data_9BW3
# 
_entry.id   9BW3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BW3         pdb_00009bw3 10.2210/pdb9bw3/pdb 
WWPDB D_1000284238 ?            ?                   
EMDB  EMD-44947    ?            ?                   
# 
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 2025-03-19 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 2 '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 2 'Structure model' '_citation.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 '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                        9BW3 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        
'Consensus model for preturnover condition of Bacillus subtilis ribonucleotide reductase complex' 
_pdbx_database_related.db_id          EMD-44947 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              nozomi.ando@cornell.edu 
_pdbx_contact_author.name_first         Nozomi 
_pdbx_contact_author.name_last          Ando 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7062-1644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, D.'       1 0000-0002-3879-039X 
'Thomas, W.C.' 2 0000-0001-5490-4900 
'Burnim, A.A.' 3 0000-0002-9962-1397 
'Ando, N.'     4 0000-0001-7062-1644 
# 
_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                2458 
_citation.page_last                 2458 
_citation.title                     
'Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57735-4 
_citation.pdbx_database_id_PubMed   40075098 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, D.'       1 ? 
primary 'Thomas, W.C.' 2 ? 
primary 'Burnim, A.A.' 3 ? 
primary 'Ando, N.'     4 ? 
# 
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 'Ribonucleoside-diphosphate reductase subunit alpha' 80791.469 2 1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase subunit beta'  40720.992 2 1.17.4.1 ? ? ? 
3 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                          482.168   2 ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                      24.305    2 ?        ? ? ? 
5 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                          507.181   2 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Ribonucleotide reductase large subunit' 
2 'Ribonucleotide reductase small subunit' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
A,B ? 
2 'polypeptide(L)' no no 
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "THYMIDINE-5'-TRIPHOSPHATE" TTP 
4 'MAGNESIUM ION'             MG  
5 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
# 
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   SER n 
1 3   GLN n 
1 4   ASN n 
1 5   GLN n 
1 6   VAL n 
1 7   PRO n 
1 8   LYS n 
1 9   TRP n 
1 10  ILE n 
1 11  GLN n 
1 12  LEU n 
1 13  ASN n 
1 14  ASN n 
1 15  GLU n 
1 16  ILE n 
1 17  MET n 
1 18  ILE n 
1 19  GLN n 
1 20  LYS n 
1 21  ASP n 
1 22  GLY n 
1 23  LYS n 
1 24  PHE n 
1 25  GLN n 
1 26  PHE n 
1 27  ASP n 
1 28  LYS n 
1 29  ASP n 
1 30  LYS n 
1 31  GLU n 
1 32  ALA n 
1 33  VAL n 
1 34  HIS n 
1 35  SER n 
1 36  TYR n 
1 37  PHE n 
1 38  VAL n 
1 39  ASP n 
1 40  TYR n 
1 41  ILE n 
1 42  ASN n 
1 43  GLN n 
1 44  ASN n 
1 45  THR n 
1 46  VAL n 
1 47  PHE n 
1 48  PHE n 
1 49  HIS n 
1 50  ASN n 
1 51  LEU n 
1 52  LYS n 
1 53  GLU n 
1 54  LYS n 
1 55  LEU n 
1 56  ASP n 
1 57  TYR n 
1 58  LEU n 
1 59  VAL n 
1 60  GLU n 
1 61  ASN n 
1 62  GLN n 
1 63  TYR n 
1 64  TYR n 
1 65  GLU n 
1 66  GLU n 
1 67  GLU n 
1 68  PHE n 
1 69  LEU n 
1 70  SER n 
1 71  LEU n 
1 72  TYR n 
1 73  SER n 
1 74  PHE n 
1 75  GLU n 
1 76  ASP n 
1 77  ILE n 
1 78  LYS n 
1 79  GLU n 
1 80  VAL n 
1 81  PHE n 
1 82  LYS n 
1 83  THR n 
1 84  ALA n 
1 85  TYR n 
1 86  ALA n 
1 87  LYS n 
1 88  LYS n 
1 89  PHE n 
1 90  ARG n 
1 91  PHE n 
1 92  PRO n 
1 93  SER n 
1 94  PHE n 
1 95  MET n 
1 96  SER n 
1 97  ALA n 
1 98  PHE n 
1 99  LYS n 
1 100 PHE n 
1 101 TYR n 
1 102 ASN n 
1 103 ASP n 
1 104 TYR n 
1 105 ALA n 
1 106 LEU n 
1 107 LYS n 
1 108 THR n 
1 109 ASN n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 ARG n 
1 118 TYR n 
1 119 GLU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 SER n 
1 124 ILE n 
1 125 VAL n 
1 126 ALA n 
1 127 LEU n 
1 128 PHE n 
1 129 PHE n 
1 130 ALA n 
1 131 ASN n 
1 132 GLY n 
1 133 ASP n 
1 134 THR n 
1 135 GLU n 
1 136 LYS n 
1 137 ALA n 
1 138 LYS n 
1 139 GLU n 
1 140 TYR n 
1 141 VAL n 
1 142 ASN n 
1 143 LEU n 
1 144 MET n 
1 145 ILE n 
1 146 ASN n 
1 147 GLN n 
1 148 GLU n 
1 149 TYR n 
1 150 GLN n 
1 151 PRO n 
1 152 SER n 
1 153 THR n 
1 154 PRO n 
1 155 THR n 
1 156 PHE n 
1 157 LEU n 
1 158 ASN n 
1 159 ALA n 
1 160 GLY n 
1 161 ARG n 
1 162 LYS n 
1 163 ARG n 
1 164 ARG n 
1 165 GLY n 
1 166 GLU n 
1 167 LEU n 
1 168 VAL n 
1 169 SER n 
1 170 CYS n 
1 171 PHE n 
1 172 LEU n 
1 173 LEU n 
1 174 GLU n 
1 175 VAL n 
1 176 ASN n 
1 177 ASP n 
1 178 SER n 
1 179 LEU n 
1 180 ASN n 
1 181 ASP n 
1 182 ILE n 
1 183 SER n 
1 184 ARG n 
1 185 ALA n 
1 186 ILE n 
1 187 ASP n 
1 188 ILE n 
1 189 SER n 
1 190 MET n 
1 191 GLN n 
1 192 LEU n 
1 193 SER n 
1 194 LYS n 
1 195 LEU n 
1 196 GLY n 
1 197 GLY n 
1 198 GLY n 
1 199 VAL n 
1 200 SER n 
1 201 LEU n 
1 202 ASN n 
1 203 LEU n 
1 204 SER n 
1 205 LYS n 
1 206 LEU n 
1 207 ARG n 
1 208 ALA n 
1 209 LYS n 
1 210 GLY n 
1 211 GLU n 
1 212 ALA n 
1 213 ILE n 
1 214 LYS n 
1 215 ASP n 
1 216 VAL n 
1 217 GLU n 
1 218 ASN n 
1 219 ALA n 
1 220 THR n 
1 221 LYS n 
1 222 GLY n 
1 223 VAL n 
1 224 VAL n 
1 225 GLY n 
1 226 VAL n 
1 227 MET n 
1 228 LYS n 
1 229 LEU n 
1 230 LEU n 
1 231 ASP n 
1 232 ASN n 
1 233 ALA n 
1 234 PHE n 
1 235 ARG n 
1 236 TYR n 
1 237 ALA n 
1 238 ASP n 
1 239 GLN n 
1 240 MET n 
1 241 GLY n 
1 242 GLN n 
1 243 ARG n 
1 244 GLN n 
1 245 GLY n 
1 246 SER n 
1 247 GLY n 
1 248 ALA n 
1 249 ALA n 
1 250 TYR n 
1 251 LEU n 
1 252 ASN n 
1 253 ILE n 
1 254 PHE n 
1 255 HIS n 
1 256 ARG n 
1 257 ASP n 
1 258 ILE n 
1 259 ASN n 
1 260 ASP n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 THR n 
1 265 LYS n 
1 266 LYS n 
1 267 ILE n 
1 268 SER n 
1 269 ALA n 
1 270 ASP n 
1 271 GLU n 
1 272 ASP n 
1 273 VAL n 
1 274 ARG n 
1 275 VAL n 
1 276 LYS n 
1 277 THR n 
1 278 LEU n 
1 279 SER n 
1 280 ILE n 
1 281 GLY n 
1 282 VAL n 
1 283 VAL n 
1 284 ILE n 
1 285 PRO n 
1 286 ASP n 
1 287 LYS n 
1 288 PHE n 
1 289 VAL n 
1 290 GLU n 
1 291 LEU n 
1 292 ALA n 
1 293 ARG n 
1 294 GLU n 
1 295 ASP n 
1 296 LYS n 
1 297 ALA n 
1 298 ALA n 
1 299 TYR n 
1 300 VAL n 
1 301 PHE n 
1 302 TYR n 
1 303 PRO n 
1 304 HIS n 
1 305 THR n 
1 306 ILE n 
1 307 TYR n 
1 308 LYS n 
1 309 GLU n 
1 310 TYR n 
1 311 GLY n 
1 312 GLN n 
1 313 HIS n 
1 314 MET n 
1 315 ASP n 
1 316 GLU n 
1 317 MET n 
1 318 ASP n 
1 319 MET n 
1 320 ASN n 
1 321 GLU n 
1 322 MET n 
1 323 TYR n 
1 324 ASP n 
1 325 LYS n 
1 326 PHE n 
1 327 VAL n 
1 328 ASP n 
1 329 ASN n 
1 330 PRO n 
1 331 ARG n 
1 332 VAL n 
1 333 LYS n 
1 334 LYS n 
1 335 GLU n 
1 336 LYS n 
1 337 ILE n 
1 338 ASN n 
1 339 PRO n 
1 340 ARG n 
1 341 LYS n 
1 342 LEU n 
1 343 LEU n 
1 344 GLU n 
1 345 LYS n 
1 346 LEU n 
1 347 ALA n 
1 348 MET n 
1 349 LEU n 
1 350 ARG n 
1 351 SER n 
1 352 GLU n 
1 353 SER n 
1 354 GLY n 
1 355 TYR n 
1 356 PRO n 
1 357 TYR n 
1 358 ILE n 
1 359 MET n 
1 360 PHE n 
1 361 GLN n 
1 362 ASP n 
1 363 ASN n 
1 364 VAL n 
1 365 ASN n 
1 366 LYS n 
1 367 VAL n 
1 368 HIS n 
1 369 ALA n 
1 370 ASN n 
1 371 ASN n 
1 372 HIS n 
1 373 ILE n 
1 374 SER n 
1 375 LYS n 
1 376 VAL n 
1 377 LYS n 
1 378 PHE n 
1 379 SER n 
1 380 ASN n 
1 381 LEU n 
1 382 CYS n 
1 383 SER n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 ALA n 
1 389 SER n 
1 390 GLN n 
1 391 VAL n 
1 392 SER n 
1 393 SER n 
1 394 TYR n 
1 395 THR n 
1 396 ASP n 
1 397 TYR n 
1 398 ASP n 
1 399 GLU n 
1 400 GLU n 
1 401 ASP n 
1 402 GLU n 
1 403 ILE n 
1 404 GLY n 
1 405 LEU n 
1 406 ASP n 
1 407 ILE n 
1 408 SER n 
1 409 CYS n 
1 410 ASN n 
1 411 LEU n 
1 412 GLY n 
1 413 SER n 
1 414 LEU n 
1 415 ASN n 
1 416 ILE n 
1 417 LEU n 
1 418 ASN n 
1 419 VAL n 
1 420 MET n 
1 421 GLU n 
1 422 HIS n 
1 423 LYS n 
1 424 SER n 
1 425 ILE n 
1 426 GLU n 
1 427 LYS n 
1 428 THR n 
1 429 VAL n 
1 430 LYS n 
1 431 LEU n 
1 432 ALA n 
1 433 THR n 
1 434 ASP n 
1 435 SER n 
1 436 LEU n 
1 437 THR n 
1 438 HIS n 
1 439 VAL n 
1 440 SER n 
1 441 GLU n 
1 442 THR n 
1 443 THR n 
1 444 ASP n 
1 445 ILE n 
1 446 ARG n 
1 447 ASN n 
1 448 ALA n 
1 449 PRO n 
1 450 ALA n 
1 451 VAL n 
1 452 ARG n 
1 453 ARG n 
1 454 ALA n 
1 455 ASN n 
1 456 LYS n 
1 457 ALA n 
1 458 MET n 
1 459 LYS n 
1 460 SER n 
1 461 ILE n 
1 462 GLY n 
1 463 LEU n 
1 464 GLY n 
1 465 ALA n 
1 466 MET n 
1 467 ASN n 
1 468 LEU n 
1 469 HIS n 
1 470 GLY n 
1 471 TYR n 
1 472 LEU n 
1 473 ALA n 
1 474 GLN n 
1 475 ASN n 
1 476 GLY n 
1 477 ILE n 
1 478 ALA n 
1 479 TYR n 
1 480 GLU n 
1 481 SER n 
1 482 PRO n 
1 483 GLU n 
1 484 ALA n 
1 485 ARG n 
1 486 ASP n 
1 487 PHE n 
1 488 ALA n 
1 489 ASN n 
1 490 THR n 
1 491 PHE n 
1 492 PHE n 
1 493 MET n 
1 494 MET n 
1 495 VAL n 
1 496 ASN n 
1 497 PHE n 
1 498 TYR n 
1 499 SER n 
1 500 ILE n 
1 501 GLN n 
1 502 ARG n 
1 503 SER n 
1 504 ALA n 
1 505 GLU n 
1 506 ILE n 
1 507 ALA n 
1 508 LYS n 
1 509 GLU n 
1 510 LYS n 
1 511 GLY n 
1 512 GLU n 
1 513 THR n 
1 514 PHE n 
1 515 ASP n 
1 516 GLN n 
1 517 TYR n 
1 518 GLU n 
1 519 GLY n 
1 520 SER n 
1 521 THR n 
1 522 TYR n 
1 523 ALA n 
1 524 THR n 
1 525 GLY n 
1 526 GLU n 
1 527 TYR n 
1 528 PHE n 
1 529 ASP n 
1 530 LYS n 
1 531 TYR n 
1 532 VAL n 
1 533 SER n 
1 534 THR n 
1 535 ASP n 
1 536 PHE n 
1 537 SER n 
1 538 PRO n 
1 539 LYS n 
1 540 TYR n 
1 541 GLU n 
1 542 LYS n 
1 543 ILE n 
1 544 ALA n 
1 545 ASN n 
1 546 LEU n 
1 547 PHE n 
1 548 GLU n 
1 549 GLY n 
1 550 MET n 
1 551 HIS n 
1 552 ILE n 
1 553 PRO n 
1 554 THR n 
1 555 THR n 
1 556 GLU n 
1 557 ASP n 
1 558 TRP n 
1 559 LYS n 
1 560 LYS n 
1 561 LEU n 
1 562 LYS n 
1 563 ALA n 
1 564 PHE n 
1 565 VAL n 
1 566 ALA n 
1 567 GLU n 
1 568 HIS n 
1 569 GLY n 
1 570 MET n 
1 571 TYR n 
1 572 HIS n 
1 573 SER n 
1 574 TYR n 
1 575 ARG n 
1 576 LEU n 
1 577 CYS n 
1 578 ILE n 
1 579 ALA n 
1 580 PRO n 
1 581 THR n 
1 582 GLY n 
1 583 SER n 
1 584 ILE n 
1 585 SER n 
1 586 TYR n 
1 587 VAL n 
1 588 GLN n 
1 589 SER n 
1 590 SER n 
1 591 THR n 
1 592 ALA n 
1 593 SER n 
1 594 VAL n 
1 595 MET n 
1 596 PRO n 
1 597 ILE n 
1 598 MET n 
1 599 GLU n 
1 600 ARG n 
1 601 ILE n 
1 602 GLU n 
1 603 GLU n 
1 604 ARG n 
1 605 THR n 
1 606 TYR n 
1 607 GLY n 
1 608 ASN n 
1 609 SER n 
1 610 LYS n 
1 611 THR n 
1 612 TYR n 
1 613 TYR n 
1 614 PRO n 
1 615 MET n 
1 616 PRO n 
1 617 GLY n 
1 618 LEU n 
1 619 ALA n 
1 620 SER n 
1 621 ASN n 
1 622 ASN n 
1 623 TRP n 
1 624 PHE n 
1 625 PHE n 
1 626 TYR n 
1 627 LYS n 
1 628 GLU n 
1 629 ALA n 
1 630 TYR n 
1 631 ASP n 
1 632 MET n 
1 633 ASP n 
1 634 MET n 
1 635 PHE n 
1 636 LYS n 
1 637 VAL n 
1 638 VAL n 
1 639 ASP n 
1 640 MET n 
1 641 ILE n 
1 642 ALA n 
1 643 THR n 
1 644 ILE n 
1 645 GLN n 
1 646 GLN n 
1 647 HIS n 
1 648 ILE n 
1 649 ASP n 
1 650 GLN n 
1 651 GLY n 
1 652 ILE n 
1 653 SER n 
1 654 PHE n 
1 655 THR n 
1 656 LEU n 
1 657 PHE n 
1 658 LEU n 
1 659 LYS n 
1 660 ASP n 
1 661 THR n 
1 662 MET n 
1 663 THR n 
1 664 THR n 
1 665 ARG n 
1 666 ASP n 
1 667 LEU n 
1 668 ASN n 
1 669 ARG n 
1 670 ILE n 
1 671 ASP n 
1 672 LEU n 
1 673 TYR n 
1 674 ALA n 
1 675 HIS n 
1 676 HIS n 
1 677 ARG n 
1 678 GLY n 
1 679 ILE n 
1 680 LYS n 
1 681 THR n 
1 682 ILE n 
1 683 TYR n 
1 684 TYR n 
1 685 ALA n 
1 686 ARG n 
1 687 THR n 
1 688 LYS n 
1 689 ASP n 
1 690 THR n 
1 691 GLY n 
1 692 GLN n 
1 693 ASP n 
1 694 SER n 
1 695 CYS n 
1 696 LEU n 
1 697 SER n 
1 698 CYS n 
1 699 VAL n 
1 700 VAL n 
2 1   MET n 
2 2   GLY n 
2 3   SER n 
2 4   SER n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  HIS n 
2 11  SER n 
2 12  SER n 
2 13  GLY n 
2 14  LEU n 
2 15  VAL n 
2 16  PRO n 
2 17  ARG n 
2 18  GLY n 
2 19  SER n 
2 20  HIS n 
2 21  MET n 
2 22  MET n 
2 23  THR n 
2 24  LYS n 
2 25  ILE n 
2 26  TYR n 
2 27  ASP n 
2 28  ALA n 
2 29  ALA n 
2 30  ASN n 
2 31  TRP n 
2 32  SER n 
2 33  LYS n 
2 34  HIS n 
2 35  GLU n 
2 36  ASP n 
2 37  ASP n 
2 38  PHE n 
2 39  THR n 
2 40  GLN n 
2 41  MET n 
2 42  PHE n 
2 43  TYR n 
2 44  ASN n 
2 45  GLN n 
2 46  ASN n 
2 47  VAL n 
2 48  LYS n 
2 49  GLN n 
2 50  PHE n 
2 51  TRP n 
2 52  LEU n 
2 53  PRO n 
2 54  GLU n 
2 55  GLU n 
2 56  ILE n 
2 57  ALA n 
2 58  LEU n 
2 59  ASN n 
2 60  GLY n 
2 61  ASP n 
2 62  LEU n 
2 63  LEU n 
2 64  THR n 
2 65  TRP n 
2 66  LYS n 
2 67  TYR n 
2 68  LEU n 
2 69  GLY n 
2 70  LYS n 
2 71  ASN n 
2 72  GLU n 
2 73  GLN n 
2 74  ASP n 
2 75  THR n 
2 76  TYR n 
2 77  MET n 
2 78  LYS n 
2 79  VAL n 
2 80  LEU n 
2 81  ALA n 
2 82  GLY n 
2 83  LEU n 
2 84  THR n 
2 85  LEU n 
2 86  LEU n 
2 87  ASP n 
2 88  THR n 
2 89  GLU n 
2 90  GLN n 
2 91  GLY n 
2 92  ASN n 
2 93  THR n 
2 94  GLY n 
2 95  MET n 
2 96  PRO n 
2 97  ILE n 
2 98  VAL n 
2 99  ALA n 
2 100 GLU n 
2 101 HIS n 
2 102 VAL n 
2 103 ASP n 
2 104 GLY n 
2 105 HIS n 
2 106 GLN n 
2 107 ARG n 
2 108 LYS n 
2 109 ALA n 
2 110 VAL n 
2 111 LEU n 
2 112 ASN n 
2 113 PHE n 
2 114 MET n 
2 115 ALA n 
2 116 MET n 
2 117 MET n 
2 118 GLU n 
2 119 ASN n 
2 120 ALA n 
2 121 VAL n 
2 122 HIS n 
2 123 ALA n 
2 124 LYS n 
2 125 SER n 
2 126 TYR n 
2 127 SER n 
2 128 ASN n 
2 129 ILE n 
2 130 PHE n 
2 131 MET n 
2 132 THR n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 THR n 
2 137 GLU n 
2 138 THR n 
2 139 ILE n 
2 140 ASN n 
2 141 GLU n 
2 142 VAL n 
2 143 PHE n 
2 144 GLU n 
2 145 TRP n 
2 146 VAL n 
2 147 LYS n 
2 148 GLN n 
2 149 ASN n 
2 150 LYS n 
2 151 TYR n 
2 152 LEU n 
2 153 GLN n 
2 154 LYS n 
2 155 LYS n 
2 156 ALA n 
2 157 GLN n 
2 158 MET n 
2 159 ILE n 
2 160 VAL n 
2 161 GLY n 
2 162 LEU n 
2 163 TYR n 
2 164 LYS n 
2 165 ALA n 
2 166 ILE n 
2 167 GLN n 
2 168 LYS n 
2 169 ASP n 
2 170 ASP n 
2 171 GLU n 
2 172 ILE n 
2 173 SER n 
2 174 LEU n 
2 175 PHE n 
2 176 LYS n 
2 177 ALA n 
2 178 MET n 
2 179 VAL n 
2 180 ALA n 
2 181 SER n 
2 182 VAL n 
2 183 TYR n 
2 184 LEU n 
2 185 GLU n 
2 186 SER n 
2 187 PHE n 
2 188 LEU n 
2 189 PHE n 
2 190 TYR n 
2 191 SER n 
2 192 GLY n 
2 193 PHE n 
2 194 TYR n 
2 195 TYR n 
2 196 PRO n 
2 197 LEU n 
2 198 TYR n 
2 199 PHE n 
2 200 TYR n 
2 201 GLY n 
2 202 GLN n 
2 203 GLY n 
2 204 LYS n 
2 205 LEU n 
2 206 MET n 
2 207 GLN n 
2 208 SER n 
2 209 GLY n 
2 210 GLU n 
2 211 ILE n 
2 212 ILE n 
2 213 ASN n 
2 214 LEU n 
2 215 ILE n 
2 216 LEU n 
2 217 ARG n 
2 218 ASP n 
2 219 GLU n 
2 220 ALA n 
2 221 ILE n 
2 222 HIS n 
2 223 GLY n 
2 224 VAL n 
2 225 TYR n 
2 226 VAL n 
2 227 GLY n 
2 228 LEU n 
2 229 LEU n 
2 230 ALA n 
2 231 GLN n 
2 232 GLU n 
2 233 ILE n 
2 234 TYR n 
2 235 ASN n 
2 236 LYS n 
2 237 GLN n 
2 238 THR n 
2 239 GLU n 
2 240 GLU n 
2 241 LYS n 
2 242 LYS n 
2 243 ALA n 
2 244 GLU n 
2 245 LEU n 
2 246 ARG n 
2 247 GLU n 
2 248 PHE n 
2 249 ALA n 
2 250 ILE n 
2 251 ASP n 
2 252 LEU n 
2 253 LEU n 
2 254 ASN n 
2 255 GLN n 
2 256 LEU n 
2 257 TYR n 
2 258 GLU n 
2 259 ASN n 
2 260 GLU n 
2 261 LEU n 
2 262 GLU n 
2 263 TYR n 
2 264 THR n 
2 265 GLU n 
2 266 ASP n 
2 267 LEU n 
2 268 TYR n 
2 269 ASP n 
2 270 GLN n 
2 271 VAL n 
2 272 GLY n 
2 273 LEU n 
2 274 SER n 
2 275 HIS n 
2 276 ASP n 
2 277 VAL n 
2 278 LYS n 
2 279 LYS n 
2 280 PHE n 
2 281 ILE n 
2 282 ARG n 
2 283 TYR n 
2 284 ASN n 
2 285 ALA n 
2 286 ASN n 
2 287 LYS n 
2 288 ALA n 
2 289 LEU n 
2 290 MET n 
2 291 ASN n 
2 292 LEU n 
2 293 GLY n 
2 294 PHE n 
2 295 ASP n 
2 296 PRO n 
2 297 TYR n 
2 298 PHE n 
2 299 GLU n 
2 300 GLU n 
2 301 GLU n 
2 302 ASP n 
2 303 ILE n 
2 304 ASN n 
2 305 PRO n 
2 306 ILE n 
2 307 VAL n 
2 308 LEU n 
2 309 ASN n 
2 310 GLY n 
2 311 LEU n 
2 312 ASN n 
2 313 THR n 
2 314 LYS n 
2 315 THR n 
2 316 LYS n 
2 317 SER n 
2 318 HIS n 
2 319 ASP n 
2 320 PHE n 
2 321 PHE n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLY n 
2 326 ASN n 
2 327 GLY n 
2 328 TYR n 
2 329 LYS n 
2 330 LYS n 
2 331 ALA n 
2 332 THR n 
2 333 VAL n 
2 334 GLU n 
2 335 PRO n 
2 336 LEU n 
2 337 LYS n 
2 338 ASP n 
2 339 ASP n 
2 340 ASP n 
2 341 PHE n 
2 342 TYR n 
2 343 PHE n 
2 344 GLU n 
2 345 ASP n 
2 346 GLU n 
2 347 LYS n 
2 348 GLU n 
2 349 GLN n 
2 350 ILE 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' 1 700 ? ? 'nrdE, nrdA, BSU17380' ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 ? ? 'nrdF, BSU17390'       ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
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 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
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 
TTP non-polymer         . "THYMIDINE-5'-TRIPHOSPHATE" ? 'C10 H17 N2 O14 P3' 482.168 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 CYS 170 170 170 CYS CYS A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 PHE 288 288 288 PHE PHE A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 TYR 307 307 307 TYR TYR A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 GLN 312 312 312 GLN GLN A . n 
A 1 313 HIS 313 313 313 HIS HIS A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 MET 317 317 317 MET MET A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 MET 319 319 319 MET MET A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 MET 322 322 322 MET MET A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 PRO 330 330 330 PRO PRO A . n 
A 1 331 ARG 331 331 331 ARG ARG A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 TYR 355 355 355 TYR TYR A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 MET 359 359 359 MET MET A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 GLN 361 361 361 GLN GLN A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 CYS 382 382 382 CYS CYS A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 TYR 394 394 394 TYR TYR A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 TYR 397 397 397 TYR TYR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ASP 401 401 401 ASP ASP A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 ASP 406 406 406 ASP ASP A . n 
A 1 407 ILE 407 407 407 ILE ILE A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 CYS 409 409 409 CYS CYS A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 ASN 418 418 418 ASN ASN A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 HIS 422 422 422 HIS HIS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLU 426 426 426 GLU GLU A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 THR 428 428 428 THR THR A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 SER 435 435 435 SER SER A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 HIS 438 438 438 HIS HIS A . n 
A 1 439 VAL 439 439 439 VAL VAL A . n 
A 1 440 SER 440 440 440 SER SER A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 ILE 445 445 445 ILE ILE A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 LYS 456 456 456 LYS LYS A . n 
A 1 457 ALA 457 457 457 ALA ALA A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 GLY 462 462 462 GLY GLY A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 MET 466 466 466 MET MET A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 LEU 468 468 468 LEU LEU A . n 
A 1 469 HIS 469 469 469 HIS HIS A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 TYR 471 471 471 TYR TYR A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 GLN 474 474 474 GLN GLN A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 GLY 476 476 476 GLY GLY A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 TYR 479 479 479 TYR TYR A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 SER 481 481 481 SER SER A . n 
A 1 482 PRO 482 482 482 PRO PRO A . n 
A 1 483 GLU 483 483 483 GLU GLU A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 PHE 491 491 491 PHE PHE A . n 
A 1 492 PHE 492 492 492 PHE PHE A . n 
A 1 493 MET 493 493 493 MET MET A . n 
A 1 494 MET 494 494 494 MET MET A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 ASN 496 496 496 ASN ASN A . n 
A 1 497 PHE 497 497 497 PHE PHE A . n 
A 1 498 TYR 498 498 498 TYR TYR A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 ILE 500 500 500 ILE ILE A . n 
A 1 501 GLN 501 501 501 GLN GLN A . n 
A 1 502 ARG 502 502 502 ARG ARG A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 GLU 505 505 505 GLU GLU A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 LYS 508 508 508 LYS LYS A . n 
A 1 509 GLU 509 509 509 GLU GLU A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 GLY 511 511 511 GLY GLY A . n 
A 1 512 GLU 512 512 512 GLU GLU A . n 
A 1 513 THR 513 513 513 THR THR A . n 
A 1 514 PHE 514 514 514 PHE PHE A . n 
A 1 515 ASP 515 515 515 ASP ASP A . n 
A 1 516 GLN 516 516 516 GLN GLN A . n 
A 1 517 TYR 517 517 517 TYR TYR A . n 
A 1 518 GLU 518 518 518 GLU GLU A . n 
A 1 519 GLY 519 519 519 GLY GLY A . n 
A 1 520 SER 520 520 520 SER SER A . n 
A 1 521 THR 521 521 521 THR THR A . n 
A 1 522 TYR 522 522 522 TYR TYR A . n 
A 1 523 ALA 523 523 523 ALA ALA A . n 
A 1 524 THR 524 524 524 THR THR A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 GLU 526 526 526 GLU GLU A . n 
A 1 527 TYR 527 527 527 TYR TYR A . n 
A 1 528 PHE 528 528 528 PHE PHE A . n 
A 1 529 ASP 529 529 529 ASP ASP A . n 
A 1 530 LYS 530 530 530 LYS LYS A . n 
A 1 531 TYR 531 531 531 TYR TYR A . n 
A 1 532 VAL 532 532 532 VAL VAL A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 THR 534 534 534 THR THR A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 PHE 536 536 536 PHE PHE A . n 
A 1 537 SER 537 537 537 SER SER A . n 
A 1 538 PRO 538 538 538 PRO PRO A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 TYR 540 540 540 TYR TYR A . n 
A 1 541 GLU 541 541 541 GLU GLU A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 ILE 543 543 543 ILE ILE A . n 
A 1 544 ALA 544 544 544 ALA ALA A . n 
A 1 545 ASN 545 545 545 ASN ASN A . n 
A 1 546 LEU 546 546 546 LEU LEU A . n 
A 1 547 PHE 547 547 547 PHE PHE A . n 
A 1 548 GLU 548 548 548 GLU GLU A . n 
A 1 549 GLY 549 549 549 GLY GLY A . n 
A 1 550 MET 550 550 550 MET MET A . n 
A 1 551 HIS 551 551 551 HIS HIS A . n 
A 1 552 ILE 552 552 552 ILE ILE A . n 
A 1 553 PRO 553 553 553 PRO PRO A . n 
A 1 554 THR 554 554 554 THR THR A . n 
A 1 555 THR 555 555 555 THR THR A . n 
A 1 556 GLU 556 556 556 GLU GLU A . n 
A 1 557 ASP 557 557 557 ASP ASP A . n 
A 1 558 TRP 558 558 558 TRP TRP A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 LYS 562 562 562 LYS LYS A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 PHE 564 564 564 PHE PHE A . n 
A 1 565 VAL 565 565 565 VAL VAL A . n 
A 1 566 ALA 566 566 566 ALA ALA A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 HIS 568 568 568 HIS HIS A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 MET 570 570 570 MET MET A . n 
A 1 571 TYR 571 571 571 TYR TYR A . n 
A 1 572 HIS 572 572 572 HIS HIS A . n 
A 1 573 SER 573 573 573 SER SER A . n 
A 1 574 TYR 574 574 574 TYR TYR A . n 
A 1 575 ARG 575 575 575 ARG ARG A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 CYS 577 577 577 CYS CYS A . n 
A 1 578 ILE 578 578 578 ILE ILE A . n 
A 1 579 ALA 579 579 579 ALA ALA A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 THR 581 581 581 THR THR A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 SER 583 583 583 SER SER A . n 
A 1 584 ILE 584 584 584 ILE ILE A . n 
A 1 585 SER 585 585 585 SER SER A . n 
A 1 586 TYR 586 586 586 TYR TYR A . n 
A 1 587 VAL 587 587 587 VAL VAL A . n 
A 1 588 GLN 588 588 588 GLN GLN A . n 
A 1 589 SER 589 589 589 SER SER A . n 
A 1 590 SER 590 590 590 SER SER A . n 
A 1 591 THR 591 591 591 THR THR A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 SER 593 593 593 SER SER A . n 
A 1 594 VAL 594 594 594 VAL VAL A . n 
A 1 595 MET 595 595 595 MET MET A . n 
A 1 596 PRO 596 596 596 PRO PRO A . n 
A 1 597 ILE 597 597 597 ILE ILE A . n 
A 1 598 MET 598 598 598 MET MET A . n 
A 1 599 GLU 599 599 599 GLU GLU A . n 
A 1 600 ARG 600 600 600 ARG ARG A . n 
A 1 601 ILE 601 601 601 ILE ILE A . n 
A 1 602 GLU 602 602 602 GLU GLU A . n 
A 1 603 GLU 603 603 603 GLU GLU A . n 
A 1 604 ARG 604 604 604 ARG ARG A . n 
A 1 605 THR 605 605 605 THR THR A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLY 607 607 607 GLY GLY A . n 
A 1 608 ASN 608 608 608 ASN ASN A . n 
A 1 609 SER 609 609 609 SER SER A . n 
A 1 610 LYS 610 610 610 LYS LYS A . n 
A 1 611 THR 611 611 611 THR THR A . n 
A 1 612 TYR 612 612 612 TYR TYR A . n 
A 1 613 TYR 613 613 613 TYR TYR A . n 
A 1 614 PRO 614 614 614 PRO PRO A . n 
A 1 615 MET 615 615 615 MET MET A . n 
A 1 616 PRO 616 616 616 PRO PRO A . n 
A 1 617 GLY 617 617 617 GLY GLY A . n 
A 1 618 LEU 618 618 618 LEU LEU A . n 
A 1 619 ALA 619 619 619 ALA ALA A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 ASN 622 622 622 ASN ASN A . n 
A 1 623 TRP 623 623 623 TRP TRP A . n 
A 1 624 PHE 624 624 624 PHE PHE A . n 
A 1 625 PHE 625 625 625 PHE PHE A . n 
A 1 626 TYR 626 626 626 TYR TYR A . n 
A 1 627 LYS 627 627 627 LYS LYS A . n 
A 1 628 GLU 628 628 628 GLU GLU A . n 
A 1 629 ALA 629 629 629 ALA ALA A . n 
A 1 630 TYR 630 630 630 TYR TYR A . n 
A 1 631 ASP 631 631 631 ASP ASP A . n 
A 1 632 MET 632 632 632 MET MET A . n 
A 1 633 ASP 633 633 633 ASP ASP A . n 
A 1 634 MET 634 634 634 MET MET A . n 
A 1 635 PHE 635 635 635 PHE PHE A . n 
A 1 636 LYS 636 636 636 LYS LYS A . n 
A 1 637 VAL 637 637 637 VAL VAL A . n 
A 1 638 VAL 638 638 638 VAL VAL A . n 
A 1 639 ASP 639 639 639 ASP ASP A . n 
A 1 640 MET 640 640 640 MET MET A . n 
A 1 641 ILE 641 641 641 ILE ILE A . n 
A 1 642 ALA 642 642 642 ALA ALA A . n 
A 1 643 THR 643 643 643 THR THR A . n 
A 1 644 ILE 644 644 644 ILE ILE A . n 
A 1 645 GLN 645 645 645 GLN GLN A . n 
A 1 646 GLN 646 646 646 GLN GLN A . n 
A 1 647 HIS 647 647 647 HIS HIS A . n 
A 1 648 ILE 648 648 648 ILE ILE A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 GLN 650 650 650 GLN GLN A . n 
A 1 651 GLY 651 651 651 GLY GLY A . n 
A 1 652 ILE 652 652 652 ILE ILE A . n 
A 1 653 SER 653 653 653 SER SER A . n 
A 1 654 PHE 654 654 654 PHE PHE A . n 
A 1 655 THR 655 655 655 THR THR A . n 
A 1 656 LEU 656 656 656 LEU LEU A . n 
A 1 657 PHE 657 657 657 PHE PHE A . n 
A 1 658 LEU 658 658 658 LEU LEU A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 ASP 660 660 660 ASP ASP A . n 
A 1 661 THR 661 661 661 THR THR A . n 
A 1 662 MET 662 662 662 MET MET A . n 
A 1 663 THR 663 663 663 THR THR A . n 
A 1 664 THR 664 664 664 THR THR A . n 
A 1 665 ARG 665 665 665 ARG ARG A . n 
A 1 666 ASP 666 666 666 ASP ASP A . n 
A 1 667 LEU 667 667 667 LEU LEU A . n 
A 1 668 ASN 668 668 668 ASN ASN A . n 
A 1 669 ARG 669 669 669 ARG ARG A . n 
A 1 670 ILE 670 670 670 ILE ILE A . n 
A 1 671 ASP 671 671 671 ASP ASP A . n 
A 1 672 LEU 672 672 672 LEU LEU A . n 
A 1 673 TYR 673 673 673 TYR TYR A . n 
A 1 674 ALA 674 674 674 ALA ALA A . n 
A 1 675 HIS 675 675 675 HIS HIS A . n 
A 1 676 HIS 676 676 676 HIS HIS A . n 
A 1 677 ARG 677 677 677 ARG ARG A . n 
A 1 678 GLY 678 678 678 GLY GLY A . n 
A 1 679 ILE 679 679 679 ILE ILE A . n 
A 1 680 LYS 680 680 680 LYS LYS A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 ILE 682 682 682 ILE ILE A . n 
A 1 683 TYR 683 683 683 TYR TYR A . n 
A 1 684 TYR 684 684 684 TYR TYR A . n 
A 1 685 ALA 685 685 685 ALA ALA A . n 
A 1 686 ARG 686 686 686 ARG ARG A . n 
A 1 687 THR 687 687 687 THR THR A . n 
A 1 688 LYS 688 688 688 LYS LYS A . n 
A 1 689 ASP 689 689 ?   ?   ?   A . n 
A 1 690 THR 690 690 ?   ?   ?   A . n 
A 1 691 GLY 691 691 ?   ?   ?   A . n 
A 1 692 GLN 692 692 ?   ?   ?   A . n 
A 1 693 ASP 693 693 ?   ?   ?   A . n 
A 1 694 SER 694 694 ?   ?   ?   A . n 
A 1 695 CYS 695 695 ?   ?   ?   A . n 
A 1 696 LEU 696 696 ?   ?   ?   A . n 
A 1 697 SER 697 697 ?   ?   ?   A . n 
A 1 698 CYS 698 698 ?   ?   ?   A . n 
A 1 699 VAL 699 699 ?   ?   ?   A . n 
A 1 700 VAL 700 700 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   LYS 8   8   8   LYS LYS B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  ILE 10  10  10  ILE ILE B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  TYR 36  36  36  TYR TYR B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  HIS 49  49  49  HIS HIS B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  ILE 77  77  77  ILE ILE B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  MET 95  95  95  MET MET B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 TYR 104 104 104 TYR TYR B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 MET 144 144 144 MET MET B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 GLN 147 147 147 GLN GLN B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 PRO 151 151 151 PRO PRO B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 CYS 170 170 170 CYS CYS B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 ASP 177 177 177 ASP ASP B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 MET 190 190 190 MET MET B . n 
B 1 191 GLN 191 191 191 GLN GLN B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 LYS 209 209 209 LYS LYS B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 ASN 218 218 218 ASN ASN B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 PHE 234 234 234 PHE PHE B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 TYR 250 250 250 TYR TYR B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 PHE 254 254 254 PHE PHE B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 ASP 257 257 257 ASP ASP B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 SER 268 268 268 SER SER B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 ASP 272 272 272 ASP ASP B . n 
B 1 273 VAL 273 273 273 VAL VAL B . n 
B 1 274 ARG 274 274 274 ARG ARG B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 SER 279 279 279 SER SER B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 LYS 287 287 287 LYS LYS B . n 
B 1 288 PHE 288 288 288 PHE PHE B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 LEU 291 291 291 LEU LEU B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 ARG 293 293 293 ARG ARG B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 TYR 307 307 307 TYR TYR B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 GLU 309 309 309 GLU GLU B . n 
B 1 310 TYR 310 310 310 TYR TYR B . n 
B 1 311 GLY 311 311 311 GLY GLY B . n 
B 1 312 GLN 312 312 312 GLN GLN B . n 
B 1 313 HIS 313 313 313 HIS HIS B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 ASP 315 315 315 ASP ASP B . n 
B 1 316 GLU 316 316 316 GLU GLU B . n 
B 1 317 MET 317 317 317 MET MET B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 MET 319 319 319 MET MET B . n 
B 1 320 ASN 320 320 320 ASN ASN B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 MET 322 322 322 MET MET B . n 
B 1 323 TYR 323 323 323 TYR TYR B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 LYS 325 325 325 LYS LYS B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ASP 328 328 328 ASP ASP B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 PRO 330 330 330 PRO PRO B . n 
B 1 331 ARG 331 331 331 ARG ARG B . n 
B 1 332 VAL 332 332 332 VAL VAL B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 GLU 335 335 335 GLU GLU B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 PRO 339 339 339 PRO PRO B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 LEU 343 343 343 LEU LEU B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 GLY 354 354 354 GLY GLY B . n 
B 1 355 TYR 355 355 355 TYR TYR B . n 
B 1 356 PRO 356 356 356 PRO PRO B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 ILE 358 358 358 ILE ILE B . n 
B 1 359 MET 359 359 359 MET MET B . n 
B 1 360 PHE 360 360 360 PHE PHE B . n 
B 1 361 GLN 361 361 361 GLN GLN B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 VAL 364 364 364 VAL VAL B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 LYS 366 366 366 LYS LYS B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 HIS 368 368 368 HIS HIS B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ASN 370 370 370 ASN ASN B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 HIS 372 372 372 HIS HIS B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 SER 374 374 374 SER SER B . n 
B 1 375 LYS 375 375 375 LYS LYS B . n 
B 1 376 VAL 376 376 376 VAL VAL B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 SER 379 379 379 SER SER B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 CYS 382 382 382 CYS CYS B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 SER 389 389 389 SER SER B . n 
B 1 390 GLN 390 390 390 GLN GLN B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 TYR 394 394 394 TYR TYR B . n 
B 1 395 THR 395 395 395 THR THR B . n 
B 1 396 ASP 396 396 396 ASP ASP B . n 
B 1 397 TYR 397 397 397 TYR TYR B . n 
B 1 398 ASP 398 398 398 ASP ASP B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 ASP 401 401 401 ASP ASP B . n 
B 1 402 GLU 402 402 402 GLU GLU B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 GLY 404 404 404 GLY GLY B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 ASP 406 406 406 ASP ASP B . n 
B 1 407 ILE 407 407 407 ILE ILE B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 CYS 409 409 409 CYS CYS B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 GLY 412 412 412 GLY GLY B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 ASN 415 415 415 ASN ASN B . n 
B 1 416 ILE 416 416 416 ILE ILE B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 ASN 418 418 418 ASN ASN B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 HIS 422 422 422 HIS HIS B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLU 426 426 426 GLU GLU B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 THR 428 428 428 THR THR B . n 
B 1 429 VAL 429 429 429 VAL VAL B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 THR 433 433 433 THR THR B . n 
B 1 434 ASP 434 434 434 ASP ASP B . n 
B 1 435 SER 435 435 435 SER SER B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 THR 437 437 437 THR THR B . n 
B 1 438 HIS 438 438 438 HIS HIS B . n 
B 1 439 VAL 439 439 439 VAL VAL B . n 
B 1 440 SER 440 440 440 SER SER B . n 
B 1 441 GLU 441 441 441 GLU GLU B . n 
B 1 442 THR 442 442 442 THR THR B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 ILE 445 445 445 ILE ILE B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 ASN 447 447 447 ASN ASN B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 PRO 449 449 449 PRO PRO B . n 
B 1 450 ALA 450 450 450 ALA ALA B . n 
B 1 451 VAL 451 451 451 VAL VAL B . n 
B 1 452 ARG 452 452 452 ARG ARG B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 LYS 456 456 456 LYS LYS B . n 
B 1 457 ALA 457 457 457 ALA ALA B . n 
B 1 458 MET 458 458 458 MET MET B . n 
B 1 459 LYS 459 459 459 LYS LYS B . n 
B 1 460 SER 460 460 460 SER SER B . n 
B 1 461 ILE 461 461 461 ILE ILE B . n 
B 1 462 GLY 462 462 462 GLY GLY B . n 
B 1 463 LEU 463 463 463 LEU LEU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 MET 466 466 466 MET MET B . n 
B 1 467 ASN 467 467 467 ASN ASN B . n 
B 1 468 LEU 468 468 468 LEU LEU B . n 
B 1 469 HIS 469 469 469 HIS HIS B . n 
B 1 470 GLY 470 470 470 GLY GLY B . n 
B 1 471 TYR 471 471 471 TYR TYR B . n 
B 1 472 LEU 472 472 472 LEU LEU B . n 
B 1 473 ALA 473 473 473 ALA ALA B . n 
B 1 474 GLN 474 474 474 GLN GLN B . n 
B 1 475 ASN 475 475 475 ASN ASN B . n 
B 1 476 GLY 476 476 476 GLY GLY B . n 
B 1 477 ILE 477 477 477 ILE ILE B . n 
B 1 478 ALA 478 478 478 ALA ALA B . n 
B 1 479 TYR 479 479 479 TYR TYR B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 SER 481 481 481 SER SER B . n 
B 1 482 PRO 482 482 482 PRO PRO B . n 
B 1 483 GLU 483 483 483 GLU GLU B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 ARG 485 485 485 ARG ARG B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 PHE 487 487 487 PHE PHE B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 ASN 489 489 489 ASN ASN B . n 
B 1 490 THR 490 490 490 THR THR B . n 
B 1 491 PHE 491 491 491 PHE PHE B . n 
B 1 492 PHE 492 492 492 PHE PHE B . n 
B 1 493 MET 493 493 493 MET MET B . n 
B 1 494 MET 494 494 494 MET MET B . n 
B 1 495 VAL 495 495 495 VAL VAL B . n 
B 1 496 ASN 496 496 496 ASN ASN B . n 
B 1 497 PHE 497 497 497 PHE PHE B . n 
B 1 498 TYR 498 498 498 TYR TYR B . n 
B 1 499 SER 499 499 499 SER SER B . n 
B 1 500 ILE 500 500 500 ILE ILE B . n 
B 1 501 GLN 501 501 501 GLN GLN B . n 
B 1 502 ARG 502 502 502 ARG ARG B . n 
B 1 503 SER 503 503 503 SER SER B . n 
B 1 504 ALA 504 504 504 ALA ALA B . n 
B 1 505 GLU 505 505 505 GLU GLU B . n 
B 1 506 ILE 506 506 506 ILE ILE B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 LYS 508 508 508 LYS LYS B . n 
B 1 509 GLU 509 509 509 GLU GLU B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 GLY 511 511 511 GLY GLY B . n 
B 1 512 GLU 512 512 512 GLU GLU B . n 
B 1 513 THR 513 513 513 THR THR B . n 
B 1 514 PHE 514 514 514 PHE PHE B . n 
B 1 515 ASP 515 515 515 ASP ASP B . n 
B 1 516 GLN 516 516 516 GLN GLN B . n 
B 1 517 TYR 517 517 517 TYR TYR B . n 
B 1 518 GLU 518 518 518 GLU GLU B . n 
B 1 519 GLY 519 519 519 GLY GLY B . n 
B 1 520 SER 520 520 520 SER SER B . n 
B 1 521 THR 521 521 521 THR THR B . n 
B 1 522 TYR 522 522 522 TYR TYR B . n 
B 1 523 ALA 523 523 523 ALA ALA B . n 
B 1 524 THR 524 524 524 THR THR B . n 
B 1 525 GLY 525 525 525 GLY GLY B . n 
B 1 526 GLU 526 526 526 GLU GLU B . n 
B 1 527 TYR 527 527 527 TYR TYR B . n 
B 1 528 PHE 528 528 528 PHE PHE B . n 
B 1 529 ASP 529 529 529 ASP ASP B . n 
B 1 530 LYS 530 530 530 LYS LYS B . n 
B 1 531 TYR 531 531 531 TYR TYR B . n 
B 1 532 VAL 532 532 532 VAL VAL B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 THR 534 534 534 THR THR B . n 
B 1 535 ASP 535 535 535 ASP ASP B . n 
B 1 536 PHE 536 536 536 PHE PHE B . n 
B 1 537 SER 537 537 537 SER SER B . n 
B 1 538 PRO 538 538 538 PRO PRO B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 TYR 540 540 540 TYR TYR B . n 
B 1 541 GLU 541 541 541 GLU GLU B . n 
B 1 542 LYS 542 542 542 LYS LYS B . n 
B 1 543 ILE 543 543 543 ILE ILE B . n 
B 1 544 ALA 544 544 544 ALA ALA B . n 
B 1 545 ASN 545 545 545 ASN ASN B . n 
B 1 546 LEU 546 546 546 LEU LEU B . n 
B 1 547 PHE 547 547 547 PHE PHE B . n 
B 1 548 GLU 548 548 548 GLU GLU B . n 
B 1 549 GLY 549 549 549 GLY GLY B . n 
B 1 550 MET 550 550 550 MET MET B . n 
B 1 551 HIS 551 551 551 HIS HIS B . n 
B 1 552 ILE 552 552 552 ILE ILE B . n 
B 1 553 PRO 553 553 553 PRO PRO B . n 
B 1 554 THR 554 554 554 THR THR B . n 
B 1 555 THR 555 555 555 THR THR B . n 
B 1 556 GLU 556 556 556 GLU GLU B . n 
B 1 557 ASP 557 557 557 ASP ASP B . n 
B 1 558 TRP 558 558 558 TRP TRP B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 LYS 560 560 560 LYS LYS B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 LYS 562 562 562 LYS LYS B . n 
B 1 563 ALA 563 563 563 ALA ALA B . n 
B 1 564 PHE 564 564 564 PHE PHE B . n 
B 1 565 VAL 565 565 565 VAL VAL B . n 
B 1 566 ALA 566 566 566 ALA ALA B . n 
B 1 567 GLU 567 567 567 GLU GLU B . n 
B 1 568 HIS 568 568 568 HIS HIS B . n 
B 1 569 GLY 569 569 569 GLY GLY B . n 
B 1 570 MET 570 570 570 MET MET B . n 
B 1 571 TYR 571 571 571 TYR TYR B . n 
B 1 572 HIS 572 572 572 HIS HIS B . n 
B 1 573 SER 573 573 573 SER SER B . n 
B 1 574 TYR 574 574 574 TYR TYR B . n 
B 1 575 ARG 575 575 575 ARG ARG B . n 
B 1 576 LEU 576 576 576 LEU LEU B . n 
B 1 577 CYS 577 577 577 CYS CYS B . n 
B 1 578 ILE 578 578 578 ILE ILE B . n 
B 1 579 ALA 579 579 579 ALA ALA B . n 
B 1 580 PRO 580 580 580 PRO PRO B . n 
B 1 581 THR 581 581 581 THR THR B . n 
B 1 582 GLY 582 582 582 GLY GLY B . n 
B 1 583 SER 583 583 583 SER SER B . n 
B 1 584 ILE 584 584 584 ILE ILE B . n 
B 1 585 SER 585 585 585 SER SER B . n 
B 1 586 TYR 586 586 586 TYR TYR B . n 
B 1 587 VAL 587 587 587 VAL VAL B . n 
B 1 588 GLN 588 588 588 GLN GLN B . n 
B 1 589 SER 589 589 589 SER SER B . n 
B 1 590 SER 590 590 590 SER SER B . n 
B 1 591 THR 591 591 591 THR THR B . n 
B 1 592 ALA 592 592 592 ALA ALA B . n 
B 1 593 SER 593 593 593 SER SER B . n 
B 1 594 VAL 594 594 594 VAL VAL B . n 
B 1 595 MET 595 595 595 MET MET B . n 
B 1 596 PRO 596 596 596 PRO PRO B . n 
B 1 597 ILE 597 597 597 ILE ILE B . n 
B 1 598 MET 598 598 598 MET MET B . n 
B 1 599 GLU 599 599 599 GLU GLU B . n 
B 1 600 ARG 600 600 600 ARG ARG B . n 
B 1 601 ILE 601 601 601 ILE ILE B . n 
B 1 602 GLU 602 602 602 GLU GLU B . n 
B 1 603 GLU 603 603 603 GLU GLU B . n 
B 1 604 ARG 604 604 604 ARG ARG B . n 
B 1 605 THR 605 605 605 THR THR B . n 
B 1 606 TYR 606 606 606 TYR TYR B . n 
B 1 607 GLY 607 607 607 GLY GLY B . n 
B 1 608 ASN 608 608 608 ASN ASN B . n 
B 1 609 SER 609 609 609 SER SER B . n 
B 1 610 LYS 610 610 610 LYS LYS B . n 
B 1 611 THR 611 611 611 THR THR B . n 
B 1 612 TYR 612 612 612 TYR TYR B . n 
B 1 613 TYR 613 613 613 TYR TYR B . n 
B 1 614 PRO 614 614 614 PRO PRO B . n 
B 1 615 MET 615 615 615 MET MET B . n 
B 1 616 PRO 616 616 616 PRO PRO B . n 
B 1 617 GLY 617 617 617 GLY GLY B . n 
B 1 618 LEU 618 618 618 LEU LEU B . n 
B 1 619 ALA 619 619 619 ALA ALA B . n 
B 1 620 SER 620 620 620 SER SER B . n 
B 1 621 ASN 621 621 621 ASN ASN B . n 
B 1 622 ASN 622 622 622 ASN ASN B . n 
B 1 623 TRP 623 623 623 TRP TRP B . n 
B 1 624 PHE 624 624 624 PHE PHE B . n 
B 1 625 PHE 625 625 625 PHE PHE B . n 
B 1 626 TYR 626 626 626 TYR TYR B . n 
B 1 627 LYS 627 627 627 LYS LYS B . n 
B 1 628 GLU 628 628 628 GLU GLU B . n 
B 1 629 ALA 629 629 629 ALA ALA B . n 
B 1 630 TYR 630 630 630 TYR TYR B . n 
B 1 631 ASP 631 631 631 ASP ASP B . n 
B 1 632 MET 632 632 632 MET MET B . n 
B 1 633 ASP 633 633 633 ASP ASP B . n 
B 1 634 MET 634 634 634 MET MET B . n 
B 1 635 PHE 635 635 635 PHE PHE B . n 
B 1 636 LYS 636 636 636 LYS LYS B . n 
B 1 637 VAL 637 637 637 VAL VAL B . n 
B 1 638 VAL 638 638 638 VAL VAL B . n 
B 1 639 ASP 639 639 639 ASP ASP B . n 
B 1 640 MET 640 640 640 MET MET B . n 
B 1 641 ILE 641 641 641 ILE ILE B . n 
B 1 642 ALA 642 642 642 ALA ALA B . n 
B 1 643 THR 643 643 643 THR THR B . n 
B 1 644 ILE 644 644 644 ILE ILE B . n 
B 1 645 GLN 645 645 645 GLN GLN B . n 
B 1 646 GLN 646 646 646 GLN GLN B . n 
B 1 647 HIS 647 647 647 HIS HIS B . n 
B 1 648 ILE 648 648 648 ILE ILE B . n 
B 1 649 ASP 649 649 649 ASP ASP B . n 
B 1 650 GLN 650 650 650 GLN GLN B . n 
B 1 651 GLY 651 651 651 GLY GLY B . n 
B 1 652 ILE 652 652 652 ILE ILE B . n 
B 1 653 SER 653 653 653 SER SER B . n 
B 1 654 PHE 654 654 654 PHE PHE B . n 
B 1 655 THR 655 655 655 THR THR B . n 
B 1 656 LEU 656 656 656 LEU LEU B . n 
B 1 657 PHE 657 657 657 PHE PHE B . n 
B 1 658 LEU 658 658 658 LEU LEU B . n 
B 1 659 LYS 659 659 659 LYS LYS B . n 
B 1 660 ASP 660 660 660 ASP ASP B . n 
B 1 661 THR 661 661 661 THR THR B . n 
B 1 662 MET 662 662 662 MET MET B . n 
B 1 663 THR 663 663 663 THR THR B . n 
B 1 664 THR 664 664 664 THR THR B . n 
B 1 665 ARG 665 665 665 ARG ARG B . n 
B 1 666 ASP 666 666 666 ASP ASP B . n 
B 1 667 LEU 667 667 667 LEU LEU B . n 
B 1 668 ASN 668 668 668 ASN ASN B . n 
B 1 669 ARG 669 669 669 ARG ARG B . n 
B 1 670 ILE 670 670 670 ILE ILE B . n 
B 1 671 ASP 671 671 671 ASP ASP B . n 
B 1 672 LEU 672 672 672 LEU LEU B . n 
B 1 673 TYR 673 673 673 TYR TYR B . n 
B 1 674 ALA 674 674 674 ALA ALA B . n 
B 1 675 HIS 675 675 675 HIS HIS B . n 
B 1 676 HIS 676 676 676 HIS HIS B . n 
B 1 677 ARG 677 677 677 ARG ARG B . n 
B 1 678 GLY 678 678 678 GLY GLY B . n 
B 1 679 ILE 679 679 679 ILE ILE B . n 
B 1 680 LYS 680 680 680 LYS LYS B . n 
B 1 681 THR 681 681 681 THR THR B . n 
B 1 682 ILE 682 682 682 ILE ILE B . n 
B 1 683 TYR 683 683 683 TYR TYR B . n 
B 1 684 TYR 684 684 684 TYR TYR B . n 
B 1 685 ALA 685 685 685 ALA ALA B . n 
B 1 686 ARG 686 686 686 ARG ARG B . n 
B 1 687 THR 687 687 687 THR THR B . n 
B 1 688 LYS 688 688 688 LYS LYS B . n 
B 1 689 ASP 689 689 ?   ?   ?   B . n 
B 1 690 THR 690 690 ?   ?   ?   B . n 
B 1 691 GLY 691 691 ?   ?   ?   B . n 
B 1 692 GLN 692 692 ?   ?   ?   B . n 
B 1 693 ASP 693 693 ?   ?   ?   B . n 
B 1 694 SER 694 694 ?   ?   ?   B . n 
B 1 695 CYS 695 695 ?   ?   ?   B . n 
B 1 696 LEU 696 696 ?   ?   ?   B . n 
B 1 697 SER 697 697 ?   ?   ?   B . n 
B 1 698 CYS 698 698 ?   ?   ?   B . n 
B 1 699 VAL 699 699 ?   ?   ?   B . n 
B 1 700 VAL 700 700 ?   ?   ?   B . n 
C 2 1   MET 1   -20 ?   ?   ?   C . n 
C 2 2   GLY 2   -19 ?   ?   ?   C . n 
C 2 3   SER 3   -18 ?   ?   ?   C . n 
C 2 4   SER 4   -17 ?   ?   ?   C . n 
C 2 5   HIS 5   -16 ?   ?   ?   C . n 
C 2 6   HIS 6   -15 ?   ?   ?   C . n 
C 2 7   HIS 7   -14 ?   ?   ?   C . n 
C 2 8   HIS 8   -13 ?   ?   ?   C . n 
C 2 9   HIS 9   -12 ?   ?   ?   C . n 
C 2 10  HIS 10  -11 ?   ?   ?   C . n 
C 2 11  SER 11  -10 ?   ?   ?   C . n 
C 2 12  SER 12  -9  ?   ?   ?   C . n 
C 2 13  GLY 13  -8  ?   ?   ?   C . n 
C 2 14  LEU 14  -7  ?   ?   ?   C . n 
C 2 15  VAL 15  -6  ?   ?   ?   C . n 
C 2 16  PRO 16  -5  ?   ?   ?   C . n 
C 2 17  ARG 17  -4  ?   ?   ?   C . n 
C 2 18  GLY 18  -3  ?   ?   ?   C . n 
C 2 19  SER 19  -2  ?   ?   ?   C . n 
C 2 20  HIS 20  -1  ?   ?   ?   C . n 
C 2 21  MET 21  0   ?   ?   ?   C . n 
C 2 22  MET 22  1   ?   ?   ?   C . n 
C 2 23  THR 23  2   ?   ?   ?   C . n 
C 2 24  LYS 24  3   ?   ?   ?   C . n 
C 2 25  ILE 25  4   ?   ?   ?   C . n 
C 2 26  TYR 26  5   ?   ?   ?   C . n 
C 2 27  ASP 27  6   ?   ?   ?   C . n 
C 2 28  ALA 28  7   ?   ?   ?   C . n 
C 2 29  ALA 29  8   ?   ?   ?   C . n 
C 2 30  ASN 30  9   ?   ?   ?   C . n 
C 2 31  TRP 31  10  ?   ?   ?   C . n 
C 2 32  SER 32  11  ?   ?   ?   C . n 
C 2 33  LYS 33  12  ?   ?   ?   C . n 
C 2 34  HIS 34  13  ?   ?   ?   C . n 
C 2 35  GLU 35  14  ?   ?   ?   C . n 
C 2 36  ASP 36  15  ?   ?   ?   C . n 
C 2 37  ASP 37  16  ?   ?   ?   C . n 
C 2 38  PHE 38  17  ?   ?   ?   C . n 
C 2 39  THR 39  18  ?   ?   ?   C . n 
C 2 40  GLN 40  19  ?   ?   ?   C . n 
C 2 41  MET 41  20  ?   ?   ?   C . n 
C 2 42  PHE 42  21  ?   ?   ?   C . n 
C 2 43  TYR 43  22  ?   ?   ?   C . n 
C 2 44  ASN 44  23  ?   ?   ?   C . n 
C 2 45  GLN 45  24  ?   ?   ?   C . n 
C 2 46  ASN 46  25  ?   ?   ?   C . n 
C 2 47  VAL 47  26  ?   ?   ?   C . n 
C 2 48  LYS 48  27  ?   ?   ?   C . n 
C 2 49  GLN 49  28  ?   ?   ?   C . n 
C 2 50  PHE 50  29  ?   ?   ?   C . n 
C 2 51  TRP 51  30  ?   ?   ?   C . n 
C 2 52  LEU 52  31  ?   ?   ?   C . n 
C 2 53  PRO 53  32  ?   ?   ?   C . n 
C 2 54  GLU 54  33  ?   ?   ?   C . n 
C 2 55  GLU 55  34  ?   ?   ?   C . n 
C 2 56  ILE 56  35  ?   ?   ?   C . n 
C 2 57  ALA 57  36  ?   ?   ?   C . n 
C 2 58  LEU 58  37  ?   ?   ?   C . n 
C 2 59  ASN 59  38  ?   ?   ?   C . n 
C 2 60  GLY 60  39  ?   ?   ?   C . n 
C 2 61  ASP 61  40  ?   ?   ?   C . n 
C 2 62  LEU 62  41  ?   ?   ?   C . n 
C 2 63  LEU 63  42  ?   ?   ?   C . n 
C 2 64  THR 64  43  ?   ?   ?   C . n 
C 2 65  TRP 65  44  ?   ?   ?   C . n 
C 2 66  LYS 66  45  ?   ?   ?   C . n 
C 2 67  TYR 67  46  ?   ?   ?   C . n 
C 2 68  LEU 68  47  ?   ?   ?   C . n 
C 2 69  GLY 69  48  ?   ?   ?   C . n 
C 2 70  LYS 70  49  ?   ?   ?   C . n 
C 2 71  ASN 71  50  ?   ?   ?   C . n 
C 2 72  GLU 72  51  ?   ?   ?   C . n 
C 2 73  GLN 73  52  ?   ?   ?   C . n 
C 2 74  ASP 74  53  ?   ?   ?   C . n 
C 2 75  THR 75  54  ?   ?   ?   C . n 
C 2 76  TYR 76  55  ?   ?   ?   C . n 
C 2 77  MET 77  56  ?   ?   ?   C . n 
C 2 78  LYS 78  57  ?   ?   ?   C . n 
C 2 79  VAL 79  58  ?   ?   ?   C . n 
C 2 80  LEU 80  59  ?   ?   ?   C . n 
C 2 81  ALA 81  60  ?   ?   ?   C . n 
C 2 82  GLY 82  61  ?   ?   ?   C . n 
C 2 83  LEU 83  62  ?   ?   ?   C . n 
C 2 84  THR 84  63  ?   ?   ?   C . n 
C 2 85  LEU 85  64  ?   ?   ?   C . n 
C 2 86  LEU 86  65  ?   ?   ?   C . n 
C 2 87  ASP 87  66  ?   ?   ?   C . n 
C 2 88  THR 88  67  ?   ?   ?   C . n 
C 2 89  GLU 89  68  ?   ?   ?   C . n 
C 2 90  GLN 90  69  ?   ?   ?   C . n 
C 2 91  GLY 91  70  ?   ?   ?   C . n 
C 2 92  ASN 92  71  ?   ?   ?   C . n 
C 2 93  THR 93  72  ?   ?   ?   C . n 
C 2 94  GLY 94  73  ?   ?   ?   C . n 
C 2 95  MET 95  74  ?   ?   ?   C . n 
C 2 96  PRO 96  75  ?   ?   ?   C . n 
C 2 97  ILE 97  76  ?   ?   ?   C . n 
C 2 98  VAL 98  77  ?   ?   ?   C . n 
C 2 99  ALA 99  78  ?   ?   ?   C . n 
C 2 100 GLU 100 79  ?   ?   ?   C . n 
C 2 101 HIS 101 80  ?   ?   ?   C . n 
C 2 102 VAL 102 81  ?   ?   ?   C . n 
C 2 103 ASP 103 82  ?   ?   ?   C . n 
C 2 104 GLY 104 83  ?   ?   ?   C . n 
C 2 105 HIS 105 84  ?   ?   ?   C . n 
C 2 106 GLN 106 85  ?   ?   ?   C . n 
C 2 107 ARG 107 86  ?   ?   ?   C . n 
C 2 108 LYS 108 87  ?   ?   ?   C . n 
C 2 109 ALA 109 88  ?   ?   ?   C . n 
C 2 110 VAL 110 89  ?   ?   ?   C . n 
C 2 111 LEU 111 90  ?   ?   ?   C . n 
C 2 112 ASN 112 91  ?   ?   ?   C . n 
C 2 113 PHE 113 92  ?   ?   ?   C . n 
C 2 114 MET 114 93  ?   ?   ?   C . n 
C 2 115 ALA 115 94  ?   ?   ?   C . n 
C 2 116 MET 116 95  ?   ?   ?   C . n 
C 2 117 MET 117 96  ?   ?   ?   C . n 
C 2 118 GLU 118 97  ?   ?   ?   C . n 
C 2 119 ASN 119 98  ?   ?   ?   C . n 
C 2 120 ALA 120 99  ?   ?   ?   C . n 
C 2 121 VAL 121 100 ?   ?   ?   C . n 
C 2 122 HIS 122 101 ?   ?   ?   C . n 
C 2 123 ALA 123 102 ?   ?   ?   C . n 
C 2 124 LYS 124 103 ?   ?   ?   C . n 
C 2 125 SER 125 104 ?   ?   ?   C . n 
C 2 126 TYR 126 105 ?   ?   ?   C . n 
C 2 127 SER 127 106 ?   ?   ?   C . n 
C 2 128 ASN 128 107 ?   ?   ?   C . n 
C 2 129 ILE 129 108 ?   ?   ?   C . n 
C 2 130 PHE 130 109 ?   ?   ?   C . n 
C 2 131 MET 131 110 ?   ?   ?   C . n 
C 2 132 THR 132 111 ?   ?   ?   C . n 
C 2 133 LEU 133 112 ?   ?   ?   C . n 
C 2 134 ALA 134 113 ?   ?   ?   C . n 
C 2 135 PRO 135 114 ?   ?   ?   C . n 
C 2 136 THR 136 115 ?   ?   ?   C . n 
C 2 137 GLU 137 116 ?   ?   ?   C . n 
C 2 138 THR 138 117 ?   ?   ?   C . n 
C 2 139 ILE 139 118 ?   ?   ?   C . n 
C 2 140 ASN 140 119 ?   ?   ?   C . n 
C 2 141 GLU 141 120 ?   ?   ?   C . n 
C 2 142 VAL 142 121 ?   ?   ?   C . n 
C 2 143 PHE 143 122 ?   ?   ?   C . n 
C 2 144 GLU 144 123 ?   ?   ?   C . n 
C 2 145 TRP 145 124 ?   ?   ?   C . n 
C 2 146 VAL 146 125 ?   ?   ?   C . n 
C 2 147 LYS 147 126 ?   ?   ?   C . n 
C 2 148 GLN 148 127 ?   ?   ?   C . n 
C 2 149 ASN 149 128 ?   ?   ?   C . n 
C 2 150 LYS 150 129 ?   ?   ?   C . n 
C 2 151 TYR 151 130 ?   ?   ?   C . n 
C 2 152 LEU 152 131 ?   ?   ?   C . n 
C 2 153 GLN 153 132 ?   ?   ?   C . n 
C 2 154 LYS 154 133 ?   ?   ?   C . n 
C 2 155 LYS 155 134 ?   ?   ?   C . n 
C 2 156 ALA 156 135 ?   ?   ?   C . n 
C 2 157 GLN 157 136 ?   ?   ?   C . n 
C 2 158 MET 158 137 ?   ?   ?   C . n 
C 2 159 ILE 159 138 ?   ?   ?   C . n 
C 2 160 VAL 160 139 ?   ?   ?   C . n 
C 2 161 GLY 161 140 ?   ?   ?   C . n 
C 2 162 LEU 162 141 ?   ?   ?   C . n 
C 2 163 TYR 163 142 ?   ?   ?   C . n 
C 2 164 LYS 164 143 ?   ?   ?   C . n 
C 2 165 ALA 165 144 ?   ?   ?   C . n 
C 2 166 ILE 166 145 ?   ?   ?   C . n 
C 2 167 GLN 167 146 ?   ?   ?   C . n 
C 2 168 LYS 168 147 ?   ?   ?   C . n 
C 2 169 ASP 169 148 ?   ?   ?   C . n 
C 2 170 ASP 170 149 ?   ?   ?   C . n 
C 2 171 GLU 171 150 ?   ?   ?   C . n 
C 2 172 ILE 172 151 ?   ?   ?   C . n 
C 2 173 SER 173 152 ?   ?   ?   C . n 
C 2 174 LEU 174 153 ?   ?   ?   C . n 
C 2 175 PHE 175 154 ?   ?   ?   C . n 
C 2 176 LYS 176 155 ?   ?   ?   C . n 
C 2 177 ALA 177 156 ?   ?   ?   C . n 
C 2 178 MET 178 157 ?   ?   ?   C . n 
C 2 179 VAL 179 158 ?   ?   ?   C . n 
C 2 180 ALA 180 159 ?   ?   ?   C . n 
C 2 181 SER 181 160 ?   ?   ?   C . n 
C 2 182 VAL 182 161 ?   ?   ?   C . n 
C 2 183 TYR 183 162 ?   ?   ?   C . n 
C 2 184 LEU 184 163 ?   ?   ?   C . n 
C 2 185 GLU 185 164 ?   ?   ?   C . n 
C 2 186 SER 186 165 ?   ?   ?   C . n 
C 2 187 PHE 187 166 ?   ?   ?   C . n 
C 2 188 LEU 188 167 ?   ?   ?   C . n 
C 2 189 PHE 189 168 ?   ?   ?   C . n 
C 2 190 TYR 190 169 ?   ?   ?   C . n 
C 2 191 SER 191 170 ?   ?   ?   C . n 
C 2 192 GLY 192 171 ?   ?   ?   C . n 
C 2 193 PHE 193 172 ?   ?   ?   C . n 
C 2 194 TYR 194 173 ?   ?   ?   C . n 
C 2 195 TYR 195 174 ?   ?   ?   C . n 
C 2 196 PRO 196 175 ?   ?   ?   C . n 
C 2 197 LEU 197 176 ?   ?   ?   C . n 
C 2 198 TYR 198 177 ?   ?   ?   C . n 
C 2 199 PHE 199 178 ?   ?   ?   C . n 
C 2 200 TYR 200 179 ?   ?   ?   C . n 
C 2 201 GLY 201 180 ?   ?   ?   C . n 
C 2 202 GLN 202 181 ?   ?   ?   C . n 
C 2 203 GLY 203 182 ?   ?   ?   C . n 
C 2 204 LYS 204 183 ?   ?   ?   C . n 
C 2 205 LEU 205 184 ?   ?   ?   C . n 
C 2 206 MET 206 185 ?   ?   ?   C . n 
C 2 207 GLN 207 186 ?   ?   ?   C . n 
C 2 208 SER 208 187 ?   ?   ?   C . n 
C 2 209 GLY 209 188 ?   ?   ?   C . n 
C 2 210 GLU 210 189 ?   ?   ?   C . n 
C 2 211 ILE 211 190 ?   ?   ?   C . n 
C 2 212 ILE 212 191 ?   ?   ?   C . n 
C 2 213 ASN 213 192 ?   ?   ?   C . n 
C 2 214 LEU 214 193 ?   ?   ?   C . n 
C 2 215 ILE 215 194 ?   ?   ?   C . n 
C 2 216 LEU 216 195 ?   ?   ?   C . n 
C 2 217 ARG 217 196 ?   ?   ?   C . n 
C 2 218 ASP 218 197 ?   ?   ?   C . n 
C 2 219 GLU 219 198 ?   ?   ?   C . n 
C 2 220 ALA 220 199 ?   ?   ?   C . n 
C 2 221 ILE 221 200 ?   ?   ?   C . n 
C 2 222 HIS 222 201 ?   ?   ?   C . n 
C 2 223 GLY 223 202 ?   ?   ?   C . n 
C 2 224 VAL 224 203 ?   ?   ?   C . n 
C 2 225 TYR 225 204 ?   ?   ?   C . n 
C 2 226 VAL 226 205 ?   ?   ?   C . n 
C 2 227 GLY 227 206 ?   ?   ?   C . n 
C 2 228 LEU 228 207 ?   ?   ?   C . n 
C 2 229 LEU 229 208 ?   ?   ?   C . n 
C 2 230 ALA 230 209 ?   ?   ?   C . n 
C 2 231 GLN 231 210 ?   ?   ?   C . n 
C 2 232 GLU 232 211 ?   ?   ?   C . n 
C 2 233 ILE 233 212 ?   ?   ?   C . n 
C 2 234 TYR 234 213 ?   ?   ?   C . n 
C 2 235 ASN 235 214 ?   ?   ?   C . n 
C 2 236 LYS 236 215 ?   ?   ?   C . n 
C 2 237 GLN 237 216 ?   ?   ?   C . n 
C 2 238 THR 238 217 ?   ?   ?   C . n 
C 2 239 GLU 239 218 ?   ?   ?   C . n 
C 2 240 GLU 240 219 ?   ?   ?   C . n 
C 2 241 LYS 241 220 ?   ?   ?   C . n 
C 2 242 LYS 242 221 ?   ?   ?   C . n 
C 2 243 ALA 243 222 ?   ?   ?   C . n 
C 2 244 GLU 244 223 ?   ?   ?   C . n 
C 2 245 LEU 245 224 ?   ?   ?   C . n 
C 2 246 ARG 246 225 ?   ?   ?   C . n 
C 2 247 GLU 247 226 ?   ?   ?   C . n 
C 2 248 PHE 248 227 ?   ?   ?   C . n 
C 2 249 ALA 249 228 ?   ?   ?   C . n 
C 2 250 ILE 250 229 ?   ?   ?   C . n 
C 2 251 ASP 251 230 ?   ?   ?   C . n 
C 2 252 LEU 252 231 ?   ?   ?   C . n 
C 2 253 LEU 253 232 ?   ?   ?   C . n 
C 2 254 ASN 254 233 ?   ?   ?   C . n 
C 2 255 GLN 255 234 ?   ?   ?   C . n 
C 2 256 LEU 256 235 ?   ?   ?   C . n 
C 2 257 TYR 257 236 ?   ?   ?   C . n 
C 2 258 GLU 258 237 ?   ?   ?   C . n 
C 2 259 ASN 259 238 ?   ?   ?   C . n 
C 2 260 GLU 260 239 ?   ?   ?   C . n 
C 2 261 LEU 261 240 ?   ?   ?   C . n 
C 2 262 GLU 262 241 ?   ?   ?   C . n 
C 2 263 TYR 263 242 ?   ?   ?   C . n 
C 2 264 THR 264 243 ?   ?   ?   C . n 
C 2 265 GLU 265 244 ?   ?   ?   C . n 
C 2 266 ASP 266 245 ?   ?   ?   C . n 
C 2 267 LEU 267 246 ?   ?   ?   C . n 
C 2 268 TYR 268 247 ?   ?   ?   C . n 
C 2 269 ASP 269 248 ?   ?   ?   C . n 
C 2 270 GLN 270 249 ?   ?   ?   C . n 
C 2 271 VAL 271 250 ?   ?   ?   C . n 
C 2 272 GLY 272 251 ?   ?   ?   C . n 
C 2 273 LEU 273 252 ?   ?   ?   C . n 
C 2 274 SER 274 253 ?   ?   ?   C . n 
C 2 275 HIS 275 254 ?   ?   ?   C . n 
C 2 276 ASP 276 255 ?   ?   ?   C . n 
C 2 277 VAL 277 256 ?   ?   ?   C . n 
C 2 278 LYS 278 257 ?   ?   ?   C . n 
C 2 279 LYS 279 258 ?   ?   ?   C . n 
C 2 280 PHE 280 259 ?   ?   ?   C . n 
C 2 281 ILE 281 260 ?   ?   ?   C . n 
C 2 282 ARG 282 261 ?   ?   ?   C . n 
C 2 283 TYR 283 262 ?   ?   ?   C . n 
C 2 284 ASN 284 263 ?   ?   ?   C . n 
C 2 285 ALA 285 264 ?   ?   ?   C . n 
C 2 286 ASN 286 265 ?   ?   ?   C . n 
C 2 287 LYS 287 266 ?   ?   ?   C . n 
C 2 288 ALA 288 267 ?   ?   ?   C . n 
C 2 289 LEU 289 268 ?   ?   ?   C . n 
C 2 290 MET 290 269 ?   ?   ?   C . n 
C 2 291 ASN 291 270 ?   ?   ?   C . n 
C 2 292 LEU 292 271 ?   ?   ?   C . n 
C 2 293 GLY 293 272 ?   ?   ?   C . n 
C 2 294 PHE 294 273 ?   ?   ?   C . n 
C 2 295 ASP 295 274 ?   ?   ?   C . n 
C 2 296 PRO 296 275 ?   ?   ?   C . n 
C 2 297 TYR 297 276 ?   ?   ?   C . n 
C 2 298 PHE 298 277 ?   ?   ?   C . n 
C 2 299 GLU 299 278 ?   ?   ?   C . n 
C 2 300 GLU 300 279 ?   ?   ?   C . n 
C 2 301 GLU 301 280 ?   ?   ?   C . n 
C 2 302 ASP 302 281 ?   ?   ?   C . n 
C 2 303 ILE 303 282 ?   ?   ?   C . n 
C 2 304 ASN 304 283 ?   ?   ?   C . n 
C 2 305 PRO 305 284 ?   ?   ?   C . n 
C 2 306 ILE 306 285 ?   ?   ?   C . n 
C 2 307 VAL 307 286 ?   ?   ?   C . n 
C 2 308 LEU 308 287 ?   ?   ?   C . n 
C 2 309 ASN 309 288 ?   ?   ?   C . n 
C 2 310 GLY 310 289 ?   ?   ?   C . n 
C 2 311 LEU 311 290 ?   ?   ?   C . n 
C 2 312 ASN 312 291 ?   ?   ?   C . n 
C 2 313 THR 313 292 ?   ?   ?   C . n 
C 2 314 LYS 314 293 ?   ?   ?   C . n 
C 2 315 THR 315 294 ?   ?   ?   C . n 
C 2 316 LYS 316 295 ?   ?   ?   C . n 
C 2 317 SER 317 296 ?   ?   ?   C . n 
C 2 318 HIS 318 297 ?   ?   ?   C . n 
C 2 319 ASP 319 298 ?   ?   ?   C . n 
C 2 320 PHE 320 299 ?   ?   ?   C . n 
C 2 321 PHE 321 300 ?   ?   ?   C . n 
C 2 322 SER 322 301 ?   ?   ?   C . n 
C 2 323 MET 323 302 ?   ?   ?   C . n 
C 2 324 LYS 324 303 ?   ?   ?   C . n 
C 2 325 GLY 325 304 ?   ?   ?   C . n 
C 2 326 ASN 326 305 ?   ?   ?   C . n 
C 2 327 GLY 327 306 ?   ?   ?   C . n 
C 2 328 TYR 328 307 ?   ?   ?   C . n 
C 2 329 LYS 329 308 ?   ?   ?   C . n 
C 2 330 LYS 330 309 ?   ?   ?   C . n 
C 2 331 ALA 331 310 ?   ?   ?   C . n 
C 2 332 THR 332 311 311 THR THR C . n 
C 2 333 VAL 333 312 312 VAL VAL C . n 
C 2 334 GLU 334 313 313 GLU GLU C . n 
C 2 335 PRO 335 314 314 PRO PRO C . n 
C 2 336 LEU 336 315 315 LEU LEU C . n 
C 2 337 LYS 337 316 316 LYS LYS C . n 
C 2 338 ASP 338 317 317 ASP ASP C . n 
C 2 339 ASP 339 318 318 ASP ASP C . n 
C 2 340 ASP 340 319 319 ASP ASP C . n 
C 2 341 PHE 341 320 320 PHE PHE C . n 
C 2 342 TYR 342 321 321 TYR TYR C . n 
C 2 343 PHE 343 322 322 PHE PHE C . n 
C 2 344 GLU 344 323 ?   ?   ?   C . n 
C 2 345 ASP 345 324 ?   ?   ?   C . n 
C 2 346 GLU 346 325 ?   ?   ?   C . n 
C 2 347 LYS 347 326 ?   ?   ?   C . n 
C 2 348 GLU 348 327 ?   ?   ?   C . n 
C 2 349 GLN 349 328 ?   ?   ?   C . n 
C 2 350 ILE 350 329 ?   ?   ?   C . n 
D 2 1   MET 1   -20 ?   ?   ?   D . n 
D 2 2   GLY 2   -19 ?   ?   ?   D . n 
D 2 3   SER 3   -18 ?   ?   ?   D . n 
D 2 4   SER 4   -17 ?   ?   ?   D . n 
D 2 5   HIS 5   -16 ?   ?   ?   D . n 
D 2 6   HIS 6   -15 ?   ?   ?   D . n 
D 2 7   HIS 7   -14 ?   ?   ?   D . n 
D 2 8   HIS 8   -13 ?   ?   ?   D . n 
D 2 9   HIS 9   -12 ?   ?   ?   D . n 
D 2 10  HIS 10  -11 ?   ?   ?   D . n 
D 2 11  SER 11  -10 ?   ?   ?   D . n 
D 2 12  SER 12  -9  ?   ?   ?   D . n 
D 2 13  GLY 13  -8  ?   ?   ?   D . n 
D 2 14  LEU 14  -7  ?   ?   ?   D . n 
D 2 15  VAL 15  -6  ?   ?   ?   D . n 
D 2 16  PRO 16  -5  ?   ?   ?   D . n 
D 2 17  ARG 17  -4  ?   ?   ?   D . n 
D 2 18  GLY 18  -3  ?   ?   ?   D . n 
D 2 19  SER 19  -2  ?   ?   ?   D . n 
D 2 20  HIS 20  -1  ?   ?   ?   D . n 
D 2 21  MET 21  0   ?   ?   ?   D . n 
D 2 22  MET 22  1   ?   ?   ?   D . n 
D 2 23  THR 23  2   ?   ?   ?   D . n 
D 2 24  LYS 24  3   ?   ?   ?   D . n 
D 2 25  ILE 25  4   ?   ?   ?   D . n 
D 2 26  TYR 26  5   ?   ?   ?   D . n 
D 2 27  ASP 27  6   ?   ?   ?   D . n 
D 2 28  ALA 28  7   ?   ?   ?   D . n 
D 2 29  ALA 29  8   ?   ?   ?   D . n 
D 2 30  ASN 30  9   ?   ?   ?   D . n 
D 2 31  TRP 31  10  ?   ?   ?   D . n 
D 2 32  SER 32  11  ?   ?   ?   D . n 
D 2 33  LYS 33  12  ?   ?   ?   D . n 
D 2 34  HIS 34  13  ?   ?   ?   D . n 
D 2 35  GLU 35  14  ?   ?   ?   D . n 
D 2 36  ASP 36  15  ?   ?   ?   D . n 
D 2 37  ASP 37  16  ?   ?   ?   D . n 
D 2 38  PHE 38  17  ?   ?   ?   D . n 
D 2 39  THR 39  18  ?   ?   ?   D . n 
D 2 40  GLN 40  19  ?   ?   ?   D . n 
D 2 41  MET 41  20  ?   ?   ?   D . n 
D 2 42  PHE 42  21  ?   ?   ?   D . n 
D 2 43  TYR 43  22  ?   ?   ?   D . n 
D 2 44  ASN 44  23  ?   ?   ?   D . n 
D 2 45  GLN 45  24  ?   ?   ?   D . n 
D 2 46  ASN 46  25  ?   ?   ?   D . n 
D 2 47  VAL 47  26  ?   ?   ?   D . n 
D 2 48  LYS 48  27  ?   ?   ?   D . n 
D 2 49  GLN 49  28  ?   ?   ?   D . n 
D 2 50  PHE 50  29  ?   ?   ?   D . n 
D 2 51  TRP 51  30  ?   ?   ?   D . n 
D 2 52  LEU 52  31  ?   ?   ?   D . n 
D 2 53  PRO 53  32  ?   ?   ?   D . n 
D 2 54  GLU 54  33  ?   ?   ?   D . n 
D 2 55  GLU 55  34  ?   ?   ?   D . n 
D 2 56  ILE 56  35  ?   ?   ?   D . n 
D 2 57  ALA 57  36  ?   ?   ?   D . n 
D 2 58  LEU 58  37  ?   ?   ?   D . n 
D 2 59  ASN 59  38  ?   ?   ?   D . n 
D 2 60  GLY 60  39  ?   ?   ?   D . n 
D 2 61  ASP 61  40  ?   ?   ?   D . n 
D 2 62  LEU 62  41  ?   ?   ?   D . n 
D 2 63  LEU 63  42  ?   ?   ?   D . n 
D 2 64  THR 64  43  ?   ?   ?   D . n 
D 2 65  TRP 65  44  ?   ?   ?   D . n 
D 2 66  LYS 66  45  ?   ?   ?   D . n 
D 2 67  TYR 67  46  ?   ?   ?   D . n 
D 2 68  LEU 68  47  ?   ?   ?   D . n 
D 2 69  GLY 69  48  ?   ?   ?   D . n 
D 2 70  LYS 70  49  ?   ?   ?   D . n 
D 2 71  ASN 71  50  ?   ?   ?   D . n 
D 2 72  GLU 72  51  ?   ?   ?   D . n 
D 2 73  GLN 73  52  ?   ?   ?   D . n 
D 2 74  ASP 74  53  ?   ?   ?   D . n 
D 2 75  THR 75  54  ?   ?   ?   D . n 
D 2 76  TYR 76  55  ?   ?   ?   D . n 
D 2 77  MET 77  56  ?   ?   ?   D . n 
D 2 78  LYS 78  57  ?   ?   ?   D . n 
D 2 79  VAL 79  58  ?   ?   ?   D . n 
D 2 80  LEU 80  59  ?   ?   ?   D . n 
D 2 81  ALA 81  60  ?   ?   ?   D . n 
D 2 82  GLY 82  61  ?   ?   ?   D . n 
D 2 83  LEU 83  62  ?   ?   ?   D . n 
D 2 84  THR 84  63  ?   ?   ?   D . n 
D 2 85  LEU 85  64  ?   ?   ?   D . n 
D 2 86  LEU 86  65  ?   ?   ?   D . n 
D 2 87  ASP 87  66  ?   ?   ?   D . n 
D 2 88  THR 88  67  ?   ?   ?   D . n 
D 2 89  GLU 89  68  ?   ?   ?   D . n 
D 2 90  GLN 90  69  ?   ?   ?   D . n 
D 2 91  GLY 91  70  ?   ?   ?   D . n 
D 2 92  ASN 92  71  ?   ?   ?   D . n 
D 2 93  THR 93  72  ?   ?   ?   D . n 
D 2 94  GLY 94  73  ?   ?   ?   D . n 
D 2 95  MET 95  74  ?   ?   ?   D . n 
D 2 96  PRO 96  75  ?   ?   ?   D . n 
D 2 97  ILE 97  76  ?   ?   ?   D . n 
D 2 98  VAL 98  77  ?   ?   ?   D . n 
D 2 99  ALA 99  78  ?   ?   ?   D . n 
D 2 100 GLU 100 79  ?   ?   ?   D . n 
D 2 101 HIS 101 80  ?   ?   ?   D . n 
D 2 102 VAL 102 81  ?   ?   ?   D . n 
D 2 103 ASP 103 82  ?   ?   ?   D . n 
D 2 104 GLY 104 83  ?   ?   ?   D . n 
D 2 105 HIS 105 84  ?   ?   ?   D . n 
D 2 106 GLN 106 85  ?   ?   ?   D . n 
D 2 107 ARG 107 86  ?   ?   ?   D . n 
D 2 108 LYS 108 87  ?   ?   ?   D . n 
D 2 109 ALA 109 88  ?   ?   ?   D . n 
D 2 110 VAL 110 89  ?   ?   ?   D . n 
D 2 111 LEU 111 90  ?   ?   ?   D . n 
D 2 112 ASN 112 91  ?   ?   ?   D . n 
D 2 113 PHE 113 92  ?   ?   ?   D . n 
D 2 114 MET 114 93  ?   ?   ?   D . n 
D 2 115 ALA 115 94  ?   ?   ?   D . n 
D 2 116 MET 116 95  ?   ?   ?   D . n 
D 2 117 MET 117 96  ?   ?   ?   D . n 
D 2 118 GLU 118 97  ?   ?   ?   D . n 
D 2 119 ASN 119 98  ?   ?   ?   D . n 
D 2 120 ALA 120 99  ?   ?   ?   D . n 
D 2 121 VAL 121 100 ?   ?   ?   D . n 
D 2 122 HIS 122 101 ?   ?   ?   D . n 
D 2 123 ALA 123 102 ?   ?   ?   D . n 
D 2 124 LYS 124 103 ?   ?   ?   D . n 
D 2 125 SER 125 104 ?   ?   ?   D . n 
D 2 126 TYR 126 105 ?   ?   ?   D . n 
D 2 127 SER 127 106 ?   ?   ?   D . n 
D 2 128 ASN 128 107 ?   ?   ?   D . n 
D 2 129 ILE 129 108 ?   ?   ?   D . n 
D 2 130 PHE 130 109 ?   ?   ?   D . n 
D 2 131 MET 131 110 ?   ?   ?   D . n 
D 2 132 THR 132 111 ?   ?   ?   D . n 
D 2 133 LEU 133 112 ?   ?   ?   D . n 
D 2 134 ALA 134 113 ?   ?   ?   D . n 
D 2 135 PRO 135 114 ?   ?   ?   D . n 
D 2 136 THR 136 115 ?   ?   ?   D . n 
D 2 137 GLU 137 116 ?   ?   ?   D . n 
D 2 138 THR 138 117 ?   ?   ?   D . n 
D 2 139 ILE 139 118 ?   ?   ?   D . n 
D 2 140 ASN 140 119 ?   ?   ?   D . n 
D 2 141 GLU 141 120 ?   ?   ?   D . n 
D 2 142 VAL 142 121 ?   ?   ?   D . n 
D 2 143 PHE 143 122 ?   ?   ?   D . n 
D 2 144 GLU 144 123 ?   ?   ?   D . n 
D 2 145 TRP 145 124 ?   ?   ?   D . n 
D 2 146 VAL 146 125 ?   ?   ?   D . n 
D 2 147 LYS 147 126 ?   ?   ?   D . n 
D 2 148 GLN 148 127 ?   ?   ?   D . n 
D 2 149 ASN 149 128 ?   ?   ?   D . n 
D 2 150 LYS 150 129 ?   ?   ?   D . n 
D 2 151 TYR 151 130 ?   ?   ?   D . n 
D 2 152 LEU 152 131 ?   ?   ?   D . n 
D 2 153 GLN 153 132 ?   ?   ?   D . n 
D 2 154 LYS 154 133 ?   ?   ?   D . n 
D 2 155 LYS 155 134 ?   ?   ?   D . n 
D 2 156 ALA 156 135 ?   ?   ?   D . n 
D 2 157 GLN 157 136 ?   ?   ?   D . n 
D 2 158 MET 158 137 ?   ?   ?   D . n 
D 2 159 ILE 159 138 ?   ?   ?   D . n 
D 2 160 VAL 160 139 ?   ?   ?   D . n 
D 2 161 GLY 161 140 ?   ?   ?   D . n 
D 2 162 LEU 162 141 ?   ?   ?   D . n 
D 2 163 TYR 163 142 ?   ?   ?   D . n 
D 2 164 LYS 164 143 ?   ?   ?   D . n 
D 2 165 ALA 165 144 ?   ?   ?   D . n 
D 2 166 ILE 166 145 ?   ?   ?   D . n 
D 2 167 GLN 167 146 ?   ?   ?   D . n 
D 2 168 LYS 168 147 ?   ?   ?   D . n 
D 2 169 ASP 169 148 ?   ?   ?   D . n 
D 2 170 ASP 170 149 ?   ?   ?   D . n 
D 2 171 GLU 171 150 ?   ?   ?   D . n 
D 2 172 ILE 172 151 ?   ?   ?   D . n 
D 2 173 SER 173 152 ?   ?   ?   D . n 
D 2 174 LEU 174 153 ?   ?   ?   D . n 
D 2 175 PHE 175 154 ?   ?   ?   D . n 
D 2 176 LYS 176 155 ?   ?   ?   D . n 
D 2 177 ALA 177 156 ?   ?   ?   D . n 
D 2 178 MET 178 157 ?   ?   ?   D . n 
D 2 179 VAL 179 158 ?   ?   ?   D . n 
D 2 180 ALA 180 159 ?   ?   ?   D . n 
D 2 181 SER 181 160 ?   ?   ?   D . n 
D 2 182 VAL 182 161 ?   ?   ?   D . n 
D 2 183 TYR 183 162 ?   ?   ?   D . n 
D 2 184 LEU 184 163 ?   ?   ?   D . n 
D 2 185 GLU 185 164 ?   ?   ?   D . n 
D 2 186 SER 186 165 ?   ?   ?   D . n 
D 2 187 PHE 187 166 ?   ?   ?   D . n 
D 2 188 LEU 188 167 ?   ?   ?   D . n 
D 2 189 PHE 189 168 ?   ?   ?   D . n 
D 2 190 TYR 190 169 ?   ?   ?   D . n 
D 2 191 SER 191 170 ?   ?   ?   D . n 
D 2 192 GLY 192 171 ?   ?   ?   D . n 
D 2 193 PHE 193 172 ?   ?   ?   D . n 
D 2 194 TYR 194 173 ?   ?   ?   D . n 
D 2 195 TYR 195 174 ?   ?   ?   D . n 
D 2 196 PRO 196 175 ?   ?   ?   D . n 
D 2 197 LEU 197 176 ?   ?   ?   D . n 
D 2 198 TYR 198 177 ?   ?   ?   D . n 
D 2 199 PHE 199 178 ?   ?   ?   D . n 
D 2 200 TYR 200 179 ?   ?   ?   D . n 
D 2 201 GLY 201 180 ?   ?   ?   D . n 
D 2 202 GLN 202 181 ?   ?   ?   D . n 
D 2 203 GLY 203 182 ?   ?   ?   D . n 
D 2 204 LYS 204 183 ?   ?   ?   D . n 
D 2 205 LEU 205 184 ?   ?   ?   D . n 
D 2 206 MET 206 185 ?   ?   ?   D . n 
D 2 207 GLN 207 186 ?   ?   ?   D . n 
D 2 208 SER 208 187 ?   ?   ?   D . n 
D 2 209 GLY 209 188 ?   ?   ?   D . n 
D 2 210 GLU 210 189 ?   ?   ?   D . n 
D 2 211 ILE 211 190 ?   ?   ?   D . n 
D 2 212 ILE 212 191 ?   ?   ?   D . n 
D 2 213 ASN 213 192 ?   ?   ?   D . n 
D 2 214 LEU 214 193 ?   ?   ?   D . n 
D 2 215 ILE 215 194 ?   ?   ?   D . n 
D 2 216 LEU 216 195 ?   ?   ?   D . n 
D 2 217 ARG 217 196 ?   ?   ?   D . n 
D 2 218 ASP 218 197 ?   ?   ?   D . n 
D 2 219 GLU 219 198 ?   ?   ?   D . n 
D 2 220 ALA 220 199 ?   ?   ?   D . n 
D 2 221 ILE 221 200 ?   ?   ?   D . n 
D 2 222 HIS 222 201 ?   ?   ?   D . n 
D 2 223 GLY 223 202 ?   ?   ?   D . n 
D 2 224 VAL 224 203 ?   ?   ?   D . n 
D 2 225 TYR 225 204 ?   ?   ?   D . n 
D 2 226 VAL 226 205 ?   ?   ?   D . n 
D 2 227 GLY 227 206 ?   ?   ?   D . n 
D 2 228 LEU 228 207 ?   ?   ?   D . n 
D 2 229 LEU 229 208 ?   ?   ?   D . n 
D 2 230 ALA 230 209 ?   ?   ?   D . n 
D 2 231 GLN 231 210 ?   ?   ?   D . n 
D 2 232 GLU 232 211 ?   ?   ?   D . n 
D 2 233 ILE 233 212 ?   ?   ?   D . n 
D 2 234 TYR 234 213 ?   ?   ?   D . n 
D 2 235 ASN 235 214 ?   ?   ?   D . n 
D 2 236 LYS 236 215 ?   ?   ?   D . n 
D 2 237 GLN 237 216 ?   ?   ?   D . n 
D 2 238 THR 238 217 ?   ?   ?   D . n 
D 2 239 GLU 239 218 ?   ?   ?   D . n 
D 2 240 GLU 240 219 ?   ?   ?   D . n 
D 2 241 LYS 241 220 ?   ?   ?   D . n 
D 2 242 LYS 242 221 ?   ?   ?   D . n 
D 2 243 ALA 243 222 ?   ?   ?   D . n 
D 2 244 GLU 244 223 ?   ?   ?   D . n 
D 2 245 LEU 245 224 ?   ?   ?   D . n 
D 2 246 ARG 246 225 ?   ?   ?   D . n 
D 2 247 GLU 247 226 ?   ?   ?   D . n 
D 2 248 PHE 248 227 ?   ?   ?   D . n 
D 2 249 ALA 249 228 ?   ?   ?   D . n 
D 2 250 ILE 250 229 ?   ?   ?   D . n 
D 2 251 ASP 251 230 ?   ?   ?   D . n 
D 2 252 LEU 252 231 ?   ?   ?   D . n 
D 2 253 LEU 253 232 ?   ?   ?   D . n 
D 2 254 ASN 254 233 ?   ?   ?   D . n 
D 2 255 GLN 255 234 ?   ?   ?   D . n 
D 2 256 LEU 256 235 ?   ?   ?   D . n 
D 2 257 TYR 257 236 ?   ?   ?   D . n 
D 2 258 GLU 258 237 ?   ?   ?   D . n 
D 2 259 ASN 259 238 ?   ?   ?   D . n 
D 2 260 GLU 260 239 ?   ?   ?   D . n 
D 2 261 LEU 261 240 ?   ?   ?   D . n 
D 2 262 GLU 262 241 ?   ?   ?   D . n 
D 2 263 TYR 263 242 ?   ?   ?   D . n 
D 2 264 THR 264 243 ?   ?   ?   D . n 
D 2 265 GLU 265 244 ?   ?   ?   D . n 
D 2 266 ASP 266 245 ?   ?   ?   D . n 
D 2 267 LEU 267 246 ?   ?   ?   D . n 
D 2 268 TYR 268 247 ?   ?   ?   D . n 
D 2 269 ASP 269 248 ?   ?   ?   D . n 
D 2 270 GLN 270 249 ?   ?   ?   D . n 
D 2 271 VAL 271 250 ?   ?   ?   D . n 
D 2 272 GLY 272 251 ?   ?   ?   D . n 
D 2 273 LEU 273 252 ?   ?   ?   D . n 
D 2 274 SER 274 253 ?   ?   ?   D . n 
D 2 275 HIS 275 254 ?   ?   ?   D . n 
D 2 276 ASP 276 255 ?   ?   ?   D . n 
D 2 277 VAL 277 256 ?   ?   ?   D . n 
D 2 278 LYS 278 257 ?   ?   ?   D . n 
D 2 279 LYS 279 258 ?   ?   ?   D . n 
D 2 280 PHE 280 259 ?   ?   ?   D . n 
D 2 281 ILE 281 260 ?   ?   ?   D . n 
D 2 282 ARG 282 261 ?   ?   ?   D . n 
D 2 283 TYR 283 262 ?   ?   ?   D . n 
D 2 284 ASN 284 263 ?   ?   ?   D . n 
D 2 285 ALA 285 264 ?   ?   ?   D . n 
D 2 286 ASN 286 265 ?   ?   ?   D . n 
D 2 287 LYS 287 266 ?   ?   ?   D . n 
D 2 288 ALA 288 267 ?   ?   ?   D . n 
D 2 289 LEU 289 268 ?   ?   ?   D . n 
D 2 290 MET 290 269 ?   ?   ?   D . n 
D 2 291 ASN 291 270 ?   ?   ?   D . n 
D 2 292 LEU 292 271 ?   ?   ?   D . n 
D 2 293 GLY 293 272 ?   ?   ?   D . n 
D 2 294 PHE 294 273 ?   ?   ?   D . n 
D 2 295 ASP 295 274 ?   ?   ?   D . n 
D 2 296 PRO 296 275 ?   ?   ?   D . n 
D 2 297 TYR 297 276 ?   ?   ?   D . n 
D 2 298 PHE 298 277 ?   ?   ?   D . n 
D 2 299 GLU 299 278 ?   ?   ?   D . n 
D 2 300 GLU 300 279 ?   ?   ?   D . n 
D 2 301 GLU 301 280 ?   ?   ?   D . n 
D 2 302 ASP 302 281 ?   ?   ?   D . n 
D 2 303 ILE 303 282 ?   ?   ?   D . n 
D 2 304 ASN 304 283 ?   ?   ?   D . n 
D 2 305 PRO 305 284 ?   ?   ?   D . n 
D 2 306 ILE 306 285 ?   ?   ?   D . n 
D 2 307 VAL 307 286 ?   ?   ?   D . n 
D 2 308 LEU 308 287 ?   ?   ?   D . n 
D 2 309 ASN 309 288 ?   ?   ?   D . n 
D 2 310 GLY 310 289 ?   ?   ?   D . n 
D 2 311 LEU 311 290 ?   ?   ?   D . n 
D 2 312 ASN 312 291 ?   ?   ?   D . n 
D 2 313 THR 313 292 ?   ?   ?   D . n 
D 2 314 LYS 314 293 ?   ?   ?   D . n 
D 2 315 THR 315 294 ?   ?   ?   D . n 
D 2 316 LYS 316 295 ?   ?   ?   D . n 
D 2 317 SER 317 296 ?   ?   ?   D . n 
D 2 318 HIS 318 297 ?   ?   ?   D . n 
D 2 319 ASP 319 298 ?   ?   ?   D . n 
D 2 320 PHE 320 299 ?   ?   ?   D . n 
D 2 321 PHE 321 300 ?   ?   ?   D . n 
D 2 322 SER 322 301 ?   ?   ?   D . n 
D 2 323 MET 323 302 ?   ?   ?   D . n 
D 2 324 LYS 324 303 ?   ?   ?   D . n 
D 2 325 GLY 325 304 ?   ?   ?   D . n 
D 2 326 ASN 326 305 ?   ?   ?   D . n 
D 2 327 GLY 327 306 ?   ?   ?   D . n 
D 2 328 TYR 328 307 ?   ?   ?   D . n 
D 2 329 LYS 329 308 ?   ?   ?   D . n 
D 2 330 LYS 330 309 ?   ?   ?   D . n 
D 2 331 ALA 331 310 ?   ?   ?   D . n 
D 2 332 THR 332 311 311 THR THR D . n 
D 2 333 VAL 333 312 312 VAL VAL D . n 
D 2 334 GLU 334 313 313 GLU GLU D . n 
D 2 335 PRO 335 314 314 PRO PRO D . n 
D 2 336 LEU 336 315 315 LEU LEU D . n 
D 2 337 LYS 337 316 316 LYS LYS D . n 
D 2 338 ASP 338 317 317 ASP ASP D . n 
D 2 339 ASP 339 318 318 ASP ASP D . n 
D 2 340 ASP 340 319 319 ASP ASP D . n 
D 2 341 PHE 341 320 320 PHE PHE D . n 
D 2 342 TYR 342 321 321 TYR TYR D . n 
D 2 343 PHE 343 322 322 PHE PHE D . n 
D 2 344 GLU 344 323 ?   ?   ?   D . n 
D 2 345 ASP 345 324 ?   ?   ?   D . n 
D 2 346 GLU 346 325 ?   ?   ?   D . n 
D 2 347 LYS 347 326 ?   ?   ?   D . n 
D 2 348 GLU 348 327 ?   ?   ?   D . n 
D 2 349 GLN 349 328 ?   ?   ?   D . n 
D 2 350 ILE 350 329 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 TTP 1 801 801 TTP TTP A . 
