CA  . LEU A 1 508 ? 131.695 102.953 92.291  1.00 99.33  ?  424 LEU A CA  1 
ATOM   2824 C C   . LEU A 1 508 ? 130.947 104.068 91.556  1.00 97.94  ?  424 LEU A C   1 
ATOM   2825 O O   . LEU A 1 508 ? 130.059 104.731 92.089  1.00 101.38 ?  424 LEU A O   1 
ATOM   2826 C CB  . LEU A 1 508 ? 131.108 102.680 93.672  1.00 101.33 ?  424 LEU A CB  1 
ATOM   2827 C CG  . LEU A 1 508 ? 129.959 101.675 93.833  1.00 103.50 ?  424 LEU A CG  1 
ATOM   2828 C CD1 . LEU A 1 508 ? 129.653 101.457 95.310  1.00 101.23 ?  424 LEU A CD1 1 
ATOM   2829 C CD2 . LEU A 1 508 ? 128.700 102.066 93.081  1.00 104.59 ?  424 LEU A CD2 1 
ATOM   2830 N N   . GLY A 1 509 ? 131.357 104.280 90.306  1.00 99.09  ?  425 GLY A N   1 
ATOM   2831 C CA  . GLY A 1 509 ? 130.839 105.367 89.495  1.00 102.44 ?  425 GLY A CA  1 
ATOM   2832 C C   . GLY A 1 509 ? 129.345 105.301 89.260  1.00 105.39 ?  425 GLY A C   1 
ATOM   2833 O O   . GLY A 1 509 ? 128.826 104.276 88.808  1.00 106.37 ?  425 GLY A O   1 
ATOM   2834 N N   . LEU A 1 510 ? 128.645 106.385 89.563  1.00 94.82  ?  426 LEU A N   1 
ATOM   2835 C CA  . LEU A 1 510 ? 127.196 106.437 89.470  1.00 94.31  ?  426 LEU A CA  1 
ATOM   2836 C C   . LEU A 1 510 ? 126.767 107.808 88.976  1.00 95.92  ?  426 LEU A C   1 
ATOM   2837 O O   . LEU A 1 510 ? 127.509 108.786 89.113  1.00 93.89  ?  426 LEU A O   1 
ATOM   2838 C CB  . LEU A 1 510 ? 126.538 106.150 90.826  1.00 93.47  ?  426 LEU A CB  1 
ATOM   2839 C CG  . LEU A 1 510 ? 126.839 104.821 91.515  1.00 94.38  ?  426 LEU A CG  1 
ATOM   2840 C CD1 . LEU A 1 510 ? 126.541 104.941 92.992  1.00 92.95  ?  426 LEU A CD1 1 
ATOM   2841 C CD2 . LEU A 1 510 ? 126.039 103.687 90.897  1.00 95.37  ?  426 LEU A CD2 1 
ATOM   2842 N N   . PRO A 1 511 ? 125.566 107.911 88.389  1.00 100.97 ?  427 PRO A N   1 
ATOM   2843 C CA  . PRO A 1 511 ? 125.022 109.232 88.044  1.00 97.93  ?  427 PRO A CA  1 
ATOM   2844 C C   . PRO A 1 511 ? 124.683 110.058 89.276  1.00 99.25  ?  427 PRO A C   1 
ATOM   2845 O O   . PRO A 1 511 ? 124.869 109.603 90.409  1.00 100.33 ?  427 PRO A O   1 
ATOM   2846 C CB  . PRO A 1 511 ? 123.762 108.903 87.230  1.00 93.89  ?  427 PRO A CB  1 
ATOM   2847 C CG  . PRO A 1 511 ? 123.471 107.466 87.497  1.00 98.03  ?  427 PRO A CG  1 
ATOM   2848 C CD  . PRO A 1 511 ? 124.767 106.811 87.824  1.00 99.88  ?  427 PRO A CD  1 
ATOM   2849 N N   . VAL A 1 512 ? 124.175 111.273 89.062  1.00 93.00  ?  428 VAL A N   1 
ATOM   2850 C CA  . VAL A 1 512 ? 123.946 112.190 90.175  1.00 89.54  ?  428 VAL A CA  1 
ATOM   2851 C C   . VAL A 1 512 ? 122.831 111.683 91.081  1.00 92.44  ?  428 VAL A C   1 
ATOM   2852 O O   . VAL A 1 512 ? 122.886 111.853 92.304  1.00 97.56  ?  428 VAL A O   1 
ATOM   2853 C CB  . VAL A 1 512 ? 123.648 113.604 89.648  1.00 91.65  ?  428 VAL A CB  1 
ATOM   2854 C CG1 . VAL A 1 512 ? 123.884 114.631 90.741  1.00 89.92  ?  428 VAL A CG1 1 
ATOM   2855 C CG2 . VAL A 1 512 ? 124.505 113.906 88.431  1.00 93.92  ?  428 VAL A CG2 1 
ATOM   2856 N N   . ARG A 1 513 ? 121.794 111.071 90.502  1.00 89.41  ?  429 ARG A N   1 
ATOM   2857 C CA  . ARG A 1 513 ? 120.694 110.556 91.313  1.00 89.59  ?  429 ARG A CA  1 
ATOM   2858 C C   . ARG A 1 513 ? 121.177 109.469 92.265  1.00 89.58  ?  429 ARG A C   1 
ATOM   2859 O O   . ARG A 1 513 ? 120.835 109.466 93.454  1.00 90.84  ?  429 ARG A O   1 
ATOM   2860 C CB  . ARG A 1 513 ? 119.583 110.021 90.409  1.00 91.12  ?  429 ARG A CB  1 
ATOM   2861 C CG  . ARG A 1 513 ? 119.231 110.930 89.247  1.00 91.26  ?  429 ARG A CG  1 
ATOM   2862 C CD  . ARG A 1 513 ? 117.729 110.972 89.019  1.00 90.19  ?  429 ARG A CD  1 
ATOM   2863 N NE  . ARG A 1 513 ? 117.058 111.856 89.964  1.00 93.19  ?  429 ARG A NE  1 