F 4 MG  1 802 802 MG  MG  A . 
G 5 ATP 1 803 803 ATP ATP A . 
H 3 TTP 1 801 801 TTP TTP B . 
I 4 MG  1 802 802 MG  MG  B . 
J 5 ATP 1 803 803 ATP ATP B . 
# 
_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                     9BW3 
_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                         9BW3 
_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                   9BW3 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BW3 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            . 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.002 ? 11690 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.407 ? 15778 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 8.942 ? 1562  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 1678  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003 ? 2014  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BW3 
_struct.title                        
'Consensus model for preturnover condition of Bacillus subtilis ribonucleotide reductase complex' 
_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        9BW3 
_struct_keywords.text            'ribonucleotide reductase preturnover condition, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
# 
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 RIR1_BACSU P50620 ? 1 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
1 
2 UNP RIR2_BACSU P50621 ? 2 
;MTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVLAGLTLLDTEQGNTGMPIVAEH
VDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIVGLYKAIQKDDEISLFKAMVAS
VYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEEKKAELREFAIDLLNQLYENEL
EYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDFFSMKGNGYKKATVEPLKDDDF
YFEDEKEQI
;
1 
# 
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 9BW3 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BW3 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BW3 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BW3 D 22 ? 350 ? P50621 1 ? 329 ? 1 329 
# 
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 
3 9BW3 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BW3 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BW3 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BW3 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BW3 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BW3 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BW3 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BW3 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BW3 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BW3 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BW3 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BW3 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BW3 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BW3 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BW3 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BW3 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BW3 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BW3 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BW3 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BW3 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BW3 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BW3 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BW3 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BW3 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BW3 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BW3 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BW3 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BW3 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BW3 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BW3 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BW3 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BW3 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BW3 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BW3 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BW3 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BW3 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BW3 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BW3 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BW3 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BW3 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BW3 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BW3 MET D 21 ? UNP P50621 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 PRO A 7   ? GLU A 15  ? PRO A 7   GLU A 15  1 ? 9  
HELX_P HELX_P2  AA2 ASP A 27  ? ILE A 41  ? ASP A 27  ILE A 41  1 ? 15 
HELX_P HELX_P3  AA3 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P4  AA4 GLU A 65  ? SER A 70  ? GLU A 65  SER A 70  1 ? 6  
HELX_P HELX_P5  AA5 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P6  AA6 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P7  AA7 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P8  AA8 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P9  AA9 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P10 AB1 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P11 AB2 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P12 AB3 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P14 AB5 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P15 AB6 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P16 AB7 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P17 AB8 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P18 AB9 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P19 AC1 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P20 AC2 ILE A 416 ? LYS A 423 ? ILE A 416 LYS A 423 1 ? 8  
HELX_P HELX_P21 AC3 SER A 424 ? THR A 442 ? SER A 424 THR A 442 1 ? 19 
HELX_P HELX_P22 AC4 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P23 AC5 ASN A 467 ? GLN A 474 ? ASN A 467 GLN A 474 1 ? 8  
HELX_P HELX_P24 AC6 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P25 AC7 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P26 AC8 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P27 AC9 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P28 AD1 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P29 AD2 SER A 583 ? SER A 589 ? SER A 583 SER A 589 1 ? 7  
HELX_P HELX_P30 AD3 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P31 AD4 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P32 AD5 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P33 AD6 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P34 AD7 ASP B 27  ? ILE B 41  ? ASP B 27  ILE B 41  1 ? 15 
HELX_P HELX_P35 AD8 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P36 AD9 GLU B 65  ? SER B 70  ? GLU B 65  SER B 70  1 ? 6  
HELX_P HELX_P37 AE1 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P38 AE2 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P39 AE3 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P40 AE4 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P41 AE5 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P42 AE6 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P43 AE7 GLY B 222 ? ALA B 237 ? GLY B 222 ALA B 237 1 ? 16 
HELX_P HELX_P44 AE8 ASP B 238 ? GLN B 242 ? ASP B 238 GLN B 242 5 ? 5  
HELX_P HELX_P45 AE9 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P46 AF1 PRO B 285 ? ASP B 295 ? PRO B 285 ASP B 295 1 ? 11 
HELX_P HELX_P47 AF2 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P48 AF3 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P49 AF4 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P50 AF5 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P51 AF6 GLN B 361 ? VAL B 367 ? GLN B 361 VAL B 367 1 ? 7  
HELX_P HELX_P52 AF7 ILE B 416 ? LYS B 423 ? ILE B 416 LYS B 423 1 ? 8  
HELX_P HELX_P53 AF8 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P54 AF9 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P55 AG1 ASN B 467 ? GLN B 474 ? ASN B 467 GLN B 474 1 ? 8  
HELX_P HELX_P56 AG2 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P57 AG3 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P58 AG4 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P59 AG5 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P60 AG6 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P61 AG7 SER B 583 ? SER B 589 ? SER B 583 SER B 589 1 ? 7  
HELX_P HELX_P62 AG8 GLU B 628 ? MET B 632 ? GLU B 628 MET B 632 5 ? 5  
HELX_P HELX_P63 AG9 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P64 AH1 THR B 663 ? ARG B 677 ? THR B 663 ARG B 677 1 ? 15 
HELX_P HELX_P65 AH2 LYS C 337 ? TYR C 342 ? LYS C 316 TYR C 321 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? E TTP . O2A ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc2 metalc ? ? E TTP . O1B ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 1.919 ? ? 
metalc3 metalc ? ? H TTP . O2A ? ? ? 1_555 I MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 1.928 ? ? 
metalc4 metalc ? ? H TTP . O1B ? ? ? 1_555 I MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc5 metalc ? ? H TTP . O3G ? ? ? 1_555 I MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 O2A ? E TTP . ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1B ? E TTP . ? A TTP 801 ? 1_555 71.4 ? 
2 O2A ? H TTP . ? B TTP 801 ? 1_555 MG ? I MG . ? B MG 802 ? 1_555 O1B ? H TTP . ? B TTP 801 ? 1_555 69.5 ? 
3 O2A ? H TTP . ? B TTP 801 ? 1_555 MG ? I MG . ? B MG 802 ? 1_555 O3G ? H TTP . ? B TTP 801 ? 1_555 94.0 ? 
4 O1B ? H TTP . ? B TTP 801 ? 1_555 MG ? I MG . ? B MG 802 ? 1_555 O3G ? H TTP . ? B TTP 801 ? 1_555 69.8 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 -3.70 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -1.59 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 7 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA7 6 7 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA1 2 ILE A 407 ? ASN A 415 ? ILE A 407 ASN A 415 
AA1 3 ILE A 461 ? MET A 466 ? ILE A 461 MET A 466 
AA2 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA2 2 ILE A 407 ? ASN A 415 ? ILE A 407 ASN A 415 
AA2 3 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 4 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 5 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 6 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 7 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 8 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA3 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA3 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA4 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA4 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA5 1 THR A 655 ? LEU A 658 ? THR A 655 LEU A 658 
AA5 2 TYR A 684 ? THR A 687 ? TYR A 684 THR A 687 
AA6 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA6 2 ASN B 410 ? ASN B 415 ? ASN B 410 ASN B 415 
AA6 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA7 1 ILE B 407 ? SER B 408 ? ILE B 407 SER B 408 
AA7 2 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 3 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 4 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 5 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 6 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 7 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA8 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA8 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AA9 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AA9 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB1 1 THR B 655 ? LYS B 659 ? THR B 655 LYS B 659 
AB1 2 TYR B 684 ? LYS B 688 ? TYR B 684 LYS B 688 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA1 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA2 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA2 2 3 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 3 4 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA2 4 5 N LEU A 201 ? N LEU A 201 O ALA A 248 ? O ALA A 248 
AA2 5 6 N ALA A 249 ? N ALA A 249 O SER A 279 ? O SER A 279 
AA2 6 7 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 7 8 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N ALA A 298 ? N ALA A 298 O ILE A 337 ? O ILE A 337 
AA4 1 2 N ARG A 604 ? N ARG A 604 O THR A 611 ? O THR A 611 
AA5 1 2 N LEU A 656 ? N LEU A 656 O TYR A 684 ? O TYR A 684 
AA6 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA6 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA7 1 2 O ILE B 407 ? O ILE B 407 N LEU B 172 ? N LEU B 172 
AA7 2 3 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 3 4 N LEU B 201 ? N LEU B 201 O ALA B 248 ? O ALA B 248 
AA7 4 5 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA7 5 6 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA7 6 7 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA8 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AA9 1 2 N GLU B 602 ? N GLU B 602 O TYR B 613 ? O TYR B 613 
AB1 1 2 N LEU B 658 ? N LEU B 658 O ARG B 686 ? O ARG B 686 
# 
_pdbx_entry_details.entry_id                   9BW3 
_pdbx_entry_details.has_ligand_of_interest     N 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B PRO 616 ? ? OH    B TYR 626 ? ? 1.99 
2  1 OG1 A THR 663 ? ? OE2   C GLU 313 ? ? 2.02 
3  1 OH  B TYR 64  ? ? OE2   B GLU 116 ? ? 2.02 
4  1 OE2 A GLU 148 ? ? OG    A SER 424 ? ? 2.03 
5  1 OH  B TYR 63  ? ? OD1   B ASN 109 ? ? 2.06 
6  1 O   A PRO 616 ? ? OH    A TYR 626 ? ? 2.07 
7  1 NZ  A LYS 530 ? ? O     A GLN 646 ? ? 2.11 
8  1 OH  A TYR 64  ? ? OE2   A GLU 116 ? ? 2.13 
9  1 NZ  B LYS 214 ? ? O1G   B TTP 801 ? ? 2.13 
10 1 O   A ILE 41  ? ? OG1   A THR 45  ? ? 2.15 
11 1 NH2 A ARG 121 ? ? O     A ALA 159 ? ? 2.16 
12 1 OE2 B GLU 441 ? ? NZ    B LYS 510 ? ? 2.16 
13 1 NZ  A LYS 377 ? ? O     A SER 389 ? ? 2.17 
14 1 NE2 A HIS 372 ? ? O     A GLN 516 ? ? 2.17 
15 1 OD1 B ASP 177 ? ? "O3'" B TTP 801 ? ? 2.18 
16 1 NE2 B HIS 372 ? ? O     B GLN 516 ? ? 2.19 
17 1 OH  A TYR 63  ? ? OD1   A ASN 109 ? ? 2.19 
# 
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 MET A 240 ? ? 74.63   -5.69   
2 1 ASP A 398 ? ? 77.21   -4.40   
3 1 SER A 593 ? ? 52.93   -147.90 
4 1 LYS B 214 ? ? 60.08   61.84   
5 1 ASP B 238 ? ? -94.43  31.24   
6 1 ARG B 243 ? ? -160.35 114.31  
7 1 ASP B 398 ? ? 79.05   -2.90   
8 1 SER B 593 ? ? 52.84   -146.29 
9 1 ASP D 317 ? ? 69.49   -4.54   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BW3 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_em_3d_fitting_list.pdb_chain_id                  . 
_em_3d_fitting_list.pdb_chain_residue_range       . 
_em_3d_fitting_list.details                       'Phenix real space refine from AF2 prediction of Uniprot entry P50620' 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   AlphaFold 
_em_3d_fitting_list.type                          'in silico model' 
_em_3d_fitting_list.accession_code                ? 
_em_3d_fitting_list.initial_refinement_model_id   ? 
# 
_em_3d_reconstruction.entry_id                    9BW3 
_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                  2.42 
_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               665600 
_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       '50 mM HEPES, 150 mM NaCl, 15 mM MgCl2, 5% (w/v) glycerol' 
_em_buffer.pH            7.6 
# 
_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                 'Bacillus subtilis ribonucleotide reductase complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9BW3 
_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           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_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             800 
_em_imaging.nominal_defocus_max             2000 
_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             'COMA FREE' 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9BW3 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   298 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BW3 
_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 1   ? A MET 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A ASP 689 ? A ASP 689 
7   1 Y 1 A THR 690 ? A THR 690 
8   1 Y 1 A GLY 691 ? A GLY 691 
9   1 Y 1 A GLN 692 ? A GLN 692 
10  1 Y 1 A ASP 693 ? A ASP 693 
11  1 Y 1 A SER 694 ? A SER 694 
12  1 Y 1 A CYS 695 ? A CYS 695 
13  1 Y 1 A LEU 696 ? A LEU 696 
14  1 Y 1 A SER 697 ? A SER 697 
15  1 Y 1 A CYS 698 ? A CYS 698 
16  1 Y 1 A VAL 699 ? A VAL 699 
17  1 Y 1 A VAL 700 ? A VAL 700 
18  1 Y 1 B MET 1   ? B MET 1   
19  1 Y 1 B SER 2   ? B SER 2   
20  1 Y 1 B GLN 3   ? B GLN 3   
21  1 Y 1 B ASN 4   ? B ASN 4   
22  1 Y 1 B GLN 5   ? B GLN 5   
23  1 Y 1 B ASP 689 ? B ASP 689 
24  1 Y 1 B THR 690 ? B THR 690 
25  1 Y 1 B GLY 691 ? B GLY 691 
26  1 Y 1 B GLN 692 ? B GLN 692 
27  1 Y 1 B ASP 693 ? B ASP 693 
28  1 Y 1 B SER 694 ? B SER 694 
29  1 Y 1 B CYS 695 ? B CYS 695 
30  1 Y 1 B LEU 696 ? B LEU 696 
31  1 Y 1 B SER 697 ? B SER 697 
32  1 Y 1 B CYS 698 ? B CYS 698 
33  1 Y 1 B VAL 699 ? B VAL 699 
34  1 Y 1 B VAL 700 ? B VAL 700 
35  1 Y 1 C MET -20 ? C MET 1   
36  1 Y 1 C GLY -19 ? C GLY 2   
37  1 Y 1 C SER -18 ? C SER 3   
38  1 Y 1 C SER -17 ? C SER 4   
39  1 Y 1 C HIS -16 ? C HIS 5   
40  1 Y 1 C HIS -15 ? C HIS 6   
41  1 Y 1 C HIS -14 ? C HIS 7   
42  1 Y 1 C HIS -13 ? C HIS 8   
43  1 Y 1 C HIS -12 ? C HIS 9   
44  1 Y 1 C HIS -11 ? C HIS 10  
45  1 Y 1 C SER -10 ? C SER 11  
46  1 Y 1 C SER -9  ? C SER 12  
47  1 Y 1 C GLY -8  ? C GLY 13  
48  1 Y 1 C LEU -7  ? C LEU 14  
49  1 Y 1 C VAL -6  ? C VAL 15  
50  1 Y 1 C PRO -5  ? C PRO 16  
51  1 Y 1 C ARG -4  ? C ARG 17  
52  1 Y 1 C GLY -3  ? C GLY 18  
53  1 Y 1 C SER -2  ? C SER 19  
54  1 Y 1 C HIS -1  ? C HIS 20  
55  1 Y 1 C MET 0   ? C MET 21  
56  1 Y 1 C MET 1   ? C MET 22  
57  1 Y 1 C THR 2   ? C THR 23  
58  1 Y 1 C LYS 3   ? C LYS 24  
59  1 Y 1 C ILE 4   ? C ILE 25  
60  1 Y 1 C TYR 5   ? C TYR 26  
61  1 Y 1 C ASP 6   ? C ASP 27  
62  1 Y 1 C ALA 7   ? C ALA 28  
63  1 Y 1 C ALA 8   ? C ALA 29  
64  1 Y 1 C ASN 9   ? C ASN 30  
65  1 Y 1 C TRP 10  ? C TRP 31  
66  1 Y 1 C SER 11  ? C SER 32  
67  1 Y 1 C LYS 12  ? C LYS 33  
68  1 Y 1 C HIS 13  ? C HIS 34  
69  1 Y 1 C GLU 14  ? C GLU 35  
70  1 Y 1 C ASP 15  ? C ASP 36  
71  1 Y 1 C ASP 16  ? C ASP 37  
72  1 Y 1 C PHE 17  ? C PHE 38  
73  1 Y 1 C THR 18  ? C THR 39  
74  1 Y 1 C GLN 19  ? C GLN 40  
75  1 Y 1 C MET 20  ? C MET 41  
76  1 Y 1 C PHE 21  ? C PHE 42  
77  1 Y 1 C TYR 22  ? C TYR 43  
78  1 Y 1 C ASN 23  ? C ASN 44  
79  1 Y 1 C GLN 24  ? C GLN 45  
80  1 Y 1 C ASN 25  ? C ASN 46  
81  1 Y 1 C VAL 26  ? C VAL 47  
82  1 Y 1 C LYS 27  ? C LYS 48  
83  1 Y 1 C GLN 28  ? C GLN 49  
84  1 Y 1 C PHE 29  ? C PHE 50  
85  1 Y 1 C TRP 30  ? C TRP 51  
86  1 Y 1 C LEU 31  ? C LEU 52  
87  1 Y 1 C PRO 32  ? C PRO 53  
88  1 Y 1 C GLU 33  ? C GLU 54  
89  1 Y 1 C GLU 34  ? C GLU 55  
90  1 Y 1 C ILE 35  ? C ILE 56  
91  1 Y 1 C ALA 36  ? C ALA 57  
92  1 Y 1 C LEU 37  ? C LEU 58  
93  1 Y 1 C ASN 38  ? C ASN 59  
94  1 Y 1 C GLY 39  ? C GLY 60  
95  1 Y 1 C ASP 40  ? C ASP 61  
96  1 Y 1 C LEU 41  ? C LEU 62  
97  1 Y 1 C LEU 42  ? C LEU 63  
98  1 Y 1 C THR 43  ? C THR 64  
99  1 Y 1 C TRP 44  ? C TRP 65  
100 1 Y 1 C LYS 45  ? C LYS 66  
101 1 Y 1 C TYR 46  ? C TYR 67  
102 1 Y 1 C LEU 47  ? C LEU 68  
103 1 Y 1 C GLY 48  ? C GLY 69  
104 1 Y 1 C LYS 49  ? C LYS 70  
105 1 Y 1 C ASN 50  ? C ASN 71  
106 1 Y 1 C GLU 51  ? C GLU 72  
107 1 Y 1 C GLN 52  ? C GLN 73  
108 1 Y 1 C ASP 53  ? C ASP 74  
109 1 Y 1 C THR 54  ? C THR 75  
110 1 Y 1 C TYR 55  ? C TYR 76  
111 1 Y 1 C MET 56  ? C MET 77  
112 1 Y 1 C LYS 57  ? C LYS 78  
113 1 Y 1 C VAL 58  ? C VAL 79  
114 1 Y 1 C LEU 59  ? C LEU 80  
115 1 Y 1 C ALA 60  ? C ALA 81  
116 1 Y 1 C GLY 61  ? C GLY 82  
117 1 Y 1 C LEU 62  ? C LEU 83  
118 1 Y 1 C THR 63  ? C THR 84  
119 1 Y 1 C LEU 64  ? C LEU 85  
120 1 Y 1 C LEU 65  ? C LEU 86  
121 1 Y 1 C ASP 66  ? C ASP 87  
122 1 Y 1 C THR 67  ? C THR 88  
123 1 Y 1 C GLU 68  ? C GLU 89  
124 1 Y 1 C GLN 69  ? C GLN 90  
125 1 Y 1 C GLY 70  ? C GLY 91  
126 1 Y 1 C ASN 71  ? C ASN 92  
127 1 Y 1 C THR 72  ? C THR 93  
128 1 Y 1 C GLY 73  ? C GLY 94  
129 1 Y 1 C MET 74  ? C MET 95  
130 1 Y 1 C PRO 75  ? C PRO 96  
131 1 Y 1 C ILE 76  ? C ILE 97  
132 1 Y 1 C VAL 77  ? C VAL 98  
133 1 Y 1 C ALA 78  ? C ALA 99  
134 1 Y 1 C GLU 79  ? C GLU 100 
135 1 Y 1 C HIS 80  ? C HIS 101 
136 1 Y 1 C VAL 81  ? C VAL 102 
137 1 Y 1 C ASP 82  ? C ASP 103 
138 1 Y 1 C GLY 83  ? C GLY 104 
139 1 Y 1 C HIS 84  ? C HIS 105 
140 1 Y 1 C GLN 85  ? C GLN 106 
141 1 Y 1 C ARG 86  ? C ARG 107 
142 1 Y 1 C LYS 87  ? C LYS 108 
143 1 Y 1 C ALA 88  ? C ALA 109 
144 1 Y 1 C VAL 89  ? C VAL 110 
145 1 Y 1 C LEU 90  ? C LEU 111 
146 1 Y 1 C ASN 91  ? C ASN 112 
147 1 Y 1 C PHE 92  ? C PHE 113 
148 1 Y 1 C MET 93  ? C MET 114 
149 1 Y 1 C ALA 94  ? C ALA 115 
150 1 Y 1 C MET 95  ? C MET 116 
151 1 Y 1 C MET 96  ? C MET 117 
152 1 Y 1 C GLU 97  ? C GLU 118 
153 1 Y 1 C ASN 98  ? C ASN 119 
154 1 Y 1 C ALA 99  ? C ALA 120 
155 1 Y 1 C VAL 100 ? C VAL 121 
156 1 Y 1 C HIS 101 ? C HIS 122 
157 1 Y 1 C ALA 102 ? C ALA 123 
158 1 Y 1 C LYS 103 ? C LYS 124 
159 1 Y 1 C SER 104 ? C SER 125 
160 1 Y 1 C TYR 105 ? C TYR 126 
161 1 Y 1 C SER 106 ? C SER 127 
162 1 Y 1 C ASN 107 ? C ASN 128 
163 1 Y 1 C ILE 108 ? C ILE 129 
164 1 Y 1 C PHE 109 ? C PHE 130 
165 1 Y 1 C MET 110 ? C MET 131 
166 1 Y 1 C THR 111 ? C THR 132 
167 1 Y 1 C LEU 112 ? C LEU 133 
168 1 Y 1 C ALA 113 ? C ALA 134 
169 1 Y 1 C PRO 114 ? C PRO 135 
170 1 Y 1 C THR 115 ? C THR 136 
171 1 Y 1 C GLU 116 ? C GLU 137 
172 1 Y 1 C THR 117 ? C THR 138 
173 1 Y 1 C ILE 118 ? C ILE 139 
174 1 Y 1 C ASN 119 ? C ASN 140 
175 1 Y 1 C GLU 120 ? C GLU 141 
176 1 Y 1 C VAL 121 ? C VAL 142 
177 1 Y 1 C PHE 122 ? C PHE 143 
178 1 Y 1 C GLU 123 ? C GLU 144 
179 1 Y 1 C TRP 124 ? C TRP 145 
180 1 Y 1 C VAL 125 ? C VAL 146 
181 1 Y 1 C LYS 126 ? C LYS 147 
182 1 Y 1 C GLN 127 ? C GLN 148 
183 1 Y 1 C ASN 128 ? C ASN 149 
184 1 Y 1 C LYS 129 ? C LYS 150 
185 1 Y 1 C TYR 130 ? C TYR 151 
186 1 Y 1 C LEU 131 ? C LEU 152 
187 1 Y 1 C GLN 132 ? C GLN 153 
188 1 Y 1 C LYS 133 ? C LYS 154 
189 1 Y 1 C LYS 134 ? C LYS 155 
190 1 Y 1 C ALA 135 ? C ALA 156 
191 1 Y 1 C GLN 136 ? C GLN 157 
192 1 Y 1 C MET 137 ? C MET 158 
193 1 Y 1 C ILE 138 ? C ILE 159 
194 1 Y 1 C VAL 139 ? C VAL 160 
195 1 Y 1 C GLY 140 ? C GLY 161 
196 1 Y 1 C LEU 141 ? C LEU 162 
197 1 Y 1 C TYR 142 ? C TYR 163 
198 1 Y 1 C LYS 143 ? C LYS 164 
199 1 Y 1 C ALA 144 ? C ALA 165 
200 1 Y 1 C ILE 145 ? C ILE 166 
201 1 Y 1 C GLN 146 ? C GLN 167 
202 1 Y 1 C LYS 147 ? C LYS 168 
203 1 Y 1 C ASP 148 ? C ASP 169 
204 1 Y 1 C ASP 149 ? C ASP 170 
205 1 Y 1 C GLU 150 ? C GLU 171 
206 1 Y 1 C ILE 151 ? C ILE 172 
207 1 Y 1 C SER 152 ? C SER 173 
208 1 Y 1 C LEU 153 ? C LEU 174 
209 1 Y 1 C PHE 154 ? C PHE 175 
210 1 Y 1 C LYS 155 ? C LYS 176 
211 1 Y 1 C ALA 156 ? C ALA 177 
212 1 Y 1 C MET 157 ? C MET 178 
213 1 Y 1 C VAL 158 ? C VAL 179 
214 1 Y 1 C ALA 159 ? C ALA 180 
215 1 Y 1 C SER 160 ? C SER 181 
216 1 Y 1 C VAL 161 ? C VAL 182 
217 1 Y 1 C TYR 162 ? C TYR 183 
218 1 Y 1 C LEU 163 ? C LEU 184 
219 1 Y 1 C GLU 164 ? C GLU 185 
220 1 Y 1 C SER 165 ? C SER 186 
221 1 Y 1 C PHE 166 ? C PHE 187 
222 1 Y 1 C LEU 167 ? C LEU 188 
223 1 Y 1 C PHE 168 ? C PHE 189 
224 1 Y 1 C TYR 169 ? C TYR 190 
225 1 Y 1 C SER 170 ? C SER 191 
226 1 Y 1 C GLY 171 ? C GLY 192 
227 1 Y 1 C PHE 172 ? C PHE 193 
228 1 Y 1 C TYR 173 ? C TYR 194 
229 1 Y 1 C TYR 174 ? C TYR 195 
230 1 Y 1 C PRO 175 ? C PRO 196 
231 1 Y 1 C LEU 176 ? C LEU 197 
232 1 Y 1 C TYR 177 ? C TYR 198 
233 1 Y 1 C PHE 178 ? C PHE 199 
234 1 Y 1 C TYR 179 ? C TYR 200 
235 1 Y 1 C GLY 180 ? C GLY 201 
236 1 Y 1 C GLN 181 ? C GLN 202 
237 1 Y 1 C GLY 182 ? C GLY 203 
238 1 Y 1 C LYS 183 ? C LYS 204 
239 1 Y 1 C LEU 184 ? C LEU 205 
240 1 Y 1 C MET 185 ? C MET 206 
241 1 Y 1 C GLN 186 ? C GLN 207 
242 1 Y 1 C SER 187 ? C SER 208 
243 1 Y 1 C GLY 188 ? C GLY 209 
244 1 Y 1 C GLU 189 ? C GLU 210 
245 1 Y 1 C ILE 190 ? C ILE 211 
246 1 Y 1 C ILE 191 ? C ILE 212 
247 1 Y 1 C ASN 192 ? C ASN 213 
248 1 Y 1 C LEU 193 ? C LEU 214 
249 1 Y 1 C ILE 194 ? C ILE 215 
250 1 Y 1 C LEU 195 ? C LEU 216 
251 1 Y 1 C ARG 196 ? C ARG 217 
252 1 Y 1 C ASP 197 ? C ASP 218 
253 1 Y 1 C GLU 198 ? C GLU 219 
254 1 Y 1 C ALA 199 ? C ALA 220 
255 1 Y 1 C ILE 200 ? C ILE 221 
256 1 Y 1 C HIS 201 ? C HIS 222 
257 1 Y 1 C GLY 202 ? C GLY 223 
258 1 Y 1 C VAL 203 ? C VAL 224 
259 1 Y 1 C TYR 204 ? C TYR 225 
260 1 Y 1 C VAL 205 ? C VAL 226 
261 1 Y 1 C GLY 206 ? C GLY 227 
262 1 Y 1 C LEU 207 ? C LEU 228 
263 1 Y 1 C LEU 208 ? C LEU 229 
264 1 Y 1 C ALA 209 ? C ALA 230 
265 1 Y 1 C GLN 210 ? C GLN 231 
266 1 Y 1 C GLU 211 ? C GLU 232 
267 1 Y 1 C ILE 212 ? C ILE 233 
268 1 Y 1 C TYR 213 ? C TYR 234 
269 1 Y 1 C ASN 214 ? C ASN 235 
270 1 Y 1 C LYS 215 ? C LYS 236 
271 1 Y 1 C GLN 216 ? C GLN 237 
272 1 Y 1 C THR 217 ? C THR 238 
273 1 Y 1 C GLU 218 ? C GLU 239 
274 1 Y 1 C GLU 219 ? C GLU 240 
275 1 Y 1 C LYS 220 ? C LYS 241 
276 1 Y 1 C LYS 221 ? C LYS 242 
277 1 Y 1 C ALA 222 ? C ALA 243 
278 1 Y 1 C GLU 223 ? C GLU 244 
279 1 Y 1 C LEU 224 ? C LEU 245 
280 1 Y 1 C ARG 225 ? C ARG 246 
281 1 Y 1 C GLU 226 ? C GLU 247 
282 1 Y 1 C PHE 227 ? C PHE 248 
283 1 Y 1 C ALA 228 ? C ALA 249 
284 1 Y 1 C ILE 229 ? C ILE 250 
285 1 Y 1 C ASP 230 ? C ASP 251 
286 1 Y 1 C LEU 231 ? C LEU 252 
287 1 Y 1 C LEU 232 ? C LEU 253 
288 1 Y 1 C ASN 233 ? C ASN 254 
289 1 Y 1 C GLN 234 ? C GLN 255 
290 1 Y 1 C LEU 235 ? C LEU 256 
291 1 Y 1 C TYR 236 ? C TYR 257 
292 1 Y 1 C GLU 237 ? C GLU 258 
293 1 Y 1 C ASN 238 ? C ASN 259 
294 1 Y 1 C GLU 239 ? C GLU 260 
295 1 Y 1 C LEU 240 ? C LEU 261 
296 1 Y 1 C GLU 241 ? C GLU 262 
297 1 Y 1 C TYR 242 ? C TYR 263 
298 1 Y 1 C THR 243 ? C THR 264 
299 1 Y 1 C GLU 244 ? C GLU 265 
300 1 Y 1 C ASP 245 ? C ASP 266 
301 1 Y 1 C LEU 246 ? C LEU 267 
302 1 Y 1 C TYR 247 ? C TYR 268 
303 1 Y 1 C ASP 248 ? C ASP 269 
304 1 Y 1 C GLN 249 ? C GLN 270 
305 1 Y 1 C VAL 250 ? C VAL 271 
306 1 Y 1 C GLY 251 ? C GLY 272 
307 1 Y 1 C LEU 252 ? C LEU 273 
308 1 Y 1 C SER 253 ? C SER 274 
309 1 Y 1 C HIS 254 ? C HIS 275 
310 1 Y 1 C ASP 255 ? C ASP 276 
311 1 Y 1 C VAL 256 ? C VAL 277 
312 1 Y 1 C LYS 257 ? C LYS 278 
313 1 Y 1 C LYS 258 ? C LYS 279 
314 1 Y 1 C PHE 259 ? C PHE 280 
315 1 Y 1 C ILE 260 ? C ILE 281 
316 1 Y 1 C ARG 261 ? C ARG 282 
317 1 Y 1 C TYR 262 ? C TYR 283 
318 1 Y 1 C ASN 263 ? C ASN 284 
319 1 Y 1 C ALA 264 ? C ALA 285 
320 1 Y 1 C ASN 265 ? C ASN 286 
321 1 Y 1 C LYS 266 ? C LYS 287 
322 1 Y 1 C ALA 267 ? C ALA 288 
323 1 Y 1 C LEU 268 ? C LEU 289 
324 1 Y 1 C MET 269 ? C MET 290 
325 1 Y 1 C ASN 270 ? C ASN 291 
326 1 Y 1 C LEU 271 ? C LEU 292 
327 1 Y 1 C GLY 272 ? C GLY 293 
328 1 Y 1 C PHE 273 ? C PHE 294 
329 1 Y 1 C ASP 274 ? C ASP 295 
330 1 Y 1 C PRO 275 ? C PRO 296 
331 1 Y 1 C TYR 276 ? C TYR 297 
332 1 Y 1 C PHE 277 ? C PHE 298 
333 1 Y 1 C GLU 278 ? C GLU 299 
334 1 Y 1 C GLU 279 ? C GLU 300 
335 1 Y 1 C GLU 280 ? C GLU 301 
336 1 Y 1 C ASP 281 ? C ASP 302 
337 1 Y 1 C ILE 282 ? C ILE 303 
338 1 Y 1 C ASN 283 ? C ASN 304 
339 1 Y 1 C PRO 284 ? C PRO 305 
340 1 Y 1 C ILE 285 ? C ILE 306 
341 1 Y 1 C VAL 286 ? C VAL 307 
342 1 Y 1 C LEU 287 ? C LEU 308 
343 1 Y 1 C ASN 288 ? C ASN 309 
344 1 Y 1 C GLY 289 ? C GLY 310 
345 1 Y 1 C LEU 290 ? C LEU 311 
346 1 Y 1 C ASN 291 ? C ASN 312 
347 1 Y 1 C THR 292 ? C THR 313 
348 1 Y 1 C LYS 293 ? C LYS 314 
349 1 Y 1 C THR 294 ? C THR 315 
350 1 Y 1 C LYS 295 ? C LYS 316 
351 1 Y 1 C SER 296 ? C SER 317 
352 1 Y 1 C HIS 297 ? C HIS 318 
353 1 Y 1 C ASP 298 ? C ASP 319 
354 1 Y 1 C PHE 299 ? C PHE 320 
355 1 Y 1 C PHE 300 ? C PHE 321 
356 1 Y 1 C SER 301 ? C SER 322 
357 1 Y 1 C MET 302 ? C MET 323 
358 1 Y 1 C LYS 303 ? C LYS 324 
359 1 Y 1 C GLY 304 ? C GLY 325 
360 1 Y 1 C ASN 305 ? C ASN 326 
361 1 Y 1 C GLY 306 ? C GLY 327 
362 1 Y 1 C TYR 307 ? C TYR 328 
363 1 Y 1 C LYS 308 ? C LYS 329 
364 1 Y 1 C LYS 309 ? C LYS 330 
365 1 Y 1 C ALA 310 ? C ALA 331 
366 1 Y 1 C GLU 323 ? C GLU 344 
367 1 Y 1 C ASP 324 ? C ASP 345 
368 1 Y 1 C GLU 325 ? C GLU 346 
369 1 Y 1 C LYS 326 ? C LYS 347 
370 1 Y 1 C GLU 327 ? C GLU 348 
371 1 Y 1 C GLN 328 ? C GLN 349 
372 1 Y 1 C ILE 329 ? C ILE 350 
373 1 Y 1 D MET -20 ? D MET 1   
374 1 Y 1 D GLY -19 ? D GLY 2   
375 1 Y 1 D SER -18 ? D SER 3   
376 1 Y 1 D SER -17 ? D SER 4   
377 1 Y 1 D HIS -16 ? D HIS 5   
378 1 Y 1 D HIS -15 ? D HIS 6   
379 1 Y 1 D HIS -14 ? D HIS 7   
380 1 Y 1 D HIS -13 ? D HIS 8   
381 1 Y 1 D HIS -12 ? D HIS 9   
382 1 Y 1 D HIS -11 ? D HIS 10  
383 1 Y 1 D SER -10 ? D SER 11  
384 1 Y 1 D SER -9  ? D SER 12  
385 1 Y 1 D GLY -8  ? D GLY 13  
386 1 Y 1 D LEU -7  ? D LEU 14  
387 1 Y 1 D VAL -6  ? D VAL 15  
388 1 Y 1 D PRO -5  ? D PRO 16  
389 1 Y 1 D ARG -4  ? D ARG 17  
390 1 Y 1 D GLY -3  ? D GLY 18  
391 1 Y 1 D SER -2  ? D SER 19  
392 1 Y 1 D HIS -1  ? D HIS 20  
393 1 Y 1 D MET 0   ? D MET 21  
394 1 Y 1 D MET 1   ? D MET 22  
395 1 Y 1 D THR 2   ? D THR 23  
396 1 Y 1 D LYS 3   ? D LYS 24  
397 1 Y 1 D ILE 4   ? D ILE 25  
398 1 Y 1 D TYR 5   ? D TYR 26  
399 1 Y 1 D ASP 6   ? D ASP 27  
400 1 Y 1 D ALA 7   ? D ALA 28  
401 1 Y 1 D ALA 8   ? D ALA 29  
402 1 Y 1 D ASN 9   ? D ASN 30  
403 1 Y 1 D TRP 10  ? D TRP 31  
404 1 Y 1 D SER 11  ? D SER 32  
405 1 Y 1 D LYS 12  ? D LYS 33  
406 1 Y 1 D HIS 13  ? D HIS 34  
407 1 Y 1 D GLU 14  ? D GLU 35  
408 1 Y 1 D ASP 15  ? D ASP 36  
409 1 Y 1 D ASP 16  ? D ASP 37  
410 1 Y 1 D PHE 17  ? D PHE 38  
411 1 Y 1 D THR 18  ? D THR 39  
412 1 Y 1 D GLN 19  ? D GLN 40  
413 1 Y 1 D MET 20  ? D MET 41  
414 1 Y 1 D PHE 21  ? D PHE 42  
415 1 Y 1 D TYR 22  ? D TYR 43  
416 1 Y 1 D ASN 23  ? D ASN 44  
417 1 Y 1 D GLN 24  ? D GLN 45  
418 1 Y 1 D ASN 25  ? D ASN 46  
419 1 Y 1 D VAL 26  ? D VAL 47  
420 1 Y 1 D LYS 27  ? D LYS 48  
421 1 Y 1 D GLN 28  ? D GLN 49  
422 1 Y 1 D PHE 29  ? D PHE 50  
423 1 Y 1 D TRP 30  ? D TRP 51  
424 1 Y 1 D LEU 31  ? D LEU 52  
425 1 Y 1 D PRO 32  ? D PRO 53  
426 1 Y 1 D GLU 33  ? D GLU 54  
427 1 Y 1 D GLU 34  ? D GLU 55  
428 1 Y 1 D ILE 35  ? D ILE 56  
429 1 Y 1 D ALA 36  ? D ALA 57  
430 1 Y 1 D LEU 37  ? D LEU 58  
431 1 Y 1 D ASN 38  ? D ASN 59  
432 1 Y 1 D GLY 39  ? D GLY 60  
433 1 Y 1 D ASP 40  ? D ASP 61  
434 1 Y 1 D LEU 41  ? D LEU 62  
435 1 Y 1 D LEU 42  ? D LEU 63  
436 1 Y 1 D THR 43  ? D THR 64  
437 1 Y 1 D TRP 44  ? D TRP 65  
438 1 Y 1 D LYS 45  ? D LYS 66  
439 1 Y 1 D TYR 46  ? D TYR 67  
440 1 Y 1 D LEU 47  ? D LEU 68  
441 1 Y 1 D GLY 48  ? D GLY 69  
442 1 Y 1 D LYS 49  ? D LYS 70  
443 1 Y 1 D ASN 50  ? D ASN 71  
444 1 Y 1 D GLU 51  ? D GLU 72  
445 1 Y 1 D GLN 52  ? D GLN 73  
446 1 Y 1 D ASP 53  ? D ASP 74  
447 1 Y 1 D THR 54  ? D THR 75  
448 1 Y 1 D TYR 55  ? D TYR 76  
449 1 Y 1 D MET 56  ? D MET 77  
450 1 Y 1 D LYS 57  ? D LYS 78  
451 1 Y 1 D VAL 58  ? D VAL 79  
452 1 Y 1 D LEU 59  ? D LEU 80  
453 1 Y 1 D ALA 60  ? D ALA 81  
454 1 Y 1 D GLY 61  ? D GLY 82  
455 1 Y 1 D LEU 62  ? D LEU 83  
456 1 Y 1 D THR 63  ? D THR 84  
457 1 Y 1 D LEU 64  ? D LEU 85  
458 1 Y 1 D LEU 65  ? D LEU 86  
459 1 Y 1 D ASP 66  ? D ASP 87  
460 1 Y 1 D THR 67  ? D THR 88  
461 1 Y 1 D GLU 68  ? D GLU 89  
462 1 Y 1 D GLN 69  ? D GLN 90  
463 1 Y 1 D GLY 70  ? D GLY 91  
464 1 Y 1 D ASN 71  ? D ASN 92  
465 1 Y 1 D THR 72  ? D THR 93  
466 1 Y 1 D GLY 73  ? D GLY 94  
467 1 Y 1 D MET 74  ? D MET 95  
468 1 Y 1 D PRO 75  ? D PRO 96  
469 1 Y 1 D ILE 76  ? D ILE 97  
470 1 Y 1 D VAL 77  ? D VAL 98  
471 1 Y 1 D ALA 78  ? D ALA 99  
472 1 Y 1 D GLU 79  ? D GLU 100 
473 1 Y 1 D HIS 80  ? D HIS 101 
474 1 Y 1 D VAL 81  ? D VAL 102 
475 1 Y 1 D ASP 82  ? D ASP 103 
476 1 Y 1 D GLY 83  ? D GLY 104 
477 1 Y 1 D HIS 84  ? D HIS 105 
478 1 Y 1 D GLN 85  ? D GLN 106 
479 1 Y 1 D ARG 86  ? D ARG 107 
480 1 Y 1 D LYS 87  ? D LYS 108 
481 1 Y 1 D ALA 88  ? D ALA 109 
482 1 Y 1 D VAL 89  ? D VAL 110 
483 1 Y 1 D LEU 90  ? D LEU 111 
484 1 Y 1 D ASN 91  ? D ASN 112 
485 1 Y 1 D PHE 92  ? D PHE 113 
486 1 Y 1 D MET 93  ? D MET 114 
487 1 Y 1 D ALA 94  ? D ALA 115 
488 1 Y 1 D MET 95  ? D MET 116 
489 1 Y 1 D MET 96  ? D MET 117 
490 1 Y 1 D GLU 97  ? D GLU 118 
491 1 Y 1 D ASN 98  ? D ASN 119 
492 1 Y 1 D ALA 99  ? D ALA 120 
493 1 Y 1 D VAL 100 ? D VAL 121 
494 1 Y 1 D HIS 101 ? D HIS 122 
495 1 Y 1 D ALA 102 ? D ALA 123 
496 1 Y 1 D LYS 103 ? D LYS 124 
497 1 Y 1 D SER 104 ? D SER 125 
498 1 Y 1 D TYR 105 ? D TYR 126 
499 1 Y 1 D SER 106 ? D SER 127 
500 1 Y 1 D ASN 107 ? D ASN 128 
501 1 Y 1 D ILE 108 ? D ILE 129 
502 1 Y 1 D PHE 109 ? D PHE 130 
503 1 Y 1 D MET 110 ? D MET 131 
504 1 Y 1 D THR 111 ? D THR 132 
505 1 Y 1 D LEU 112 ? D LEU 133 
506 1 Y 1 D ALA 113 ? D ALA 134 
507 1 Y 1 D PRO 114 ? D PRO 135 
508 1 Y 1 D THR 115 ? D THR 136 
509 1 Y 1 D GLU 116 ? D GLU 137 
510 1 Y 1 D THR 117 ? D THR 138 
511 1 Y 1 D ILE 118 ? D ILE 139 
512 1 Y 1 D ASN 119 ? D ASN 140 
513 1 Y 1 D GLU 120 ? D GLU 141 
514 1 Y 1 D VAL 121 ? D VAL 142 
515 1 Y 1 D PHE 122 ? D PHE 143 
516 1 Y 1 D GLU 123 ? D GLU 144 
517 1 Y 1 D TRP 124 ? D TRP 145 
518 1 Y 1 D VAL 125 ? D VAL 146 
519 1 Y 1 D LYS 126 ? D LYS 147 
520 1 Y 1 D GLN 127 ? D GLN 148 
521 1 Y 1 D ASN 128 ? D ASN 149 
522 1 Y 1 D LYS 129 ? D LYS 150 
523 1 Y 1 D TYR 130 ? D TYR 151 
524 1 Y 1 D LEU 131 ? D LEU 152 
525 1 Y 1 D GLN 132 ? D GLN 153 
526 1 Y 1 D LYS 133 ? D LYS 154 
527 1 Y 1 D LYS 134 ? D LYS 155 
528 1 Y 1 D ALA 135 ? D ALA 156 
529 1 Y 1 D GLN 136 ? D GLN 157 
530 1 Y 1 D MET 137 ? D MET 158 
531 1 Y 1 D ILE 138 ? D ILE 159 
532 1 Y 1 D VAL 139 ? D VAL 160 
533 1 Y 1 D GLY 140 ? D GLY 161 
534 1 Y 1 D LEU 141 ? D LEU 162 
535 1 Y 1 D TYR 142 ? D TYR 163 
536 1 Y 1 D LYS 143 ? D LYS 164 
537 1 Y 1 D ALA 144 ? D ALA 165 
538 1 Y 1 D ILE 145 ? D ILE 166 
539 1 Y 1 D GLN 146 ? D GLN 167 
540 1 Y 1 D LYS 147 ? D LYS 168 
541 1 Y 1 D ASP 148 ? D ASP 169 
542 1 Y 1 D ASP 149 ? D ASP 170 
543 1 Y 1 D GLU 150 ? D GLU 171 
544 1 Y 1 D ILE 151 ? D ILE 172 
545 1 Y 1 D SER 152 ? D SER 173 
546 1 Y 1 D LEU 153 ? D LEU 174 
547 1 Y 1 D PHE 154 ? D PHE 175 
548 1 Y 1 D LYS 155 ? D LYS 176 
549 1 Y 1 D ALA 156 ? D ALA 177 
550 1 Y 1 D MET 157 ? D MET 178 
551 1 Y 1 D VAL 158 ? D VAL 179 
552 1 Y 1 D ALA 159 ? D ALA 180 
553 1 Y 1 D SER 160 ? D SER 181 
554 1 Y 1 D VAL 161 ? D VAL 182 
555 1 Y 1 D TYR 162 ? D TYR 183 
556 1 Y 1 D LEU 163 ? D LEU 184 
557 1 Y 1 D GLU 164 ? D GLU 185 
558 1 Y 1 D SER 165 ? D SER 186 
559 1 Y 1 D PHE 166 ? D PHE 187 
560 1 Y 1 D LEU 167 ? D LEU 188 
561 1 Y 1 D PHE 168 ? D PHE 189 
562 1 Y 1 D TYR 169 ? D TYR 190 
563 1 Y 1 D SER 170 ? D SER 191 
564 1 Y 1 D GLY 171 ? D GLY 192 
565 1 Y 1 D PHE 172 ? D PHE 193 
566 1 Y 1 D TYR 173 ? D TYR 194 
567 1 Y 1 D TYR 174 ? D TYR 195 
568 1 Y 1 D PRO 175 ? D PRO 196 
569 1 Y 1 D LEU 176 ? D LEU 197 
570 1 Y 1 D TYR 177 ? D TYR 198 
571 1 Y 1 D PHE 178 ? D PHE 199 
572 1 Y 1 D TYR 179 ? D TYR 200 
573 1 Y 1 D GLY 180 ? D GLY 201 
574 1 Y 1 D GLN 181 ? D GLN 202 
575 1 Y 1 D GLY 182 ? D GLY 203 
576 1 Y 1 D LYS 183 ? D LYS 204 
577 1 Y 1 D LEU 184 ? D LEU 205 
578 1 Y 1 D MET 185 ? D MET 206 
579 1 Y 1 D GLN 186 ? D GLN 207 
580 1 Y 1 D SER 187 ? D SER 208 
581 1 Y 1 D GLY 188 ? D GLY 209 
582 1 Y 1 D GLU 189 ? D GLU 210 
583 1 Y 1 D ILE 190 ? D ILE 211 
584 1 Y 1 D ILE 191 ? D ILE 212 
585 1 Y 1 D ASN 192 ? D ASN 213 
586 1 Y 1 D LEU 193 ? D LEU 214 
587 1 Y 1 D ILE 194 ? D ILE 215 
588 1 Y 1 D LEU 195 ? D LEU 216 
589 1 Y 1 D ARG 196 ? D ARG 217 
590 1 Y 1 D ASP 197 ? D ASP 218 
591 1 Y 1 D GLU 198 ? D GLU 219 
592 1 Y 1 D ALA 199 ? D ALA 220 
593 1 Y 1 D ILE 200 ? D ILE 221 
594 1 Y 1 D HIS 201 ? D HIS 222 
595 1 Y 1 D GLY 202 ? D GLY 223 
596 1 Y 1 D VAL 203 ? D VAL 224 
597 1 Y 1 D TYR 204 ? D TYR 225 
598 1 Y 1 D VAL 205 ? D VAL 226 
599 1 Y 1 D GLY 206 ? D GLY 227 
600 1 Y 1 D LEU 207 ? D LEU 228 
601 1 Y 1 D LEU 208 ? D LEU 229 
602 1 Y 1 D ALA 209 ? D ALA 230 
603 1 Y 1 D GLN 210 ? D GLN 231 
604 1 Y 1 D GLU 211 ? D GLU 232 
605 1 Y 1 D ILE 212 ? D ILE 233 
606 1 Y 1 D TYR 213 ? D TYR 234 
607 1 Y 1 D ASN 214 ? D ASN 235 
608 1 Y 1 D LYS 215 ? D LYS 236 
609 1 Y 1 D GLN 216 ? D GLN 237 
610 1 Y 1 D THR 217 ? D THR 238 
611 1 Y 1 D GLU 218 ? D GLU 239 
612 1 Y 1 D GLU 219 ? D GLU 240 
613 1 Y 1 D LYS 220 ? D LYS 241 
614 1 Y 1 D LYS 221 ? D LYS 242 
615 1 Y 1 D ALA 222 ? D ALA 243 
616 1 Y 1 D GLU 223 ? D GLU 244 
617 1 Y 1 D LEU 224 ? D LEU 245 
618 1 Y 1 D ARG 225 ? D ARG 246 
619 1 Y 1 D GLU 226 ? D GLU 247 
620 1 Y 1 D PHE 227 ? D PHE 248 
621 1 Y 1 D ALA 228 ? D ALA 249 
622 1 Y 1 D ILE 229 ? D ILE 250 
623 1 Y 1 D ASP 230 ? D ASP 251 
624 1 Y 1 D LEU 231 ? D LEU 252 
625 1 Y 1 D LEU 232 ? D LEU 253 
626 1 Y 1 D ASN 233 ? D ASN 254 
627 1 Y 1 D GLN 234 ? D GLN 255 
628 1 Y 1 D LEU 235 ? D LEU 256 
629 1 Y 1 D TYR 236 ? D TYR 257 
630 1 Y 1 D GLU 237 ? D GLU 258 
631 1 Y 1 D ASN 238 ? D ASN 259 
632 1 Y 1 D GLU 239 ? D GLU 260 
633 1 Y 1 D LEU 240 ? D LEU 261 
634 1 Y 1 D GLU 241 ? D GLU 262 
635 1 Y 1 D TYR 242 ? D TYR 263 
636 1 Y 1 D THR 243 ? D THR 264 
637 1 Y 1 D GLU 244 ? D GLU 265 
638 1 Y 1 D ASP 245 ? D ASP 266 
639 1 Y 1 D LEU 246 ? D LEU 267 
640 1 Y 1 D TYR 247 ? D TYR 268 
641 1 Y 1 D ASP 248 ? D ASP 269 
642 1 Y 1 D GLN 249 ? D GLN 270 
643 1 Y 1 D VAL 250 ? D VAL 271 
644 1 Y 1 D GLY 251 ? D GLY 272 
645 1 Y 1 D LEU 252 ? D LEU 273 
646 1 Y 1 D SER 253 ? D SER 274 
647 1 Y 1 D HIS 254 ? D HIS 275 
648 1 Y 1 D ASP 255 ? D ASP 276 
649 1 Y 1 D VAL 256 ? D VAL 277 
650 1 Y 1 D LYS 257 ? D LYS 278 
651 1 Y 1 D LYS 258 ? D LYS 279 
652 1 Y 1 D PHE 259 ? D PHE 280 
653 1 Y 1 D ILE 260 ? D ILE 281 
654 1 Y 1 D ARG 261 ? D ARG 282 
655 1 Y 1 D TYR 262 ? D TYR 283 
656 1 Y 1 D ASN 263 ? D ASN 284 
657 1 Y 1 D ALA 264 ? D ALA 285 
658 1 Y 1 D ASN 265 ? D ASN 286 
659 1 Y 1 D LYS 266 ? D LYS 287 
660 1 Y 1 D ALA 267 ? D ALA 288 
661 1 Y 1 D LEU 268 ? D LEU 289 
662 1 Y 1 D MET 269 ? D MET 290 
663 1 Y 1 D ASN 270 ? D ASN 291 
664 1 Y 1 D LEU 271 ? D LEU 292 
665 1 Y 1 D GLY 272 ? D GLY 293 
666 1 Y 1 D PHE 273 ? D PHE 294 
667 1 Y 1 D ASP 274 ? D ASP 295 
668 1 Y 1 D PRO 275 ? D PRO 296 
669 1 Y 1 D TYR 276 ? D TYR 297 
670 1 Y 1 D PHE 277 ? D PHE 298 
671 1 Y 1 D GLU 278 ? D GLU 299 
672 1 Y 1 D GLU 279 ? D GLU 300 
673 1 Y 1 D GLU 280 ? D GLU 301 
674 1 Y 1 D ASP 281 ? D ASP 302 
675 1 Y 1 D ILE 282 ? D ILE 303 
676 1 Y 1 D ASN 283 ? D ASN 304 
677 1 Y 1 D PRO 284 ? D PRO 305 
678 1 Y 1 D ILE 285 ? D ILE 306 
679 1 Y 1 D VAL 286 ? D VAL 307 
680 1 Y 1 D LEU 287 ? D LEU 308 
681 1 Y 1 D ASN 288 ? D ASN 309 
682 1 Y 1 D GLY 289 ? D GLY 310 
683 1 Y 1 D LEU 290 ? D LEU 311 
684 1 Y 1 D ASN 291 ? D ASN 312 
685 1 Y 1 D THR 292 ? D THR 313 
686 1 Y 1 D LYS 293 ? D LYS 314 
687 1 Y 1 D THR 294 ? D THR 315 
688 1 Y 1 D LYS 295 ? D LYS 316 
689 1 Y 1 D SER 296 ? D SER 317 
690 1 Y 1 D HIS 297 ? D HIS 318 
691 1 Y 1 D ASP 298 ? D ASP 319 
692 1 Y 1 D PHE 299 ? D PHE 320 
693 1 Y 1 D PHE 300 ? D PHE 321 
694 1 Y 1 D SER 301 ? D SER 322 
695 1 Y 1 D MET 302 ? D MET 323 
696 1 Y 1 D LYS 303 ? D LYS 324 
697 1 Y 1 D GLY 304 ? D GLY 325 
698 1 Y 1 D ASN 305 ? D ASN 326 
699 1 Y 1 D GLY 306 ? D GLY 327 
700 1 Y 1 D TYR 307 ? D TYR 328 
701 1 Y 1 D LYS 308 ? D LYS 329 
702 1 Y 1 D LYS 309 ? D LYS 330 
703 1 Y 1 D ALA 310 ? D ALA 331 
704 1 Y 1 D GLU 323 ? D GLU 344 
705 1 Y 1 D ASP 324 ? D ASP 345 
706 1 Y 1 D GLU 325 ? D GLU 346 
707 1 Y 1 D LYS 326 ? D LYS 347 
708 1 Y 1 D GLU 327 ? D GLU 348 
709 1 Y 1 D GLN 328 ? D GLN 349 
710 1 Y 1 D ILE 329 ? D ILE 350 
# 
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  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GLN N      N  N N 135 
GLN CA     C  N S 136 
GLN C      C  N N 137 
GLN O      O  N N 138 
GLN CB     C  N N 139 
GLN CG     C  N N 140 
GLN CD     C  N N 141 
GLN OE1    O  N N 142 
GLN NE2    N  N N 143 
GLN OXT    O  N N 144 
GLN H      H  N N 145 
GLN H2     H  N N 146 
GLN HA     H  N N 147 
GLN HB2    H  N N 148 
GLN HB3    H  N N 149 
GLN HG2    H  N N 150 
GLN HG3    H  N N 151 
GLN HE21   H  N N 152 
GLN HE22   H  N N 153 
GLN HXT    H  N N 154 
GLU N      N  N N 155 
GLU CA     C  N S 156 
GLU C      C  N N 157 
GLU O      O  N N 158 
GLU CB     C  N N 159 
GLU CG     C  N N 160 
GLU CD     C  N N 161 
GLU OE1    O  N N 162 
GLU OE2    O  N N 163 
GLU OXT    O  N N 164 
GLU H      H  N N 165 
GLU H2     H  N N 166 
GLU HA     H  N N 167 
GLU HB2    H  N N 168 
GLU HB3    H  N N 169 
GLU HG2    H  N N 170 
GLU HG3    H  N N 171 
GLU HE2    H  N N 172 
GLU HXT    H  N N 173 
GLY N      N  N N 174 
GLY CA     C  N N 175 
GLY C      C  N N 176 
GLY O      O  N N 177 
GLY OXT    O  N N 178 
GLY H      H  N N 179 
GLY H2     H  N N 180 
GLY HA2    H  N N 181 
GLY HA3    H  N N 182 
GLY HXT    H  N N 183 
HIS N      N  N N 184 
HIS CA     C  N S 185 
HIS C      C  N N 186 
HIS O      O  N N 187 
HIS CB     C  N N 188 
HIS CG     C  Y N 189 
HIS ND1    N  Y N 190 
HIS CD2    C  Y N 191 
HIS CE1    C  Y N 192 
HIS NE2    N  Y N 193 
HIS OXT    O  N N 194 
HIS H      H  N N 195 
HIS H2     H  N N 196 
HIS HA     H  N N 197 
HIS HB2    H  N N 198 
HIS HB3    H  N N 199 
HIS HD1    H  N N 200 
HIS HD2    H  N N 201 
HIS HE1    H  N N 202 
HIS HE2    H  N N 203 
HIS HXT    H  N N 204 
ILE N      N  N N 205 
ILE CA     C  N S 206 
ILE C      C  N N 207 
ILE O      O  N N 208 
ILE CB     C  N S 209 
ILE CG1    C  N N 210 
ILE CG2    C  N N 211 
ILE CD1    C  N N 212 
ILE OXT    O  N N 213 
ILE H      H  N N 214 
ILE H2     H  N N 215 
ILE HA     H  N N 216 
ILE HB     H  N N 217 
ILE HG12   H  N N 218 
ILE HG13   H  N N 219 
ILE HG21   H  N N 220 
ILE HG22   H  N N 221 
ILE HG23   H  N N 222 
ILE HD11   H  N N 223 
ILE HD12   H  N N 224 
ILE HD13   H  N N 225 
ILE HXT    H  N N 226 
LEU N      N  N N 227 
LEU CA     C  N S 228 
LEU C      C  N N 229 
LEU O      O  N N 230 
LEU CB     C  N N 231 
LEU CG     C  N N 232 
LEU CD1    C  N N 233 
LEU CD2    C  N N 234 
LEU OXT    O  N N 235 
LEU H      H  N N 236 
LEU H2     H  N N 237 
LEU HA     H  N N 238 
LEU HB2    H  N N 239 
LEU HB3    H  N N 240 
LEU HG     H  N N 241 
LEU HD11   H  N N 242 
LEU HD12   H  N N 243 
LEU HD13   H  N N 244 
LEU HD21   H  N N 245 
LEU HD22   H  N N 246 
LEU HD23   H  N N 247 
LEU HXT    H  N N 248 
LYS N      N  N N 249 
LYS CA     C  N S 250 
LYS C      C  N N 251 
LYS O      O  N N 252 
LYS CB     C  N N 253 
LYS CG     C  N N 254 
LYS CD     C  N N 255 
LYS CE     C  N N 256 
LYS NZ     N  N N 257 
LYS OXT    O  N N 258 
LYS H      H  N N 259 
LYS H2     H  N N 260 
LYS HA     H  N N 261 
LYS HB2    H  N N 262 
LYS HB3    H  N N 263 
LYS HG2    H  N N 264 
LYS HG3    H  N N 265 
LYS HD2    H  N N 266 
LYS HD3    H  N N 267 
LYS HE2    H  N N 268 
LYS HE3    H  N N 269 
LYS HZ1    H  N N 270 
LYS HZ2    H  N N 271 
LYS HZ3    H  N N 272 
LYS HXT    H  N N 273 
MET N      N  N N 274 
MET CA     C  N S 275 
MET C      C  N N 276 
MET O      O  N N 277 
MET CB     C  N N 278 
MET CG     C  N N 279 
MET SD     S  N N 280 
MET CE     C  N N 281 
MET OXT    O  N N 282 
MET H      H  N N 283 
MET H2     H  N N 284 
MET HA     H  N N 285 
MET HB2    H  N N 286 
MET HB3    H  N N 287 
MET HG2    H  N N 288 
MET HG3    H  N N 289 
MET HE1    H  N N 290 
MET HE2    H  N N 291 
MET HE3    H  N N 292 
MET HXT    H  N N 293 
MG  MG     MG N N 294 
PHE N      N  N N 295 
PHE CA     C  N S 296 
PHE C      C  N N 297 
PHE O      O  N N 298 
PHE CB     C  N N 299 
PHE CG     C  Y N 300 
PHE CD1    C  Y N 301 
PHE CD2    C  Y N 302 
PHE CE1    C  Y N 303 
PHE CE2    C  Y N 304 
PHE CZ     C  Y N 305 
PHE OXT    O  N N 306 
PHE H      H  N N 307 
PHE H2     H  N N 308 
PHE HA     H  N N 309 
PHE HB2    H  N N 310 
PHE HB3    H  N N 311 
PHE HD1    H  N N 312 
PHE HD2    H  N N 313 
PHE HE1    H  N N 314 
PHE HE2    H  N N 315 
PHE HZ     H  N N 316 
PHE HXT    H  N N 317 
PRO N      N  N N 318 
PRO CA     C  N S 319 
PRO C      C  N N 320 
PRO O      O  N N 321 
PRO CB     C  N N 322 
PRO CG     C  N N 323 
PRO CD     C  N N 324 
PRO OXT    O  N N 325 
PRO H      H  N N 326 
PRO HA     H  N N 327 
PRO HB2    H  N N 328 
PRO HB3    H  N N 329 
PRO HG2    H  N N 330 
PRO HG3    H  N N 331 
PRO HD2    H  N N 332 
PRO HD3    H  N N 333 
PRO HXT    H  N N 334 
SER N      N  N N 335 
SER CA     C  N S 336 
SER C      C  N N 337 
SER O      O  N N 338 
SER CB     C  N N 339 
SER OG     O  N N 340 
SER OXT    O  N N 341 
SER H      H  N N 342 
SER H2     H  N N 343 
SER HA     H  N N 344 
SER HB2    H  N N 345 
SER HB3    H  N N 346 
SER HG     H  N N 347 
SER HXT    H  N N 348 
THR N      N  N N 349 
THR CA     C  N S 350 
THR C      C  N N 351 
THR O      O  N N 352 
THR CB     C  N R 353 
THR OG1    O  N N 354 
THR CG2    C  N N 355 
THR OXT    O  N N 356 
THR H      H  N N 357 
THR H2     H  N N 358 
THR HA     H  N N 359 
THR HB     H  N N 360 
THR HG1    H  N N 361 
THR HG21   H  N N 362 
THR HG22   H  N N 363 
THR HG23   H  N N 364 
THR HXT    H  N N 365 
TRP N      N  N N 366 
TRP CA     C  N S 367 
TRP C      C  N N 368 
TRP O      O  N N 369 
TRP CB     C  N N 370 
TRP CG     C  Y N 371 
TRP CD1    C  Y N 372 
TRP CD2    C  Y N 373 
TRP NE1    N  Y N 374 
TRP CE2    C  Y N 375 
TRP CE3    C  Y N 376 
TRP CZ2    C  Y N 377 
TRP CZ3    C  Y N 378 
TRP CH2    C  Y N 379 
TRP OXT    O  N N 380 
TRP H      H  N N 381 
TRP H2     H  N N 382 
TRP HA     H  N N 383 
TRP HB2    H  N N 384 
TRP HB3    H  N N 385 
TRP HD1    H  N N 386 
TRP HE1    H  N N 387 
TRP HE3    H  N N 388 
TRP HZ2    H  N N 389 
TRP HZ3    H  N N 390 
TRP HH2    H  N N 391 
TRP HXT    H  N N 392 
TTP PA     P  N S 393 
TTP O1A    O  N N 394 
TTP O2A    O  N N 395 
TTP O3A    O  N N 396 
TTP PB     P  N S 397 
TTP O1B    O  N N 398 
TTP O2B    O  N N 399 
TTP O3B    O  N N 400 
TTP PG     P  N N 401 
TTP O1G    O  N N 402 
TTP O2G    O  N N 403 
TTP O3G    O  N N 404 
TTP "O5'"  O  N N 405 
TTP "C5'"  C  N N 406 
TTP "C4'"  C  N R 407 
TTP "O4'"  O  N N 408 
TTP "C3'"  C  N S 409 
TTP "O3'"  O  N N 410 
TTP "C2'"  C  N N 411 
TTP "C1'"  C  N R 412 
TTP N1     N  N N 413 
TTP C2     C  N N 414 
TTP O2     O  N N 415 
TTP N3     N  N N 416 
TTP C4     C  N N 417 
TTP O4     O  N N 418 
TTP C5     C  N N 419 
TTP C5M    C  N N 420 
TTP C6     C  N N 421 
TTP HOA2   H  N N 422 
TTP HOB2   H  N N 423 
TTP HOG2   H  N N 424 
TTP HOG3   H  N N 425 
TTP "H5'1" H  N N 426 
TTP "H5'2" H  N N 427 
TTP "H4'"  H  N N 428 
TTP "H3'"  H  N N 429 
TTP "HO3'" H  N N 430 
TTP "H2'1" H  N N 431 
TTP "H2'2" H  N N 432 
TTP "H1'"  H  N N 433 
TTP HN3    H  N N 434 
TTP HM51   H  N N 435 
TTP HM52   H  N N 436 
TTP HM53   H  N N 437 
TTP H6     H  N N 438 
TYR N      N  N N 439 
TYR CA     C  N S 440 
TYR C      C  N N 441 
TYR O      O  N N 442 
TYR CB     C  N N 443 
TYR CG     C  Y N 444 
TYR CD1    C  Y N 445 
TYR CD2    C  Y N 446 
TYR CE1    C  Y N 447 
TYR CE2    C  Y N 448 
TYR CZ     C  Y N 449 
TYR OH     O  N N 450 
TYR OXT    O  N N 451 
TYR H      H  N N 452 
TYR H2     H  N N 453 
TYR HA     H  N N 454 
TYR HB2    H  N N 455 
TYR HB3    H  N N 456 
TYR HD1    H  N N 457 
TYR HD2    H  N N 458 
TYR HE1    H  N N 459 
TYR HE2    H  N N 460 
TYR HH     H  N N 461 
TYR HXT    H  N N 462 
VAL N      N  N N 463 
VAL CA     C  N S 464 
VAL C      C  N N 465 
VAL O      O  N N 466 
VAL CB     C  N N 467 
VAL CG1    C  N N 468 
VAL CG2    C  N N 469 
VAL OXT    O  N N 470 
VAL H      H  N N 471 
VAL H2     H  N N 472 
VAL HA     H  N N 473 
VAL HB     H  N N 474 
VAL HG11   H  N N 475 
VAL HG12   H  N N 476 
VAL HG13   H  N N 477 
VAL HG21   H  N N 478 
VAL HG22   H  N N 479 
VAL HG23   H  N N 480 
VAL HXT    H  N N 481 
# 
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  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GLN N     CA     sing N N 132 
GLN N     H      sing N N 133 
GLN N     H2     sing N N 134 
GLN CA    C      sing N N 135 
GLN CA    CB     sing N N 136 
GLN CA    HA     sing N N 137 
GLN C     O      doub N N 138 
GLN C     OXT    sing N N 139 
GLN CB    CG     sing N N 140 
GLN CB    HB2    sing N N 141 
GLN CB    HB3    sing N N 142 
GLN CG    CD     sing N N 143 
GLN CG    HG2    sing N N 144 
GLN CG    HG3    sing N N 145 
GLN CD    OE1    doub N N 146 
GLN CD    NE2    sing N N 147 
GLN NE2   HE21   sing N N 148 
GLN NE2   HE22   sing N N 149 
GLN OXT   HXT    sing N N 150 
GLU N     CA     sing N N 151 
GLU N     H      sing N N 152 
GLU N     H2     sing N N 153 
GLU CA    C      sing N N 154 
GLU CA    CB     sing N N 155 
GLU CA    HA     sing N N 156 
GLU C     O      doub N N 157 
GLU C     OXT    sing N N 158 
GLU CB    CG     sing N N 159 
GLU CB    HB2    sing N N 160 
GLU CB    HB3    sing N N 161 
GLU CG    CD     sing N N 162 
GLU CG    HG2    sing N N 163 
GLU CG    HG3    sing N N 164 
GLU CD    OE1    doub N N 165 
GLU CD    OE2    sing N N 166 
GLU OE2   HE2    sing N N 167 
GLU OXT   HXT    sing N N 168 
GLY N     CA     sing N N 169 
GLY N     H      sing N N 170 
GLY N     H2     sing N N 171 
GLY CA    C      sing N N 172 
GLY CA    HA2    sing N N 173 
GLY CA    HA3    sing N N 174 
GLY C     O      doub N N 175 
GLY C     OXT    sing N N 176 
GLY OXT   HXT    sing N N 177 
HIS N     CA     sing N N 178 
HIS N     H      sing N N 179 
HIS N     H2     sing N N 180 
HIS CA    C      sing N N 181 
HIS CA    CB     sing N N 182 
HIS CA    HA     sing N N 183 
HIS C     O      doub N N 184 
HIS C     OXT    sing N N 185 
HIS CB    CG     sing N N 186 
HIS CB    HB2    sing N N 187 
HIS CB    HB3    sing N N 188 
HIS CG    ND1    sing Y N 189 
HIS CG    CD2    doub Y N 190 
HIS ND1   CE1    doub Y N 191 
HIS ND1   HD1    sing N N 192 
HIS CD2   NE2    sing Y N 193 
HIS CD2   HD2    sing N N 194 
HIS CE1   NE2    sing Y N 195 
HIS CE1   HE1    sing N N 196 
HIS NE2   HE2    sing N N 197 
HIS OXT   HXT    sing N N 198 
ILE N     CA     sing N N 199 
ILE N     H      sing N N 200 
ILE N     H2     sing N N 201 
ILE CA    C      sing N N 202 
ILE CA    CB     sing N N 203 
ILE CA    HA     sing N N 204 
ILE C     O      doub N N 205 
ILE C     OXT    sing N N 206 
ILE CB    CG1    sing N N 207 
ILE CB    CG2    sing N N 208 
ILE CB    HB     sing N N 209 
ILE CG1   CD1    sing N N 210 
ILE CG1   HG12   sing N N 211 
ILE CG1   HG13   sing N N 212 
ILE CG2   HG21   sing N N 213 
ILE CG2   HG22   sing N N 214 
ILE CG2   HG23   sing N N 215 
ILE CD1   HD11   sing N N 216 
ILE CD1   HD12   sing N N 217 
ILE CD1   HD13   sing N N 218 
ILE OXT   HXT    sing N N 219 
LEU N     CA     sing N N 220 
LEU N     H      sing N N 221 
LEU N     H2     sing N N 222 
LEU CA    C      sing N N 223 
LEU CA    CB     sing N N 224 
LEU CA    HA     sing N N 225 
LEU C     O      doub N N 226 
LEU C     OXT    sing N N 227 
LEU CB    CG     sing N N 228 
LEU CB    HB2    sing N N 229 
LEU CB    HB3    sing N N 230 
LEU CG    CD1    sing N N 231 
LEU CG    CD2    sing N N 232 
LEU CG    HG     sing N N 233 
LEU CD1   HD11   sing N N 234 
LEU CD1   HD12   sing N N 235 
LEU CD1   HD13   sing N N 236 
LEU CD2   HD21   sing N N 237 
LEU CD2   HD22   sing N N 238 
LEU CD2   HD23   sing N N 239 
LEU OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
THR N     CA     sing N N 337 
THR N     H      sing N N 338 
THR N     H2     sing N N 339 
THR CA    C      sing N N 340 
THR CA    CB     sing N N 341 
THR CA    HA     sing N N 342 
THR C     O      doub N N 343 
THR C     OXT    sing N N 344 
THR CB    OG1    sing N N 345 
THR CB    CG2    sing N N 346 
THR CB    HB     sing N N 347 
THR OG1   HG1    sing N N 348 
THR CG2   HG21   sing N N 349 
THR CG2   HG22   sing N N 350 
THR CG2   HG23   sing N N 351 
THR OXT   HXT    sing N N 352 
TRP N     CA     sing N N 353 
TRP N     H      sing N N 354 
TRP N     H2     sing N N 355 
TRP CA    C      sing N N 356 
TRP CA    CB     sing N N 357 
TRP CA    HA     sing N N 358 
TRP C     O      doub N N 359 
TRP C     OXT    sing N N 360 
TRP CB    CG     sing N N 361 
TRP CB    HB2    sing N N 362 
TRP CB    HB3    sing N N 363 
TRP CG    CD1    doub Y N 364 
TRP CG    CD2    sing Y N 365 
TRP CD1   NE1    sing Y N 366 
TRP CD1   HD1    sing N N 367 
TRP CD2   CE2    doub Y N 368 
TRP CD2   CE3    sing Y N 369 
TRP NE1   CE2    sing Y N 370 
TRP NE1   HE1    sing N N 371 
TRP CE2   CZ2    sing Y N 372 
TRP CE3   CZ3    doub Y N 373 
TRP CE3   HE3    sing N N 374 
TRP CZ2   CH2    doub Y N 375 
TRP CZ2   HZ2    sing N N 376 
TRP CZ3   CH2    sing Y N 377 
TRP CZ3   HZ3    sing N N 378 
TRP CH2   HH2    sing N N 379 
TRP OXT   HXT    sing N N 380 
TTP PA    O1A    doub N N 381 
TTP PA    O2A    sing N N 382 
TTP PA    O3A    sing N N 383 
TTP PA    "O5'"  sing N N 384 
TTP O2A   HOA2   sing N N 385 
TTP O3A   PB     sing N N 386 
TTP PB    O1B    doub N N 387 
TTP PB    O2B    sing N N 388 
TTP PB    O3B    sing N N 389 
TTP O2B   HOB2   sing N N 390 
TTP O3B   PG     sing N N 391 
TTP PG    O1G    doub N N 392 
TTP PG    O2G    sing N N 393 
TTP PG    O3G    sing N N 394 
TTP O2G   HOG2   sing N N 395 
TTP O3G   HOG3   sing N N 396 
TTP "O5'" "C5'"  sing N N 397 
TTP "C5'" "C4'"  sing N N 398 
TTP "C5'" "H5'1" sing N N 399 
TTP "C5'" "H5'2" sing N N 400 
TTP "C4'" "O4'"  sing N N 401 
TTP "C4'" "C3'"  sing N N 402 
TTP "C4'" "H4'"  sing N N 403 
TTP "O4'" "C1'"  sing N N 404 
TTP "C3'" "O3'"  sing N N 405 
TTP "C3'" "C2'"  sing N N 406 
TTP "C3'" "H3'"  sing N N 407 
TTP "O3'" "HO3'" sing N N 408 
TTP "C2'" "C1'"  sing N N 409 
TTP "C2'" "H2'1" sing N N 410 
TTP "C2'" "H2'2" sing N N 411 
TTP "C1'" N1     sing N N 412 
TTP "C1'" "H1'"  sing N N 413 
TTP N1    C2     sing N N 414 
TTP N1    C6     sing N N 415 
TTP C2    O2     doub N N 416 
TTP C2    N3     sing N N 417 
TTP N3    C4     sing N N 418 
TTP N3    HN3    sing N N 419 
TTP C4    O4     doub N N 420 
TTP C4    C5     sing N N 421 
TTP C5    C5M    sing N N 422 
TTP C5    C6     doub N N 423 
TTP C5M   HM51   sing N N 424 
TTP C5M   HM52   sing N N 425 
TTP C5M   HM53   sing N N 426 
TTP C6    H6     sing N N 427 
TYR N     CA     sing N N 428 
TYR N     H      sing N N 429 
TYR N     H2     sing N N 430 
TYR CA    C      sing N N 431 
TYR CA    CB     sing N N 432 
TYR CA    HA     sing N N 433 
TYR C     O      doub N N 434 
TYR C     OXT    sing N N 435 
TYR CB    CG     sing N N 436 
TYR CB    HB2    sing N N 437 
TYR CB    HB3    sing N N 438 
TYR CG    CD1    doub Y N 439 
TYR CG    CD2    sing Y N 440 
TYR CD1   CE1    sing Y N 441 
TYR CD1   HD1    sing N N 442 
TYR CD2   CE2    doub Y N 443 
TYR CD2   HD2    sing N N 444 
TYR CE1   CZ     doub Y N 445 
TYR CE1   HE1    sing N N 446 
TYR CE2   CZ     sing Y N 447 
TYR CE2   HE2    sing N N 448 
TYR CZ    OH     sing N N 449 
TYR OH    HH     sing N N 450 
TYR OXT   HXT    sing N N 451 
VAL N     CA     sing N N 452 
VAL N     H      sing N N 453 
VAL N     H2     sing N N 454 
VAL CA    C      sing N N 455 
VAL CA    CB     sing N N 456 
VAL CA    HA     sing N N 457 
VAL C     O      doub N N 458 
VAL C     OXT    sing N N 459 
VAL CB    CG1    sing N N 460 
VAL CB    CG2    sing N N 461 
VAL CB    HB     sing N N 462 
VAL CG1   HG11   sing N N 463 
VAL CG1   HG12   sing N N 464 
VAL CG1   HG13   sing N N 465 
VAL CG2   HG21   sing N N 466 
VAL CG2   HG22   sing N N 467 
VAL CG2   HG23   sing N N 468 
VAL OXT   HXT    sing N N 469 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-20 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BW3 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Consensus model for preturnover condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_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          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_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          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_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         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k 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                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
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 ? 1 ?         ?            
MASKING                    ? 3  1 1 1 ?         ?            
'CTF CORRECTION'           ? 4  1 ? ? ?         ?            
'LAYERLINE INDEXING'       ? 5  1 1 1 ?         ?            
'DIFFRACTION INDEXING'     ? 6  1 1 1 ?         ?            
'MODEL FITTING'            ? 7  1 1 ? ?         ?            
OTHER                      ? 8  1 1 1 ?         ?            
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? cryoSPARC ?            
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? cryoSPARC ?            
CLASSIFICATION             ? 11 1 ? ? ?         ?            
RECONSTRUCTION             ? 12 1 ? ? ?         ?            
'MODEL REFINEMENT'         ? 13 ? 1 ? PHENIX    1.20.1_4487: 
# 
_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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' MCB-1942668 1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1719875 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
# 
_atom_sites.entry_id                    9BW3 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . VAL A 1 6   ? 104.280 117.631 99.928  1.00 57.38 ? 6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.460 117.869 99.106  1.00 58.84 ? 6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.125 118.816 97.959  1.00 58.88 ? 6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 104.299 118.495 97.103  1.00 57.73 ? 6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 106.040 116.550 98.571  1.00 59.47 ? 6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 107.241 116.822 97.678  1.00 58.72 ? 6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 106.422 115.635 99.724  1.00 58.99 ? 6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.768 119.980 97.940  1.00 57.06 ? 7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.488 120.962 96.887  1.00 50.95 ? 7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 105.940 120.466 95.523  1.00 51.58 ? 7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 106.829 119.622 95.394  1.00 54.10 ? 7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.280 122.200 97.319  1.00 48.35 ? 7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.268 121.727 98.320  1.00 51.97 ? 7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.791 120.435 98.896  1.00 53.84 ? 7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.302 121.017 94.487  1.00 48.70 ? 8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.577 120.573 93.124  1.00 47.13 ? 8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.025 120.834 92.730  1.00 51.09 ? 8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.658 119.997 92.075  1.00 51.64 ? 8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.626 121.262 92.146  1.00 49.32 ? 8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.974 121.030 90.685  1.00 51.24 ? 8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.077 121.840 89.767  1.00 52.40 ? 8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.516 121.715 88.318  1.00 50.26 ? 8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 103.774 122.650 87.429  1.00 50.69 ? 8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.565 121.998 93.103  1.00 52.70 ? 9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.945 122.307 92.744  1.00 48.35 ? 9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 109.914 121.345 93.416  1.00 49.36 ? 9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 110.921 120.949 92.819  1.00 51.99 ? 9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.284 123.753 93.105  1.00 47.11 ? 9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.903 124.158 94.493  1.00 42.54 ? 9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.696 124.126 95.601  1.00 44.10 ? 9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.641 124.682 94.917  1.00 45.15 ? 9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.003 124.587 96.693  1.00 44.97 ? 9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.738 124.935 96.299  1.00 46.11 ? 9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.436 124.955 94.265  1.00 46.87 ? 9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.677 125.449 97.039  1.00 46.18 ? 9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.384 125.465 95.001  1.00 48.58 ? 9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.511 125.706 96.373  1.00 47.62 ? 9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.631 120.959 94.661  1.00 50.06 ? 10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.468 119.971 95.331  1.00 51.15 ? 10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.379 118.628 94.619  1.00 51.21 ? 10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.379 117.911 94.489  1.00 53.07 ? 10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.076 119.853 96.814  1.00 51.35 ? 10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.575 121.071 97.593  1.00 49.98 ? 10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.633 118.571 97.406  1.00 49.70 ? 10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 111.908 121.595 97.114  1.00 51.52 ? 10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.184 118.260 94.151  1.00 53.37 ? 11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.039 117.013 93.408  1.00 53.79 ? 11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 109.857 117.043 92.124  1.00 52.95 ? 11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 110.525 116.061 91.781  1.00 56.25 ? 11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 107.565 116.753 93.097  1.00 52.33 ? 11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 106.811 116.029 94.199  1.00 54.46 ? 11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 105.377 116.502 94.329  1.00 57.73 ? 11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 104.616 116.487 93.361  1.00 56.42 ? 11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 105.000 116.926 95.529  1.00 54.44 ? 11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 109.814 118.162 91.399  1.00 49.15 ? 12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.599 118.277 90.175  1.00 49.66 ? 12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.092 118.230 90.473  1.00 50.29 ? 12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 112.856 117.566 89.762  1.00 52.22 ? 12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.236 119.567 89.440  1.00 48.98 ? 12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.019 119.496 88.519  1.00 47.93 ? 12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.510 120.890 88.195  1.00 49.80 ? 12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.353 118.735 87.247  1.00 50.18 ? 12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.527 118.928 91.524  1.00 47.73 ? 13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 113.943 118.939 91.874  1.00 47.85 ? 13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.421 117.552 92.283  1.00 50.76 ? 13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 115.526 117.135 91.917  1.00 54.40 ? 13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.195 119.949 92.993  1.00 50.68 ? 13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.615 119.900 93.514  1.00 49.14 ? 13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 115.895 119.261 94.526  1.00 51.51 ? 13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.521 120.580 92.822  1.00 50.96 ? 13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.605 116.822 93.046  1.00 54.17 ? 14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 113.978 115.472 93.449  1.00 54.23 ? 14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.083 114.527 92.261  1.00 55.31 ? 14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 114.692 113.459 92.386  1.00 59.49 ? 14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 112.973 114.927 94.463  1.00 54.11 ? 14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.197 115.476 95.856  1.00 56.75 ? 14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 112.725 114.910 96.842  1.00 58.87 ? 14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.921 116.585 95.945  1.00 56.50 ? 14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 113.503 114.891 91.117  1.00 53.98 ? 15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 113.648 114.095 89.907  1.00 55.74 ? 15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.050 114.176 89.322  1.00 56.99 ? 15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.360 113.421 88.395  1.00 58.83 ? 15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.624 114.541 88.862  1.00 56.39 ? 15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.289 113.821 88.957  1.00 57.14 ? 15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.185 114.538 88.205  1.00 61.00 ? 15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.313 114.707 86.974  1.00 60.78 ? 15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.189 114.935 88.846  1.00 60.40 ? 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 115.896 115.072 89.833  1.00 57.72 ? 16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.272 115.164 89.352  1.00 57.43 ? 16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 117.986 113.833 89.546  1.00 57.92 ? 16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 118.648 113.322 88.636  1.00 57.58 ? 16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.016 116.305 90.071  1.00 58.11 ? 16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.424 117.665 89.696  1.00 55.27 ? 16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.501 116.260 89.745  1.00 57.10 ? 16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 117.496 117.979 88.228  1.00 55.09 ? 16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 117.855 113.249 90.739  1.00 59.08 ? 17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.584 112.030 91.064  1.00 58.90 ? 17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 117.959 110.790 90.441  1.00 58.88 ? 17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 118.599 109.733 90.423  1.00 59.27 ? 17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.672 111.864 92.581  1.00 58.46 ? 17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.334 113.035 93.286  1.00 58.20 ? 17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.956 113.426 92.608  1.00 64.09 ? 17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 122.007 112.397 93.628  1.00 59.51 ? 17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 116.732 110.889 89.934  1.00 62.11 ? 18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.079 109.766 89.265  1.00 62.69 ? 18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 116.718 109.637 87.886  1.00 63.15 ? 18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 116.362 110.357 86.952  1.00 64.19 ? 18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 114.564 109.955 89.174  1.00 62.13 ? 18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 113.936 109.889 90.568  1.00 62.42 ? 18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 113.951 108.910 88.255  1.00 61.08 ? 18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 112.440 110.097 90.575  1.00 63.95 ? 18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 117.668 108.716 87.755  1.00 66.16 ? 19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 118.411 108.580 86.511  1.00 67.05 ? 19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 117.510 108.040 85.409  1.00 66.62 ? 19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 116.828 107.026 85.588  1.00 68.63 ? 19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 119.615 107.661 86.713  1.00 68.03 ? 19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 120.680 108.237 87.632  1.00 67.68 ? 19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 121.963 107.432 87.617  1.00 69.35 ? 19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 122.049 106.391 86.965  1.00 68.61 ? 19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 122.970 107.910 88.339  1.00 66.70 ? 19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 117.510 108.722 84.267  1.00 67.41 ? 20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 116.763 108.302 83.089  1.00 68.91 ? 20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 117.749 108.104 81.949  1.00 70.42 ? 20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 118.526 109.011 81.634  1.00 70.57 ? 20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 115.697 109.333 82.712  1.00 68.12 ? 20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.348 109.359 81.233  1.00 68.29 ? 20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 115.486 110.759 80.659  1.00 68.94 ? 20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 115.500 110.736 79.139  1.00 70.09 ? 20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 115.448 112.107 78.562  1.00 68.36 ? 20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 117.719 106.922 81.337  1.00 71.02 ? 21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 118.657 106.546 80.285  1.00 70.06 ? 21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 120.086 106.433 80.802  1.00 70.99 ? 21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 121.040 106.545 80.025  1.00 70.57 ? 21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 118.596 107.535 79.114  1.00 70.71 ? 21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 119.292 107.015 77.872  1.00 72.79 ? 21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 119.219 105.795 77.615  1.00 73.04 ? 21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 119.912 107.827 77.153  1.00 72.01 ? 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 120.256 106.214 82.104  1.00 70.01 ? 22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 121.568 106.128 82.705  1.00 69.00 ? 22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 122.189 107.452 83.089  1.00 70.59 ? 22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 123.304 107.459 83.627  1.00 71.85 ? 22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 121.512 108.569 82.839  1.00 68.91 ? 23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.046 109.892 83.115  1.00 65.65 ? 23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.086 110.673 84.000  1.00 66.16 ? 23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 119.867 110.485 83.941  1.00 67.79 ? 23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.300 110.667 81.817  1.00 64.19 ? 23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.420 110.098 80.964  1.00 66.42 ? 23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.655 110.943 79.725  1.00 65.91 ? 23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.736 110.340 78.844  1.00 65.49 ? 23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.913 111.106 77.580  1.00 66.02 ? 23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 121.649 111.553 84.825  1.00 62.03 ? 24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 120.831 112.416 85.664  1.00 57.74 ? 24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 119.987 113.345 84.802  1.00 57.55 ? 24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 120.417 113.793 83.735  1.00 56.57 ? 24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 121.712 113.236 86.606  1.00 55.83 ? 24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 122.388 112.423 87.668  1.00 57.34 ? 24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 121.732 112.119 88.848  1.00 58.06 ? 24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 123.681 111.965 87.490  1.00 57.22 ? 24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 122.352 111.372 89.828  1.00 57.82 ? 24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 124.305 111.218 88.466  1.00 55.59 ? 24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 123.640 110.921 89.637  1.00 56.13 ? 24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 118.773 113.631 85.269  1.00 59.14 ? 25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 117.866 114.536 84.563  1.00 57.92 ? 25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.113 115.968 85.038  1.00 58.07 ? 25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.340 116.558 85.794  1.00 59.36 ? 25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 116.419 114.112 84.776  1.00 58.55 ? 25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.057 112.789 84.128  1.00 58.49 ? 25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 114.694 112.289 84.560  1.00 59.66 ? 25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 113.669 112.708 84.025  1.00 59.76 ? 25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.676 111.386 85.533  1.00 58.81 ? 25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.229 116.526 84.564  1.00 53.84 ? 26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 119.617 117.868 84.982  1.00 50.41 ? 26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 118.616 118.916 84.513  1.00 51.31 ? 26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.506 119.984 85.125  1.00 50.82 ? 26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.016 118.196 84.459  1.00 49.05 ? 26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.103 117.365 85.079  1.00 50.87 ? 26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.294 117.360 86.450  1.00 49.00 ? 26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 122.930 116.584 84.291  1.00 49.74 ? 26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.292 116.594 87.022  1.00 48.13 ? 26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 123.929 115.817 84.858  1.00 48.73 ? 26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.110 115.823 86.225  1.00 49.15 ? 26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 117.879 118.633 83.437  1.00 53.81 ? 27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 116.898 119.588 82.937  1.00 52.97 ? 27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 115.718 119.758 83.885  1.00 53.10 ? 27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 114.949 120.712 83.731  1.00 52.04 ? 27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.399 119.158 81.558  1.00 54.53 ? 27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 115.889 117.730 81.541  1.00 57.76 ? 27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.699 116.806 81.762  1.00 55.72 ? 27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 114.678 117.534 81.307  1.00 57.67 ? 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 115.556 118.858 84.857  1.00 49.79 ? 28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.472 118.993 85.821  1.00 52.49 ? 28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.652 120.198 86.734  1.00 54.07 ? 28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.672 120.658 87.329  1.00 55.04 ? 28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.351 117.720 86.661  1.00 54.50 ? 28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 113.305 116.740 86.155  1.00 52.75 ? 28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 113.440 116.513 84.660  1.00 56.69 ? 28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.089 116.256 84.017  1.00 54.64 ? 28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 111.265 115.307 84.814  1.00 55.04 ? 28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.874 120.719 86.859  1.00 52.08 ? 29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.106 121.878 87.711  1.00 50.49 ? 29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.525 123.160 87.131  1.00 47.92 ? 29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.007 123.986 87.889  1.00 46.99 ? 29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.604 122.060 87.960  1.00 47.41 ? 29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.911 122.437 89.394  1.00 48.01 ? 29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.958 122.571 90.190  1.00 48.39 ? 29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 119.104 122.602 89.724  1.00 49.55 ? 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.602 123.350 85.812  1.00 47.25 ? 30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.918 124.478 85.195  1.00 49.43 ? 30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.411 124.376 85.380  1.00 50.80 ? 30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.761 125.371 85.722  1.00 53.07 ? 30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.272 124.558 83.708  1.00 49.11 ? 30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 114.453 125.557 82.903  1.00 49.92 ? 30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 114.221 126.851 83.668  1.00 55.07 ? 30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 113.069 127.646 83.074  1.00 53.37 ? 30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 112.533 128.655 84.031  1.00 51.67 ? 30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.846 123.183 85.181  1.00 49.84 ? 31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.437 122.964 85.480  1.00 49.76 ? 31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.150 123.166 86.961  1.00 46.63 ? 31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.119 123.741 87.324  1.00 50.34 ? 31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.016 121.560 85.048  1.00 49.44 ? 31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.415 121.487 83.658  1.00 49.18 ? 31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 110.370 120.072 83.121  1.00 54.68 ? 31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.332 119.312 83.364  1.00 55.84 ? 31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 109.371 119.717 82.461  1.00 50.92 ? 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.045 122.691 87.828  1.00 43.42 ? 32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.838 122.855 89.261  1.00 43.56 ? 32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.794 124.327 89.645  1.00 47.51 ? 32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.918 124.749 90.407  1.00 48.81 ? 32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.935 122.128 90.038  1.00 44.72 ? 32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.717 125.130 89.112  1.00 48.98 ? 33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.742 126.551 89.447  1.00 45.53 ? 33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.539 127.266 88.843  1.00 44.38 ? 33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.950 128.155 89.470  1.00 45.65 ? 33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 114.074 127.186 89.000  1.00 42.77 ? 33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.053 127.501 87.513  1.00 41.59 ? 33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.361 128.440 89.810  1.00 43.68 ? 33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 111.154 126.896 87.620  1.00 44.87 ? 34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.981 127.506 87.004  1.00 45.97 ? 34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.729 127.242 87.831  1.00 45.69 ? 34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.937 128.156 88.092  1.00 49.21 ? 34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.805 126.982 85.580  1.00 48.40 ? 34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.877 127.805 84.744  1.00 49.36 ? 34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.506 127.739 84.870  1.00 46.93 ? 34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 109.121 128.714 83.772  1.00 50.27 ? 34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.946 128.571 84.011  1.00 48.16 ? 34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.904 129.175 83.332  1.00 49.60 ? 34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.529 125.988 88.244  1.00 46.39 ? 35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.372 125.660 89.068  1.00 46.46 ? 35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.447 126.359 90.418  1.00 45.88 ? 35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.444 126.893 90.905  1.00 49.64 ? 35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.267 124.147 89.250  1.00 46.71 ? 35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 107.742 123.754 90.525  1.00 48.41 ? 35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.631 126.372 91.035  1.00 47.65 ? 36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.810 127.079 92.296  1.00 48.20 ? 36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.338 128.517 92.177  1.00 46.09 ? 36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.513 128.981 92.969  1.00 47.50 ? 36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.281 127.025 92.711  1.00 44.96 ? 36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.632 127.871 93.914  1.00 42.67 ? 36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.026 127.657 95.143  1.00 41.35 ? 36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.579 128.881 93.819  1.00 44.15 ? 36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.353 128.426 96.242  1.00 42.72 ? 36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.911 129.655 94.910  1.00 43.57 ? 36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.296 129.424 96.119  1.00 45.46 ? 36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.625 130.195 97.209  1.00 47.21 ? 36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.826 129.229 91.163  1.00 47.56 ? 37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.393 130.606 90.970  1.00 45.84 ? 37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.886 130.674 90.772  1.00 47.72 ? 37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 106.168 131.223 91.614  1.00 52.74 ? 37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 109.137 131.238 89.794  1.00 48.82 ? 37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.380 131.970 90.201  1.00 49.00 ? 37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.314 133.285 90.628  1.00 48.77 ? 37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.609 131.338 90.184  1.00 46.41 ? 37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.453 133.958 91.015  1.00 47.40 ? 37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.750 132.008 90.569  1.00 48.12 ? 37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.672 133.318 90.986  1.00 47.73 ? 37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.388 130.040 89.707  1.00 52.14 ? 38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 105.001 130.220 89.288  1.00 52.73 ? 38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 104.018 129.823 90.381  1.00 52.09 ? 38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.886 130.322 90.412  1.00 54.14 ? 38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.742 129.432 87.989  1.00 50.57 ? 38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 103.258 129.171 87.815  1.00 51.77 ? 38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 105.299 130.184 86.794  1.00 50.15 ? 38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.413 128.933 91.293  1.00 48.30 ? 39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.467 128.431 92.280  1.00 49.72 ? 39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.688 128.968 93.687  1.00 52.34 ? 39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.774 128.869 94.512  1.00 56.20 ? 39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.508 126.899 92.322  1.00 51.59 ? 39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.353 126.274 90.949  1.00 55.57 ? 39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.713 126.900 90.078  1.00 55.11 ? 39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 103.870 125.158 90.740  1.00 56.65 ? 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.858 129.527 93.995  1.00 48.49 ? 40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 105.106 130.069 95.324  1.00 48.52 ? 40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.453 131.548 95.298  1.00 53.38 ? 40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.870 132.330 96.057  1.00 55.01 ? 40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.232 129.271 96.005  1.00 50.02 ? 40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.314 129.460 97.503  1.00 51.00 ? 40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 106.780 130.648 98.050  1.00 51.01 ? 40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 105.924 128.449 98.370  1.00 52.07 ? 40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 106.857 130.822 99.417  1.00 51.12 ? 40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 105.997 128.614 99.737  1.00 52.58 ? 40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.463 129.802 100.256 1.00 52.64 ? 40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.537 129.969 101.619 1.00 53.27 ? 40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.374 131.961 94.427  1.00 50.58 ? 41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.938 133.302 94.526  1.00 48.64 ? 41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.986 134.332 93.936  1.00 47.09 ? 41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.717 135.372 94.547  1.00 50.90 ? 41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.319 133.350 93.844  1.00 50.18 ? 41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.261 132.321 94.473  1.00 48.40 ? 41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.914 134.744 93.942  1.00 47.77 ? 41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.430 132.480 95.963  1.00 45.19 ? 41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.459 134.061 92.741  1.00 49.10 ? 42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.493 134.977 92.148  1.00 51.69 ? 42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.239 135.090 93.003  1.00 53.22 ? 42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.606 136.151 93.037  1.00 54.19 ? 42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 104.137 134.523 90.734  1.00 51.53 ? 42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.345 134.457 89.821  1.00 51.51 ? 42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.428 134.919 90.175  1.00 53.29 ? 42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.164 133.881 88.639  1.00 53.15 ? 42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.865 134.012 93.695  1.00 57.15 ? 43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.699 134.061 94.570  1.00 55.18 ? 43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.987 134.854 95.839  1.00 54.33 ? 43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 101.165 135.674 96.264  1.00 56.82 ? 43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.250 132.642 94.919  1.00 54.33 ? 43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.327 131.662 93.760  1.00 55.66 ? 43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.411 132.040 92.613  1.00 57.37 ? 43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.595 133.073 91.970  1.00 56.74 ? 43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.420  131.198 92.348  1.00 55.86 ? 43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.149 134.631 96.454  1.00 47.34 ? 44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.474 135.195 97.756  1.00 50.29 ? 44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.243 136.508 97.657  1.00 51.03 ? 44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.911 136.901 98.619  1.00 50.25 ? 44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.267 134.181 98.580  1.00 50.19 ? 44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.429 132.992 99.003  1.00 50.75 ? 44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 102.982 132.205 98.169  1.00 52.81 ? 44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.216 132.850 100.306 1.00 50.51 ? 44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.163 137.194 96.521  1.00 51.03 ? 45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.838 138.470 96.328  1.00 53.63 ? 45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.835 139.596 96.540  1.00 54.11 ? 45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.811 139.658 95.851  1.00 54.84 ? 45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.459 138.559 94.934  1.00 55.43 ? 45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.315 137.431 94.717  1.00 57.72 ? 45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.272 139.836 94.794  1.00 51.71 ? 45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 104.131 140.483 97.493  1.00 52.94 ? 46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.246 141.610 97.755  1.00 51.69 ? 46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.110 142.441 96.490  1.00 53.87 ? 46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.105 142.784 95.840  1.00 52.85 ? 46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.776 142.449 98.926  1.00 51.04 ? 46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.875 143.649 99.166  1.00 49.80 ? 46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.884 141.598 100.179 1.00 49.66 ? 46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 101.872 142.770 96.134  1.00 60.05 ? 47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 101.589 143.458 94.883  1.00 57.43 ? 47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.508 144.960 95.115  1.00 59.22 ? 47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.838 145.419 96.045  1.00 60.06 ? 47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 100.286 142.942 94.269  1.00 57.28 ? 47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 99.868  143.676 93.025  1.00 59.79 ? 47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 99.108  144.831 93.104  1.00 58.17 ? 47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.241 143.212 91.775  1.00 60.27 ? 47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 98.726  145.506 91.961  1.00 60.79 ? 47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 99.862  143.883 90.628  1.00 59.21 ? 47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 99.103  145.031 90.722  1.00 59.06 ? 47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.198 145.717 94.267  1.00 60.22 ? 48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 102.139 147.170 94.266  1.00 57.93 ? 48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.815 147.641 92.858  1.00 56.29 ? 48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 102.311 147.078 91.878  1.00 57.19 ? 48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 103.458 147.787 94.743  1.00 56.80 ? 48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 103.802 147.455 96.165  1.00 54.31 ? 48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 103.216 148.145 97.212  1.00 56.43 ? 48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 104.709 146.452 96.456  1.00 53.85 ? 48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 103.530 147.840 98.521  1.00 57.20 ? 48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 105.027 146.144 97.762  1.00 55.99 ? 48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 104.436 146.839 98.796  1.00 55.96 ? 48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.976 148.674 92.760  1.00 59.22 ? 49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 100.556 149.152 91.448  1.00 61.42 ? 49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 101.746 149.629 90.627  1.00 61.66 ? 49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 101.859 149.309 89.438  1.00 62.30 ? 49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 99.526  150.272 91.602  1.00 63.34 ? 49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 98.312  149.873 92.380  1.00 64.55 ? 49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 98.127  150.219 93.701  1.00 64.53 ? 49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 97.220  149.154 92.024  1.00 63.21 ? 49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.974  149.733 94.125  1.00 64.24 ? 49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 96.404  149.082 93.127  1.00 64.21 ? 49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 102.648 150.386 91.245  1.00 62.57 ? 50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.802 150.931 90.547  1.00 60.54 ? 50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.964 151.037 91.523  1.00 60.31 ? 50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 104.814 150.827 92.729  1.00 61.06 ? 50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 103.482 152.291 89.920  1.00 58.89 ? 50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.880 153.263 90.913  1.00 61.20 ? 50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 103.542 153.694 91.857  1.00 61.62 ? 50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 101.617 153.614 90.705  1.00 60.72 ? 50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 106.138 151.368 90.980  1.00 54.62 ? 51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 107.335 151.458 91.809  1.00 54.23 ? 51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 107.194 152.540 92.872  1.00 54.39 ? 51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.715 152.397 93.983  1.00 56.36 ? 51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 108.561 151.720 90.935  1.00 54.04 ? 51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.901 151.842 91.664  1.00 52.67 ? 51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 110.271 150.529 92.336  1.00 49.93 ? 51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.993 152.285 90.705  1.00 52.24 ? 51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 106.504 153.635 92.549  1.00 57.84 ? 52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 106.344 154.716 93.516  1.00 55.42 ? 52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 105.599 154.238 94.755  1.00 56.26 ? 52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 106.023 154.494 95.888  1.00 55.50 ? 52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 105.616 155.894 92.869  1.00 52.67 ? 52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 105.510 157.121 93.760  1.00 54.53 ? 52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 106.209 158.317 93.133  1.00 57.10 ? 52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 106.321 159.470 94.117  1.00 57.34 ? 52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 107.486 159.310 95.030  1.00 57.53 ? 52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 104.483 153.535 94.556  1.00 59.05 ? 53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.710 153.040 95.689  1.00 59.68 ? 53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 104.514 152.041 96.509  1.00 57.99 ? 53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 104.488 152.076 97.745  1.00 59.66 ? 53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 102.407 152.411 95.195  1.00 58.03 ? 53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 101.658 151.618 96.250  1.00 58.63 ? 53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 100.610 150.703 95.650  1.00 62.49 ? 53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 100.004 151.082 94.626  1.00 64.11 ? 53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 100.391 149.603 96.202  1.00 61.28 ? 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 105.238 151.142 95.839  1.00 57.02 ? 54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 106.040 150.152 96.552  1.00 54.41 ? 54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 107.126 150.820 97.385  1.00 49.51 ? 54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 107.345 150.460 98.547  1.00 51.78 ? 54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.656 149.166 95.560  1.00 54.31 ? 54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.597 148.157 96.197  1.00 52.88 ? 54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 108.107 147.158 95.173  1.00 52.56 ? 54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.967 146.090 95.825  1.00 54.60 ? 54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 109.231 144.958 94.897  1.00 53.54 ? 54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.823 151.797 96.801  1.00 50.55 ? 55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.883 152.484 97.530  1.00 51.94 ? 55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 108.322 153.277 98.702  1.00 53.70 ? 55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.913 153.290 99.788  1.00 56.98 ? 55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 109.664 153.396 96.584  1.00 53.82 ? 55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 110.571 152.687 95.577  1.00 54.01 ? 55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 111.461 153.686 94.858  1.00 54.11 ? 55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 111.404 151.618 96.266  1.00 52.34 ? 55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 107.185 153.947 98.503  1.00 58.44 ? 56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 106.567 154.682 99.600  1.00 58.34 ? 56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 106.158 153.742 100.725 1.00 58.00 ? 56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 106.366 154.046 101.904 1.00 59.76 ? 56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 105.362 155.471 99.089  1.00 57.76 ? 56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 105.765 156.719 98.326  1.00 60.79 ? 56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 106.603 157.488 98.843  1.00 60.29 ? 56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 105.246 156.930 97.211  1.00 60.54 ? 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 105.579 152.589 100.381 1.00 53.74 ? 57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 105.203 151.620 101.404 1.00 54.05 ? 57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 106.428 151.111 102.152 1.00 54.65 ? 57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 106.413 151.004 103.384 1.00 55.10 ? 57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 104.429 150.465 100.762 1.00 53.65 ? 57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 104.208 149.257 101.652 1.00 55.16 ? 57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 105.234 148.358 101.918 1.00 54.92 ? 57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 102.967 149.017 102.225 1.00 55.05 ? 57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 105.031 147.260 102.728 1.00 58.46 ? 57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 102.754 147.921 103.036 1.00 56.42 ? 57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.789 147.046 103.284 1.00 57.76 ? 57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 103.580 145.953 104.092 1.00 55.65 ? 57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 107.499 150.791 101.424 1.00 51.68 ? 58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.691 150.242 102.061 1.00 49.39 ? 58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 109.351 151.263 102.979 1.00 49.36 ? 58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.805 150.916 104.075 1.00 48.16 ? 58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.672 149.754 100.996 1.00 48.40 ? 58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 109.259 148.477 100.261 1.00 48.42 ? 58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 110.084 148.284 99.002  1.00 49.02 ? 58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 109.382 147.268 101.175 1.00 48.06 ? 58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 109.420 152.524 102.549 1.00 52.24 ? 59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 110.035 153.554 103.381 1.00 53.97 ? 59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 109.162 153.862 104.591 1.00 55.71 ? 59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.662 154.015 105.712 1.00 53.73 ? 59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 110.315 154.816 102.547 1.00 52.20 ? 59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.645 155.986 103.457 1.00 53.79 ? 59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 111.448 154.562 101.566 1.00 52.68 ? 59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.846 153.962 104.386 1.00 58.72 ? 60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.947 154.312 105.481 1.00 57.37 ? 60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.955 153.249 106.573 1.00 56.97 ? 60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.933 153.575 107.766 1.00 59.67 ? 60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 105.530 154.523 104.942 1.00 56.25 ? 60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.619 153.312 105.077 1.00 58.58 ? 60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.392 153.397 104.188 1.00 60.27 ? 60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 103.253 154.396 103.452 1.00 59.44 ? 60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 102.567 152.460 104.225 1.00 58.16 ? 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.988 151.974 106.189 1.00 52.26 ? 61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.889 150.871 107.134 1.00 53.93 ? 61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 108.234 150.489 107.741 1.00 54.74 ? 61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 108.373 149.380 108.269 1.00 55.20 ? 61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 106.250 149.657 106.458 1.00 56.03 ? 61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.748 149.795 106.320 1.00 58.58 ? 61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 104.241 150.162 105.260 1.00 57.79 ? 61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 104.026 149.502 107.395 1.00 57.00 ? 61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 109.222 151.381 107.682 1.00 53.30 ? 62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 110.521 151.151 108.312 1.00 53.93 ? 62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 111.246 149.963 107.686 1.00 53.54 ? 62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.947 149.212 108.366 1.00 53.09 ? 62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 110.371 150.959 109.823 1.00 54.39 ? 62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.524 152.021 110.506 1.00 52.62 ? 62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.997 153.428 110.203 1.00 54.90 ? 62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.988 153.895 110.764 1.00 57.28 ? 62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 109.289 154.112 109.313 1.00 52.77 ? 62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 111.076 149.787 106.375 1.00 49.69 ? 63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.801 148.767 105.625 1.00 47.31 ? 63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 113.069 149.333 104.995 1.00 49.70 ? 63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 114.168 148.824 105.232 1.00 46.66 ? 63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.901 148.158 104.541 1.00 48.86 ? 63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.850 147.209 105.063 1.00 50.12 ? 63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 110.200 146.109 105.833 1.00 48.82 ? 63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 108.506 147.405 104.775 1.00 50.82 ? 63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 109.243 145.237 106.307 1.00 48.46 ? 63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 107.542 146.538 105.245 1.00 48.80 ? 63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.916 145.456 106.009 1.00 52.11 ? 63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.958 144.589 106.480 1.00 53.81 ? 63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.931 150.385 104.196 1.00 47.09 ? 64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 114.052 151.017 103.519 1.00 42.55 ? 64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 114.422 152.318 104.215 1.00 46.64 ? 64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.551 153.130 104.539 1.00 49.04 ? 64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.716 151.308 102.055 1.00 42.06 ? 64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.696 150.096 101.161 1.00 44.45 ? 64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 114.103 148.855 101.627 1.00 43.06 ? 64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 113.272 150.195 99.844  1.00 44.58 ? 64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 114.083 147.747 100.807 1.00 39.71 ? 64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 113.249 149.095 99.019  1.00 42.68 ? 64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.654 147.874 99.504  1.00 41.13 ? 64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.631 146.777 98.676  1.00 44.46 ? 64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.717 152.513 104.440 1.00 51.56 ? 65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 116.200 153.804 104.907 1.00 47.56 ? 65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.924 154.863 103.847 1.00 50.10 ? 65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 116.158 154.639 102.656 1.00 51.87 ? 65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.695 153.732 105.217 1.00 44.92 ? 65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 118.027 153.049 106.536 1.00 48.31 ? 65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 119.449 152.517 106.580 1.00 52.51 ? 65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 120.258 152.904 105.711 1.00 52.91 ? 65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.758 151.713 107.484 1.00 52.38 ? 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 115.418 156.018 104.277 1.00 49.85 ? 66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 115.107 157.095 103.346 1.00 49.11 ? 66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 116.317 157.979 103.068 1.00 49.64 ? 66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 116.245 158.862 102.209 1.00 51.18 ? 66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.965 157.953 103.903 1.00 50.03 ? 66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 113.366 158.997 102.952 1.00 51.19 ? 66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 113.360 158.566 101.488 1.00 55.13 ? 66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 114.429 158.432 100.866 1.00 53.06 ? 66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.252 158.358 100.951 1.00 54.23 ? 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 117.420 157.782 103.790 1.00 50.01 ? 67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 118.592 158.629 103.595 1.00 50.68 ? 67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 119.201 158.415 102.214 1.00 54.08 ? 67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 119.487 159.376 101.491 1.00 53.40 ? 67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 119.622 158.351 104.690 1.00 53.18 ? 67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 119.179 158.770 106.086 1.00 51.07 ? 67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 118.163 157.818 106.689 1.00 53.44 ? 67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 117.422 157.172 105.919 1.00 56.49 ? 67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 118.106 157.714 107.932 1.00 54.46 ? 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 119.404 157.153 101.829 1.00 46.95 ? 68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 120.028 156.863 100.543 1.00 45.50 ? 68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 119.063 157.052 99.381  1.00 43.44 ? 68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 119.487 157.446 98.290  1.00 47.42 ? 68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 120.597 155.442 100.542 1.00 45.65 ? 68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 119.604 154.385 100.155 1.00 43.74 ? 68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 118.717 153.874 101.086 1.00 44.00 ? 68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 119.572 153.887 98.863  1.00 40.40 ? 68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.807 152.898 100.732 1.00 44.80 ? 68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.665 152.912 98.504  1.00 40.10 ? 68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.783 152.416 99.440  1.00 42.76 ? 68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 117.773 156.781 99.588  1.00 41.54 ? 69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 116.804 156.950 98.511  1.00 46.16 ? 69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 116.555 158.420 98.201  1.00 45.30 ? 69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 116.259 158.769 97.053  1.00 43.43 ? 69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 115.492 156.254 98.872  1.00 45.60 ? 69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 115.488 154.731 98.749  1.00 43.57 ? 69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 114.242 154.141 99.389  1.00 44.02 ? 69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 115.598 154.315 97.293  1.00 41.68 ? 69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 116.671 159.293 99.204  1.00 47.73 ? 70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 116.407 160.712 99.002  1.00 46.02 ? 70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 117.450 161.383 98.119  1.00 49.29 ? 70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 117.190 162.470 97.594  1.00 46.15 ? 70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 116.336 161.426 100.351 1.00 45.91 ? 70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 117.585 161.369 101.017 1.00 46.73 ? 70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 118.622 160.768 97.946  1.00 47.60 ? 71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 119.661 161.354 97.109  1.00 40.40 ? 71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 119.316 161.316 95.628  1.00 43.87 ? 71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.965 162.013 94.841  1.00 43.42 ? 71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.992 160.638 97.342  1.00 42.06 ? 71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 121.421 160.453 98.797  1.00 43.09 ? 71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 122.626 159.535 98.886  1.00 43.85 ? 71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 121.722 161.797 99.435  1.00 43.57 ? 71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 118.321 160.529 95.233  1.00 40.21 ? 72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 117.932 160.386 93.839  1.00 43.18 ? 72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 116.540 160.960 93.624  1.00 44.27 ? 72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 115.638 160.748 94.441  1.00 46.32 ? 72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.933 158.916 93.410  1.00 41.20 ? 72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 119.224 158.178 93.663  1.00 37.84 ? 72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 120.202 158.092 92.682  1.00 39.85 ? 72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.458 157.553 94.879  1.00 36.73 ? 72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 121.378 157.410 92.910  1.00 36.98 ? 72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.629 156.872 95.115  1.00 38.23 ? 72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 121.586 156.802 94.128  1.00 37.38 ? 72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 122.755 156.122 94.363  1.00 38.78 ? 72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 116.367 161.683 92.524  1.00 45.32 ? 73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 115.026 162.006 92.069  1.00 47.20 ? 73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 114.311 160.722 91.672  1.00 45.93 ? 73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 114.928 159.767 91.196  1.00 48.65 ? 73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 115.074 162.977 90.890  1.00 48.08 ? 73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 115.387 162.302 89.686  1.00 47.44 ? 73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 112.993 160.694 91.882  1.00 52.60 ? 74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 112.265 159.455 91.633  1.00 50.35 ? 74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 112.428 158.979 90.198  1.00 49.64 ? 74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 112.347 157.775 89.934  1.00 51.10 ? 74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 110.784 159.609 91.963  1.00 49.96 ? 74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 110.048 158.307 91.961  1.00 52.81 ? 74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 110.110 157.459 93.052  1.00 51.35 ? 74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 109.326 157.911 90.850  1.00 51.23 ? 74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 109.447 156.251 93.042  1.00 50.59 ? 74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 108.662 156.705 90.834  1.00 51.41 ? 74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 108.726 155.874 91.929  1.00 53.24 ? 74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 112.652 159.896 89.257  1.00 50.26 ? 75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 112.934 159.476 87.889  1.00 48.78 ? 75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 114.203 158.636 87.831  1.00 52.58 ? 75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 114.256 157.625 87.122  1.00 52.01 ? 75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 113.050 160.697 86.977  1.00 50.87 ? 75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 111.719 161.345 86.634  1.00 51.09 ? 75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 110.810 160.426 85.842  1.00 55.71 ? 75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 111.274 159.854 84.833  1.00 53.25 ? 75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 109.631 160.275 86.226  1.00 56.26 ? 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 115.234 159.036 88.578  1.00 46.87 ? 76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 116.475 158.269 88.604  1.00 43.10 ? 76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 116.259 156.883 89.200  1.00 42.41 ? 76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 116.776 155.887 88.680  1.00 49.64 ? 76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 117.539 159.033 89.392  1.00 46.78 ? 76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 117.988 160.297 88.686  1.00 49.09 ? 76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 117.760 160.411 87.464  1.00 47.03 ? 76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 118.567 161.178 89.356  1.00 48.32 ? 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 115.503 156.800 90.297  1.00 42.08 ? 77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 115.229 155.505 90.914  1.00 40.41 ? 77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 114.444 154.617 89.959  1.00 42.85 ? 77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 114.717 153.417 89.834  1.00 44.94 ? 77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 114.487 155.696 92.249  1.00 44.68 ? 77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 115.395 156.387 93.267  1.00 44.62 ? 77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.997 154.360 92.783  1.00 42.39 ? 77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 114.677 156.837 94.518  1.00 45.67 ? 77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 113.449 155.191 89.280  1.00 45.88 ? 78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 112.671 154.424 88.315  1.00 43.84 ? 78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 113.550 153.928 87.176  1.00 44.16 ? 78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 113.407 152.788 86.724  1.00 47.73 ? 78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 111.521 155.276 87.777  1.00 46.03 ? 78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 110.445 154.487 87.053  1.00 46.22 ? 78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 109.236 155.357 86.752  1.00 49.77 ? 78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 108.240 155.335 87.899  1.00 50.88 ? 78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.834 155.340 87.413  1.00 46.64 ? 78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 114.464 154.773 86.695  1.00 46.14 ? 79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 115.363 154.357 85.626  1.00 46.20 ? 79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 116.272 153.223 86.083  1.00 43.46 ? 79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 116.511 152.269 85.334  1.00 46.42 ? 79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 116.190 155.548 85.142  1.00 44.45 ? 79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 116.485 155.535 83.652  1.00 45.99 ? 79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 115.290 155.103 82.824  1.00 49.45 ? 79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 114.145 155.396 83.230  1.00 47.31 ? 79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 115.494 154.471 81.766  1.00 51.71 ? 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 116.784 153.306 87.311  1.00 34.57 ? 80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 117.640 152.241 87.828  1.00 34.97 ? 80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.858 150.938 87.946  1.00 40.30 ? 80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 117.348 149.862 87.574  1.00 41.55 ? 80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 118.257 152.659 89.175  1.00 35.63 ? 80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 118.904 151.466 89.858  1.00 37.11 ? 80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 119.269 153.773 88.969  1.00 34.56 ? 80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 115.630 151.012 88.462  1.00 39.64 ? 81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.817 149.808 88.602  1.00 36.51 ? 81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 114.477 149.211 87.242  1.00 39.64 ? 81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 114.468 147.986 87.078  1.00 40.42 ? 81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 113.548 150.120 89.393  1.00 35.84 ? 81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 113.714 149.973 90.878  1.00 34.75 ? 81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 114.308 150.975 91.624  1.00 38.47 ? 81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 113.282 148.830 91.526  1.00 35.09 ? 81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 114.464 150.842 92.989  1.00 39.49 ? 81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 113.434 148.693 92.891  1.00 37.04 ? 81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 114.027 149.699 93.623  1.00 36.38 ? 81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 114.190 150.061 86.254  1.00 38.74 ? 82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.952 149.571 84.901  1.00 37.68 ? 82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 115.199 148.911 84.331  1.00 39.14 ? 82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 115.110 147.896 83.630  1.00 41.98 ? 82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 113.490 150.719 84.003  1.00 40.82 ? 82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 113.389 150.358 82.532  1.00 43.26 ? 82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 114.152 151.349 81.669  1.00 43.55 ? 82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 115.653 151.139 81.778  1.00 44.55 ? 82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 116.134 150.063 80.868  1.00 42.89 ? 82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 116.372 149.477 84.617  1.00 38.75 ? 83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 117.618 148.855 84.186  1.00 38.79 ? 83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.779 147.471 84.800  1.00 38.81 ? 83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 118.211 146.530 84.125  1.00 38.66 ? 83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.805 149.745 84.554  1.00 37.57 ? 83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 118.736 150.969 83.811  1.00 42.51 ? 83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 120.115 149.044 84.241  1.00 37.00 ? 83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 117.440 147.329 86.082  1.00 34.23 ? 84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 117.537 146.022 86.723  1.00 34.01 ? 84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.607 145.010 86.063  1.00 31.30 ? 84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.989 143.855 85.845  1.00 35.96 ? 84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 117.228 146.141 88.214  1.00 37.65 ? 84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 115.381 145.424 85.740  1.00 43.37 ? 85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 114.403 144.526 85.139  1.00 39.12 ? 85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 114.593 144.347 83.639  1.00 39.81 ? 85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 114.011 143.419 83.067  1.00 43.97 ? 85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.986 145.033 85.417  1.00 34.41 ? 85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 112.499 144.749 86.819  1.00 37.78 ? 85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.846 143.562 87.120  1.00 35.98 ? 85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 112.696 145.665 87.841  1.00 41.78 ? 85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.400 143.298 88.399  1.00 38.93 ? 85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 112.255 145.411 89.122  1.00 40.65 ? 85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.608 144.225 89.397  1.00 40.90 ? 85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 111.168 143.970 90.674  1.00 39.07 ? 85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 115.385 145.201 82.989  1.00 41.18 ? 86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 115.584 145.083 81.550  1.00 37.49 ? 86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 116.297 143.795 81.164  1.00 41.22 ? 86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 116.128 143.324 80.034  1.00 40.95 ? 86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 116.370 146.285 81.025  1.00 38.40 ? 86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 117.087 143.217 82.070  1.00 42.93 ? 87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.830 142.007 81.747  1.00 40.77 ? 87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.939 140.775 81.662  1.00 40.22 ? 87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.329 139.789 81.028  1.00 41.69 ? 87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.933 141.776 82.782  1.00 38.11 ? 87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.467 140.354 82.806  1.00 39.12 ? 87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.767 140.257 83.576  1.00 40.10 ? 87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 121.788 139.434 82.812  1.00 42.23 ? 87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.144 140.059 81.510  1.00 35.91 ? 87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.755 140.810 82.269  1.00 39.98 ? 88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.892 139.632 82.343  1.00 41.24 ? 88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.630 138.465 82.991  1.00 40.43 ? 88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.561 137.325 82.528  1.00 44.88 ? 88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.364 139.244 80.961  1.00 40.78 ? 88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 113.051 139.909 80.586  1.00 42.80 ? 88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 113.284 141.188 79.801  1.00 43.97 ? 88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 114.329 140.986 78.717  1.00 45.87 ? 88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 114.288 142.068 77.695  1.00 44.82 ? 88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.351 138.758 84.071  1.00 35.31 ? 89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 117.161 137.747 84.734  1.00 33.90 ? 89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 116.302 136.572 85.178  1.00 36.85 ? 89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.221 136.753 85.746  1.00 38.49 ? 89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.882 138.358 85.936  1.00 32.94 ? 89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.484 137.341 86.861  1.00 32.95 ? 89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.762 136.860 86.643  1.00 31.02 ? 89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.770 136.861 87.944  1.00 34.33 ? 89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.316 135.922 87.490  1.00 33.46 ? 89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.318 135.923 88.792  1.00 32.16 ? 89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.593 135.454 88.565  1.00 31.03 ? 89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.791 135.362 84.921  1.00 40.85 ? 90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 116.122 134.137 85.332  1.00 36.91 ? 90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 117.093 133.289 86.136  1.00 34.22 ? 90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 118.230 133.068 85.706  1.00 41.57 ? 90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.611 133.347 84.123  1.00 41.18 ? 90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.573 134.075 83.293  1.00 38.80 ? 90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 113.276 134.258 84.057  1.00 42.42 ? 90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 112.330 135.081 83.314  1.00 45.45 ? 90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 112.076 136.355 83.579  1.00 46.11 ? 90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.671 136.984 84.579  1.00 44.01 ? 90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.202 137.013 82.824  1.00 43.91 ? 90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.650 132.820 87.291  1.00 35.83 ? 91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.458 131.892 88.067  1.00 36.78 ? 91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.570 130.572 87.313  1.00 40.06 ? 91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.545 129.986 86.944  1.00 39.46 ? 91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.843 131.673 89.447  1.00 34.19 ? 91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 117.102 132.796 90.411  1.00 39.21 ? 91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 118.311 132.889 91.078  1.00 38.81 ? 91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 116.139 133.761 90.646  1.00 39.41 ? 91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.552 133.920 91.964  1.00 34.55 ? 91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 116.375 134.794 91.530  1.00 36.78 ? 91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 117.583 134.874 92.190  1.00 35.61 ? 91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.784 130.071 87.061  1.00 41.81 ? 92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.918 128.864 86.235  1.00 38.91 ? 92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.599 127.575 86.967  1.00 38.07 ? 92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.359 126.556 86.307  1.00 41.26 ? 92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.389 128.903 85.808  1.00 39.48 ? 92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 121.070 129.559 86.964  1.00 38.34 ? 92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 120.090 130.565 87.532  1.00 38.09 ? 92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.587 127.584 88.296  1.00 36.08 ? 93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.339 126.383 89.076  1.00 38.07 ? 93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.451 126.732 90.260  1.00 37.43 ? 93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.369 127.886 90.684  1.00 37.95 ? 93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.647 125.741 89.559  1.00 39.54 ? 93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 120.139 126.391 90.718  1.00 43.18 ? 93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.782 125.708 90.792  1.00 36.79 ? 94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.868 125.926 91.908  1.00 37.11 ? 94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.602 126.449 93.135  1.00 38.67 ? 94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.082 127.308 93.857  1.00 39.59 ? 94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.130 124.631 92.243  1.00 37.19 ? 94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.500 124.632 93.604  1.00 38.80 ? 94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.402 125.430 93.873  1.00 38.16 ? 94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 115.016 123.847 94.620  1.00 38.53 ? 94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.826 125.437 95.127  1.00 37.33 ? 94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.444 123.851 95.874  1.00 41.01 ? 94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.348 124.647 96.128  1.00 36.13 ? 94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.807 125.939 93.394  1.00 36.84 ? 95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.500 126.276 94.633  1.00 34.89 ? 95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.841 127.759 94.704  1.00 40.41 ? 95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.761 128.365 95.776  1.00 40.24 ? 95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.762 125.429 94.778  1.00 40.42 ? 95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.089 125.059 96.213  1.00 40.61 ? 95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.618 124.659 97.175  1.00 55.80 ? 95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.593 122.876 97.021  1.00 43.92 ? 95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.234 128.362 93.582  1.00 32.85 ? 96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.589 129.778 93.597  1.00 27.12 ? 96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.402 130.640 94.015  1.00 31.10 ? 96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.508 131.469 94.931  1.00 35.60 ? 96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 120.107 130.196 92.222  1.00 31.75 ? 96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 119.214 129.797 91.199  1.00 37.38 ? 96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 117.259 130.455 93.352  1.00 35.08 ? 97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 116.070 131.231 93.685  1.00 30.29 ? 97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.587 130.923 95.095  1.00 31.64 ? 97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 115.158 131.826 95.822  1.00 36.51 ? 97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.966 130.958 92.667  1.00 32.63 ? 97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.634 129.651 95.491  1.00 33.15 ? 98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.236 129.282 96.844  1.00 33.97 ? 98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 116.092 130.003 97.876  1.00 35.30 ? 98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.574 130.579 98.838  1.00 42.81 ? 98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.339 127.767 97.015  1.00 37.73 ? 98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 115.118 127.300 98.422  1.00 39.23 ? 98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.837 127.105 98.907  1.00 37.42 ? 98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.192 127.055 99.260  1.00 39.26 ? 98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.632 126.675 100.200 1.00 39.97 ? 98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.992 126.627 100.556 1.00 40.02 ? 98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.711 126.436 101.026 1.00 38.19 ? 98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.411 129.993 97.680  1.00 36.81 ? 99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.310 130.667 98.607  1.00 31.95 ? 99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 118.012 132.156 98.662  1.00 36.41 ? 99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.913 132.741 99.747  1.00 39.69 ? 99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.762 130.424 98.196  1.00 35.08 ? 99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.262 129.016 98.459  1.00 36.81 ? 99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.779 128.501 99.798  1.00 40.26 ? 99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.909 127.854 100.574 1.00 36.36 ? 99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.803 128.126 102.031 1.00 38.62 ? 99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.851 132.790 97.498  1.00 31.30 ? 100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.590 134.224 97.501  1.00 31.04 ? 100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.301 134.545 98.244  1.00 34.51 ? 100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.287 135.383 99.152  1.00 38.12 ? 100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.525 134.777 96.081  1.00 30.06 ? 100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 117.133 136.224 96.033  1.00 32.94 ? 100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 118.022 137.208 96.431  1.00 32.65 ? 100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.862 136.599 95.636  1.00 29.07 ? 100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.660 138.539 96.407  1.00 32.22 ? 100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.494 137.928 95.610  1.00 32.10 ? 100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.394 138.899 95.996  1.00 35.82 ? 100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.210 133.872 97.891  1.00 37.41 ? 101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.907 134.220 98.438  1.00 36.25 ? 101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.665 133.643 99.825  1.00 37.30 ? 101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.618 133.925 100.417 1.00 45.50 ? 101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.805 133.775 97.476  1.00 36.15 ? 101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.766 134.600 96.213  1.00 33.19 ? 101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 112.306 135.908 96.231  1.00 35.00 ? 101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 113.207 134.078 95.006  1.00 36.37 ? 101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 112.274 136.671 95.084  1.00 32.75 ? 101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 113.179 134.834 93.852  1.00 38.45 ? 101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.711 136.130 93.897  1.00 37.51 ? 101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.682 136.887 92.749  1.00 35.01 ? 101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.592 132.848 100.359 1.00 36.84 ? 102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.501 132.411 101.743 1.00 39.77 ? 102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.517 133.066 102.666 1.00 41.82 ? 102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.360 132.972 103.886 1.00 47.87 ? 102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.662 130.886 101.834 1.00 42.05 ? 102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.360 130.181 102.153 1.00 44.84 ? 102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.307 130.811 102.256 1.00 46.50 ? 102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.425 128.868 102.320 1.00 40.40 ? 102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.546 133.720 102.130 1.00 41.33 ? 103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.544 134.363 102.975 1.00 40.20 ? 103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.652 135.864 102.766 1.00 39.91 ? 103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.758 136.607 103.743 1.00 42.50 ? 103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.924 133.727 102.741 1.00 43.32 ? 103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.960 132.255 103.105 1.00 45.08 ? 103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 117.892 131.688 103.414 1.00 42.76 ? 103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.060 131.664 103.083 1.00 45.74 ? 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.627 136.337 101.520 1.00 31.73 ? 104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.927 137.730 101.219 1.00 35.21 ? 104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.722 138.543 100.779 1.00 37.40 ? 104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.697 139.752 101.013 1.00 46.96 ? 104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 119.004 137.811 100.129 1.00 36.58 ? 104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.249 137.021 100.457 1.00 38.85 ? 104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 120.344 135.675 100.130 1.00 34.70 ? 104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 121.326 137.615 101.102 1.00 36.22 ? 104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 121.475 134.944 100.430 1.00 34.04 ? 104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 122.462 136.891 101.406 1.00 36.35 ? 104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.531 135.556 101.069 1.00 37.61 ? 104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.658 134.829 101.368 1.00 40.33 ? 104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.728 137.923 100.150 1.00 37.29 ? 105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.552 138.664 99.718  1.00 38.83 ? 105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.851 139.285 100.919 1.00 41.44 ? 105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.629 138.622 101.936 1.00 42.36 ? 105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.594 137.747 98.959  1.00 33.28 ? 105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.506 140.564 100.800 1.00 40.97 ? 106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.834 141.257 101.890 1.00 40.39 ? 106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.428 140.703 102.076 1.00 45.20 ? 106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.647 140.626 101.123 1.00 40.09 ? 106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.784 142.759 101.616 1.00 43.14 ? 106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 112.159 143.626 102.711 1.00 41.18 ? 106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 113.082 143.723 103.915 1.00 40.23 ? 106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.827 145.009 102.174 1.00 39.44 ? 106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 111.109 140.321 103.307 1.00 51.51 ? 107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.807 139.779 103.655 1.00 47.35 ? 107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 109.157 140.649 104.721 1.00 51.88 ? 107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.841 141.293 105.522 1.00 53.15 ? 107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.920 138.334 104.154 1.00 47.37 ? 107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 110.268 137.327 103.071 1.00 48.02 ? 107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.306 135.913 103.627 1.00 51.38 ? 107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.648 134.901 102.546 1.00 50.36 ? 107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 110.894 133.546 103.113 1.00 47.47 ? 107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.827 140.661 104.723 1.00 56.50 ? 108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 107.086 141.441 105.701 1.00 54.17 ? 108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 107.495 141.047 107.119 1.00 54.39 ? 108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 108.106 140.000 107.352 1.00 54.60 ? 108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.582 141.247 105.512 1.00 55.05 ? 108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 105.272 139.849 105.540 1.00 54.87 ? 108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 105.137 141.831 104.180 1.00 52.43 ? 108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 107.149 141.911 108.078 1.00 57.51 ? 109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 107.551 141.675 109.461 1.00 58.26 ? 109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 107.042 140.335 109.975 1.00 57.97 ? 109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.672 139.727 110.848 1.00 58.16 ? 109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 107.052 142.807 110.358 1.00 57.94 ? 109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 107.428 144.174 109.831 1.00 57.80 ? 109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 107.309 144.444 108.637 1.00 60.60 ? 109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 107.893 145.044 110.718 1.00 58.36 ? 109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.915 139.862 109.453 1.00 60.40 ? 110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.384 138.554 109.807 1.00 60.89 ? 110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 106.020 137.427 109.004 1.00 61.85 ? 110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.676 136.260 109.221 1.00 62.03 ? 110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.863 138.537 109.626 1.00 61.32 ? 110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 103.430 139.080 108.280 1.00 63.42 ? 110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 104.263 139.710 107.596 1.00 62.74 ? 110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 102.253 138.889 107.912 1.00 63.00 ? 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.934 137.747 108.088 1.00 60.15 ? 111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.682 136.746 107.326 1.00 59.76 ? 111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.761 135.841 106.514 1.00 60.20 ? 111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 107.051 134.659 106.319 1.00 61.30 ? 111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.577 135.906 108.243 1.00 57.94 ? 111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.023 136.608 109.519 1.00 58.81 ? 111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.696 137.939 109.227 1.00 60.97 ? 111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 111.207 137.827 109.333 1.00 60.02 ? 111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 111.876 139.148 109.176 1.00 59.34 ? 111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.644 136.387 106.030 1.00 58.23 ? 112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.689 135.616 105.246 1.00 58.33 ? 112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.643 136.005 103.777 1.00 58.77 ? 112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.161 135.212 102.963 1.00 58.01 ? 112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 103.278 135.757 105.833 1.00 58.50 ? 112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.682 137.145 105.668 1.00 60.56 ? 112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 101.172 137.124 105.834 1.00 59.20 ? 112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 100.566 138.483 105.522 1.00 60.12 ? 112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 101.571 139.577 105.632 1.00 59.02 ? 112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 105.126 137.191 103.419 1.00 54.52 ? 113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 105.059 137.682 102.052 1.00 52.89 ? 113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 106.428 138.191 101.622 1.00 51.97 ? 113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 107.279 138.528 102.449 1.00 52.72 ? 113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 104.012 138.795 101.907 1.00 54.23 ? 113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.583 138.291 101.796 1.00 52.37 ? 113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 102.332 137.632 100.451 1.00 53.52 ? 113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.864 137.290 100.268 1.00 54.02 ? 113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.620 136.561 98.994  1.00 53.32 ? 113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.629 138.241 100.310 1.00 49.95 ? 114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.893 138.662 99.719  1.00 49.11 ? 114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.724 140.076 99.183  1.00 46.53 ? 114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.969 140.304 98.231  1.00 46.02 ? 114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 108.341 137.701 98.607  1.00 48.91 ? 114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.719 136.342 99.197  1.00 47.86 ? 114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.505 138.292 97.828  1.00 46.56 ? 114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.805 135.236 98.170  1.00 45.94 ? 114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.432 141.025 99.792  1.00 44.44 ? 115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.392 142.412 99.351  1.00 44.73 ? 115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.403 142.709 98.253  1.00 45.33 ? 115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 109.168 143.601 97.431  1.00 46.89 ? 115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.643 143.349 100.535 1.00 45.97 ? 115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.540 143.443 101.589 1.00 43.44 ? 115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 108.079 144.074 102.858 1.00 41.79 ? 115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.360 144.234 101.054 1.00 43.57 ? 115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.516 141.985 98.221  1.00 43.16 ? 116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.605 142.245 97.291  1.00 39.91 ? 116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.772 141.080 96.328  1.00 39.29 ? 116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.812 139.920 96.750  1.00 43.71 ? 116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.919 142.477 98.040  1.00 39.97 ? 116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 113.294 143.930 98.226  1.00 39.88 ? 116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.518 144.094 99.101  1.00 42.48 ? 116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 115.030 143.072 99.603  1.00 42.74 ? 116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.971 145.241 99.285  1.00 41.82 ? 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.870 141.394 95.041  1.00 39.85 ? 117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.354 140.446 94.053  1.00 38.83 ? 117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.875 140.543 93.976  1.00 41.84 ? 117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.507 141.355 94.655  1.00 45.88 ? 117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.711 140.710 92.692  1.00 39.03 ? 117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 110.193 140.685 92.699  1.00 42.97 ? 117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.672 139.317 93.105  1.00 45.73 ? 117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.722 138.368 92.000  1.00 42.39 ? 117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.664 137.746 91.497  1.00 45.30 ? 117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.450 137.948 91.980  1.00 43.06 ? 117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.830 136.899 90.486  1.00 45.39 ? 117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.481 139.699 93.140  1.00 35.54 ? 118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.919 139.802 92.921  1.00 29.20 ? 118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.279 141.153 92.315  1.00 32.30 ? 118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.249 141.797 92.735  1.00 34.04 ? 118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.391 138.659 92.024  1.00 32.77 ? 118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.889 138.474 91.988  1.00 31.94 ? 118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.607 138.242 93.152  1.00 29.32 ? 118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.584 138.525 90.789  1.00 30.79 ? 118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.974 138.070 93.123  1.00 30.43 ? 118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.951 138.351 90.750  1.00 27.06 ? 118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.641 138.126 91.919  1.00 32.55 ? 118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 122.004 137.955 91.883  1.00 40.53 ? 118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.493 141.605 91.336  1.00 39.97 ? 119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.756 142.893 90.705  1.00 34.12 ? 119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.599 144.040 91.695  1.00 34.96 ? 119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 116.381 144.994 91.669  1.00 41.43 ? 119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.831 143.088 89.505  1.00 33.17 ? 119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.207 142.250 88.296  1.00 32.54 ? 119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.554 140.884 88.306  1.00 38.69 ? 119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.291 140.356 89.407  1.00 41.82 ? 119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.307 140.334 87.213  1.00 40.34 ? 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.592 143.975 92.568  1.00 36.99 ? 120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 114.411 145.036 93.554  1.00 36.79 ? 120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.590 145.104 94.516  1.00 36.14 ? 120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 116.092 146.192 94.821  1.00 36.96 ? 120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 113.106 144.827 94.321  1.00 37.13 ? 120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.913 144.663 93.405  1.00 39.88 ? 120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.669 145.564 92.577  1.00 41.40 ? 120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 111.219 143.631 93.512  1.00 43.96 ? 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 116.044 143.949 95.006  1.00 31.02 ? 121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 117.198 143.924 95.897  1.00 28.88 ? 121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 118.441 144.464 95.202  1.00 31.20 ? 121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 119.200 145.248 95.786  1.00 36.18 ? 121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.436 142.498 96.396  1.00 31.12 ? 121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.709 142.306 97.197  1.00 25.99 ? 121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 118.473 142.577 98.668  1.00 28.01 ? 121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 119.019 143.864 99.080  1.00 36.89 ? 121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.447 144.673 99.960  1.00 31.79 ? 121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 117.289 144.374 100.522 1.00 39.02 ? 121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 119.050 145.814 100.279 1.00 25.87 ? 121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.658 144.065 93.947  1.00 29.83 ? 122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.831 144.535 93.218  1.00 27.00 ? 122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.756 146.040 92.992  1.00 25.91 ? 122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.759 146.748 93.120  1.00 33.48 ? 122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.982 143.767 91.894  1.00 29.29 ? 122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.589 142.387 92.150  1.00 24.59 ? 122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.840 144.552 90.917  1.00 26.32 ? 122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.629 141.510 90.930  1.00 28.71 ? 122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.574 146.553 92.643  1.00 30.25 ? 123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 118.420 147.988 92.432  1.00 28.76 ? 123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.646 148.765 93.721  1.00 30.67 ? 123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 119.270 149.831 93.707  1.00 35.69 ? 123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 117.034 148.291 91.864  1.00 29.06 ? 123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.820 147.605 90.645  1.00 32.21 ? 123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 118.143 148.252 94.844  1.00 25.89 ? 124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 118.358 148.927 96.120  1.00 30.38 ? 124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.840 148.947 96.466  1.00 29.18 ? 124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 120.375 149.969 96.916  1.00 30.48 ? 124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 117.521 148.260 97.226  1.00 37.25 ? 124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 116.046 148.629 97.065  1.00 34.62 ? 124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 118.029 148.664 98.600  1.00 32.25 ? 124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.783 150.117 97.119  1.00 31.86 ? 124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 120.529 147.823 96.258  1.00 24.45 ? 125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.959 147.769 96.550  1.00 23.87 ? 125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.726 148.725 95.644  1.00 22.33 ? 125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.663 149.402 96.081  1.00 28.15 ? 125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 122.476 146.325 96.423  1.00 32.37 ? 125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.981 146.279 96.625  1.00 31.27 ? 125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.774 145.424 97.425  1.00 22.03 ? 125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 122.345 148.793 94.367  1.00 24.26 ? 126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 123.014 149.696 93.437  1.00 21.60 ? 126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.790 151.153 93.818  1.00 26.03 ? 126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.715 151.968 93.739  1.00 34.23 ? 126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 122.530 149.432 92.012  1.00 26.68 ? 126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 121.567 151.504 94.219  1.00 29.34 ? 127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 121.299 152.869 94.661  1.00 27.49 ? 127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 122.092 153.201 95.917  1.00 22.93 ? 127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 122.622 154.309 96.053  1.00 25.67 ? 127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.802 153.058 94.901  1.00 26.33 ? 127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.924 153.082 93.649  1.00 26.66 ? 127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 117.454 152.989 94.018  1.00 32.31 ? 127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 119.194 154.331 92.830  1.00 26.91 ? 127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 122.185 152.250 96.848  1.00 23.26 ? 128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 123.000 152.457 98.039  1.00 25.09 ? 128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 124.461 152.682 97.670  1.00 23.34 ? 128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 125.124 153.560 98.234  1.00 32.48 ? 128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.851 151.259 98.978  1.00 25.42 ? 128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.790 151.279 100.147 1.00 29.14 ? 128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 123.485 152.005 101.285 1.00 29.76 ? 128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.974 150.562 100.115 1.00 30.16 ? 128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 124.346 152.022 102.363 1.00 28.79 ? 128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.838 150.577 101.190 1.00 28.97 ? 128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 125.523 151.306 102.315 1.00 28.30 ? 128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.977 151.901 96.721  1.00 25.63 ? 129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 126.373 152.035 96.314  1.00 20.47 ? 129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 126.630 153.374 95.632  1.00 23.13 ? 129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 127.621 154.051 95.927  1.00 28.77 ? 129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.759 150.883 95.386  1.00 24.00 ? 129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 127.028 149.590 96.098  1.00 22.07 ? 129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 127.422 149.582 97.425  1.00 22.86 ? 129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.891 148.381 95.437  1.00 22.34 ? 129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 127.671 148.393 98.080  1.00 26.57 ? 129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 127.140 147.188 96.088  1.00 22.49 ? 129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 127.530 147.195 97.411  1.00 25.99 ? 129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.746 153.772 94.714  1.00 29.37 ? 130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 126.011 154.941 93.883  1.00 27.31 ? 130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 126.087 156.222 94.702  1.00 34.83 ? 130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.774 157.170 94.305  1.00 40.53 ? 130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.942 155.067 92.799  1.00 28.89 ? 130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 125.394 156.275 95.838  1.00 33.49 ? 131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 125.419 157.449 96.708  1.00 34.89 ? 131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.992 158.709 95.956  1.00 34.70 ? 131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 125.598 159.773 96.094  1.00 39.75 ? 131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 126.801 157.633 97.337  1.00 37.35 ? 131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 126.788 158.596 98.504  1.00 39.60 ? 131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 125.932 158.512 99.384  1.00 36.96 ? 131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 127.741 159.519 98.519  1.00 34.51 ? 131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 123.937 158.589 95.152  1.00 34.98 ? 132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 123.396 159.707 94.411  1.00 35.21 ? 132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 123.737 159.732 92.936  1.00 39.57 ? 132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 123.115 160.499 92.190  1.00 41.56 ? 132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 124.695 158.924 92.491  1.00 40.04 ? 133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 125.098 158.890 91.088  1.00 38.58 ? 133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 124.182 157.929 90.339  1.00 39.99 ? 133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 124.277 156.710 90.510  1.00 45.57 ? 133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 126.560 158.472 90.959  1.00 40.60 ? 133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 127.169 158.883 89.635  1.00 44.02 ? 133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 126.405 159.166 88.689  1.00 43.13 ? 133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 128.413 158.919 89.540  1.00 43.39 ? 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 123.295 158.478 89.507  1.00 39.22 ? 134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 122.340 157.637 88.792  1.00 39.54 ? 134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 123.035 156.747 87.769  1.00 38.53 ? 134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 122.698 155.566 87.638  1.00 41.70 ? 134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 121.281 158.505 88.114  1.00 42.17 ? 134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 120.640 159.326 89.096  1.00 45.64 ? 134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 120.238 157.634 87.433  1.00 40.52 ? 134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.999 157.295 87.027  1.00 42.00 ? 135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 124.750 156.478 86.079  1.00 41.30 ? 135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 125.602 155.442 86.800  1.00 41.99 ? 135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 125.709 154.294 86.353  1.00 46.40 ? 135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 125.615 157.367 85.188  1.00 40.30 ? 135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.856 158.524 84.565  1.00 41.05 ? 135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 123.777 158.059 83.608  1.00 48.39 ? 135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 124.101 157.305 82.667  1.00 48.59 ? 135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 122.604 158.442 83.800  1.00 49.65 ? 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 126.222 155.829 87.916  1.00 30.68 ? 136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.934 154.856 88.737  1.00 30.77 ? 136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.987 153.773 89.236  1.00 33.25 ? 136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 126.345 152.590 89.274  1.00 35.39 ? 136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 127.616 155.562 89.909  1.00 34.75 ? 136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 128.618 154.707 90.663  1.00 30.74 ? 136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.970 154.704 89.974  1.00 34.15 ? 136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 131.056 154.189 90.903  1.00 38.76 ? 136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 132.415 154.393 90.334  1.00 37.35 ? 136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 124.771 154.161 89.629  1.00 31.32 ? 137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 123.793 153.180 90.084  1.00 26.86 ? 137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 123.412 152.221 88.964  1.00 25.22 ? 137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 123.257 151.018 89.195  1.00 28.27 ? 137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 122.556 153.887 90.634  1.00 30.14 ? 137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 123.250 152.735 87.744  1.00 28.96 ? 138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.935 151.863 86.616  1.00 32.28 ? 138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 124.092 150.921 86.309  1.00 32.08 ? 138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.877 149.752 85.966  1.00 36.44 ? 138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 122.575 152.699 85.389  1.00 35.73 ? 138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 121.169 153.272 85.428  1.00 32.89 ? 138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.852 154.053 84.167  1.00 32.21 ? 138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 120.597 155.517 84.480  1.00 37.66 ? 138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 120.682 156.371 83.264  1.00 37.28 ? 138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 125.328 151.411 86.423  1.00 33.92 ? 139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 126.485 150.542 86.237  1.00 28.27 ? 139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 126.518 149.441 87.289  1.00 26.37 ? 139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.813 148.283 86.977  1.00 33.53 ? 139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 127.772 151.364 86.275  1.00 29.26 ? 139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 128.258 151.812 84.908  1.00 32.42 ? 139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.983 153.141 84.952  1.00 42.41 ? 139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 129.753 153.369 85.908  1.00 41.78 ? 139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 128.785 153.959 84.028  1.00 42.28 ? 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 126.212 149.781 88.542  1.00 22.17 ? 140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 126.152 148.767 89.591  1.00 22.02 ? 140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 125.037 147.764 89.323  1.00 22.73 ? 140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 125.195 146.562 89.571  1.00 29.88 ? 140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.955 149.428 90.954  1.00 22.18 ? 140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 127.208 150.046 91.525  1.00 28.54 ? 140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 128.368 149.299 91.678  1.00 29.45 ? 140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 127.230 151.377 91.916  1.00 27.65 ? 140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 129.514 149.861 92.200  1.00 25.69 ? 140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 128.370 151.947 92.439  1.00 24.73 ? 140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 129.509 151.186 92.580  1.00 23.36 ? 140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 130.646 151.755 93.101  1.00 37.72 ? 140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.894 148.245 88.832  1.00 31.82 ? 141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.783 147.354 88.514  1.00 31.16 ? 141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 123.186 146.378 87.421  1.00 22.39 ? 141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.884 145.184 87.495  1.00 28.49 ? 141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 121.538 148.169 88.115  1.00 28.73 ? 141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.618 147.335 87.240  1.00 30.63 ? 141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.804 148.649 89.350  1.00 24.45 ? 141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.863 146.871 86.384  1.00 26.21 ? 142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 124.334 145.981 85.328  1.00 26.02 ? 142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 125.370 144.997 85.857  1.00 28.81 ? 142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 125.369 143.819 85.482  1.00 31.34 ? 142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.906 146.795 84.169  1.00 25.33 ? 142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.827 147.374 83.280  1.00 32.33 ? 142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.800 146.741 83.040  1.00 31.96 ? 142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 124.054 148.584 82.784  1.00 32.46 ? 142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 126.263 145.463 86.732  1.00 26.78 ? 143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 127.294 144.591 87.282  1.00 22.41 ? 143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.687 143.454 88.095  1.00 26.41 ? 143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 127.120 142.302 87.983  1.00 28.39 ? 143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 128.258 145.411 88.141  1.00 24.64 ? 143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 129.546 144.751 88.637  1.00 25.69 ? 143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 130.557 144.643 87.514  1.00 24.50 ? 143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 130.126 145.526 89.807  1.00 24.92 ? 143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.684 143.757 88.920  1.00 28.04 ? 144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 125.119 142.735 89.796  1.00 21.95 ? 144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 124.091 141.865 89.078  1.00 22.60 ? 144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.995 140.664 89.352  1.00 27.35 ? 144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 124.500 143.384 91.034  1.00 21.82 ? 144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 125.522 143.817 92.074  1.00 24.14 ? 144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.804 144.721 93.460  1.00 40.23 ? 144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 124.106 146.139 92.623  1.00 25.78 ? 144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 123.312 142.447 88.164  1.00 22.04 ? 145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 122.328 141.670 87.419  1.00 26.08 ? 145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 123.023 140.726 86.447  1.00 29.52 ? 145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 122.567 139.600 86.220  1.00 31.11 ? 145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 121.335 142.607 86.707  1.00 28.33 ? 145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.966 141.937 86.574  1.00 25.36 ? 145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.861 143.031 85.345  1.00 27.22 ? 145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 119.273 141.698 87.892  1.00 24.83 ? 145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 124.135 141.168 85.856  1.00 26.32 ? 146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.991 140.259 85.106  1.00 22.53 ? 146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.685 139.255 86.012  1.00 20.02 ? 146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 126.255 138.280 85.511  1.00 31.41 ? 146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 126.034 141.048 84.313  1.00 23.96 ? 146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 125.419 141.875 83.203  1.00 27.08 ? 146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 124.290 141.628 82.783  1.00 30.83 ? 146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 126.161 142.864 82.721  1.00 29.05 ? 146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.642 139.470 87.325  1.00 26.01 ? 147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 126.257 138.577 88.300  1.00 18.84 ? 147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.765 138.483 88.099  1.00 21.99 ? 147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 128.377 137.448 88.367  1.00 33.70 ? 147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.612 137.190 88.263  1.00 22.15 ? 147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 124.173 137.188 88.755  1.00 20.62 ? 147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.686 135.810 89.140  1.00 23.70 ? 147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 123.986 134.824 88.470  1.00 34.92 ? 147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 122.931 135.734 90.228  1.00 22.81 ? 147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 128.371 139.569 87.620  1.00 23.14 ? 148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.824 139.658 87.567  1.00 19.09 ? 148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 130.415 139.934 88.942  1.00 17.50 ? 148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 131.497 139.430 89.263  1.00 20.52 ? 148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 130.247 140.749 86.584  1.00 15.83 ? 148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.816 140.495 85.152  1.00 16.21 ? 148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.927 141.733 84.283  1.00 29.63 ? 148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 129.005 142.573 84.321  1.00 32.15 ? 148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.937 141.867 83.562  1.00 34.07 ? 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.722 140.720 89.760  1.00 22.08 ? 149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 130.160 141.051 91.107  1.00 17.98 ? 149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 129.032 140.745 92.078  1.00 19.06 ? 149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.873 141.082 91.815  1.00 25.42 ? 149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.567 142.524 91.210  1.00 16.38 ? 149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.813 142.996 92.624  1.00 18.83 ? 149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.894 142.524 93.355  1.00 14.37 ? 149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.964 143.913 93.227  1.00 16.89 ? 149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 132.123 142.952 94.645  1.00 13.85 ? 149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 130.186 144.346 94.516  1.00 20.78 ? 149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 131.267 143.863 95.221  1.00 17.58 ? 149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 131.493 144.291 96.507  1.00 18.36 ? 149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 129.368 140.099 93.186  1.00 13.82 ? 150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.399 139.786 94.234  1.00 2.91  ? 150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.834 140.426 95.542  1.00 10.80 ? 150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.858 140.013 96.118  1.00 17.70 ? 150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 128.255 138.273 94.400  1.00 8.60  ? 150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.410 137.842 95.589  1.00 17.32 ? 150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 126.004 138.410 95.557  1.00 17.02 ? 150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 125.196 138.049 94.705  1.00 29.99 ? 150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.706 139.301 96.492  1.00 4.33  ? 150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 128.115 141.424 96.050  1.00 21.61 ? 151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 128.437 141.952 97.379  1.00 10.77 ? 151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 128.275 140.870 98.434  1.00 12.20 ? 151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.472 139.947 98.291  1.00 18.95 ? 151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 127.422 143.084 97.574  1.00 9.11  ? 151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.927 143.410 96.204  1.00 16.40 ? 151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.989 142.136 95.425  1.00 19.25 ? 151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 129.058 140.988 99.502  1.00 18.27 ? 152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 129.027 139.978 100.546 1.00 13.17 ? 152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.639 139.905 101.176 1.00 25.07 ? 152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.816 140.815 101.044 1.00 25.53 ? 152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 130.080 140.274 101.613 1.00 18.64 ? 152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.700 141.375 102.417 1.00 25.88 ? 152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 127.383 138.795 101.864 1.00 21.66 ? 153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 126.075 138.580 102.480 1.00 18.45 ? 153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.642 139.738 103.366 1.00 23.18 ? 153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.484 140.170 103.252 1.00 22.84 ? 153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 126.096 137.262 103.267 1.00 25.04 ? 153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 126.187 136.161 102.354 1.00 28.17 ? 153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.835 137.115 104.101 1.00 23.83 ? 153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.488 140.286 104.243 1.00 28.94 ? 154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 126.056 141.460 105.021 1.00 23.17 ? 154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.669 142.645 104.153 1.00 21.05 ? 154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.565 143.183 104.302 1.00 28.46 ? 154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 127.280 141.758 105.898 1.00 18.15 ? 154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.999 140.465 105.990 1.00 18.10 ? 154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.812 139.802 104.664 1.00 20.40 ? 154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 126.547 143.069 103.243 1.00 20.27 ? 155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 126.234 144.210 102.390 1.00 17.95 ? 155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 125.008 143.935 101.529 1.00 21.86 ? 155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 124.112 144.778 101.416 1.00 21.76 ? 155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 127.436 144.555 101.509 1.00 18.71 ? 155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.588 144.775 102.331 1.00 24.76 ? 155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 127.153 145.804 100.690 1.00 14.02 ? 155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.952 142.754 100.912 1.00 24.71 ? 156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.851 142.451 100.005 1.00 21.16 ? 156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.518 142.406 100.741 1.00 25.46 ? 156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 121.514 142.937 100.255 1.00 31.98 ? 156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 124.115 141.127 99.289  1.00 22.97 ? 156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 123.239 140.903 98.092  1.00 25.02 ? 156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 123.242 141.799 97.039  1.00 21.50 ? 156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.411 139.796 98.022  1.00 24.32 ? 156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 122.436 141.596 95.937  1.00 22.52 ? 156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.605 139.588 96.923  1.00 19.36 ? 156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.616 140.489 95.880  1.00 19.98 ? 156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.489 141.775 101.916 1.00 27.84 ? 157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 121.236 141.616 102.645 1.00 25.53 ? 157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.795 142.917 103.305 1.00 28.18 ? 157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.612 143.271 103.258 1.00 36.58 ? 157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.384 140.508 103.688 1.00 30.08 ? 157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.166 140.186 104.554 1.00 31.40 ? 157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 119.435 138.973 104.013 1.00 32.28 ? 157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.585 139.958 105.996 1.00 28.67 ? 157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.728 143.645 103.918 1.00 30.35 ? 158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 121.375 144.775 104.766 1.00 27.14 ? 158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 121.367 146.113 104.040 1.00 26.55 ? 158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.779 147.070 104.552 1.00 34.14 ? 158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 122.340 144.857 105.953 1.00 27.54 ? 158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 122.230 143.661 106.875 1.00 32.01 ? 158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 121.133 143.198 107.181 1.00 34.73 ? 158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 123.371 143.149 107.317 1.00 34.25 ? 158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.988 146.207 102.867 1.00 33.54 ? 159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 122.106 147.497 102.199 1.00 28.33 ? 159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.732 148.111 101.966 1.00 33.48 ? 159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.830 147.463 101.429 1.00 38.30 ? 159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.848 147.339 100.873 1.00 30.01 ? 159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 120.578 149.369 102.373 1.00 41.52 ? 160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 119.337 150.089 102.180 1.00 37.03 ? 160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 118.209 149.720 103.115 1.00 37.91 ? 160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 117.076 150.154 102.886 1.00 40.86 ? 160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 118.474 148.941 104.159 1.00 40.22 ? 161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 117.443 148.479 105.080 1.00 41.75 ? 161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 117.566 149.212 106.408 1.00 41.16 ? 161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 118.669 149.344 106.949 1.00 44.06 ? 161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 117.541 146.968 105.302 1.00 35.72 ? 161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 117.187 146.137 104.084 1.00 33.73 ? 161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.896 144.698 104.469 1.00 37.32 ? 161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.732 143.844 103.299 1.00 42.28 ? 161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.566 142.530 103.347 1.00 43.35 ? 161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.512 141.882 104.499 1.00 42.61 ? 161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.452 141.848 102.211 1.00 40.13 ? 161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 116.432 149.685 106.929 1.00 48.78 ? 162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 116.443 150.383 108.211 1.00 50.61 ? 162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.844 149.449 109.346 1.00 48.94 ? 162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.681 149.802 110.185 1.00 50.65 ? 162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 115.070 151.000 108.478 1.00 48.62 ? 162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 115.092 152.193 109.416 1.00 48.84 ? 162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.777 152.950 109.362 1.00 50.73 ? 162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.872 154.155 108.440 1.00 49.89 ? 162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 112.614 154.369 107.673 1.00 51.21 ? 162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 116.261 148.252 109.386 1.00 47.82 ? 163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 116.616 147.251 110.384 1.00 48.14 ? 163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 117.996 146.653 110.147 1.00 52.78 ? 163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 118.506 145.941 111.018 1.00 52.32 ? 163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 115.559 146.141 110.400 1.00 50.01 ? 163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 115.445 145.372 111.710 1.00 52.31 ? 163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 116.470 144.252 111.806 1.00 52.82 ? 163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 116.722 143.629 110.513 1.00 52.65 ? 163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 117.922 143.278 110.071 1.00 54.50 ? 163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 119.010 143.472 110.800 1.00 52.21 ? 163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 118.034 142.720 108.869 1.00 52.96 ? 163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 118.610 146.944 109.001 1.00 52.20 ? 164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.879 146.335 108.626 1.00 45.55 ? 164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.899 146.414 109.753 1.00 46.04 ? 164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.945 147.388 110.509 1.00 49.82 ? 164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 120.435 147.030 107.382 1.00 46.78 ? 164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 121.250 148.281 107.685 1.00 40.97 ? 164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 122.036 148.739 106.466 1.00 47.97 ? 164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 122.963 149.824 106.767 1.00 48.06 ? 164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 123.952 149.748 107.647 1.00 48.66 ? 164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 124.168 148.651 108.352 1.00 46.43 ? 164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 124.746 150.800 107.823 1.00 46.01 ? 164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.717 145.371 109.859 1.00 43.15 ? 165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.893 145.398 110.697 1.00 40.03 ? 165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 124.068 146.012 109.959 1.00 41.98 ? 165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.927 146.644 108.911 1.00 41.83 ? 165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 125.255 145.811 110.523 1.00 38.08 ? 166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 126.460 146.341 109.903 1.00 34.16 ? 166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.729 145.648 108.572 1.00 34.67 ? 166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 126.555 144.434 108.436 1.00 36.22 ? 166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.659 146.172 110.833 1.00 31.63 ? 166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.679 147.141 112.001 1.00 37.16 ? 166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 127.530 148.585 111.564 1.00 41.47 ? 166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.880 148.899 110.407 1.00 44.48 ? 166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 127.063 149.408 112.379 1.00 36.82 ? 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 127.150 146.435 107.581 1.00 26.17 ? 167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 127.516 145.880 106.286 1.00 21.40 ? 167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.854 145.156 106.324 1.00 28.61 ? 167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 129.129 144.338 105.439 1.00 26.45 ? 167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.551 146.986 105.231 1.00 22.39 ? 167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 126.222 147.694 104.960 1.00 25.66 ? 167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 126.162 148.190 103.527 1.00 25.14 ? 167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 125.051 146.774 105.261 1.00 24.98 ? 167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.685 145.438 107.322 1.00 28.00 ? 168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.929 144.718 107.560 1.00 21.08 ? 168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.644 143.597 108.547 1.00 24.86 ? 168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.878 143.776 109.502 1.00 30.29 ? 168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 132.027 145.660 108.089 1.00 24.72 ? 168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 133.316 144.894 108.333 1.00 24.42 ? 168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 132.256 146.805 107.115 1.00 30.28 ? 168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 131.253 142.436 108.320 1.00 25.77 ? 169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.997 141.266 109.146 1.00 21.85 ? 169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 132.258 140.611 109.690 1.00 16.36 ? 169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 132.152 139.696 110.513 1.00 23.91 ? 169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 130.186 140.229 108.356 1.00 25.12 ? 169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 129.964 139.062 109.126 1.00 32.55 ? 169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 133.440 141.044 109.263 1.00 20.89 ? 170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.702 140.471 109.715 1.00 15.50 ? 170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 135.402 141.476 110.618 1.00 15.65 ? 170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 135.639 142.619 110.213 1.00 19.52 ? 170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.593 140.100 108.529 1.00 21.76 ? 170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.026 138.667 107.583 1.00 51.87 ? 170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.728 141.051 111.836 1.00 18.48 ? 171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 136.388 141.916 112.805 1.00 13.00 ? 171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.544 141.171 113.449 1.00 1.67  ? 171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 137.401 140.007 113.832 1.00 18.41 ? 171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 135.407 142.395 113.880 1.00 16.80 ? 171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 134.211 143.110 113.331 1.00 13.33 ? 171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 134.327 144.392 112.822 1.00 8.43  ? 171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.968 142.501 113.321 1.00 11.33 ? 171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 133.228 145.052 112.316 1.00 9.30  ? 171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.866 143.155 112.814 1.00 9.30  ? 171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.996 144.433 112.312 1.00 9.33  ? 171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.683 141.846 113.567 1.00 15.02 ? 172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.849 141.326 114.267 1.00 8.01  ? 172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 140.205 142.285 115.391 1.00 5.20  ? 172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 140.328 143.492 115.164 1.00 14.37 ? 172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 141.038 141.149 113.319 1.00 10.01 ? 172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.948 140.015 112.297 1.00 2.63  ? 172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.961 140.359 111.195 1.00 8.28  ? 172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 142.316 139.714 111.718 1.00 7.58  ? 