ATOM   2864 C CZ  . ARG A 1 513 ? 117.042 113.178 89.867  1.00 93.57  ?  429 ARG A CZ  1 
ATOM   2865 N NH1 . ARG A 1 513 ? 117.653 113.806 88.877  1.00 94.36  1  429 ARG A NH1 1 
ATOM   2866 N NH2 . ARG A 1 513 ? 116.397 113.888 90.788  1.00 91.45  ?  429 ARG A NH2 1 
ATOM   2867 N N   . LYS A 1 514 ? 122.002 108.557 91.748  1.00 82.49  ?  430 LYS A N   1 
ATOM   2868 C CA  . LYS A 1 514 ? 122.545 107.470 92.605  1.00 82.25  ?  430 LYS A CA  1 
ATOM   2869 C C   . LYS A 1 514 ? 123.511 108.078 93.629  1.00 82.32  ?  430 LYS A C   1 
ATOM   2870 O O   . LYS A 1 514 ? 123.537 107.581 94.771  1.00 84.64  ?  430 LYS A O   1 
ATOM   2871 C CB  . LYS A 1 514 ? 123.190 106.389 91.733  1.00 84.85  ?  430 LYS A CB  1 
ATOM   2872 C CG  . LYS A 1 514 ? 122.252 105.769 90.706  1.00 89.11  ?  430 LYS A CG  1 
ATOM   2873 C CD  . LYS A 1 514 ? 122.853 104.600 89.960  1.00 87.61  ?  430 LYS A CD  1 
ATOM   2874 C CE  . LYS A 1 514 ? 121.937 104.046 88.889  1.00 84.22  ?  430 LYS A CE  1 
ATOM   2875 N NZ  . LYS A 1 514 ? 122.572 102.927 88.153  1.00 84.68  1  430 LYS A NZ  1 
ATOM   2876 N N   . GLN A 1 515 ? 124.261 109.117 93.245  1.00 76.82  ?  431 GLN A N   1 
ATOM   2877 C CA  . GLN A 1 515 ? 125.143 109.783 94.198  1.00 77.36  ?  431 GLN A CA  1 
ATOM   2878 C C   . GLN A 1 515 ? 124.351 110.368 95.358  1.00 77.40  ?  431 GLN A C   1 
ATOM   2879 O O   . GLN A 1 515 ? 124.744 110.234 96.523  1.00 81.21  ?  431 GLN A O   1 
ATOM   2880 C CB  . GLN A 1 515 ? 125.945 110.878 93.497  1.00 74.02  ?  431 GLN A CB  1 
ATOM   2881 C CG  . GLN A 1 515 ? 127.163 110.379 92.752  1.00 78.55  ?  431 GLN A CG  1 
ATOM   2882 C CD  . GLN A 1 515 ? 127.982 111.507 92.163  1.00 80.70  ?  431 GLN A CD  1 
ATOM   2883 O OE1 . GLN A 1 515 ? 128.299 112.480 92.845  1.00 78.58  ?  431 GLN A OE1 1 
ATOM   2884 N NE2 . GLN A 1 515 ? 128.325 111.385 90.887  1.00 81.48  ?  431 GLN A NE2 1 
ATOM   2885 N N   . PHE A 1 516 ? 123.223 111.014 95.061  1.00 72.71  ?  432 PHE A N   1 
ATOM   2886 C CA  . PHE A 1 516 ? 122.402 111.572 96.128  1.00 71.25  ?  432 PHE A CA  1 
ATOM   2887 C C   . PHE A 1 516 ? 121.737 110.481 96.954  1.00 74.60  ?  432 PHE A C   1 
ATOM   2888 O O   . PHE A 1 516 ? 121.546 110.651 98.162  1.00 81.74  ?  432 PHE A O   1 
ATOM   2889 C CB  . PHE A 1 516 ? 121.360 112.524 95.549  1.00 66.32  ?  432 PHE A CB  1 
ATOM   2890 C CG  . PHE A 1 516 ? 121.749 113.965 95.650  1.00 69.54  ?  432 PHE A CG  1 
ATOM   2891 C CD1 . PHE A 1 516 ? 122.877 114.436 95.006  1.00 71.42  ?  432 PHE A CD1 1 
ATOM   2892 C CD2 . PHE A 1 516 ? 120.997 114.846 96.402  1.00 72.52  ?  432 PHE A CD2 1 
ATOM   2893 C CE1 . PHE A 1 516 ? 123.241 115.758 95.101  1.00 71.43  ?  432 PHE A CE1 1 
ATOM   2894 C CE2 . PHE A 1 516 ? 121.356 116.171 96.501  1.00 74.87  ?  432 PHE A CE2 1 
ATOM   2895 C CZ  . PHE A 1 516 ? 122.480 116.627 95.851  1.00 75.09  ?  432 PHE A CZ  1 
ATOM   2896 N N   . GLN A 1 517 ? 121.384 109.356 96.330  1.00 73.08  ?  433 GLN A N   1 
ATOM   2897 C CA  . GLN A 1 517 ? 120.880 108.228 97.107  1.00 69.30  ?  433 GLN A CA  1 
ATOM   2898 C C   . GLN A 1 517 ? 121.932 107.727 98.090  1.00 72.07  ?  433 GLN A C   1 
ATOM   2899 O O   . GLN A 1 517 ? 121.622 107.443 99.254  1.00 78.23  ?  433 GLN A O   1 
ATOM   2900 C CB  . GLN A 1 517 ? 120.430 107.102 96.178  1.00 71.50  ?  433 GLN A CB  1 
ATOM   2901 C CG  . GLN A 1 517 ? 119.157 107.406 95.410  1.00 75.67  ?  433 GLN A CG  1 
ATOM   2902 C CD  . GLN A 1 517 ? 118.866 106.379 94.338  1.00 77.73  ?  433 GLN A CD  1 
ATOM   2903 O OE1 . GLN A 1 517 ? 119.560 105.369 94.224  1.00 74.83  ?  433 GLN A OE1 1 