172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 140.367 141.752 116.598 1.00 20.17 ? 173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.654 142.554 117.778 1.00 7.81  ? 173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.971 142.114 118.396 1.00 0.13  ? 173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 142.212 140.915 118.569 1.00 17.25 ? 173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.528 142.442 118.810 1.00 14.81 ? 173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 138.100 142.699 118.329 1.00 19.18 ? 173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 137.113 142.491 119.469 1.00 21.83 ? 173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.971 144.096 117.745 1.00 7.96  ? 173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.820 143.084 118.718 1.00 19.13 ? 174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 144.018 142.841 119.507 1.00 19.22 ? 174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.679 143.011 120.982 1.00 13.79 ? 174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 143.036 143.992 121.367 1.00 22.95 ? 174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 145.139 143.799 119.107 1.00 19.12 ? 174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.650 143.617 117.690 1.00 12.28 ? 174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 147.037 143.010 117.647 1.00 21.52 ? 174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.146 141.771 117.738 1.00 31.40 ? 174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 148.018 143.772 117.524 1.00 24.80 ? 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 144.107 142.057 121.802 1.00 15.11 ? 175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.844 142.074 123.236 1.00 16.57 ? 175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 145.162 142.314 123.956 1.00 15.15 ? 175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 146.122 141.552 123.782 1.00 22.59 ? 175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 143.185 140.771 123.710 1.00 17.30 ? 175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.684 140.921 125.139 1.00 8.95  ? 175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 142.052 140.380 122.776 1.00 14.40 ? 175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 145.209 143.369 124.761 1.00 16.81 ? 176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 146.391 143.666 125.551 1.00 17.31 ? 176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 146.362 142.884 126.862 1.00 24.13 ? 176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 145.310 142.449 127.337 1.00 19.69 ? 176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.491 145.166 125.823 1.00 13.84 ? 176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.906 145.686 125.706 1.00 16.03 ? 176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.863 144.914 125.691 1.00 25.03 ? 176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 148.047 147.001 125.622 1.00 14.07 ? 176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.546 142.710 127.450 1.00 26.03 ? 177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.719 141.849 128.620 1.00 21.59 ? 177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 147.374 142.632 129.886 1.00 20.79 ? 177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 148.238 143.080 130.643 1.00 28.07 ? 177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 149.138 141.299 128.669 1.00 12.52 ? 177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.326 140.269 129.763 1.00 22.16 ? 177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.407 139.453 129.978 1.00 23.72 ? 177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.398 140.273 130.400 1.00 26.54 ? 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 146.074 142.789 130.119 1.00 22.22 ? 178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.598 143.459 131.320 1.00 16.63 ? 178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 144.117 143.162 131.495 1.00 17.50 ? 178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.406 142.868 130.532 1.00 27.24 ? 178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.849 144.969 131.258 1.00 15.95 ? 178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.762 145.647 130.659 1.00 20.77 ? 178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.663 143.243 132.748 1.00 22.15 ? 179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 142.253 143.000 133.037 1.00 14.10 ? 179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 141.365 144.027 132.350 1.00 16.79 ? 179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 140.293 143.687 131.838 1.00 21.89 ? 179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 142.013 143.009 134.545 1.00 21.44 ? 179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.586 142.669 134.984 1.00 21.18 ? 179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.265 141.212 134.692 1.00 16.78 ? 179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.382 142.985 136.457 1.00 18.66 ? 179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.787 145.292 132.338 1.00 21.01 ? 180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 141.021 146.317 131.638 1.00 16.97 ? 180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.886 145.973 130.162 1.00 16.44 ? 180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.796 146.061 129.584 1.00 29.16 ? 180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.690 147.680 131.809 1.00 19.64 ? 180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 141.454 148.279 133.178 1.00 18.06 ? 180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 140.537 147.879 133.894 1.00 29.57 ? 180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 142.288 149.239 133.553 1.00 17.19 ? 180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.991 145.561 129.539 1.00 19.89 ? 181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.964 145.220 128.123 1.00 9.81  ? 181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 141.136 143.967 127.867 1.00 15.38 ? 181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 140.438 143.881 126.855 1.00 23.66 ? 181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 143.390 145.051 127.606 1.00 14.61 ? 181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 144.121 146.374 127.486 1.00 28.54 ? 181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.679 147.227 126.690 1.00 23.68 ? 181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 145.136 146.563 128.188 1.00 29.30 ? 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 141.190 142.988 128.772 1.00 16.53 ? 182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 140.398 141.774 128.595 1.00 15.50 ? 182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.909 142.080 128.711 1.00 16.91 ? 182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 138.092 141.574 127.930 1.00 26.13 ? 182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.839 140.699 129.604 1.00 21.71 ? 182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 142.138 140.039 129.141 1.00 14.32 ? 182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.742 139.662 129.794 1.00 18.95 ? 182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.867 139.298 130.233 1.00 16.86 ? 182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.530 142.907 129.687 1.00 21.80 ? 183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 137.133 143.307 129.819 1.00 12.50 ? 183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.670 144.087 128.597 1.00 17.20 ? 183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.564 143.864 128.088 1.00 21.49 ? 183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.945 144.135 131.090 1.00 14.47 ? 183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 136.985 143.315 132.243 1.00 29.38 ? 183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 137.502 145.011 128.112 1.00 19.90 ? 184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 137.145 145.759 126.913 1.00 17.12 ? 184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 137.016 144.836 125.709 1.00 16.10 ? 184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 136.143 145.033 124.860 1.00 25.00 ? 184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 138.177 146.853 126.647 1.00 14.11 ? 184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 137.798 147.780 125.512 1.00 22.46 ? 184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.399 148.329 125.706 1.00 18.83 ? 184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 136.332 149.251 126.832 1.00 27.26 ? 184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 135.297 150.036 127.097 1.00 30.15 ? 184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.204 150.014 126.353 1.00 21.33 ? 184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 135.361 150.864 128.135 1.00 24.47 ? 184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.884 143.829 125.613 1.00 20.72 ? 185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.797 142.875 124.514 1.00 17.33 ? 185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 136.502 142.081 124.578 1.00 22.17 ? 185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.853 141.863 123.552 1.00 25.69 ? 185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 139.002 141.937 124.536 1.00 10.98 ? 185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 136.115 141.635 125.774 1.00 16.78 ? 186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.848 140.921 125.922 1.00 13.99 ? 186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.688 141.817 125.505 1.00 14.20 ? 186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.785 141.400 124.766 1.00 20.87 ? 186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.680 140.419 127.367 1.00 22.90 ? 186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.623 139.249 127.646 1.00 21.76 ? 186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 133.237 140.014 127.630 1.00 17.35 ? 186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.850 138.992 129.117 1.00 18.47 ? 186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.704 143.069 125.966 1.00 21.72 ? 187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.633 144.000 125.632 1.00 12.41 ? 187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 132.557 144.237 124.129 1.00 22.18 ? 187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 131.471 144.229 123.541 1.00 22.42 ? 187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.838 145.320 126.375 1.00 14.31 ? 187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.966 146.437 125.832 1.00 28.20 ? 187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.746 146.221 125.675 1.00 33.73 ? 187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.502 147.532 125.565 1.00 31.72 ? 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.708 144.451 123.489 1.00 19.20 ? 188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.729 144.737 122.059 1.00 14.95 ? 188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 133.312 143.510 121.261 1.00 17.40 ? 188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.628 143.623 120.240 1.00 24.57 ? 188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 135.120 145.242 121.635 1.00 20.96 ? 188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 135.442 146.563 122.334 1.00 19.72 ? 188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 135.190 145.402 120.126 1.00 16.78 ? 188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.859 147.039 122.120 1.00 14.56 ? 188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.723 142.321 121.704 1.00 16.77 ? 189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 133.297 141.099 121.036 1.00 11.88 ? 189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.787 140.943 121.106 1.00 18.36 ? 189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 131.145 140.603 120.107 1.00 23.10 ? 189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.990 139.890 121.661 1.00 14.70 ? 189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 135.397 140.027 121.618 1.00 26.80 ? 189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 131.199 141.189 122.279 1.00 23.28 ? 190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.746 141.109 122.395 1.00 15.47 ? 190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 129.066 142.167 121.534 1.00 14.64 ? 190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 128.045 141.895 120.894 1.00 24.52 ? 190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 129.328 141.245 123.859 1.00 18.04 ? 190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 129.636 140.019 124.702 1.00 21.51 ? 190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.773 140.015 126.282 1.00 31.52 ? 190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 129.285 141.597 126.946 1.00 23.05 ? 190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.627 143.377 121.495 1.00 19.73 ? 191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 129.040 144.445 120.693 1.00 14.63 ? 191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 129.067 144.104 119.208 1.00 19.24 ? 191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 128.095 144.358 118.487 1.00 24.70 ? 191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.782 145.757 120.949 1.00 17.25 ? 191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 129.639 146.301 122.359 1.00 18.81 ? 191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 128.252 146.840 122.642 1.00 21.53 ? 191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.486 147.126 121.723 1.00 24.01 ? 191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 127.923 146.986 123.918 1.00 17.88 ? 191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 130.175 143.536 118.731 1.00 22.40 ? 192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 130.306 143.223 117.313 1.00 12.07 ? 192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 129.497 141.990 116.933 1.00 20.22 ? 192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.929 141.935 115.837 1.00 27.28 ? 192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.779 143.034 116.953 1.00 17.80 ? 192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.638 144.299 116.998 1.00 16.27 ? 192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 134.113 143.956 116.902 1.00 16.26 ? 192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 132.235 145.267 115.897 1.00 12.37 ? 192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 129.433 140.991 117.816 1.00 14.29 ? 193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.558 139.851 117.571 1.00 17.27 ? 193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 127.102 140.287 117.528 1.00 27.53 ? 193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 126.322 139.798 116.704 1.00 34.38 ? 193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.768 138.785 118.644 1.00 21.56 ? 193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 130.065 138.224 118.558 1.00 35.11 ? 193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.719 141.213 118.410 1.00 24.70 ? 194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 125.374 141.774 118.368 1.00 23.74 ? 194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 125.055 142.322 116.984 1.00 24.84 ? 194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.914 142.233 116.518 1.00 30.70 ? 194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 125.242 142.865 119.433 1.00 22.38 ? 194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.966 143.675 119.362 1.00 22.18 ? 194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.993 144.804 120.378 1.00 27.87 ? 194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.668 145.547 120.427 1.00 29.10 ? 194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.679 146.615 121.463 1.00 27.13 ? 194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 126.055 142.887 116.310 1.00 26.31 ? 195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.893 143.365 114.944 1.00 24.51 ? 195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.913 142.241 113.917 1.00 21.78 ? 195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 125.679 142.503 112.734 1.00 29.53 ? 195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.987 144.383 114.615 1.00 26.92 ? 195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 127.001 145.639 115.486 1.00 31.21 ? 195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 128.207 146.507 115.162 1.00 22.94 ? 195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.708 146.419 115.313 1.00 24.81 ? 195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 126.191 141.008 114.335 1.00 24.13 ? 196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 126.193 139.871 113.442 1.00 20.02 ? 196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 127.516 139.562 112.778 1.00 26.63 ? 196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.583 138.616 111.983 1.00 30.27 ? 196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 128.568 140.320 113.074 1.00 23.62 ? 197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.865 140.089 112.464 1.00 17.26 ? 197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.705 139.102 113.259 1.00 17.42 ? 197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 130.659 139.070 114.486 1.00 22.64 ? 197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 131.469 138.289 112.534 1.00 12.64 ? 198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 132.405 137.391 113.184 1.00 6.08  ? 198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.582 138.159 113.759 1.00 9.69  ? 198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 134.124 139.071 113.133 1.00 18.78 ? 198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.975 137.786 114.973 1.00 12.61 ? 199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 135.015 138.487 115.714 1.00 8.78  ? 199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 136.165 137.527 115.972 1.00 5.93  ? 199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.961 136.433 116.508 1.00 19.57 ? 199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.480 139.064 117.037 1.00 11.11 ? 199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.582 139.807 117.773 1.00 15.89 ? 199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 133.294 139.979 116.773 1.00 6.05  ? 199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 137.370 137.942 115.593 1.00 5.43  ? 200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.588 137.181 115.829 1.00 0.79  ? 200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 139.484 137.970 116.772 1.00 11.34 ? 200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.689 139.173 116.578 1.00 21.76 ? 200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 139.319 136.889 114.517 1.00 6.10  ? 200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 140.289 135.874 114.693 1.00 12.10 ? 200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 140.012 137.297 117.789 1.00 4.10  ? 201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.841 137.928 118.803 1.00 8.50  ? 201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 142.230 137.306 118.802 1.00 6.58  ? 201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 142.382 136.100 118.589 1.00 10.13 ? 201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 140.213 137.793 120.196 1.00 13.43 ? 201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.900 138.541 120.435 1.00 16.60 ? 201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.715 137.599 120.308 1.00 10.05 ? 201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.908 139.218 121.792 1.00 17.75 ? 201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 143.238 138.140 119.034 1.00 10.22 ? 202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.613 137.691 119.200 1.00 5.13  ? 202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.915 137.583 120.689 1.00 14.00 ? 202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.895 138.590 121.404 1.00 22.10 ? 202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.588 138.652 118.522 1.00 2.65  ? 202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.991 138.093 118.438 1.00 7.30  ? 202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 147.191 136.881 118.483 1.00 17.32 ? 202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.972 138.976 118.311 1.00 12.80 ? 202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 145.189 136.366 121.152 1.00 10.42 ? 203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.476 136.112 122.556 1.00 8.77  ? 203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.964 135.945 122.833 1.00 9.89  ? 203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 147.337 135.586 123.953 1.00 19.62 ? 203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.713 134.876 123.031 1.00 15.72 ? 203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 143.196 134.903 122.839 1.00 17.57 ? 203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.538 133.810 123.664 1.00 16.21 ? 203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.628 136.265 123.199 1.00 15.11 ? 203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.821 136.204 121.843 1.00 14.40 ? 204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 149.250 135.967 122.010 1.00 11.50 ? 204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.903 136.947 122.977 1.00 11.38 ? 204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.975 136.645 123.511 1.00 19.83 ? 204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.952 136.030 120.655 1.00 5.83  ? 204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.346 135.149 119.728 1.00 20.47 ? 204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.291 138.108 123.217 1.00 15.38 ? 205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.856 139.064 124.161 1.00 14.55 ? 205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.523 138.733 125.608 1.00 13.03 ? 205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 150.266 139.140 126.506 1.00 20.87 ? 205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.379 140.481 123.838 1.00 14.44 ? 205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 150.053 141.090 122.628 1.00 11.13 ? 205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.573 142.506 122.394 1.00 17.98 ? 205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 150.400 143.194 121.326 1.00 25.05 ? 205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 150.225 142.558 119.994 1.00 22.20 ? 205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.433 138.012 125.855 1.00 17.42 ? 206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 148.111 137.603 127.213 1.00 7.53  ? 206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 149.215 136.714 127.767 1.00 11.02 ? 206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.737 135.838 127.073 1.00 24.19 ? 206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.775 136.862 127.242 1.00 17.65 ? 206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.572 137.589 126.640 1.00 21.51 ? 206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 144.326 136.724 126.734 1.00 19.69 ? 206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.354 138.926 127.324 1.00 22.98 ? 206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.577 136.946 129.024 1.00 23.36 ? 207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.606 136.133 129.651 1.00 18.86 ? 207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 150.094 134.716 129.884 1.00 21.81 ? 207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.892 134.478 130.026 1.00 23.25 ? 207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 151.064 136.760 130.968 1.00 17.60 ? 207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.949 137.063 131.946 1.00 19.45 ? 207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.441 137.968 133.061 1.00 17.01 ? 207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.564 139.352 132.621 1.00 21.57 ? 207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.953 140.354 133.397 1.00 20.67 ? 207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 151.256 140.164 134.670 1.00 24.08 ? 207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 151.034 141.577 132.885 1.00 14.54 ? 207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 151.026 133.769 129.913 1.00 25.28 ? 208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.675 132.365 130.017 1.00 19.75 ? 208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 150.193 132.031 131.428 1.00 26.37 ? 208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 150.367 132.797 132.379 1.00 24.88 ? 208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.868 131.489 129.640 1.00 19.28 ? 208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.566 130.864 131.550 1.00 22.92 ? 209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.128 130.384 132.852 1.00 17.48 ? 209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.327 130.168 133.765 1.00 27.23 ? 209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.363 129.643 133.348 1.00 26.90 ? 209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.337 129.085 132.697 1.00 18.78 ? 209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.874 128.475 134.006 1.00 27.88 ? 209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.642 126.981 133.860 1.00 26.54 ? 209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.698 126.343 132.971 1.00 29.48 ? 209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.603 124.856 132.968 1.00 29.60 ? 209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.182 130.579 135.021 1.00 31.73 ? 210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.262 130.494 135.978 1.00 27.72 ? 210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.195 131.682 136.008 1.00 30.06 ? 210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.302 131.563 136.544 1.00 39.04 ? 210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.792 132.817 135.450 1.00 29.71 ? 211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.592 134.030 135.506 1.00 26.63 ? 211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 152.084 134.945 136.616 1.00 28.52 ? 211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.950 134.829 137.083 1.00 32.35 ? 211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.572 134.753 134.158 1.00 24.91 ? 211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 153.293 133.993 133.055 1.00 21.97 ? 211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.871 134.903 131.991 1.00 26.54 ? 211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 154.907 135.545 132.256 1.00 29.34 ? 211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.299 134.964 130.884 1.00 28.56 ? 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.947 135.866 137.036 1.00 31.84 ? 212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.686 136.687 138.208 1.00 30.36 ? 212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.872 137.924 137.851 1.00 31.54 ? 212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 152.071 138.533 136.796 1.00 30.03 ? 212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 154.000 137.104 138.869 1.00 33.43 ? 212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.949 138.286 138.739 1.00 31.45 ? 213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 150.189 139.527 138.647 1.00 30.07 ? 213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 150.581 140.379 139.845 1.00 32.96 ? 213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 150.298 140.013 140.992 1.00 38.37 ? 213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.675 139.285 138.623 1.00 32.59 ? 213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 148.326 138.134 137.679 1.00 31.87 ? 213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.941 140.554 138.217 1.00 27.26 ? 213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.916 137.622 137.852 1.00 23.86 ? 213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 151.223 141.517 139.585 1.00 33.00 ? 214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.671 142.419 140.643 1.00 34.11 ? 214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.572 141.680 141.635 1.00 38.50 ? 214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 152.257 141.532 142.817 1.00 38.12 ? 214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.477 143.063 141.355 1.00 31.05 ? 214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 149.552 143.850 140.444 1.00 31.09 ? 214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 150.033 145.280 140.257 1.00 33.13 ? 214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 151.260 145.339 139.363 1.00 36.61 ? 214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 151.496 146.711 138.838 1.00 38.60 ? 214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.703 141.197 141.115 1.00 39.12 ? 215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.706 140.471 141.901 1.00 41.55 ? 215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 154.080 139.381 142.770 1.00 42.07 ? 215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.586 139.057 143.847 1.00 44.51 ? 215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 155.555 141.432 142.745 1.00 41.84 ? 215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.758 142.135 143.832 1.00 43.77 ? 215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 154.067 141.454 144.619 1.00 40.93 ? 215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 154.825 143.381 143.896 1.00 44.01 ? 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.977 138.802 142.304 1.00 38.63 ? 216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 152.358 137.643 142.939 1.00 39.53 ? 216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 152.412 136.496 141.940 1.00 39.96 ? 216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.738 136.536 140.904 1.00 44.58 ? 216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.915 137.928 143.380 1.00 35.85 ? 216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 150.112 136.639 143.425 1.00 37.26 ? 216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.906 138.611 144.735 1.00 41.63 ? 216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 153.205 135.477 142.252 1.00 35.17 ? 217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.516 134.420 141.303 1.00 37.98 ? 217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.378 133.409 141.202 1.00 41.03 ? 217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.568 133.247 142.116 1.00 42.61 ? 217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.813 133.711 141.700 1.00 39.61 ? 217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 156.080 134.422 141.245 1.00 41.55 ? 217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.105 135.888 141.635 1.00 42.46 ? 217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 155.411 136.259 142.604 1.00 45.18 ? 217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.813 136.670 140.968 1.00 41.34 ? 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.334 132.722 140.059 1.00 37.75 ? 218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.365 131.655 139.813 1.00 36.17 ? 218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.934 132.146 140.017 1.00 40.00 ? 218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 149.079 131.438 140.553 1.00 44.48 ? 218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.657 130.441 140.696 1.00 39.01 ? 218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 151.460 129.128 139.965 1.00 44.31 ? 218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.240 128.774 139.081 1.00 44.80 ? 218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 150.416 128.396 140.335 1.00 42.91 ? 218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.668 133.374 139.576 1.00 31.28 ? 219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.352 133.985 139.715 1.00 28.79 ? 219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.563 134.011 138.414 1.00 29.32 ? 219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.337 133.868 138.437 1.00 29.01 ? 219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.489 135.412 140.254 1.00 29.12 ? 219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 148.235 134.192 137.281 1.00 30.29 ? 220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.544 134.294 136.004 1.00 24.99 ? 220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.915 132.958 135.624 1.00 28.23 ? 220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.476 131.891 135.884 1.00 27.57 ? 220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.515 134.753 134.915 1.00 24.77 ? 220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 149.034 136.046 135.251 1.00 30.16 ? 220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.819 134.828 133.570 1.00 24.85 ? 220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.737 133.024 135.008 1.00 29.43 ? 221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 145.017 131.836 134.571 1.00 20.76 ? 221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.342 131.434 133.140 1.00 24.22 ? 221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.874 130.385 132.686 1.00 29.08 ? 221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.507 132.051 134.713 1.00 24.24 ? 221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 143.003 131.895 136.132 1.00 29.99 ? 221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.519 131.589 136.165 1.00 28.99 ? 221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.935 131.925 137.522 1.00 30.70 ? 221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.682 133.044 138.156 1.00 27.58 ? 221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 146.130 132.228 132.426 1.00 24.00 ? 222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.491 131.903 131.068 1.00 23.11 ? 222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.436 132.324 130.064 1.00 26.71 ? 222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.438 132.977 130.381 1.00 27.18 ? 222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.677 131.929 128.812 1.00 21.20 ? 223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.769 132.291 127.733 1.00 22.03 ? 223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.490 131.470 127.764 1.00 18.61 ? 223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.508 131.843 127.118 1.00 25.80 ? 223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.466 132.146 126.367 1.00 23.94 ? 223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.772 132.924 126.350 1.00 17.78 ? 223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.703 130.679 126.042 1.00 24.94 ? 223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.465 130.360 128.503 1.00 22.77 ? 224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.279 129.510 128.496 1.00 24.41 ? 224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 141.154 130.109 129.337 1.00 23.56 ? 224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.977 129.943 129.004 1.00 25.09 ? 224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.636 128.089 128.961 1.00 27.50 ? 224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.381 127.249 129.102 1.00 22.48 ? 224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.599 127.448 127.977 1.00 23.60 ? 224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.476 130.817 130.420 1.00 19.62 ? 225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.436 131.518 131.157 1.00 19.68 ? 225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.819 132.645 130.348 1.00 16.24 ? 225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.595 132.821 130.332 1.00 24.88 ? 225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.659 133.418 129.658 1.00 16.42 ? 226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 140.150 134.446 128.758 1.00 21.37 ? 226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 139.328 133.812 127.646 1.00 17.81 ? 226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 138.324 134.375 127.199 1.00 17.93 ? 226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 141.311 135.289 128.198 1.00 20.17 ? 226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.788 136.326 127.220 1.00 16.86 ? 226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 142.073 135.952 129.330 1.00 15.53 ? 226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.746 132.635 127.173 1.00 22.50 ? 227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.983 131.941 126.143 1.00 16.48 ? 227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.621 131.502 126.661 1.00 17.01 ? 227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.633 131.553 125.928 1.00 22.93 ? 227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.765 130.740 125.616 1.00 18.98 ? 227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.943 131.100 124.735 1.00 18.34 ? 227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 142.096 129.731 124.569 1.00 40.30 ? 227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 141.112 128.594 123.600 1.00 20.81 ? 227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.551 131.044 127.912 1.00 19.66 ? 228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 136.256 130.712 128.498 1.00 19.79 ? 228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.370 131.947 128.593 1.00 21.88 ? 228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 134.170 131.890 128.290 1.00 21.96 ? 228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.446 130.084 129.878 1.00 22.37 ? 228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.445 128.568 129.879 1.00 26.01 ? 228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.815 128.025 130.245 1.00 28.98 ? 228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.111 128.240 131.721 1.00 28.91 ? 228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.492 127.815 132.081 1.00 32.43 ? 228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.948 133.076 129.007 1.00 20.01 ? 229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 135.186 134.321 129.048 1.00 13.31 ? 229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.659 134.684 127.665 1.00 17.92 ? 229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.490 135.052 127.507 1.00 19.84 ? 229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 136.054 135.451 129.601 1.00 21.01 ? 229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.599 135.304 131.020 1.00 17.69 ? 229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.775 136.240 131.223 1.00 20.51 ? 229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 135.508 135.588 132.034 1.00 15.64 ? 229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.518 134.588 126.648 1.00 23.65 ? 230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 135.119 134.924 125.285 1.00 16.70 ? 230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 134.057 133.965 124.764 1.00 14.44 ? 230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 133.131 134.379 124.063 1.00 21.19 ? 230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 136.341 134.918 124.367 1.00 18.26 ? 230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 137.400 135.989 124.634 1.00 21.80 ? 230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.678 135.684 123.870 1.00 21.36 ? 230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.870 137.366 124.272 1.00 20.80 ? 230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 134.192 132.676 125.076 1.00 24.38 ? 231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 133.200 131.695 124.658 1.00 21.03 ? 231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.842 132.001 125.270 1.00 23.72 ? 231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.816 131.946 124.584 1.00 26.17 ? 231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.667 130.292 125.044 1.00 23.79 ? 231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.730 129.208 124.554 1.00 34.16 ? 231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.838 128.820 123.373 1.00 36.46 ? 231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.890 128.741 125.349 1.00 33.98 ? 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.816 132.340 126.560 1.00 28.14 ? 232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.555 132.713 127.192 1.00 25.56 ? 232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.988 133.994 126.592 1.00 18.76 ? 232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.774 134.109 126.391 1.00 25.01 ? 232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.745 132.857 128.699 1.00 27.90 ? 232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.134 131.709 129.468 1.00 30.52 ? 232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 130.811 130.736 129.795 1.00 39.33 ? 232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 128.854 131.829 129.789 1.00 28.37 ? 232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.850 134.971 126.305 1.00 22.71 ? 233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.382 136.218 125.708 1.00 13.56 ? 233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.783 135.984 124.326 1.00 22.65 ? 233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.744 136.561 123.985 1.00 26.82 ? 233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.528 137.225 125.635 1.00 17.00 ? 233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.428 135.146 123.514 1.00 25.06 ? 234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.913 134.857 122.180 1.00 18.95 ? 234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.640 134.026 122.250 1.00 21.86 ? 234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.743 134.181 121.414 1.00 27.40 ? 234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.980 134.143 121.350 1.00 19.45 ? 234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 132.028 135.062 120.794 1.00 17.62 ? 234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.678 136.101 119.952 1.00 21.11 ? 234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 133.362 134.894 121.120 1.00 21.98 ? 234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.638 136.951 119.440 1.00 14.86 ? 234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 134.326 135.741 120.611 1.00 23.66 ? 234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.962 136.771 119.770 1.00 19.45 ? 234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.545 133.135 123.238 1.00 29.93 ? 235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 127.316 132.384 123.447 1.00 21.52 ? 235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 126.165 133.298 123.842 1.00 26.13 ? 235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 125.032 133.097 123.394 1.00 36.77 ? 235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.546 131.316 124.514 1.00 26.29 ? 235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.551 130.176 124.505 1.00 33.68 ? 235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.395 129.588 125.900 1.00 34.66 ? 235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.673 129.420 126.586 1.00 38.36 ? 235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.743 128.828 126.071 1.00 37.30 ? 235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 128.727 128.301 124.859 1.00 32.83 ? 235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.857 128.761 126.794 1.00 29.60 ? 235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.434 134.303 124.677 1.00 23.31 ? 236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.378 135.213 125.105 1.00 23.28 ? 236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.901 136.092 123.955 1.00 26.10 ? 236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.693 136.265 123.759 1.00 28.46 ? 236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.872 136.066 126.273 1.00 21.62 ? 236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.895 137.128 126.712 1.00 27.39 ? 236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.804 136.809 127.508 1.00 21.08 ? 236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 125.063 138.452 126.332 1.00 27.32 ? 236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.910 137.775 127.909 1.00 17.22 ? 236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 124.174 139.424 126.729 1.00 20.26 ? 236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 123.100 139.081 127.519 1.00 20.03 ? 236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 122.213 140.049 127.918 1.00 29.04 ? 236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.831 136.654 123.182 1.00 32.91 ? 237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.488 137.477 122.022 1.00 31.61 ? 237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 125.324 136.559 120.814 1.00 37.73 ? 237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 126.163 136.498 119.913 1.00 44.18 ? 237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.548 138.545 121.788 1.00 30.27 ? 237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 124.208 135.833 120.804 1.00 48.38 ? 238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.934 134.824 119.790 1.00 49.78 ? 238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 123.189 135.379 118.583 1.00 54.33 ? 238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.837 134.613 117.682 1.00 59.77 ? 238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.142 133.667 120.400 1.00 53.03 ? 238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 124.021 132.486 120.757 1.00 53.55 ? 238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 125.251 132.586 120.572 1.00 51.83 ? 238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 123.483 131.461 121.224 1.00 53.86 ? 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.936 136.684 118.544 1.00 55.66 ? 239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 122.298 137.326 117.397 1.00 58.32 ? 239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 120.910 136.730 117.141 1.00 60.26 ? 239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 120.592 136.251 116.053 1.00 61.25 ? 239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 123.181 137.195 116.154 1.00 55.81 ? 239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 124.636 137.550 116.382 1.00 55.86 ? 239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 125.536 137.050 115.268 1.00 59.30 ? 239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 125.132 136.995 114.107 1.00 59.97 ? 239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 126.764 136.684 115.618 1.00 56.61 ? 239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 120.088 136.771 118.187 1.00 69.07 ? 240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 118.726 136.256 118.216 1.00 72.61 ? 240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.732 134.727 118.285 1.00 72.93 ? 240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.670 134.126 118.436 1.00 72.00 ? 240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 117.890 136.708 117.000 1.00 72.86 ? 240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 116.454 136.194 116.917 1.00 73.56 ? 240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 115.616 135.904 118.489 1.00 77.56 ? 240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 113.911 135.925 117.950 1.00 71.23 ? 240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.891 134.076 118.194 1.00 72.42 ? 241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.960 132.632 118.206 1.00 72.66 ? 241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.815 131.967 116.857 1.00 75.72 ? 241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.152 130.783 116.733 1.00 74.49 ? 241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.329 132.681 115.838 1.00 81.30 ? 242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 119.232 132.090 114.507 1.00 81.24 ? 242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.609 131.702 113.986 1.00 81.16 ? 242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.782 130.623 113.406 1.00 78.78 ? 242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.548 133.065 113.549 1.00 78.99 ? 242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 117.076 133.302 113.849 1.00 80.38 ? 242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 116.398 134.159 112.798 1.00 81.42 ? 242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 117.009 134.530 111.795 1.00 81.05 ? 242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 115.129 134.479 113.023 1.00 81.09 ? 242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.599 132.568 114.186 1.00 74.37 ? 243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.992 132.264 113.886 1.00 71.72 ? 243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.793 132.446 115.164 1.00 71.12 ? 243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.982 133.577 115.623 1.00 70.24 ? 243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.533 133.163 112.771 1.00 71.85 ? 243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 125.047 133.127 112.627 1.00 72.58 ? 243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.460 132.995 111.169 1.00 72.09 ? 243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 126.904 132.868 111.016 1.00 72.54 ? 243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 127.548 132.986 109.863 1.00 71.99 ? 243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 126.905 133.231 108.734 1.00 71.48 ? 243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 128.871 132.852 109.842 1.00 71.10 ? 243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 124.264 131.338 115.732 1.00 64.26 ? 244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.965 131.397 117.006 1.00 63.95 ? 244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 126.210 132.268 116.890 1.00 62.50 ? 244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.874 132.309 115.850 1.00 62.12 ? 244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 125.347 129.991 117.471 1.00 62.31 ? 244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 124.161 129.127 117.874 1.00 62.90 ? 244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.582 127.827 118.532 1.00 63.70 ? 244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.479 127.135 118.050 1.00 61.66 ? 244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 123.936 127.490 119.642 1.00 62.88 ? 244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.518 132.978 117.972 1.00 48.01 ? 245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.677 133.848 117.993 1.00 45.96 ? 245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.955 133.105 117.669 1.00 42.66 ? 245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 129.256 132.076 118.282 1.00 38.57 ? 245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.717 133.619 116.708 1.00 36.22 ? 246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.926 132.966 116.224 1.00 30.55 ? 246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 132.132 133.836 116.544 1.00 28.98 ? 246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 132.178 135.010 116.161 1.00 25.27 ? 246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.839 132.700 114.721 1.00 22.13 ? 246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.943 131.640 114.444 1.00 38.58 ? 246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 133.099 133.258 117.240 1.00 20.26 ? 247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.341 133.947 117.531 1.00 3.36  ? 247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.515 133.012 117.346 1.00 11.84 ? 247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.406 131.798 117.532 1.00 20.16 ? 247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.645 133.593 116.964 1.00 22.65 ? 248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.888 132.859 116.796 1.00 11.23 ? 248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.958 133.471 117.685 1.00 9.84  ? 248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 139.036 134.695 117.828 1.00 18.09 ? 248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.349 132.868 115.335 1.00 2.83  ? 248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.768 132.614 118.296 1.00 15.25 ? 249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.919 133.035 119.080 1.00 9.82  ? 249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 142.178 132.514 118.409 1.00 5.01  ? 249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 142.240 131.344 118.020 1.00 14.33 ? 249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.830 132.527 120.521 1.00 11.29 ? 249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 143.170 133.382 118.263 1.00 8.60  ? 250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.440 133.024 117.654 1.00 2.74  ? 250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.542 133.097 118.699 1.00 11.07 ? 250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.584 134.028 119.507 1.00 9.95  ? 250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.773 133.946 116.479 1.00 6.02  ? 250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 144.086 133.564 115.188 1.00 9.07  ? 250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.745 133.854 114.984 1.00 4.27  ? 250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.776 132.910 114.177 1.00 4.71  ? 250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 142.111 133.509 113.811 1.00 0.00  ? 250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 144.150 132.561 112.997 1.00 6.93  ? 250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.817 132.861 112.822 1.00 0.00  ? 250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.183 132.521 111.650 1.00 7.84  ? 250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.424 132.106 118.684 1.00 14.47 ? 251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.557 132.068 119.592 1.00 9.53  ? 251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.810 131.698 118.818 1.00 7.55  ? 251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.782 130.816 117.956 1.00 20.94 ? 251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.333 131.070 120.732 1.00 18.23 ? 251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 148.285 131.228 121.917 1.00 13.66 ? 251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 148.009 132.532 122.649 1.00 5.11  ? 251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.191 130.041 122.861 1.00 8.21  ? 251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.907 132.379 119.129 1.00 17.45 ? 252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 151.187 132.034 118.533 1.00 11.76 ? 252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.642 130.669 119.028 1.00 14.62 ? 252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.408 130.297 120.181 1.00 17.57 ? 252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 152.233 133.096 118.863 1.00 12.75 ? 252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.380 133.109 117.875 1.00 17.84 ? 252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.288 132.283 117.949 1.00 24.68 ? 252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.342 134.047 116.939 1.00 15.90 ? 252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.292 129.913 118.140 1.00 14.64 ? 253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.762 128.583 118.502 1.00 13.94 ? 253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.838 128.639 119.576 1.00 17.54 ? 253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 154.020 127.666 120.316 1.00 21.09 ? 253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 153.271 127.840 117.253 1.00 18.72 ? 253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.266 126.331 117.496 1.00 11.73 ? 253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.658 128.331 116.863 1.00 10.80 ? 253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 153.066 125.518 116.244 1.00 15.33 ? 253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.552 129.754 119.687 1.00 19.66 ? 254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.598 129.908 120.687 1.00 14.59 ? 254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 155.072 130.430 122.015 1.00 19.65 ? 254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.862 130.641 122.940 1.00 25.26 ? 254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.694 130.836 120.158 1.00 16.72 ? 254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.645 130.164 119.213 1.00 20.70 ? 254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.534 129.208 119.670 1.00 19.29 ? 254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.641 130.477 117.865 1.00 24.20 ? 254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.409 128.584 118.803 1.00 22.11 ? 254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.513 129.855 116.994 1.00 26.72 ? 254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.399 128.907 117.465 1.00 21.56 ? 254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.766 130.648 122.127 1.00 21.33 ? 255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 153.166 130.984 123.406 1.00 15.28 ? 255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 153.219 129.782 124.341 1.00 13.42 ? 255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 153.121 128.629 123.916 1.00 26.25 ? 255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.720 131.436 123.211 1.00 14.01 ? 255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 151.170 132.231 124.354 1.00 12.50 ? 255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.656 131.646 125.490 1.00 11.93 ? 255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 151.035 133.567 124.526 1.00 16.09 ? 255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 150.234 132.586 126.315 1.00 13.60 ? 255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 150.454 133.761 125.755 1.00 10.35 ? 255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.381 130.064 125.633 1.00 22.23 ? 256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.465 128.990 126.617 1.00 15.94 ? 256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.170 128.188 126.672 1.00 17.88 ? 256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.196 126.955 126.747 1.00 21.73 ? 256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.797 129.574 127.989 1.00 20.69 ? 256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.820 128.787 128.769 1.00 22.00 ? 256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 154.232 127.483 129.246 1.00 27.03 ? 256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 152.944 127.671 129.901 1.00 27.03 ? 256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 152.296 126.718 130.556 1.00 28.37 ? 256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.796 125.500 130.676 1.00 25.73 ? 256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 151.117 126.994 131.103 1.00 28.04 ? 256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 151.029 128.871 126.621 1.00 18.26 ? 257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.718 128.245 126.732 1.00 16.32 ? 257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.283 127.526 125.461 1.00 16.93 ? 257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 148.104 127.180 125.344 1.00 19.11 ? 257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.670 129.295 127.108 1.00 20.18 ? 257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.772 129.728 128.555 1.00 25.04 ? 257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.438 129.025 129.343 1.00 28.63 ? 257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 148.186 130.772 128.905 1.00 29.07 ? 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.195 127.290 124.515 1.00 22.17 ? 258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.795 126.732 123.226 1.00 22.87 ? 258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.185 125.346 123.401 1.00 16.21 ? 258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.183 125.010 122.757 1.00 23.27 ? 258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.990 126.710 122.254 1.00 24.80 ? 258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.530 126.285 120.857 1.00 18.01 ? 258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 152.089 125.792 122.767 1.00 16.80 ? 258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.353 127.079 120.335 1.00 4.53  ? 258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.774 124.519 124.264 1.00 23.69 ? 259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.242 123.175 124.468 1.00 19.77 ? 259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.865 123.220 125.118 1.00 20.98 ? 259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.942 122.518 124.690 1.00 26.48 ? 259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.215 122.346 125.305 1.00 23.49 ? 259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.291 121.693 124.464 1.00 26.06 ? 259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 150.998 120.928 123.547 1.00 27.00 ? 259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.546 121.993 124.771 1.00 27.46 ? 259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.705 124.044 126.155 1.00 22.71 ? 260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.386 124.230 126.750 1.00 19.55 ? 260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.429 124.882 125.761 1.00 22.32 ? 260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.233 124.570 125.740 1.00 26.23 ? 260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.496 125.065 128.025 1.00 21.77 ? 260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.698 124.687 128.868 1.00 34.95 ? 260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 148.090 123.502 128.852 1.00 35.74 ? 260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.253 125.576 129.549 1.00 35.96 ? 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.942 125.798 124.937 1.00 29.37 ? 261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 145.116 126.437 123.919 1.00 19.65 ? 261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.538 125.406 122.958 1.00 17.09 ? 261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.364 125.485 122.581 1.00 20.94 ? 261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.950 127.481 123.172 1.00 9.26  ? 261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 145.256 128.101 121.993 1.00 19.56 ? 261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.354 129.136 122.168 1.00 16.56 ? 261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.531 127.671 120.706 1.00 22.12 ? 261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.727 129.717 121.083 1.00 13.63 ? 261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.906 128.248 119.620 1.00 13.12 ? 261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 144.004 129.272 119.810 1.00 16.89 ? 261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.348 124.425 122.558 1.00 22.31 ? 262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.878 123.371 121.667 1.00 18.92 ? 262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.996 122.358 122.386 1.00 27.00 ? 262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.097 121.779 121.766 1.00 25.80 ? 262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 146.068 122.657 121.025 1.00 25.66 ? 262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 147.005 123.517 120.177 1.00 22.95 ? 262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.177 122.689 119.682 1.00 22.20 ? 262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.255 124.146 119.014 1.00 18.08 ? 262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.234 122.128 123.679 1.00 36.79 ? 263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.466 121.133 124.417 1.00 26.23 ? 263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.008 121.534 124.591 1.00 29.36 ? 263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.175 120.673 124.893 1.00 39.48 ? 263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.101 120.886 125.785 1.00 27.46 ? 263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.435 120.182 125.686 1.00 36.58 ? 263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.652 119.459 124.691 1.00 36.42 ? 263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.269 120.353 126.601 1.00 37.70 ? 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.680 122.814 124.412 1.00 31.07 ? 264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.291 123.245 124.514 1.00 30.28 ? 264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.420 122.641 123.422 1.00 32.41 ? 264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.195 122.599 123.574 1.00 34.42 ? 264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.204 124.771 124.455 1.00 30.49 ? 264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.663 125.228 123.177 1.00 28.79 ? 264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 141.053 125.398 125.547 1.00 29.12 ? 264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.020 122.182 122.326 1.00 32.31 ? 265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.281 121.619 121.205 1.00 34.53 ? 265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.282 120.098 121.190 1.00 34.64 ? 265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.702 119.502 120.277 1.00 38.78 ? 265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.848 122.148 119.884 1.00 33.44 ? 265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.395 123.553 119.551 1.00 33.83 ? 265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.883 123.645 119.583 1.00 34.15 ? 265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.414 125.074 119.437 1.00 34.53 ? 265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.964 125.204 119.741 1.00 37.67 ? 265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.915 119.456 122.167 1.00 39.80 ? 266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 139.865 118.005 122.255 1.00 43.62 ? 266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.504 117.553 122.767 1.00 46.69 ? 266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.942 118.147 123.692 1.00 47.18 ? 266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 140.970 117.486 123.174 1.00 40.50 ? 266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.343 117.427 122.533 1.00 42.26 ? 266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.356 116.791 123.469 1.00 46.15 ? 266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 144.646 116.452 122.740 1.00 45.54 ? 266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 145.743 116.100 123.683 1.00 45.99 ? 266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 137.970 116.493 122.157 1.00 51.59 ? 267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 136.696 115.952 122.617 1.00 55.10 ? 267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.831 115.384 124.023 1.00 54.32 ? 267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.902 115.486 124.834 1.00 52.67 ? 267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.173 114.895 121.627 1.00 55.25 ? 267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 137.226 113.810 121.399 1.00 53.82 ? 267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 135.779 115.547 120.311 1.00 54.86 ? 267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 136.989 112.984 120.156 1.00 52.95 ? 267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 137.978 114.781 124.337 1.00 54.54 ? 268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.223 114.244 125.669 1.00 56.26 ? 268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.442 115.330 126.714 1.00 58.15 ? 268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 138.509 115.012 127.906 1.00 58.96 ? 268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.432 113.309 125.640 1.00 59.71 ? 268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.587 113.987 125.177 1.00 58.15 ? 268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.555 116.590 126.302 1.00 60.24 ? 269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.829 117.666 127.244 1.00 58.79 ? 269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.698 117.802 128.257 1.00 60.81 ? 269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 136.526 117.562 127.955 1.00 57.94 ? 269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 139.029 118.987 126.501 1.00 56.63 ? 269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 138.065 118.189 129.476 1.00 65.87 ? 270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.083 118.403 130.528 1.00 66.22 ? 270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.170 119.570 130.169 1.00 67.58 ? 270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.576 120.527 129.504 1.00 68.60 ? 270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.784 118.663 131.862 1.00 66.37 ? 270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.861 119.264 132.904 1.00 69.72 ? 270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.675 118.876 132.947 1.00 69.96 ? 270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 137.323 120.126 133.681 1.00 69.74 ? 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.916 119.482 130.619 1.00 67.22 ? 271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.928 120.489 130.253 1.00 68.55 ? 271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.269 121.867 130.803 1.00 67.53 ? 271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.912 122.873 130.181 1.00 65.95 ? 271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.540 120.061 130.731 1.00 65.80 ? 271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.851 119.089 129.792 1.00 66.11 ? 271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.478 119.729 128.470 1.00 68.50 ? 271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.992 120.879 128.482 1.00 69.16 ? 271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.676 119.085 127.418 1.00 67.17 ? 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 134.947 121.940 131.947 1.00 65.15 ? 272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.372 123.227 132.482 1.00 67.04 ? 272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.481 123.867 131.657 1.00 63.93 ? 272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 136.755 125.058 131.836 1.00 64.01 ? 272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 135.832 123.070 133.934 1.00 67.11 ? 272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 134.671 123.011 134.909 1.00 68.90 ? 272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 133.560 123.447 134.541 1.00 67.26 ? 272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 134.868 122.527 136.044 1.00 66.57 ? 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.118 123.109 130.766 1.00 53.34 ? 273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.124 123.651 129.871 1.00 53.29 ? 273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.627 123.750 128.431 1.00 52.72 ? 273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.159 124.558 127.660 1.00 53.88 ? 273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.420 122.817 129.943 1.00 55.72 ? 273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.043 122.669 128.563 1.00 53.38 ? 273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.404 123.450 130.914 1.00 53.25 ? 273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.620 122.968 128.052 1.00 49.54 ? 274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.128 122.983 126.682 1.00 48.60 ? 274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.559 124.351 126.327 1.00 48.89 ? 274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.875 124.988 127.132 1.00 50.39 ? 274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 135.061 121.904 126.499 1.00 49.61 ? 274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.684 121.631 125.054 1.00 48.02 ? 274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 135.603 120.588 124.437 1.00 48.62 ? 274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.458 120.506 122.988 1.00 51.37 ? 274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.613 121.527 122.155 1.00 49.76 ? 274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 135.928 122.735 122.592 1.00 45.00 ? 274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 135.450 121.330 120.851 1.00 48.59 ? 274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.847 124.801 125.108 1.00 37.65 ? 275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.328 126.057 124.578 1.00 36.21 ? 275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.516 125.701 123.340 1.00 42.73 ? 275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 135.077 125.440 122.269 1.00 44.48 ? 275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 136.443 127.057 124.252 1.00 36.09 ? 275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.857 128.312 123.646 1.00 37.12 ? 275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.238 127.390 125.504 1.00 34.21 ? 275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.189 125.691 123.479 1.00 41.83 ? 276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.336 125.141 122.430 1.00 41.06 ? 276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 132.222 126.077 121.232 1.00 37.01 ? 276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.296 125.629 120.082 1.00 45.04 ? 276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.951 124.834 122.998 1.00 41.69 ? 276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 130.880 123.544 123.799 1.00 41.65 ? 276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.651 123.515 124.693 1.00 41.95 ? 276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 129.610 124.717 125.623 1.00 43.02 ? 276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 130.973 125.213 125.965 1.00 41.03 ? 276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 132.039 127.372 121.473 1.00 33.19 ? 277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.658 128.310 120.425 1.00 31.91 ? 277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.816 129.143 119.894 1.00 34.60 ? 277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.577 130.097 119.147 1.00 36.13 ? 277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.555 129.247 120.932 1.00 35.16 ? 277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 131.148 130.394 121.556 1.00 35.11 ? 277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.670 128.531 121.938 1.00 35.02 ? 277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 134.053 128.821 120.250 1.00 29.37 ? 278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 135.203 129.635 119.879 1.00 22.84 ? 278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 136.121 128.835 118.966 1.00 24.15 ? 278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.698 127.828 119.389 1.00 33.76 ? 278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.956 130.108 121.121 1.00 28.15 ? 278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.830 131.353 120.976 1.00 28.27 ? 278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.968 132.589 120.782 1.00 19.40 ? 278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.731 131.509 122.190 1.00 23.94 ? 278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 136.253 129.283 117.722 1.00 22.79 ? 279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 137.248 128.717 116.825 1.00 9.91  ? 279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.640 129.175 117.240 1.00 13.74 ? 279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.822 130.265 117.786 1.00 24.52 ? 279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.965 129.127 115.381 1.00 15.14 ? 279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.725 128.609 114.938 1.00 25.34 ? 279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.631 128.329 116.981 1.00 18.08 ? 280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 141.002 128.589 117.399 1.00 17.25 ? 280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.912 128.516 116.183 1.00 13.23 ? 280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.815 127.581 115.383 1.00 19.17 ? 280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.469 127.599 118.483 1.00 14.16 ? 280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.423 126.165 117.954 1.00 20.90 ? 280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.624 127.748 119.734 1.00 15.09 ? 280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.334 125.216 118.690 1.00 17.14 ? 280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.783 129.508 116.044 1.00 11.70 ? 281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.821 129.488 115.035 1.00 2.98  ? 281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 145.182 129.618 115.689 1.00 1.52  ? 281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.324 130.236 116.745 1.00 15.42 ? 281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 146.186 129.020 115.057 1.00 20.67 ? 282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.558 129.054 115.545 1.00 10.29 ? 282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.415 129.799 114.533 1.00 4.73  ? 282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.280 129.598 113.322 1.00 4.67  ? 282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 148.114 127.637 115.796 1.00 11.77 ? 282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.549 127.711 116.290 1.00 16.14 ? 282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.243 126.898 116.797 1.00 18.28 ? 282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 149.291 130.663 115.034 1.00 8.24  ? 283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 150.216 131.424 114.205 1.00 7.30  ? 283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.583 130.768 114.317 1.00 8.77  ? 283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 152.159 130.695 115.409 1.00 17.43 ? 283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 150.267 132.900 114.626 1.00 9.04  ? 283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 151.077 133.710 113.628 1.00 7.42  ? 283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.860 133.457 114.763 1.00 6.05  ? 283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 152.103 130.292 113.192 1.00 18.40 ? 284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.313 129.480 113.151 1.00 13.48 ? 284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.390 130.273 112.412 1.00 19.53 ? 284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 154.322 130.410 111.181 1.00 17.56 ? 284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 153.060 128.125 112.479 1.00 10.81 ? 284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.950 127.370 113.212 1.00 18.08 ? 284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.336 127.303 112.439 1.00 13.41 ? 284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.674 125.995 112.654 1.00 17.46 ? 284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.388 130.810 113.107 1.00 22.61 ? 285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.517 131.437 112.414 1.00 24.25 ? 285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.410 130.395 111.758 1.00 23.30 ? 285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.365 129.204 112.072 1.00 25.92 ? 285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 157.262 132.176 113.532 1.00 13.02 ? 285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 156.314 132.201 114.695 1.00 19.84 ? 285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.478 130.975 114.564 1.00 17.57 ? 285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 158.240 130.870 110.827 1.00 24.52 ? 286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 159.178 129.980 110.152 1.00 18.59 ? 286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 160.118 129.302 111.140 1.00 27.79 ? 286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.617 128.205 110.867 1.00 31.34 ? 286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.981 130.755 109.107 1.00 21.56 ? 286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 159.378 130.663 107.722 1.00 33.70 ? 286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 158.197 130.273 107.609 1.00 33.00 ? 286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 160.085 130.980 106.744 1.00 38.28 ? 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.375 129.939 112.285 1.00 27.82 ? 287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 161.280 129.359 113.271 1.00 21.83 ? 287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.769 128.015 113.773 1.00 20.83 ? 287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.549 127.074 113.949 1.00 27.76 ? 287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.477 130.326 114.437 1.00 23.47 ? 287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.606 129.934 115.371 1.00 24.04 ? 287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.890 129.701 114.596 1.00 29.40 ? 287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 165.064 129.468 115.525 1.00 28.82 ? 287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.351 129.418 114.782 1.00 29.89 ? 287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.463 127.908 114.025 1.00 21.04 ? 288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.912 126.646 114.507 1.00 19.62 ? 288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 159.062 125.543 113.467 1.00 25.33 ? 288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.412 124.405 113.801 1.00 30.75 ? 288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.446 126.828 114.891 1.00 21.23 ? 288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.865 125.655 115.620 1.00 21.23 ? 288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.956 125.566 116.998 1.00 22.02 ? 288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 156.231 124.639 114.928 1.00 19.94 ? 288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.423 124.486 117.670 1.00 24.99 ? 288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.697 123.558 115.595 1.00 20.56 ? 288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.793 123.481 116.968 1.00 23.16 ? 288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.789 125.858 112.200 1.00 24.09 ? 289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.939 124.863 111.144 1.00 24.98 ? 289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.396 124.443 111.019 1.00 27.24 ? 289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.703 123.266 110.802 1.00 29.43 ? 289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.386 125.405 109.814 1.00 29.12 ? 289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.449 124.334 108.739 1.00 23.61 ? 289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.963 125.903 109.998 1.00 17.98 ? 289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 161.317 125.399 111.153 1.00 31.13 ? 290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.738 125.070 111.116 1.00 26.58 ? 290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 163.123 124.157 112.273 1.00 32.07 ? 290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.901 123.213 112.098 1.00 39.10 ? 290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.569 126.352 111.143 1.00 29.39 ? 290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 165.062 126.122 111.284 1.00 38.87 ? 290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.800 127.360 111.750 1.00 43.21 ? 290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 165.568 128.444 111.175 1.00 43.15 ? 290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.613 127.249 112.691 1.00 36.98 ? 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.592 124.430 113.467 1.00 25.93 ? 291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.902 123.599 114.625 1.00 25.67 ? 291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.360 122.186 114.453 1.00 29.23 ? 291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 163.031 121.210 114.807 1.00 37.20 ? 291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.338 124.237 115.895 1.00 30.21 ? 291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.911 125.595 116.305 1.00 30.90 ? 291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.086 126.208 117.424 1.00 24.81 ? 291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.366 125.464 116.715 1.00 27.65 ? 291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 161.145 122.057 113.918 1.00 30.57 ? 292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.569 120.732 113.709 1.00 22.63 ? 292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.302 119.977 112.606 1.00 23.61 ? 292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.467 118.755 112.686 1.00 27.40 ? 292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 159.081 120.850 113.386 1.00 25.00 ? 292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.746 120.688 111.568 1.00 32.85 ? 293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.448 120.036 110.468 1.00 33.50 ? 293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.763 119.428 110.935 1.00 36.87 ? 293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.136 118.329 110.506 1.00 41.04 ? 293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.688 121.037 109.339 1.00 31.28 ? 293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.696 120.579 108.305 1.00 33.73 ? 293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.613 121.428 107.051 1.00 38.14 ? 293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 163.998 122.812 107.300 1.00 39.04 ? 293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 163.156 123.836 107.297 1.00 37.39 ? 293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 161.864 123.667 107.068 1.00 31.67 ? 293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 163.621 125.059 107.527 1.00 35.16 ? 293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.481 120.126 111.809 1.00 37.78 ? 294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.739 119.634 112.352 1.00 37.00 ? 294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.548 118.762 113.584 1.00 37.33 ? 294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.539 118.309 114.163 1.00 43.13 ? 294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.661 120.808 112.691 1.00 34.88 ? 294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.807 121.825 111.574 1.00 35.88 ? 294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.948 123.241 112.095 1.00 46.62 ? 294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.745 123.452 113.310 1.00 46.88 ? 294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 167.263 124.143 111.291 1.00 46.27 ? 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.305 118.523 114.000 1.00 34.26 ? 295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 163.996 117.706 115.170 1.00 35.24 ? 295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.587 118.285 116.449 1.00 39.67 ? 295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 164.659 117.597 117.472 1.00 39.11 ? 295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.471 116.262 114.975 1.00 37.98 ? 295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.532 115.250 115.599 1.00 43.02 ? 295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.604 115.664 116.325 1.00 40.66 ? 295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 163.721 114.039 115.361 1.00 40.33 ? 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.012 119.544 116.407 1.00 39.92 ? 296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.588 120.189 117.577 1.00 39.25 ? 296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.524 120.420 118.643 1.00 39.31 ? 296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.345 120.628 118.344 1.00 41.50 ? 296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.229 121.521 117.189 1.00 37.45 ? 296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.469 121.391 116.325 1.00 37.85 ? 296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.029 122.756 115.962 1.00 39.42 ? 296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.281 122.633 115.108 1.00 38.50 ? 296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.677 123.940 114.515 1.00 40.21 ? 296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 164.952 120.375 119.901 1.00 35.70 ? 297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.057 120.706 121.000 1.00 36.32 ? 297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.746 122.197 120.978 1.00 36.78 ? 297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.649 123.029 120.855 1.00 42.72 ? 297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.683 120.311 122.336 1.00 37.50 ? 297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.468 122.534 121.094 1.00 29.21 ? 298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 162.017 123.915 121.060 1.00 29.37 ? 298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.522 124.338 122.436 1.00 28.51 ? 298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.316 123.519 123.333 1.00 32.57 ? 298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.916 124.105 120.011 1.00 29.64 ? 298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.337 125.644 122.592 1.00 26.72 ? 299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.862 126.220 123.838 1.00 27.93 ? 299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.653 127.099 123.569 1.00 28.57 ? 299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.598 127.805 122.558 1.00 34.09 ? 299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.957 127.044 124.528 1.00 26.43 ? 299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 163.131 126.223 125.002 1.00 29.08 ? 299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 164.219 125.991 124.174 1.00 27.39 ? 299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.149 125.678 126.278 1.00 29.78 ? 299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 165.294 125.240 124.603 1.00 29.88 ? 299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.219 124.925 126.716 1.00 33.58 ? 299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 165.289 124.710 125.876 1.00 36.69 ? 299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 166.359 123.961 126.309 1.00 39.80 ? 299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.685 127.042 124.472 1.00 31.06 ? 300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.568 127.975 124.493 1.00 24.84 ? 300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.806 128.948 125.635 1.00 22.95 ? 300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.173 128.546 126.746 1.00 28.79 ? 300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.221 127.246 124.643 1.00 23.88 ? 300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.839 126.575 123.336 1.00 23.03 ? 300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.288 126.230 125.769 1.00 24.43 ? 300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.607 130.230 125.366 1.00 22.94 ? 301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 158.017 131.280 126.282 1.00 19.43 ? 301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.819 131.851 127.023 1.00 23.22 ? 301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.692 131.849 126.522 1.00 26.83 ? 301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.746 132.394 125.530 1.00 18.45 ? 301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.799 131.891 124.589 1.00 17.87 ? 301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 161.090 131.669 125.032 1.00 19.99 ? 301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.495 131.627 123.266 1.00 16.92 ? 301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 162.060 131.200 124.171 1.00 27.38 ? 301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.460 131.157 122.401 1.00 18.48 ? 301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.745 130.944 122.855 1.00 26.27 ? 301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 157.077 132.328 128.236 1.00 26.31 ? 302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 156.077 133.050 129.005 1.00 20.27 ? 302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 156.081 134.498 128.536 1.00 22.18 ? 302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 157.076 135.210 128.721 1.00 24.02 ? 302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.366 132.945 130.502 1.00 22.45 ? 302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 156.128 131.563 131.066 1.00 18.56 ? 302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 157.023 130.530 130.824 1.00 21.59 ? 302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 155.007 131.291 131.836 1.00 20.28 ? 302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.809 129.266 131.335 1.00 20.62 ? 302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.785 130.029 132.352 1.00 24.17 ? 302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.688 129.020 132.098 1.00 27.85 ? 302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.470 127.762 132.610 1.00 32.06 ? 302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.991 134.966 127.922 1.00 21.76 ? 303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 155.039 136.279 127.255 1.00 20.00 ? 303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 155.394 137.429 128.178 1.00 21.87 ? 303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 156.092 138.359 127.755 1.00 29.71 ? 303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.621 136.427 126.684 1.00 19.58 ? 303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 153.093 135.039 126.606 1.00 21.86 ? 303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.683 134.311 127.764 1.00 15.00 ? 303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.935 137.399 129.431 1.00 21.32 ? 304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 155.183 138.532 130.314 1.00 21.76 ? 304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.654 138.650 130.687 1.00 23.88 ? 304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 157.155 139.764 130.859 1.00 30.71 ? 304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 154.325 138.430 131.573 1.00 24.40 ? 304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 154.311 139.684 132.388 1.00 23.67 ? 304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 154.338 139.679 133.765 1.00 29.90 ? 304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 154.284 140.986 132.017 1.00 23.54 ? 304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 154.322 140.923 134.208 1.00 27.67 ? 304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 154.290 141.736 133.167 1.00 29.14 ? 304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 157.362 137.527 130.816 1.00 20.70 ? 305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.796 137.606 131.071 1.00 21.11 ? 305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.516 138.289 129.915 1.00 22.04 ? 305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 160.395 139.131 130.131 1.00 31.28 ? 305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 159.371 136.210 131.313 1.00 22.84 ? 305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 159.358 135.464 130.090 1.00 30.92 ? 305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.551 135.475 132.359 1.00 23.35 ? 305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 159.141 137.954 128.679 1.00 26.16 ? 306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.731 138.611 127.516 1.00 25.10 ? 306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 159.392 140.095 127.513 1.00 22.56 ? 306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 160.250 140.943 127.240 1.00 27.10 ? 306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 159.266 137.921 126.221 1.00 21.72 ? 306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.951 136.562 126.064 1.00 21.27 ? 306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.541 138.806 125.016 1.00 21.73 ? 306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 159.431 135.750 124.905 1.00 24.02 ? 306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 158.135 140.432 127.806 1.00 28.01 ? 307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.726 141.833 127.807 1.00 26.26 ? 307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 158.489 142.632 128.856 1.00 27.25 ? 307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.893 143.774 128.607 1.00 30.25 ? 307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 156.219 141.939 128.041 1.00 21.38 ? 307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.713 143.359 128.123 1.00 26.74 ? 307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 155.479 144.101 126.974 1.00 24.71 ? 307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 155.474 143.960 129.350 1.00 28.34 ? 307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 155.021 145.399 127.045 1.00 26.43 ? 307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 155.017 145.258 129.432 1.00 27.16 ? 307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.791 145.973 128.276 1.00 31.59 ? 307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 154.332 147.267 128.351 1.00 34.08 ? 307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.688 142.052 130.039 1.00 27.54 ? 308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 159.448 142.731 131.081 1.00 27.50 ? 308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.916 142.866 130.699 1.00 27.38 ? 308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 161.533 143.909 130.942 1.00 33.42 ? 308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 159.301 141.983 132.405 1.00 27.28 ? 308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.983 142.243 133.114 1.00 26.79 ? 308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.952 141.597 134.487 1.00 32.68 ? 308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 158.494 140.179 134.440 1.00 35.77 ? 308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 157.401 139.168 134.421 1.00 31.06 ? 308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 161.493 141.823 130.098 1.00 28.15 ? 309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.908 141.863 129.748 1.00 29.71 ? 309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 163.185 142.867 128.636 1.00 34.09 ? 309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 164.213 143.554 128.656 1.00 36.59 ? 309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 163.383 140.469 129.340 1.00 26.11 ? 309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.796 140.434 128.793 1.00 35.09 ? 309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.832 140.787 129.839 1.00 39.96 ? 309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 165.488 140.789 131.039 1.00 37.09 ? 309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.990 141.062 129.462 1.00 41.57 ? 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 162.283 142.971 127.660 1.00 32.87 ? 310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.530 143.772 126.471 1.00 25.52 ? 310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.587 144.953 126.306 1.00 29.46 ? 310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.788 145.752 125.384 1.00 34.95 ? 310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 162.447 142.892 125.215 1.00 27.02 ? 310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 163.450 141.763 125.200 1.00 29.74 ? 310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.724 141.947 124.684 1.00 27.44 ? 310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 163.123 140.513 125.709 1.00 26.49 ? 310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.643 140.919 124.673 1.00 28.34 ? 310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 164.036 139.480 125.703 1.00 27.42 ? 310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 165.294 139.688 125.182 1.00 29.82 ? 310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 166.209 138.662 125.171 1.00 33.31 ? 310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.574 145.094 127.156 1.00 24.55 ? 311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.640 146.189 127.006 1.00 29.06 ? 311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.742 146.099 125.796 1.00 28.29 ? 311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 158.033 147.063 125.496 1.00 35.81 ? 311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.755 144.974 125.086 1.00 27.39 ? 312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.874 144.747 123.952 1.00 26.24 ? 312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 157.290 143.347 124.044 1.00 29.53 ? 312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.872 142.451 124.660 1.00 30.24 ? 312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.606 144.927 122.616 1.00 26.60 ? 312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 160.105 144.728 122.692 1.00 33.29 ? 312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.808 145.121 121.408 1.00 36.07 ? 312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 160.183 145.227 120.354 1.00 35.30 ? 312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 162.116 145.334 121.491 1.00 32.34 ? 312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 156.127 143.171 123.427 1.00 27.72 ? 313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 155.436 141.892 123.475 1.00 21.37 ? 313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 156.169 140.845 122.644 1.00 25.03 ? 313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.869 141.159 121.679 1.00 30.70 ? 313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 154.002 142.049 122.977 1.00 23.52 ? 313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 153.178 142.985 123.804 1.00 25.52 ? 313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.545 142.592 124.963 1.00 25.05 ? 313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.886 144.297 123.641 1.00 26.44 ? 313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.897 143.621 125.478 1.00 24.26 ? 313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 152.088 144.668 124.695 1.00 25.04 ? 313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.997 139.579 123.035 1.00 32.55 ? 314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.628 138.488 122.301 1.00 24.31 ? 314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 156.136 138.435 120.861 1.00 31.07 ? 314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.928 138.237 119.933 1.00 35.42 ? 314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 156.365 137.157 123.004 1.00 17.50 ? 314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 157.184 136.000 122.457 1.00 25.56 ? 314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.387 134.395 122.668 1.00 39.70 ? 314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 155.336 134.721 124.077 1.00 22.66 ? 314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.833 138.613 120.651 1.00 23.27 ? 315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 154.275 138.572 119.306 1.00 28.91 ? 315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.498 139.861 118.527 1.00 23.59 ? 315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 154.126 139.927 117.351 1.00 29.14 ? 315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.782 138.202 119.369 1.00 25.26 ? 315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.859 139.401 119.578 1.00 30.96 ? 315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.326 140.553 119.689 1.00 39.91 ? 315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.631 139.180 119.618 1.00 21.49 ? 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 155.091 140.876 119.146 1.00 25.98 ? 316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 155.511 142.083 118.449 1.00 21.42 ? 316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.949 142.003 117.958 1.00 26.71 ? 316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 157.424 142.944 117.315 1.00 30.21 ? 316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 155.350 143.304 119.360 1.00 26.82 ? 316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 154.620 144.467 118.716 1.00 24.65 ? 316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 153.236 144.092 118.238 1.00 34.40 ? 316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 152.570 143.289 118.922 1.00 39.85 ? 316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 152.816 144.597 117.176 1.00 32.45 ? 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.647 140.909 118.244 1.00 34.07 ? 317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 159.045 140.730 117.890 1.00 32.63 ? 317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 159.185 139.688 116.789 1.00 32.10 ? 317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 158.269 138.908 116.517 1.00 35.92 ? 317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.865 140.305 119.113 1.00 31.06 ? 317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 160.371 141.458 119.957 1.00 31.36 ? 317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.472 141.039 121.705 1.00 42.35 ? 317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.882 142.024 122.194 1.00 32.40 ? 317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 160.354 139.684 116.154 1.00 34.35 ? 318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.671 138.695 115.130 1.00 32.66 ? 318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 161.218 137.447 115.811 1.00 31.89 ? 318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 162.333 137.458 116.340 1.00 30.17 ? 318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.675 139.261 114.130 1.00 34.08 ? 318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.829 138.386 112.901 1.00 38.56 ? 318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.806 137.868 112.406 1.00 37.65 ? 318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.972 138.218 112.427 1.00 40.46 ? 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.433 136.368 115.802 1.00 31.18 ? 319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.873 135.142 116.458 1.00 29.53 ? 319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 162.080 134.533 115.759 1.00 25.58 ? 319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.928 133.924 116.417 1.00 31.73 ? 319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.726 134.134 116.521 1.00 25.73 ? 319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 160.116 132.788 117.109 1.00 34.42 ? 319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.560 132.862 118.856 1.00 38.25 ? 319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 159.223 133.851 119.518 1.00 28.62 ? 319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 162.188 134.701 114.440 1.00 34.53 ? 320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 163.335 134.157 113.724 1.00 32.41 ? 320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.628 134.849 114.133 1.00 36.54 ? 320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.715 134.295 113.939 1.00 35.83 ? 320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 163.116 134.277 112.217 1.00 32.63 ? 320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.740 133.804 111.791 1.00 35.05 ? 320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 161.367 132.655 112.021 1.00 33.69 ? 320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 160.978 134.693 111.167 1.00 36.81 ? 320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.532 136.052 114.695 1.00 36.14 ? 321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.694 136.772 115.197 1.00 33.78 ? 321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.801 136.759 116.714 1.00 34.37 ? 321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.899 136.944 117.247 1.00 38.65 ? 321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.665 138.227 114.717 1.00 34.83 ? 321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 166.824 139.067 115.228 1.00 38.53 ? 321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 166.388 140.441 115.702 1.00 45.02 ? 321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 165.308 140.905 115.279 1.00 41.40 ? 321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 167.126 141.055 116.500 1.00 42.94 ? 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.692 136.541 117.419 1.00 30.41 ? 322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.660 136.668 118.868 1.00 29.22 ? 322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.572 135.337 119.601 1.00 30.27 ? 322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.662 135.327 120.831 1.00 37.10 ? 322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.478 137.550 119.292 1.00 30.12 ? 322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.767 139.041 119.262 1.00 31.21 ? 322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 165.496 139.435 119.577 1.00 44.25 ? 322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 165.414 139.972 121.283 1.00 32.76 ? 322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.395 134.220 118.892 1.00 27.14 ? 323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 164.225 132.940 119.572 1.00 27.14 ? 323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.484 132.550 120.337 1.00 31.08 ? 323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.413 132.126 121.497 1.00 28.39 ? 323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.847 131.858 118.560 1.00 29.95 ? 323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.758 130.470 119.150 1.00 25.55 ? 323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.596 130.031 119.767 1.00 21.39 ? 323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.835 129.598 119.086 1.00 22.93 ? 323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.511 128.765 120.307 1.00 21.37 ? 323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.759 128.332 119.621 1.00 24.34 ? 323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.595 127.920 120.231 1.00 24.93 ? 323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.520 126.656 120.765 1.00 28.14 ? 323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.649 132.687 119.702 1.00 33.24 ? 324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.894 132.326 120.370 1.00 29.56 ? 324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 168.171 133.245 121.552 1.00 33.54 ? 324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.643 132.792 122.600 1.00 37.17 ? 324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 169.050 132.356 119.372 1.00 34.78 ? 324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 169.134 131.089 118.544 1.00 40.95 ? 324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.637 130.042 119.007 1.00 38.13 ? 324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 169.697 131.138 117.430 1.00 43.01 ? 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.887 134.540 121.402 1.00 34.44 ? 325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 168.066 135.466 122.515 1.00 30.60 ? 325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 167.145 135.116 123.676 1.00 31.45 ? 325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.557 135.163 124.841 1.00 35.11 ? 325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.828 136.900 122.045 1.00 33.36 ? 325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.660 137.295 120.837 1.00 30.85 ? 325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.626 138.794 120.602 1.00 33.53 ? 325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 169.374 139.170 119.335 1.00 35.25 ? 325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 170.555 140.030 119.620 1.00 33.33 ? 325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.891 134.767 123.382 1.00 30.52 ? 326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.974 134.352 124.438 1.00 28.34 ? 326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.478 133.099 125.138 1.00 28.20 ? 326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 165.431 133.003 126.369 1.00 35.69 ? 326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.579 134.108 123.861 1.00 26.88 ? 326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.934 135.333 123.283 1.00 30.62 ? 326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 163.333 136.599 123.675 1.00 31.76 ? 326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.922 135.217 122.346 1.00 30.28 ? 326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.737 137.724 123.141 1.00 27.25 ? 326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 161.323 136.338 121.810 1.00 31.62 ? 326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.731 137.593 122.208 1.00 29.38 ? 326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.963 132.125 124.366 1.00 35.53 ? 327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.444 130.879 124.957 1.00 32.17 ? 327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.660 131.138 125.836 1.00 34.08 ? 327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.795 130.562 126.922 1.00 42.68 ? 327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.748 129.848 123.855 1.00 33.81 ? 327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.274 128.560 124.465 1.00 38.30 ? 327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.506 129.581 123.022 1.00 27.14 ? 327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.564 132.006 125.383 1.00 32.69 ? 328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.794 132.290 126.112 1.00 31.55 ? 328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.607 133.297 127.239 1.00 37.68 ? 328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 170.545 133.511 128.014 1.00 43.72 ? 328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.866 132.804 125.148 1.00 33.69 ? 328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 171.312 131.748 124.159 1.00 42.39 ? 328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 171.222 130.547 124.488 1.00 42.93 ? 328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.752 132.120 123.051 1.00 44.94 ? 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.433 133.916 127.352 1.00 35.58 ? 329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 168.208 134.942 128.360 1.00 29.66 ? 329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.640 134.301 129.618 1.00 38.47 ? 329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.509 133.791 129.583 1.00 39.45 ? 329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 167.260 136.009 127.831 1.00 32.94 ? 329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 167.285 137.273 128.663 1.00 36.06 ? 329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 167.519 137.232 129.869 1.00 43.25 ? 329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 167.041 138.408 128.020 1.00 33.20 ? 329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.367 134.297 130.738 1.00 40.94 ? 330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.821 133.686 131.960 1.00 34.05 ? 330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.558 134.359 132.462 1.00 32.70 ? 330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.691 133.682 133.028 1.00 39.56 ? 330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.975 133.824 132.962 1.00 35.18 ? 330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.774 134.974 132.459 1.00 33.93 ? 330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.688 134.906 130.964 1.00 34.65 ? 330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.425 135.673 132.276 1.00 32.52 ? 331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 165.247 136.388 132.752 1.00 34.98 ? 331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.991 136.048 131.962 1.00 36.66 ? 331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.892 136.412 132.393 1.00 35.04 ? 331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.498 137.894 132.704 1.00 38.38 ? 331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.272 138.425 133.896 1.00 34.08 ? 331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.760 139.843 133.647 1.00 36.76 ? 331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.800 139.928 132.627 1.00 40.37 ? 331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.819 139.087 132.496 1.00 41.02 ? 331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.008 138.086 133.340 1.00 42.66 ? 331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 169.679 139.262 131.497 1.00 37.79 ? 331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 164.124 135.373 130.826 1.00 30.98 ? 332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.980 134.915 130.049 1.00 25.80 ? 332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.638 133.499 130.487 1.00 31.94 ? 332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.508 132.622 130.521 1.00 31.83 ? 332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 163.279 134.973 128.542 1.00 28.75 ? 332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 162.200 134.242 127.756 1.00 23.70 ? 332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 163.398 136.415 128.080 1.00 29.02 ? 332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.374 133.274 130.830 1.00 31.11 ? 333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.919 131.963 131.264 1.00 24.27 ? 333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.380 131.176 130.078 1.00 26.16 ? 333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.561 131.677 129.303 1.00 29.65 ? 333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.844 132.089 132.343 1.00 24.08 ? 333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.591 130.803 133.109 1.00 27.87 ? 333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.450 130.959 134.098 1.00 28.76 ? 333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.188 129.661 134.843 1.00 28.51 ? 333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 157.071 129.797 135.817 1.00 36.63 ? 333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.846 129.938 129.946 1.00 29.21 ? 334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.460 129.084 128.835 1.00 26.28 ? 334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.414 127.642 129.315 1.00 31.26 ? 334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 161.101 127.270 130.269 1.00 39.37 ? 334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.436 129.219 127.661 1.00 30.47 ? 334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 162.805 128.616 127.927 1.00 28.31 ? 334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 163.921 129.576 127.561 1.00 26.17 ? 334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.190 130.561 128.684 1.00 28.70 ? 334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.520 131.214 128.556 1.00 29.22 ? 334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.591 126.835 128.650 1.00 29.82 ? 335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.554 125.402 128.894 1.00 28.27 ? 335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.739 124.664 127.578 1.00 27.29 ? 335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.304 125.127 126.520 1.00 31.61 ? 335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 158.248 124.961 129.574 1.00 33.09 ? 335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.989 125.176 128.760 1.00 32.84 ? 335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 155.739 124.803 129.535 1.00 38.85 ? 335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 155.820 124.698 130.776 1.00 35.82 ? 335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 154.676 124.616 128.906 1.00 36.99 ? 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.401 123.515 127.655 1.00 31.33 ? 336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.761 122.762 126.463 1.00 25.70 ? 336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.550 122.044 125.885 1.00 30.06 ? 336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.664 121.595 126.617 1.00 36.10 ? 336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.862 121.753 126.787 1.00 33.64 ? 336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.844 121.522 125.655 1.00 37.70 ? 336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.656 120.260 125.884 1.00 36.04 ? 336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.959 120.567 126.603 1.00 36.55 ? 336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 166.110 120.634 125.662 1.00 36.80 ? 336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.516 121.945 124.556 1.00 32.75 ? 337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.481 121.218 123.834 1.00 28.79 ? 337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.137 120.462 122.687 1.00 30.88 ? 337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.297 120.691 122.342 1.00 32.89 ? 337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.372 122.146 123.295 1.00 27.88 ? 337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.958 123.151 122.301 1.00 26.31 ? 337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.669 122.858 124.439 1.00 27.97 ? 337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.990 123.578 121.226 1.00 28.92 ? 337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.376 119.543 122.098 1.00 32.84 ? 338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.816 118.847 120.900 1.00 30.64 ? 338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.108 119.455 119.701 1.00 33.74 ? 338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.890 119.272 119.558 1.00 37.29 ? 338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.515 117.353 120.998 1.00 31.47 ? 338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.465 116.514 120.171 1.00 31.89 ? 338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.392 116.500 118.944 1.00 33.11 ? 338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 160.368 115.809 120.842 1.00 33.53 ? 338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.804 120.189 118.830 1.00 31.04 ? 339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.107 120.798 117.685 1.00 27.31 ? 339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.420 119.782 116.790 1.00 25.07 ? 339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.318 120.047 116.294 1.00 29.82 ? 339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.229 121.548 116.952 1.00 31.40 ? 339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.499 120.943 117.449 1.00 31.31 ? 339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.234 120.529 118.856 1.00 29.87 ? 339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.034 118.618 116.572 1.00 30.49 ? 340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.391 117.594 115.755 1.00 25.29 ? 340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.195 116.987 116.476 1.00 27.61 ? 340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.171 116.691 115.851 1.00 36.56 ? 340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.400 116.514 115.371 1.00 25.28 ? 340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.416 116.975 114.347 1.00 25.03 ? 340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.144 115.810 113.710 1.00 26.84 ? 340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.106 116.270 112.718 1.00 29.83 ? 340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.904 115.474 112.021 1.00 33.07 ? 340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.881 114.161 112.180 1.00 31.52 ? 340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.746 116.009 111.142 1.00 28.94 ? 340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.302 116.800 117.792 1.00 27.14 ? 341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.149 116.347 118.562 1.00 27.99 ? 341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.024 117.372 118.509 1.00 28.35 ? 341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.847 117.008 118.421 1.00 32.19 ? 341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.556 116.067 120.008 1.00 35.76 ? 341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.445 114.607 120.412 1.00 30.81 ? 341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.381 113.736 119.591 1.00 33.67 ? 341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.273 112.275 119.997 1.00 38.82 ? 341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 156.370 111.365 118.823 1.00 37.99 ? 341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.366 118.660 118.555 1.00 27.46 ? 342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.346 119.698 118.454 1.00 25.54 ? 342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.695 119.702 117.076 1.00 28.62 ? 342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.479 119.885 116.960 1.00 29.44 ? 342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.956 121.063 118.772 1.00 26.79 ? 342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.977 122.217 118.999 1.00 26.83 ? 342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.839 121.788 119.909 1.00 24.03 ? 342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.702 123.420 119.576 1.00 21.82 ? 342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.486 119.509 116.019 1.00 29.94 ? 343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.916 119.426 114.677 1.00 25.86 ? 343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.987 118.226 114.546 1.00 26.47 ? 343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.910 118.323 113.943 1.00 31.89 ? 343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.034 119.354 113.638 1.00 26.95 ? 343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.515 120.687 113.071 1.00 31.94 ? 343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.627 120.464 112.062 1.00 28.55 ? 343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.359 121.450 112.443 1.00 26.90 ? 343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.391 117.079 115.095 1.00 30.13 ? 344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.532 115.901 115.062 1.00 27.34 ? 344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.250 116.135 115.850 1.00 24.90 ? 344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.171 115.698 115.437 1.00 32.61 ? 344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.288 114.688 115.601 1.00 28.63 ? 344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 153.516 114.320 114.785 1.00 30.54 ? 344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.476 113.434 115.550 1.00 37.92 ? 344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.118 112.994 116.663 1.00 38.38 ? 344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.588 113.181 115.042 1.00 34.64 ? 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.350 116.813 116.994 1.00 21.93 ? 345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.157 117.152 117.762 1.00 23.10 ? 345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.238 118.073 116.972 1.00 26.68 ? 345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.013 117.916 117.004 1.00 28.15 ? 345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.558 117.799 119.087 1.00 26.73 ? 345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.386 118.221 119.955 1.00 24.29 ? 345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.863 118.811 121.270 1.00 28.34 ? 345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.693 119.239 122.139 1.00 32.65 ? 345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.141 119.749 123.462 1.00 30.46 ? 345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.812 119.044 116.260 1.00 33.70 ? 346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.005 119.919 115.417 1.00 26.20 ? 346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.287 119.126 114.335 1.00 24.08 ? 346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.099 119.348 114.077 1.00 26.62 ? 346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.882 121.001 114.786 1.00 24.08 ? 346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.385 122.120 115.697 1.00 24.04 ? 346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.288 123.062 114.921 1.00 25.20 ? 346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.223 122.872 116.315 1.00 28.47 ? 346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 147.996 118.201 113.685 1.00 23.10 ? 347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.371 117.386 112.647 1.00 22.59 ? 347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.254 116.523 113.220 1.00 29.04 ? 347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.179 116.404 112.620 1.00 34.39 ? 347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.420 116.518 111.954 1.00 24.23 ? 347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.491 115.912 114.381 1.00 31.23 ? 348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.464 115.091 115.014 1.00 28.43 ? 348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.240 115.920 115.382 1.00 24.75 ? 348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.101 115.486 115.176 1.00 33.07 ? 348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.042 114.399 116.248 1.00 32.04 ? 348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.003 113.955 117.263 1.00 37.47 ? 348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.548 114.217 118.962 1.00 56.11 ? 348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 144.725 115.758 119.359 1.00 33.90 ? 348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.456 117.118 115.929 1.00 21.09 ? 349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.337 117.977 116.297 1.00 17.55 ? 349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.565 118.435 115.066 1.00 19.53 ? 349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.334 118.531 115.099 1.00 22.80 ? 349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.842 119.178 117.094 1.00 23.66 ? 349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.848 119.814 118.065 1.00 29.22 ? 349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.650 118.926 119.284 1.00 31.70 ? 349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.306 121.205 118.472 1.00 25.30 ? 349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.271 118.727 113.971 1.00 25.18 ? 350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.594 119.148 112.750 1.00 21.90 ? 350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.809 117.998 112.133 1.00 25.50 ? 350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.744 118.211 111.543 1.00 30.93 ? 350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.609 119.710 111.755 1.00 21.04 ? 350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.111 121.101 112.112 1.00 19.63 ? 350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.227 121.556 111.188 1.00 24.23 ? 350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.797 121.620 109.797 1.00 32.56 ? 350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.101 122.618 109.272 1.00 31.40 ? 350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 143.734 123.662 109.997 1.00 19.20 ? 350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.762 122.567 107.988 1.00 24.43 ? 350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.322 116.773 112.250 1.00 30.43 ? 351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.567 115.615 111.783 1.00 26.14 ? 351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.320 115.392 112.630 1.00 31.13 ? 351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 139.236 115.134 112.094 1.00 38.89 ? 351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.451 114.369 111.793 1.00 26.47 ? 351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.773 114.673 111.385 1.00 37.52 ? 351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.452 115.486 113.955 1.00 28.97 ? 352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.314 115.223 114.830 1.00 28.01 ? 352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.239 116.295 114.689 1.00 28.74 ? 352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.055 115.981 114.521 1.00 35.53 ? 352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.780 115.117 116.283 1.00 32.36 ? 352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.945 114.162 116.494 1.00 33.22 ? 352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 141.513 114.232 117.899 1.00 39.75 ? 352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.613 115.348 118.450 1.00 39.07 ? 352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 141.864 113.168 118.452 1.00 42.88 ? 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.628 117.569 114.750 1.00 34.78 ? 353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.672 118.666 114.782 1.00 26.15 ? 353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.856 119.682 113.664 1.00 27.16 ? 353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.035 120.598 113.545 1.00 33.29 ? 353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.745 119.387 116.135 1.00 27.76 ? 353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.018 119.975 116.330 1.00 28.71 ? 353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.896 119.555 112.846 1.00 20.25 ? 354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.173 120.543 111.826 1.00 19.20 ? 354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.907 121.771 112.313 1.00 21.42 ? 354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.227 122.644 111.498 1.00 24.99 ? 354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.182 121.866 113.606 1.00 16.98 ? 355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.899 122.974 114.208 1.00 11.96 ? 355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.322 122.566 114.556 1.00 16.82 ? 355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.639 121.375 114.634 1.00 27.20 ? 355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 140.188 123.463 115.476 1.00 22.11 ? 355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.877 124.162 115.212 1.00 25.86 ? 355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.829 125.321 114.451 1.00 17.32 ? 355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.687 123.664 115.723 1.00 27.95 ? 355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.635 125.962 114.206 1.00 20.44 ? 355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.488 124.301 115.483 1.00 23.54 ? 355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.468 125.449 114.724 1.00 23.46 ? 355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 135.275 126.088 114.480 1.00 30.57 ? 355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.215 123.534 114.770 1.00 19.69 ? 356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 143.012 124.981 114.638 1.00 14.43 ? 356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.247 125.468 113.216 1.00 11.89 ? 356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.795 124.742 112.393 1.00 17.30 ? 356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.054 125.553 115.604 1.00 10.89 ? 356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.189 124.576 115.511 1.00 11.24 ? 356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.543 123.221 115.327 1.00 14.30 ? 356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.842 126.692 112.893 1.00 21.77 ? 357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.332 127.321 111.677 1.00 13.74 ? 357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.838 127.520 111.788 1.00 7.83  ? 357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.372 127.789 112.867 1.00 14.53 ? 357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.645 128.667 111.439 1.00 8.72  ? 357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 141.153 128.675 111.677 1.00 7.28  ? 357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.371 127.571 111.372 1.00 13.76 ? 357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.526 129.794 112.205 1.00 13.63 ? 357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 139.008 127.580 111.584 1.00 12.91 ? 357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 139.164 129.812 112.423 1.00 14.19 ? 357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.410 128.702 112.111 1.00 17.35 ? 357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 137.053 128.718 112.326 1.00 26.80 ? 357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.531 127.372 110.666 1.00 13.94 ? 358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.979 127.528 110.616 1.00 13.42 ? 358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.292 128.802 109.848 1.00 15.14 ? 358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.891 128.953 108.688 1.00 19.31 ? 358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.665 126.315 109.969 1.00 24.00 ? 358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 147.206 125.014 110.631 1.00 15.08 ? 358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 149.177 126.460 110.051 1.00 17.35 ? 358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.650 124.866 112.064 1.00 15.92 ? 358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 148.006 129.716 110.494 1.00 14.53 ? 359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.545 130.903 109.848 1.00 3.56  ? 359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 150.062 130.787 109.819 1.00 13.17 ? 359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.697 130.670 110.872 1.00 13.36 ? 359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 148.121 132.175 110.579 1.00 9.22  ? 359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 149.080 133.332 110.375 1.00 18.45 ? 359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 148.294 134.949 110.380 1.00 32.53 ? 359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.739 136.001 110.418 1.00 2.39  ? 359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.636 130.818 108.622 1.00 10.75 ? 360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 152.087 130.807 108.461 1.00 1.81  ? 360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.549 132.258 108.467 1.00 13.50 ? 360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.444 132.963 107.462 1.00 23.47 ? 360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.483 130.073 107.187 1.00 8.17  ? 360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 152.142 128.611 107.209 1.00 15.69 ? 360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.627 127.789 108.212 1.00 13.48 ? 360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 151.320 128.062 106.241 1.00 8.72  ? 360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 152.308 126.446 108.242 1.00 14.08 ? 360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.998 126.719 106.266 1.00 15.48 ? 360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.493 125.911 107.269 1.00 17.40 ? 360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 153.064 132.702 109.616 1.00 14.29 ? 361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 153.338 134.121 109.818 1.00 5.00  ? 361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 154.374 134.642 108.829 1.00 4.06  ? 361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 154.224 135.741 108.287 1.00 11.39 ? 361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.801 134.356 111.255 1.00 14.61 ? 361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 154.141 135.798 111.575 1.00 17.65 ? 361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.866 136.152 113.019 1.00 22.82 ? 361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 154.357 135.493 113.934 1.00 25.87 ? 361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 153.075 137.196 113.232 1.00 18.69 ? 361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.435 133.871 108.584 1.00 20.62 ? 362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.486 134.339 107.687 1.00 10.72 ? 362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 156.028 134.342 106.235 1.00 11.20 ? 362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.444 135.208 105.459 1.00 18.14 ? 362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.740 133.485 107.856 1.00 18.62 ? 362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 158.496 133.812 109.130 1.00 26.98 ? 362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 158.031 133.415 110.217 1.00 26.50 ? 362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.556 134.466 109.043 1.00 29.52 ? 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 155.179 133.390 105.848 1.00 10.83 ? 363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.589 133.436 104.515 1.00 12.56 ? 363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.749 134.692 104.339 1.00 15.55 ? 363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.743 135.302 103.264 1.00 21.41 ? 363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.742 132.187 104.268 1.00 12.06 ? 363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.579 130.964 103.964 1.00 8.91  ? 363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.707 131.071 103.486 1.00 19.44 ? 363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 154.031 129.791 104.244 1.00 12.12 ? 363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 153.026 135.089 105.387 1.00 13.53 ? 364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 152.191 136.281 105.311 1.00 9.34  ? 364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 153.048 137.540 105.265 1.00 11.03 ? 364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.799 138.446 104.462 1.00 20.71 ? 364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 151.206 136.314 106.493 1.00 4.20  ? 364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 150.334 137.558 106.423 1.00 4.29  ? 364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 150.354 135.056 106.513 1.00 0.00  ? 364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 154.069 137.619 106.116 1.00 16.63 ? 365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.801 138.862 106.313 1.00 7.00  ? 365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.956 139.062 105.343 1.00 11.08 ? 365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 156.482 140.177 105.264 1.00 17.79 ? 365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 155.327 138.939 107.748 1.00 5.65  ? 365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 154.222 139.157 108.756 1.00 6.23  ? 365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 153.401 140.060 108.604 1.00 8.00  ? 365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 154.192 138.330 109.790 1.00 11.93 ? 365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 156.367 138.032 104.604 1.00 17.03 ? 366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 157.415 138.233 103.611 1.00 11.52 ? 366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.902 138.952 102.372 1.00 15.40 ? 366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.706 139.482 101.598 1.00 23.08 ? 366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 158.047 136.896 103.216 1.00 17.58 ? 366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 157.236 136.068 102.235 1.00 18.19 ? 366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.812 134.668 102.106 1.00 20.44 ? 366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 156.724 133.607 102.114 1.00 23.00 ? 366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 155.671 133.877 101.096 1.00 25.28 ? 366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.586 138.984 102.173 1.00 23.51 ? 367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.959 139.731 101.091 1.00 9.42  ? 367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 154.052 140.836 101.603 1.00 9.83  ? 367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 153.408 141.514 100.797 1.00 20.43 ? 367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 154.178 138.797 100.144 1.00 14.14 ? 367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 155.134 137.898 99.380  1.00 12.11 ? 367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 153.176 137.970 100.927 1.00 6.53  ? 367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.982 141.037 102.915 1.00 16.31 ? 368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 153.124 142.068 103.481 1.00 2.49  ? 368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 153.640 143.449 103.098 1.00 15.02 ? 368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.828 143.746 103.253 1.00 23.85 ? 368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 153.065 141.917 104.999 1.00 6.65  ? 368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 152.083 142.828 105.664 1.00 1.87  ? 368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 152.281 143.337 106.929 1.00 13.82 ? 368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.892 143.316 105.245 1.00 1.23  ? 368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 151.256 144.101 107.258 1.00 12.06 ? 368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 150.399 144.106 106.254 1.00 7.17  ? 368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 152.742 144.294 102.590 1.00 12.15 ? 369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 153.129 145.621 102.129 1.00 9.24  ? 369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 153.184 146.651 103.248 1.00 12.23 ? 369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 153.762 147.725 103.052 1.00 12.21 ? 369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 152.164 146.102 101.044 1.00 1.40  ? 369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 152.608 146.354 104.408 1.00 20.76 ? 370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 152.476 147.320 105.490 1.00 11.71 ? 370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 153.177 146.839 106.754 1.00 2.28  ? 370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 152.693 147.039 107.868 1.00 12.93 ? 370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 151.005 147.618 105.769 1.00 5.58  ? 370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 150.309 148.254 104.586 1.00 7.70  ? 370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 150.795 149.230 104.019 1.00 23.31 ? 370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 149.167 147.701 104.204 1.00 9.87  ? 370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 154.336 146.196 106.594 1.00 9.68  ? 371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 155.103 145.775 107.759 1.00 11.08 ? 371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 155.529 146.964 108.608 1.00 10.85 ? 371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.741 146.819 109.817 1.00 21.21 ? 371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 156.326 144.968 107.324 1.00 9.10  ? 371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 156.014 143.502 107.126 1.00 9.16  ? 371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 155.089 142.966 107.734 1.00 10.93 ? 371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 156.786 142.843 106.275 1.00 16.42 ? 371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 155.666 148.143 107.998 1.00 14.48 ? 372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 156.034 149.331 108.760 1.00 9.89  ? 372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.956 149.688 109.775 1.00 13.87 ? 372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 155.263 150.102 110.898 1.00 26.28 ? 372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 156.296 150.502 107.814 1.00 14.30 ? 372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 155.070 150.995 107.110 1.00 21.90 ? 372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 154.320 150.195 106.277 1.00 8.45  ? 372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 154.462 152.204 107.119 1.00 18.03 ? 372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 153.302 150.890 105.801 1.00 10.91 ? 372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 153.367 152.113 106.295 1.00 21.38 ? 372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 153.685 149.548 109.394 1.00 15.79 ? 373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 152.601 149.777 110.343 1.00 14.88 ? 373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 152.613 148.703 111.422 1.00 10.11 ? 373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 152.547 148.998 112.621 1.00 25.47 ? 373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 151.250 149.825 109.610 1.00 16.28 ? 373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 151.255 150.931 108.554 1.00 13.05 ? 373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 150.112 150.021 110.597 1.00 13.26 ? 373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 150.072 150.887 107.619 1.00 9.33  ? 373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 152.694 147.443 111.010 1.00 14.43 ? 374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.816 146.311 111.914 1.00 6.43  ? 374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.884 145.051 111.066 1.00 11.38 ? 374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 152.481 145.048 109.900 1.00 19.25 ? 374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 151.646 146.234 112.899 1.00 12.86 ? 374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.759 145.101 113.740 1.00 17.11 ? 374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 153.401 143.984 111.662 1.00 21.62 ? 375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 153.328 142.681 111.028 1.00 7.63  ? 375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.958 142.059 111.274 1.00 10.67 ? 375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 151.251 142.403 112.224 1.00 18.59 ? 375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 154.427 141.757 111.549 1.00 4.80  ? 375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.828 142.307 111.391 1.00 7.54  ? 375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.633 141.479 110.409 1.00 14.83 ? 375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 158.075 141.946 110.348 1.00 17.19 ? 375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.182 143.424 110.484 1.00 17.81 ? 375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 151.580 141.139 110.392 1.00 4.07  ? 376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 150.327 140.408 110.544 1.00 14.83 ? 376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 150.546 139.336 111.606 1.00 7.14  ? 376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 151.335 138.409 111.413 1.00 22.02 ? 376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.865 139.798 109.216 1.00 7.92  ? 376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 148.541 139.071 109.390 1.00 0.00  ? 376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.752 140.881 108.155 1.00 0.00  ? 376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.852 139.466 112.736 1.00 5.16  ? 377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 150.052 138.571 113.866 1.00 9.42  ? 377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 149.004 137.474 113.967 1.00 7.95  ? 377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 149.262 136.456 114.617 1.00 18.96 ? 377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 150.061 139.363 115.180 1.00 10.68 ? 377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 151.052 140.509 115.222 1.00 9.38  ? 377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 150.438 141.713 115.911 1.00 21.66 ? 377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 151.066 143.008 115.440 1.00 20.05 ? 377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 150.261 144.181 115.868 1.00 20.67 ? 377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.839 137.651 113.356 1.00 7.13  ? 378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.778 136.656 113.427 1.00 7.24  ? 378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.814 136.898 112.273 1.00 9.38  ? 378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.975 137.838 111.490 1.00 13.84 ? 378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 146.071 136.691 114.787 1.00 0.79  ? 378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 145.217 137.910 115.007 1.00 6.65  ? 378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.765 139.179 114.961 1.00 7.64  ? 378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.866 137.782 115.280 1.00 1.31  ? 378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.982 140.295 115.169 1.00 3.48  ? 378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 143.080 138.894 115.484 1.00 3.99  ? 378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.638 140.151 115.435 1.00 10.30 ? 378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.814 136.033 112.170 1.00 0.00  ? 379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.833 136.077 111.097 1.00 4.78  ? 379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.431 136.192 111.694 1.00 5.09  ? 379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 142.260 136.363 112.903 1.00 10.25 ? 379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.972 134.850 110.195 1.00 6.43  ? 379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.340 135.064 108.949 1.00 10.12 ? 379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 141.424 136.102 110.833 1.00 0.00  ? 380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 140.040 136.284 111.233 1.00 0.00  ? 380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 139.358 134.928 111.398 1.00 3.32  ? 380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.995 133.872 111.361 1.00 12.17 ? 380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 139.309 137.163 110.217 1.00 2.88  ? 380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 139.149 136.490 108.873 1.00 6.84  ? 380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 140.096 135.926 108.331 1.00 17.39 ? 380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.942 136.543 108.330 1.00 7.76  ? 380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 138.040 134.957 111.596 1.00 15.33 ? 381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 137.273 133.733 111.784 1.00 8.00  ? 381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 137.221 132.879 110.524 1.00 7.12  ? 381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.954 131.677 110.617 1.00 16.05 ? 381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.856 134.077 112.247 1.00 14.89 ? 381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.849 132.937 112.402 1.00 13.05 ? 381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 135.278 131.975 113.497 1.00 17.61 ? 381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.469 133.492 112.686 1.00 12.16 ? 381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 137.470 133.465 109.355 1.00 12.12 ? 382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.482 132.730 108.098 1.00 0.00  ? 382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.888 132.500 107.560 1.00 5.60  ? 382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 139.040 131.834 106.533 1.00 12.94 ? 382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.637 133.463 107.052 1.00 17.28 ? 382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.896 133.654 107.502 1.00 30.70 ? 382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.911 133.036 108.222 1.00 3.93  ? 383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 141.327 132.777 107.961 1.00 6.81  ? 383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.869 133.439 106.700 1.00 17.81 ? 383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.964 133.067 106.257 1.00 21.39 ? 383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.621 131.276 107.874 1.00 7.53  ? 383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 141.306 130.625 109.090 1.00 32.06 ? 383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 141.166 134.399 106.103 1.00 7.03  ? 384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.666 135.047 104.899 1.00 9.42  ? 384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 142.027 136.514 105.093 1.00 6.00  ? 384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.605 137.114 104.182 1.00 21.79 ? 384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.648 134.914 103.752 1.00 0.00  ? 384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.824 136.156 103.460 1.00 7.53  ? 384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.758 136.418 104.502 1.00 19.90 ? 384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 138.143 137.504 104.465 1.00 17.81 ? 384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 138.521 135.532 105.347 1.00 8.34  ? 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.722 137.102 106.244 1.00 1.82  ? 385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 142.054 138.496 106.512 1.00 2.90  ? 385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 143.445 138.552 107.130 1.00 16.10 ? 385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.681 137.983 108.200 1.00 16.66 ? 385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 141.013 139.151 107.431 1.00 4.72  ? 385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 141.424 140.574 107.764 1.00 10.24 ? 385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.649 139.129 106.776 1.00 0.00  ? 385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 144.367 139.240 106.453 1.00 7.97  ? 386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.762 139.344 106.890 1.00 0.00  ? 386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 146.175 140.810 106.773 1.00 5.13  ? 386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 146.582 141.268 105.703 1.00 15.28 ? 386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.665 138.435 106.068 1.00 3.36  ? 386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 146.281 136.956 106.033 1.00 8.27  ? 386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 147.169 136.206 105.062 1.00 8.33  ? 386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 146.367 136.347 107.423 1.00 0.00  ? 386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 146.076 141.537 107.884 1.00 14.48 ? 387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 146.363 142.962 107.903 1.00 2.49  ? 387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 147.167 143.309 109.146 1.00 9.61  ? 387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 147.147 142.593 110.149 1.00 14.33 ? 387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 145.077 143.796 107.862 1.00 0.00  ? 387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 144.151 143.447 106.717 1.00 0.00  ? 387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.942 144.350 106.660 1.00 7.72  ? 387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.936 145.434 107.240 1.00 19.89 ? 387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.907 143.908 105.961 1.00 9.75  ? 387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.886 144.424 109.059 1.00 8.13  ? 388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 148.607 144.948 110.209 1.00 6.05  ? 388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 147.631 145.450 111.265 1.00 10.83 ? 388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 146.645 146.123 110.954 1.00 23.06 ? 388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 149.541 146.079 109.779 1.00 4.01  ? 388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.914 145.124 112.522 1.00 15.63 ? 389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 147.095 145.556 113.642 1.00 0.00  ? 389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.985 146.155 114.720 1.00 13.98 ? 389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 149.140 145.757 114.888 1.00 21.13 ? 389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 146.277 144.396 114.232 1.00 13.55 ? 389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 147.081 143.245 114.425 1.00 17.08 ? 389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 147.436 147.125 115.444 1.00 19.32 ? 390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 148.108 147.741 116.580 1.00 12.56 ? 390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 147.216 147.584 117.801 1.00 11.21 ? 390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 146.051 147.992 117.779 1.00 24.29 ? 390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 148.413 149.215 116.310 1.00 11.58 ? 390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 149.489 149.431 115.260 1.00 10.90 ? 390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.740 150.895 114.967 1.00 17.06 ? 390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 149.026 151.769 115.456 1.00 31.36 ? 390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.758 151.169 114.162 1.00 17.47 ? 390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.764 146.992 118.863 1.00 15.83 ? 391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.977 146.736 120.061 1.00 16.86 ? 391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 146.594 148.055 120.720 1.00 16.06 ? 391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 147.306 149.063 120.620 1.00 19.15 ? 391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.751 145.830 121.035 1.00 19.54 ? 391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.806 146.630 121.783 1.00 15.01 ? 391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.796 145.148 122.001 1.00 7.30  ? 391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 145.451 148.051 121.397 1.00 21.95 ? 392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.963 149.212 122.123 1.00 14.67 ? 392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 145.330 149.099 123.596 1.00 22.52 ? 392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.550 148.004 124.119 1.00 28.47 ? 392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 143.448 149.355 121.975 1.00 16.16 ? 392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 143.080 149.513 120.617 1.00 23.92 ? 392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 145.398 150.245 124.261 1.00 22.99 ? 393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.689 150.318 125.689 1.00 20.74 ? 393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 144.454 150.876 126.384 1.00 21.33 ? 393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 144.300 152.093 126.518 1.00 23.79 ? 393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.919 151.179 125.956 1.00 26.23 ? 393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 147.171 151.285 127.345 1.00 29.03 ? 393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 143.576 149.981 126.826 1.00 24.40 ? 394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 142.370 150.366 127.547 1.00 23.04 ? 394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.724 150.503 129.023 1.00 23.25 ? 394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 143.038 149.513 129.691 1.00 26.60 ? 394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 141.261 149.344 127.320 1.00 19.37 ? 394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.816 149.279 125.879 1.00 24.16 ? 394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 140.053 150.294 125.321 1.00 17.87 ? 394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 141.175 148.210 125.069 1.00 20.10 ? 394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 139.651 150.242 124.004 1.00 20.32 ? 394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 140.778 148.150 123.751 1.00 18.67 ? 394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 140.016 149.168 123.223 1.00 26.76 ? 394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 139.619 149.111 121.908 1.00 32.78 ? 394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 142.683 151.731 129.523 1.00 25.83 ? 395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 143.121 152.060 130.866 1.00 29.00 ? 395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.931 152.081 131.824 1.00 26.44 ? 395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.817 151.671 131.483 1.00 26.81 ? 395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.867 153.395 130.848 1.00 30.37 ? 395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.978 154.433 130.421 1.00 32.71 ? 395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 145.044 153.327 129.892 1.00 28.05 ? 395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 142.168 152.557 133.042 1.00 31.54 ? 396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 141.123 152.622 134.049 1.00 31.54 ? 396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 140.063 153.647 133.659 1.00 28.16 ? 396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 140.283 154.525 132.822 1.00 35.50 ? 396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 141.712 152.985 135.412 1.00 27.95 ? 396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 142.663 151.931 135.935 1.00 34.85 ? 396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 142.310 150.735 135.895 1.00 36.98 ? 396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 143.765 152.301 136.392 1.00 40.08 ? 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.893 153.520 134.279 1.00 28.45 ? 397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 137.848 154.516 134.098 1.00 27.80 ? 397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 138.367 155.892 134.496 1.00 32.55 ? 397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 139.104 156.037 135.475 1.00 38.66 ? 397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 136.617 154.155 134.931 1.00 31.38 ? 397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 135.338 154.797 134.446 1.00 30.56 ? 397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 134.521 154.155 133.526 1.00 30.51 ? 397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.951 156.050 134.904 1.00 26.46 ? 397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 133.354 154.738 133.081 1.00 24.97 ? 397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 133.786 156.641 134.463 1.00 28.75 ? 397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.991 155.980 133.553 1.00 27.24 ? 397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 131.829 156.565 133.110 1.00 36.56 ? 397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 137.979 156.905 133.728 1.00 35.84 ? 398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.421 158.290 133.866 1.00 40.14 ? 398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.822 158.487 133.301 1.00 42.08 ? 398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 140.304 159.626 133.273 1.00 44.94 ? 398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.396 158.785 135.321 1.00 38.45 ? 398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 136.998 158.808 135.906 1.00 45.01 ? 398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 136.090 159.367 135.256 1.00 44.45 ? 398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 136.808 158.268 137.016 1.00 47.36 ? 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.492 157.429 132.855 1.00 40.94 ? 399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.785 157.532 132.194 1.00 34.67 ? 399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 141.585 157.417 130.689 1.00 38.63 ? 399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 140.811 156.572 130.225 1.00 41.58 ? 399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.741 156.445 132.684 1.00 34.73 ? 399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 143.796 156.932 133.660 1.00 38.74 ? 399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 144.952 155.960 133.796 1.00 45.84 ? 399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.907 155.099 134.699 1.00 44.50 ? 399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 145.907 156.056 132.996 1.00 46.70 ? 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 142.272 158.270 129.934 1.00 39.04 ? 400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 142.176 158.218 128.482 1.00 34.05 ? 400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 142.720 156.895 127.958 1.00 34.81 ? 400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.752 156.401 128.419 1.00 31.67 ? 400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 142.941 159.383 127.853 1.00 33.64 ? 400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 142.159 160.685 127.791 1.00 38.20 ? 400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.663 160.463 127.696 1.00 44.87 ? 400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 140.160 160.249 126.574 1.00 43.14 ? 400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 139.988 160.505 128.746 1.00 45.42 ? 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 142.016 156.322 126.988 1.00 31.72 ? 401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 142.445 155.089 126.348 1.00 25.80 ? 401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 143.380 155.391 125.185 1.00 25.58 ? 401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 143.282 156.437 124.538 1.00 28.01 ? 401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 141.242 154.288 125.848 1.00 22.94 ? 401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 140.434 153.682 126.976 1.00 29.01 ? 401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 141.028 153.339 128.018 1.00 28.66 ? 401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 139.204 153.544 126.817 1.00 30.86 ? 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 144.295 154.461 124.927 1.00 30.01 ? 402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 145.211 154.545 123.792 1.00 24.91 ? 402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 144.664 153.633 122.700 1.00 22.14 ? 402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.979 152.442 122.654 1.00 28.63 ? 402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 146.626 154.151 124.200 1.00 26.08 ? 402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 147.326 155.174 125.075 1.00 27.99 ? 402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 148.012 154.544 126.272 1.00 39.47 ? 402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 147.339 154.337 127.303 1.00 38.05 ? 402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 149.225 154.258 126.180 1.00 40.37 ? 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.846 154.197 121.821 1.00 22.07 ? 403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 143.169 153.412 120.797 1.00 22.67 ? 403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 144.169 153.030 119.716 1.00 23.60 ? 403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.854 153.890 119.151 1.00 26.02 ? 403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.985 154.193 120.207 1.00 18.54 ? 403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 141.023 154.619 121.320 1.00 21.77 ? 403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 141.264 153.356 119.164 1.00 13.00 ? 403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 140.630 153.497 122.254 1.00 21.95 ? 403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 144.258 151.740 119.432 1.00 21.16 ? 404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 145.123 151.215 118.393 1.00 3.41  ? 404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 144.381 151.019 117.089 1.00 14.72 ? 404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 143.461 151.773 116.754 1.00 28.63 ? 404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.787 149.998 116.341 1.00 22.00 ? 405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 144.168 149.659 115.067 1.00 5.36  ? 405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 143.644 148.234 115.140 1.00 7.03  ? 405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 144.418 147.294 115.348 1.00 10.10 ? 405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 145.165 149.809 113.915 1.00 12.69 ? 405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 145.709 151.215 113.652 1.00 15.33 ? 405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.779 151.184 112.576 1.00 16.24 ? 405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 144.589 152.170 113.273 1.00 13.02 ? 405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 142.335 148.078 114.974 1.00 16.96 ? 406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 141.706 146.773 114.867 1.00 15.39 ? 406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 141.249 146.550 113.433 1.00 15.17 ? 406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 140.745 147.464 112.776 1.00 26.28 ? 406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 140.521 146.643 115.828 1.00 6.55  ? 406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.944 146.216 117.219 1.00 23.91 ? 406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 142.147 145.951 117.423 1.00 26.78 ? 406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 140.073 146.144 118.110 1.00 28.59 ? 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 141.423 145.329 112.954 1.00 12.78 ? 407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 141.237 145.010 111.544 1.00 15.53 ? 407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.767 144.744 111.267 1.00 10.41 ? 407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 139.065 144.117 112.070 1.00 17.18 ? 407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 142.103 143.808 111.126 1.00 7.27  ? 407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 143.580 144.099 111.395 1.00 2.93  ? 407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.881 143.477 109.664 1.00 13.04 ? 407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 144.353 142.904 111.887 1.00 5.97  ? 407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 139.300 145.238 110.125 1.00 18.24 ? 408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.978 144.941 109.598 1.00 11.26 ? 408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 138.001 145.201 108.102 1.00 14.79 ? 408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 138.716 146.091 107.633 1.00 27.92 ? 408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.893 145.789 110.270 1.00 19.43 ? 408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 136.769 147.050 109.639 1.00 26.85 ? 408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 137.233 144.419 107.353 1.00 17.50 ? 409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 137.104 144.623 105.919 1.00 25.81 ? 409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.731 144.161 105.459 1.00 15.78 ? 409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 135.210 143.152 105.942 1.00 18.36 ? 409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 138.204 143.882 105.144 1.00 13.30 ? 409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 138.052 142.082 105.137 1.00 41.51 ? 409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 135.149 144.911 104.531 1.00 16.54 ? 410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.899 144.534 103.894 1.00 19.49 ? 410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.207 143.770 102.614 1.00 19.75 ? 410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 135.127 144.123 101.871 1.00 13.93 ? 410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 133.031 145.761 103.603 1.00 20.33 ? 410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 133.662 146.700 102.598 1.00 25.86 ? 410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.786 147.164 102.784 1.00 24.82 ? 410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 132.936 146.989 101.527 1.00 26.94 ? 410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.437 142.718 102.366 1.00 20.42 ? 411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.794 141.700 101.393 1.00 6.35  ? 411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.966 141.834 100.124 1.00 16.52 ? 411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.812 142.272 100.160 1.00 20.82 ? 411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.605 140.302 101.985 1.00 13.72 ? 411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 134.421 140.010 103.242 1.00 14.19 ? 411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 134.720 138.531 103.347 1.00 21.72 ? 411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.706 140.816 103.234 1.00 15.31 ? 411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.574 141.454 99.008  1.00 18.57 ? 412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.865 141.313 97.753  1.00 12.82 ? 412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.554 140.264 96.918  1.00 6.96  ? 412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.756 140.025 97.065  1.00 13.66 ? 412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.788 139.623 96.041  1.00 9.16  ? 413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 133.304 138.523 95.240  1.00 11.11 ? 413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 133.018 138.768 93.769  1.00 10.69 ? 413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.874 139.033 93.389  1.00 19.31 ? 413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.694 137.186 95.672  1.00 6.34  ? 413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 133.177 136.794 96.942  1.00 28.09 ? 413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 134.060 138.677 92.952  1.00 14.37 ? 414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.890 138.601 91.511  1.00 6.86  ? 414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.423 137.206 91.127  1.00 10.61 ? 414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.881 136.207 91.688  1.00 10.15 ? 414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 135.201 138.923 90.796  1.00 10.43 ? 414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.877 140.253 91.121  1.00 16.75 ? 414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 137.190 140.364 90.372  1.00 14.53 ? 414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.962 141.412 90.777  1.00 21.36 ? 414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.499 137.140 90.175  1.00 18.74 ? 415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 132.096 135.871 89.584  1.00 15.27 ? 415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 133.011 135.608 88.395  1.00 20.01 ? 415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.870 136.239 87.343  1.00 26.49 ? 415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.628 135.901 89.169  1.00 19.59 ? 415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 130.069 134.518 88.904  1.00 21.07 ? 415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.714 133.689 88.265  1.00 27.82 ? 415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.866 134.260 89.400  1.00 20.68 ? 415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.952 134.677 88.564  1.00 8.34  ? 416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.986 134.472 87.554  1.00 19.57 ? 416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 134.365 134.064 86.225  1.00 21.69 ? 416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.753 134.564 85.164  1.00 26.04 ? 416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 136.015 133.436 88.041  1.00 23.15 ? 416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.820 133.996 89.215  1.00 14.39 ? 416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.945 133.032 86.908  1.00 6.35  ? 416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.568 132.946 90.002  1.00 19.08 ? 416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 133.392 133.152 86.260  1.00 14.60 ? 417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.765 132.696 85.024  1.00 20.86 ? 417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 132.091 133.849 84.293  1.00 15.50 ? 417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 132.263 134.019 83.081  1.00 29.35 ? 417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.755 131.589 85.328  1.00 23.56 ? 417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 131.010 131.007 84.125  1.00 23.99 ? 417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 131.134 129.494 84.102  1.00 20.66 ? 417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.550 131.429 84.138  1.00 25.86 ? 417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 131.324 134.661 85.020  1.00 21.99 ? 418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.605 135.766 84.399  1.00 22.88 ? 418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 131.530 136.919 84.034  1.00 17.70 ? 418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 131.277 137.622 83.051  1.00 21.99 ? 418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 129.492 136.249 85.329  1.00 22.90 ? 418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 128.284 135.337 85.309  1.00 21.88 ? 418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.840 134.902 84.248  1.00 33.50 ? 418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.750 135.036 86.485  1.00 20.65 ? 418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.595 137.130 84.809  1.00 21.16 ? 419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 133.559 138.171 84.473  1.00 23.41 ? 419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 134.320 137.804 83.206  1.00 25.12 ? 419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 134.638 138.670 82.383  1.00 27.83 ? 419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 134.512 138.417 85.657  1.00 23.02 ? 419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.649 139.327 85.239  1.00 25.65 ? 419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.755 139.012 86.829  1.00 13.81 ? 419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.632 136.519 83.033  1.00 26.00 ? 420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 135.335 136.072 81.836  1.00 22.39 ? 420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 134.410 136.014 80.628  1.00 24.13 ? 420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 134.833 136.318 79.507  1.00 28.60 ? 420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.973 134.706 82.086  1.00 24.55 ? 420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 137.044 134.714 83.159  1.00 15.53 ? 420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 138.439 135.760 82.711  1.00 32.02 ? 420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 139.040 134.906 81.257  1.00 25.36 ? 420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 133.150 135.626 80.833  1.00 27.73 ? 421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 132.198 135.605 79.728  1.00 27.36 ? 421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.947 137.009 79.195  1.00 28.43 ? 421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 131.838 137.209 77.980  1.00 32.52 ? 421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.889 134.954 80.175  1.00 29.60 ? 421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.906 133.434 80.118  1.00 33.80 ? 421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.596 132.817 80.569  1.00 39.35 ? 421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 128.707 133.570 81.018  1.00 38.38 ? 421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 129.456 131.580 80.473  1.00 35.89 ? 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.855 137.993 80.088  1.00 25.57 ? 422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.656 139.378 79.684  1.00 27.46 ? 422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 132.955 140.088 79.334  1.00 32.28 ? 422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.906 141.217 78.833  1.00 32.89 ? 422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 130.938 140.149 80.793  1.00 26.44 ? 422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.495 139.785 80.947  1.00 25.99 ? 422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 129.066 138.792 81.800  1.00 29.10 ? 422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 128.382 140.282 80.357  1.00 29.83 ? 422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 127.750 138.692 81.730  1.00 31.93 ? 422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 127.311 139.585 80.861  1.00 35.30 ? 422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 134.106 139.463 79.577  1.00 36.06 ? 423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 135.401 140.075 79.286  1.00 31.84 ? 423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 135.520 141.438 79.961  1.00 32.52 ? 423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 136.014 142.406 79.379  1.00 32.08 ? 423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.624 140.191 77.778  1.00 28.99 ? 423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.946 138.874 77.099  1.00 36.29 ? 423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.060 138.648 75.886  1.00 36.89 ? 423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.834 138.006 74.748  1.00 33.64 ? 423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 136.785 136.972 75.239  1.00 37.61 ? 423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 135.065 141.512 81.208  1.00 25.49 ? 424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.973 142.764 81.946  1.00 23.26 ? 424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.722 142.675 83.266  1.00 24.11 ? 424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 135.222 143.095 84.313  1.00 28.59 ? 424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.515 143.145 82.182  1.00 27.76 ? 424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.865 142.180 82.991  1.00 29.90 ? 424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.936 142.122 83.244  1.00 23.36 ? 425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.726 142.035 84.469  1.00 16.21 ? 425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 138.015 143.428 85.014  1.00 22.37 ? 425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.803 143.707 86.199  1.00 29.85 ? 425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 139.027 141.250 84.222  1.00 26.18 ? 425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.732 139.760 84.042  1.00 24.20 ? 425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 140.004 141.469 85.367  1.00 18.95 ? 425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.964 138.929 83.762  1.00 23.95 ? 425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 138.497 144.326 84.154  1.00 22.18 ? 426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.885 145.656 84.613  1.00 19.52 ? 426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 137.688 146.428 85.157  1.00 23.80 ? 426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 137.725 146.948 86.279  1.00 28.49 ? 426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 139.543 146.427 83.469  1.00 19.84 ? 426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 139.683 147.916 83.727  1.00 19.42 ? 426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 140.109 148.683 82.493  1.00 31.56 ? 426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 140.086 148.098 81.390  1.00 31.42 ? 426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 140.467 149.872 82.624  1.00 37.46 ? 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 136.616 146.516 84.367  1.00 31.50 ? 427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 135.455 147.297 84.780  1.00 22.49 ? 427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.802 146.699 86.017  1.00 27.63 ? 427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 134.424 147.426 86.944  1.00 32.13 ? 427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 134.454 147.391 83.630  1.00 25.19 ? 427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 133.024 147.658 84.064  1.00 25.08 ? 427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 132.030 146.980 83.137  1.00 29.56 ? 427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 131.832 145.522 83.507  1.00 29.78 ? 427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 130.851 145.356 84.612  1.00 33.25 ? 427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.658 145.373 86.049  1.00 20.47 ? 428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 134.061 144.728 87.211  1.00 20.89 ? 428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.902 144.962 88.458  1.00 21.84 ? 428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 134.365 145.268 89.528  1.00 26.14 ? 428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.891 143.231 86.955  1.00 18.66 ? 428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 133.094 143.034 85.780  1.00 24.95 ? 428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 133.214 142.564 88.139  1.00 17.49 ? 428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 136.224 144.831 88.338  1.00 21.06 ? 429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 137.100 145.027 89.488  1.00 19.50 ? 429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 137.004 146.459 89.993  1.00 21.08 ? 429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.946 146.703 91.202  1.00 24.10 ? 429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 138.549 144.649 89.129  1.00 16.05 ? 429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 139.501 145.112 90.217  1.00 14.45 ? 429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.669 143.151 88.918  1.00 19.28 ? 429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.994 147.430 89.078  1.00 20.46 ? 430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.953 148.826 89.501  1.00 18.36 ? 430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 135.616 149.176 90.146  1.00 18.17 ? 430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 135.578 149.877 91.165  1.00 27.94 ? 430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 137.249 149.735 88.310  1.00 20.04 ? 430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 138.644 149.522 87.747  1.00 20.12 ? 430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 139.082 150.669 86.861  1.00 25.89 ? 430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 140.556 150.552 86.517  1.00 26.96 ? 430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 141.014 151.666 85.645  1.00 32.66 ? 430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 134.510 148.688 89.582  1.00 26.53 ? 431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 133.208 148.934 90.193  1.00 14.85 ? 431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 133.100 148.262 91.557  1.00 18.65 ? 431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 132.539 148.839 92.497  1.00 23.37 ? 431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 132.094 148.457 89.264  1.00 23.13 ? 431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 131.656 149.465 88.203  1.00 27.06 ? 431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 130.681 148.828 87.230  1.00 27.61 ? 431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 131.042 150.691 88.858  1.00 29.96 ? 431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 133.628 147.043 91.685  1.00 22.81 ? 432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 133.616 146.367 92.977  1.00 11.62 ? 432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 134.460 147.119 93.995  1.00 21.04 ? 432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 134.084 147.223 95.168  1.00 27.23 ? 432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 134.110 144.930 92.821  1.00 14.37 ? 432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 135.609 147.645 93.566  1.00 26.21 ? 433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 136.440 148.441 94.462  1.00 18.84 ? 433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.708 149.695 94.915  1.00 20.68 ? 433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.777 150.072 96.089  1.00 31.14 ? 433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.755 148.808 93.773  1.00 24.87 ? 433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 138.455 147.613 93.405  1.00 26.67 ? 433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 138.629 149.636 94.701  1.00 20.10 ? 433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.999 150.354 93.997  1.00 20.99 ? 434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 134.238 151.542 94.370  1.00 16.86 ? 434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 133.133 151.205 95.364  1.00 20.98 ? 434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.919 151.935 96.339  1.00 25.19 ? 434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 133.657 152.204 93.122  1.00 20.99 ? 434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 134.727 152.756 92.206  1.00 29.52 ? 434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.771 153.208 92.717  1.00 33.51 ? 434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 134.525 152.740 90.974  1.00 36.09 ? 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 132.417 150.102 95.136  1.00 21.46 ? 435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 131.354 149.714 96.060  1.00 15.53 ? 435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.916 149.354 97.432  1.00 17.52 ? 435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 131.343 149.729 98.464  1.00 21.78 ? 435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 130.553 148.549 95.481  1.00 14.71 ? 435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 131.313 147.356 95.470  1.00 18.74 ? 435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 133.034 148.627 97.464  1.00 16.89 ? 436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.659 148.282 98.736  1.00 9.65  ? 436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 134.139 149.530 99.463  1.00 12.75 ? 436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 134.014 149.631 100.688 1.00 19.25 ? 436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.815 147.309 98.503  1.00 16.82 ? 436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 134.435 145.896 98.050  1.00 17.77 ? 436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 135.660 145.128 97.581  1.00 12.55 ? 436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 133.715 145.140 99.151  1.00 11.14 ? 436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 134.698 150.491 98.723  1.00 20.18 ? 437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 135.118 151.748 99.331  1.00 13.38 ? 437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.930 152.502 99.910  1.00 16.99 ? 437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 134.024 153.080 100.998 1.00 26.34 ? 437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.848 152.611 98.303  1.00 15.89 ? 437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.933 151.867 97.738  1.00 21.46 ? 437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 136.390 153.869 98.957  1.00 16.60 ? 437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.806 152.521 99.192  1.00 17.40 ? 438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 131.616 153.177 99.724  1.00 15.58 ? 438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 131.147 152.502 101.007 1.00 14.53 ? 438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 130.815 153.178 101.989 1.00 22.90 ? 438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 130.498 153.180 98.683  1.00 19.81 ? 438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 129.207 153.738 99.193  1.00 23.82 ? 438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.933 155.089 99.204  1.00 21.59 ? 438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 128.123 153.131 99.731  1.00 22.15 ? 438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 127.733 155.288 99.718  1.00 27.71 ? 438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 127.220 154.116 100.046 1.00 26.99 ? 438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 131.122 151.169 101.019 1.00 16.47 ? 439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.705 150.454 102.222 1.00 10.97 ? 439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 131.643 150.771 103.380 1.00 24.06 ? 439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 131.202 150.983 104.516 1.00 32.08 ? 439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.630 148.940 101.950 1.00 19.33 ? 439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 130.310 148.190 103.230 1.00 16.76 ? 439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 129.592 148.646 100.884 1.00 15.44 ? 439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.950 150.811 103.111 1.00 20.67 ? 440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.915 151.143 104.154 1.00 14.42 ? 440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 133.701 152.559 104.677 1.00 18.64 ? 440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 133.798 152.804 105.885 1.00 28.14 ? 440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 135.337 150.977 103.617 1.00 23.39 ? 440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 136.302 151.227 104.624 1.00 24.99 ? 440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 133.413 153.505 103.782 1.00 20.39 ? 441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 133.248 154.894 104.196 1.00 15.51 ? 441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.940 155.112 104.943 1.00 26.37 ? 441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.830 156.060 105.728 1.00 37.16 ? 441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 133.315 155.816 102.980 1.00 17.29 ? 441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 134.721 156.146 102.518 1.00 21.07 ? 441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 134.792 156.419 101.030 1.00 31.75 ? 441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.739 156.355 100.360 1.00 32.05 ? 441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 135.899 156.704 100.529 1.00 29.99 ? 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.944 154.262 104.713 1.00 27.62 ? 442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 129.657 154.395 105.382 1.00 20.78 ? 442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 129.571 153.595 106.675 1.00 23.71 ? 442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 128.507 153.572 107.301 1.00 31.25 ? 442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 128.522 153.971 104.442 1.00 25.87 ? 442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 128.675 152.590 104.092 1.00 27.27 ? 442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 128.540 154.814 103.179 1.00 24.09 ? 442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 130.653 152.945 107.090 1.00 26.43 ? 443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 130.661 152.155 108.314 1.00 26.74 ? 443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 131.186 152.993 109.472 1.00 30.28 ? 443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 132.197 153.689 109.335 1.00 36.96 ? 443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 131.517 150.900 108.143 1.00 29.68 ? 443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.839 149.971 107.288 1.00 35.30 ? 443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 131.779 150.246 109.489 1.00 25.72 ? 443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 130.494 152.925 110.610 1.00 34.48 ? 444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.920 153.639 111.813 1.00 35.10 ? 444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 130.508 152.792 113.015 1.00 34.53 ? 444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 129.326 152.741 113.364 1.00 36.05 ? 444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 130.312 155.033 111.873 1.00 39.53 ? 444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 131.178 156.013 112.638 1.00 39.50 ? 444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 132.329 156.245 112.214 1.00 37.61 ? 444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 130.709 156.550 113.662 1.00 36.08 ? 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 131.484 152.138 113.637 1.00 31.43 ? 445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 131.235 151.257 114.773 1.00 34.20 ? 445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 131.339 152.082 116.049 1.00 33.28 ? 445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 132.382 152.682 116.328 1.00 30.07 ? 445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 132.220 150.080 114.789 1.00 32.94 ? 445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 132.063 149.242 113.518 1.00 24.82 ? 445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 132.005 149.221 116.025 1.00 30.86 ? 445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.864 148.324 113.533 1.00 26.05 ? 445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 130.260 152.105 116.829 1.00 36.64 ? 446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 130.153 152.998 117.974 1.00 35.05 ? 446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.691 152.405 119.270 1.00 37.34 ? 446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 130.807 153.134 120.261 1.00 31.04 ? 446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.692 153.414 118.176 1.00 31.59 ? 446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 128.129 154.245 117.035 1.00 34.69 ? 446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 128.765 155.624 116.994 1.00 33.44 ? 446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 128.264 156.424 115.882 1.00 38.23 ? 446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 128.676 157.652 115.599 1.00 37.24 ? 446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 129.593 158.261 116.333 1.00 36.49 ? 446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 128.154 158.285 114.552 1.00 36.37 ? 446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 131.027 151.112 119.295 1.00 25.31 ? 447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 131.524 150.476 120.510 1.00 18.99 ? 447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 132.831 149.729 120.275 1.00 26.39 ? 447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 133.251 148.944 121.131 1.00 33.83 ? 447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 130.473 149.529 121.097 1.00 27.77 ? 447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 129.338 150.268 121.774 1.00 23.83 ? 447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.516 150.859 122.838 1.00 24.53 ? 447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 128.161 150.234 121.163 1.00 26.65 ? 447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 133.480 149.952 119.135 1.00 29.78 ? 448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 134.776 149.355 118.821 1.00 17.54 ? 448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 135.704 150.479 118.385 1.00 24.71 ? 448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 135.925 150.689 117.185 1.00 28.00 ? 448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 134.650 148.277 117.744 1.00 22.68 ? 448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 136.258 151.232 119.338 1.00 27.79 ? 449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 137.065 152.404 118.958 1.00 16.37 ? 449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 138.224 152.065 118.039 1.00 13.05 ? 449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 138.486 152.804 117.083 1.00 17.71 ? 449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 137.554 152.947 120.310 1.00 13.11 ? 449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.668 152.330 121.331 1.00 19.65 ? 449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 136.244 151.010 120.792 1.00 16.60 ? 449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.916 150.953 118.292 1.00 24.37 ? 450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 140.045 150.585 117.445 1.00 14.74 ? 450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 139.575 150.131 116.071 1.00 19.69 ? 450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 140.210 150.443 115.060 1.00 24.71 ? 450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.880 149.498 118.120 1.00 10.02 ? 450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 138.455 149.409 116.012 1.00 19.65 ? 451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.901 149.005 114.723 1.00 18.15 ? 451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 137.560 150.231 113.888 1.00 14.55 ? 451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 137.904 150.314 112.705 1.00 21.64 ? 451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 136.670 148.103 114.925 1.00 19.34 ? 451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 135.925 147.927 113.614 1.00 18.65 ? 451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 137.086 146.759 115.487 1.00 14.36 ? 451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.875 151.201 114.494 1.00 17.21 ? 452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 136.474 152.399 113.763 1.00 17.62 ? 452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 137.684 153.223 113.338 1.00 16.63 ? 452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 137.742 153.718 112.204 1.00 25.20 ? 452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 135.517 153.222 114.626 1.00 11.88 ? 452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 134.995 154.490 113.987 1.00 20.24 ? 452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 134.041 155.199 114.932 1.00 18.64 ? 452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.511 156.428 114.358 1.00 31.56 ? 452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 134.114 157.608 114.422 1.00 36.94 ? 452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 135.271 157.759 115.046 1.00 29.02 ? 452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 133.540 158.661 113.849 1.00 27.74 ? 452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 138.668 153.367 114.227 1.00 17.85 ? 453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.863 154.125 113.878 1.00 13.61 ? 453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 140.629 153.457 112.743 1.00 21.96 ? 453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 141.095 154.132 111.818 1.00 23.36 ? 453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 140.753 154.295 115.109 1.00 13.96 ? 453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 142.231 154.351 114.798 1.00 19.66 ? 453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.949 155.344 115.688 1.00 18.23 ? 453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 144.274 155.661 115.172 1.00 22.47 ? 453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 145.377 154.998 115.487 1.00 22.02 ? 453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 145.354 153.977 116.327 1.00 19.20 ? 453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 146.533 155.367 114.944 1.00 23.17 ? 453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 140.761 152.128 112.788 1.00 21.35 ? 454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 141.468 151.421 111.728 1.00 11.94 ? 454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 140.692 151.447 110.421 1.00 13.76 ? 454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 141.298 151.490 109.349 1.00 22.39 ? 454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 141.749 149.982 112.151 1.00 18.86 ? 454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 139.361 151.415 110.482 1.00 18.74 ? 455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 138.574 151.564 109.265 1.00 12.28 ? 455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 138.797 152.934 108.640 1.00 14.93 ? 455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 138.939 153.051 107.417 1.00 21.59 ? 455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 137.092 151.339 109.567 1.00 14.03 ? 455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 136.219 151.458 108.333 1.00 22.05 ? 455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 136.330 150.665 107.400 1.00 28.74 ? 455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 135.344 152.454 108.324 1.00 22.92 ? 455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 138.834 153.984 109.463 1.00 17.53 ? 456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 139.075 155.320 108.926 1.00 16.85 ? 456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 140.485 155.451 108.358 1.00 15.81 ? 456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 140.680 156.070 107.306 1.00 25.71 ? 456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 138.834 156.376 110.004 1.00 20.81 ? 456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 137.402 156.447 110.501 1.00 23.57 ? 456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 137.261 157.441 111.646 1.00 29.88 ? 456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 138.436 157.360 112.610 1.00 26.26 ? 456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 137.996 157.362 114.034 1.00 24.39 ? 456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 141.482 154.880 109.037 1.00 16.00 ? 457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 142.872 155.127 108.668 1.00 14.82 ? 457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 143.331 154.234 107.519 1.00 25.27 ? 457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 144.001 154.700 106.591 1.00 27.24 ? 457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 143.777 154.931 109.885 1.00 12.93 ? 457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.985 152.950 107.564 1.00 21.70 ? 458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 143.494 151.980 106.604 1.00 14.20 ? 458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 142.635 151.870 105.355 1.00 17.26 ? 458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 143.171 151.636 104.267 1.00 27.24 ? 458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 143.606 150.602 107.262 1.00 14.00 ? 458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 144.400 150.595 108.556 1.00 14.93 ? 458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 146.151 150.933 108.305 1.00 31.01 ? 458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 146.814 149.270 108.240 1.00 10.74 ? 458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 141.320 152.036 105.481 1.00 14.29 ? 459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 140.411 151.905 104.345 1.00 18.18 ? 459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 140.570 150.543 103.675 1.00 17.29 ? 459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 140.522 150.420 102.450 1.00 19.20 ? 459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 140.625 153.036 103.337 1.00 14.82 ? 459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 140.702 154.416 103.963 1.00 15.46 ? 459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 141.675 155.303 103.207 1.00 21.93 ? 459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 141.855 156.643 103.894 1.00 25.50 ? 459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 140.553 157.273 104.243 1.00 31.64 ? 459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 140.763 149.510 104.489 1.00 23.68 ? 460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.975 148.168 103.967 1.00 10.27 ? 460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 139.679 147.600 103.404 1.00 16.14 ? 460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 138.617 147.709 104.024 1.00 19.66 ? 460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 141.519 147.257 105.065 1.00 4.46  ? 460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 141.063 145.929 104.897 1.00 25.58 ? 460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.769 146.992 102.222 1.00 12.17 ? 461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 138.644 146.318 101.593 1.00 7.67  ? 461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 139.086 144.915 101.206 1.00 15.24 ? 461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 140.274 144.639 101.029 1.00 26.01 ? 461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 138.120 147.073 100.354 1.00 13.43 ? 461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 139.216 147.172 99.292  1.00 6.10  ? 461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 137.621 148.453 100.744 1.00 8.84  ? 461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 138.770 147.823 98.009  1.00 1.21  ? 461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 138.114 144.019 101.091 1.00 17.83 ? 462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 138.407 142.685 100.610 1.00 5.86  ? 462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.607 142.316 99.381  1.00 1.98  ? 462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 136.393 142.115 99.460  1.00 18.87 ? 462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 138.278 142.210 98.241  1.00 6.37  ? 463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.649 141.816 96.987  1.00 10.33 ? 463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 138.066 140.384 96.683  1.00 4.94  ? 463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 139.211 140.135 96.293  1.00 26.27 ? 463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 138.039 142.761 95.852  1.00 14.77 ? 463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.595 142.359 94.443  1.00 11.15 ? 463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 136.101 142.091 94.405  1.00 6.23  ? 463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.974 143.432 93.437  1.00 6.43  ? 463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 137.139 139.448 96.865  1.00 6.62  ? 464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.395 138.052 96.596  1.00 0.13  ? 464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.948 137.645 95.208  1.00 2.23  ? 464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 136.619 138.468 94.353  1.00 11.59 ? 464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.948 136.335 94.987  1.00 14.24 ? 465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.479 135.763 93.736  1.00 7.11  ? 465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.808 134.433 94.036  1.00 8.22  ? 465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 136.080 133.795 95.055  1.00 16.85 ? 465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.622 135.587 92.730  1.00 7.62  ? 465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.914 134.028 93.139  1.00 14.80 ? 466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 134.200 132.769 93.274  1.00 16.83 ? 466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.950 132.195 91.888  1.00 14.14 ? 466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.068 132.887 90.875  1.00 19.76 ? 466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.881 132.947 94.035  1.00 17.61 ? 466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.895 133.875 93.355  1.00 13.78 ? 466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.293 133.888 94.171  1.00 30.65 ? 466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.799 135.577 93.870  1.00 26.32 ? 466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.604 130.910 91.853  1.00 10.76 ? 467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 133.316 130.189 90.618  1.00 12.46 ? 467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.572 129.844 89.830  1.00 16.95 ? 467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.511 129.690 88.607  1.00 25.18 ? 467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 132.348 130.978 89.730  1.00 16.76 ? 467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 131.293 130.100 89.093  1.00 17.05 ? 467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 131.036 128.988 89.551  1.00 30.53 ? 467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.671 130.598 88.034  1.00 18.67 ? 467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.724 129.737 90.495  1.00 15.20 ? 468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.930 129.299 89.802  1.00 12.59 ? 468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.770 127.877 89.282  1.00 19.47 ? 468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.993 127.607 88.096  1.00 23.75 ? 468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 138.141 129.398 90.730  1.00 20.28 ? 468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.460 128.904 90.129  1.00 14.18 ? 468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.897 129.794 88.978  1.00 13.09 ? 468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.543 128.817 91.190  1.00 12.22 ? 468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.371 126.952 90.158  1.00 19.12 ? 469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.182 125.572 89.727  1.00 10.32 ? 469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 135.033 125.452 88.738  1.00 24.18 ? 469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.122 124.691 87.771  1.00 33.67 ? 469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.944 124.658 90.926  1.00 17.08 ? 469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.075 123.203 90.598  1.00 20.75 ? 469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.735 122.204 91.483  1.00 25.77 ? 469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.509 122.580 89.477  1.00 18.02 ? 469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.953 121.028 90.922  1.00 23.75 ? 469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.423 121.229 89.704  1.00 15.87 ? 469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.936 126.173 88.973  1.00 22.60 ? 470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.836 126.140 88.024  1.00 14.30 ? 470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.254 126.622 86.650  1.00 16.51 ? 470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.943 125.996 85.634  1.00 31.02 ? 470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.985 127.736 86.604  1.00 10.33 ? 471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.461 128.260 85.330  1.00 17.29 ? 471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.398 127.270 84.648  1.00 20.73 ? 471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.289 127.024 83.442  1.00 22.81 ? 471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 135.161 129.602 85.548  1.00 17.21 ? 471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.888 130.116 84.328  1.00 17.22 ? 471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 135.211 130.809 83.336  1.00 14.36 ? 471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 137.248 129.897 84.162  1.00 9.73  ? 471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.867 131.279 82.219  1.00 15.30 ? 471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.912 130.360 83.046  1.00 12.50 ? 471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 137.217 131.051 82.078  1.00 19.26 ? 471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 137.873 131.517 80.965  1.00 25.49 ? 471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.331 126.693 85.407  1.00 20.58 ? 472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.295 125.768 84.819  1.00 21.54 ? 472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.605 124.519 84.282  1.00 22.65 ? 472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.899 124.062 83.172  1.00 25.03 ? 472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.358 125.394 85.853  1.00 20.17 ? 472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.276 126.520 86.332  1.00 21.47 ? 472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 140.126 126.051 87.500  1.00 16.96 ? 472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.146 127.031 85.195  1.00 18.15 ? 472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.684 123.949 85.061  1.00 25.02 ? 473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.975 122.752 84.626  1.00 20.45 ? 473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.104 123.039 83.412  1.00 26.10 ? 473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 134.017 122.216 82.493  1.00 38.80 ? 473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.135 122.194 85.774  1.00 22.16 ? 473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.449 124.199 83.389  1.00 19.22 ? 474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.635 124.571 82.240  1.00 18.94 ? 474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.469 124.982 81.037  1.00 24.02 ? 474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.905 125.464 80.049  1.00 33.67 ? 474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.678 125.697 82.627  1.00 27.07 ? 474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.552 125.250 83.542  1.00 25.38 ? 474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.725 126.406 84.057  1.00 26.67 ? 474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 129.762 126.729 85.244  1.00 28.88 ? 474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 128.972 127.037 83.167  1.00 31.20 ? 474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.789 124.807 81.095  1.00 26.99 ? 475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.679 125.134 79.988  1.00 27.26 ? 475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.634 123.995 79.659  1.00 28.16 ? 475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.612 124.210 78.934  1.00 28.62 ? 475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.470 126.408 80.302  1.00 28.63 ? 475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.630 127.661 80.169  1.00 27.91 ? 475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.541 128.252 79.094  1.00 31.54 ? 475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 135.003 128.070 81.264  1.00 21.63 ? 475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.378 122.795 80.169  1.00 26.26 ? 476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.230 121.653 79.889  1.00 28.05 ? 476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.628 121.761 80.456  1.00 29.16 ? 476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.598 121.419 79.769  1.00 36.23 ? 476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.759 122.233 81.693  1.00 24.03 ? 477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 140.052 122.376 82.349  1.00 26.32 ? 477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.983 121.699 83.709  1.00 26.19 ? 477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 139.087 121.991 84.508  1.00 28.05 ? 477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.458 123.854 82.502  1.00 23.27 ? 477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 140.573 124.522 81.131  1.00 22.06 ? 477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.766 123.970 83.264  1.00 26.14 ? 477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.584 126.029 81.189  1.00 30.51 ? 477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.923 120.795 83.967  1.00 25.33 ? 478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 141.004 120.157 85.273  1.00 23.87 ? 478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.500 121.151 86.315  1.00 25.48 ? 478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.380 121.971 86.045  1.00 30.55 ? 478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.930 118.942 85.217  1.00 24.77 ? 478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.925 121.074 87.516  1.00 24.48 ? 479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.324 121.986 88.582  1.00 17.19 ? 479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.800 121.822 88.921  1.00 25.60 ? 479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.515 122.812 89.112  1.00 34.72 ? 479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.458 121.755 89.820  1.00 15.66 ? 479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.647 122.784 90.912  1.00 23.73 ? 479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 141.648 122.641 91.865  1.00 27.17 ? 479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 139.823 123.897 90.993  1.00 20.86 ? 479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.823 123.578 92.865  1.00 23.55 ? 479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.989 124.838 91.988  1.00 17.58 ? 479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.990 124.675 92.921  1.00 24.53 ? 479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.156 125.612 93.914  1.00 22.94 ? 479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.276 120.579 88.996  1.00 22.29 ? 480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.663 120.305 89.346  1.00 21.55 ? 480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.620 120.450 88.171  1.00 27.60 ? 480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.836 120.378 88.375  1.00 35.43 ? 480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.790 118.894 89.922  1.00 29.48 ? 480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.980 118.650 91.180  1.00 27.89 ? 480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.718 117.176 91.417  1.00 33.63 ? 480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.819 116.618 90.755  1.00 36.90 ? 480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.417 116.573 92.257  1.00 35.90 ? 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.111 120.649 86.959  1.00 27.27 ? 481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.964 120.685 85.786  1.00 25.58 ? 481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.807 121.958 85.759  1.00 28.50 ? 481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.450 122.969 86.368  1.00 28.04 ? 481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 145.122 120.587 84.518  1.00 26.82 ? 481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.766 121.871 84.041  1.00 25.94 ? 481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.942 121.926 85.058  1.00 36.55 ? 482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.748 123.149 84.916  1.00 29.40 ? 482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.998 124.289 84.252  1.00 29.26 ? 482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.254 125.456 84.573  1.00 37.32 ? 482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.940 122.687 84.066  1.00 25.33 ? 482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 150.005 121.214 84.268  1.00 31.14 ? 482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.591 120.757 84.442  1.00 31.54 ? 482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 147.083 123.988 83.328  1.00 33.59 ? 483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.335 125.043 82.653  1.00 29.87 ? 483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.431 125.792 83.625  1.00 27.33 ? 483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 145.238 127.006 83.492  1.00 30.12 ? 483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.518 124.452 81.504  1.00 31.54 ? 483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.359 123.810 80.416  1.00 30.89 ? 483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.659 122.350 80.696  1.00 36.68 ? 483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.523 121.926 81.863  1.00 36.17 ? 483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.033 121.627 79.749  1.00 38.37 ? 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.858 125.085 84.601  1.00 27.11 ? 484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 144.043 125.756 85.606  1.00 23.82 ? 484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.870 126.758 86.398  1.00 22.48 ? 484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.430 127.890 86.635  1.00 25.38 ? 484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.403 124.726 86.536  1.00 19.89 ? 484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 146.077 126.364 86.808  1.00 26.99 ? 485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.946 127.285 87.531  1.00 19.10 ? 485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.391 128.437 86.642  1.00 15.83 ? 485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.534 129.567 87.113  1.00 28.41 ? 485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 148.153 126.539 88.097  1.00 22.03 ? 485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.829 125.684 89.308  1.00 18.81 ? 485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 149.086 125.108 89.933  1.00 25.87 ? 485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.818 124.253 89.007  1.00 27.92 ? 485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.506 122.990 88.749  1.00 25.00 ? 485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.473 122.402 89.327  1.00 24.54 ? 485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.251 122.302 87.890  1.00 22.93 ? 485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.615 128.173 85.354  1.00 24.59 ? 486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.972 129.246 84.430  1.00 21.28 ? 486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.854 130.277 84.331  1.00 24.18 ? 486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 147.097 131.492 84.405  1.00 31.44 ? 486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.289 128.658 83.055  1.00 27.44 ? 486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.815 129.692 82.085  1.00 36.45 ? 486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.831 130.344 82.400  1.00 37.53 ? 486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 148.210 129.852 81.005  1.00 35.40 ? 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.614 129.809 84.165  1.00 24.13 ? 487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.492 130.737 84.110  1.00 18.44 ? 487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 144.350 131.502 85.416  1.00 25.00 ? 487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 144.103 132.710 85.406  1.00 27.50 ? 487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 143.183 130.013 83.804  1.00 17.37 ? 487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.969 130.829 84.149  1.00 17.64 ? 487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.504 131.803 83.280  1.00 17.12 ? 487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 141.321 130.660 85.361  1.00 18.38 ? 487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.405 132.571 83.603  1.00 21.94 ? 487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 140.222 131.427 85.688  1.00 16.04 ? 487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.763 132.383 84.808  1.00 20.75 ? 487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.465 130.810 86.551  1.00 18.69 ? 488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.338 131.496 87.830  1.00 14.01 ? 488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.411 132.563 87.978  1.00 22.50 ? 488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 145.128 133.686 88.411  1.00 33.94 ? 488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.412 130.490 88.977  1.00 16.39 ? 488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.647 132.234 87.603  1.00 20.62 ? 489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.733 133.202 87.659  1.00 19.04 ? 489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 147.399 134.438 86.839  1.00 15.55 ? 489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.444 135.563 87.348  1.00 31.24 ? 489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 149.024 132.551 87.161  1.00 20.07 ? 489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 150.240 133.420 87.382  1.00 25.70 ? 489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.371 134.076 88.414  1.00 31.84 ? 489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 151.146 133.425 86.412  1.00 29.94 ? 489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 147.036 134.248 85.569  1.00 20.42 ? 490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.762 135.402 84.717  1.00 20.52 ? 490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.575 136.209 85.233  1.00 18.82 ? 490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.639 137.443 85.316  1.00 22.42 ? 490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.513 134.951 83.278  1.00 25.70 ? 490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.688 134.307 82.772  1.00 32.93 ? 490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 146.175 136.144 82.398  1.00 18.48 ? 490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.489 135.529 85.604  1.00 17.56 ? 491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 143.271 136.221 86.005  1.00 18.90 ? 491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 143.486 137.020 87.282  1.00 17.13 ? 491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 143.079 138.183 87.374  1.00 21.08 ? 491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 142.134 135.214 86.184  1.00 19.50 ? 491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.873 135.815 86.735  1.00 17.98 ? 491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.918 136.349 85.888  1.00 13.46 ? 491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.639 135.842 88.100  1.00 15.09 ? 491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.759 136.903 86.391  1.00 16.01 ? 491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 139.483 136.394 88.607  1.00 11.00 ? 491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.541 136.926 87.751  1.00 16.39 ? 491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 144.123 136.416 88.284  1.00 17.22 ? 492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 144.309 137.122 89.542  1.00 13.10 ? 492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 145.412 138.166 89.450  1.00 12.68 ? 492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 145.358 139.171 90.163  1.00 19.88 ? 492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.567 136.119 90.665  1.00 15.05 ? 492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 143.339 135.355 91.068  1.00 14.18 ? 492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.373 135.945 91.866  1.00 11.90 ? 492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 143.130 134.063 90.620  1.00 18.32 ? 492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 141.235 135.251 92.226  1.00 10.68 ? 492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.994 133.366 90.976  1.00 13.34 ? 492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 141.046 133.960 91.782  1.00 13.29 ? 492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 146.387 137.987 88.554  1.00 6.28  ? 493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 147.312 139.076 88.266  1.00 9.65  ? 493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 146.577 140.271 87.677  1.00 11.75 ? 493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.824 141.416 88.070  1.00 20.85 ? 493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 148.411 138.596 87.318  1.00 17.64 ? 493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 149.535 139.594 87.110  1.00 13.36 ? 493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 149.211 140.781 85.792  1.00 35.30 ? 493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 148.338 139.754 84.615  1.00 18.31 ? 493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.666 140.026 86.732  1.00 15.16 ? 494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.888 141.123 86.164  1.00 14.63 ? 494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 144.007 141.775 87.222  1.00 15.89 ? 494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.858 143.004 87.251  1.00 23.64 ? 494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 144.041 140.617 84.997  1.00 12.54 ? 494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.846 140.011 83.861  1.00 16.88 ? 494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.961 140.013 82.293  1.00 30.82 ? 494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.562 141.056 82.688  1.00 24.74 ? 494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 143.407 140.964 88.095  1.00 16.52 ? 495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 142.563 141.501 89.158  1.00 8.67  ? 495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 143.380 142.396 90.080  1.00 13.82 ? 495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.952 143.497 90.443  1.00 21.27 ? 495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.887 140.360 89.938  1.00 16.31 ? 495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 141.142 140.912 91.145  1.00 12.57 ? 495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.948 139.585 89.034  1.00 13.81 ? 495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 144.568 141.935 90.477  1.00 21.62 ? 496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 145.431 142.749 91.325  1.00 9.43  ? 496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.840 144.032 90.618  1.00 6.68  ? 496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.839 145.111 91.221  1.00 19.01 ? 496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.665 141.947 91.738  1.00 11.85 ? 496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 147.410 142.580 92.893  1.00 10.57 ? 496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.808 143.176 93.783  1.00 21.83 ? 496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.729 142.452 92.885  1.00 11.35 ? 496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 146.188 143.937 89.335  1.00 8.85  ? 497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 146.584 145.122 88.585  1.00 9.34  ? 497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 145.469 146.156 88.575  1.00 19.93 ? 497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 145.694 147.334 88.873  1.00 22.70 ? 497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.967 144.727 87.158  1.00 14.60 ? 497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 147.329 145.889 86.282  1.00 17.98 ? 497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 146.355 146.559 85.562  1.00 16.90 ? 497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 148.643 146.307 86.171  1.00 17.85 ? 497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 146.683 147.627 84.755  1.00 16.93 ? 497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 148.978 147.374 85.363  1.00 17.69 ? 497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.996 148.035 84.654  1.00 20.30 ? 497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 144.248 145.730 88.251  1.00 17.48 ? 498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 143.160 146.691 88.125  1.00 12.66 ? 498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 142.680 147.189 89.481  1.00 18.78 ? 498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 142.244 148.339 89.590  1.00 23.45 ? 498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 142.015 146.085 87.317  1.00 20.13 ? 498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 142.346 145.998 85.848  1.00 19.29 ? 498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 142.727 147.130 85.140  1.00 19.47 ? 498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 142.304 144.786 85.173  1.00 17.54 ? 498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 143.045 147.062 83.802  1.00 19.64 ? 498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 142.620 144.708 83.832  1.00 21.16 ? 498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.989 145.850 83.151  1.00 22.67 ? 498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 143.303 145.781 81.815  1.00 27.43 ? 498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.786 146.373 90.531  1.00 17.80 ? 499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 142.433 146.865 91.857  1.00 10.72 ? 499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 143.451 147.886 92.346  1.00 8.85  ? 499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 143.082 148.890 92.963  1.00 14.04 ? 499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 142.311 145.703 92.844  1.00 10.23 ? 499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 143.582 145.238 93.256  1.00 21.33 ? 499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.736 147.660 92.061  1.00 13.24 ? 500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.754 148.647 92.406  1.00 12.65 ? 500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 145.538 149.927 91.613  1.00 14.95 ? 500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 145.680 151.035 92.142  1.00 22.37 ? 500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 147.161 148.069 92.174  1.00 21.08 ? 500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 147.506 147.055 93.264  1.00 15.11 ? 500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 148.191 149.186 92.127  1.00 12.81 ? 500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 148.728 146.229 92.961  1.00 10.87 ? 500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 145.204 149.796 90.328  1.00 18.63 ? 501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.955 150.976 89.510  1.00 14.56 ? 501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 143.763 151.765 90.034  1.00 18.79 ? 501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 143.809 152.997 90.105  1.00 29.77 ? 501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 144.734 150.565 88.054  1.00 20.35 ? 501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 145.112 151.635 87.048  1.00 19.80 ? 501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 144.829 151.217 85.620  1.00 25.12 ? 501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 143.706 150.847 85.281  1.00 28.02 ? 501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.850 151.269 84.776  1.00 26.48 ? 501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 142.687 151.072 90.416  1.00 20.30 ? 502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 141.526 151.757 90.972  1.00 15.38 ? 502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 141.849 152.405 92.313  1.00 12.78 ? 502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 141.382 153.511 92.598  1.00 28.68 ? 502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 140.356 150.787 91.114  1.00 19.73 ? 502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 139.042 151.467 91.455  1.00 18.36 ? 502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 138.706 152.549 90.446  1.00 16.95 ? 502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 137.629 153.414 90.911  1.00 22.83 ? 502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 137.529 154.704 90.625  1.00 22.42 ? 502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 138.428 155.318 89.873  1.00 26.12 ? 502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 136.502 155.397 91.106  1.00 20.31 ? 502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 142.634 151.732 93.155  1.00 14.56 ? 503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 143.020 152.323 94.431  1.00 15.09 ? 503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 143.844 153.588 94.222  1.00 20.29 ? 503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 143.620 154.605 94.890  1.00 19.19 ? 503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 143.793 151.300 95.263  1.00 12.70 ? 503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 143.907 151.709 96.612  1.00 12.35 ? 503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 144.796 153.547 93.288  1.00 22.69 ? 504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 145.596 154.730 92.990  1.00 16.87 ? 504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 144.737 155.846 92.408  1.00 21.25 ? 504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 144.926 157.022 92.740  1.00 30.28 ? 504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 146.730 154.367 92.032  1.00 20.07 ? 504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 143.789 155.500 91.534  1.00 21.39 ? 505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 142.906 156.508 90.959  1.00 22.88 ? 505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 142.029 157.147 92.028  1.00 22.16 ? 505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 141.786 158.358 92.000  1.00 28.83 ? 505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 142.046 155.884 89.861  1.00 23.46 ? 505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 142.814 155.519 88.603  1.00 23.03 ? 505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 142.051 154.559 87.713  1.00 31.96 ? 505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.905 154.206 88.061  1.00 37.45 ? 505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 142.596 154.160 86.663  1.00 33.24 ? 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 141.534 156.345 92.971  1.00 22.41 ? 506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 140.739 156.883 94.068  1.00 20.23 ? 506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 141.587 157.797 94.941  1.00 25.70 ? 506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 141.131 158.858 95.379  1.00 30.60 ? 506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 140.114 155.740 94.887  1.00 21.42 ? 506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 139.121 154.950 94.032  1.00 22.59 ? 506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 139.438 156.286 96.132  1.00 23.20 ? 506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 138.722 153.623 94.634  1.00 18.03 ? 506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 142.831 157.398 95.213  1.00 25.82 ? 507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 143.723 158.255 95.985  1.00 21.00 ? 507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 143.972 159.575 95.265  1.00 26.01 ? 507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 144.039 160.634 95.898  1.00 29.46 ? 507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 145.041 157.531 96.256  1.00 17.37 ? 507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 144.117 159.528 93.941  1.00 26.95 ? 508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 144.323 160.750 93.170  1.00 26.34 ? 508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 143.083 161.636 93.183  1.00 33.38 ? 508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 143.190 162.862 93.297  1.00 38.44 ? 508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 144.714 160.401 91.735  1.00 32.58 ? 508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 144.860 161.602 90.819  1.00 29.57 ? 508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 145.121 161.170 89.387  1.00 31.00 ? 508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 145.345 162.368 88.481  1.00 36.32 ? 508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 146.271 162.051 87.359  1.00 37.35 ? 508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 141.898 161.035 93.063  1.00 30.65 ? 509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 140.672 161.824 93.007  1.00 29.65 ? 509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 140.347 162.444 94.360  1.00 35.83 ? 509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 139.940 163.609 94.433  1.00 43.17 ? 509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 139.514 160.955 92.511  1.00 28.18 ? 509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 138.635 160.384 93.610  1.00 32.33 ? 509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 137.884 159.143 93.172  1.00 41.95 ? 509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 137.981 158.776 91.981  1.00 39.51 ? 509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 137.198 158.532 94.018  1.00 38.40 ? 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 140.517 161.685 95.441  1.00 32.55 ? 510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 140.261 162.186 96.783  1.00 26.51 ? 510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 141.451 162.922 97.381  1.00 35.32 ? 510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 141.290 163.598 98.402  1.00 42.94 ? 510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 139.860 161.032 97.706  1.00 27.97 ? 510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 138.633 160.273 97.242  1.00 31.90 ? 510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 138.098 159.365 98.333  1.00 30.01 ? 510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 136.762 158.762 97.938  1.00 30.76 ? 510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 135.893 158.519 99.120  1.00 33.43 ? 510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 142.632 162.808 96.778  1.00 30.22 ? 511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 143.799 163.500 97.279  1.00 28.44 ? 511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 144.403 162.921 98.536  1.00 34.08 ? 511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 145.291 163.547 99.121  1.00 35.87 ? 511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 143.957 161.744 98.972  1.00 32.26 ? 512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 144.449 161.146 100.202 1.00 26.54 ? 512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 144.763 159.675 99.979  1.00 25.73 ? 512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 144.103 158.992 99.193  1.00 28.97 ? 512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 143.434 161.285 101.344 1.00 29.37 ? 512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 142.090 160.641 101.059 1.00 24.48 ? 512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 141.249 160.476 102.308 1.00 33.51 ? 512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 141.832 160.343 103.404 1.00 36.74 ? 512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 140.004 160.482 102.196 1.00 34.30 ? 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 145.783 159.200 100.683 1.00 28.69 ? 513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 146.150 157.795 100.742 1.00 22.47 ? 513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 145.760 157.235 102.105 1.00 22.48 ? 513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 145.238 157.945 102.968 1.00 37.27 ? 513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 147.647 157.617 100.478 1.00 23.85 ? 513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 148.395 158.359 101.449 1.00 25.68 ? 513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 148.007 158.114 99.089  1.00 22.37 ? 513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 146.011 155.944 102.300 1.00 20.66 ? 514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 145.760 155.361 103.608 1.00 19.63 ? 514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 146.868 155.757 104.580 1.00 17.72 ? 514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 147.992 156.084 104.189 1.00 23.22 ? 514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 145.627 153.839 103.513 1.00 7.37  ? 514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 146.883 153.133 103.095 1.00 14.08 ? 514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 147.168 152.934 101.757 1.00 10.96 ? 514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 147.770 152.648 104.043 1.00 14.22 ? 514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 148.317 152.277 101.370 1.00 15.00 ? 514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.922 151.992 103.660 1.00 8.99  ? 514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 149.195 151.805 102.323 1.00 10.67 ? 514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 146.530 155.740 105.867 1.00 26.78 ? 515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 147.454 156.216 106.887 1.00 17.30 ? 515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 148.729 155.385 106.890 1.00 21.11 ? 515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 148.684 154.152 106.876 1.00 34.00 ? 515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 146.790 156.173 108.261 1.00 23.24 ? 515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 146.042 157.449 108.585 1.00 30.03 ? 515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 145.576 158.122 107.642 1.00 28.63 ? 515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 145.919 157.779 109.783 1.00 35.73 ? 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 149.871 156.070 106.917 1.00 22.04 ? 516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 151.180 155.423 106.882 1.00 20.91 ? 516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 151.426 154.719 105.552 1.00 22.78 ? 516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 152.090 153.682 105.498 1.00 27.50 ? 516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 151.347 154.443 108.046 1.00 23.68 ? 516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 151.339 155.107 109.411 1.00 18.67 ? 516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 151.526 154.117 110.540 1.00 25.84 ? 516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 152.642 153.676 110.813 1.00 30.70 ? 516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 150.433 153.760 111.203 1.00 25.68 ? 516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 150.884 155.277 104.468 1.00 20.85 ? 517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 151.149 154.724 103.146 1.00 17.93 ? 517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 152.595 154.948 102.722 1.00 22.42 ? 517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 153.155 154.134 101.980 1.00 28.71 ? 517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 150.200 155.337 102.116 1.00 12.73 ? 517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 150.764 155.339 100.715 1.00 21.03 ? 517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 150.718 154.199 99.924  1.00 21.02 ? 517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 151.360 156.476 100.189 1.00 20.49 ? 517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 151.242 154.195 98.648  1.00 24.00 ? 517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 151.886 156.481 98.916  1.00 17.91 ? 517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 151.825 155.338 98.150  1.00 22.04 ? 517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 152.347 155.339 96.879  1.00 34.56 ? 517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 153.214 156.036 103.186 1.00 24.24 ? 518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 154.548 156.391 102.714 1.00 24.89 ? 518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 155.572 155.313 103.040 1.00 30.90 ? 518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 156.513 155.099 102.267 1.00 34.36 ? 518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 154.975 157.729 103.318 1.00 25.13 ? 518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 154.186 158.918 102.801 1.00 26.54 ? 518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 154.272 159.064 101.296 1.00 37.43 ? 518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 155.296 158.647 100.714 1.00 38.33 ? 518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 153.316 159.597 100.694 1.00 37.31 ? 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 155.418 154.633 104.171 1.00 16.61 ? 519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 156.322 153.567 104.539 1.00 12.28 ? 519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.994 152.209 103.965 1.00 19.56 ? 519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 156.719 151.246 104.230 1.00 28.97 ? 519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 154.927 152.099 103.180 1.00 14.92 ? 520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 154.516 150.820 102.625 1.00 13.56 ? 520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 155.362 150.459 101.407 1.00 19.92 ? 520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 156.059 151.295 100.828 1.00 26.87 ? 520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 153.036 150.851 102.242 1.00 13.57 ? 520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 152.798 151.768 101.190 1.00 24.51 ? 520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 155.294 149.182 101.025 1.00 17.69 ? 521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 156.024 148.719 99.851  1.00 12.98 ? 521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 155.424 149.245 98.555  1.00 20.20 ? 521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 156.106 149.241 97.526  1.00 18.42 ? 521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 156.071 147.190 99.826  1.00 19.62 ? 521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 154.770 146.674 99.522  1.00 27.93 ? 521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 156.524 146.653 101.172 1.00 9.54  ? 521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 154.164 149.685 98.577  1.00 26.92 ? 522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 153.604 150.373 97.419  1.00 15.59 ? 522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 154.330 151.687 97.160  1.00 22.05 ? 522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 154.632 152.023 96.009  1.00 22.74 ? 522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 152.111 150.628 97.622  1.00 11.46 ? 522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 151.279 149.390 97.857  1.00 18.10 ? 522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 151.089 148.455 96.849  1.00 15.84 ? 522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 150.672 149.163 99.084  1.00 22.57 ? 522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 150.323 147.328 97.059  1.00 11.58 ? 522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.907 148.039 99.303  1.00 12.10 ? 522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 149.736 147.124 98.287  1.00 14.40 ? 522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.974 146.002 98.504  1.00 30.15 ? 522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 154.614 152.444 98.222  1.00 23.29 ? 523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 155.249 153.748 98.059  1.00 21.38 ? 523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 156.689 153.612 97.583  1.00 20.91 ? 523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 157.133 154.364 96.708  1.00 25.20 ? 523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 155.189 154.527 99.372  1.00 18.74 ? 523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 157.435 152.663 98.146  1.00 22.63 ? 524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 158.829 152.472 97.771  1.00 22.13 ? 524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.994 151.724 96.456  1.00 28.46 ? 524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 160.108 151.682 95.924  1.00 37.22 ? 524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 159.577 151.723 98.878  1.00 21.56 ? 524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 159.163 150.352 98.898  1.00 29.78 ? 524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 159.294 152.353 100.232 1.00 19.56 ? 524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.924 151.138 95.924  1.00 23.38 ? 525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.995 150.382 94.694  1.00 20.79 ? 525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 158.433 148.944 94.851  1.00 25.00 ? 525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 158.427 148.201 93.862  1.00 25.58 ? 525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.808 148.524 96.061  1.00 26.64 ? 526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 159.213 147.142 96.283  1.00 27.54 ? 526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 158.078 146.162 96.022  1.00 27.46 ? 526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 158.336 144.977 95.790  1.00 32.80 ? 526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 159.735 146.981 97.711  1.00 27.09 ? 526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.976 145.545 98.137  1.00 29.67 ? 526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 160.178 145.412 99.632  1.00 33.09 ? 526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 160.453 146.439 100.288 1.00 36.03 ? 526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 160.055 144.285 100.154 1.00 36.37 ? 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.829 146.631 96.055  1.00 26.45 ? 527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.695 145.753 95.786  1.00 20.57 ? 527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 155.683 145.284 94.336  1.00 23.44 ? 527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 155.343 144.130 94.054  1.00 26.02 ? 527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 154.391 146.474 96.127  1.00 15.63 ? 527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 153.151 145.651 95.882  1.00 24.05 ? 527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 152.644 144.817 96.868  1.00 21.38 ? 527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 152.484 145.708 94.665  1.00 17.80 ? 527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 151.511 144.064 96.650  1.00 17.90 ? 527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 151.351 144.956 94.438  1.00 14.73 ? 527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.869 144.136 95.434  1.00 14.13 ? 527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.739 143.386 95.214  1.00 25.61 ? 527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 156.054 146.160 93.407  1.00 25.91 ? 528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.916 145.907 91.980  1.00 23.96 ? 528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 157.129 145.220 91.367  1.00 31.53 ? 528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 157.212 145.126 90.139  1.00 34.81 ? 528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 155.649 147.221 91.241  1.00 23.86 ? 528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 154.448 147.965 91.742  1.00 26.63 ? 528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 153.201 147.745 91.185  1.00 25.04 ? 528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 154.564 148.884 92.771  1.00 21.56 ? 528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 152.094 148.427 91.643  1.00 21.86 ? 528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 153.460 149.567 93.233  1.00 20.61 ? 528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 152.224 149.339 92.669  1.00 22.71 ? 528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 158.070 144.743 92.184  1.00 30.67 ? 529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 159.293 144.161 91.639  1.00 29.59 ? 529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.985 142.978 90.729  1.00 28.10 ? 529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 159.434 142.930 89.577  1.00 35.43 ? 529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 160.219 143.737 92.779  1.00 30.14 ? 529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.986 144.901 93.370  1.00 36.33 ? 529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.988 145.989 92.756  1.00 33.74 ? 529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 161.587 144.729 94.451  1.00 41.24 ? 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 158.208 142.015 91.227  1.00 27.94 ? 530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.910 140.826 90.436  1.00 30.02 ? 530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 157.034 141.150 89.235  1.00 28.41 ? 530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 157.153 140.503 88.190  1.00 32.28 ? 530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 157.243 139.767 91.311  1.00 27.67 ? 530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.727 139.753 91.228  1.00 26.86 ? 530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 155.140 138.764 92.216  1.00 29.21 ? 530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.659 138.558 91.976  1.00 29.78 ? 530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.922 138.397 93.255  1.00 29.23 ? 530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 156.152 142.142 89.361  1.00 26.17 ? 531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 155.271 142.484 88.251  1.00 23.07 ? 531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 156.013 143.233 87.154  1.00 26.31 ? 531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 155.691 143.076 85.971  1.00 34.31 ? 531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 154.090 143.307 88.759  1.00 23.75 ? 531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 153.120 142.517 89.602  1.00 22.52 ? 531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 152.463 141.411 89.082  1.00 17.27 ? 531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.856 142.880 90.915  1.00 15.45 ? 531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.573 140.687 89.846  1.00 23.31 ? 531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.968 142.161 91.686  1.00 20.76 ? 531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 151.328 141.065 91.146  1.00 23.27 ? 531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 150.442 140.346 91.912  1.00 23.99 ? 531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 157.001 144.052 87.520  1.00 31.86 ? 532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.804 144.738 86.516  1.00 30.66 ? 532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.909 143.847 85.965  1.00 31.43 ? 532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 159.458 144.146 84.897  1.00 35.11 ? 532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 158.414 146.031 87.084  1.00 29.95 ? 532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 157.318 147.010 87.474  1.00 26.39 ? 532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 159.313 145.721 88.270  1.00 29.26 ? 532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 159.251 142.759 86.657  1.00 32.66 ? 533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 160.297 141.859 86.190  1.00 31.21 ? 533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.766 140.594 85.529  1.00 38.10 ? 533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 160.481 139.995 84.719  1.00 41.83 ? 533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 161.215 141.464 87.352  1.00 35.09 ? 533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.601 140.492 88.179  1.00 40.68 ? 533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 158.545 140.173 85.847  1.00 34.86 ? 