ATOM   2904 N NE2 . GLN A 1 517 ? 117.835 106.632 93.541  1.00 78.85  ?  433 GLN A NE2 1 
ATOM   2905 N N   . LEU A 1 518 ? 123.186 107.619 97.643  1.00 70.68  ?  434 LEU A N   1 
ATOM   2906 C CA  . LEU A 1 518 ? 124.246 107.188 98.552  1.00 68.94  ?  434 LEU A CA  1 
ATOM   2907 C C   . LEU A 1 518 ? 124.504 108.220 99.642  1.00 74.23  ?  434 LEU A C   1 
ATOM   2908 O O   . LEU A 1 518 ? 124.819 107.855 100.777 1.00 83.28  ?  434 LEU A O   1 
ATOM   2909 C CB  . LEU A 1 518 ? 125.533 106.883 97.789  1.00 69.82  ?  434 LEU A CB  1 
ATOM   2910 C CG  . LEU A 1 518 ? 125.479 105.807 96.707  1.00 79.35  ?  434 LEU A CG  1 
ATOM   2911 C CD1 . LEU A 1 518 ? 126.874 105.255 96.487  1.00 77.23  ?  434 LEU A CD1 1 
ATOM   2912 C CD2 . LEU A 1 518 ? 124.517 104.692 97.087  1.00 77.32  ?  434 LEU A CD2 1 
ATOM   2913 N N   . TYR A 1 519 ? 124.392 109.511 99.321  1.00 68.31  ?  435 TYR A N   1 
ATOM   2914 C CA  . TYR A 1 519 ? 124.530 110.530 100.360 1.00 64.56  ?  435 TYR A CA  1 
ATOM   2915 C C   . TYR A 1 519 ? 123.415 110.417 101.394 1.00 69.04  ?  435 TYR A C   1 
ATOM   2916 O O   . TYR A 1 519 ? 123.653 110.573 102.599 1.00 77.21  ?  435 TYR A O   1 
ATOM   2917 C CB  . TYR A 1 519 ? 124.548 111.926 99.742  1.00 60.85  ?  435 TYR A CB  1 
ATOM   2918 C CG  . TYR A 1 519 ? 125.672 112.143 98.760  1.00 68.05  ?  435 TYR A CG  1 
ATOM   2919 C CD1 . TYR A 1 519 ? 126.880 111.479 98.903  1.00 63.50  ?  435 TYR A CD1 1 
ATOM   2920 C CD2 . TYR A 1 519 ? 125.527 113.016 97.693  1.00 74.28  ?  435 TYR A CD2 1 
ATOM   2921 C CE1 . TYR A 1 519 ? 127.910 111.674 98.008  1.00 67.67  ?  435 TYR A CE1 1 
ATOM   2922 C CE2 . TYR A 1 519 ? 126.550 113.217 96.794  1.00 73.43  ?  435 TYR A CE2 1 
ATOM   2923 C CZ  . TYR A 1 519 ? 127.739 112.544 96.956  1.00 73.96  ?  435 TYR A CZ  1 
ATOM   2924 O OH  . TYR A 1 519 ? 128.762 112.744 96.060  1.00 75.58  ?  435 TYR A OH  1 
ATOM   2925 N N   . SER A 1 520 ? 122.189 110.147 100.941 1.00 59.20  ?  436 SER A N   1 
ATOM   2926 C CA  . SER A 1 520 ? 121.087 109.931 101.872 1.00 57.49  ?  436 SER A CA  1 
ATOM   2927 C C   . SER A 1 520 ? 121.342 108.718 102.755 1.00 62.81  ?  436 SER A C   1 
ATOM   2928 O O   . SER A 1 520 ? 121.084 108.756 103.962 1.00 68.29  ?  436 SER A O   1 
ATOM   2929 C CB  . SER A 1 520 ? 119.776 109.765 101.106 1.00 61.91  ?  436 SER A CB  1 
ATOM   2930 O OG  . SER A 1 520 ? 118.811 109.098 101.898 1.00 68.17  ?  436 SER A OG  1 
ATOM   2931 N N   . VAL A 1 521 ? 121.848 107.631 102.171 1.00 60.71  ?  437 VAL A N   1 
ATOM   2932 C CA  . VAL A 1 521 ? 122.149 106.440 102.963 1.00 58.47  ?  437 VAL A CA  1 
ATOM   2933 C C   . VAL A 1 521 ? 123.278 106.722 103.949 1.00 59.36  ?  437 VAL A C   1 
ATOM   2934 O O   . VAL A 1 521 ? 123.279 106.211 105.073 1.00 69.87  ?  437 VAL A O   1 
ATOM   2935 C CB  . VAL A 1 521 ? 122.475 105.251 102.042 1.00 58.42  ?  437 VAL A CB  1 
ATOM   2936 C CG1 . VAL A 1 521 ? 122.875 104.037 102.861 1.00 58.50  ?  437 VAL A CG1 1 
ATOM   2937 C CG2 . VAL A 1 521 ? 121.277 104.918 101.174 1.00 60.92  ?  437 VAL A CG2 1 
ATOM   2938 N N   . TYR A 1 522 ? 124.255 107.535 103.547 1.00 47.08  ?  438 TYR A N   1 
ATOM   2939 C CA  . TYR A 1 522 ? 125.347 107.912 104.440 1.00 53.51  ?  438 TYR A CA  1 
ATOM   2940 C C   . TYR A 1 522 ? 124.827 108.702 105.637 1.00 58.75  ?  438 TYR A C   1 
ATOM   2941 O O   . TYR A 1 522 ? 125.201 108.438 106.789 1.00 62.66  ?  438 TYR A O   1 
ATOM   2942 C CB  . TYR A 1 522 ? 126.381 108.713 103.644 1.00 49.64  ?  438 TYR A CB  1 
ATOM   2943 C CG  . TYR A 1 522 ? 127.328 109.574 104.446 1.00 47.36  ?  438 TYR A CG  1 