534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.994 138.917 85.359  1.00 33.04 ? 534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.734 139.168 84.544  1.00 37.50 ? 534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.930 140.045 84.878  1.00 40.26 ? 534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.673 137.965 86.518  1.00 35.08 ? 534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.799 137.885 87.400  1.00 39.42 ? 534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 157.347 136.578 85.991  1.00 34.43 ? 534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.567 138.392 83.476  1.00 38.18 ? 535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 155.367 138.446 82.653  1.00 36.03 ? 535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 154.391 137.372 83.113  1.00 39.82 ? 535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.762 136.201 83.242  1.00 42.09 ? 535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.712 138.253 81.176  1.00 39.26 ? 535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.608 138.726 80.253  1.00 44.38 ? 535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 153.686 139.418 80.732  1.00 42.50 ? 535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.660 138.403 79.048  1.00 44.53 ? 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 153.144 137.773 83.360  1.00 29.72 ? 536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 152.124 136.870 83.878  1.00 26.55 ? 536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 151.064 136.530 82.836  1.00 28.65 ? 536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.949 136.140 83.196  1.00 30.93 ? 536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 151.477 137.468 85.127  1.00 28.50 ? 536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 152.373 137.464 86.330  1.00 23.38 ? 536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.460 136.346 87.140  1.00 24.91 ? 536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 153.138 138.573 86.645  1.00 24.14 ? 536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.288 136.337 88.245  1.00 26.23 ? 536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.968 138.568 87.749  1.00 29.84 ? 536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 154.042 137.449 88.549  1.00 26.93 ? 536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 151.388 136.673 81.555  1.00 31.01 ? 537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.469 136.259 80.510  1.00 30.52 ? 537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.367 134.735 80.475  1.00 32.02 ? 537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 151.306 134.033 80.860  1.00 37.06 ? 537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.930 136.780 79.152  1.00 31.32 ? 537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 150.301 138.010 78.838  1.00 43.54 ? 537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 149.237 134.198 80.020  1.00 30.40 ? 538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 149.076 132.740 80.000  1.00 33.09 ? 538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 150.150 132.074 79.153  1.00 38.13 ? 538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 150.507 132.553 78.075  1.00 36.40 ? 538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.680 132.546 79.397  1.00 32.09 ? 538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.981 133.847 79.624  1.00 31.18 ? 538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 148.041 134.894 79.518  1.00 32.34 ? 538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.664 130.953 79.656  1.00 41.73 ? 539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.679 130.181 78.953  1.00 39.47 ? 539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 151.094 129.072 78.089  1.00 41.95 ? 539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.840 128.439 77.334  1.00 44.96 ? 539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.673 129.581 79.952  1.00 40.52 ? 539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 153.893 130.450 80.193  1.00 41.16 ? 539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 154.329 130.408 81.646  1.00 40.56 ? 539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 155.216 131.595 81.979  1.00 43.89 ? 539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 154.493 132.888 81.824  1.00 43.08 ? 539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 149.792 128.823 78.180  1.00 39.62 ? 540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 149.118 127.828 77.360  1.00 37.96 ? 540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 148.204 128.524 76.363  1.00 42.02 ? 540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 147.546 129.514 76.696  1.00 46.43 ? 540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.308 126.857 78.222  1.00 37.93 ? 540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 149.148 126.022 79.159  1.00 41.62 ? 540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 149.465 126.479 80.431  1.00 41.00 ? 540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.627 124.779 78.772  1.00 40.53 ? 540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 150.234 125.720 81.291  1.00 40.30 ? 540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.396 124.013 79.624  1.00 38.00 ? 540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 150.697 124.488 80.883  1.00 41.90 ? 540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.463 123.728 81.735  1.00 44.18 ? 540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 148.171 128.005 75.134  1.00 44.74 ? 541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 147.311 128.593 74.114  1.00 41.66 ? 541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 145.845 128.510 74.518  1.00 41.02 ? 541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 145.075 129.448 74.285  1.00 41.08 ? 541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.539 127.901 72.770  1.00 44.47 ? 541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 147.159 128.748 71.569  1.00 43.34 ? 541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 147.507 130.211 71.757  1.00 49.38 ? 541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 148.658 130.505 72.145  1.00 47.30 ? 541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 146.631 131.069 71.518  1.00 52.24 ? 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.440 127.392 75.124  1.00 40.50 ? 542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 144.057 127.255 75.566  1.00 37.99 ? 542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.698 128.322 76.592  1.00 39.01 ? 542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 142.618 128.920 76.525  1.00 39.17 ? 542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 143.826 125.859 76.144  1.00 38.81 ? 542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.427 125.646 76.694  1.00 40.89 ? 542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.202 124.200 77.100  1.00 37.30 ? 542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 140.792 123.992 77.626  1.00 39.48 ? 542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 140.503 122.558 77.895  1.00 39.92 ? 542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.590 128.573 77.552  1.00 36.30 ? 543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 144.328 129.602 78.551  1.00 33.83 ? 543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 144.403 130.988 77.924  1.00 30.83 ? 543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.569 131.856 78.204  1.00 34.63 ? 543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 145.302 129.459 79.734  1.00 31.87 ? 543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 145.130 128.094 80.400  1.00 35.39 ? 543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 145.088 130.579 80.737  1.00 31.48 ? 543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 143.695 127.752 80.731  1.00 31.57 ? 543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 145.402 131.221 77.069  1.00 33.09 ? 544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 145.529 132.522 76.423  1.00 37.65 ? 544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 144.300 132.856 75.590  1.00 39.42 ? 544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.959 134.033 75.431  1.00 40.99 ? 544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.786 132.558 75.553  1.00 35.91 ? 544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.624 131.839 75.051  1.00 43.05 ? 545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 142.419 132.085 74.269  1.00 41.41 ? 545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 141.256 132.519 75.150  1.00 40.66 ? 545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 140.411 133.308 74.714  1.00 43.34 ? 545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 142.047 130.835 73.473  1.00 42.14 ? 545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 142.780 130.750 72.151  1.00 45.30 ? 545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 143.082 131.769 71.530  1.00 45.27 ? 545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 143.074 129.531 71.714  1.00 43.65 ? 545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 141.193 132.017 76.386  1.00 36.33 ? 546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 140.129 132.427 77.296  1.00 35.08 ? 546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 140.175 133.923 77.571  1.00 36.30 ? 546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 139.134 134.542 77.812  1.00 42.81 ? 546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 140.230 131.645 78.605  1.00 37.78 ? 546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 140.056 130.130 78.509  1.00 35.08 ? 546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 140.254 129.487 79.870  1.00 32.85 ? 546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.692 129.780 77.940  1.00 33.23 ? 546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 141.364 134.518 77.537  1.00 35.63 ? 547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 141.536 135.943 77.773  1.00 34.26 ? 547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 141.461 136.765 76.494  1.00 34.34 ? 547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 141.679 137.980 76.540  1.00 41.84 ? 547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.868 136.203 78.483  1.00 35.24 ? 547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.904 135.708 79.900  1.00 36.31 ? 547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 142.408 136.486 80.932  1.00 33.10 ? 547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 143.428 134.463 80.199  1.00 30.43 ? 547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 142.438 136.032 82.236  1.00 30.24 ? 547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 143.460 134.005 81.501  1.00 31.27 ? 547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.966 134.791 82.520  1.00 32.67 ? 547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 141.166 136.136 75.358  1.00 43.06 ? 548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 141.028 136.878 74.113  1.00 43.82 ? 548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 139.919 137.914 74.238  1.00 46.10 ? 548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 138.861 137.651 74.815  1.00 49.14 ? 548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 140.733 135.925 72.953  1.00 45.60 ? 548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 140.734 136.574 71.570  1.00 45.56 ? 548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 141.958 137.438 71.298  1.00 48.72 ? 548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 142.804 137.605 72.201  1.00 46.81 ? 548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 142.070 137.957 70.167  1.00 51.28 ? 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 140.169 139.102 73.691  1.00 42.07 ? 549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 139.278 140.227 73.857  1.00 37.87 ? 549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 139.528 141.045 75.103  1.00 40.82 ? 549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.884 142.087 75.282  1.00 44.34 ? 549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 140.439 140.608 75.967  1.00 42.38 ? 550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.815 141.326 77.174  1.00 38.69 ? 550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 142.301 141.642 77.120  1.00 39.92 ? 550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 143.107 140.807 76.696  1.00 42.16 ? 550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 140.499 140.505 78.430  1.00 34.47 ? 550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 139.298 141.000 79.217  1.00 40.49 ? 550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.976 140.016 80.693  1.00 49.34 ? 550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.925 138.365 80.001  1.00 41.03 ? 550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.663 142.848 77.544  1.00 37.35 ? 551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 144.062 143.252 77.563  1.00 32.69 ? 551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.720 142.735 78.837  1.00 36.52 ? 551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 144.318 143.106 79.945  1.00 37.67 ? 551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 144.184 144.770 77.470  1.00 36.67 ? 551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 145.577 145.275 77.674  1.00 39.24 ? 551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 146.592 145.043 76.771  1.00 37.67 ? 551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 146.127 145.997 78.680  1.00 40.22 ? 551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.706 145.601 77.210  1.00 40.74 ? 551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 147.451 146.186 78.366  1.00 42.59 ? 551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.725 141.882 78.680  1.00 33.92 ? 552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 146.467 141.329 79.809  1.00 30.56 ? 552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 147.637 142.265 80.102  1.00 30.98 ? 552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 148.487 142.464 79.221  1.00 37.94 ? 552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.962 139.908 79.517  1.00 33.70 ? 552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.797 139.021 79.074  1.00 31.69 ? 552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.650 139.322 80.741  1.00 30.72 ? 552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 146.208 137.620 78.693  1.00 31.52 ? 552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 147.714 142.853 81.294  1.00 36.41 ? 553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.807 143.789 81.579  1.00 32.19 ? 553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 150.166 143.129 81.409  1.00 31.07 ? 553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 150.367 141.969 81.774  1.00 33.31 ? 553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 148.555 144.192 83.035  1.00 28.23 ? 553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 147.095 143.974 83.235  1.00 25.80 ? 553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.749 142.775 82.403  1.00 32.22 ? 553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 151.103 143.885 80.849  1.00 37.00 ? 554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 152.466 143.427 80.650  1.00 34.57 ? 554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 153.384 144.073 81.683  1.00 27.83 ? 554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.948 144.806 82.573  1.00 29.94 ? 554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.939 143.739 79.228  1.00 29.67 ? 554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 153.045 145.157 79.057  1.00 33.54 ? 554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.961 143.182 78.208  1.00 29.42 ? 554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 154.682 143.790 81.561  1.00 33.36 ? 555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 155.652 144.430 82.441  1.00 30.19 ? 555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 155.673 145.938 82.238  1.00 30.46 ? 555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.892 146.688 83.194  1.00 30.85 ? 555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 157.045 143.842 82.217  1.00 33.15 ? 555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 157.354 143.855 80.818  1.00 38.14 ? 555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 157.108 142.413 82.736  1.00 29.63 ? 555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 155.455 146.402 81.005  1.00 32.60 ? 556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 155.366 147.839 80.761  1.00 27.27 ? 556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 154.137 148.439 81.435  1.00 30.19 ? 556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 154.208 149.530 82.013  1.00 33.86 ? 556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 155.346 148.114 79.258  1.00 32.88 ? 556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 155.576 149.570 78.888  1.00 32.99 ? 556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 156.656 150.223 79.730  1.00 40.00 ? 556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 156.356 151.229 80.405  1.00 37.66 ? 556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 157.804 149.730 79.715  1.00 41.27 ? 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 153.001 147.741 81.369  1.00 32.95 ? 557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.804 148.219 82.052  1.00 27.38 ? 557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 152.020 148.274 83.557  1.00 28.61 ? 557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 151.583 149.220 84.222  1.00 32.50 ? 557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 150.610 147.327 81.713  1.00 30.45 ? 557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 150.269 147.346 80.238  1.00 36.09 ? 557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 150.260 148.444 79.644  1.00 37.91 ? 557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 150.007 146.264 79.673  1.00 37.91 ? 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 152.692 147.267 84.115  1.00 24.42 ? 558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.979 147.284 85.543  1.00 21.42 ? 558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.966 148.386 85.905  1.00 29.67 ? 558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.859 148.974 86.983  1.00 30.80 ? 558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 153.503 145.924 85.991  1.00 19.36 ? 558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 152.420 144.922 86.248  1.00 21.76 ? 558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 152.033 143.908 85.425  1.00 21.95 ? 558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 151.586 144.835 87.411  1.00 18.35 ? 558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 151.012 143.194 86.000  1.00 25.03 ? 558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 150.719 143.743 87.221  1.00 20.33 ? 558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 151.491 145.573 88.594  1.00 23.54 ? 558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.768 143.371 88.168  1.00 16.43 ? 558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 150.545 145.203 89.533  1.00 17.21 ? 558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.697 144.112 89.314  1.00 10.44 ? 558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.927 148.683 85.028  1.00 31.65 ? 559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.820 149.813 85.269  1.00 27.07 ? 559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 155.044 151.123 85.291  1.00 27.97 ? 559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 155.274 151.982 86.153  1.00 32.21 ? 559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.909 149.858 84.198  1.00 28.23 ? 559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 158.133 149.019 84.511  1.00 28.41 ? 559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.940 148.742 83.253  1.00 30.82 ? 559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.347 147.280 83.163  1.00 30.92 ? 559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.621 147.013 83.886  1.00 34.07 ? 559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 154.119 151.292 84.345  1.00 28.19 ? 560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 153.291 152.493 84.327  1.00 23.26 ? 560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 152.444 152.593 85.589  1.00 30.49 ? 560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 152.307 153.675 86.169  1.00 34.68 ? 560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 152.404 152.503 83.083  1.00 28.33 ? 560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 153.148 152.241 81.787  1.00 34.39 ? 560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 153.268 153.505 80.955  1.00 35.43 ? 560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 153.354 153.177 79.475  1.00 34.68 ? 560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 152.397 152.104 79.090  1.00 34.77 ? 560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.860 151.475 86.025  1.00 32.14 ? 561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 151.059 151.487 87.244  1.00 25.21 ? 561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.916 151.795 88.465  1.00 26.06 ? 561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 151.471 152.494 89.381  1.00 30.96 ? 561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 150.338 150.151 87.418  1.00 24.45 ? 561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 149.526 150.006 88.708  1.00 24.63 ? 561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 148.433 151.062 88.773  1.00 25.61 ? 561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.936 148.613 88.825  1.00 19.48 ? 561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 153.140 151.269 88.503  1.00 24.34 ? 562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 154.054 151.568 89.599  1.00 29.12 ? 562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 154.371 153.056 89.653  1.00 29.38 ? 562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 154.355 153.671 90.726  1.00 31.79 ? 562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 155.330 150.742 89.435  1.00 27.82 ? 562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 156.450 151.084 90.395  1.00 24.32 ? 562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 157.689 150.269 90.065  1.00 24.94 ? 562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.819 150.546 91.036  1.00 28.29 ? 562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.841 149.467 91.002  1.00 33.18 ? 562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 154.655 153.657 88.495  1.00 29.64 ? 563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 154.908 155.094 88.455  1.00 27.02 ? 563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 153.676 155.882 88.885  1.00 23.40 ? 563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 153.783 156.868 89.624  1.00 37.33 ? 563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 155.353 155.510 87.054  1.00 30.13 ? 563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 152.495 155.457 88.433  1.00 28.06 ? 564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 151.262 156.141 88.806  1.00 27.54 ? 564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 151.028 156.076 90.311  1.00 29.61 ? 564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 150.628 157.069 90.929  1.00 30.43 ? 564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 150.088 155.528 88.044  1.00 25.25 ? 564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 148.779 156.222 88.277  1.00 26.14 ? 564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 148.446 157.360 87.565  1.00 24.82 ? 564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 147.876 155.728 89.201  1.00 28.58 ? 564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 147.241 157.996 87.777  1.00 29.91 ? 564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 146.670 156.360 89.416  1.00 30.30 ? 564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 146.351 157.496 88.704  1.00 29.02 ? 564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 151.267 154.912 90.916  1.00 26.58 ? 565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 151.118 154.776 92.360  1.00 25.02 ? 565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 152.127 155.656 93.085  1.00 30.31 ? 565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 151.785 156.351 94.049  1.00 34.28 ? 565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 151.252 153.300 92.777  1.00 25.45 ? 565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 151.303 153.181 94.290  1.00 21.98 ? 565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 150.102 152.484 92.212  1.00 24.32 ? 565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 153.383 155.644 92.634  1.00 31.54 ? 566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 154.387 156.514 93.236  1.00 27.98 ? 566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.951 157.972 93.174  1.00 32.56 ? 566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 154.202 158.745 94.106  1.00 38.96 ? 566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 155.733 156.325 92.538  1.00 26.75 ? 566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 153.299 158.365 92.081  1.00 35.03 ? 567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.841 159.744 91.948  1.00 31.84 ? 567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 151.682 160.042 92.894  1.00 34.60 ? 567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 151.691 161.056 93.600  1.00 40.33 ? 567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 152.433 160.021 90.502  1.00 31.03 ? 567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.321 161.495 90.165  1.00 37.45 ? 567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 152.941 161.835 88.826  1.00 42.76 ? 567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 154.034 162.440 88.811  1.00 42.85 ? 567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 152.335 161.498 87.787  1.00 41.56 ? 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 150.677 159.167 92.926  1.00 37.42 ? 568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 149.419 159.466 93.594  1.00 30.32 ? 568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 149.158 158.630 94.838  1.00 30.71 ? 568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 148.234 158.953 95.592  1.00 37.74 ? 568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 148.251 159.285 92.614  1.00 27.15 ? 568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 148.416 160.051 91.338  1.00 33.19 ? 568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 148.973 159.498 90.205  1.00 34.83 ? 568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 148.115 161.332 91.023  1.00 31.93 ? 568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 148.998 160.403 89.244  1.00 31.68 ? 568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 148.482 161.525 89.714  1.00 35.00 ? 568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 149.933 157.582 95.079  1.00 25.45 ? 569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 149.709 156.751 96.240  1.00 24.13 ? 569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 148.597 155.740 96.033  1.00 25.45 ? 569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 148.137 155.479 94.919  1.00 31.68 ? 569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 148.163 155.158 97.148  1.00 20.61 ? 570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 147.147 154.114 97.132  1.00 20.61 ? 570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 146.127 154.395 98.225  1.00 24.28 ? 570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 146.501 154.684 99.364  1.00 28.37 ? 570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 147.782 152.733 97.327  1.00 28.02 ? 570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 148.239 152.080 96.031  1.00 13.66 ? 570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 148.251 150.281 96.089  1.00 36.82 ? 570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 146.501 149.927 96.078  1.00 22.63 ? 570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 144.843 154.317 97.872  1.00 16.87 ? 571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 143.781 154.649 98.816  1.00 6.12  ? 571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 143.535 153.546 99.837  1.00 1.89  ? 571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 143.090 153.833 100.953 1.00 15.95 ? 571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 142.485 154.952 98.063  1.00 19.17 ? 571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 141.400 155.549 98.928  1.00 20.50 ? 571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 141.445 156.883 99.310  1.00 18.47 ? 571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 140.332 154.778 99.366  1.00 10.97 ? 571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 140.455 157.430 100.100 1.00 21.45 ? 571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 139.338 155.317 100.156 1.00 14.54 ? 571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 139.404 156.645 100.520 1.00 27.11 ? 571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 138.418 157.189 101.307 1.00 22.71 ? 571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 143.806 152.295 99.484  1.00 16.56 ? 572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 143.509 151.154 100.339 1.00 8.34  ? 572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 144.804 150.492 100.784 1.00 7.83  ? 572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 145.684 150.224 99.961  1.00 24.05 ? 572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 142.628 150.134 99.612  1.00 7.09  ? 572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 141.386 150.718 99.014  1.00 6.52  ? 572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 141.352 151.254 97.746  1.00 12.94 ? 572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 140.132 150.842 99.508  1.00 8.49  ? 572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 140.132 151.689 97.486  1.00 11.27 ? 572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 139.372 151.449 98.539  1.00 11.83 ? 572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.917 150.235 102.088 1.00 8.36  ? 573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 146.048 149.463 102.590 1.00 3.50  ? 573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.931 147.998 102.196 1.00 7.58  ? 573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.948 147.315 102.040 1.00 19.77 ? 573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 146.149 149.600 104.108 1.00 6.56  ? 573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.914 149.300 104.732 1.00 21.83 ? 573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 144.706 147.506 102.033 1.00 8.95  ? 574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 144.443 146.141 101.611 1.00 0.00  ? 574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 143.258 146.147 100.660 1.00 1.66  ? 574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 142.286 146.875 100.877 1.00 11.30 ? 574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 144.171 145.234 102.814 1.00 4.56  ? 574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 145.306 145.231 103.806 1.00 0.00  ? 574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 146.361 144.340 103.678 1.00 8.11  ? 574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.338 146.138 104.857 1.00 0.00  ? 574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 147.405 144.342 104.574 1.00 4.62  ? 574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.380 146.147 105.758 1.00 0.00  ? 574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 147.410 145.246 105.612 1.00 0.00  ? 574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 148.451 145.247 106.508 1.00 8.55  ? 574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 143.346 145.345 99.607  1.00 10.85 ? 575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 142.334 145.340 98.560  1.00 0.04  ? 575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.708 143.978 98.318  1.00 5.67  ? 575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 140.496 143.894 98.113  1.00 16.34 ? 575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.937 145.851 97.245  1.00 9.59  ? 575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 143.381 147.300 97.274  1.00 5.68  ? 575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 144.410 147.563 96.189  1.00 9.26  ? 575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.654 146.844 96.436  1.00 15.70 ? 575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 146.002 145.718 95.828  1.00 12.15 ? 575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 145.219 145.149 94.927  1.00 11.04 ? 575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 147.164 145.149 96.133  1.00 6.02  ? 575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 142.497 142.907 98.337  1.00 15.50 ? 576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 142.059 141.598 97.873  1.00 8.00  ? 576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 142.134 140.581 99.002  1.00 0.00  ? 576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 143.178 140.434 99.644  1.00 17.06 ? 576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.913 141.129 96.692  1.00 6.19  ? 576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.937 142.066 95.483  1.00 4.56  ? 576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.782 141.488 94.361  1.00 10.67 ? 576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.524 142.356 95.007  1.00 2.13  ? 576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 141.025 139.884 99.233  1.00 1.90  ? 577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.991 138.730 100.118 1.00 5.66  ? 577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.891 137.804 99.623  1.00 12.97 ? 577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.809 138.263 99.249  1.00 19.66 ? 577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.754 139.131 101.579 1.00 6.49  ? 577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 139.022 139.369 102.043 1.00 30.39 ? 577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 140.172 136.507 99.614  1.00 2.38  ? 578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 139.253 135.514 99.062  1.00 4.34  ? 578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.584 134.821 100.244 1.00 3.31  ? 578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 139.117 133.878 100.830 1.00 10.58 ? 578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.965 134.533 98.134  1.00 12.38 ? 578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.610 135.289 96.970  1.00 4.83  ? 578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.991 133.487 97.618  1.00 7.14  ? 578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 141.309 134.404 95.975  1.00 6.94  ? 578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 137.397 135.299 100.596 1.00 13.36 ? 579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.606 134.715 101.663 1.00 3.78  ? 579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.844 133.490 101.166 1.00 20.57 ? 579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.712 133.273 99.960  1.00 23.45 ? 579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.636 135.747 102.224 1.00 4.12  ? 579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.343 132.662 102.086 1.00 25.65 ? 580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.639 131.438 101.666 1.00 16.82 ? 580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.434 131.681 100.769 1.00 20.33 ? 580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 133.186 130.875 99.863  1.00 31.10 ? 580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.227 130.795 103.000 1.00 12.24 ? 580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.471 131.836 104.053 1.00 13.13 ? 580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.561 132.704 103.539 1.00 13.70 ? 580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.673 132.757 100.981 1.00 19.82 ? 581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.469 133.035 100.193 1.00 30.23 ? 581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.491 131.857 100.271 1.00 28.59 ? 581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 130.181 131.193 99.281  1.00 33.19 ? 581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.812 133.353 98.732  1.00 29.54 ? 581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.840 132.141 97.970  1.00 18.90 ? 581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 133.154 134.053 98.629  1.00 23.55 ? 581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 130.018 131.614 101.489 1.00 31.94 ? 582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 129.275 130.403 101.768 1.00 27.15 ? 582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.915 130.291 101.112 1.00 32.97 ? 582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.722 129.447 100.232 1.00 38.73 ? 582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.966 131.136 101.511 1.00 33.28 ? 583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.586 130.969 101.070 1.00 35.83 ? 583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 125.228 131.816 99.858  1.00 34.23 ? 583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.263 131.497 99.156  1.00 35.35 ? 583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.623 131.296 102.215 1.00 39.63 ? 583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 124.615 130.263 103.184 1.00 42.36 ? 583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.979 132.886 99.588  1.00 33.40 ? 584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.671 133.736 98.446  1.00 29.00 ? 584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 126.091 133.116 97.124  1.00 26.22 ? 584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.715 133.628 96.065  1.00 32.21 ? 584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.322 135.124 98.614  1.00 30.65 ? 584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 125.507 136.180 97.869  1.00 31.33 ? 584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 127.757 135.105 98.124  1.00 28.54 ? 584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 124.025 136.114 98.141  1.00 26.82 ? 584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.859 132.025 97.156  1.00 25.17 ? 585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.236 131.354 95.918  1.00 22.39 ? 585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 126.033 130.708 95.243  1.00 27.91 ? 585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.989 130.625 94.011  1.00 23.29 ? 585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.315 130.308 96.194  1.00 21.47 ? 585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.861 129.342 97.124  1.00 27.37 ? 585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 125.057 130.243 96.026  1.00 29.33 ? 586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.852 129.666 95.438  1.00 29.17 ? 586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 123.107 130.691 94.596  1.00 26.67 ? 586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.656 130.384 93.487  1.00 29.85 ? 586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.940 129.119 96.536  1.00 31.88 ? 586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.499 127.923 97.267  1.00 34.69 ? 586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.545 126.676 96.661  1.00 34.84 ? 586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.979 128.040 98.563  1.00 32.82 ? 586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.053 125.580 97.324  1.00 34.44 ? 586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.489 126.949 99.234  1.00 32.24 ? 586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.524 125.721 98.610  1.00 34.20 ? 586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.032 124.630 99.275  1.00 36.60 ? 586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.973 131.916 95.103  1.00 26.92 ? 587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 122.267 132.957 94.363  1.00 24.89 ? 587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.961 133.226 93.036  1.00 27.85 ? 587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.310 133.418 92.002  1.00 30.31 ? 587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 122.158 134.234 95.214  1.00 26.14 ? 587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.497 135.345 94.419  1.00 28.30 ? 587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.397 133.951 96.496  1.00 27.68 ? 587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.292 133.249 93.045  1.00 31.94 ? 588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 125.066 133.487 91.835  1.00 21.23 ? 588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 125.202 132.246 90.967  1.00 24.26 ? 588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.750 132.342 89.863  1.00 28.76 ? 588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.456 134.013 92.202  1.00 21.98 ? 588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.451 135.388 92.848  1.00 20.05 ? 588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.687 136.499 91.849  1.00 18.65 ? 588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.537 136.386 90.968  1.00 23.61 ? 588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.933 137.583 91.979  1.00 26.61 ? 588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.718 131.095 91.431  1.00 27.32 ? 589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.863 129.832 90.712  1.00 21.98 ? 589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.329 129.576 90.372  1.00 22.16 ? 589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.686 129.210 89.251  1.00 23.53 ? 589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.987 129.812 89.458  1.00 22.22 ? 589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 124.395 130.799 88.528  1.00 29.30 ? 589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 127.187 129.781 91.367  1.00 27.19 ? 590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.625 129.663 91.204  1.00 23.59 ? 590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 129.193 128.754 92.282  1.00 17.02 ? 590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.604 128.594 93.354  1.00 26.80 ? 590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 129.307 131.037 91.270  1.00 19.75 ? 590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.704 131.345 92.593  1.00 23.22 ? 590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.341 128.152 91.987  1.00 19.89 ? 591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 131.047 127.378 92.994  1.00 17.09 ? 591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.612 128.303 94.068  1.00 15.48 ? 591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.842 129.494 93.845  1.00 19.01 ? 591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.169 126.554 92.360  1.00 16.11 ? 591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.229 127.422 91.943  1.00 25.14 ? 591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.650 125.776 91.161  1.00 22.01 ? 591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.830 127.739 95.251  1.00 14.93 ? 592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 132.221 128.529 96.411  1.00 13.02 ? 592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.685 128.938 96.303  1.00 21.17 ? 592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.571 128.081 96.214  1.00 23.38 ? 592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.975 127.742 97.696  1.00 17.41 ? 592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.932 130.241 96.315  1.00 25.76 ? 593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 135.283 130.799 96.384  1.00 8.84  ? 593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 136.137 130.185 95.274  1.00 11.68 ? 593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.638 129.858 94.193  1.00 23.67 ? 593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.828 130.601 97.788  1.00 20.48 ? 593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 137.033 131.318 97.980  1.00 26.35 ? 593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.435 130.025 95.533  1.00 16.17 ? 594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.355 129.418 94.581  1.00 14.92 ? 594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.636 127.958 94.921  1.00 12.07 ? 594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.469 127.323 94.270  1.00 16.26 ? 594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.663 130.221 94.492  1.00 19.74 ? 594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 139.396 131.603 93.918  1.00 13.82 ? 594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 140.319 130.325 95.860  1.00 15.47 ? 594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.959 127.414 95.928  1.00 11.93 ? 595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 138.121 126.018 96.284  1.00 11.57 ? 595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.462 125.122 95.240  1.00 20.67 ? 595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.527 125.535 94.551  1.00 29.55 ? 595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.508 125.742 97.654  1.00 11.70 ? 595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 138.211 126.417 98.821  1.00 24.50 ? 595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 139.850 125.746 99.150  1.00 31.79 ? 595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 140.842 126.729 98.037  1.00 15.77 ? 595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.940 123.889 95.100  1.00 24.82 ? 596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.216 122.911 94.285  1.00 16.68 ? 596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.926 122.487 94.970  1.00 19.22 ? 596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.785 122.545 96.193  1.00 22.79 ? 596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.200 121.744 94.169  1.00 15.41 ? 596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.047 121.852 95.387  1.00 18.68 ? 596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.156 123.319 95.706  1.00 26.44 ? 596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.968 122.056 94.149  1.00 22.75 ? 597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.663 121.666 94.663  1.00 27.22 ? 597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.803 120.449 95.568  1.00 25.80 ? 597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.649 119.572 95.350  1.00 29.83 ? 597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.688 121.387 93.506  1.00 25.54 ? 597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.077 120.093 92.789  1.00 25.37 ? 597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.666 122.556 92.537  1.00 23.49 ? 597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 131.967 119.489 91.971  1.00 25.95 ? 597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 132.960 120.393 96.600  1.00 33.24 ? 598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 132.979 119.258 97.515  1.00 36.15 ? 598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.201 118.075 96.953  1.00 37.11 ? 598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.648 116.928 97.059  1.00 39.74 ? 598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.412 119.667 98.873  1.00 35.42 ? 598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.443 119.741 99.982  1.00 35.26 ? 598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.858 120.693 101.393 1.00 55.84 ? 598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 132.740 122.326 100.671 1.00 37.43 ? 598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.039 118.335 96.358  1.00 37.84 ? 599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.207 117.302 95.763  1.00 33.20 ? 599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.751 117.752 94.384  1.00 35.94 ? 599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.590 118.947 94.127  1.00 40.13 ? 599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 128.981 116.992 96.632  1.00 35.05 ? 599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.139 117.366 98.095  1.00 39.30 ? 599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 127.919 117.008 98.920  1.00 42.47 ? 599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.783 117.531 100.045 1.00 41.41 ? 599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.094 116.200 98.443  1.00 44.46 ? 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.548 116.780 93.494  1.00 37.36 ? 600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 128.991 117.094 92.182  1.00 30.77 ? 600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.529 117.504 92.293  1.00 31.76 ? 600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.094 118.464 91.647  1.00 34.02 ? 600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.143 115.898 91.245  1.00 31.74 ? 600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 130.511 115.784 90.605  1.00 34.72 ? 600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 130.524 114.703 89.545  1.00 32.25 ? 600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 131.843 114.533 88.949  1.00 27.20 ? 600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 132.803 113.777 89.462  1.00 33.17 ? 600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 132.629 113.113 90.592  1.00 34.45 ? 600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 133.967 113.688 88.827  1.00 32.94 ? 600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 126.757 116.786 93.104  1.00 41.06 ? 601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.362 117.110 93.372  1.00 40.39 ? 601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.205 117.247 94.878  1.00 37.86 ? 601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.566 116.334 95.629  1.00 41.19 ? 601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.402 116.046 92.816  1.00 38.37 ? 601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.658 115.835 91.323  1.00 36.86 ? 601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 122.960 116.455 93.058  1.00 39.32 ? 601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 123.764 114.798 90.689  1.00 40.47 ? 601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.674 118.383 95.317  1.00 43.07 ? 602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.579 118.709 96.735  1.00 45.74 ? 602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.186 118.341 97.232  1.00 47.42 ? 602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.193 118.954 96.830  1.00 49.18 ? 602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 124.876 120.191 96.951  1.00 44.85 ? 602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.549 120.718 98.332  1.00 46.79 ? 602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.640 121.619 98.873  1.00 49.55 ? 602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.324 122.276 98.059  1.00 50.93 ? 602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 125.811 121.680 100.107 1.00 49.45 ? 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.113 117.339 98.103  1.00 53.21 ? 603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 121.854 116.886 98.678  1.00 52.63 ? 603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.679 117.521 100.051 1.00 52.59 ? 603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.526 117.343 100.933 1.00 53.99 ? 603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.816 115.362 98.787  1.00 53.98 ? 603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.536 114.822 99.404  1.00 54.68 ? 603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.661 113.377 99.844  1.00 57.28 ? 603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 120.642 112.483 98.972  1.00 57.07 ? 603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.779 113.134 101.064 1.00 56.37 ? 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.585 118.254 100.229 1.00 55.60 ? 604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.300 118.930 101.483 1.00 54.99 ? 604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 118.827 118.771 101.827 1.00 56.22 ? 604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 117.977 118.631 100.944 1.00 55.39 ? 604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.668 120.417 101.412 1.00 57.47 ? 604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 122.155 120.672 101.231 1.00 55.20 ? 604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.897 120.549 102.551 1.00 54.94 ? 604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 124.343 120.513 102.373 1.00 54.17 ? 604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.001 119.539 101.760 1.00 55.03 ? 604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 124.372 118.494 101.249 1.00 56.51 ? 604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.325 119.615 101.656 1.00 55.14 ? 604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.535 118.790 103.123 1.00 62.18 ? 605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.174 118.676 103.630 1.00 65.27 ? 605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 116.748 120.018 104.210 1.00 63.58 ? 605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.351 120.503 105.173 1.00 62.70 ? 605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.069 117.573 104.684 1.00 63.47 ? 605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 115.722 117.501 105.170 1.00 63.37 ? 605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 118.013 117.846 105.847 1.00 63.16 ? 605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.718 120.614 103.618 1.00 62.34 ? 606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.128 121.851 104.110 1.00 64.18 ? 606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 113.705 121.555 104.554 1.00 65.17 ? 606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 112.924 120.970 103.796 1.00 63.38 ? 606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.152 122.942 103.035 1.00 62.44 ? 606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.548 123.419 102.697 1.00 61.54 ? 606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.268 124.204 103.587 1.00 61.67 ? 606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.148 123.076 101.493 1.00 59.87 ? 606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.544 124.638 103.286 1.00 62.27 ? 606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.424 123.505 101.184 1.00 61.73 ? 606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 119.117 124.286 102.084 1.00 64.14 ? 606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.388 124.717 101.780 1.00 63.86 ? 606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 113.371 121.956 105.776 1.00 68.83 ? 607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.111 121.514 106.348 1.00 68.01 ? 607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.109 120.003 106.459 1.00 69.32 ? 607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.039 119.397 107.004 1.00 68.82 ? 607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.056 119.376 105.938 1.00 70.48 ? 608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 110.972 117.922 105.881 1.00 71.30 ? 608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.107 117.388 104.461 1.00 72.99 ? 608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.876 116.194 104.233 1.00 72.97 ? 608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.662 117.434 106.507 1.00 72.60 ? 608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.615 117.658 108.008 1.00 73.19 ? 608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.622 118.001 108.628 1.00 72.23 ? 608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.443 117.460 108.599 1.00 72.85 ? 608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.474 118.235 103.504 1.00 70.53 ? 609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 111.713 117.823 102.129 1.00 68.79 ? 609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.177 118.049 101.783 1.00 67.87 ? 609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 113.748 119.095 102.109 1.00 67.63 ? 609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 110.817 118.593 101.152 1.00 67.60 ? 609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 111.100 119.980 101.185 1.00 67.40 ? 609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.781 117.066 101.124 1.00 60.37 ? 610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.181 117.130 100.736 1.00 60.85 ? 610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.305 117.668 99.317  1.00 59.67 ? 610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.459 117.396 98.460  1.00 57.44 ? 610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.839 115.753 100.837 1.00 61.21 ? 610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 115.805 114.948 99.552  1.00 59.06 ? 610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.706 113.729 99.649  1.00 60.92 ? 610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 116.523 113.014 100.978 1.00 60.42 ? 610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 115.134 112.507 101.147 1.00 59.93 ? 610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.365 118.436 99.076  1.00 58.18 ? 611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.595 119.077 97.791  1.00 55.98 ? 611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.971 118.695 97.267  1.00 52.58 ? 611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.895 118.424 98.039  1.00 54.63 ? 611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.488 120.602 97.896  1.00 55.57 ? 611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 117.185 121.052 99.064  1.00 58.06 ? 611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 115.031 121.025 97.991  1.00 53.48 ? 611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.098 118.676 95.944  1.00 47.77 ? 612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.341 118.318 95.275  1.00 48.23 ? 612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.844 119.512 94.479  1.00 47.48 ? 612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.095 120.099 93.692  1.00 48.33 ? 612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.141 117.112 94.355  1.00 49.47 ? 612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 118.702 115.865 95.085  1.00 50.46 ? 612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 119.602 115.124 95.837  1.00 50.76 ? 612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 117.385 115.430 95.024  1.00 51.82 ? 612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 119.203 113.984 96.507  1.00 53.21 ? 612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 116.977 114.292 95.690  1.00 52.82 ? 612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 117.890 113.572 96.430  1.00 53.27 ? 612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.488 112.437 97.096  1.00 52.85 ? 612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.110 119.867 94.683  1.00 43.41 ? 613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.732 120.988 93.979  1.00 37.57 ? 613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.937 120.510 93.184  1.00 36.56 ? 613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.034 120.352 93.750  1.00 39.27 ? 613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.145 122.086 94.957  1.00 34.69 ? 613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.814 123.263 94.286  1.00 36.41 ? 613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.160 123.988 93.300  1.00 38.38 ? 613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.101 123.646 94.635  1.00 35.25 ? 613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.767 125.063 92.684  1.00 39.18 ? 613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.716 124.718 94.024  1.00 38.00 ? 613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 124.045 125.424 93.049  1.00 41.26 ? 613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.654 126.494 92.438  1.00 41.73 ? 613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.794 120.264 91.886  1.00 36.10 ? 614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 123.971 119.972 91.065  1.00 35.12 ? 614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.868 121.193 90.954  1.00 37.62 ? 614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.410 122.337 90.991  1.00 37.53 ? 614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.376 119.592 89.701  1.00 30.57 ? 614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 121.909 119.382 89.945  1.00 36.98 ? 614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.556 120.263 91.094  1.00 35.02 ? 614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.163 120.937 90.813  1.00 33.94 ? 615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 127.105 122.032 90.658  1.00 28.62 ? 615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.757 122.834 89.407  1.00 33.88 ? 615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.371 122.254 88.386  1.00 31.44 ? 615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.537 121.505 90.570  1.00 27.87 ? 615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.170 121.219 91.919  1.00 29.84 ? 615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.782 122.479 93.148  1.00 46.79 ? 615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.572 121.617 94.146  1.00 33.00 ? 615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.871 124.160 89.451  1.00 38.73 ? 616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.429 124.975 88.312  1.00 31.32 ? 616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.110 124.546 87.022  1.00 26.96 ? 616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.323 124.336 86.977  1.00 35.28 ? 616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.831 126.396 88.721  1.00 30.83 ? 616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.892 126.353 90.211  1.00 30.91 ? 616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.382 124.984 90.559  1.00 27.02 ? 616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.312 124.422 85.965  1.00 32.97 ? 617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.821 123.975 84.687  1.00 30.37 ? 617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.124 122.499 84.600  1.00 35.37 ? 617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.684 122.056 83.593  1.00 38.06 ? 617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.772 121.720 85.620  1.00 37.16 ? 618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.081 120.297 85.615  1.00 33.74 ? 618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.285 119.584 84.531  1.00 34.47 ? 618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.074 119.785 84.398  1.00 34.67 ? 618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.784 119.685 86.982  1.00 34.16 ? 618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.073 118.190 87.126  1.00 32.65 ? 618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.529 117.891 86.816  1.00 35.11 ? 618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 126.711 117.705 88.519  1.00 31.33 ? 618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 126.969 118.748 83.759  1.00 41.83 ? 619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.347 117.993 82.681  1.00 40.85 ? 619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.204 116.765 82.408  1.00 44.63 ? 619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.272 116.585 82.999  1.00 48.82 ? 619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.175 118.854 81.427  1.00 38.79 ? 619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 126.723 115.911 81.503  1.00 47.22 ? 620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 127.467 114.702 81.165  1.00 45.44 ? 620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 128.815 115.039 80.541  1.00 47.65 ? 620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 129.826 114.393 80.843  1.00 51.51 ? 620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 126.642 113.826 80.224  1.00 50.13 ? 620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 125.342 113.604 80.742  1.00 54.72 ? 620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 128.852 116.046 79.666  1.00 45.36 ? 621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.095 116.378 78.977  1.00 45.40 ? 621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.166 116.851 79.954  1.00 47.04 ? 621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.340 116.488 79.821  1.00 47.61 ? 621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.836 117.439 77.908  1.00 45.46 ? 621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 128.889 118.523 78.380  1.00 50.47 ? 621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.134 118.332 79.332  1.00 53.07 ? 621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 128.926 119.671 77.715  1.00 46.38 ? 621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 130.783 117.663 80.940  1.00 40.61 ? 622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.725 118.215 81.906  1.00 37.99 ? 622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.640 117.524 83.263  1.00 39.49 ? 622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.122 118.067 84.261  1.00 44.34 ? 622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.509 119.722 82.057  1.00 37.69 ? 622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.140 120.068 82.613  1.00 39.58 ? 622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.417 119.205 83.106  1.00 44.38 ? 622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.778 121.342 82.533  1.00 34.93 ? 622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.031 116.338 83.320  1.00 36.02 ? 623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 130.929 115.623 84.589  1.00 36.48 ? 623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.307 115.297 85.149  1.00 38.08 ? 623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.549 115.452 86.352  1.00 33.98 ? 623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.105 114.347 84.406  1.00 36.65 ? 623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.068 113.460 85.617  1.00 35.78 ? 623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.002 112.536 85.986  1.00 34.35 ? 623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.039 113.408 86.612  1.00 34.12 ? 623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 130.622 111.918 87.150  1.00 35.06 ? 623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.418 112.433 87.554  1.00 32.85 ? 623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 127.833 114.091 86.797  1.00 32.92 ? 623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.639 112.127 88.666  1.00 35.36 ? 623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.060 113.784 87.901  1.00 33.49 ? 623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.466 112.811 88.821  1.00 37.25 ? 623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.225 114.846 84.293  1.00 42.26 ? 624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 134.547 114.441 84.750  1.00 36.47 ? 624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.408 115.621 85.177  1.00 37.14 ? 624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.286 115.453 86.030  1.00 40.43 ? 624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.253 113.645 83.648  1.00 36.56 ? 624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 136.750 113.629 83.767  1.00 41.53 ? 624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 137.382 112.710 84.588  1.00 41.76 ? 624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 137.528 114.519 83.044  1.00 38.59 ? 624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 138.759 112.686 84.696  1.00 37.98 ? 624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 138.905 114.501 83.148  1.00 37.80 ? 624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 139.522 113.582 83.975  1.00 39.35 ? 624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.177 116.808 84.614  1.00 33.43 ? 625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 135.921 117.989 85.029  1.00 30.19 ? 625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.440 118.545 86.361  1.00 27.58 ? 625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.164 119.324 86.989  1.00 31.10 ? 625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.833 119.073 83.954  1.00 24.81 ? 625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.596 118.748 82.706  1.00 28.61 ? 625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.978 118.687 82.723  1.00 31.02 ? 625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 135.934 118.504 81.516  1.00 32.99 ? 625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.686 118.390 81.577  1.00 29.76 ? 625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.637 118.205 80.366  1.00 29.83 ? 625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.014 118.148 80.397  1.00 31.69 ? 625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.246 118.165 86.804  1.00 26.30 ? 626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.753 118.555 88.123  1.00 24.54 ? 626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.216 117.573 89.191  1.00 26.72 ? 626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.431 117.058 89.984  1.00 32.12 ? 626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.234 118.663 88.101  1.00 27.19 ? 626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.727 120.046 87.771  1.00 29.11 ? 626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.758 121.060 88.718  1.00 30.20 ? 626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.217 120.337 86.514  1.00 27.68 ? 626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.295 122.324 88.422  1.00 31.36 ? 626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.753 121.598 86.209  1.00 27.60 ? 626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.793 122.588 87.167  1.00 27.48 ? 626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.331 123.847 86.870  1.00 28.03 ? 626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.520 117.318 89.214  1.00 31.12 ? 627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.087 116.400 90.187  1.00 22.95 ? 627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 135.915 116.954 91.595  1.00 22.58 ? 627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.108 118.148 91.839  1.00 30.10 ? 627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.564 116.160 89.882  1.00 25.52 ? 627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.219 115.088 90.727  1.00 27.84 ? 627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 139.596 114.749 90.187  1.00 27.25 ? 627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.297 113.720 91.052  1.00 35.49 ? 627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 141.697 113.493 90.603  1.00 33.70 ? 627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.546 116.081 92.524  1.00 29.56 ? 628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.316 116.504 93.895  1.00 30.84 ? 628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.638 116.722 94.617  1.00 33.93 ? 628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.659 116.107 94.296  1.00 33.12 ? 628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.464 115.476 94.638  1.00 32.63 ? 628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.033 115.394 94.133  1.00 31.08 ? 628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.289 114.193 94.676  1.00 39.92 ? 628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 132.771 113.585 95.655  1.00 37.40 ? 628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.221 113.856 94.124  1.00 35.79 ? 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.609 117.617 95.606  1.00 31.49 ? 629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.833 117.996 96.302  1.00 24.63 ? 629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.461 116.804 97.012  1.00 32.29 ? 629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.688 116.646 97.008  1.00 32.41 ? 629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.541 119.121 97.293  1.00 27.46 ? 629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.639 115.957 97.633  1.00 34.86 ? 630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.177 114.817 98.366  1.00 29.83 ? 630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 138.916 113.855 97.447  1.00 33.81 ? 630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 139.858 113.183 97.882  1.00 37.55 ? 630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.052 114.098 99.107  1.00 32.55 ? 630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.281 114.996 100.045 1.00 33.05 ? 630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.801 115.349 101.283 1.00 28.38 ? 630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.034 115.494 99.693  1.00 30.38 ? 630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.101 116.169 102.143 1.00 28.79 ? 630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.328 116.315 100.546 1.00 32.85 ? 630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.865 116.648 101.770 1.00 36.39 ? 630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.161 117.466 102.622 1.00 42.84 ? 630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.514 113.777 96.181  1.00 33.06 ? 631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.208 112.953 95.201  1.00 31.55 ? 631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.424 113.647 94.605  1.00 34.55 ? 631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.141 113.031 93.810  1.00 39.06 ? 631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.249 112.550 94.077  1.00 33.38 ? 631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 136.959 111.950 94.598  1.00 40.82 ? 631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.002 111.247 95.628  1.00 42.06 ? 631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 135.902 112.182 93.975  1.00 41.39 ? 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.674 114.899 94.970  1.00 31.74 ? 632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 141.755 115.680 94.391  1.00 26.53 ? 632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.043 115.496 95.182  1.00 33.68 ? 632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.027 115.194 96.377  1.00 36.23 ? 632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.387 117.164 94.355  1.00 30.33 ? 632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 141.025 117.690 92.979  1.00 29.63 ? 632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.012 119.176 93.054  1.00 41.20 ? 632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 138.986 118.964 91.604  1.00 26.41 ? 632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.166 115.684 94.494  1.00 32.99 ? 633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.472 115.709 95.141  1.00 26.74 ? 633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.622 117.042 95.863  1.00 27.86 ? 633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.705 118.096 95.225  1.00 33.68 ? 633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.581 115.509 94.111  1.00 20.19 ? 633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 147.961 115.471 94.737  1.00 34.04 ? 633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.056 115.462 95.982  1.00 32.83 ? 633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 148.954 115.455 93.981  1.00 36.35 ? 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.652 117.001 97.197  1.00 26.66 ? 634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.748 118.235 97.968  1.00 20.33 ? 634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.018 119.012 97.655  1.00 20.38 ? 634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.060 120.224 97.884  1.00 23.75 ? 634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.675 117.932 99.464  1.00 18.29 ? 634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.276 118.031 100.056 1.00 27.62 ? 634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.304 119.396 99.387  1.00 39.60 ? 634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.310 118.547 98.163  1.00 23.24 ? 634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.052 118.347 97.135  1.00 24.05 ? 635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.248 119.068 96.711  1.00 18.01 ? 635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.953 119.965 95.516  1.00 20.24 ? 635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.447 121.095 95.445  1.00 25.08 ? 635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.370 118.082 96.389  1.00 16.95 ? 635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.238 117.750 97.567  1.00 19.59 ? 635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.680 117.529 98.814  1.00 22.38 ? 635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.611 117.663 97.430  1.00 19.99 ? 635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.474 117.225 99.901  1.00 18.18 ? 635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.411 117.361 98.515  1.00 21.64 ? 635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.841 117.141 99.751  1.00 20.29 ? 635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.139 119.489 94.573  1.00 23.58 ? 636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.760 120.326 93.440  1.00 23.59 ? 636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.839 121.462 93.864  1.00 20.43 ? 636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.922 122.566 93.313  1.00 30.82 ? 636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.098 119.475 92.357  1.00 23.62 ? 636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 147.893 118.239 91.978  1.00 22.38 ? 636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 149.345 118.585 91.702  1.00 30.04 ? 636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 149.686 118.433 90.230  1.00 32.09 ? 636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 151.073 118.884 89.935  1.00 33.16 ? 636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.958 121.217 94.835  1.00 19.67 ? 637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.134 122.293 95.376  1.00 12.60 ? 637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 146.012 123.343 96.043  1.00 23.32 ? 637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.785 124.551 95.897  1.00 29.42 ? 637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.084 121.724 96.349  1.00 16.96 ? 637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.163 122.826 96.846  1.00 17.95 ? 637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.287 120.616 95.680  1.00 23.83 ? 637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 147.027 122.899 96.787  1.00 19.97 ? 638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.975 123.828 97.393  1.00 16.81 ? 638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.705 124.619 96.316  1.00 13.76 ? 638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.924 125.826 96.455  1.00 26.75 ? 638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.959 123.071 98.305  1.00 21.09 ? 638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.170 123.933 98.613  1.00 12.35 ? 638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.271 122.640 99.587  1.00 17.66 ? 638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.101 123.951 95.232  1.00 17.64 ? 639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.766 124.646 94.135  1.00 13.68 ? 639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.868 125.721 93.537  1.00 19.11 ? 639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.316 126.843 93.275  1.00 29.72 ? 639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.182 123.647 93.056  1.00 15.64 ? 639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.497 122.968 93.366  1.00 31.15 ? 639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.397 123.636 93.917  1.00 30.96 ? 639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.631 121.766 93.057  1.00 34.85 ? 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.595 125.396 93.315  1.00 14.24 ? 640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.672 126.370 92.743  1.00 21.16 ? 640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.461 127.550 93.684  1.00 14.03 ? 640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.463 128.711 93.253  1.00 21.70 ? 640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.341 125.694 92.416  1.00 21.46 ? 640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 144.150 126.632 92.381  1.00 22.08 ? 640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 144.178 127.695 90.928  1.00 37.25 ? 640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 143.196 126.726 89.790  1.00 19.97 ? 640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.283 127.273 94.977  1.00 16.90 ? 641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 146.057 128.344 95.941  1.00 15.84 ? 641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 147.292 129.229 96.062  1.00 17.07 ? 641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 147.183 130.453 96.191  1.00 27.77 ? 641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.637 127.756 97.299  1.00 22.78 ? 641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.331 126.976 97.153  1.00 15.27 ? 641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.481 128.857 98.332  1.00 16.29 ? 641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.280 127.705 96.343  1.00 12.64 ? 641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.485 128.629 96.021  1.00 7.07  ? 642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.713 129.414 96.058  1.00 13.08 ? 642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.866 130.254 94.798  1.00 9.87  ? 642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.364 131.384 94.857  1.00 22.51 ? 642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.919 128.495 96.242  1.00 14.78 ? 642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.455 129.718 93.648  1.00 16.00 ? 643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.470 130.508 92.423  1.00 16.27 ? 643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.553 131.717 92.550  1.00 19.67 ? 643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.929 132.839 92.192  1.00 17.44 ? 643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 149.057 129.642 91.232  1.00 16.71 ? 643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.941 128.519 91.124  1.00 28.34 ? 643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 149.109 130.445 89.944  1.00 17.21 ? 643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 147.340 131.504 93.064  1.00 16.31 ? 644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.428 132.622 93.287  1.00 14.27 ? 644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.994 133.571 94.335  1.00 6.91  ? 644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.952 134.796 94.174  1.00 18.71 ? 644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 145.033 132.108 93.689  1.00 17.71 ? 644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.431 131.254 92.573  1.00 16.60 ? 644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 144.111 133.271 94.025  1.00 7.29  ? 644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 143.213 130.473 93.001  1.00 16.45 ? 644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.543 133.018 95.420  1.00 12.73 ? 645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.957 133.833 96.556  1.00 5.74  ? 645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 149.061 134.821 96.206  1.00 15.51 ? 645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 149.211 135.831 96.901  1.00 29.01 ? 645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.414 132.939 97.709  1.00 3.53  ? 645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.858 133.712 98.940  1.00 9.86  ? 645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.693 134.313 99.701  1.00 13.12 ? 645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 147.054 133.643 100.507 1.00 13.09 ? 645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 147.408 135.582 99.441  1.00 2.50  ? 645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.837 134.561 95.156  1.00 18.98 ? 646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.891 135.495 94.785  1.00 9.12  ? 646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 150.343 136.820 94.272  1.00 12.44 ? 646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 151.110 137.779 94.147  1.00 15.54 ? 646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.809 134.866 93.737  1.00 15.66 ? 646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 151.217 134.799 92.345  1.00 22.58 ? 646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 152.129 134.096 91.359  1.00 26.10 ? 646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 153.160 134.634 90.959  1.00 31.75 ? 646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 151.749 132.890 90.958  1.00 17.02 ? 646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 149.045 136.899 93.986  1.00 21.22 ? 647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 148.416 138.131 93.534  1.00 9.59  ? 647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 147.394 138.670 94.524  1.00 4.58  ? 647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.807 139.726 94.273  1.00 19.79 ? 647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.755 137.912 92.170  1.00 9.55  ? 647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.645 137.239 91.173  1.00 11.48 ? 647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.776 137.838 90.663  1.00 12.35 ? 647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.578 136.014 90.603  1.00 9.90  ? 647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 150.363 137.013 89.816  1.00 14.00 ? 647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.656 135.900 89.760  1.00 14.85 ? 647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 147.167 137.978 95.635  1.00 8.38  ? 648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 146.275 138.437 96.691  1.00 11.23 ? 648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 147.127 139.016 97.810  1.00 14.39 ? 648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 148.040 138.349 98.312  1.00 22.87 ? 648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 145.387 137.292 97.208  1.00 14.37 ? 648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.715 136.560 96.045  1.00 13.82 ? 648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 144.346 137.818 98.184  1.00 4.66  ? 648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.926 137.456 95.123  1.00 3.40  ? 648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.844 140.262 98.193  1.00 8.54  ? 649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.621 140.892 99.253  1.00 2.67  ? 649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 147.220 140.385 100.632 1.00 8.36  ? 649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 148.059 140.337 101.537 1.00 26.53 ? 649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 147.486 142.415 99.174  1.00 17.18 ? 649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 146.042 142.878 99.172  1.00 17.71 ? 649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 145.395 142.809 98.108  1.00 21.42 ? 649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 145.555 143.317 100.233 1.00 19.13 ? 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.958 140.016 100.811 1.00 12.94 ? 650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.497 139.342 102.015 1.00 0.00  ? 650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.542 137.830 101.799 1.00 4.79  ? 650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 146.160 137.331 100.856 1.00 18.53 ? 650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 144.109 139.841 102.399 1.00 7.15  ? 650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 144.088 141.301 102.810 1.00 3.35  ? 650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.728 141.749 103.287 1.00 8.71  ? 650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 142.292 141.388 104.378 1.00 19.62 ? 650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 142.048 142.546 102.472 1.00 8.07  ? 650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.904 137.076 102.692 1.00 7.53  ? 651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.909 135.632 102.608 1.00 10.36 ? 651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.768 135.073 101.775 1.00 1.38  ? 651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.973 135.792 101.175 1.00 8.76  ? 651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.713 133.744 101.738 1.00 17.84 ? 652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.672 132.996 101.044 1.00 0.46  ? 652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 142.180 131.901 101.977 1.00 2.56  ? 652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.983 131.114 102.489 1.00 17.59 ? 652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 143.186 132.382 99.728  1.00 10.04 ? 652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.833 133.449 98.844  1.00 6.60  ? 652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 142.059 131.663 99.000  1.00 8.14  ? 652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.508 132.889 97.617  1.00 11.05 ? 652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.871 131.846 102.197 1.00 2.74  ? 653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 140.293 130.771 102.994 1.00 7.42  ? 653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.534 129.449 102.275 1.00 12.02 ? 653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.952 129.192 101.217 1.00 21.43 ? 653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.806 131.017 103.221 1.00 8.07  ? 653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.597 131.799 104.381 1.00 13.84 ? 653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.391 128.612 102.847 1.00 15.20 ? 654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.867 127.396 102.199 1.00 5.12  ? 654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.463 126.201 103.054 1.00 14.46 ? 654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 142.091 125.923 104.081 1.00 20.38 ? 654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.381 127.454 102.001 1.00 8.01  ? 654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.944 126.288 101.241 1.00 16.28 ? 654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.127 125.479 100.470 1.00 18.59 ? 654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.297 126.005 101.293 1.00 14.04 ? 654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.648 124.410 99.772  1.00 15.60 ? 654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.824 124.938 100.595 1.00 17.76 ? 654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.998 124.140 99.835  1.00 11.94 ? 654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.419 125.499 102.628 1.00 21.33 ? 655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.961 124.299 103.311 1.00 17.27 ? 655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.687 123.082 102.755 1.00 17.65 ? 655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.825 122.935 101.538 1.00 18.34 ? 655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.449 124.127 103.155 1.00 21.24 ? 655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.775 125.188 103.840 1.00 25.30 ? 655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 138.001 122.794 103.729 1.00 21.11 ? 655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.153 122.218 103.650 1.00 21.36 ? 656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.775 120.963 103.258 1.00 24.93 ? 656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.722 119.866 103.241 1.00 23.08 ? 656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.009 119.665 104.229 1.00 26.02 ? 656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.912 120.595 104.212 1.00 27.30 ? 656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.096 121.561 104.266 1.00 25.09 ? 656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.226 120.967 105.089 1.00 25.52 ? 656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.569 121.911 102.866 1.00 18.64 ? 656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.624 119.164 102.120 1.00 22.62 ? 657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.640 118.106 101.929 1.00 23.75 ? 657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.368 116.771 102.006 1.00 29.80 ? 657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.102 116.402 101.084 1.00 29.31 ? 657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.917 118.280 100.597 1.00 26.07 ? 657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.315 119.642 100.419 1.00 29.61 ? 657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.071 119.938 100.948 1.00 26.86 ? 657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.001 120.633 99.739  1.00 29.43 ? 657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.519 121.192 100.791 1.00 33.03 ? 657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.453 121.889 99.578  1.00 29.56 ? 657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.209 122.168 100.105 1.00 28.58 ? 657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.161 116.052 103.104 1.00 31.15 ? 658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.923 114.854 103.417 1.00 37.05 ? 658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.015 113.634 103.417 1.00 39.77 ? 658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.883 113.690 103.905 1.00 39.32 ? 658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.606 114.983 104.780 1.00 37.70 ? 658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.090 116.385 105.150 1.00 35.10 ? 658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.247 116.508 106.654 1.00 30.32 ? 658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.389 116.711 104.437 1.00 36.23 ? 658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.517 112.537 102.862 1.00 45.15 ? 659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 139.831 111.260 102.960 1.00 44.20 ? 659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.045 110.656 104.342 1.00 46.29 ? 659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.047 110.923 105.012 1.00 47.06 ? 659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.327 110.299 101.881 1.00 43.72 ? 659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.108 110.798 100.464 1.00 46.24 ? 659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.533 109.762 99.437  1.00 45.93 ? 659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 140.328 110.274 98.021  1.00 45.96 ? 659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 140.378 109.178 97.015  1.00 49.03 ? 659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.085 109.835 104.771 1.00 51.38 ? 660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.186 109.208 106.083 1.00 51.18 ? 660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.410 108.309 106.200 1.00 52.59 ? 660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 140.868 108.047 107.317 1.00 49.41 ? 660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 137.920 108.405 106.387 1.00 51.32 ? 660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.519 107.493 105.245 1.00 52.96 ? 660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.767 107.947 104.356 1.00 52.20 ? 660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 137.955 106.323 105.236 1.00 53.50 ? 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 140.951 107.835 105.077 1.00 51.72 ? 661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.106 106.947 105.113 1.00 49.45 ? 661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.425 107.693 105.264 1.00 50.80 ? 661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.455 107.054 105.504 1.00 54.64 ? 661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.153 106.089 103.848 1.00 52.39 ? 661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.144 106.936 102.693 1.00 52.82 ? 661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 140.957 105.152 103.795 1.00 53.59 ? 661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 143.424 109.017 105.129 1.00 49.01 ? 662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 144.656 109.779 105.277 1.00 46.87 ? 662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 145.050 109.863 106.745 1.00 48.12 ? 662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 144.240 110.237 107.599 1.00 48.49 ? 662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 144.493 111.180 104.690 1.00 45.07 ? 662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.092 111.201 103.227 1.00 49.04 ? 662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.082 112.865 102.534 1.00 59.62 ? 662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.730 113.419 102.962 1.00 46.79 ? 662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.300 109.515 107.037 1.00 42.22 ? 663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.813 109.550 108.395 1.00 37.71 ? 663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.145 110.986 108.796 1.00 41.47 ? 663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 147.063 111.920 107.994 1.00 43.87 ? 663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 148.042 108.655 108.520 1.00 37.17 ? 663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 149.135 109.247 107.810 1.00 35.34 ? 663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 147.757 107.278 107.942 1.00 43.66 ? 663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.525 111.168 110.062 1.00 36.41 ? 664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 147.965 112.485 110.503 1.00 37.31 ? 664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.235 112.912 109.783 1.00 34.11 ? 664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.492 114.112 109.635 1.00 41.32 ? 664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.183 112.496 112.017 1.00 34.39 ? 664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 149.110 111.465 112.376 1.00 35.91 ? 664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.868 112.269 112.743 1.00 35.43 ? 664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.039 111.950 109.326 1.00 35.86 ? 665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 151.237 112.293 108.568 1.00 36.15 ? 665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 150.880 112.938 107.236 1.00 38.51 ? 665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.577 113.848 106.779 1.00 39.30 ? 665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.101 111.053 108.348 1.00 33.67 ? 665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.588 111.355 108.265 1.00 36.12 ? 665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.326 110.317 107.439 1.00 35.15 ? 665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 154.007 110.418 106.021 1.00 41.17 ? 665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 154.849 110.121 105.041 1.00 41.27 ? 665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 156.079 109.701 105.290 1.00 36.02 ? 665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 154.449 110.252 103.779 1.00 41.06 ? 665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.809 112.473 106.591 1.00 35.19 ? 666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.380 113.095 105.342 1.00 33.62 ? 666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 148.957 114.542 105.564 1.00 34.50 ? 666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.305 115.428 104.775 1.00 35.97 ? 666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.242 112.288 104.719 1.00 36.42 ? 666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 148.655 110.872 104.370 1.00 42.38 ? 666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 149.735 110.697 103.770 1.00 41.00 ? 666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 147.900 109.933 104.697 1.00 42.92 ? 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.210 114.802 106.638 1.00 31.91 ? 667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.825 116.173 106.956 1.00 27.34 ? 667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.044 117.029 107.274 1.00 26.05 ? 667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.136 118.183 106.836 1.00 31.33 ? 667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.837 116.179 108.123 1.00 34.59 ? 667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 145.925 117.400 108.237 1.00 34.46 ? 667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 145.227 117.671 106.916 1.00 30.86 ? 667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 144.910 117.204 109.349 1.00 27.50 ? 667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.993 116.482 108.036 1.00 26.84 ? 668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.208 117.228 108.345 1.00 22.67 ? 668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.992 117.546 107.080 1.00 24.12 ? 668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.520 118.653 106.932 1.00 29.24 ? 668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.074 116.442 109.328 1.00 26.11 ? 668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.726 116.731 110.772 1.00 24.21 ? 668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.271 117.824 111.106 1.00 28.33 ? 668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.941 115.750 111.639 1.00 31.48 ? 668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.085 116.587 106.159 1.00 26.16 ? 669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.779 116.827 104.899 1.00 27.33 ? 669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.060 117.876 104.064 1.00 21.77 ? 669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.706 118.695 103.404 1.00 23.42 ? 669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.919 115.522 104.117 1.00 25.51 ? 669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.292 114.887 104.218 1.00 27.72 ? 669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.317 113.516 103.565 1.00 31.23 ? 669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 154.377 113.599 102.110 1.00 32.73 ? 669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.339 114.207 101.431 1.00 30.20 ? 669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 156.354 114.794 102.044 1.00 28.83 ? 669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 155.284 114.225 100.103 1.00 31.07 ? 669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.726 117.865 104.071 1.00 20.63 ? 670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.983 118.885 103.335 1.00 21.74 ? 670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.260 120.266 103.915 1.00 24.68 ? 670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.486 121.232 103.177 1.00 24.61 ? 670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.478 118.562 103.336 1.00 28.30 ? 670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.182 117.384 102.407 1.00 22.76 ? 670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.674 119.779 102.917 1.00 25.42 ? 670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.913 116.644 102.752 1.00 24.66 ? 670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.252 120.381 105.244 1.00 24.26 ? 671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.557 121.663 105.874 1.00 17.88 ? 671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.985 122.105 105.573 1.00 19.78 ? 671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 152.237 123.287 105.308 1.00 22.58 ? 671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.330 121.578 107.384 1.00 21.90 ? 671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 149.028 120.891 107.741 1.00 31.39 ? 671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 148.223 120.624 106.826 1.00 37.35 ? 671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.811 120.611 108.940 1.00 35.50 ? 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.936 121.170 105.612 1.00 17.20 ? 672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.327 121.514 105.343 1.00 13.21 ? 672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.521 121.945 103.897 1.00 17.50 ? 672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.304 122.858 103.616 1.00 20.21 ? 672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.234 120.330 105.676 1.00 20.55 ? 672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.348 119.946 107.152 1.00 22.69 ? 672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.214 118.708 107.313 1.00 14.55 ? 672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.901 121.104 107.965 1.00 21.59 ? 672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.825 121.294 102.964 1.00 20.66 ? 673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.901 121.692 101.564 1.00 18.14 ? 673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.251 123.052 101.345 1.00 15.50 ? 673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.741 123.858 100.546 1.00 13.78 ? 673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.246 120.628 100.684 1.00 9.21  ? 673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.365 120.898 99.204  1.00 16.93 ? 673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.565 120.696 98.539  1.00 14.05 ? 673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.278 121.357 98.473  1.00 12.97 ? 673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.680 120.943 97.188  1.00 17.27 ? 673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.384 121.607 97.121  1.00 13.98 ? 673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.587 121.398 96.484  1.00 18.52 ? 673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.701 121.644 95.137  1.00 23.10 ? 673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 152.145 123.324 102.043 1.00 16.43 ? 674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.524 124.641 101.953 1.00 14.42 ? 674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.463 125.723 102.465 1.00 17.93 ? 674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.594 126.786 101.849 1.00 25.93 ? 674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 150.210 124.657 102.730 1.00 14.68 ? 674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 153.127 125.469 103.594 1.00 12.83 ? 675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 154.106 126.422 104.104 1.00 14.42 ? 675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 155.267 126.589 103.132 1.00 15.87 ? 675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.769 127.701 102.935 1.00 23.85 ? 675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.613 125.973 105.474 1.00 16.66 ? 675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.829 126.711 105.936 1.00 17.85 ? 675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 157.099 126.187 105.838 1.00 21.81 ? 675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.971 127.940 106.486 1.00 13.70 ? 675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.971 127.058 106.313 1.00 22.54 ? 675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 157.312 128.130 106.713 1.00 21.60 ? 675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.708 125.491 102.519 1.00 19.54 ? 676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.802 125.550 101.555 1.00 13.67 ? 676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.407 126.332 100.309 1.00 17.84 ? 676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 157.240 127.025 99.715  1.00 19.01 ? 676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.237 124.133 101.184 1.00 19.36 ? 676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.192 124.071 100.033 1.00 24.14 ? 676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.494 124.512 100.121 1.00 23.04 ? 676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 158.032 123.617 98.768  1.00 19.65 ? 676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 160.097 124.332 98.960  1.00 25.39 ? 676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.232 123.790 98.121  1.00 27.08 ? 676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 155.146 126.234 99.898  1.00 19.33 ? 677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.684 126.842 98.659  1.00 15.91 ? 677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 154.221 128.281 98.832  1.00 16.61 ? 677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.770 128.890 97.857  1.00 26.31 ? 677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.552 126.007 98.056  1.00 18.02 ? 677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 154.023 124.741 97.365  1.00 20.37 ? 677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.699 125.055 96.042  1.00 17.36 ? 677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.779 125.669 95.093  1.00 22.72 ? 677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.947 126.871 94.558  1.00 28.42 ? 677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 155.000 127.616 94.849  1.00 27.11 ? 677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 153.034 127.337 93.711  1.00 23.61 ? 677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.321 128.839 100.033 1.00 20.75 ? 678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.912 130.204 100.278 1.00 8.11  ? 678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.508 130.382 100.807 1.00 6.78  ? 678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 152.056 131.525 100.930 1.00 19.62 ? 678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.804 129.294 101.126 1.00 11.83 ? 679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.445 129.408 101.636 1.00 6.57  ? 679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.464 130.176 102.948 1.00 14.24 ? 679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 151.270 129.892 103.842 1.00 26.21 ? 679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.819 128.016 101.803 1.00 12.90 ? 679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.658 127.335 100.441 1.00 10.07 ? 679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.484 128.110 102.523 1.00 9.37  ? 679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.742 128.066 99.494  1.00 11.69 ? 679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.573 131.160 103.068 1.00 10.38 ? 680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.565 132.016 104.248 1.00 0.00  ? 680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.764 131.396 105.386 1.00 2.35  ? 680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 149.212 131.386 106.537 1.00 17.00 ? 680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 149.007 133.393 103.889 1.00 7.57  ? 680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.950 134.259 103.077 1.00 1.39  ? 680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 149.258 135.526 102.613 1.00 0.95  ? 680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 150.150 136.346 101.700 1.00 3.31  ? 680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.441 137.544 101.175 1.00 7.74  ? 680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.578 130.875 105.087 1.00 7.02  ? 681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.704 130.310 106.101 1.00 8.47  ? 681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 146.080 129.026 105.578 1.00 6.78  ? 681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.945 128.831 104.368 1.00 23.08 ? 681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.593 131.294 106.511 1.00 18.71 ? 681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.949 131.809 105.339 1.00 20.93 ? 681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 146.164 132.453 107.313 1.00 4.47  ? 681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.707 128.150 106.505 1.00 14.55 ? 682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.931 126.952 106.208 1.00 9.87  ? 682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.668 127.018 107.053 1.00 9.32  ? 682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.745 127.157 108.279 1.00 16.81 ? 682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.723 125.667 106.492 1.00 11.95 ? 682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 147.104 125.738 105.839 1.00 6.77  ? 682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.963 124.460 105.986 1.00 20.21 ? 682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.998 124.572 106.179 1.00 22.66 ? 682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.508 126.934 106.401 1.00 14.36 ? 683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 141.252 127.219 107.094 1.00 8.32  ? 683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.732 126.006 107.860 1.00 18.43 ? 683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.671 126.012 109.091 1.00 34.55 ? 683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 140.209 127.712 106.087 1.00 10.02 ? 683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.913 128.166 106.711 1.00 15.54 ? 683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.871 128.604 108.027 1.00 4.29  ? 683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.733 128.169 105.982 1.00 11.18 ? 683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.693 129.023 108.600 1.00 6.88  ? 683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.548 128.591 106.548 1.00 15.90 ? 683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.535 129.016 107.858 1.00 9.16  ? 683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.357 129.437 108.427 1.00 25.35 ? 683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.377 124.944 107.146 1.00 21.25 ? 684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.701 123.813 107.759 1.00 20.69 ? 684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.265 122.517 107.207 1.00 27.70 ? 684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.741 122.458 106.071 1.00 27.91 ? 684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.187 123.850 107.515 1.00 22.55 ? 684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.395 124.497 108.624 1.00 17.78 ? 684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 136.500 125.522 108.354 1.00 22.27 ? 684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 137.538 124.082 109.940 1.00 24.81 ? 684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 135.770 126.116 109.363 1.00 19.37 ? 684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 136.812 124.671 110.957 1.00 28.52 ? 684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.930 125.689 110.662 1.00 25.95 ? 684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 135.204 126.280 111.670 1.00 30.12 ? 684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.207 121.479 108.031 1.00 27.05 ? 685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.516 120.118 107.617 1.00 24.07 ? 685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.184 119.380 107.538 1.00 27.04 ? 685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.661 118.901 108.546 1.00 37.09 ? 685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.484 119.450 108.584 1.00 25.34 ? 685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.632 119.300 106.332 1.00 27.20 ? 686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.391 118.580 106.094 1.00 27.31 ? 686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.708 117.156 105.664 1.00 35.40 ? 686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.488 116.941 104.730 1.00 37.84 ? 686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.549 119.279 105.027 1.00 35.96 ? 686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.861 120.545 105.498 1.00 35.93 ? 686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.644 120.847 104.641 1.00 36.37 ? 686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.586 119.862 104.831 1.00 40.91 ? 686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.325 120.162 105.111 1.00 40.00 ? 686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.924 121.416 105.237 1.00 38.08 ? 686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.444 119.178 105.269 1.00 34.97 ? 686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.104 116.188 106.343 1.00 37.97 ? 687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.306 114.779 106.047 1.00 40.41 ? 687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.025 114.187 105.476 1.00 40.78 ? 687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.929 114.455 105.975 1.00 44.07 ? 687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.729 114.004 107.298 1.00 41.96 ? 687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 138.946 114.557 107.815 1.00 44.55 ? 687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 137.951 112.539 106.965 1.00 37.91 ? 687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.172 113.387 104.425 1.00 44.78 ? 688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 135.031 112.754 103.777 1.00 44.60 ? 688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 134.564 111.535 104.565 1.00 48.36 ? 688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 135.348 110.908 105.277 1.00 49.47 ? 688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 135.385 112.353 102.344 1.00 44.44 ? 688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 134.181 112.107 101.454 1.00 41.12 ? 688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 134.522 111.148 100.328 1.00 42.19 ? 688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.661 111.404 99.105  1.00 44.47 ? 688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 132.842 110.214 98.746  1.00 48.98 ? 688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.501 115.077 164.750 1.00 71.22 ? 6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.489 116.037 165.172 1.00 71.80 ? 6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 153.090 117.069 166.118 1.00 71.79 ? 6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 153.840 116.722 167.030 1.00 71.31 ? 6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.293 115.332 165.830 0.43 75.82 ? 6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.330 116.356 166.408 0.84 73.49 ? 6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 150.587 114.442 164.821 0.98 74.68 ? 6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 152.768 118.340 165.891 1.00 63.32 ? 7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.283 119.401 166.768 1.00 59.19 ? 7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 152.885 119.196 168.220 1.00 60.15 ? 7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 151.807 118.668 168.508 1.00 62.72 ? 7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 152.648 120.675 166.199 1.00 61.28 ? 7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.191 120.337 164.821 1.00 63.19 ? 7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.255 118.858 164.612 1.00 62.23 ? 7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 153.752 119.612 169.145 1.00 58.92 ? 8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.455 119.451 170.565 1.00 58.81 ? 8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 152.211 120.234 170.964 1.00 60.29 ? 8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.372 119.739 171.727 1.00 62.54 ? 8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.654 119.890 171.404 1.00 58.70 ? 8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.389 119.920 172.898 1.00 59.51 ? 8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 155.596 120.448 173.657 1.00 60.94 ? 8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 155.302 120.582 175.141 1.00 59.69 ? 8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 156.450 121.169 175.886 1.00 58.68 ? 8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 152.073 121.463 170.460 1.00 59.06 ? 9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.902 122.264 170.797 1.00 54.81 ? 9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.626 121.605 170.292 1.00 54.14 ? 9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.583 121.670 170.950 1.00 57.27 ? 9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 151.036 123.674 170.225 1.00 55.32 ? 9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.424 123.719 168.782 1.00 52.28 ? 9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.583 123.779 167.710 1.00 51.80 ? 9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.753 123.723 168.249 1.00 52.73 ? 9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.305 123.815 166.543 1.00 51.91 ? 9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.640 123.783 166.847 1.00 54.06 ? 9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 154.027 123.681 168.822 1.00 52.40 ? 9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.751 123.798 166.009 1.00 53.08 ? 9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 155.129 123.697 167.988 1.00 54.60 ? 9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.984 123.755 166.598 1.00 54.01 ? 9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.687 120.974 169.119 1.00 57.82 ? 10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.512 120.298 168.582 1.00 58.12 ? 10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 148.150 119.092 169.439 1.00 57.87 ? 10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 146.967 118.798 169.651 1.00 59.84 ? 10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 148.750 119.906 167.114 1.00 56.85 ? 10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.296 121.035 166.189 1.00 58.22 ? 10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 148.019 118.617 166.785 1.00 57.86 ? 10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 148.574 120.778 164.731 1.00 59.43 ? 10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 149.154 118.371 169.942 1.00 60.46 ? 11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 148.874 117.272 170.860 1.00 61.16 ? 11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 148.235 117.782 172.144 1.00 60.47 ? 11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 147.304 117.163 172.672 1.00 62.33 ? 11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 150.153 116.495 171.168 1.00 61.84 ? 11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 150.723 115.743 169.978 1.00 64.00 ? 11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 152.027 115.044 170.301 1.00 65.38 ? 11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 152.751 115.447 171.210 1.00 63.22 ? 11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.334 113.989 169.554 1.00 63.35 ? 11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.723 118.910 172.663 1.00 59.28 ? 12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 148.106 119.495 173.849 1.00 57.80 ? 12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.660 119.892 173.576 1.00 59.59 ? 12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 145.777 119.673 174.413 1.00 60.35 ? 12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 148.916 120.702 174.320 1.00 56.35 ? 12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 150.164 120.404 175.151 1.00 57.99 ? 12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 151.096 121.604 175.165 1.00 58.06 ? 12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 149.781 120.002 176.566 1.00 58.85 ? 12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.401 120.481 172.407 1.00 57.31 ? 13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 145.044 120.883 172.054 1.00 54.74 ? 13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 144.129 119.672 171.919 1.00 58.08 ? 13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 142.990 119.685 172.398 1.00 62.06 ? 13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.063 121.695 170.759 1.00 57.67 ? 13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.675 121.943 170.206 1.00 56.43 ? 13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 143.219 121.240 169.307 1.00 57.89 ? 13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 142.998 122.951 170.740 1.00 55.93 ? 13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 144.611 118.612 171.265 1.00 60.09 ? 14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 143.801 117.410 171.105 1.00 57.54 ? 14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.445 116.778 172.442 1.00 58.65 ? 14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.476 116.016 172.517 1.00 61.30 ? 14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 144.526 116.397 170.221 1.00 58.96 ? 14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.595 116.834 168.772 1.00 59.82 ? 14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 145.238 116.187 167.946 1.00 60.88 ? 14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 143.932 117.938 168.457 1.00 60.27 ? 14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 144.204 117.077 173.497 1.00 63.90 ? 15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 143.854 116.614 174.832 1.00 63.78 ? 15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.588 117.274 175.357 1.00 65.18 ? 15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 142.058 116.832 176.382 1.00 64.21 ? 15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 145.014 116.872 175.795 1.00 63.55 ? 15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 144.815 116.288 177.184 1.00 65.72 ? 15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 146.124 115.896 177.842 1.00 67.86 ? 15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 146.127 114.931 178.636 1.00 66.86 ? 15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 147.151 116.551 177.565 1.00 67.63 ? 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 142.099 118.319 174.686 1.00 64.83 ? 16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 140.840 118.944 175.081 1.00 62.78 ? 16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.722 117.910 175.089 1.00 63.00 ? 16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 138.950 117.807 176.049 1.00 63.39 ? 16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.507 120.117 174.141 1.00 62.92 ? 16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.476 121.282 174.352 1.00 61.45 ? 16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 139.071 120.576 174.351 1.00 63.29 ? 16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 141.316 121.976 175.676 1.00 61.70 ? 16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.626 117.123 174.016 1.00 64.80 ? 17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.534 116.169 173.871 1.00 65.03 ? 17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 138.698 114.946 174.762 1.00 64.56 ? 17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 137.709 114.255 175.028 1.00 64.64 ? 17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.414 115.735 172.411 1.00 65.08 ? 17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 137.965 116.843 171.479 1.00 64.77 ? 17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 136.892 118.039 172.292 1.00 70.79 ? 17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 135.293 117.528 171.670 1.00 65.85 ? 17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 139.912 114.662 175.229 1.00 65.95 ? 18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.141 113.509 176.091 1.00 67.12 ? 18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 139.494 113.779 177.441 1.00 67.95 ? 18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 140.004 114.570 178.242 1.00 69.06 ? 18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 141.642 113.205 176.239 1.00 67.46 ? 18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.151 112.435 175.019 1.00 67.61 ? 18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 141.904 112.422 177.514 1.00 66.97 ? 18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 143.500 112.902 174.521 1.00 68.44 ? 18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 138.366 113.125 177.700 1.00 71.29 ? 19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 137.614 113.382 178.920 1.00 71.26 ? 19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 138.377 112.869 180.134 1.00 72.15 ? 19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 138.869 111.737 180.142 1.00 74.43 ? 19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.238 112.724 178.840 1.00 71.94 ? 19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.332 113.311 177.769 1.00 70.92 ? 19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 134.314 114.279 178.336 1.00 72.03 ? 19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 134.513 115.493 178.308 1.00 72.82 ? 19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 133.215 113.746 178.855 1.00 72.55 ? 19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 138.475 113.710 181.160 1.00 74.08 ? 20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.089 113.342 182.429 1.00 75.80 ? 20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.082 113.616 183.533 1.00 76.47 ? 20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 137.623 114.753 183.687 1.00 74.85 ? 20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 140.386 114.120 182.665 1.00 73.30 ? 20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 140.576 114.608 184.090 1.00 73.86 ? 20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 142.049 114.818 184.400 1.00 75.64 ? 20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 142.243 115.537 185.723 1.00 76.33 ? 20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 143.634 115.386 186.233 1.00 75.39 ? 20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 137.740 112.581 184.299 1.00 78.89 ? 21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 136.670 112.674 185.290 1.00 78.53 ? 21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 135.341 113.010 184.615 1.00 78.34 ? 21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 134.505 113.731 185.164 1.00 76.62 ? 21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.009 113.701 186.374 1.00 78.82 ? 21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 136.045 113.659 187.544 1.00 79.68 ? 21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 135.120 112.819 187.527 1.00 79.69 ? 21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 136.210 114.468 188.481 1.00 78.43 ? 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.150 112.486 183.406 1.00 75.88 ? 22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 133.951 112.770 182.645 1.00 75.32 ? 22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 133.804 114.205 182.198 1.00 75.66 ? 22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 132.708 114.601 181.789 1.00 74.57 ? 22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 134.871 114.998 182.260 1.00 71.81 ? 23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 134.824 116.411 181.919 1.00 69.41 ? 23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 135.902 116.729 180.895 1.00 70.13 ? 23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 137.004 116.176 180.949 1.00 71.59 ? 23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 135.014 117.287 183.162 1.00 69.88 ? 23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 133.743 117.532 183.952 1.00 69.55 ? 23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 133.831 118.828 184.737 1.00 69.23 ? 23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 133.826 118.568 186.233 1.00 70.35 ? 23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 134.732 119.500 186.958 1.00 69.04 ? 23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 135.579 117.623 179.966 1.00 65.90 ? 24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 136.555 118.056 178.978 1.00 63.90 ? 24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 137.698 118.800 179.656 1.00 64.99 ? 24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.488 119.574 180.594 1.00 63.07 ? 24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 135.893 118.951 177.931 1.00 61.73 ? 24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 135.087 118.198 176.913 1.00 62.89 ? 24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 135.711 117.473 175.914 1.00 64.72 ? 24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 133.704 118.216 176.955 1.00 63.05 ? 24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 134.972 116.780 174.977 1.00 63.96 ? 24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 132.960 117.526 176.020 1.00 62.28 ? 24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 133.595 116.807 175.031 1.00 62.62 ? 24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 138.916 118.560 179.176 1.00 66.03 ? 25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 140.107 119.208 179.725 1.00 64.65 ? 25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 140.306 120.562 179.044 1.00 64.47 ? 25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 141.174 120.754 178.192 1.00 67.27 ? 25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.325 118.309 179.558 1.00 65.60 ? 25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.230 116.990 180.301 1.00 65.05 ? 25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 142.395 116.070 179.999 1.00 66.24 ? 25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 143.441 116.143 180.642 1.00 65.74 ? 25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.218 115.195 179.015 1.00 65.73 ? 25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 139.470 121.518 179.452 1.00 56.80 ? 26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 139.502 122.839 178.834 1.00 57.18 ? 26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 140.798 123.578 179.138 1.00 58.23 ? 26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 141.259 124.378 178.316 1.00 57.57 ? 26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 138.298 123.661 179.293 1.00 55.35 ? 26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 136.986 123.154 178.769 1.00 55.07 ? 26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 136.803 122.941 177.413 1.00 54.07 ? 26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 135.935 122.891 179.630 1.00 54.85 ? 26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.598 122.476 176.927 1.00 55.22 ? 26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.728 122.426 179.149 1.00 55.24 ? 26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.559 122.218 177.796 1.00 54.19 ? 26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 141.402 123.327 180.302 1.00 63.25 ? 27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.660 123.983 180.639 1.00 61.34 ? 27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 143.786 123.590 179.692 1.00 61.34 ? 27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 144.815 124.273 179.654 1.00 62.82 ? 27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 143.056 123.656 182.080 1.00 62.48 ? 27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 142.774 122.213 182.448 1.00 67.13 ? 27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 141.629 121.758 182.242 1.00 67.32 ? 27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 143.699 121.532 182.941 1.00 64.32 ? 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.617 122.507 178.931 1.00 59.53 ? 28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 144.653 122.082 177.999 1.00 61.01 ? 28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 144.829 123.056 176.842 1.00 63.11 ? 28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 145.867 123.022 176.174 1.00 64.90 ? 28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.333 120.688 177.458 1.00 60.60 ? 28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 144.673 119.559 178.414 1.00 63.35 ? 28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 146.171 119.330 178.487 1.00 63.05 ? 28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.573 118.766 179.839 1.00 63.28 ? 28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 146.157 119.661 180.952 1.00 61.44 ? 28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 143.842 123.917 176.587 1.00 58.76 ? 29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 143.961 124.865 175.484 1.00 54.37 ? 29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 144.930 125.990 175.823 1.00 55.40 ? 29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.668 126.463 174.952 1.00 56.37 ? 29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.586 125.424 175.122 1.00 54.64 ? 29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.436 125.685 173.637 1.00 57.44 ? 29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 143.005 124.913 172.837 1.00 58.95 ? 29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 141.744 126.655 173.270 1.00 56.07 ? 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 144.941 126.436 177.081 1.00 55.49 ? 30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.934 127.419 177.499 1.00 55.27 ? 30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.342 126.853 177.372 1.00 56.41 ? 30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 148.250 127.526 176.870 1.00 57.78 ? 30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.661 127.868 178.934 1.00 56.36 ? 30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 146.845 128.541 179.611 1.00 58.91 ? 30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 147.120 129.913 179.016 1.00 59.23 ? 30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 148.586 130.292 179.160 1.00 58.72 ? 30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 149.159 130.817 177.889 1.00 56.91 ? 30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.538 125.608 177.812 1.00 56.55 ? 31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 148.821 124.949 177.600 1.00 56.86 ? 31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.109 124.791 176.114 1.00 56.41 ? 31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.253 124.949 175.676 1.00 56.82 ? 31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 148.841 123.589 178.297 1.00 57.67 ? 31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 149.029 123.659 179.801 1.00 59.14 ? 31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.291 122.555 180.529 1.00 62.13 ? 31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.249 121.422 180.006 1.00 62.68 ? 31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 147.755 122.818 181.626 1.00 60.15 ? 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 148.082 124.476 175.323 1.00 51.13 ? 32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 148.279 124.335 173.886 1.00 48.66 ? 32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.738 125.645 173.260 1.00 49.72 ? 32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.659 125.656 172.438 1.00 48.78 ? 32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 146.992 123.844 173.224 1.00 50.11 ? 32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 148.120 126.763 173.645 1.00 53.80 ? 33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.505 128.052 173.075 1.00 51.79 ? 33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.901 128.450 173.541 1.00 52.05 ? 33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.705 128.976 172.760 1.00 51.98 ? 33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.457 129.127 173.416 1.00 48.71 ? 33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 147.576 129.560 174.867 1.00 50.36 ? 33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 147.605 130.322 172.490 1.00 50.20 ? 33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.213 128.214 174.817 1.00 51.12 ? 34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.546 128.536 175.314 1.00 50.31 ? 34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.614 127.729 174.587 1.00 53.18 ? 34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.657 128.270 174.200 1.00 54.82 ? 34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.621 128.288 176.819 1.00 54.11 ? 34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.896 128.759 177.445 1.00 55.25 ? 34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.957 127.916 177.696 1.00 53.96 ? 34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 153.280 129.984 177.874 1.00 55.26 ? 34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.940 128.602 178.250 1.00 54.06 ? 34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 154.555 129.859 178.369 1.00 56.25 ? 34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.375 126.429 174.402 1.00 55.43 ? 35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.319 125.598 173.665 1.00 52.25 ? 35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.437 126.057 172.220 1.00 52.47 ? 35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.545 126.154 171.681 1.00 55.50 ? 35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 152.889 124.133 173.729 1.00 54.18 ? 35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 153.511 123.378 172.707 1.00 57.69 ? 35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.304 126.347 171.576 1.00 52.24 ? 36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.330 126.854 170.211 1.00 49.64 ? 36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 153.236 128.067 170.107 1.00 48.93 ? 36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 154.149 128.108 169.276 1.00 50.52 ? 36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.911 127.205 169.762 1.00 48.54 ? 36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.831 127.867 168.407 1.00 48.68 ? 36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.288 127.222 167.267 1.00 48.99 ? 36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 150.292 129.139 168.268 1.00 47.07 ? 36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.212 127.825 166.028 1.00 47.59 ? 36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 150.212 129.750 167.034 1.00 46.68 ? 36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 150.672 129.088 165.917 1.00 48.68 ? 36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.595 129.694 164.685 1.00 49.59 ? 36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 153.019 129.057 170.970 1.00 53.82 ? 37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.865 130.242 170.941 1.00 53.91 ? 37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.324 129.868 171.153 1.00 53.80 ? 37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 156.142 130.004 170.237 1.00 56.45 ? 37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 153.395 131.261 171.979 1.00 53.21 ? 37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.487 132.311 171.412 1.00 53.35 ? 37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 153.010 133.453 170.832 1.00 53.37 ? 37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 151.114 132.146 171.434 1.00 54.29 ? 37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 152.181 134.418 170.299 1.00 53.62 ? 37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.281 133.108 170.902 1.00 53.68 ? 37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 150.815 134.244 170.334 1.00 53.77 ? 37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.641 129.306 172.322 1.00 54.84 ? 38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 157.031 129.095 172.717 1.00 56.79 ? 38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.787 128.246 171.703 1.00 56.86 ? 38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 159.003 128.406 171.541 1.00 57.58 ? 38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 157.086 128.465 174.122 1.00 56.33 ? 38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 158.342 127.628 174.276 1.00 57.40 ? 38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 157.017 129.542 175.191 1.00 54.65 ? 38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 157.103 127.337 171.006 1.00 55.26 ? 39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.793 126.401 170.130 1.00 55.07 ? 39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.765 126.787 168.657 1.00 57.32 ? 39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.646 126.347 167.911 1.00 61.25 ? 39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.203 124.994 170.287 1.00 57.43 ? 39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.244 124.502 171.720 1.00 61.80 ? 39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.136 124.943 172.474 1.00 60.48 ? 39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.386 123.674 172.091 1.00 61.41 ? 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.793 127.581 168.210 1.00 55.65 ? 40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.720 127.961 166.806 1.00 56.27 ? 40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.783 129.464 166.595 1.00 59.84 ? 40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.555 129.932 165.752 1.00 59.13 ? 40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.435 127.393 166.182 1.00 54.62 ? 40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.311 127.638 164.696 1.00 57.18 ? 40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 154.738 128.805 164.211 1.00 56.89 ? 40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 155.770 126.705 163.778 1.00 57.49 ? 40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 154.623 129.036 162.857 1.00 56.96 ? 40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 155.660 126.926 162.419 1.00 58.71 ? 40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.087 128.094 161.965 1.00 58.49 ? 40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.974 128.320 160.613 1.00 60.97 ? 40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.996 130.241 167.338 1.00 57.19 ? 41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 155.844 131.656 167.012 1.00 54.39 ? 41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 157.109 132.423 167.367 1.00 54.64 ? 41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 157.617 133.220 166.570 1.00 57.54 ? 41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 154.607 132.239 167.718 1.00 54.01 ? 41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.328 131.659 167.114 1.00 53.69 ? 41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.604 133.755 167.621 1.00 53.29 ? 41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 153.219 131.849 165.623 1.00 51.15 ? 41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 157.640 132.192 168.569 1.00 54.90 ? 42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 158.875 132.860 168.963 1.00 57.86 ? 42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 160.036 132.435 168.072 1.00 59.81 ? 42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 160.891 133.255 167.718 1.00 60.21 ? 42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 159.184 132.570 170.431 1.00 58.43 ? 42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 158.097 133.069 171.364 1.00 56.92 ? 42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 157.198 133.800 170.952 1.00 58.97 ? 42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 158.179 132.680 172.630 1.00 57.21 ? 42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 160.085 131.154 167.702 1.00 60.35 ? 43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 161.162 130.669 166.846 1.00 59.27 ? 43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 161.101 131.306 165.463 1.00 58.62 ? 43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 162.122 131.754 164.929 1.00 60.00 ? 43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 161.098 129.145 166.738 1.00 59.80 ? 43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 160.664 128.443 168.014 1.00 59.57 ? 43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.628 128.659 169.164 1.00 61.93 ? 43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 162.479 129.547 169.120 1.00 60.27 ? 43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 161.497 127.844 170.204 1.00 60.23 ? 43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 159.911 131.359 164.868 1.00 59.37 ? 44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 159.731 131.850 163.509 1.00 59.15 ? 44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 159.454 133.346 163.446 1.00 58.96 ? 44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 159.098 133.851 162.377 1.00 60.09 ? 44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.601 131.083 162.817 1.00 58.97 ? 44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 158.759 129.580 162.937 1.00 60.59 ? 44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 159.137 129.064 163.988 1.00 60.04 ? 44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 158.470 128.868 161.854 1.00 61.38 ? 44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.605 134.061 164.556 1.00 58.43 ? 45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 159.433 135.508 164.575 1.00 60.95 ? 45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.777 136.170 164.296 1.00 60.44 ? 45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 161.750 135.938 165.021 1.00 60.64 ? 45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.873 135.973 165.918 1.00 59.91 ? 45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 157.555 135.440 166.100 1.00 60.33 ? 45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.810 137.490 165.974 1.00 57.53 ? 45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.828 136.992 163.245 1.00 61.75 ? 46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 162.064 137.687 162.911 1.00 60.80 ? 46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 162.490 138.556 164.084 1.00 61.78 ? 46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 161.655 139.076 164.836 1.00 61.93 ? 46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.889 138.524 161.634 1.00 60.37 ? 46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 163.189 139.225 161.279 1.00 59.83 ? 46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.420 137.648 160.485 1.00 59.44 ? 46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 163.799 138.717 164.246 1.00 65.67 ? 47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 164.361 139.484 165.349 1.00 65.84 ? 47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 164.826 140.843 164.844 1.00 66.98 ? 47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 165.513 140.930 163.822 1.00 67.85 ? 47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 165.526 138.738 165.998 1.00 67.07 ? 47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 166.337 139.584 166.938 1.00 66.52 ? 47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 167.616 139.989 166.599 1.00 66.70 ? 47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 165.819 139.972 168.163 1.00 66.64 ? 47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 168.364 140.767 167.463 1.00 68.38 ? 47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 166.562 140.749 169.031 1.00 67.17 ? 47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 167.836 141.147 168.681 1.00 67.51 ? 47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 164.446 141.895 165.563 1.00 64.38 ? 48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.870 143.253 165.260 1.00 63.41 ? 48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 165.397 143.896 166.533 1.00 65.01 ? 48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.786 143.776 167.599 1.00 66.11 ? 48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 163.720 144.080 164.676 1.00 62.50 ? 48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.273 143.620 163.318 1.00 61.79 ? 48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 163.929 144.045 162.177 1.00 62.51 ? 48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 162.200 142.756 163.184 1.00 62.87 ? 48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 163.520 143.622 160.926 1.00 62.69 ? 48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 161.786 142.330 161.937 1.00 63.33 ? 48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.448 142.763 160.807 1.00 62.40 ? 48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.538 144.578 166.416 1.00 66.19 ? 49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 167.189 145.129 167.600 1.00 66.99 ? 49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 166.305 146.161 168.289 1.00 68.58 ? 49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 166.236 146.206 169.522 1.00 68.66 ? 49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.538 145.737 167.219 1.00 68.16 ? 49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 169.552 144.726 166.783 1.00 70.31 ? 49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 169.606 144.233 165.497 1.00 69.87 ? 49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.548 144.110 167.464 1.00 68.93 ? 49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 170.593 143.360 165.404 1.00 68.33 ? 49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 171.180 143.267 166.583 1.00 69.18 ? 49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.622 146.997 167.512 1.00 67.68 ? 50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.735 148.010 168.063 1.00 65.85 ? 50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.555 148.191 167.118 1.00 64.59 ? 50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.499 147.595 166.038 1.00 63.73 ? 50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.479 149.331 168.289 1.00 64.40 ? 50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 166.548 149.582 167.245 1.00 65.74 ? 50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 166.405 149.190 166.088 1.00 66.16 ? 50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.628 150.240 167.649 1.00 66.48 ? 50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.600 149.023 167.538 1.00 60.91 ? 51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 161.446 149.310 166.693 1.00 60.80 ? 51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.834 150.135 165.475 1.00 60.47 ? 51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 161.228 149.986 164.409 1.00 61.02 ? 51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 160.369 150.034 167.500 1.00 60.35 ? 51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 159.152 150.526 166.715 1.00 59.64 ? 51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 158.436 149.368 166.036 1.00 59.45 ? 51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 158.205 151.288 167.625 1.00 58.36 ? 51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.826 151.014 165.614 1.00 61.57 ? 52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 163.253 151.836 164.487 1.00 61.65 ? 52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.778 150.960 163.356 1.00 61.32 ? 52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 163.425 151.151 162.184 1.00 61.55 ? 52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 164.318 152.831 164.956 1.00 59.50 ? 52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 164.484 154.073 164.091 1.00 60.36 ? 52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 164.808 153.757 162.650 1.00 62.69 ? 52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 165.226 155.013 161.909 1.00 63.70 ? 52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 164.106 155.989 161.806 1.00 61.64 ? 52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 164.618 149.979 163.695 1.00 62.63 ? 53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 165.145 149.062 162.690 1.00 63.18 ? 53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 164.033 148.243 162.049 1.00 64.15 ? 53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 164.032 148.032 160.832 1.00 62.89 ? 53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 166.189 148.141 163.319 1.00 62.43 ? 53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.736 147.086 162.374 1.00 63.21 ? 53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 167.502 145.996 163.098 1.00 66.91 ? 53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 167.986 146.253 164.221 1.00 67.30 ? 53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 167.614 144.880 162.548 1.00 65.68 ? 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 163.087 147.756 162.855 1.00 62.96 ? 54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.981 146.980 162.305 1.00 60.21 ? 54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 161.159 147.812 161.330 1.00 56.85 ? 54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.797 147.337 160.247 1.00 60.10 ? 54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 161.098 146.453 163.435 1.00 59.39 ? 54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 160.189 145.307 163.028 1.00 61.35 ? 54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.828 145.431 163.688 1.00 59.66 ? 54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 158.120 144.091 163.750 1.00 60.39 ? 54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 158.413 143.372 165.018 1.00 60.10 ? 54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.856 149.057 161.698 1.00 57.53 ? 55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 160.084 149.923 160.815 1.00 58.31 ? 55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.843 150.214 159.529 1.00 59.79 ? 55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 160.259 150.201 158.439 1.00 62.77 ? 55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 159.723 151.220 161.538 1.00 59.74 ? 55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 158.620 151.092 162.591 1.00 60.26 ? 55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 158.362 152.421 163.278 1.00 59.51 ? 55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 157.348 150.560 161.957 1.00 58.76 ? 55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 162.147 150.480 159.633 1.00 63.38 ? 56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.939 150.716 158.431 1.00 62.93 ? 56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.942 149.492 157.526 1.00 61.71 ? 56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.744 149.608 156.312 1.00 63.50 ? 56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 164.366 151.109 158.810 1.00 63.86 ? 56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 164.440 152.482 159.437 1.00 64.66 ? 56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 163.465 153.251 159.296 1.00 65.30 ? 56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 165.470 152.797 160.068 1.00 63.09 ? 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 163.150 148.306 158.100 1.00 60.06 ? 57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 163.156 147.088 157.298 1.00 60.41 ? 57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.810 146.879 156.619 1.00 59.60 ? 57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.752 146.501 155.443 1.00 60.58 ? 57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 163.528 145.892 158.181 1.00 59.86 ? 57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 163.522 144.532 157.501 1.00 62.65 ? 57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 162.351 143.982 156.991 1.00 61.65 ? 57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 164.694 143.801 157.370 1.00 62.64 ? 57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 162.348 142.748 156.375 1.00 62.17 ? 57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 164.701 142.565 156.754 1.00 61.99 ? 57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 163.524 142.044 156.259 1.00 62.25 ? 57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 163.518 140.814 155.644 1.00 62.16 ? 57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.716 147.115 157.344 1.00 56.72 ? 58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 159.394 146.886 156.772 1.00 56.41 ? 58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 159.082 147.889 155.667 1.00 54.72 ? 58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 158.467 147.532 154.656 1.00 54.88 ? 58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 158.339 146.940 157.876 1.00 54.88 ? 58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 158.395 145.767 158.857 1.00 54.81 ? 58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 157.605 146.070 160.115 1.00 56.03 ? 58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.881 144.499 158.197 1.00 54.22 ? 58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 159.493 149.146 155.840 1.00 58.44 ? 59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 159.217 150.161 154.827 1.00 60.84 ? 59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 160.067 149.927 153.583 1.00 62.35 ? 59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 159.560 149.933 152.455 1.00 61.66 ? 59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 159.441 151.569 155.405 1.00 59.39 ? 59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 159.352 152.609 154.304 1.00 59.69 ? 59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 158.426 151.858 156.500 1.00 59.38 ? 59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 161.374 149.719 153.767 1.00 63.79 ? 60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 162.265 149.567 152.620 1.00 63.65 ? 60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.939 148.312 151.821 1.00 64.59 ? 60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.987 148.324 150.586 1.00 64.55 ? 60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 163.724 149.547 153.078 1.00 63.53 ? 60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 164.071 150.598 154.117 1.00 64.97 ? 60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 165.567 150.763 154.299 1.00 65.82 ? 60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.982 151.348 155.322 1.00 65.63 ? 60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 166.328 150.303 153.422 1.00 65.44 ? 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 161.603 147.219 152.504 1.00 60.99 ? 61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 161.341 145.951 151.838 1.00 59.00 ? 61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.938 145.867 151.251 1.00 60.44 ? 61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 159.466 144.762 150.956 1.00 61.07 ? 61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.580 144.791 152.805 1.00 59.83 ? 61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 163.054 144.499 153.004 1.00 62.45 ? 61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.625 143.644 152.328 1.00 62.32 ? 61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.678 145.211 153.933 1.00 61.82 ? 61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 159.268 147.005 151.074 1.00 58.23 ? 62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.971 147.057 150.401 1.00 59.45 ? 62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.913 146.259 151.159 1.00 59.25 ? 62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 156.005 145.675 150.564 1.00 60.07 ? 62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 158.086 146.570 148.956 1.00 59.80 ? 62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 159.094 147.340 148.116 1.00 58.76 ? 62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 158.929 148.842 148.234 1.00 60.56 ? 62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 159.342 149.448 149.221 1.00 61.95 ? 62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 158.323 149.452 147.222 1.00 60.55 ? 62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 157.030 146.229 152.485 1.00 55.32 ? 63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 156.029 145.599 153.337 1.00 54.92 ? 63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.986 146.581 153.846 1.00 54.34 ? 63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.803 146.237 153.924 1.00 54.52 ? 63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.699 144.912 154.531 1.00 55.05 ? 63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 157.320 143.575 154.203 1.00 55.07 ? 63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.563 142.557 153.640 1.00 55.40 ? 63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.661 143.329 154.461 1.00 54.98 ? 63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 157.125 141.333 153.339 1.00 56.61 ? 63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 159.232 142.109 154.165 1.00 55.13 ? 63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.460 141.114 153.604 1.00 59.02 ? 63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 159.026 139.897 153.308 1.00 59.51 ? 63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 155.397 147.799 154.189 1.00 52.38 ? 64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 154.506 148.823 154.708 1.00 50.15 ? 64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 154.443 150.000 153.745 1.00 54.26 ? 64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 155.392 150.268 153.004 1.00 57.81 ? 64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.966 149.328 156.079 1.00 49.22 ? 64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 154.660 148.399 157.226 1.00 51.83 ? 64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.786 147.333 157.071 1.00 49.70 ? 64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 155.242 148.594 158.469 1.00 52.20 ? 64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 153.506 146.484 158.122 1.00 47.75 ? 64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.967 147.754 159.524 1.00 50.63 ? 64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 154.101 146.700 159.346 1.00 50.89 ? 64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.828 145.861 160.400 1.00 52.81 ? 64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 153.313 150.699 153.766 1.00 58.95 ? 65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 153.187 151.963 153.054 1.00 54.85 ? 65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.852 153.057 153.879 1.00 58.41 ? 65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 153.461 153.303 155.025 1.00 59.30 ? 65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.718 152.290 152.799 1.00 53.95 ? 65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 151.031 151.346 151.826 1.00 55.54 ? 65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 149.550 151.638 151.678 1.00 59.40 ? 65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 149.007 152.405 152.500 1.00 58.44 ? 65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.930 151.103 150.735 1.00 58.34 ? 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.862 153.710 153.304 1.00 60.04 ? 66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 155.620 154.712 154.041 1.00 60.90 ? 66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 154.849 156.008 154.249 1.00 59.82 ? 66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 155.196 156.779 155.150 1.00 58.64 ? 66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 156.938 155.011 153.322 1.00 60.59 ? 66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 156.775 155.681 151.967 1.00 60.27 ? 66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 156.430 154.696 150.867 1.00 62.64 ? 66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 155.481 153.905 151.052 1.00 60.54 ? 66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 157.108 154.712 149.819 1.00 63.06 ? 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 153.816 156.265 153.445 1.00 58.67 ? 67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 153.112 157.541 153.530 1.00 57.19 ? 67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 152.413 157.704 154.874 1.00 58.31 ? 67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 152.522 158.753 155.520 1.00 58.16 ? 67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 152.109 157.665 152.382 1.00 57.54 ? 67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 152.706 157.427 151.005 1.00 57.43 ? 67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 152.355 156.063 150.445 1.00 60.26 ? 67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 151.157 155.814 150.195 1.00 61.69 ? 67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 153.275 155.240 150.256 1.00 59.48 ? 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 151.686 156.674 155.316 1.00 53.23 ? 68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 150.925 156.802 156.555 1.00 49.62 ? 68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 151.836 156.838 157.774 1.00 49.25 ? 68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 151.507 157.492 158.770 1.00 51.75 ? 68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 149.905 155.667 156.672 1.00 50.52 ? 68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 150.410 154.459 157.409 1.00 50.26 ? 68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 151.114 153.471 156.744 1.00 50.23 ? 68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 150.169 154.306 158.763 1.00 47.60 ? 68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 151.575 152.359 157.418 1.00 48.45 ? 68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.628 153.197 159.441 1.00 47.29 ? 68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 151.331 152.222 158.767 1.00 49.87 ? 68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.975 156.148 157.721 1.00 52.57 ? 69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.929 156.191 158.821 1.00 51.01 ? 69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 154.718 157.492 158.859 1.00 52.61 ? 69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 155.327 157.801 159.888 1.00 54.42 ? 69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.893 155.008 158.731 1.00 50.68 ? 69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 154.396 153.679 159.301 1.00 52.11 ? 69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 155.322 152.546 158.895 1.00 50.25 ? 69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 154.274 153.759 160.814 1.00 51.59 ? 69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 154.720 158.256 157.766 1.00 56.41 ? 70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 155.453 159.515 157.717 1.00 51.99 ? 70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 154.735 160.646 158.440 1.00 54.26 ? 70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 155.326 161.716 158.616 1.00 54.38 ? 70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 155.708 159.915 156.265 1.00 52.30 ? 70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 154.551 160.488 155.684 1.00 53.84 ? 70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 153.485 160.442 158.856 1.00 48.97 ? 71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 152.737 161.472 159.563 1.00 46.80 ? 71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 153.063 161.527 161.048 1.00 48.65 ? 71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 152.571 162.425 161.739 1.00 48.52 ? 71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 151.234 161.252 159.378 1.00 47.76 ? 71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 150.761 160.992 157.947 1.00 50.60 ? 71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 149.318 160.519 157.935 1.00 48.23 ? 71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 150.927 162.241 157.098 1.00 47.53 ? 71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 153.871 160.599 161.550 1.00 46.98 ? 72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 154.240 160.550 162.956 1.00 48.27 ? 72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 155.750 160.653 163.098 1.00 49.47 ? 72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 156.498 160.031 162.337 1.00 50.17 ? 72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 153.770 159.250 163.616 1.00 47.83 ? 72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 152.293 158.975 163.502 1.00 44.54 ? 72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 151.403 159.446 164.457 1.00 45.65 ? 72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 151.789 158.231 162.446 1.00 42.27 ? 72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 150.052 159.189 164.357 1.00 44.51 ? 72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 150.441 157.970 162.338 1.00 43.12 ? 72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 149.577 158.450 163.296 1.00 43.65 ? 72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 148.233 158.191 163.190 1.00 45.48 ? 72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 156.194 161.437 164.074 1.00 53.22 ? 73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 157.576 161.345 164.509 1.00 53.40 ? 73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 157.817 159.970 165.117 1.00 55.37 ? 73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 156.921 159.368 165.715 1.00 56.47 ? 73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 157.896 162.441 165.524 1.00 53.52 ? 73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 157.389 162.112 166.805 1.00 53.84 ? 73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 159.040 159.461 164.956 1.00 58.57 ? 74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 159.315 158.114 165.444 1.00 55.78 ? 74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 159.064 157.999 166.941 1.00 57.34 ? 74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 158.781 156.904 167.438 1.00 59.32 ? 74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 160.747 157.699 165.118 1.00 56.37 ? 74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 161.097 156.330 165.623 1.00 58.50 ? 74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 160.568 155.201 165.020 1.00 57.38 ? 74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.932 156.172 166.715 1.00 57.76 ? 74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 160.877 153.941 165.488 1.00 59.23 ? 74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 162.245 154.912 167.187 1.00 57.76 ? 74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 161.716 153.797 166.574 1.00 58.74 ? 74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 159.155 159.109 167.674 1.00 57.08 ? 75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 158.808 159.079 169.090 1.00 58.59 ? 75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 157.346 158.697 169.285 1.00 59.43 ? 75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 157.017 157.883 170.157 1.00 60.88 ? 75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 159.098 160.436 169.731 1.00 57.15 ? 75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 160.576 160.728 169.925 1.00 58.75 ? 75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 161.264 159.694 170.793 1.00 63.37 ? 75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.766 159.424 171.906 1.00 63.27 ? 75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 162.305 159.152 170.364 1.00 61.33 ? 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 156.453 159.266 168.472 1.00 54.43 ? 76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 155.035 158.944 168.588 1.00 52.61 ? 76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 154.757 157.499 168.190 1.00 52.27 ? 76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 153.942 156.821 168.826 1.00 55.28 ? 76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 154.209 159.905 167.736 1.00 53.89 ? 76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 154.281 161.333 168.237 1.00 55.39 ? 76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 154.174 161.539 169.464 1.00 55.40 ? 76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 154.438 162.250 167.404 1.00 56.07 ? 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 155.415 157.014 167.136 1.00 49.21 ? 77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 155.244 155.619 166.738 1.00 49.91 ? 77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 155.715 154.691 167.849 1.00 48.30 ? 77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 155.072 153.677 168.149 1.00 49.81 ? 77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 155.987 155.345 165.418 1.00 50.14 ? 77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 155.342 156.126 164.272 1.00 49.52 ? 77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 155.997 153.856 165.113 1.00 49.43 ? 77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 156.154 156.123 163.000 1.00 49.59 ? 77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 156.849 155.019 168.472 1.00 50.52 ? 78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 157.343 154.218 169.584 1.00 52.84 ? 78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 156.366 154.239 170.751 1.00 51.60 ? 78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 156.136 153.210 171.394 1.00 54.07 ? 78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 158.719 154.722 170.021 1.00 53.36 ? 78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 159.436 153.814 171.004 1.00 52.49 ? 78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 160.846 154.312 171.282 1.00 54.69 ? 78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.254 154.050 172.722 1.00 53.89 ? 78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 161.512 155.316 173.463 1.00 53.15 ? 78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 155.786 155.404 171.044 1.00 49.46 ? 79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.803 155.485 172.119 1.00 48.04 ? 79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 153.583 154.624 171.815 1.00 48.82 ? 79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 153.067 153.930 172.699 1.00 50.05 ? 79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 154.390 156.939 172.346 1.00 49.01 ? 79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 155.039 157.586 173.558 1.00 51.41 ? 79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 155.262 156.604 174.690 1.00 54.22 ? 79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 154.315 156.366 175.470 1.00 54.73 ? 79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 156.385 156.068 174.801 1.00 53.47 ? 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 153.111 154.652 170.568 1.00 44.17 ? 80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.954 153.845 170.193 1.00 41.84 ? 80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 152.272 152.361 170.325 1.00 46.95 ? 80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 151.468 151.579 170.851 1.00 47.24 ? 80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 151.495 154.203 168.767 1.00 44.04 ? 80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 150.385 153.269 168.312 1.00 43.48 ? 80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 151.041 155.651 168.706 1.00 43.56 ? 80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 153.448 151.947 169.850 1.00 46.81 ? 81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.823 150.540 169.946 1.00 42.94 ? 81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.980 150.107 171.399 1.00 46.11 ? 81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 153.604 148.987 171.760 1.00 47.25 ? 81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 155.104 150.283 169.155 1.00 42.74 ? 81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.862 149.921 167.719 1.00 39.78 ? 81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 154.555 150.897 166.789 1.00 43.14 ? 81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.934 148.605 167.301 1.00 41.98 ? 81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 154.329 150.567 165.467 1.00 45.50 ? 81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.708 148.269 165.981 1.00 42.11 ? 81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 154.406 149.252 165.064 1.00 43.10 ? 81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 154.531 150.978 172.247 1.00 45.24 ? 82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 154.610 150.672 173.671 1.00 44.33 ? 82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 153.220 150.534 174.275 1.00 45.15 ? 82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.983 149.657 175.114 1.00 46.39 ? 82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 155.404 151.755 174.401 1.00 45.21 ? 82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 156.824 151.942 173.898 1.00 48.52 ? 82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 157.720 152.519 174.982 1.00 50.57 ? 82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 159.178 152.162 174.745 1.00 49.94 ? 82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.338 151.210 173.613 1.00 52.44 ? 82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 152.289 151.396 173.865 1.00 44.66 ? 83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.917 151.284 174.343 1.00 44.49 ? 83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 150.315 149.940 173.959 1.00 44.38 ? 83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 149.652 149.290 174.776 1.00 42.46 ? 83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 150.070 152.427 173.786 1.00 41.84 ? 83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 150.614 153.681 174.216 1.00 46.55 ? 83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 148.635 152.312 174.271 1.00 43.58 ? 83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 150.535 149.506 172.717 1.00 42.38 ? 84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 150.039 148.197 172.305 1.00 40.25 ? 84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.693 147.080 173.109 1.00 40.87 ? 84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 150.019 146.139 173.542 1.00 46.06 ? 84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 150.272 147.992 170.810 1.00 39.61 ? 84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 152.007 147.168 173.322 1.00 46.99 ? 85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.733 146.119 174.027 1.00 43.73 ? 85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 152.555 146.178 175.538 1.00 45.98 ? 85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.707 145.149 176.204 1.00 45.42 ? 85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 154.222 146.194 173.684 1.00 42.93 ? 85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 154.611 145.356 172.489 1.00 42.52 ? 85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 154.700 143.975 172.587 1.00 44.89 ? 85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.885 145.945 171.263 1.00 45.35 ? 85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 155.054 143.204 171.498 1.00 45.34 ? 85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 155.240 145.184 170.169 1.00 45.77 ? 85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 155.323 143.813 170.292 1.00 46.03 ? 85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 155.675 143.049 169.206 1.00 50.43 ? 85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 152.239 147.350 176.093 1.00 47.59 ? 86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 152.117 147.469 177.542 1.00 43.98 ? 86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 151.025 146.565 178.096 1.00 45.34 ? 86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 151.097 146.147 179.257 1.00 47.43 ? 86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 151.846 148.923 177.928 1.00 44.33 ? 86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 150.011 146.251 177.289 1.00 45.81 ? 87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 148.906 145.426 177.762 1.00 45.91 ? 87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 149.331 143.997 178.073 1.00 48.49 ? 87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 148.670 143.331 178.876 1.00 47.12 ? 87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 147.779 145.412 176.730 1.00 47.53 ? 87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 146.407 145.142 177.319 1.00 48.20 ? 87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 145.684 144.052 176.547 1.00 46.35 ? 87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 144.241 143.920 177.002 1.00 45.89 ? 87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 144.097 144.161 178.463 1.00 46.33 ? 87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 150.413 143.514 177.464 1.00 50.02 ? 88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.840 142.125 177.622 1.00 45.05 ? 88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 149.708 141.171 177.246 1.00 43.42 ? 88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 149.399 140.217 177.963 1.00 47.99 ? 88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 151.335 141.860 179.045 1.00 45.92 ? 88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 152.260 142.933 179.589 1.00 47.07 ? 88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 153.711 142.621 179.271 1.00 48.45 ? 88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 154.283 141.611 180.250 1.00 49.55 ? 88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 154.151 142.075 181.659 1.00 48.03 ? 88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 149.081 141.445 176.105 1.00 42.54 ? 89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 147.949 140.645 175.663 1.00 38.86 ? 89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 148.368 139.200 175.426 1.00 41.78 ? 89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 149.402 138.926 174.811 1.00 43.45 ? 89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 147.353 141.232 174.383 1.00 40.58 ? 89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 146.329 140.348 173.736 1.00 38.45 ? 89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 145.019 140.344 174.180 1.00 37.30 ? 89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.677 139.514 172.688 1.00 39.93 ? 89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 144.078 139.528 173.591 1.00 39.83 ? 89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.738 138.697 172.095 1.00 36.99 ? 89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 144.437 138.704 172.547 1.00 37.52 ? 89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 147.549 138.274 175.915 1.00 46.37 ? 90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 147.780 136.847 175.744 1.00 42.24 ? 90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 146.556 136.222 175.094 1.00 44.30 ? 90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 145.427 136.464 175.531 1.00 47.76 ? 90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 148.071 136.167 177.085 1.00 46.37 ? 90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 149.307 136.690 177.789 1.00 47.77 ? 90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 150.563 136.368 177.002 1.00 48.86 ? 90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 151.754 136.927 177.628 1.00 49.24 ? 90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 152.409 137.986 177.175 1.00 49.26 ? 90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 152.018 138.626 176.086 1.00 49.65 ? 90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 153.485 138.412 177.829 1.00 48.11 ? 90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 146.780 135.433 174.054 1.00 40.35 ? 91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 145.685 134.705 173.431 1.00 39.15 ? 91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 145.158 133.653 174.400 1.00 43.83 ? 91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.947 132.880 174.955 1.00 46.77 ? 91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 146.145 134.050 172.133 1.00 38.31 ? 91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 146.327 135.016 171.000 1.00 40.70 ? 91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 145.239 135.453 170.263 1.00 41.68 ? 91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 147.584 135.490 170.672 1.00 41.13 ? 91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 145.404 136.342 169.220 1.00 40.33 ? 91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 147.754 136.379 169.631 1.00 41.67 ? 91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.663 136.805 168.904 1.00 38.79 ? 91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 143.844 133.590 174.634 1.00 43.98 ? 92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 143.323 132.631 175.617 1.00 42.98 ? 92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 143.214 131.212 175.094 1.00 44.07 ? 92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.059 130.286 175.901 1.00 45.15 ? 92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.942 133.200 175.954 1.00 45.11 ? 92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 141.515 133.855 174.680 1.00 44.05 ? 92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 142.770 134.396 174.027 1.00 42.67 ? 92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 143.293 131.008 173.782 1.00 41.81 ? 93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 143.142 129.688 173.194 1.00 40.61 ? 93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 144.125 129.535 172.044 1.00 42.30 ? 93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 144.621 130.517 171.488 1.00 44.47 ? 93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.707 129.451 172.706 1.00 43.98 ? 93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.513 129.977 171.406 1.00 45.31 ? 93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.406 128.279 171.696 1.00 44.94 ? 94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.331 128.008 170.601 1.00 43.39 ? 94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.772 128.491 169.269 1.00 41.45 ? 94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.521 128.981 168.417 1.00 45.37 ? 94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.646 126.515 170.533 1.00 43.45 ? 94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.214 126.079 169.213 1.00 43.45 ? 94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.476 126.487 168.818 1.00 42.49 ? 94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.478 125.278 168.359 1.00 45.55 ? 94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.996 126.093 167.600 1.00 43.20 ? 94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 145.993 124.882 167.141 1.00 43.74 ? 94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.254 125.290 166.762 1.00 42.28 ? 94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.460 128.351 169.065 1.00 42.07 ? 95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.881 128.682 167.768 1.00 40.51 ? 95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.986 130.171 167.467 1.00 44.61 ? 95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 143.178 130.556 166.312 1.00 47.46 ? 95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.426 128.223 167.706 1.00 45.56 ? 95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.953 127.864 166.307 1.00 47.18 ? 95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 142.054 126.706 165.473 1.00 58.80 ? 95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.062 125.353 166.644 1.00 47.39 ? 95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.861 131.025 168.484 1.00 38.62 ? 96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 142.968 132.463 168.250 1.00 34.16 ? 96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 144.336 132.826 167.688 1.00 37.96 ? 96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.444 133.484 166.644 1.00 40.50 ? 96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 142.703 133.223 169.548 1.00 39.21 ? 96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 141.544 132.735 170.196 1.00 48.18 ? 96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.399 132.396 168.372 1.00 39.34 ? 97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 146.750 132.696 167.915 1.00 37.47 ? 97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 147.042 132.024 166.582 1.00 38.76 ? 97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 147.691 132.616 165.713 1.00 41.59 ? 97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 147.767 132.267 168.970 1.00 38.84 ? 97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.577 130.787 166.401 1.00 36.26 ? 98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.795 130.101 165.134 1.00 36.34 ? 98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 146.152 130.866 163.985 1.00 40.58 ? 98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 146.782 131.098 162.948 1.00 44.37 ? 98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 146.247 128.677 165.207 1.00 40.04 ? 98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.350 127.923 163.914 1.00 43.09 ? 98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.544 127.336 163.533 1.00 43.71 ? 98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.257 127.809 163.073 1.00 42.58 ? 98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.644 126.646 162.343 1.00 43.05 ? 98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.351 127.122 161.881 1.00 44.08 ? 98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.545 126.539 161.516 1.00 43.95 ? 98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.897 131.283 164.161 1.00 39.75 ? 99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 144.205 132.024 163.115 1.00 40.49 ? 99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 144.911 133.339 162.825 1.00 41.72 ? 99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 145.126 133.697 161.661 1.00 43.38 ? 99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 142.752 132.272 163.522 1.00 41.00 ? 99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.878 131.030 163.506 1.00 45.10 ? 99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 142.071 130.231 162.231 1.00 44.72 ? 99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.742 129.945 161.556 1.00 42.86 ? 99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 140.888 129.770 160.086 1.00 45.26 ? 99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 145.294 134.073 163.873 1.00 37.29 ? 100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 145.965 135.347 163.644 1.00 36.78 ? 100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 147.268 135.151 162.882 1.00 37.00 ? 100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.499 135.790 161.851 1.00 42.39 ? 100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 146.229 136.067 164.964 1.00 37.42 ? 100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 147.047 137.315 164.802 1.00 39.02 ? 100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 146.499 138.448 164.224 1.00 38.29 ? 100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 148.372 137.347 165.199 1.00 34.34 ? 100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 147.252 139.593 164.061 1.00 39.20 ? 100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 149.130 138.488 165.039 1.00 37.15 ? 100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 148.570 139.613 164.469 1.00 39.31 ? 100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 148.125 134.251 163.361 1.00 40.77 ? 101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.446 134.087 162.774 1.00 40.40 ? 101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.431 133.302 161.471 1.00 40.20 ? 101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.472 133.215 160.813 1.00 47.74 ? 101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 150.380 133.422 163.785 1.00 39.30 ? 101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 150.796 134.365 164.887 1.00 39.69 ? 101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.749 135.347 164.661 1.00 36.35 ? 101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 150.212 134.297 166.143 1.00 41.02 ? 101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 152.124 136.219 165.659 1.00 38.63 ? 101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.579 135.167 167.147 1.00 39.74 ? 101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.535 136.126 166.900 1.00 40.12 ? 101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 151.906 136.995 167.898 1.00 39.35 ? 101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 148.293 132.729 161.082 1.00 43.08 ? 102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 148.188 132.092 159.779 1.00 43.24 ? 102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 147.470 132.945 158.743 1.00 43.01 ? 102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.712 132.762 157.545 1.00 44.96 ? 102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.468 130.744 159.903 1.00 41.97 ? 102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.382 129.639 160.389 1.00 47.53 ? 102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 149.213 129.848 161.272 1.00 49.01 ? 102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 148.237 128.455 159.809 1.00 46.37 ? 102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.607 133.869 159.160 1.00 41.74 ? 103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.836 134.677 158.224 1.00 41.03 ? 103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 146.241 136.142 158.191 1.00 40.03 ? 103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 146.366 136.713 157.107 1.00 45.56 ? 103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 144.342 134.584 158.556 1.00 41.56 ? 103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 143.878 133.157 158.769 1.00 44.06 ? 103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.630 132.370 159.380 1.00 45.77 ? 103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.757 132.824 158.330 1.00 48.17 ? 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 146.452 136.772 159.346 1.00 35.25 ? 104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.621 138.217 159.414 1.00 39.29 ? 104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 148.032 138.662 159.762 1.00 40.58 ? 104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 148.417 139.774 159.397 1.00 44.14 ? 104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.645 138.812 160.438 1.00 37.09 ? 104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 144.215 138.382 160.209 1.00 39.90 ? 104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 143.730 137.201 160.756 1.00 34.86 ? 104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.354 139.144 159.432 1.00 38.68 ? 104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 142.429 136.798 160.544 1.00 37.19 ? 104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 142.051 138.749 159.215 1.00 37.12 ? 104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.593 137.575 159.773 1.00 40.17 ? 104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 140.295 137.176 159.559 1.00 39.01 ? 104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.810 137.833 160.452 1.00 43.93 ? 105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 150.172 138.216 160.798 1.00 40.43 ? 105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 151.015 138.361 159.539 1.00 44.75 ? 105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 151.068 137.455 158.703 1.00 44.56 ? 105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.793 137.183 161.737 1.00 39.65 ? 105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.673 139.510 159.404 1.00 49.54 ? 106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.523 139.746 158.246 1.00 46.86 ? 106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.691 138.769 158.239 1.00 49.23 ? 106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 154.379 138.595 159.249 1.00 47.13 ? 106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 153.036 141.186 158.248 1.00 47.92 ? 106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.962 141.581 157.095 1.00 45.94 ? 106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 153.181 141.723 155.801 1.00 45.49 ? 106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.704 142.867 157.418 1.00 48.66 ? 106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.913 138.135 157.093 1.00 55.82 ? 107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 154.989 137.175 156.916 1.00 54.78 ? 107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.898 137.622 155.781 1.00 56.39 ? 107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.480 138.356 154.881 1.00 58.89 ? 107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.444 135.773 156.623 1.00 54.78 ? 107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 154.242 134.919 157.859 1.00 53.47 ? 107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 153.265 133.792 157.592 1.00 55.25 ? 107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 152.375 133.546 158.795 1.00 55.87 ? 107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 152.440 132.134 159.264 1.00 56.81 ? 107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 157.150 137.176 155.837 1.00 63.32 ? 108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 158.102 137.486 154.783 1.00 62.76 ? 108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.559 137.031 153.430 1.00 62.84 ? 108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.629 136.226 153.341 1.00 63.04 ? 108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.449 136.822 155.066 1.00 61.77 ? 108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 159.257 135.418 155.277 1.00 64.87 ? 108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 160.090 137.430 156.304 1.00 58.88 ? 108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 158.161 137.562 152.362 1.00 63.95 ? 109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.649 137.295 151.021 1.00 64.76 ? 109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.608 135.803 150.717 1.00 67.24 ? 109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.804 135.362 149.888 1.00 66.93 ? 109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.496 138.025 149.978 1.00 63.21 ? 109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.972 139.381 150.458 1.00 65.72 ? 109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 159.736 139.479 151.418 1.00 67.07 ? 109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 158.518 140.437 149.793 1.00 64.37 ? 109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.458 135.015 151.369 1.00 69.11 ? 110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.458 133.568 151.202 1.00 69.08 ? 110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.492 132.863 152.146 1.00 70.67 ? 110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.389 131.633 152.099 1.00 70.16 ? 110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 159.874 133.016 151.398 1.00 68.81 ? 110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.356 133.139 152.830 1.00 71.80 ? 110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 159.716 133.868 153.616 1.00 72.04 ? 110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.380 132.510 153.169 1.00 71.42 ? 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.784 133.609 152.995 1.00 68.77 ? 111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 155.854 133.027 153.962 1.00 68.39 ? 111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.561 132.022 154.868 1.00 69.29 ? 111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 156.015 130.972 155.209 1.00 70.03 ? 111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.658 132.382 153.260 1.00 68.72 ? 111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.665 133.380 152.686 1.00 69.14 ? 111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 154.151 133.945 151.362 1.00 69.28 ? 111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 153.298 135.120 150.914 1.00 69.63 ? 111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 153.390 136.268 151.858 1.00 69.38 ? 111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 157.789 132.348 155.260 1.00 68.98 ? 112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.600 131.492 156.116 1.00 68.89 ? 112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 158.747 132.023 157.532 1.00 68.08 ? 112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.700 131.243 158.486 1.00 68.93 ? 112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.992 131.301 155.498 1.00 68.36 ? 112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 161.090 130.940 156.488 1.00 68.62 ? 112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 160.779 129.648 157.227 1.00 69.50 ? 112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.386 129.652 158.621 1.00 69.40 ? 112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.846 130.753 159.464 1.00 68.38 ? 112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 158.916 133.331 157.696 1.00 62.09 ? 113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 159.096 133.953 158.998 1.00 60.97 ? 113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 157.940 134.901 159.288 1.00 61.58 ? 113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 157.195 135.308 158.393 1.00 60.32 ? 113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.431 134.704 159.068 1.00 60.66 ? 113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.628 133.819 159.358 1.00 61.33 ? 113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.655 133.400 160.816 1.00 63.61 ? 113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 162.916 132.620 161.143 1.00 62.03 ? 113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 162.916 132.145 162.553 1.00 61.63 ? 113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 157.799 135.251 160.563 1.00 55.72 ? 114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 156.752 136.152 161.033 1.00 53.62 ? 114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 157.382 137.512 161.296 1.00 54.58 ? 114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 158.306 137.631 162.110 1.00 56.68 ? 114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 156.064 135.613 162.296 1.00 54.14 ? 114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 155.290 134.333 161.980 1.00 54.38 ? 114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 155.142 136.664 162.892 1.00 54.93 ? 114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 154.977 133.496 163.199 1.00 52.29 ? 114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.881 138.538 160.609 1.00 51.13 ? 115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 157.363 139.899 160.797 1.00 51.57 ? 115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 156.507 140.715 161.754 1.00 51.66 ? 115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.999 141.702 162.311 1.00 51.75 ? 115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 157.438 140.627 159.451 1.00 51.71 ? 115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 158.635 140.283 158.565 1.00 50.05 ? 115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 158.415 140.800 157.157 1.00 49.98 ? 115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 159.915 140.851 159.155 1.00 52.37 ? 115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 155.250 140.332 161.958 1.00 50.83 ? 116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 154.329 141.063 162.815 1.00 47.69 ? 116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.791 140.158 163.912 1.00 46.32 ? 116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 153.430 139.005 163.659 1.00 48.09 ? 116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 153.154 141.628 162.015 1.00 47.33 ? 116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 153.326 143.059 161.558 1.00 48.08 ? 116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 152.179 143.519 160.685 1.00 49.28 ? 116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 151.266 142.708 160.427 1.00 47.76 ? 116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 152.185 144.693 160.263 1.00 50.76 ? 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.738 140.692 165.127 1.00 41.46 ? 117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 152.985 140.076 166.203 1.00 41.30 ? 117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.597 140.709 166.261 1.00 43.58 ? 117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 151.256 141.592 165.471 1.00 45.06 ? 117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.720 140.228 167.533 1.00 44.32 ? 117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 155.202 139.916 167.465 1.00 44.87 ? 117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 155.446 138.509 166.946 1.00 47.44 ? 117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 155.123 137.487 167.936 1.00 46.63 ? 117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.634 137.431 169.158 1.00 48.01 ? 117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.501 138.333 169.589 1.00 47.56 ? 117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 155.267 136.444 169.970 1.00 47.81 ? 117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.778 140.255 167.210 1.00 41.39 ? 118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 149.468 140.870 167.387 1.00 36.05 ? 118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 149.608 142.344 167.745 1.00 36.86 ? 118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.879 143.193 167.218 1.00 36.77 ? 118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.678 140.123 168.460 1.00 33.74 ? 118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 147.204 140.446 168.469 1.00 36.39 ? 118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 146.423 140.235 167.342 1.00 32.81 ? 118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 146.593 140.961 169.603 1.00 37.20 ? 118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 145.078 140.528 167.343 1.00 33.45 ? 118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 145.246 141.255 169.614 1.00 33.90 ? 118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 144.494 141.036 168.481 1.00 37.27 ? 118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 143.150 141.330 168.485 1.00 41.16 ? 118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 150.552 142.666 168.631 1.00 42.55 ? 119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 150.773 144.057 169.008 1.00 36.31 ? 119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 151.228 144.890 167.816 1.00 41.45 ? 119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.803 146.038 167.659 1.00 43.98 ? 119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 151.796 144.138 170.140 1.00 39.22 ? 119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 151.254 143.723 171.495 1.00 36.97 ? 119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 151.317 142.227 171.715 1.00 43.98 ? 119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.260 141.476 170.719 1.00 44.85 ? 119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 151.420 141.802 172.885 1.00 48.91 ? 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 152.097 144.335 166.970 1.00 44.13 ? 120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 152.574 145.084 165.811 1.00 39.61 ? 120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 151.434 145.395 164.848 1.00 40.19 ? 120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 151.302 146.526 164.367 1.00 43.73 ? 120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.684 144.306 165.104 1.00 42.08 ? 120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.886 144.066 165.994 1.00 48.21 ? 120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 155.443 145.052 166.521 1.00 48.42 ? 120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 155.279 142.893 166.164 1.00 48.19 ? 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 150.598 144.397 164.553 1.00 38.70 ? 121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 149.461 144.628 163.669 1.00 34.15 ? 121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 148.493 145.636 164.273 1.00 37.85 ? 121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.993 146.525 163.573 1.00 38.98 ? 121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.751 143.308 163.371 1.00 35.06 ? 121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 147.588 143.424 162.396 1.00 33.76 ? 121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 148.028 143.166 160.965 1.00 34.49 ? 121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 148.890 144.226 160.455 1.00 38.32 ? 121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 148.521 145.127 159.555 1.00 36.58 ? 121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 147.308 145.123 159.029 1.00 36.22 ? 121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 149.392 146.055 159.172 1.00 38.63 ? 121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 148.218 145.517 165.575 1.00 34.10 ? 122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 147.316 146.458 166.231 1.00 28.86 ? 122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.873 147.873 166.151 1.00 32.66 ? 122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 147.143 148.826 165.859 1.00 36.59 ? 122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 147.064 146.033 167.689 1.00 34.88 ? 122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 146.274 144.723 167.741 1.00 32.72 ? 122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 146.322 147.126 168.444 1.00 32.93 ? 122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 145.124 144.670 166.772 1.00 32.81 ? 122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 149.170 148.035 166.418 1.00 36.22 ? 123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 149.779 149.360 166.379 1.00 31.64 ? 123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 149.751 149.942 164.973 1.00 33.17 ? 123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 149.481 151.134 164.794 1.00 35.89 ? 123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 151.215 149.294 166.901 1.00 35.47 ? 123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 151.255 148.800 168.226 1.00 40.71 ? 123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 150.035 149.120 163.961 1.00 33.64 ? 124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 150.005 149.613 162.588 1.00 33.53 ? 124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 148.594 150.041 162.208 1.00 34.79 ? 124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 148.393 151.089 161.583 1.00 34.99 ? 124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 150.556 148.550 161.622 1.00 39.81 ? 124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 152.065 148.394 161.814 1.00 40.04 ? 124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 150.236 148.920 160.183 1.00 37.06 ? 124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 152.853 149.638 161.473 1.00 37.38 ? 124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 147.593 149.242 162.585 1.00 34.47 ? 125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 146.209 149.593 162.280 1.00 29.71 ? 125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 145.812 150.878 162.995 1.00 25.63 ? 125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 145.124 151.734 162.427 1.00 31.47 ? 125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 145.271 148.427 162.640 1.00 34.08 ? 125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.821 148.846 162.488 1.00 30.22 ? 125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 145.574 147.218 161.770 1.00 28.40 ? 125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 146.227 151.032 164.254 1.00 24.38 ? 126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 145.891 152.236 165.006 1.00 28.06 ? 126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 146.555 153.469 164.408 1.00 31.07 ? 126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 145.942 154.539 164.342 1.00 33.55 ? 126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 146.290 152.070 166.472 1.00 30.21 ? 126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 147.811 153.342 163.976 1.00 34.66 ? 127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 148.493 154.470 163.351 1.00 29.43 ? 127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 147.859 154.818 162.011 1.00 29.40 ? 127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 147.771 155.996 161.646 1.00 34.33 ? 127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.979 154.156 163.181 1.00 32.39 ? 127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 150.826 154.146 164.455 1.00 32.68 ? 127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 152.160 153.464 164.208 1.00 37.16 ? 127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 151.036 155.556 164.976 1.00 32.27 ? 127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 147.417 153.806 161.263 1.00 32.02 ? 128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 146.701 154.061 160.019 1.00 33.45 ? 128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 145.382 154.778 160.283 1.00 30.39 ? 128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 145.014 155.707 159.556 1.00 38.92 ? 128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 146.468 152.741 159.281 1.00 30.62 ? 128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 145.489 152.839 158.151 1.00 33.33 ? 128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 145.878 153.341 156.922 1.00 36.79 ? 128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 144.179 152.424 158.315 1.00 34.22 ? 128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 144.979 153.430 155.879 1.00 36.17 ? 128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 143.275 152.512 157.276 1.00 33.83 ? 128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.676 153.017 156.057 1.00 34.21 ? 128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 144.658 154.357 161.322 1.00 29.93 ? 129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 143.388 154.994 161.656 1.00 27.26 ? 129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 143.587 156.437 162.102 1.00 27.36 ? 129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 142.846 157.332 161.681 1.00 34.41 ? 129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 142.678 154.200 162.753 1.00 25.10 ? 129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 142.040 152.932 162.272 1.00 24.05 ? 129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.710 152.766 160.939 1.00 27.86 ? 129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 141.762 151.906 163.158 1.00 25.80 ? 129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 141.120 151.599 160.498 1.00 27.45 ? 129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 141.171 150.737 162.723 1.00 25.75 ? 129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 140.851 150.584 161.391 1.00 28.81 ? 129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 144.584 156.682 162.956 1.00 32.00 ? 130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 144.736 157.999 163.563 1.00 33.63 ? 130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 145.078 159.067 162.534 1.00 40.38 ? 130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 144.820 160.252 162.769 1.00 45.65 ? 130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 145.802 157.951 164.655 1.00 35.72 ? 130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 145.653 158.675 161.398 1.00 42.21 ? 131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.949 159.610 160.314 1.00 42.29 ? 131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 146.803 160.778 160.803 1.00 39.98 ? 131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 146.574 161.934 160.442 1.00 43.09 ? 131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 144.659 160.113 159.663 1.00 40.56 ? 131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.901 160.770 158.321 1.00 43.24 ? 131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.659 160.262 157.496 1.00 45.35 ? 131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 144.251 161.904 158.094 1.00 40.55 ? 131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 147.797 160.476 161.636 1.00 43.78 ? 132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 148.708 161.480 162.141 1.00 43.02 ? 132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 148.436 161.964 163.548 1.00 45.94 ? 132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 149.151 162.855 164.023 1.00 49.85 ? 132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 147.437 161.413 164.230 1.00 46.67 ? 133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 147.110 161.798 165.597 1.00 43.16 ? 133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 147.652 160.742 166.552 1.00 47.28 ? 133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 147.201 159.592 166.532 1.00 49.37 ? 133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 145.601 161.961 165.771 1.00 46.65 ? 133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 145.237 162.708 167.037 1.00 50.59 ? 133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 146.057 162.722 167.979 1.00 48.86 ? 133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 144.130 163.282 167.090 1.00 49.37 ? 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 148.611 161.136 167.392 1.00 47.44 ? 134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 149.245 160.174 168.288 1.00 45.03 ? 134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 148.308 159.760 169.416 1.00 46.86 ? 134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 148.233 158.576 169.762 1.00 50.29 ? 134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 150.540 160.756 168.851 1.00 48.82 ? 134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 151.432 161.060 167.772 1.00 52.88 ? 134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 151.208 159.761 169.787 1.00 46.52 ? 134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 147.593 160.717 170.010 1.00 47.80 ? 135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 146.636 160.370 171.056 1.00 45.55 ? 135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 145.504 159.517 170.499 1.00 48.24 ? 135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 145.067 158.551 171.138 1.00 51.24 ? 135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 146.088 161.639 171.707 1.00 48.34 ? 135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.011 161.573 173.222 1.00 51.71 ? 135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.284 161.035 173.846 1.00 54.19 ? 135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 148.379 161.488 173.451 1.00 51.32 ? 135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 147.190 160.160 174.732 1.00 53.53 ? 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 145.015 159.859 169.306 1.00 38.66 ? 136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.996 159.037 168.665 1.00 37.35 ? 136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 144.536 157.649 168.350 1.00 40.63 ? 136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 143.820 156.650 168.482 1.00 43.48 ? 136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 143.491 159.726 167.397 1.00 42.97 ? 136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 142.255 159.088 166.790 1.00 43.16 ? 136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.995 159.539 167.506 1.00 42.12 ? 136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 139.769 159.381 166.622 1.00 43.86 ? 136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 139.674 160.459 165.600 1.00 45.48 ? 136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 145.799 157.566 167.925 1.00 39.55 ? 137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 146.407 156.265 167.671 1.00 34.83 ? 137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 146.486 155.438 168.947 1.00 36.53 ? 137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 146.244 154.227 168.926 1.00 36.69 ? 137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 147.794 156.441 167.057 1.00 34.83 ? 137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 146.828 156.073 170.070 1.00 36.28 ? 138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 146.859 155.359 171.342 1.00 38.15 ? 138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 145.467 154.889 171.742 1.00 36.95 ? 138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 145.303 153.783 172.269 1.00 36.98 ? 138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 147.458 156.247 172.432 1.00 42.16 ? 138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.968 156.375 172.369 1.00 41.21 ? 138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 149.473 157.396 173.371 1.00 38.44 ? 138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 150.836 157.934 172.973 1.00 42.07 ? 138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 151.621 158.373 174.159 1.00 42.27 ? 138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 144.451 155.723 171.512 1.00 38.85 ? 139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 143.082 155.305 171.797 1.00 34.91 ? 139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 142.687 154.102 170.949 1.00 34.12 ? 139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 142.060 153.159 171.446 1.00 37.10 ? 139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 142.117 156.467 171.566 1.00 35.50 ? 139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 142.053 157.457 172.715 1.00 38.56 ? 139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 141.644 158.845 172.265 1.00 46.22 ? 139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 140.948 158.955 171.233 1.00 44.64 ? 139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 142.016 159.826 172.942 1.00 44.36 ? 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 143.048 154.115 169.665 1.00 30.27 ? 140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 142.757 152.974 168.801 1.00 28.66 ? 140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 143.502 151.729 169.264 1.00 27.60 ? 140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.962 150.618 169.218 1.00 31.03 ? 140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 143.118 153.302 167.353 1.00 29.53 ? 140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 142.132 154.205 166.653 1.00 30.49 ? 140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 140.790 153.863 166.561 1.00 33.25 ? 140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 142.545 155.396 166.075 1.00 31.96 ? 140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 139.888 154.685 165.918 1.00 30.48 ? 140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 141.651 156.223 165.431 1.00 34.85 ? 140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 140.324 155.864 165.355 1.00 27.48 ? 140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 139.432 156.689 164.713 1.00 35.22 ? 140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 144.754 151.896 169.694 1.00 37.61 ? 141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 145.529 150.766 170.196 1.00 33.06 ? 141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 144.864 150.175 171.429 1.00 29.85 ? 141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 144.770 148.953 171.575 1.00 37.72 ? 141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.978 151.194 170.490 1.00 33.47 ? 141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 147.574 150.319 171.578 1.00 32.93 ? 141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 147.819 151.120 169.230 1.00 33.37 ? 141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 144.406 151.030 172.343 1.00 32.01 ? 142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 143.721 150.533 173.531 1.00 29.93 ? 142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 142.424 149.828 173.159 1.00 34.45 ? 142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 142.077 148.797 173.747 1.00 37.53 ? 142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 143.452 151.680 174.502 1.00 28.26 ? 142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 144.692 152.104 175.258 1.00 35.14 ? 142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 145.416 151.271 175.802 1.00 34.81 ? 142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.946 153.406 175.296 1.00 38.07 ? 142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 141.691 150.371 172.186 1.00 31.90 ? 143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 140.440 149.750 171.765 1.00 25.18 ? 143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 140.682 148.361 171.184 1.00 28.65 ? 143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.989 147.399 171.534 1.00 32.22 ? 143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 139.735 150.647 170.747 1.00 26.45 ? 143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 138.231 150.444 170.556 1.00 31.32 ? 143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 137.464 151.025 171.732 1.00 29.40 ? 143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 137.768 151.067 169.250 1.00 30.09 ? 143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 141.667 148.237 170.291 1.00 33.31 ? 144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.904 146.961 169.622 1.00 29.92 ? 144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 142.579 145.945 170.539 1.00 25.46 ? 144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 142.223 144.763 170.521 1.00 29.05 ? 144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 142.737 147.176 168.359 1.00 28.91 ? 144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 142.007 147.927 167.259 1.00 27.41 ? 144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 142.967 148.045 165.740 1.00 40.83 ? 144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.112 149.820 165.573 1.00 29.96 ? 144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 143.554 146.379 171.339 1.00 30.59 ? 145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 144.255 145.457 172.227 1.00 30.85 ? 145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 143.322 144.966 173.326 1.00 34.05 ? 145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 143.386 143.802 173.738 1.00 40.32 ? 145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 145.522 146.120 172.799 1.00 33.09 ? 145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 146.593 145.065 173.082 1.00 34.34 ? 145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 145.202 146.908 174.059 1.00 34.93 ? 145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 147.103 144.362 171.844 1.00 32.49 ? 145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 142.442 145.839 173.818 1.00 33.03 ? 146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 141.370 145.393 174.696 1.00 27.98 ? 146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 140.348 144.544 173.958 1.00 30.90 ? 146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 139.484 143.939 174.601 1.00 34.77 ? 146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.679 146.594 175.343 1.00 28.88 ? 146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 141.553 147.287 176.367 1.00 33.31 ? 146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 142.530 146.719 176.851 1.00 38.75 ? 146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 141.203 148.522 176.705 1.00 35.88 ? 146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 140.428 144.493 172.629 1.00 32.52 ? 147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 139.545 143.674 171.805 1.00 23.87 ? 147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 138.089 144.094 171.950 1.00 25.34 ? 147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 137.177 143.280 171.796 1.00 32.91 ? 147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.716 142.188 172.125 1.00 29.39 ? 147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 141.077 141.642 171.732 1.00 25.93 ? 147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 141.099 140.133 171.658 1.00 27.96 ? 147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.467 139.452 172.463 1.00 38.08 ? 147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.828 139.599 170.687 1.00 29.55 ? 147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.863 145.373 172.253 1.00 27.46 ? 148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 136.511 145.915 172.248 1.00 21.60 ? 148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 136.004 146.148 170.833 1.00 24.47 ? 148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.791 146.122 170.600 1.00 30.89 ? 148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 136.470 147.219 173.042 1.00 19.64 ? 148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.939 147.080 174.476 1.00 24.15 ? 148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 137.311 148.409 175.097 1.00 33.55 ? 148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 138.410 148.919 174.796 1.00 36.20 ? 148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 136.507 148.945 175.887 1.00 38.62 ? 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.909 146.382 169.886 1.00 21.13 ? 149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 136.550 146.624 168.497 1.00 19.58 ? 149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 137.479 145.830 167.595 1.00 23.84 ? 149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 138.695 145.816 167.810 1.00 28.18 ? 149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 136.628 148.115 168.154 1.00 22.74 ? 149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 136.432 148.409 166.687 1.00 24.58 ? 149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 135.218 148.153 166.066 1.00 16.12 ? 149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 137.460 148.941 165.922 1.00 20.86 ? 149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 135.035 148.417 164.726 1.00 20.54 ? 149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 137.285 149.210 164.582 1.00 21.12 ? 149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 136.070 148.946 163.989 1.00 18.27 ? 149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.889 149.212 162.653 1.00 19.79 ? 149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.908 145.173 166.594 1.00 17.03 ? 150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.677 144.417 165.608 1.00 14.05 ? 150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 137.396 144.965 164.219 1.00 17.76 ? 150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 136.274 144.791 163.705 1.00 25.64 ? 150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 137.331 142.930 165.675 1.00 17.05 ? 150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 138.017 142.071 164.623 1.00 24.08 ? 150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 139.521 142.252 164.605 1.00 22.70 ? 150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 140.218 141.825 165.523 1.00 27.40 ? 150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 140.028 142.888 163.558 1.00 20.09 ? 150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 138.352 145.629 163.573 1.00 23.46 ? 151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 138.148 146.024 162.176 1.00 16.90 ? 151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.951 144.800 161.297 1.00 19.23 ? 151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 138.490 143.723 161.561 1.00 23.18 ? 151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 139.440 146.770 161.822 1.00 16.91 ? 151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 140.023 147.178 163.130 1.00 17.70 ? 151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 139.631 146.119 164.110 1.00 22.38 ? 151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 137.157 144.973 160.242 1.00 26.94 ? 152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.858 143.875 159.331 1.00 20.38 ? 152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 138.142 143.231 158.825 1.00 24.29 ? 152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 139.210 143.848 158.867 1.00 26.67 ? 152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 136.011 144.365 158.156 1.00 24.05 ? 152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.791 145.124 157.249 1.00 28.88 ? 152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 138.048 141.991 158.352 1.00 30.33 ? 153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 139.231 141.294 157.858 1.00 24.21 ? 153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 140.001 142.089 156.813 1.00 31.06 ? 153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 141.239 142.135 156.906 1.00 30.87 ? 153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.827 139.924 157.295 1.00 25.95 ? 153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 138.534 139.028 158.374 1.00 34.00 ? 153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.951 139.340 156.453 1.00 29.49 ? 153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 139.369 142.715 155.816 1.00 27.98 ? 154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 140.152 143.522 154.863 1.00 24.02 ? 154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.933 144.644 155.524 1.00 25.34 ? 154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 142.136 144.787 155.276 1.00 33.81 ? 154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 139.078 144.053 153.903 1.00 23.98 ? 154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.970 143.071 154.001 1.00 24.86 ? 154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.953 142.618 155.424 1.00 25.61 ? 154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 140.282 145.448 156.365 1.00 28.84 ? 155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.980 146.545 157.030 1.00 26.26 ? 155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 142.070 146.022 157.956 1.00 26.47 ? 155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 143.203 146.517 157.944 1.00 27.03 ? 155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.986 147.407 157.808 1.00 25.89 ? 155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.939 147.843 156.932 1.00 32.29 ? 155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 140.684 148.618 158.406 1.00 23.96 ? 155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.745 145.015 158.768 1.00 28.77 ? 156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.714 144.494 159.726 1.00 29.52 ? 156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.937 143.922 159.021 1.00 31.57 ? 156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 145.073 144.133 159.461 1.00 34.87 ? 156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 142.054 143.432 160.605 1.00 27.59 ? 156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.840 143.088 161.836 1.00 32.83 ? 156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 143.142 144.060 162.774 1.00 27.40 ? 156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 143.271 141.792 162.059 1.00 29.13 ? 156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.864 143.746 163.907 1.00 27.88 ? 156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.993 141.472 163.191 1.00 21.66 ? 156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 144.289 142.450 164.116 1.00 31.62 ? 156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.724 143.192 157.927 1.00 33.91 ? 157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.821 142.543 157.220 1.00 30.18 ? 157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 145.637 143.527 156.388 1.00 33.13 ? 157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.868 143.431 156.347 1.00 41.80 ? 157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 144.271 141.429 156.330 1.00 34.45 ? 157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 145.271 140.696 155.436 1.00 37.23 ? 157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 146.116 139.733 156.254 1.00 35.67 ? 157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 144.551 139.970 154.312 1.00 35.10 ? 157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.980 144.478 155.725 1.00 34.24 ? 158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 145.630 145.276 154.694 1.00 33.42 ? 158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 146.053 146.664 155.152 1.00 34.46 ? 158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.870 147.293 154.472 1.00 35.86 ? 158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.704 145.420 153.481 1.00 34.46 ? 158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 144.402 144.093 152.819 1.00 37.64 ? 158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 145.239 143.192 152.799 1.00 42.29 ? 158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 143.199 143.964 152.276 1.00 38.70 ? 158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 145.527 147.161 156.268 1.00 36.17 ? 159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.844 148.520 156.685 1.00 35.39 ? 159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 147.346 148.688 156.868 1.00 40.98 ? 159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.996 147.891 157.550 1.00 45.47 ? 159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 145.111 148.861 157.982 1.00 33.17 ? 159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.896 149.733 156.254 1.00 46.22 ? 160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 149.306 150.036 156.380 1.00 44.34 ? 160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 150.240 149.167 155.569 1.00 44.83 ? 160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 151.454 149.225 155.790 1.00 50.06 ? 160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.724 148.366 154.642 1.00 45.47 ? 161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 150.541 147.473 153.834 1.00 44.83 ? 161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 150.603 147.971 152.397 1.00 49.26 ? 161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.580 148.343 151.813 1.00 52.84 ? 161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.997 146.042 153.864 1.00 42.20 ? 161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 150.139 145.350 155.207 1.00 45.66 ? 161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.929 143.853 155.072 1.00 47.01 ? 161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.747 143.205 156.364 1.00 48.17 ? 161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 149.400 141.935 156.521 1.00 47.62 ? 161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 149.207 141.138 155.483 1.00 46.27 ? 161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 149.241 141.452 157.749 1.00 47.84 ? 161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.811 147.974 151.831 1.00 56.98 ? 162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.989 148.435 150.458 1.00 55.92 ? 162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 151.296 147.504 149.470 1.00 55.34 ? 162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.533 147.954 148.607 1.00 58.11 ? 162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 153.479 148.551 150.137 1.00 56.96 ? 162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.783 148.827 148.674 1.00 58.29 ? 162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 154.080 150.298 148.442 1.00 56.92 ? 162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 155.379 150.707 149.114 1.00 57.96 ? 162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 155.344 152.122 149.570 1.00 59.35 ? 162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.550 146.202 149.579 1.00 56.78 ? 163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.938 145.214 148.690 1.00 59.81 ? 163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.648 144.676 149.310 1.00 60.44 ? 163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.558 143.537 149.767 1.00 59.18 ? 163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.924 144.092 148.387 1.00 60.02 ? 163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 153.122 144.526 147.561 1.00 59.81 ? 163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 154.203 143.461 147.568 1.00 60.25 ? 163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.854 143.356 148.868 1.00 61.40 ? 163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.468 142.268 149.311 1.00 62.84 ? 163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.534 141.166 148.581 1.00 62.81 ? 163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.029 142.286 150.516 1.00 60.15 ? 163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.635 145.535 149.314 1.00 58.13 ? 164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 147.368 145.263 149.971 1.00 52.84 ? 164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 146.212 145.426 148.994 1.00 52.28 ? 164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 146.286 146.206 148.040 1.00 53.46 ? 164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 147.158 146.206 151.158 1.00 50.90 ? 164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.740 147.607 150.738 1.00 51.16 ? 164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 146.184 148.407 151.901 1.00 53.64 ? 164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.533 149.632 151.453 1.00 54.05 ? 164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 145.557 150.780 152.116 1.00 56.05 ? 164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 146.200 150.901 153.267 1.00 50.62 ? 164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.918 151.833 151.614 1.00 53.97 ? 164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 145.141 144.678 149.243 1.00 49.55 ? 165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.882 144.917 148.576 1.00 47.34 ? 165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 143.125 146.057 149.228 1.00 50.15 ? 165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.582 146.691 150.179 1.00 50.07 ? 165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.936 146.321 148.699 1.00 41.91 ? 166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 141.111 147.384 149.252 1.00 40.23 ? 166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.643 147.023 150.658 1.00 40.11 ? 166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.432 145.853 150.987 1.00 39.45 ? 166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.909 147.654 148.349 1.00 40.78 ? 166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 140.240 148.473 147.115 1.00 42.66 ? 166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.923 149.784 147.454 1.00 47.21 ? 166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 140.735 150.279 148.585 1.00 46.32 ? 166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 141.651 150.318 146.591 1.00 45.81 ? 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 140.487 148.050 151.495 1.00 35.68 ? 167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.985 147.839 152.846 1.00 32.26 ? 167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 138.481 147.613 152.874 1.00 32.36 ? 167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.959 147.122 153.880 1.00 34.58 ? 167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 140.354 149.024 153.740 1.00 34.94 ? 167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 141.850 149.235 153.987 1.00 32.75 ? 167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.077 150.144 155.182 1.00 32.22 ? 167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 142.559 147.905 154.178 1.00 32.47 ? 167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.781 147.960 151.799 1.00 33.87 ? 168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 136.365 147.651 151.646 1.00 26.64 ? 168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 136.247 146.390 150.802 1.00 30.85 ? 168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.895 146.270 149.756 1.00 33.76 ? 168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 135.612 148.824 150.999 1.00 29.73 ? 168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 134.144 148.477 150.818 1.00 30.93 ? 168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.774 150.084 151.835 1.00 33.68 ? 168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 135.424 145.444 151.255 1.00 32.04 ? 169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 135.343 144.135 150.619 1.00 26.37 ? 169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.928 143.749 150.204 1.00 24.67 ? 169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.727 142.634 149.711 1.00 33.18 ? 169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.922 143.065 151.550 1.00 30.72 ? 169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 135.878 141.783 150.949 1.00 34.76 ? 169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.944 144.629 150.379 1.00 26.04 ? 170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 131.561 144.338 150.013 1.00 21.21 ? 170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 131.059 145.436 149.082 1.00 19.19 ? 170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 131.088 146.620 149.433 1.00 22.78 ? 170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 130.681 144.198 151.259 1.00 29.68 ? 170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 129.832 145.691 151.826 1.00 55.25 ? 170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.624 145.042 147.887 1.00 15.23 ? 171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 130.145 145.971 146.873 1.00 11.10 ? 171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.824 145.479 146.305 1.00 9.50  ? 171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.617 144.274 146.143 1.00 19.10 ? 171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 131.169 146.138 145.741 1.00 18.55 ? 171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.545 146.489 146.219 1.00 18.39 ? 171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.878 147.803 146.496 1.00 14.76 ? 171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 133.504 145.508 146.397 1.00 13.76 ? 171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 134.140 148.131 146.942 1.00 14.78 ? 171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.768 145.831 146.842 1.00 16.07 ? 171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 135.086 147.144 147.114 1.00 12.80 ? 171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.934 146.421 146.006 1.00 15.87 ? 172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.644 146.136 145.395 1.00 9.32  ? 172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 126.531 146.929 144.103 1.00 10.44 ? 172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 126.729 148.148 144.101 1.00 16.85 ? 172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.492 146.487 146.340 1.00 15.54 ? 172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 125.354 145.638 147.604 1.00 11.15 ? 172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 126.405 146.024 148.634 1.00 12.17 ? 172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.955 145.770 148.182 1.00 10.83 ? 172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 126.208 146.241 143.012 1.00 21.17 ? 173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 126.184 146.841 141.686 1.00 9.03  ? 173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.779 146.781 141.107 1.00 15.26 ? 173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 124.177 145.706 141.036 1.00 25.70 ? 173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 127.161 146.133 140.744 1.00 15.52 ? 173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.633 146.103 141.153 1.00 20.33 ? 173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 129.462 145.375 140.105 1.00 16.74 ? 173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 129.156 147.509 141.377 1.00 15.13 ? 173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 124.263 147.937 140.702 1.00 23.06 ? 174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 123.056 147.990 139.893 1.00 19.27 ? 174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 123.412 147.769 138.429 1.00 17.32 ? 174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 124.399 148.314 137.928 1.00 26.14 ? 174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 122.354 149.337 140.060 1.00 23.43 ? 174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.701 149.547 141.412 1.00 17.66 ? 174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 120.226 149.208 141.402 1.00 23.21 ? 174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.669 149.001 140.305 1.00 30.48 ? 174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 119.621 149.149 142.492 1.00 25.79 ? 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.605 146.965 137.744 1.00 18.77 ? 175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.810 146.657 136.335 1.00 19.51 ? 175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.610 147.166 135.551 1.00 18.54 ? 175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 120.468 146.796 135.845 1.00 21.00 ? 175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 123.015 145.149 136.103 1.00 22.56 ? 175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.665 144.907 134.753 1.00 16.09 ? 175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.849 144.549 137.221 1.00 18.87 ? 175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.869 148.007 134.558 1.00 22.18 ? 176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.823 148.516 133.686 1.00 19.90 ? 176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.577 147.549 132.531 1.00 21.94 ? 176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 121.426 146.727 132.180 1.00 29.28 ? 176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 121.193 149.899 133.152 1.00 15.03 ? 176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 120.014 150.845 133.120 1.00 20.29 ? 176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.862 150.419 133.162 1.00 27.79 ? 176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 120.296 152.139 133.048 1.00 19.69 ? 176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 119.393 147.665 131.935 1.00 20.94 ? 177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.942 146.740 130.896 1.00 23.95 ? 177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 119.502 147.187 129.551 1.00 22.61 ? 177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.831 147.854 128.763 1.00 25.78 ? 177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 117.421 146.667 130.879 1.00 20.59 ? 177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.899 145.577 129.971 1.00 26.59 ? 177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 117.557 144.522 129.868 1.00 30.90 ? 177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.825 145.774 129.368 1.00 26.29 ? 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.750 146.813 129.284 1.00 20.40 ? 178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 121.394 147.108 128.011 1.00 19.79 ? 178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.700 146.330 127.944 1.00 20.76 ? 178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 123.265 145.945 128.970 1.00 27.35 ? 178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.650 148.607 127.834 1.00 15.37 ? 178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.875 148.991 128.429 1.00 18.83 ? 178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 123.171 146.101 126.715 1.00 25.00 ? 179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 124.424 145.377 126.526 1.00 19.31 ? 179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.604 146.151 127.100 1.00 22.35 ? 179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.498 145.560 127.717 1.00 23.18 ? 179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.645 145.086 125.042 1.00 20.33 ? 179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.800 144.138 124.714 1.00 19.58 ? 179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.554 142.767 125.322 1.00 21.13 ? 179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 126.003 144.036 123.213 1.00 20.77 ? 179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.631 147.470 126.899 1.00 22.76 ? 180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.694 148.279 127.484 1.00 19.52 ? 180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.716 148.134 128.997 1.00 19.51 ? 180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.781 147.963 129.600 1.00 22.73 ? 180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 126.517 149.748 127.099 1.00 21.95 ? 180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.743 149.997 125.626 1.00 22.82 ? 180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.714 149.514 125.046 1.00 30.13 ? 180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.850 150.762 125.012 1.00 27.44 ? 180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.542 148.190 129.627 1.00 22.65 ? 181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.469 148.071 131.077 1.00 18.27 ? 181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.882 146.681 131.545 1.00 16.25 ? 181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.557 146.547 132.567 1.00 26.24 ? 181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 124.062 148.413 131.557 1.00 22.11 ? 181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.712 149.868 131.327 1.00 27.67 ? 181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 124.450 150.740 131.828 1.00 27.90 ? 181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.707 150.139 130.640 1.00 33.09 ? 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.493 145.636 130.814 1.00 18.74 ? 182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.877 144.281 131.202 1.00 20.29 ? 182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 127.387 144.096 131.095 1.00 18.02 ? 182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 128.022 143.517 131.986 1.00 22.60 ? 182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 125.116 143.248 130.351 1.00 23.79 ? 182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.663 143.139 130.816 1.00 22.48 ? 182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.799 141.893 130.418 1.00 16.31 ? 182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.740 142.522 129.793 1.00 21.31 ? 182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.984 144.572 130.002 1.00 21.31 ? 183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 129.429 144.458 129.844 1.00 21.13 ? 183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 130.163 145.259 130.912 1.00 19.61 ? 183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 131.163 144.793 131.474 1.00 24.54 ? 183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.839 144.913 128.443 1.00 17.24 ? 183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 129.796 146.323 128.331 1.00 31.53 ? 183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.678 146.466 131.212 1.00 19.95 ? 184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 130.284 147.257 132.275 1.00 19.80 ? 184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 130.134 146.573 133.625 1.00 22.55 ? 184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 131.033 146.644 134.465 1.00 24.43 ? 184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.670 148.654 132.311 1.00 19.35 ? 184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 130.398 149.609 133.233 1.00 24.70 ? 184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.863 149.702 132.862 1.00 25.62 ? 184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 132.064 150.454 131.630 1.00 33.16 ? 184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 133.242 150.877 131.195 1.00 36.43 ? 184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 134.357 150.623 131.861 1.00 27.27 ? 184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.304 151.571 130.063 1.00 30.06 ? 184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.995 145.920 133.861 1.00 24.87 ? 185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.805 145.187 135.105 1.00 14.62 ? 185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.802 144.046 135.222 1.00 18.34 ? 185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 130.378 143.825 136.292 1.00 19.91 ? 185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 127.374 144.660 135.192 1.00 13.71 ? 185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 130.019 143.310 134.132 1.00 24.67 ? 186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 131.009 142.234 134.155 1.00 22.88 ? 186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 132.394 142.799 134.450 1.00 21.01 ? 186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 133.144 142.264 135.278 1.00 24.96 ? 186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.990 141.455 132.828 1.00 25.71 ? 186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.677 140.687 132.672 1.00 22.12 ? 186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 132.177 140.508 132.750 1.00 19.04 ? 186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 129.383 140.274 131.249 1.00 21.88 ? 186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.748 143.898 133.780 1.00 21.86 ? 187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 134.059 144.504 133.989 1.00 20.72 ? 187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 134.230 144.977 135.428 1.00 25.75 ? 187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 135.282 144.762 136.040 1.00 26.10 ? 187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 134.257 145.665 133.015 1.00 18.17 ? 187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 135.361 146.609 133.448 1.00 31.04 ? 187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 136.459 146.129 133.797 1.00 28.37 ? 187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 135.128 147.835 133.444 1.00 39.42 ? 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 133.206 145.627 135.983 1.00 26.86 ? 188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 133.283 146.137 137.347 1.00 19.95 ? 188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 133.360 144.990 138.343 1.00 25.91 ? 188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 134.098 145.059 139.331 1.00 27.44 ? 188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 132.087 147.058 137.641 1.00 25.16 ? 188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 132.202 148.360 136.847 1.00 23.76 ? 188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.988 147.343 139.131 1.00 21.08 ? 188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.971 149.228 136.928 1.00 20.01 ? 188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.585 143.928 138.118 1.00 20.84 ? 189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.651 142.769 138.998 1.00 14.99 ? 189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 134.043 142.162 138.990 1.00 19.05 ? 189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.578 141.801 140.044 1.00 25.64 ? 189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.611 141.731 138.580 1.00 21.93 ? 189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 130.298 142.246 138.698 1.00 26.71 ? 189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.649 142.045 137.807 1.00 27.49 ? 190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 136.002 141.506 137.726 1.00 22.83 ? 190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 137.004 142.422 138.420 1.00 24.83 ? 190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.903 141.948 139.123 1.00 27.49 ? 190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.379 141.285 136.264 1.00 21.60 ? 190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.780 140.022 135.667 1.00 24.36 ? 190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.951 139.057 134.703 1.00 40.38 ? 190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.970 140.006 133.185 1.00 28.15 ? 190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.859 143.737 138.241 1.00 22.77 ? 191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.761 144.682 138.891 1.00 22.47 ? 191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.644 144.610 140.408 1.00 23.48 ? 191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.650 144.694 141.121 1.00 30.05 ? 191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.471 146.103 138.407 1.00 25.32 ? 191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.645 146.317 136.915 1.00 21.80 ? 191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 139.078 146.144 136.461 1.00 25.92 ? 191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 140.002 146.143 137.272 1.00 22.72 ? 191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.271 145.999 135.156 1.00 26.51 ? 191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.420 144.469 140.919 1.00 23.27 ? 192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 136.203 144.451 142.361 1.00 21.03 ? 192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.627 143.125 142.977 1.00 24.24 ? 192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 137.155 143.101 144.094 1.00 33.46 ? 192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.735 144.742 142.675 1.00 21.12 ? 192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 134.217 146.128 142.285 1.00 21.56 ? 192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.712 146.210 142.468 1.00 16.19 ? 192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.918 147.214 143.081 1.00 16.21 ? 192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 136.401 142.013 142.274 1.00 24.20 ? 193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.883 140.727 142.763 1.00 21.04 ? 193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 138.401 140.653 142.710 1.00 27.93 ? 193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 139.020 140.005 143.561 1.00 35.38 ? 