ATOM   2944 C CD1 . TYR A 1 522 ? 128.462 109.034 105.031 1.00 53.37  ?  438 TYR A CD1 1 
ATOM   2945 C CD2 . TYR A 1 522 ? 127.106 110.936 104.587 1.00 49.45  ?  438 TYR A CD2 1 
ATOM   2946 C CE1 . TYR A 1 522 ? 129.337 109.822 105.749 1.00 56.72  ?  438 TYR A CE1 1 
ATOM   2947 C CE2 . TYR A 1 522 ? 127.974 111.731 105.304 1.00 50.88  ?  438 TYR A CE2 1 
ATOM   2948 C CZ  . TYR A 1 522 ? 129.087 111.169 105.884 1.00 55.47  ?  438 TYR A CZ  1 
ATOM   2949 O OH  . TYR A 1 522 ? 129.955 111.956 106.600 1.00 63.12  ?  438 TYR A OH  1 
ATOM   2950 N N   . PHE A 1 523 ? 123.943 109.668 105.381 1.00 51.16  ?  439 PHE A N   1 
ATOM   2951 C CA  . PHE A 1 523 ? 123.349 110.429 106.475 1.00 42.87  ?  439 PHE A CA  1 
ATOM   2952 C C   . PHE A 1 523 ? 122.483 109.540 107.360 1.00 53.15  ?  439 PHE A C   1 
ATOM   2953 O O   . PHE A 1 523 ? 122.456 109.712 108.582 1.00 64.77  ?  439 PHE A O   1 
ATOM   2954 C CB  . PHE A 1 523 ? 122.536 111.597 105.924 1.00 53.92  ?  439 PHE A CB  1 
ATOM   2955 C CG  . PHE A 1 523 ? 123.337 112.847 105.709 1.00 58.08  ?  439 PHE A CG  1 
ATOM   2956 C CD1 . PHE A 1 523 ? 123.532 113.744 106.741 1.00 59.91  ?  439 PHE A CD1 1 
ATOM   2957 C CD2 . PHE A 1 523 ? 123.887 113.127 104.473 1.00 57.20  ?  439 PHE A CD2 1 
ATOM   2958 C CE1 . PHE A 1 523 ? 124.264 114.894 106.546 1.00 55.55  ?  439 PHE A CE1 1 
ATOM   2959 C CE2 . PHE A 1 523 ? 124.620 114.275 104.273 1.00 52.79  ?  439 PHE A CE2 1 
ATOM   2960 C CZ  . PHE A 1 523 ? 124.808 115.160 105.312 1.00 52.82  ?  439 PHE A CZ  1 
ATOM   2961 N N   . LEU A 1 524 ? 121.764 108.588 106.762 1.00 54.63  ?  440 LEU A N   1 
ATOM   2962 C CA  . LEU A 1 524 ? 120.969 107.650 107.550 1.00 50.85  ?  440 LEU A CA  1 
ATOM   2963 C C   . LEU A 1 524 ? 121.854 106.784 108.436 1.00 52.72  ?  440 LEU A C   1 
ATOM   2964 O O   . LEU A 1 524 ? 121.507 106.500 109.587 1.00 55.57  ?  440 LEU A O   1 
ATOM   2965 C CB  . LEU A 1 524 ? 120.121 106.779 106.625 1.00 48.01  ?  440 LEU A CB  1 
ATOM   2966 C CG  . LEU A 1 524 ? 119.260 105.707 107.291 1.00 51.69  ?  440 LEU A CG  1 
ATOM   2967 C CD1 . LEU A 1 524 ? 118.075 106.335 108.000 1.00 55.16  ?  440 LEU A CD1 1 
ATOM   2968 C CD2 . LEU A 1 524 ? 118.795 104.689 106.265 1.00 57.56  ?  440 LEU A CD2 1 
ATOM   2969 N N   . ILE A 1 525 ? 122.997 106.343 107.909 1.00 53.61  ?  441 ILE A N   1 
ATOM   2970 C CA  . ILE A 1 525 ? 123.937 105.553 108.698 1.00 52.30  ?  441 ILE A CA  1 
ATOM   2971 C C   . ILE A 1 525 ? 124.459 106.369 109.871 1.00 54.83  ?  441 ILE A C   1 
ATOM   2972 O O   . ILE A 1 525 ? 124.563 105.869 110.997 1.00 62.88  ?  441 ILE A O   1 
ATOM   2973 C CB  . ILE A 1 525 ? 125.083 105.042 107.805 1.00 50.79  ?  441 ILE A CB  1 
ATOM   2974 C CG1 . ILE A 1 525 ? 124.594 103.899 106.915 1.00 55.22  ?  441 ILE A CG1 1 
ATOM   2975 C CG2 . ILE A 1 525 ? 126.268 104.599 108.647 1.00 48.03  ?  441 ILE A CG2 1 
ATOM   2976 C CD1 . ILE A 1 525 ? 125.615 103.439 105.902 1.00 55.88  ?  441 ILE A CD1 1 
ATOM   2977 N N   . LEU A 1 526 ? 124.775 107.639 109.615 1.00 49.29  ?  442 LEU A N   1 
ATOM   2978 C CA  . LEU A 1 526 ? 125.242 108.518 110.718 1.00 49.82  ?  442 LEU A CA  1 
ATOM   2979 C C   . LEU A 1 526 ? 124.127 108.637 111.760 1.00 54.68  ?  442 LEU A C   1 
ATOM   2980 O O   . LEU A 1 526 ? 124.426 108.509 112.962 1.00 58.64  ?  442 LEU A O   1 
ATOM   2981 C CB  . LEU A 1 526 ? 125.616 109.890 110.154 1.00 49.61  ?  442 LEU A CB  1 
ATOM   2982 C CG  . LEU A 1 526 ? 127.104 110.219 110.228 1.00 49.32  ?  442 LEU A CG  1 
ATOM   2983 C CD1 . LEU A 1 526 ? 127.698 110.320 108.837 1.00 56.54  ?  442 LEU A CD1 1 
ATOM   2984 C CD2 . LEU A 1 526 ? 127.344 111.501 111.007 1.00 46.77  ?  442 LEU A CD2 1 
ATOM   2985 N N   . SER A 1 527 ? 122.893 108.870 111.308 1.00 54.11  ?  443 SER A N   1 
ATOM   2986 C CA  . SER A 1 527 ? 121.784 109.027 112.244 1.00 51.60  ?  443 SER A CA  1 
ATOM   2987 C C   . SER A 1 527 ? 121.593 107.774 113.088 1.00 55.79  ?  443 SER A C   1 
ATOM   2988 O O   . SER A 1 527 ? 121.334 107.861 114.292 1.00 60.81  ?  443 SER A O   1 
ATOM   2989 C CB  . SER A 1 527 ? 120.501 109.361 111.487 1.00 56.15  ?  443 SER A CB  1 
ATOM   2990 O OG  . SER A 1 527 ? 119.369 108.863 112.176 1.00 65.80  ?  443 SER A OG  1 
ATOM   2991 N N   . ILE A 1 528 ? 121.715 106.598 112.471 1.00 57.68  ?  444 ILE A N   1 
ATOM   2992 C CA  . ILE A 1 528 ? 121.599 105.347 113.215 1.00 62.51  ?  444 ILE A CA  1 
ATOM   2993 C C   . ILE A 1 528 ? 122.741 105.211 114.216 1.00 63.85  ?  444 ILE A C   1 
ATOM   2994 O O   . ILE A 1 528 ? 122.538 104.771 115.353 1.00 67.75  ?  444 ILE A O   1 
ATOM   2995 C CB  . ILE A 1 528 ? 121.542 104.154 112.245 1.00 64.46  ?  444 ILE A CB  1 
ATOM   2996 C CG1 . ILE A 1 528 ? 120.242 104.189 111.440 1.00 63.81  ?  444 ILE A CG1 1 
ATOM   2997 C CG2 . ILE A 1 528 ? 121.661 102.841 112.998 1.00 59.76  ?  444 ILE A CG2 1 
ATOM   2998 C CD1 . ILE A 1 528 ? 120.201 103.195 110.305 1.00 61.91  ?  444 ILE A CD1 1 
ATOM   2999 N N   . ILE A 1 529 ? 123.956 105.588 113.813 1.00 53.04  ?  445 ILE A N   1 
ATOM   3000 C CA  . ILE A 1 529 ? 125.100 105.530 114.721 1.00 48.91  ?  445 ILE A CA  1 
ATOM   3001 C C   . ILE A 1 529 ? 124.875 106.443 115.919 1.00 52.82  ?  445 ILE A C   1 
ATOM   3002 O O   . ILE A 1 529 ? 125.148 106.070 117.068 1.00 59.02  ?  445 ILE A O   1 
ATOM   3003 C CB  . ILE A 1 529 ? 126.394 105.889 113.966 1.00 50.16  ?  445 ILE A CB  1 
ATOM   3004 C CG1 . ILE A 1 529 ? 126.977 104.650 113.288 1.00 59.47  ?  445 ILE A CG1 1 
ATOM   3005 C CG2 . ILE A 1 529 ? 127.415 106.512 114.902 1.00 52.35  ?  445 ILE A CG2 1 
ATOM   3006 C CD1 . ILE A 1 529 ? 128.265 104.915 112.547 1.00 57.26  ?  445 ILE A CD1 1 
ATOM   3007 N N   . TYR A 1 530 ? 124.363 107.650 115.675 1.00 56.73  ?  446 TYR A N   1 
ATOM   3008 C CA  . TYR A 1 530 ? 124.134 108.582 116.773 1.00 56.16  ?  446 TYR A CA  1 
ATOM   3009 C C   . TYR A 1 530 ? 122.977 108.135 117.657 1.00 60.18  ?  446 TYR A C   1 
ATOM   3010 O O   . TYR A 1 530 ? 123.000 108.371 118.869 1.00 66.04  ?  446 TYR A O   1 
ATOM   3011 C CB  . TYR A 1 530 ? 123.890 109.982 116.219 1.00 53.88  ?  446 TYR A CB  1 
ATOM   3012 C CG  . TYR A 1 530 ? 125.173 110.723 115.944 1.00 60.52  ?  446 TYR A CG  1 
ATOM   3013 C CD1 . TYR A 1 530 ? 126.142 110.856 116.927 1.00 60.13  ?  446 TYR A CD1 1 
ATOM   3014 C CD2 . TYR A 1 530 ? 125.432 111.262 114.693 1.00 60.67  ?  446 TYR A CD2 1 
ATOM   3015 C CE1 . TYR A 1 530 ? 127.321 111.520 116.677 1.00 57.86  ?  446 TYR A CE1 1 
ATOM   3016 C CE2 . TYR A 1 530 ? 126.608 111.930 114.436 1.00 61.55  ?  446 TYR A CE2 1 
ATOM   3017 C CZ  . TYR A 1 530 ? 127.549 112.056 115.431 1.00 61.69  ?  446 TYR A CZ  1 
ATOM   3018 O OH  . TYR A 1 530 ? 128.725 112.719 115.181 1.00 65.18  ?  446 TYR A OH  1 
ATOM   3019 N N   . PHE A 1 531 ? 121.965 107.485 117.081 1.00 61.63  ?  447 PHE A N   1 
ATOM   3020 C CA  . PHE A 1 531 ? 120.901 106.912 117.899 1.00 55.16  ?  447 PHE A CA  1 
ATOM   3021 C C   . PHE A 1 531 ? 121.432 105.791 118.783 1.00 63.82  ?  447 PHE A C   1 
ATOM   3022 O O   . PHE A 1 531 ? 121.041 105.676 119.950 1.00 71.97  ?  447 PHE A O   1 
ATOM   3023 C CB  . PHE A 1 531 ? 119.766 106.410 117.010 1.00 56.88  ?  447 PHE A CB  1 
ATOM   3024 C CG  . PHE A 1 531 ? 118.704 107.439 116.748 1.00 66.20  ?  447 PHE A CG  1 
ATOM   3025 C CD1 . PHE A 1 531 ? 118.142 108.154 117.790 1.00 62.14  ?  447 PHE A CD1 1 
ATOM   3026 C CD2 . PHE A 1 531 ? 118.269 107.693 115.458 1.00 71.27  ?  447 PHE A CD2 1 
ATOM   3027 C CE1 . PHE A 1 531 ? 117.165 109.103 117.550 1.00 68.13  ?  447 PHE A CE1 1 
ATOM   3028 C CE2 . PHE A 1 531 ? 117.291 108.641 115.212 1.00 64.24  ?  447 PHE A CE2 1 
ATOM   3029 C CZ  . PHE A 1 531 ? 116.739 109.346 116.260 1.00 63.54  ?  447 PHE A CZ  1 
ATOM   3030 N N   . LEU A 1 532 ? 122.325 104.954 118.247 1.00 71.00  ?  448 LEU A N   1 
ATOM   3031 C CA  . LEU A 1 532 ? 122.968 103.936 119.074 1.00 67.58  ?  448 LEU A CA  1 
ATOM   3032 C C   . LEU A 1 532 ? 123.788 104.574 120.186 1.00 64.92  ?  448 LEU A C   1 
ATOM   3033 O O   . LEU A 1 532 ? 123.800 104.082 121.320 1.00 67.58  ?  448 LEU A O   1 
ATOM   3034 C CB  . LEU A 1 532 ? 123.851 103.026 118.219 1.00 64.38  ?  448 LEU A CB  1 
ATOM   3035 C CG  . LEU A 1 532 ? 123.206 102.234 117.081 1.00 67.49  ?  448 LEU A CG  1 
ATOM   3036 C CD1 . LEU A 1 532 ? 124.056 101.026 116.731 1.00 65.50  ?  448 LEU A CD1 1 
ATOM   3037 C CD2 . LEU A 1 532 ? 121.794 101.804 117.451 1.00 72.45  ?  448 LEU A CD2 1 
ATOM   3038 N N   . GLY A 1 533 ? 124.490 105.665 119.878 1.00 66.31  ?  449 GLY A N   1 
ATOM   3039 C CA  . GLY A 1 533 ? 125.236 106.365 120.912 1.00 66.88  ?  449 GLY A CA  1 
ATOM   3040 C C   . GLY A 1 533 ? 124.340 106.925 122.001 1.00 68.40  ?  449 GLY A C   1 
ATOM   3041 O O   . GLY A 1 533 ? 124.664 106.846 123.189 1.00 74.69  ?  449 GLY A O   1 
ATOM   3042 N N   . ALA A 1 534 ? 123.202 107.500 121.611 1.00 67.25  ?  450 ALA A N   1 
ATOM   3043 C CA  . ALA A 1 534 ? 122.256 108.016 122.596 1.00 70.75  ?  450 ALA A CA  1 
ATOM   3044 C C   . ALA A 1 534 ? 121.680 106.892 123.448 1.00 74.91  ?  450 ALA A C   1 
ATOM   3045 O O   . ALA A 1 534 ? 121.494 107.052 124.660 1.00 77.42  ?  450 ALA A O   1 
ATOM   3046 C CB  . ALA A 1 534 ? 121.139 108.788 121.899 1.00 70.12  ?  450 ALA A CB  1 
ATOM   3047 N N   . MET A 1 535 ? 121.386 105.746 122.829 1.00 81.09  ?  451 MET A N   1 
ATOM   3048 C CA  . MET A 1 535 ? 120.897 104.599 123.586 1.00 79.23  ?  451 MET A CA  1 
ATOM   3049 C C   . MET A 1 535 ? 121.947 104.100 124.571 1.00 81.97  ?  451 MET A C   1 
ATOM   3050 O O   . MET A 1 535 ? 121.620 103.738 125.706 1.00 85.13  ?  451 MET A O   1 
ATOM   3051 C CB  . MET A 1 535 ? 120.478 103.481 122.633 1.00 79.67  ?  451 MET A CB  1 
ATOM   3052 C CG  . MET A 1 535 ? 119.102 103.674 122.020 1.00 83.74  ?  451 MET A CG  1 
ATOM   3053 S SD  . MET A 1 535 ? 117.775 103.100 123.097 1.00 94.80  ?  451 MET A SD  1 
ATOM   3054 C CE  . MET A 1 535 ? 116.777 102.167 121.939 1.00 81.22  ?  451 MET A CE  1 
ATOM   3055 N N   . LEU A 1 536 ? 123.213 104.065 124.151 1.00 82.54  ?  452 LEU A N   1 
ATOM   3056 C CA  . LEU A 1 536 ? 124.284 103.666 125.060 1.00 80.78  ?  452 LEU A CA  1 
ATOM   3057 C C   . LEU A 1 536 ? 124.422 104.646 126.217 1.00 80.69  ?  452 LEU A C   1 
ATOM   3058 O O   . LEU A 1 536 ? 124.625 104.236 127.366 1.00 85.54  ?  452 LEU A O   1 
ATOM   3059 C CB  . LEU A 1 536 ? 125.607 103.545 124.303 1.00 79.95  ?  452 LEU A CB  1 
ATOM   3060 C CG  . LEU A 1 536 ? 125.999 102.173 123.747 1.00 82.76  ?  452 LEU A CG  1 
ATOM   3061 C CD1 . LEU A 1 536 ? 126.528 101.290 124.864 1.00 80.60  ?  452 LEU A CD1 1 
ATOM   3062 C CD2 . LEU A 1 536 ? 124.839 101.496 123.032 1.00 82.77  ?  452 LEU A CD2 1 
ATOM   3063 N N   . ASP A 1 537 ? 124.325 105.946 125.934 1.00 83.73  ?  453 ASP A N   1 
ATOM   3064 C CA  . ASP A 1 537 ? 124.408 106.940 127.000 1.00 87.69  ?  453 ASP A CA  1 
ATOM   3065 C C   . ASP A 1 537 ? 123.250 106.797 127.980 1.00 90.62  ?  453 ASP A C   1 
ATOM   3066 O O   . ASP A 1 537 ? 123.438 106.914 129.196 1.00 90.55  ?  453 ASP A O   1 
ATOM   3067 C CB  . ASP A 1 537 ? 124.439 108.348 126.406 1.00 92.64  ?  453 ASP A CB  1 
ATOM   3068 C CG  . ASP A 1 537 ? 125.851 108.861 126.197 1.00 97.87  ?  453 ASP A CG  1 
ATOM   3069 O OD1 . ASP A 1 537 ? 126.750 108.038 125.923 1.00 95.89  ?  453 ASP A OD1 1 
ATOM   3070 O OD2 . ASP A 1 537 ? 126.062 110.087 126.308 1.00 98.17  -1 453 ASP A OD2 1 
ATOM   3071 N N   . GLY A 1 538 ? 122.043 106.551 127.469 1.00 88.52  ?  454 GLY A N   1 
ATOM   3072 C CA  . GLY A 1 538 ? 120.904 106.362 128.351 1.00 87.48  ?  454 GLY A CA  1 
ATOM   3073 C C   . GLY A 1 538 ? 121.001 105.095 129.179 1.00 88.26  ?  454 GLY A C   1 
ATOM   3074 O O   . GLY A 1 538 ? 120.635 105.083 130.357 1.00 90.70  ?  454 GLY A O   1 
ATOM   3075 N N   . LEU A 1 539 ? 121.493 104.010 128.576 1.00 86.49  ?  455 LEU A N   1 
ATOM   3076 C CA  . LEU A 1 539 ? 121.590 102.741 129.290 1.00 89.17  ?  455 LEU A CA  1 
ATOM   3077 C C   . LEU A 1 539 ? 122.624 102.793 130.406 1.00 91.04  ?  455 LEU A C   1 
ATOM   3078 O O   . LEU A 1 539 ? 122.455 102.131 131.435 1.00 90.45  ?  455 LEU A O   1 
ATOM   3079 C CB  . LEU A 1 539 ? 121.927 101.613 128.314 1.00 87.63  ?  455 LEU A CB  1 
ATOM   3080 C CG  . LEU A 1 539 ? 120.801 100.634 127.982 1.00 87.92  ?  455 LEU A CG  1 
ATOM   3081 C CD1 . LEU A 1 539 ? 119.787 101.276 127.050 1.00 87.66  ?  455 LEU A CD1 1 
ATOM   3082 C CD2 . LEU A 1 539 ? 121.363 99.360  127.373 1.00 86.60  ?  455 LEU A CD2 1 
ATOM   3083 N N   . ARG A 1 540 ? 123.694 103.567 130.226 1.00 91.42  ?  456 ARG A N   1 
ATOM   3084 C CA  . ARG A 1 540 ? 124.763 103.667 131.208 1.00 90.78  ?  456 ARG A CA  1 
ATOM   3085 C C   . ARG A 1 540 ? 124.494 104.743 132.256 1.00 92.49  ?  456 ARG A C   1 
ATOM   3086 O O   . ARG A 1 540 ? 125.401 105.108 133.013 1.00 95.94  ?  456 ARG A O   1 
ATOM   3087 C CB  . ARG A 1 540 ? 126.100 103.908 130.501 1.00 89.85  ?  456 ARG A CB  1 
ATOM   3088 C CG  . ARG A 1 540 ? 126.402 105.358 130.149 1.00 93.71  ?  456 ARG A CG  1 
ATOM   3089 C CD  . ARG A 1 540 ? 127.888 105.556 129.896 1.00 91.81  ?  456 ARG A CD  1 
ATOM   3090 N NE  . ARG A 1 540 ? 128.360 104.737 128.786 1.00 94.14  ?  456 ARG A NE  1 
ATOM   3091 C CZ  . ARG A 1 540 ? 129.297 103.803 128.889 1.00 93.89  ?  456 ARG A CZ  1 
ATOM   3092 N NH1 . ARG A 1 540 ? 129.890 103.544 130.042 1.00 94.43  1  456 ARG A NH1 1 
ATOM   3093 N NH2 . ARG A 1 540 ? 129.645 103.111 127.808 1.00 90.88  ?  456 ARG A NH2 1 
ATOM   3094 N N   . HIS A 1 541 ? 123.257 105.248 132.283 1.00 95.18  ?  457 HIS A N   1 
ATOM   3095 C CA  . HIS A 1 541 ? 122.883 106.310 133.257 1.00 99.06  ?  457 HIS A CA  1 
ATOM   3096 C C   . HIS A 1 541 ? 121.937 105.714 134.304 1.00 101.88 ?  457 HIS A C   1 
ATOM   3097 O O   . HIS A 1 541 ? 120.900 105.163 133.875 1.00 98.07  ?  457 HIS A O   1 
ATOM   3098 C CB  . HIS A 1 541 ? 122.254 107.501 132.527 1.00 98.12  ?  457 HIS A CB  1 
ATOM   3099 C CG  . HIS A 1 541 ? 122.025 108.697 133.390 1.00 103.17 ?  457 HIS A CG  1 
ATOM   3100 N ND1 . HIS A 1 541 ? 121.435 109.850 132.919 1.00 104.65 ?  457 HIS A ND1 1 
ATOM   3101 C CD2 . HIS A 1 541 ? 122.298 108.923 134.682 1.00 101.75 ?  457 HIS A CD2 1 
ATOM   3102 C CE1 . HIS A 1 541 ? 121.361 110.736 133.901 1.00 103.11 ?  457 HIS A CE1 1 
ATOM   3103 N NE2 . HIS A 1 541 ? 121.879 110.194 134.981 1.00 101.75 ?  457 HIS A NE2 1 
HETATM 3104 C C3  . COP B 2 .   ? 135.740 129.565 89.385  1.00 20.00  ?  701 COP A C3  1 
HETATM 3105 C C1  . COP B 2 .   ? 136.243 129.770 91.624  1.00 20.00  ?  701 COP A C1  1 
HETATM 3106 C C10 . COP B 2 .   ? 134.910 130.041 91.881  1.00 20.00  ?  701 COP A C10 1 
HETATM 3107 C C8  . COP B 2 .   ? 133.223 130.547 93.330  1.00 20.00  ?  701 COP A C8  1 
HETATM 3108 C C7  . COP B 2 .   ? 132.315 130.562 92.266  1.00 20.00  ?  701 COP A C7  1 
HETATM 3109 C C5  . COP B 2 .   ? 134.003 130.062 90.817  1.00 20.00  ?  701 COP A C5  1 
HETATM 3110 C C11 . COP B 2 .   ? 132.777 130.818 94.736  1.00 20.00  ?  701 COP A C11 1 
HETATM 3111 C C13 . COP B 2 .   ? 131.793 129.386 96.476  1.00 20.00  ?  701 COP A C13 1 
HETATM 3112 C C18 . COP B 2 .   ? 130.689 129.753 97.225  1.00 20.00  ?  701 COP A C18 1 
HETATM 3113 C C17 . COP B 2 .   ? 130.587 129.346 98.532  1.00 20.00  ?  701 COP A C17 1 
HETATM 3114 C C16 . COP B 2 .   ? 131.584 128.583 99.113  1.00 20.00  ?  701 COP A C16 1 
HETATM 3115 C C15 . COP B 2 .   ? 132.680 128.201 98.359  1.00 20.00  ?  701 COP A C15 1 
HETATM 3116 C C14 . COP B 2 .   ? 132.791 128.609 97.051  1.00 20.00  ?  701 COP A C14 1 
HETATM 3117 C C19 . COP B 2 .   ? 131.372 128.162 100.530 1.00 20.00  ?  701 COP A C19 1 
HETATM 3118 C C21 . COP B 2 .   ? 129.589 128.046 102.211 1.00 20.00  ?  701 COP A C21 1 
HETATM 3119 C C24 . COP B 2 .   ? 128.135 127.568 102.185 1.00 20.00  ?  701 COP A C24 1 
HETATM 3120 C C27 . COP B 2 .   ? 129.696 129.481 102.709 1.00 20.00  ?  701 COP A C27 1 
HETATM 3121 C C28 . COP B 2 .   ? 128.869 129.746 103.955 1.00 20.00  ?  701 COP A C28 1 
HETATM 3122 C C29 . COP B 2 .   ? 129.268 131.073 104.548 1.00 20.00  ?  701 COP A C29 1 
HETATM 3123 N N4  . COP B 2 .   ? 134.432 129.823 89.552  1.00 20.00  ?  701 COP A N4  1 
HETATM 3124 N N3  . COP B 2 .   ? 136.167 129.307 88.150  1.00 20.00  ?  701 COP A N3  1 
HETATM 3125 N N2  . COP B 2 .   ? 136.646 129.534 90.377  1.00 20.00  ?  701 COP A N2  1 
HETATM 3126 N N1  . COP B 2 .   ? 137.136 129.735 92.619  1.00 20.00  ?  701 COP A N1  1 
HETATM 3127 N N9  . COP B 2 .   ? 134.489 130.276 93.151  1.00 20.00  ?  701 COP A N9  1 
HETATM 3128 N N6  . COP B 2 .   ? 132.687 130.323 91.026  1.00 20.00  ?  701 COP A N6  1 
HETATM 3129 N N12 . COP B 2 .   ? 131.889 129.791 95.179  1.00 20.00  ?  701 COP A N12 1 
HETATM 3130 N N20 . COP B 2 .   ? 130.105 127.923 100.863 1.00 20.00  ?  701 COP A N20 1 
HETATM 3131 O O19 . COP B 2 .   ? 132.313 128.019 101.300 1.00 20.00  ?  701 COP A O19 1 
HETATM 3132 O O24 . COP B 2 .   ? 127.525 127.751 101.126 1.00 20.00  ?  701 COP A O24 1 
HETATM 3133 O O25 . COP B 2 .   ? 127.684 127.007 103.196 1.00 20.00  ?  701 COP A O25 1 
HETATM 3134 N N30 . COP B 2 .   ? 129.710 130.942 105.924 1.00 20.00  ?  701 COP A N30 1 
HETATM 3135 C C31 . COP B 2 .   ? 130.935 130.526 106.217 1.00 20.00  ?  701 COP A C31 1 
HETATM 3136 O O32 . COP B 2 .   ? 131.315 129.390 105.965 1.00 20.00  ?  701 COP A O32 1 
HETATM 3137 C C33 . COP B 2 .   ? 131.838 131.534 106.881 1.00 20.00  ?  701 COP A C33 1 
HETATM 3138 C C38 . COP B 2 .   ? 132.308 131.364 108.185 1.00 20.00  ?  701 COP A C38 1 
HETATM 3139 C C37 . COP B 2 .   ? 133.135 132.333 108.735 1.00 20.00  ?  701 COP A C37 1 
HETATM 3140 C C36 . COP B 2 .   ? 133.491 133.453 108.020 1.00 20.00  ?  701 COP A C36 1 
HETATM 3141 C C35 . COP B 2 .   ? 133.028 133.619 106.739 1.00 20.00  ?  701 COP A C35 1 
HETATM 3142 C C34 . COP B 2 .   ? 132.209 132.668 106.170 1.00 20.00  ?  701 COP A C34 1 
HETATM 3143 C C39 . COP B 2 .   ? 131.959 130.171 109.011 1.00 20.00  ?  701 COP A C39 1 
HETATM 3144 O O40 . COP B 2 .   ? 132.328 129.055 108.715 1.00 20.00  ?  701 COP A O40 1 
HETATM 3145 O O41 . COP B 2 .   ? 131.229 130.472 110.084 1.00 20.00  ?  701 COP A O41 1 
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