193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 136.259 139.591 141.956 1.00 24.36 ? 193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 134.847 139.622 142.052 1.00 37.63 ? 193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 139.015 141.305 141.721 1.00 29.41 ? 194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.466 141.434 141.701 1.00 28.40 ? 194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.979 142.104 142.969 1.00 34.56 ? 194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 142.099 141.824 143.411 1.00 36.23 ? 194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.894 142.220 140.461 1.00 28.18 ? 194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 142.358 142.605 140.419 1.00 30.58 ? 194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.639 143.497 139.222 1.00 32.32 ? 194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 144.124 143.789 139.072 1.00 35.35 ? 194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 144.384 144.763 137.975 1.00 32.65 ? 194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 140.177 142.984 143.566 1.00 29.96 ? 195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.530 143.643 144.816 1.00 26.87 ? 195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 140.201 142.803 146.043 1.00 28.58 ? 195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.494 143.232 147.163 1.00 40.29 ? 195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.816 144.992 144.917 1.00 34.53 ? 195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 140.068 145.994 143.790 1.00 36.26 ? 195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 139.213 147.236 143.981 1.00 31.63 ? 195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.540 146.357 143.710 1.00 30.96 ? 195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.601 141.627 145.863 1.00 26.93 ? 196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 139.257 140.755 146.963 1.00 29.52 ? 196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.878 140.965 147.549 1.00 34.36 ? 196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.463 140.176 148.406 1.00 34.21 ? 196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 137.154 141.994 147.117 1.00 28.37 ? 197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.833 142.242 147.654 1.00 23.86 ? 197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.766 141.381 147.003 1.00 23.54 ? 197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.846 141.024 145.829 1.00 27.42 ? 197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.750 141.043 147.795 1.00 13.20 ? 198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.594 140.342 147.263 1.00 11.25 ? 198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.646 141.307 146.568 1.00 15.33 ? 198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.409 142.422 147.030 1.00 17.15 ? 198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 131.101 140.862 145.440 1.00 17.11 ? 199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 130.283 141.701 144.573 1.00 11.18 ? 199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.883 141.110 144.496 1.00 10.70 ? 199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.718 139.926 144.185 1.00 15.52 ? 199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.894 141.833 143.166 1.00 15.15 ? 199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 130.114 142.844 142.343 1.00 10.87 ? 199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 132.357 142.227 143.260 1.00 14.25 ? 199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.882 141.938 144.775 1.00 12.17 ? 200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.482 141.577 144.622 1.00 3.11  ? 200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.883 142.418 143.505 1.00 13.17 ? 200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 126.077 143.637 143.470 1.00 22.36 ? 200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.710 141.790 145.925 1.00 6.79  ? 200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.509 141.043 145.931 1.00 20.98 ? 200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 125.165 141.771 142.595 1.00 16.32 ? 201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.595 142.435 141.434 1.00 7.40  ? 201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 123.081 142.297 141.449 1.00 9.06  ? 201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.547 141.223 141.739 1.00 16.94 ? 201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 125.162 141.861 140.133 1.00 22.38 ? 201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.647 142.136 139.888 1.00 16.51 ? 201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 127.467 140.874 140.092 1.00 18.91 ? 201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.866 142.708 138.498 1.00 18.93 ? 201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 122.398 143.394 141.142 1.00 12.73 ? 202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.946 143.416 141.037 1.00 13.50 ? 202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.568 143.194 139.579 1.00 21.99 ? 202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.911 144.007 138.714 1.00 30.10 ? 202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 120.381 144.739 141.552 1.00 8.96  ? 202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.900 144.662 141.854 1.00 11.60 ? 202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 118.344 143.578 142.014 1.00 24.55 ? 202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 118.253 145.816 141.937 1.00 14.23 ? 202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.869 142.094 139.310 1.00 13.29 ? 203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.483 141.726 137.955 1.00 12.69 ? 203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 118.002 141.949 137.688 1.00 12.56 ? 203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.477 141.430 136.699 1.00 22.15 ? 203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.854 140.267 137.685 1.00 16.29 ? 203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 121.314 139.884 137.939 1.00 20.17 ? 203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.598 138.483 137.425 1.00 19.83 ? 203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 122.258 140.892 137.301 1.00 14.50 ? 203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 117.315 142.709 138.543 1.00 18.55 ? 204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.876 142.886 138.395 1.00 13.82 ? 204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.515 143.834 137.260 1.00 16.78 ? 204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.382 143.788 136.772 1.00 30.11 ? 204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 115.275 143.392 139.705 1.00 17.67 ? 204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.542 142.493 140.765 1.00 25.80 ? 204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 116.440 144.691 136.831 1.00 17.66 ? 205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 116.167 145.590 135.719 1.00 16.64 ? 205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 116.424 144.951 134.363 1.00 20.34 ? 205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.995 145.506 133.346 1.00 25.78 ? 205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.997 146.867 135.854 1.00 17.44 ? 205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.540 147.781 136.973 1.00 17.56 ? 205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.416 149.015 137.067 1.00 21.80 ? 205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.798 150.061 137.979 1.00 27.15 ? 205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.647 149.570 139.374 1.00 19.73 ? 205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 117.105 143.810 134.320 1.00 23.50 ? 206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 117.269 143.084 133.070 1.00 18.04 ? 206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.937 142.486 132.638 1.00 22.84 ? 206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 115.177 141.966 133.459 1.00 29.66 ? 206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 118.312 141.980 133.228 1.00 21.21 ? 206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.685 142.391 133.759 1.00 24.90 ? 206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.592 141.178 133.873 1.00 20.27 ? 206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 120.310 143.450 132.866 1.00 27.59 ? 206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.653 142.562 131.342 1.00 25.66 ? 207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.411 142.001 130.836 1.00 19.38 ? 207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.461 140.479 130.870 1.00 27.98 ? 207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.529 139.865 130.811 1.00 32.11 ? 207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 114.131 142.494 129.416 1.00 22.23 ? 207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 115.328 142.506 128.496 1.00 24.60 ? 207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 115.003 143.261 127.222 1.00 25.09 ? 207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 115.424 144.654 127.305 1.00 28.91 ? 207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 115.325 145.528 126.314 1.00 26.60 ? 207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.833 145.183 125.136 1.00 30.50 ? 207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.731 146.778 126.509 1.00 18.12 ? 207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.285 139.872 130.978 1.00 31.28 ? 208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 113.186 138.433 131.135 1.00 23.27 ? 208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.457 137.726 129.810 1.00 33.70 ? 208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.479 138.333 128.737 1.00 30.69 ? 208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.811 138.049 131.677 1.00 26.67 ? 208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.675 136.417 129.901 1.00 33.56 ? 209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.894 135.612 128.710 1.00 25.82 ? 209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.691 135.702 127.781 1.00 34.11 ? 209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.539 135.648 128.221 1.00 37.27 ? 209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 114.157 134.157 129.098 1.00 28.65 ? 209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.647 133.286 127.957 1.00 31.19 ? 209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.797 131.839 128.394 1.00 33.94 ? 209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.455 131.230 128.765 1.00 34.85 ? 209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 113.611 129.945 129.502 1.00 36.81 ? 209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.963 135.839 126.488 1.00 35.76 ? 210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.909 135.948 125.504 1.00 33.53 ? 210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.397 137.346 125.256 1.00 38.74 ? 210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 110.301 137.499 124.707 1.00 43.88 ? 210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 112.147 138.370 125.644 1.00 38.62 ? 211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.759 139.747 125.387 1.00 34.86 ? 211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 112.440 140.259 124.122 1.00 37.44 ? 211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 113.425 139.694 123.642 1.00 37.18 ? 211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 112.107 140.638 126.580 1.00 33.52 ? 211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 111.253 140.371 127.809 1.00 32.28 ? 211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.872 141.639 128.547 1.00 36.70 ? 211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 110.048 142.412 128.015 1.00 38.81 ? 211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 111.387 141.860 129.661 1.00 36.04 ? 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.897 141.344 123.581 1.00 39.59 ? 212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 112.380 141.880 122.317 1.00 38.04 ? 212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 113.631 142.724 122.517 1.00 40.28 ? 212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.744 143.478 123.488 1.00 44.48 ? 212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 111.292 142.716 121.642 1.00 39.13 ? 212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 114.574 142.589 121.589 1.00 39.02 ? 213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.778 143.414 121.542 1.00 40.56 ? 213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 115.684 144.238 120.265 1.00 40.90 ? 213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.886 143.716 119.163 1.00 43.16 ? 213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 117.063 142.579 121.569 1.00 41.77 ? 213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 117.052 141.606 122.748 1.00 40.24 ? 213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 118.283 143.485 121.634 1.00 34.80 ? 213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 118.174 140.594 122.702 1.00 37.24 ? 213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 115.386 145.529 120.403 1.00 45.52 ? 214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 115.229 146.420 119.256 1.00 45.86 ? 214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 114.102 145.933 118.342 1.00 50.52 ? 214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 114.311 145.578 117.181 1.00 49.88 ? 214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 116.546 146.559 118.486 1.00 46.76 ? 214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 117.371 147.770 118.882 1.00 48.27 ? 214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 116.619 149.061 118.600 1.00 49.61 ? 214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 117.226 150.236 119.352 1.00 50.11 ? 214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 116.419 150.623 120.540 1.00 47.74 ? 214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.897 145.900 118.909 1.00 51.04 ? 215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.659 145.549 118.212 1.00 52.23 ? 215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.738 144.204 117.492 1.00 54.27 ? 215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.983 143.960 116.546 1.00 54.60 ? 215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.224 146.666 117.245 1.00 55.74 ? 215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 112.096 146.766 115.997 1.00 55.59 ? 215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 112.534 145.729 115.457 1.00 54.59 ? 215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 112.346 147.905 115.551 1.00 54.52 ? 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.634 143.318 117.921 1.00 49.40 ? 216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.665 141.936 117.454 1.00 48.34 ? 216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.353 141.049 118.652 1.00 49.42 ? 216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 113.067 141.081 119.662 1.00 50.00 ? 216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.014 141.570 116.810 1.00 48.97 ? 216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.491 142.698 115.910 1.00 48.25 ? 216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 115.062 141.249 117.861 1.00 49.10 ? 216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.279 140.273 118.547 1.00 51.48 ? 217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.739 139.568 119.699 1.00 51.06 ? 217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.538 138.307 120.005 1.00 48.90 ? 217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 112.191 137.730 119.133 1.00 50.27 ? 217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 109.272 139.208 119.461 1.00 51.21 ? 217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.348 140.412 119.366 1.00 50.36 ? 217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.223 141.160 120.679 1.00 56.79 ? 217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 108.169 140.502 121.740 1.00 54.40 ? 217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 108.180 142.408 120.650 1.00 54.39 ? 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 111.479 137.885 121.269 1.00 45.04 ? 218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 112.073 136.625 121.719 1.00 45.44 ? 218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 113.593 136.618 121.588 1.00 47.53 ? 218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 114.212 135.555 121.503 1.00 48.65 ? 218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 111.475 135.436 120.964 1.00 45.49 ? 218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.288 134.832 121.680 1.00 47.79 ? 218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 110.369 133.727 122.213 1.00 49.57 ? 218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 109.176 135.556 121.696 1.00 49.63 ? 218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 114.211 137.796 121.578 1.00 38.24 ? 219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.651 137.887 121.375 1.00 36.45 ? 219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.446 137.810 122.672 1.00 35.16 ? 219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.632 137.463 122.640 1.00 35.39 ? 219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.996 139.184 120.641 1.00 37.36 ? 219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.826 138.116 123.807 1.00 37.12 ? 220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.550 138.213 125.067 1.00 30.59 ? 220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.790 136.838 125.676 1.00 34.79 ? 220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.919 135.965 125.646 1.00 38.67 ? 220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.780 139.088 126.056 1.00 30.57 ? 220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.488 140.352 125.449 1.00 34.91 ? 220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.603 139.317 127.311 1.00 36.69 ? 220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.986 136.653 126.235 1.00 32.64 ? 221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.333 135.433 126.951 1.00 28.15 ? 221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.882 135.447 128.405 1.00 30.28 ? 221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.899 134.395 129.051 1.00 32.61 ? 221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.847 135.195 126.894 1.00 33.82 ? 221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.425 135.235 125.492 1.00 31.64 ? 221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.987 133.882 125.092 1.00 30.57 ? 221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.443 133.882 123.643 1.00 34.30 ? 221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 122.916 133.731 123.525 1.00 36.68 ? 221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.480 136.599 128.928 1.00 32.19 ? 222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 117.046 136.693 130.302 1.00 30.14 ? 222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 118.203 136.829 131.274 1.00 29.34 ? 222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 119.369 136.983 130.901 1.00 31.42 ? 222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.856 136.762 132.562 1.00 26.63 ? 223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.853 136.945 133.607 1.00 25.95 ? 223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.789 135.750 133.726 1.00 23.61 ? 223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.867 135.879 134.309 1.00 27.64 ? 223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 118.182 137.230 134.965 1.00 27.02 ? 223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 117.140 138.326 134.826 1.00 19.80 ? 223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.567 135.961 135.536 1.00 26.00 ? 223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.412 134.586 133.195 1.00 25.89 ? 224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.268 133.410 133.332 1.00 25.77 ? 224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.509 133.510 132.447 1.00 27.73 ? 224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.591 133.061 132.840 1.00 32.00 ? 224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.474 132.128 133.037 1.00 30.66 ? 224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.404 130.928 133.007 1.00 27.16 ? 224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.388 131.932 134.081 1.00 26.16 ? 224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.389 134.082 131.248 1.00 26.17 ? 225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.571 134.286 130.425 1.00 24.61 ? 225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.549 135.260 131.054 1.00 25.16 ? 225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.762 135.021 131.072 1.00 32.16 ? 225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 123.034 136.369 131.588 1.00 22.20 ? 226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.883 137.302 132.317 1.00 24.32 ? 226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.467 136.631 133.549 1.00 22.22 ? 226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.595 136.930 133.952 1.00 24.90 ? 226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 123.092 138.572 132.684 1.00 25.42 ? 226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.961 139.524 133.488 1.00 23.80 ? 226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.569 139.247 131.429 1.00 20.09 ? 226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.713 135.721 134.168 1.00 23.79 ? 227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 124.223 134.991 135.322 1.00 22.66 ? 227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.396 134.102 134.935 1.00 23.46 ? 227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.374 133.999 135.678 1.00 27.26 ? 227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 123.109 134.155 135.949 1.00 20.00 ? 227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 122.254 134.900 136.952 1.00 20.10 ? 227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.858 133.908 137.510 1.00 37.71 ? 227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.599 133.038 138.888 1.00 25.15 ? 227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.306 133.435 133.784 1.00 26.29 ? 228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.430 132.633 133.309 1.00 24.72 ? 228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.638 133.511 133.012 1.00 23.89 ? 228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.775 133.167 133.368 1.00 28.24 ? 228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 126.027 131.841 132.066 1.00 27.55 ? 228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.871 130.882 132.279 1.00 29.63 ? 228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.660 130.001 131.059 1.00 32.87 ? 228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.187 129.880 130.707 1.00 34.75 ? 228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.783 130.845 129.647 1.00 32.61 ? 228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.408 134.654 132.362 1.00 22.85 ? 229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.494 135.599 132.121 1.00 23.92 ? 229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 129.166 135.998 133.429 1.00 20.23 ? 229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.396 135.964 133.548 1.00 21.32 ? 229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.964 136.836 131.395 1.00 24.19 ? 229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.761 136.759 129.882 1.00 21.86 ? 229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.869 137.898 129.419 1.00 25.03 ? 229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 129.095 136.794 129.160 1.00 22.53 ? 229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.365 136.378 134.426 1.00 24.38 ? 230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.905 136.831 135.703 1.00 19.42 ? 230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.617 135.706 136.440 1.00 14.02 ? 230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.643 135.936 137.087 1.00 22.06 ? 230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.785 137.410 136.567 1.00 21.31 ? 230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 127.215 138.755 136.120 1.00 24.40 ? 230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.947 139.077 136.893 1.00 26.46 ? 230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 128.249 139.854 136.290 1.00 24.91 ? 230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 129.078 134.489 136.377 1.00 25.52 ? 231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.722 133.360 137.033 1.00 27.18 ? 231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 131.092 133.091 136.429 1.00 27.18 ? 231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 132.068 132.871 137.156 1.00 30.55 ? 231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.831 132.122 136.935 1.00 24.21 ? 231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.520 130.867 137.424 1.00 39.00 ? 231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.834 130.791 138.630 1.00 41.43 ? 231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.748 129.954 136.603 1.00 39.34 ? 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.192 133.125 135.099 1.00 31.93 ? 232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.498 132.954 134.473 1.00 28.68 ? 232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.432 134.112 134.808 1.00 25.71 ? 232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.636 133.909 134.997 1.00 32.51 ? 232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.349 132.797 132.963 1.00 27.96 ? 232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 133.280 131.746 132.401 1.00 32.58 ? 232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 134.501 131.881 132.474 1.00 34.93 ? 232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 132.710 130.681 131.857 1.00 32.70 ? 232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.900 135.334 134.876 1.00 20.16 ? 233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.734 136.482 135.216 1.00 20.33 ? 233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 134.291 136.361 136.630 1.00 25.62 ? 233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.459 136.680 136.876 1.00 28.47 ? 233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.935 137.775 135.060 1.00 22.81 ? 233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.464 135.910 137.573 1.00 27.71 ? 234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.924 135.730 138.946 1.00 21.60 ? 234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.906 134.571 139.050 1.00 21.70 ? 234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.869 134.636 139.822 1.00 30.60 ? 234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.732 135.512 139.877 1.00 20.77 ? 234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.994 136.772 140.221 1.00 19.39 ? 234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.636 137.811 140.874 1.00 17.65 ? 234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.659 136.921 139.891 1.00 21.24 ? 234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.960 138.972 141.189 1.00 20.10 ? 234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.978 138.079 140.202 1.00 22.40 ? 234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.629 139.106 140.855 1.00 25.70 ? 234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.678 133.501 138.287 1.00 31.13 ? 235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.621 132.389 138.288 1.00 26.11 ? 235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.974 132.815 137.734 1.00 29.72 ? 235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 138.019 132.388 138.236 1.00 38.28 ? 235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 135.050 131.218 137.490 1.00 27.82 ? 235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.526 130.083 138.354 1.00 35.95 ? 235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.082 128.894 137.516 1.00 35.98 ? 235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.864 129.176 136.767 1.00 36.53 ? 235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.833 129.495 135.480 1.00 38.45 ? 235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.941 129.582 134.763 1.00 39.29 ? 235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.661 129.731 134.898 1.00 33.61 ? 235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.976 133.657 136.699 1.00 30.26 ? 236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.234 134.127 136.130 1.00 27.97 ? 236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.979 135.025 137.109 1.00 27.48 ? 236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 140.179 134.845 137.344 1.00 31.32 ? 236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.973 134.869 134.820 1.00 25.91 ? 236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.224 135.428 134.185 1.00 28.92 ? 236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 140.083 134.612 133.465 1.00 22.51 ? 236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.553 136.770 134.319 1.00 28.56 ? 236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.227 135.116 132.887 1.00 23.34 ? 236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.697 137.283 133.746 1.00 26.36 ? 236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.530 136.452 133.030 1.00 25.39 ? 236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.670 136.957 132.456 1.00 31.15 ? 236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 138.282 136.002 137.686 1.00 33.74 ? 237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.887 136.941 138.629 1.00 34.91 ? 237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.729 136.399 140.049 1.00 42.38 ? 237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 138.043 136.961 140.903 1.00 43.99 ? 237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 138.266 138.323 138.477 1.00 34.25 ? 237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.397 135.270 140.290 1.00 58.69 ? 238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.300 134.554 141.554 1.00 58.72 ? 238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.412 134.944 142.521 1.00 63.19 ? 238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 140.864 134.115 143.317 1.00 64.11 ? 238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 139.308 133.044 141.317 1.00 58.39 ? 238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 140.667 132.528 140.888 1.00 63.63 ? 238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 141.480 133.332 140.385 1.00 62.41 ? 238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 140.926 131.318 141.059 1.00 62.74 ? 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.878 136.190 142.449 1.00 70.72 ? 239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.862 136.711 143.394 1.00 72.43 ? 239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.176 135.938 143.303 1.00 74.48 ? 239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.742 135.503 144.308 1.00 73.10 ? 239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.310 136.687 144.820 1.00 71.23 ? 239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.962 137.365 144.971 1.00 69.76 ? 239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.316 137.078 146.310 1.00 71.81 ? 239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 139.992 137.019 147.337 1.00 72.08 ? 239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 138.001 136.898 146.308 1.00 69.75 ? 239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.661 135.766 142.074 1.00 81.51 ? 240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 144.943 135.113 141.824 1.00 81.02 ? 240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 144.971 133.691 142.379 1.00 81.75 ? 240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.041 133.136 142.642 1.00 81.47 ? 240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.095 135.936 142.405 1.00 79.98 ? 240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.040 137.411 142.037 1.00 80.89 ? 240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 147.654 138.208 142.038 1.00 87.62 ? 240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 147.180 139.934 142.052 1.00 80.18 ? 240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 143.796 133.093 142.562 1.00 79.74 ? 241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 143.687 131.744 143.074 1.00 79.44 ? 241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 143.756 131.615 144.579 1.00 81.57 ? 241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 143.487 130.526 145.101 1.00 81.23 ? 241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.108 132.684 145.295 1.00 86.15 ? 242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.175 132.620 146.750 1.00 85.28 ? 242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 142.791 132.574 147.384 1.00 87.22 ? 242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 142.651 132.126 148.528 1.00 87.40 ? 242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 144.964 133.813 147.292 1.00 85.00 ? 242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.414 133.853 146.833 1.00 87.21 ? 242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 147.275 134.760 147.690 1.00 87.25 ? 242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 146.871 135.176 148.776 1.00 87.19 ? 242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 148.472 135.071 147.204 1.00 85.90 ? 242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 141.767 133.029 146.665 1.00 77.44 ? 243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.396 133.002 147.161 1.00 76.61 ? 243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.461 133.117 145.969 1.00 76.25 ? 243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.428 134.161 145.312 1.00 74.78 ? 243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.146 134.136 148.158 1.00 75.91 ? 243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.684 134.529 148.308 1.00 76.87 ? 243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.440 135.248 149.626 1.00 77.01 ? 243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.032 135.244 150.007 1.00 77.32 ? 243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.530 135.926 151.027 1.00 77.17 ? 243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 137.296 136.678 151.800 1.00 74.45 ? 243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 135.226 135.851 151.279 1.00 77.42 ? 243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.694 132.061 145.706 1.00 70.00 ? 244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.839 132.039 144.528 1.00 69.77 ? 244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.901 133.239 144.522 1.00 68.45 ? 244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.314 133.596 145.547 1.00 67.65 ? 244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 137.031 130.742 144.481 1.00 68.17 ? 244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.858 129.498 144.202 1.00 69.96 ? 244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 137.009 128.245 144.100 1.00 69.44 ? 244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 136.082 128.044 144.884 1.00 67.64 ? 244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.322 127.396 143.129 1.00 66.69 ? 244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.767 133.866 143.356 1.00 51.71 ? 245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.878 135.000 143.211 1.00 49.76 ? 245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.455 134.657 143.595 1.00 48.89 ? 245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.875 133.705 143.065 1.00 47.37 ? 245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.883 135.423 144.520 1.00 36.53 ? 246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.544 135.173 145.032 1.00 32.75 ? 246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.639 136.339 144.672 1.00 31.52 ? 246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 131.959 137.496 144.966 1.00 27.84 ? 246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.562 134.965 146.549 1.00 31.49 ? 246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.146 133.719 146.884 1.00 37.44 ? 246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.510 136.030 144.040 1.00 20.76 ? 247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.544 137.045 143.687 1.00 9.87  ? 247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 128.140 136.575 144.000 1.00 14.49 ? 247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.866 135.378 144.102 1.00 23.22 ? 247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.250 137.547 144.153 1.00 17.60 ? 248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.850 137.284 144.437 1.00 16.56 ? 248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.990 137.984 143.399 1.00 14.06 ? 248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.295 139.103 142.978 1.00 18.30 ? 248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.466 137.755 145.845 1.00 8.53  ? 248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.921 137.316 142.983 1.00 16.63 ? 249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.943 137.881 142.066 1.00 15.22 ? 249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.595 137.922 142.765 1.00 9.37  ? 249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 121.189 136.940 143.393 1.00 21.90 ? 249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.855 137.066 140.774 1.00 15.46 ? 249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.911 139.054 142.664 1.00 9.10  ? 250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.607 139.234 143.280 1.00 10.63 ? 250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.565 139.485 142.203 1.00 9.21  ? 250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.801 140.245 141.260 1.00 14.17 ? 250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.617 140.393 144.281 1.00 4.32  ? 250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 120.181 140.021 145.632 1.00 13.55 ? 250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.543 139.819 145.802 1.00 5.37  ? 250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 119.353 139.871 146.734 1.00 11.37 ? 250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 122.064 139.476 147.030 1.00 1.19  ? 250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.866 139.527 147.967 1.00 6.52  ? 250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 121.221 139.332 148.110 1.00 6.94  ? 250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.739 138.993 149.336 1.00 12.71 ? 250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.418 138.833 142.345 1.00 12.70 ? 251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.306 139.005 141.427 1.00 14.35 ? 251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 115.029 139.171 142.230 1.00 7.35  ? 251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.779 138.409 143.168 1.00 18.98 ? 251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 116.183 137.816 140.470 1.00 16.46 ? 251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.385 138.088 139.195 1.00 14.88 ? 251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 116.183 138.969 138.246 1.00 11.96 ? 251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.984 136.787 138.525 1.00 11.94 ? 251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 114.230 140.170 141.869 1.00 19.74 ? 252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.931 140.334 142.498 1.00 15.62 ? 252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 112.052 139.129 142.190 1.00 16.47 ? 252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 112.097 138.569 141.092 1.00 14.84 ? 252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 112.264 141.622 142.015 1.00 12.84 ? 252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 111.140 142.071 142.925 1.00 22.34 ? 252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 110.051 141.500 142.912 1.00 31.43 ? 252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.402 143.094 143.727 1.00 17.56 ? 252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 111.251 138.725 143.177 1.00 13.22 ? 253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.424 137.533 143.021 1.00 18.45 ? 253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.420 137.707 141.891 1.00 17.23 ? 253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.993 136.724 141.274 1.00 19.43 ? 253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.726 137.192 144.352 1.00 24.07 ? 253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.352 135.710 144.386 1.00 16.93 ? 253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.502 138.071 144.557 1.00 15.17 ? 253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.359 135.114 145.767 1.00 20.58 ? 253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 109.029 138.943 141.597 1.00 23.37 ? 254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 108.063 139.204 140.538 1.00 16.78 ? 254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.694 139.248 139.154 1.00 16.01 ? 254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.969 139.399 138.166 1.00 29.25 ? 254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 107.323 140.513 140.819 1.00 23.00 ? 254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 106.290 140.400 141.900 1.00 25.89 ? 254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 105.148 139.644 141.706 1.00 24.24 ? 254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 106.468 141.036 143.115 1.00 22.38 ? 254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 104.197 139.535 142.698 1.00 23.61 ? 254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 105.520 140.929 144.111 1.00 25.79 ? 254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 104.383 140.178 143.902 1.00 25.04 ? 254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 110.013 139.127 139.057 1.00 22.92 ? 255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.657 139.027 137.756 1.00 17.11 ? 255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 110.272 137.715 137.087 1.00 21.85 ? 255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 110.179 136.671 137.737 1.00 29.52 ? 255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 112.175 139.120 137.903 1.00 17.93 ? 255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.888 139.427 136.624 1.00 20.66 ? 255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 113.102 138.481 135.645 1.00 20.79 ? 255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.441 140.573 136.165 1.00 15.43 ? 255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.753 139.032 134.637 1.00 18.42 ? 255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.971 140.301 134.928 1.00 14.47 ? 255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 110.044 137.773 135.774 1.00 22.96 ? 256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.601 136.586 135.053 1.00 22.29 ? 256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.633 135.468 135.120 1.00 21.05 ? 256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 110.267 134.288 135.161 1.00 24.44 ? 256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 109.295 136.940 133.598 1.00 28.47 ? 256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 108.435 135.915 132.889 1.00 25.93 ? 256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 109.086 135.441 131.604 1.00 30.06 ? 256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 110.362 134.778 131.837 1.00 30.29 ? 256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.513 133.464 131.922 1.00 32.06 ? 256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.481 132.643 131.824 1.00 28.20 ? 256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.730 132.962 132.116 1.00 28.53 ? 256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.917 135.812 135.136 1.00 16.39 ? 257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.994 134.832 135.188 1.00 17.48 ? 257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 113.194 134.233 136.575 1.00 21.91 ? 257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 114.208 133.565 136.799 1.00 25.32 ? 257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 114.304 135.466 134.713 1.00 26.04 ? 257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 114.341 135.677 133.214 1.00 29.51 ? 257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.404 135.223 132.526 1.00 30.46 ? 257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 115.307 136.294 132.725 1.00 28.05 ? 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 112.261 134.450 137.504 1.00 22.98 ? 258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.465 134.006 138.881 1.00 24.35 ? 258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.620 132.492 138.946 1.00 18.36 ? 258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.467 131.972 139.682 1.00 27.67 ? 258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.315 134.499 139.780 1.00 26.38 ? 258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.615 134.184 141.248 1.00 24.14 ? 258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.993 133.885 139.350 1.00 18.24 ? 258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.871 134.846 141.772 1.00 11.71 ? 258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.809 131.758 138.182 1.00 25.18 ? 259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.894 130.302 138.218 1.00 25.73 ? 259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.167 129.805 137.544 1.00 27.07 ? 259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.826 128.890 138.050 1.00 24.79 ? 259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.659 129.688 137.564 1.00 26.38 ? 259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.438 129.757 138.456 1.00 30.12 ? 259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.343 129.042 139.451 1.00 27.87 ? 259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.495 130.621 138.101 1.00 30.12 ? 259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.526 130.390 136.401 1.00 28.34 ? 260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.810 130.072 135.786 1.00 23.04 ? 260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.963 130.516 136.675 1.00 24.90 ? 260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.973 129.814 136.793 1.00 28.41 ? 260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.907 130.726 134.409 1.00 25.95 ? 260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.879 130.187 133.434 1.00 37.41 ? 260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.438 129.031 133.609 1.00 36.83 ? 260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.511 130.920 132.493 1.00 36.61 ? 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.827 131.686 137.303 1.00 32.30 ? 261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.850 132.174 138.220 1.00 23.80 ? 261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 117.042 131.216 139.389 1.00 22.32 ? 261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.177 130.908 139.770 1.00 20.91 ? 261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.460 133.575 138.702 1.00 17.89 ? 261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.278 134.092 139.851 1.00 23.47 ? 261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.426 134.831 139.623 1.00 19.36 ? 261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.873 133.882 141.158 1.00 20.63 ? 261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.170 135.324 140.676 1.00 17.45 ? 261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.614 134.372 142.214 1.00 20.67 ? 261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 118.763 135.094 141.972 1.00 18.35 ? 261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.942 130.727 139.965 1.00 25.93 ? 262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.042 129.771 141.062 1.00 25.19 ? 262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.573 128.423 140.594 1.00 28.19 ? 262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.291 127.750 141.342 1.00 28.98 ? 262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.681 129.597 141.733 1.00 26.24 ? 262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.162 130.796 142.526 1.00 25.45 ? 262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.771 130.514 143.062 1.00 26.03 ? 262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 115.117 131.138 143.655 1.00 25.33 ? 262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.238 128.013 139.369 1.00 37.38 ? 263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.652 126.705 138.879 1.00 30.44 ? 263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.154 126.615 138.646 1.00 34.98 ? 263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.684 125.505 138.536 1.00 42.28 ? 263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.905 126.366 137.589 1.00 31.92 ? 263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.469 125.957 137.841 1.00 42.55 ? 263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.152 125.584 138.990 1.00 40.70 ? 263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.659 126.006 136.893 1.00 42.68 ? 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.850 127.750 138.566 1.00 40.11 ? 264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.300 127.715 138.418 1.00 36.40 ? 264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 120.982 127.087 139.625 1.00 38.73 ? 264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.151 126.700 139.531 1.00 39.65 ? 264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.847 129.125 138.192 1.00 36.12 ? 264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.573 129.936 139.341 1.00 39.75 ? 264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.206 129.756 136.968 1.00 36.42 ? 264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.284 126.984 140.755 1.00 36.03 ? 265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.835 126.393 141.966 1.00 37.45 ? 265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.318 124.989 142.238 1.00 38.68 ? 265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.647 124.417 143.282 1.00 44.06 ? 265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.547 127.293 143.173 1.00 38.86 ? 265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.473 128.485 143.270 1.00 40.18 ? 265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.915 128.041 143.131 1.00 38.64 ? 265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.862 129.220 143.142 1.00 36.53 ? 265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.241 128.809 142.768 1.00 40.03 ? 265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.520 124.421 141.341 1.00 45.68 ? 266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.125 123.028 141.480 1.00 47.64 ? 266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.303 122.117 141.163 1.00 52.73 ? 266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.030 122.330 140.189 1.00 50.50 ? 266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 117.949 122.705 140.559 1.00 45.49 ? 266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.595 123.099 141.117 1.00 48.53 ? 266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.471 122.676 140.184 1.00 50.08 ? 266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.121 122.752 140.879 1.00 50.45 ? 266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 112.991 122.676 139.914 1.00 51.69 ? 266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.497 121.097 142.001 1.00 58.01 ? 267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.575 120.144 141.760 1.00 60.36 ? 267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.364 119.431 140.432 1.00 62.31 ? 267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.305 119.248 139.650 1.00 60.80 ? 267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.682 119.149 142.931 1.00 61.48 ? 267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 120.293 118.832 143.487 1.00 61.67 ? 267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.587 119.706 144.018 1.00 60.78 ? 267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.315 117.962 144.723 1.00 61.28 ? 267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.127 119.023 140.153 1.00 62.02 ? 268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 119.790 118.383 138.888 1.00 62.91 ? 268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 119.882 119.328 137.698 1.00 64.82 ? 268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 119.686 118.882 136.562 1.00 65.26 ? 268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 118.383 117.789 138.965 1.00 65.62 ? 268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.428 118.787 139.283 1.00 63.67 ? 268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.167 120.609 137.923 1.00 68.59 ? 269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.217 121.566 136.827 1.00 67.41 ? 269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.301 121.187 135.826 1.00 68.34 ? 269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.372 120.699 136.197 1.00 67.67 ? 269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 120.468 122.975 137.366 1.00 65.07 ? 269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.012 121.411 134.547 1.00 71.68 ? 270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 121.997 121.160 133.506 1.00 71.95 ? 270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.194 122.087 133.677 1.00 73.10 ? 270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.066 123.231 134.120 1.00 73.96 ? 270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.371 121.350 132.124 1.00 71.48 ? 270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 122.296 120.923 130.999 1.00 74.76 ? 270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.419 121.463 130.909 1.00 72.79 ? 270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.900 120.047 130.201 1.00 74.81 ? 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.374 121.579 133.315 1.00 72.29 ? 271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.592 122.367 133.468 1.00 74.01 ? 271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.532 123.656 132.660 1.00 72.52 ? 271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.185 124.643 133.017 1.00 71.40 ? 271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.808 121.537 133.058 1.00 72.42 ? 271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.158 120.430 134.037 1.00 72.18 ? 271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.758 120.959 135.324 1.00 74.32 ? 271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.618 121.862 135.253 1.00 74.47 ? 271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.367 120.475 136.407 1.00 73.06 ? 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.761 123.671 131.571 1.00 71.11 ? 272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.628 124.889 130.780 1.00 71.57 ? 272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.919 125.991 131.557 1.00 70.87 ? 272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 124.299 127.162 131.453 1.00 70.56 ? 272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.886 124.593 129.475 1.00 70.27 ? 272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.411 124.314 129.692 1.00 72.06 ? 272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 122.047 123.867 130.800 1.00 70.11 ? 272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.617 124.543 128.756 1.00 71.58 ? 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.896 125.642 132.335 1.00 64.49 ? 273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 122.117 126.626 133.079 1.00 64.25 ? 273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.668 126.768 134.490 1.00 62.49 ? 273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.609 127.851 135.083 1.00 62.53 ? 273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.626 126.247 133.111 1.00 64.83 ? 273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.938 126.916 134.290 1.00 62.29 ? 273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.954 126.642 131.807 1.00 62.42 ? 273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.202 125.680 135.039 1.00 62.19 ? 274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.706 125.712 136.404 1.00 61.09 ? 274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.794 126.767 136.547 1.00 59.75 ? 274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.692 126.874 135.707 1.00 62.34 ? 274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.249 124.341 136.808 1.00 63.71 ? 274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.767 124.253 136.780 1.00 63.60 ? 274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 126.279 123.001 137.473 1.00 63.45 ? 274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.804 122.896 138.848 1.00 63.48 ? 274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.078 121.889 139.314 1.00 65.86 ? 274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.721 120.878 138.539 1.00 66.57 ? 274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 124.702 121.896 140.590 1.00 64.53 ? 274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.698 127.559 137.610 1.00 45.55 ? 275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.729 128.512 137.996 1.00 45.60 ? 275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.371 127.996 139.275 1.00 47.96 ? 275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.670 127.697 140.250 1.00 47.96 ? 275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.151 129.924 138.191 1.00 42.64 ? 275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 126.094 130.763 139.019 1.00 44.97 ? 275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.890 130.581 136.845 1.00 40.18 ? 275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.698 127.884 139.273 1.00 45.78 ? 276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.385 127.189 140.355 1.00 45.52 ? 276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.888 128.123 141.449 1.00 43.63 ? 276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.712 127.829 142.635 1.00 49.13 ? 276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.554 126.374 139.794 1.00 47.07 ? 276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.640 127.211 139.138 1.00 48.44 ? 276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.629 126.339 138.382 1.00 48.48 ? 276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.925 125.491 137.335 1.00 49.23 ? 276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.741 126.190 136.764 1.00 48.31 ? 276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.513 129.241 141.084 1.00 38.25 ? 277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.179 130.107 142.049 1.00 39.10 ? 277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.414 131.395 142.331 1.00 37.84 ? 277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.965 132.301 142.965 1.00 42.57 ? 277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.594 130.443 141.570 1.00 41.83 ? 277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.528 131.117 140.307 1.00 38.78 ? 277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.419 129.173 141.421 1.00 41.64 ? 277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.168 131.503 141.885 1.00 29.04 ? 278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.380 132.714 142.073 1.00 26.38 ? 278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.277 132.447 143.089 1.00 26.26 ? 278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.422 131.584 142.870 1.00 32.93 ? 278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.785 133.187 140.748 1.00 28.73 ? 278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.337 134.645 140.660 1.00 29.60 ? 278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.540 135.565 140.552 1.00 25.07 ? 278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.403 134.836 139.478 1.00 28.18 ? 278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.304 133.181 144.196 1.00 26.16 ? 279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.220 133.133 145.163 1.00 17.88 ? 279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 124.018 133.903 144.632 1.00 19.80 ? 279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 124.158 134.883 143.895 1.00 26.95 ? 279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.668 133.715 146.503 1.00 18.48 ? 279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.688 132.923 147.086 1.00 26.37 ? 279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.826 133.451 145.008 1.00 16.54 ? 280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.586 134.040 144.521 1.00 20.51 ? 280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.716 134.428 145.706 1.00 17.69 ? 280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.586 133.669 146.672 1.00 24.93 ? 280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.824 133.085 143.579 1.00 15.73 ? 280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.521 131.762 144.282 1.00 20.28 ? 280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.616 132.856 142.305 1.00 18.14 ? 280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 119.391 130.986 143.653 1.00 20.08 ? 280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 120.135 135.617 145.632 1.00 11.91 ? 281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 119.160 136.049 146.610 1.00 5.48  ? 281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.895 136.520 145.924 1.00 11.20 ? 281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.912 136.958 144.775 1.00 18.17 ? 281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.789 136.418 146.651 1.00 17.78 ? 282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.474 136.791 146.146 1.00 15.80 ? 282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.946 137.953 146.974 1.00 14.77 ? 282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 115.042 137.945 148.205 1.00 23.13 ? 282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.492 135.601 146.179 1.00 18.83 ? 282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 113.078 136.069 145.893 1.00 24.27 ? 282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.912 134.544 145.174 1.00 18.11 ? 282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.396 138.951 146.294 1.00 8.41  ? 283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.785 140.105 146.941 1.00 8.29  ? 283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.278 139.897 146.896 1.00 12.94 ? 283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.676 139.883 145.818 1.00 24.86 ? 283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 114.196 141.418 146.264 1.00 10.39 ? 283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.777 142.607 147.112 1.00 10.02 ? 283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.694 141.432 146.011 1.00 6.61  ? 283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.667 139.734 148.063 1.00 15.70 ? 284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 110.256 139.385 148.175 1.00 15.72 ? 284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.512 140.595 148.739 1.00 21.28 ? 284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.649 140.904 149.931 1.00 25.31 ? 284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 110.048 138.146 149.056 1.00 15.70 ? 284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.780 136.942 148.462 1.00 20.07 ? 284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.567 137.851 149.213 1.00 17.05 ? 284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.543 135.657 149.214 1.00 18.94 ? 284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.727 141.303 147.933 1.00 24.50 ? 285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.863 142.352 148.481 1.00 26.39 ? 285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.717 141.755 149.283 1.00 28.51 ? 285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.378 140.577 149.163 1.00 27.94 ? 285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 107.346 143.079 147.234 1.00 23.78 ? 285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 108.284 142.684 146.136 1.00 22.92 ? 285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.717 141.295 146.463 1.00 22.72 ? 285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 106.114 142.600 150.122 1.00 29.38 ? 286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.959 142.163 150.897 1.00 26.82 ? 286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.817 141.701 150.005 1.00 29.43 ? 286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.974 140.918 150.453 1.00 33.67 ? 286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.477 143.289 151.812 1.00 27.51 ? 286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 105.263 143.369 153.102 1.00 36.86 ? 286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 106.008 142.415 153.407 1.00 36.87 ? 286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 105.139 144.389 153.809 1.00 39.91 ? 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.772 142.167 148.755 1.00 32.86 ? 287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.713 141.747 147.845 1.00 28.20 ? 287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.772 140.249 147.580 1.00 29.41 ? 287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.736 139.577 147.549 1.00 31.45 ? 287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.809 142.527 146.534 1.00 31.58 ? 287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.610 142.346 145.622 1.00 29.73 ? 287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 100.327 142.715 146.341 1.00 33.27 ? 287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 99.159  142.805 145.380 1.00 34.66 ? 287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.958  143.389 146.034 1.00 36.29 ? 287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.975 139.708 147.375 1.00 26.20 ? 288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 104.102 138.276 147.125 1.00 24.98 ? 288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.663 137.461 148.335 1.00 24.99 ? 288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.982 136.439 148.191 1.00 33.36 ? 288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.539 137.932 146.742 1.00 28.00 ? 288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.738 136.487 146.392 1.00 27.32 ? 288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.436 136.021 145.125 1.00 25.01 ? 288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 106.221 135.593 147.331 1.00 25.08 ? 288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.615 134.692 144.802 1.00 28.29 ? 288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 106.400 134.263 147.013 1.00 26.64 ? 288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 106.099 133.813 145.747 1.00 29.49 ? 288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 104.052 137.890 149.536 1.00 33.02 ? 289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.647 137.176 150.742 1.00 30.50 ? 289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 102.137 137.245 150.914 1.00 30.11 ? 289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.498 136.267 151.317 1.00 31.62 ? 289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.386 137.735 151.973 1.00 33.18 ? 289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.963 136.988 153.227 1.00 26.82 ? 289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 105.889 137.644 151.774 1.00 27.72 ? 289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.542 138.401 150.616 1.00 32.94 ? 290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 100.091 138.528 150.699 1.00 32.99 ? 290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.399  137.605 149.704 1.00 37.61 ? 290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.400  136.958 150.035 1.00 42.86 ? 290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.681  139.981 150.460 1.00 34.40 ? 290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 98.189  140.234 150.568 1.00 40.67 ? 290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.762  141.499 149.851 1.00 46.34 ? 290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 98.496  142.506 149.933 1.00 47.28 ? 290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.691  141.489 149.209 1.00 41.71 ? 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 99.916  137.534 148.475 1.00 35.80 ? 291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 99.327  136.652 147.472 1.00 29.14 ? 291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.431  135.193 147.894 1.00 32.47 ? 291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.467  134.430 147.766 1.00 38.09 ? 291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 100.006 136.868 146.120 1.00 33.73 ? 291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.879  138.260 145.496 1.00 34.16 ? 291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.845 138.421 144.331 1.00 26.85 ? 291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 98.450  138.524 145.056 1.00 30.09 ? 291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.598 134.785 148.399 1.00 33.87 ? 292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.771 133.405 148.840 1.00 32.72 ? 292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.872  133.089 150.027 1.00 30.27 ? 292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.337  131.980 150.135 1.00 33.49 ? 292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 102.236 133.146 149.189 1.00 30.51 ? 292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.697  134.053 150.932 1.00 35.07 ? 293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.856  133.835 152.102 1.00 39.31 ? 293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.414  133.559 151.702 1.00 42.47 ? 293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.754  132.692 152.285 1.00 46.76 ? 293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.937  135.048 153.028 1.00 38.96 ? 293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 98.072  134.958 154.269 1.00 39.79 ? 293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 98.037  136.294 154.986 1.00 40.12 ? 293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.381  136.797 155.243 1.00 46.79 ? 293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.800  138.013 154.924 1.00 43.52 ? 293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 99.000  138.888 154.337 1.00 40.47 ? 293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 101.054 138.360 155.199 1.00 39.58 ? 293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.909  134.287 150.711 1.00 43.91 ? 294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.542  134.123 150.241 1.00 43.41 ? 294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.402  133.026 149.195 1.00 45.15 ? 294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.282  132.744 148.760 1.00 48.19 ? 294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 95.022  135.446 149.671 1.00 41.69 ? 294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.569  136.434 150.730 1.00 44.82 ? 294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 95.004  137.852 150.425 1.00 50.68 ? 294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 95.055  138.216 149.231 1.00 54.03 ? 294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 95.295  138.604 151.379 1.00 50.01 ? 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.503  132.403 148.783 1.00 44.36 ? 295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.511  131.344 147.780 1.00 44.02 ? 295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 96.036  131.828 146.416 1.00 49.42 ? 295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.711  131.007 145.550 1.00 47.80 ? 295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.667  130.146 148.232 1.00 43.26 ? 295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.318  128.816 147.905 1.00 51.14 ? 295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.446  128.819 147.370 1.00 50.13 ? 295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 95.703  127.767 148.188 1.00 48.43 ? 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.988  133.139 146.204 1.00 48.35 ? 296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.551  133.683 144.928 1.00 48.05 ? 296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.612  133.465 143.857 1.00 46.29 ? 296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.816  133.500 144.124 1.00 47.50 ? 296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.250  135.176 145.062 1.00 46.67 ? 296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.163  135.505 146.068 1.00 47.44 ? 296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 94.108  136.996 146.350 1.00 45.72 ? 296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.830  137.370 147.082 1.00 47.69 ? 296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 92.049  136.166 147.480 1.00 48.50 ? 296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.151  133.235 142.630 1.00 42.92 ? 297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.067  133.133 141.503 1.00 43.43 ? 297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.823  134.442 141.328 1.00 46.22 ? 297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.227  135.523 141.325 1.00 48.95 ? 297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.301  132.785 140.228 1.00 44.36 ? 297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.139  134.344 141.181 1.00 34.63 ? 298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 100.004 135.505 141.050 1.00 33.95 ? 298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.568 135.582 139.639 1.00 36.25 ? 298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.489 134.633 138.855 1.00 38.45 ? 298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.138 135.458 142.080 1.00 36.65 ? 298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 101.148 136.735 139.324 1.00 32.89 ? 299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.725 136.989 138.014 1.00 27.75 ? 299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 103.156 137.476 138.168 1.00 31.69 ? 299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.457 138.279 139.055 1.00 35.93 ? 299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.905 138.025 137.235 1.00 29.23 ? 299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.533  137.539 136.835 1.00 32.39 ? 299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.334  136.880 135.631 1.00 32.50 ? 299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.438  137.734 137.665 1.00 33.35 ? 299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.083  136.432 135.262 1.00 34.83 ? 299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 97.183  137.288 137.306 1.00 32.83 ? 299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 97.011  136.638 136.103 1.00 35.71 ? 299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.761  136.193 135.740 1.00 39.10 ? 299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 104.034 136.979 137.304 1.00 31.74 ? 300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.392 137.486 137.169 1.00 28.56 ? 300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.465 138.257 135.861 1.00 27.71 ? 300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.949 137.806 134.832 1.00 32.86 ? 300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.439 136.357 137.217 1.00 27.18 ? 300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.634 135.885 138.648 1.00 24.92 ? 300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 106.021 135.202 136.324 1.00 24.65 ? 300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 106.098 139.422 135.901 1.00 25.68 ? 301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 106.013 140.387 134.818 1.00 26.87 ? 301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 107.301 140.413 134.007 1.00 27.89 ? 301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.381 140.087 134.507 1.00 33.84 ? 301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.715 141.785 135.365 1.00 25.04 ? 301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.542 141.825 136.298 1.00 27.44 ? 301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 103.262 142.026 135.814 1.00 23.45 ? 301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.718 141.649 137.659 1.00 26.71 ? 301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 102.183 142.057 136.669 1.00 29.52 ? 301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.642 141.678 138.520 1.00 29.30 ? 301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 102.371 141.882 138.024 1.00 32.83 ? 301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 107.166 140.795 132.740 1.00 26.11 ? 302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 108.317 141.049 131.889 1.00 28.19 ? 302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.788 142.478 132.118 1.00 25.47 ? 302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 108.036 143.417 131.828 1.00 26.95 ? 302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.963 140.840 130.428 1.00 27.05 ? 302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.725 139.395 130.055 1.00 25.57 ? 302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.569 138.736 130.452 1.00 27.78 ? 302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.656 138.690 129.305 1.00 25.01 ? 302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.347 137.418 130.114 1.00 22.94 ? 302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.441 137.372 128.961 1.00 29.69 ? 302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.285 136.741 129.367 1.00 31.65 ? 302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 107.069 135.426 129.028 1.00 36.08 ? 302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.996 142.690 132.638 1.00 26.33 ? 303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 110.391 144.050 133.036 1.00 24.96 ? 303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 110.393 145.055 131.899 1.00 27.12 ? 303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 110.059 146.225 132.124 1.00 29.57 ? 303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.802 143.847 133.608 1.00 25.50 ? 303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.860 142.405 133.975 1.00 24.33 ? 303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 111.036 141.698 132.953 1.00 24.85 ? 303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.759 144.645 130.683 1.00 25.31 ? 304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.870 145.614 129.599 1.00 27.00 ? 304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 109.506 146.118 129.150 1.00 31.50 ? 304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 109.373 147.288 128.776 1.00 38.10 ? 304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.628 145.010 128.420 1.00 28.11 ? 304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.926 145.995 127.334 1.00 31.21 ? 304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.536 147.206 127.579 1.00 30.63 ? 304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.699 145.951 126.000 1.00 33.73 ? 304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.672 147.866 126.443 1.00 29.27 ? 304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 112.173 147.126 125.470 1.00 33.08 ? 304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 108.486 145.259 129.176 1.00 32.76 ? 305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 107.138 145.721 128.868 1.00 29.31 ? 305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.686 146.778 129.867 1.00 27.87 ? 305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 106.099 147.795 129.484 1.00 32.35 ? 305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 106.167 144.540 128.853 1.00 29.83 ? 305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.924 144.099 130.194 1.00 27.92 ? 305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.743 143.390 128.045 1.00 26.96 ? 305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.969 146.562 131.154 1.00 33.23 ? 306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.621 147.549 132.170 1.00 28.31 ? 306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 107.393 148.842 131.945 1.00 29.72 ? 306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.839 149.941 132.061 1.00 35.61 ? 306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.872 146.978 133.578 1.00 29.76 ? 306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.776 145.980 133.950 1.00 26.38 ? 306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.959 148.101 134.603 1.00 28.58 ? 306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 106.129 145.098 135.118 1.00 24.09 ? 306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.686 148.735 131.634 1.00 34.43 ? 307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 109.485 149.933 131.399 1.00 31.36 ? 307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.946 150.732 130.219 1.00 29.85 ? 307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.873 151.964 130.275 1.00 36.50 ? 307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.947 149.555 131.166 1.00 27.46 ? 307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.854 150.744 130.952 1.00 34.47 ? 307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 112.406 151.423 132.028 1.00 31.14 ? 307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 112.154 151.191 129.672 1.00 34.90 ? 307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 113.231 152.512 131.838 1.00 30.15 ? 307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.978 152.279 129.472 1.00 31.46 ? 307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 113.514 152.936 130.558 1.00 32.46 ? 307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 114.337 154.020 130.364 1.00 34.70 ? 307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 108.571 150.046 129.139 1.00 34.00 ? 308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 108.018 150.737 127.979 1.00 32.68 ? 308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.664 151.358 128.296 1.00 32.72 ? 308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 106.366 152.472 127.849 1.00 40.87 ? 308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.906 149.770 126.801 1.00 32.62 ? 308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 109.244 149.288 126.269 1.00 33.82 ? 308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 109.066 148.382 125.065 1.00 36.45 ? 308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.940 147.386 125.286 1.00 38.24 ? 308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 108.454 146.005 125.496 1.00 36.79 ? 308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.830 150.656 129.067 1.00 31.67 ? 309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 104.488 151.153 129.349 1.00 34.22 ? 309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 104.515 152.351 130.291 1.00 36.38 ? 309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.771 153.318 130.094 1.00 40.54 ? 309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.631 150.031 129.933 1.00 31.66 ? 309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 102.308 150.495 130.511 1.00 37.37 ? 309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 101.374 151.048 129.456 1.00 42.64 ? 309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.653 150.856 128.254 1.00 43.06 ? 309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 100.361 151.676 129.828 1.00 41.52 ? 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 105.362 152.309 131.318 1.00 35.82 ? 310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 105.367 153.329 132.356 1.00 33.79 ? 310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.606 154.210 132.342 1.00 34.51 ? 310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.606 155.254 133.003 1.00 36.36 ? 310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 105.230 152.672 133.737 1.00 31.60 ? 310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.958 151.875 133.900 1.00 33.05 ? 310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.759 152.500 134.209 1.00 32.48 ? 310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.955 150.498 133.732 1.00 29.80 ? 310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.595 151.776 134.354 1.00 34.01 ? 310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.796 149.766 133.874 1.00 33.22 ? 310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.619 150.409 134.185 1.00 34.96 ? 310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.462 149.682 134.328 1.00 38.32 ? 310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.651 153.829 131.613 1.00 35.37 ? 311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.879 154.591 131.592 1.00 30.45 ? 311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.788 154.366 132.777 1.00 33.26 ? 311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.844 155.005 132.856 1.00 38.61 ? 311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 109.415 153.485 133.700 1.00 34.80 ? 312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 110.223 153.175 134.867 1.00 32.98 ? 312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 110.440 151.672 134.943 1.00 35.08 ? 312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 109.697 150.884 134.354 1.00 39.51 ? 312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 109.566 153.672 136.162 1.00 34.26 ? 312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.884 155.021 136.043 1.00 36.83 ? 312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.898 155.272 137.166 1.00 42.15 ? 312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.692 155.365 136.940 1.00 41.87 ? 312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 108.408 155.380 138.388 1.00 35.76 ? 312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 111.478 151.282 135.676 1.00 29.29 ? 313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.746 149.869 135.890 1.00 28.67 ? 313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.774 149.289 136.911 1.00 31.24 ? 313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 110.266 149.990 137.788 1.00 33.68 ? 313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 113.187 149.662 136.353 1.00 26.64 ? 313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 114.211 150.060 135.336 1.00 31.26 ? 313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 114.900 151.251 135.399 1.00 33.56 ? 313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.658 149.425 134.227 1.00 29.27 ? 313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 115.730 151.332 134.375 1.00 32.43 ? 313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.603 150.236 133.649 1.00 30.92 ? 313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.521 147.984 136.787 1.00 33.35 ? 314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.588 147.325 137.694 1.00 26.39 ? 314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 110.065 147.412 139.138 1.00 33.28 ? 314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 109.263 147.646 140.050 1.00 34.74 ? 314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 109.393 145.866 137.279 1.00 27.71 ? 314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.222 145.182 137.963 1.00 31.62 ? 314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.363 143.386 137.983 1.00 44.06 ? 314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 109.428 143.111 136.573 1.00 28.34 ? 314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 111.366 147.232 139.370 1.00 27.60 ? 315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.901 147.306 140.723 1.00 34.62 ? 315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 112.076 148.737 141.214 1.00 35.11 ? 315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 112.397 148.934 142.391 1.00 37.21 ? 315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 113.239 146.569 140.807 1.00 34.05 ? 315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 114.223 147.030 139.759 1.00 37.86 ? 315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.782 147.363 138.640 1.00 38.45 ? 315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.436 147.059 140.053 1.00 33.67 ? 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.885 149.730 140.350 1.00 29.30 ? 316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.872 151.124 140.767 1.00 28.25 ? 316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 110.493 151.594 141.206 1.00 36.50 ? 316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 110.368 152.716 141.710 1.00 34.14 ? 316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 112.374 152.022 139.631 1.00 34.22 ? 316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 113.867 151.939 139.394 1.00 33.75 ? 316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.668 152.286 140.629 1.00 39.66 ? 316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.453 153.380 141.190 1.00 42.72 ? 316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 115.511 151.463 141.041 1.00 38.84 ? 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 109.465 150.771 141.030 1.00 41.05 ? 317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 108.095 151.120 141.363 1.00 37.51 ? 317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.649 150.372 142.612 1.00 37.60 ? 317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 108.269 149.392 143.034 1.00 40.83 ? 317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 107.150 150.799 140.200 1.00 36.80 ? 317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.647 151.255 138.840 1.00 33.38 ? 317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.341 151.257 137.600 1.00 47.15 ? 317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 107.309 151.245 136.095 1.00 38.32 ? 317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.557 150.852 143.201 1.00 42.01 ? 318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.987 150.234 144.394 1.00 41.09 ? 318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 105.117 149.058 143.969 1.00 41.95 ? 318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 104.015 149.249 143.444 1.00 43.92 ? 318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 105.184 151.258 145.190 1.00 41.53 ? 318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.646 150.695 146.488 1.00 49.87 ? 318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.262 149.755 147.033 1.00 49.03 ? 318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.605 151.194 146.966 1.00 53.23 ? 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.610 147.839 144.194 1.00 39.81 ? 319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.864 146.654 143.783 1.00 34.96 ? 319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 103.533 146.555 144.517 1.00 33.65 ? 319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 102.513 146.197 143.919 1.00 37.42 ? 319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 105.701 145.398 144.018 1.00 38.21 ? 319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.988 144.106 143.663 1.00 39.00 ? 319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.280 144.117 142.005 1.00 44.45 ? 319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 105.762 144.102 141.003 1.00 35.22 ? 319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 103.521 146.878 145.812 1.00 44.15 ? 320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 102.290 146.768 146.587 1.00 44.56 ? 320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 101.172 147.612 145.991 1.00 43.48 ? 320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.992  147.282 146.153 1.00 44.34 ? 320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 102.549 147.174 148.038 1.00 42.46 ? 320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 103.380 146.153 148.789 1.00 45.56 ? 320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 104.150 145.401 148.191 1.00 41.93 ? 320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 103.229 146.122 150.107 1.00 45.01 ? 320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 101.518 148.696 145.301 1.00 44.61 ? 321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 100.538 149.564 144.660 1.00 44.17 ? 321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 100.381 149.291 143.172 1.00 45.45 ? 321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 99.270  149.393 142.642 1.00 47.33 ? 321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.921 151.032 144.865 1.00 44.45 ? 321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 100.218 151.993 143.920 1.00 47.40 ? 321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.140 153.078 143.398 1.00 51.98 ? 321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.807 153.697 142.365 1.00 51.32 ? 321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.199 153.312 144.020 1.00 48.45 ? 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 101.464 148.942 142.485 1.00 40.34 ? 322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.457 148.809 141.035 1.00 35.55 ? 322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 101.171 147.393 140.553 1.00 36.47 ? 322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 101.091 147.180 139.341 1.00 43.32 ? 322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.797 149.279 140.460 1.00 38.97 ? 322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 103.152 150.714 140.804 1.00 40.69 ? 322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 102.131 151.913 139.930 1.00 49.44 ? 322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 102.184 151.255 138.267 1.00 37.96 ? 322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 101.012 146.422 141.454 1.00 30.83 ? 323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.787 145.048 141.016 1.00 33.09 ? 323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 99.464  144.915 140.271 1.00 34.82 ? 323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 99.398  144.306 139.197 1.00 38.11 ? 323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.829 144.102 142.216 1.00 32.65 ? 323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.495 142.667 141.878 1.00 31.38 ? 323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.455 141.819 141.345 1.00 29.11 ? 323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 99.220  142.162 142.091 1.00 30.69 ? 323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 101.156 140.511 141.034 1.00 29.01 ? 323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.913  140.854 141.784 1.00 29.46 ? 323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.884  140.033 141.255 1.00 30.76 ? 323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.580  138.729 140.949 1.00 34.31 ? 323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 98.394  145.480 140.832 1.00 38.67 ? 324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 97.092  145.397 140.179 1.00 38.13 ? 324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 97.091  146.149 138.855 1.00 39.69 ? 324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.494  145.691 137.875 1.00 43.58 ? 324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 96.005  145.932 141.108 1.00 40.78 ? 324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.658  144.959 142.216 1.00 44.96 ? 324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 96.040  143.774 142.110 1.00 43.95 ? 324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.003  145.377 143.194 1.00 47.92 ? 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.751  147.307 138.808 1.00 40.35 ? 325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.842  148.054 137.558 1.00 38.99 ? 325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.599  147.265 136.498 1.00 38.53 ? 325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 98.207  147.252 135.326 1.00 43.75 ? 325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 98.506  149.408 137.805 1.00 41.04 ? 325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.689  150.341 138.683 1.00 40.79 ? 325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 98.363  151.692 138.838 1.00 41.41 ? 325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 97.600  152.577 139.808 1.00 43.51 ? 325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 98.387  153.774 140.209 1.00 47.04 ? 325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.690  146.601 136.888 1.00 36.38 ? 326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 100.418 145.760 135.945 1.00 36.01 ? 326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.548  144.611 135.455 1.00 33.17 ? 326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.564  144.270 134.267 1.00 39.01 ? 326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.691 145.214 136.593 1.00 32.40 ? 326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.686 146.269 136.978 1.00 33.99 ? 326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.609 147.546 136.452 1.00 34.14 ? 326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.704 145.978 137.869 1.00 34.59 ? 326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.527 148.513 136.812 1.00 32.80 ? 326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.624 146.940 138.229 1.00 37.39 ? 326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.536 148.208 137.700 1.00 37.04 ? 326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.786  143.996 136.360 1.00 34.23 ? 327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.942  142.870 135.976 1.00 38.56 ? 327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.828  143.319 135.040 1.00 40.65 ? 327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.418  142.567 134.147 1.00 43.61 ? 327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.380  142.174 137.229 1.00 34.79 ? 327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.391  141.090 136.835 1.00 37.26 ? 327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.508  141.590 138.058 1.00 31.11 ? 327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 96.318  144.535 135.222 1.00 41.63 ? 328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 95.219  145.041 134.413 1.00 38.98 ? 328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.677  145.758 133.150 1.00 42.38 ? 328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.830  146.147 132.339 1.00 45.08 ? 328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 94.350  145.991 135.245 1.00 37.32 ? 328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.512  145.262 136.273 1.00 47.02 ? 328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 93.366  145.782 137.399 1.00 48.18 ? 328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 93.000  144.167 135.956 1.00 47.25 ? 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.981  145.939 132.959 1.00 40.90 ? 329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 97.485  146.649 131.791 1.00 39.35 ? 329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.715  145.668 130.651 1.00 40.86 ? 329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 98.559  144.772 130.783 1.00 40.80 ? 329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.777  147.375 132.121 1.00 35.27 ? 329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 99.115  148.448 131.109 1.00 38.52 ? 329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 99.220  148.179 129.914 1.00 45.56 ? 329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 99.287  149.675 131.583 1.00 38.14 ? 329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 97.001  145.791 129.528 1.00 42.59 ? 330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 97.228  144.862 128.411 1.00 39.90 ? 330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.602  144.994 127.780 1.00 38.78 ? 330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 99.080  144.028 127.173 1.00 41.12 ? 330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 96.121  145.232 127.418 1.00 39.33 ? 330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.829  146.663 127.714 1.00 38.66 ? 330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.997  146.817 129.199 1.00 38.23 ? 330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 99.248  146.150 127.900 1.00 39.76 ? 331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 100.561 146.378 127.316 1.00 38.93 ? 331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.694 145.863 128.192 1.00 38.09 ? 331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.860 145.965 127.797 1.00 38.70 ? 331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.758 147.871 127.039 1.00 38.97 ? 331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 100.284 148.310 125.665 1.00 40.30 ? 331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.501  149.606 125.748 1.00 41.83 ? 331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.423  149.525 126.727 1.00 42.04 ? 331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 98.084  150.507 127.550 1.00 42.47 ? 331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 98.719  151.667 127.539 1.00 43.60 ? 331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 97.083  150.321 128.405 1.00 40.30 ? 331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 101.381 145.322 129.365 1.00 33.10 ? 332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 102.365 144.718 130.255 1.00 34.26 ? 332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 102.216 143.208 130.149 1.00 35.23 ? 332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 101.128 142.666 130.382 1.00 35.12 ? 332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 102.190 145.189 131.707 1.00 33.10 ? 332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 103.035 144.341 132.646 1.00 30.16 ? 332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.553 146.659 131.838 1.00 31.42 ? 332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 103.302 142.531 129.794 1.00 35.77 ? 333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 103.302 141.081 129.678 1.00 28.47 ? 333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.594 140.453 131.033 1.00 29.81 ? 333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.482 140.904 131.762 1.00 35.54 ? 333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 104.335 140.624 128.647 1.00 27.74 ? 333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 104.127 139.209 128.137 1.00 34.16 ? 333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 105.227 138.807 127.170 1.00 32.56 ? 333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 105.037 137.383 126.678 1.00 35.52 ? 333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 106.104 136.983 125.719 1.00 41.63 ? 333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.839 139.410 131.367 1.00 32.18 ? 334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.969 138.763 132.662 1.00 29.24 ? 334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.682 137.278 132.511 1.00 33.45 ? 334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 102.006 136.847 131.574 1.00 38.30 ? 334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 102.030 139.391 133.698 1.00 33.66 ? 334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.557 139.192 133.400 1.00 33.14 ? 334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.777  140.477 133.605 1.00 31.85 ? 334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.563  141.202 132.289 1.00 35.68 ? 334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 99.108  142.605 132.484 1.00 34.45 ? 334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 103.208 136.498 133.451 1.00 35.26 ? 335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 103.058 135.051 133.460 1.00 32.76 ? 335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 102.409 134.621 134.767 1.00 34.49 ? 335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.879 134.991 135.848 1.00 42.46 ? 335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 104.414 134.361 133.288 1.00 35.59 ? 335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.328 132.909 132.860 1.00 37.32 ? 335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.679 132.218 132.869 1.00 43.51 ? 335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.711 132.922 132.861 1.00 36.14 ? 335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.708 130.970 132.885 1.00 49.28 ? 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 101.335 133.844 134.666 1.00 33.30 ? 336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.665 133.345 135.858 1.00 31.66 ? 336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.560 132.363 136.602 1.00 33.16 ? 336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.205 131.502 135.998 1.00 35.59 ? 336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.345  132.672 135.484 1.00 36.15 ? 336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.402  132.459 136.657 1.00 37.74 ? 336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 98.325  130.990 137.041 1.00 36.67 ? 336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 98.156  130.819 138.542 1.00 39.32 ? 336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 98.150  129.386 138.950 1.00 34.60 ? 336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.599 132.500 137.927 1.00 34.12 ? 337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.385 131.633 138.794 1.00 32.58 ? 337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.543 131.265 140.009 1.00 31.43 ? 337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.497 131.858 140.274 1.00 38.39 ? 337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.707 132.290 139.243 1.00 30.85 ? 337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.421 133.500 140.135 1.00 32.57 ? 337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.539 132.692 138.039 1.00 32.14 ? 337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.443 133.715 141.222 1.00 30.24 ? 337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 102.017 130.265 140.749 1.00 35.65 ? 338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.415 129.904 142.021 1.00 35.68 ? 338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.309 130.422 143.136 1.00 33.34 ? 338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.403 129.876 143.340 1.00 36.63 ? 338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.243 128.391 142.131 1.00 33.54 ? 338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.326 127.989 143.267 1.00 38.56 ? 338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.529 128.383 144.414 1.00 37.74 ? 338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.306  127.201 142.952 1.00 38.81 ? 338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.908 131.465 143.868 1.00 34.93 ? 339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.815 132.026 144.884 1.00 31.65 ? 339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.220 131.031 145.958 1.00 31.80 ? 339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.379 131.032 146.389 1.00 34.62 ? 339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.008 133.198 145.459 1.00 34.58 ? 339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.583 132.875 145.144 1.00 36.73 ? 339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.613 132.163 143.831 1.00 35.88 ? 339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.300 130.173 146.403 1.00 36.07 ? 340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.655 129.192 147.423 1.00 29.21 ? 340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.594 128.134 146.864 1.00 30.63 ? 340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.494 127.660 147.567 1.00 37.82 ? 340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.397 128.550 148.003 1.00 28.55 ? 340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.578 129.502 148.844 1.00 32.05 ? 340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.627  128.772 149.766 1.00 28.36 ? 340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.762  129.711 150.467 1.00 35.17 ? 340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.807  129.365 151.316 1.00 35.59 ? 340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.564  128.097 151.603 1.00 33.02 ? 340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.077  130.314 151.892 1.00 34.96 ? 340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.407 127.752 145.601 1.00 33.14 ? 341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.349 126.835 144.973 1.00 31.41 ? 341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.736 127.456 144.884 1.00 28.60 ? 341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.742 126.774 145.095 1.00 36.30 ? 341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.848 126.426 143.590 1.00 37.77 ? 341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.192 125.058 143.557 1.00 35.05 ? 341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.103 124.528 142.140 1.00 36.20 ? 341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 104.411 124.736 141.396 1.00 36.30 ? 341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 104.223 124.704 139.921 1.00 37.55 ? 341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.810 128.753 144.574 1.00 25.64 ? 342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.102 129.432 144.538 1.00 26.84 ? 342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.733 129.498 145.925 1.00 25.53 ? 342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.947 129.317 146.071 1.00 31.95 ? 342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.938 130.833 143.950 1.00 29.04 ? 342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.222 131.601 143.635 1.00 27.45 ? 342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 109.186 130.735 142.843 1.00 25.48 ? 342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.902 132.878 142.879 1.00 26.16 ? 342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.927 129.759 146.956 1.00 28.69 ? 343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.447 129.755 148.319 1.00 24.58 ? 343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 107.998 128.384 148.694 1.00 29.71 ? 343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.081 128.277 149.285 1.00 33.17 ? 343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.351 130.175 149.297 1.00 26.68 ? 343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.398 131.618 149.796 1.00 32.46 ? 343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.362 131.837 150.885 1.00 27.63 ? 343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.791 131.960 150.296 1.00 31.72 ? 343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.262 127.323 148.362 1.00 36.15 ? 344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.719 125.973 148.674 1.00 31.00 ? 344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 108.964 125.614 147.874 1.00 27.49 ? 344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 109.844 124.903 148.370 1.00 35.90 ? 344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.593 124.975 148.415 1.00 32.41 ? 344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.331 125.271 149.209 1.00 34.14 ? 344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.095 124.643 148.599 1.00 41.96 ? 344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.172 124.176 147.444 1.00 42.09 ? 344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.044 124.621 149.273 1.00 39.34 ? 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.055 126.096 146.633 1.00 26.71 ? 345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.266 125.896 145.846 1.00 25.53 ? 345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.456 126.588 146.492 1.00 29.35 ? 345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.555 126.027 146.546 1.00 33.79 ? 345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.053 126.411 144.422 1.00 27.37 ? 345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.270 126.285 143.525 1.00 27.21 ? 345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 110.955 126.729 142.110 1.00 29.89 ? 345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.164 126.580 141.205 1.00 33.64 ? 345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.854 126.958 139.801 1.00 35.71 ? 345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.256 127.810 146.989 1.00 30.43 ? 346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.321 128.497 147.711 1.00 24.40 ? 346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.747 127.703 148.937 1.00 24.07 ? 346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 113.945 127.549 149.204 1.00 25.69 ? 346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.864 129.897 148.121 1.00 24.07 ? 346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.697 130.940 147.019 1.00 27.02 ? 346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 111.132 132.223 147.599 1.00 27.55 ? 346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 113.018 131.201 146.322 1.00 26.09 ? 346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.776 127.190 149.694 1.00 27.71 ? 347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.102 126.420 150.890 1.00 25.06 ? 347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 112.885 125.159 150.544 1.00 30.53 ? 347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 113.877 124.833 151.207 1.00 35.78 ? 347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 110.824 126.067 151.651 1.00 25.87 ? 347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.461 124.439 149.504 1.00 32.38 ? 348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.158 123.215 149.124 1.00 31.00 ? 348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.556 123.514 148.595 1.00 30.50 ? 348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.506 122.779 148.888 1.00 32.57 ? 348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.340 122.441 148.090 1.00 32.60 ? 348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 112.366 123.035 146.693 1.00 38.10 ? 348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 113.463 122.154 145.567 1.00 54.11 ? 348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 113.450 123.253 144.152 1.00 34.43 ? 348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.703 124.588 147.817 1.00 31.09 ? 349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.017 124.953 147.305 1.00 27.14 ? 349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 116.953 125.355 148.436 1.00 27.69 ? 349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.147 125.040 148.402 1.00 28.78 ? 349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 115.886 126.084 146.288 1.00 27.70 ? 349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.983 126.163 145.227 1.00 33.11 ? 349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 116.513 125.526 143.931 1.00 34.14 ? 349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.412 127.605 145.000 1.00 32.64 ? 349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.430 126.051 149.447 1.00 26.66 ? 350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.257 126.412 150.593 1.00 21.97 ? 350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.632 125.183 151.409 1.00 30.07 ? 350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.755 125.085 151.914 1.00 33.38 ? 350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.528 127.435 151.461 1.00 19.95 ? 350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.200 128.728 150.740 1.00 25.27 ? 350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.629 129.756 151.691 1.00 25.83 ? 350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.680 130.349 152.508 1.00 38.19 ? 350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.519 130.755 153.758 1.00 32.23 ? 350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 115.348 130.673 154.366 1.00 29.86 ? 350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 117.561 131.254 154.416 1.00 28.74 ? 350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.703 124.237 151.552 1.00 35.52 ? 351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.015 123.002 152.262 1.00 31.15 ? 351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.100 122.213 151.542 1.00 35.41 ? 351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.001 121.656 152.179 1.00 42.58 ? 351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 115.753 122.156 152.420 1.00 32.65 ? 351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.010 122.556 153.557 1.00 46.43 ? 351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.027 122.147 150.212 1.00 33.71 ? 352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 118.986 121.345 149.461 1.00 32.65 ? 352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.345 122.030 149.350 1.00 35.54 ? 352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.383 121.369 149.457 1.00 39.99 ? 352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.433 121.030 148.071 1.00 34.18 ? 352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 119.161 121.729 146.938 1.00 39.71 ? 352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 118.423 121.632 145.620 1.00 43.24 ? 352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.530 120.768 145.498 1.00 42.47 ? 352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 118.739 122.420 144.704 1.00 42.15 ? 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.364 123.348 149.140 1.00 35.25 ? 353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.604 124.070 148.893 1.00 31.52 ? 353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 121.822 125.279 149.790 1.00 26.89 ? 353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 122.928 125.828 149.785 1.00 33.67 ? 353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.672 124.531 147.429 1.00 34.13 ? 353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 120.729 125.557 147.171 1.00 35.87 ? 353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 120.819 125.714 150.549 1.00 25.74 ? 354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 120.932 126.910 151.353 1.00 27.31 ? 354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.601 128.197 150.631 1.00 24.29 ? 354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.596 129.259 151.264 1.00 27.63 ? 354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.329 128.138 149.335 1.00 27.88 ? 355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.960 129.287 148.529 1.00 18.23 ? 355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.476 129.257 148.198 1.00 22.56 ? 355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.831 128.207 148.274 1.00 32.04 ? 355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.767 129.329 147.225 1.00 26.40 ? 355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.247 129.555 147.419 1.00 30.52 ? 355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.725 130.760 147.918 1.00 20.53 ? 355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.167 128.569 147.094 1.00 26.62 ? 355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 124.077 130.971 148.093 1.00 24.63 ? 355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.519 128.772 147.264 1.00 24.77 ? 355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.969 129.973 147.763 1.00 26.55 ? 355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.318 130.176 147.933 1.00 30.94 ? 355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.897 130.399 147.823 1.00 24.60 ? 356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.516 131.725 147.715 1.00 12.86 ? 356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.518 132.490 149.033 1.00 16.56 ? 356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.864 132.092 149.992 1.00 23.01 ? 356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.634 132.414 146.670 1.00 17.42 ? 356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.271 131.853 146.949 1.00 22.21 ? 356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.508 130.409 147.331 1.00 19.89 ? 356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.258 133.593 149.110 1.00 21.42 ? 357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 119.052 134.541 150.192 1.00 15.45 ? 357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.680 135.185 150.042 1.00 16.10 ? 357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 117.190 135.399 148.931 1.00 20.78 ? 357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 120.131 135.624 150.189 1.00 11.98 ? 357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.548 135.117 150.058 1.00 14.29 ? 357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.915 133.881 150.565 1.00 14.00 ? 357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.522 135.881 149.432 1.00 16.82 ? 357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.208 133.417 150.451 1.00 17.50 ? 357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.819 135.426 149.312 1.00 15.86 ? 357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 124.156 134.193 149.824 1.00 19.47 ? 357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.446 133.734 149.709 1.00 29.92 ? 357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 117.055 135.495 151.171 1.00 17.75 ? 358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.726 136.092 151.187 1.00 12.47 ? 358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.853 137.521 151.691 1.00 17.94 ? 358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 116.328 137.754 152.809 1.00 20.13 ? 358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.746 135.290 152.057 1.00 20.66 ? 358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.695 133.830 151.602 1.00 18.68 ? 358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 113.365 135.920 152.012 1.00 15.10 ? 358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 114.286 133.653 150.162 1.00 17.12 ? 358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.434 138.473 150.867 1.00 16.54 ? 359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 115.327 139.871 151.260 1.00 8.55  ? 359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.854 140.247 151.266 1.00 15.52 ? 359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 113.192 140.187 150.225 1.00 18.17 ? 359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 116.115 140.775 150.310 1.00 14.17 ? 359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 116.559 142.090 150.933 1.00 17.85 ? 359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 116.761 143.425 149.741 1.00 31.27 ? 359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.232 144.323 149.963 1.00 6.74  ? 359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 113.342 140.622 152.433 1.00 13.75 ? 360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.964 141.091 152.559 1.00 9.65  ? 360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.975 142.590 152.292 1.00 13.77 ? 360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 112.340 143.387 153.158 1.00 22.86 ? 360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 111.397 140.749 153.931 1.00 13.59 ? 360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 111.252 139.274 154.170 1.00 17.20 ? 360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.460 138.499 153.338 1.00 17.03 ? 360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.910 138.658 155.220 1.00 16.86 ? 360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.326 137.142 153.551 1.00 19.11 ? 360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.779 137.301 155.437 1.00 17.35 ? 360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.986 136.543 154.602 1.00 16.26 ? 360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.574 142.970 151.077 1.00 17.17 ? 361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.772 144.341 150.618 1.00 8.05  ? 361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 111.004 145.340 151.475 1.00 11.93 ? 361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.534 146.398 151.831 1.00 16.63 ? 361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 111.357 144.460 149.153 1.00 17.68 ? 361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 111.389 145.874 148.607 1.00 23.75 ? 361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 112.088 145.959 147.268 1.00 19.90 ? 361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 112.104 144.997 146.504 1.00 23.37 ? 361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.677 147.113 146.979 1.00 21.17 ? 361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.754 145.027 151.817 1.00 22.00 ? 362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.948 145.977 152.575 1.00 19.82 ? 362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 109.407 146.077 154.023 1.00 18.30 ? 362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 109.282 147.141 154.638 1.00 23.43 ? 362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.472 145.590 152.504 1.00 21.56 ? 362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.841 145.958 151.176 1.00 30.35 ? 362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.084 145.242 150.183 1.00 31.69 ? 362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 106.104 146.964 151.125 1.00 34.61 ? 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.938 144.989 154.582 1.00 20.36 ? 363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.551 145.070 155.903 1.00 11.06 ? 363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.762 145.993 155.880 1.00 15.96 ? 363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.981 146.771 156.815 1.00 23.67 ? 363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.950 143.675 156.383 1.00 13.21 ? 363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.809 142.940 157.053 1.00 15.44 ? 363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.775 143.525 157.365 1.00 25.26 ? 363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 109.993 141.646 157.278 1.00 12.07 ? 363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.562 145.915 154.817 1.00 14.39 ? 364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.742 146.763 154.696 1.00 12.62 ? 364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 113.346 148.227 154.554 1.00 12.74 ? 364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.955 149.110 155.168 1.00 23.96 ? 364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.610 146.294 153.514 1.00 3.08  ? 364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.779 147.238 153.307 1.00 2.95  ? 364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 115.098 144.876 153.746 1.00 5.13  ? 364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 112.325 148.510 153.749 1.00 11.88 ? 365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 112.015 149.879 153.364 1.00 7.76  ? 365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 111.006 150.563 154.276 1.00 12.20 ? 365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.894 151.792 154.230 1.00 18.39 ? 365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 111.501 149.915 151.922 1.00 12.75 ? 365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 112.592 149.630 150.913 1.00 10.98 ? 365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.628 150.290 150.904 1.00 16.32 ? 365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 112.366 148.644 150.058 1.00 16.41 ? 365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 110.270 149.815 155.099 1.00 22.06 ? 366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 109.362 150.461 156.038 1.00 20.05 ? 366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 110.114 151.220 157.121 1.00 19.07 ? 366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 109.548 152.134 157.730 1.00 26.64 ? 366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 108.423 149.430 156.666 1.00 17.73 ? 366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 109.086 148.496 157.659 1.00 25.05 ? 366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 108.049 147.788 158.512 1.00 25.50 ? 366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 107.014 147.085 157.651 1.00 23.94 ? 366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 106.251 146.068 158.425 1.00 27.64 ? 366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 111.373 150.863 157.369 1.00 23.17 ? 367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 112.235 151.574 158.302 1.00 16.05 ? 367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 113.406 152.249 157.609 1.00 14.41 ? 367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 114.250 152.845 158.285 1.00 23.62 ? 367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.744 150.637 159.417 1.00 13.36 ? 367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 111.597 150.209 160.312 1.00 14.06 ? 367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 113.438 149.427 158.815 1.00 10.72 ? 367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 113.484 152.175 156.284 1.00 17.11 ? 368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 114.621 152.724 155.562 1.00 4.16  ? 368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 114.624 154.244 155.660 1.00 14.95 ? 368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 113.627 154.901 155.347 1.00 27.75 ? 368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 114.575 152.278 154.103 1.00 6.95  ? 368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.745 152.735 153.291 1.00 13.98 ? 368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.621 153.167 151.989 1.00 14.53 ? 368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 117.060 152.825 153.595 1.00 7.49  ? 368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.812 153.499 151.524 1.00 15.00 ? 368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.702 153.302 152.479 1.00 14.14 ? 368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.755 154.802 156.091 1.00 18.35 ? 369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.850 156.235 156.335 1.00 13.28 ? 369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 116.102 157.044 155.071 1.00 17.10 ? 369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.915 158.264 155.090 1.00 22.09 ? 369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.956 156.521 157.352 1.00 11.71 ? 369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 116.508 156.403 153.979 1.00 15.45 ? 370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 116.889 157.097 152.755 1.00 14.76 ? 370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 116.047 156.638 151.571 1.00 12.57 ? 370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 116.558 156.415 150.473 1.00 22.93 ? 370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 118.375 156.904 152.465 1.00 8.88  ? 370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 119.259 157.434 153.575 1.00 12.32 ? 370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 119.196 158.611 153.925 1.00 26.71 ? 370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 120.084 156.565 154.140 1.00 19.98 ? 370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 114.738 156.491 151.780 1.00 16.55 ? 371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.853 156.151 150.673 1.00 11.89 ? 371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 113.758 157.272 149.648 1.00 18.30 ? 371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 113.442 157.006 148.484 1.00 19.21 ? 371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 112.459 155.804 151.194 1.00 10.15 ? 371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 112.350 154.366 151.651 1.00 17.31 ? 371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 113.125 153.508 151.232 1.00 21.88 ? 371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 111.382 154.095 152.512 1.00 18.49 ? 371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 114.023 158.516 150.052 1.00 25.92 ? 372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 114.029 159.616 149.095 1.00 17.44 ? 372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 115.127 159.432 148.057 1.00 20.87 ? 372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.929 159.726 146.872 1.00 28.82 ? 372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 114.194 160.948 149.826 1.00 19.41 ? 372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 115.529 161.116 150.479 1.00 22.84 ? 372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 115.953 160.321 151.521 1.00 23.35 ? 372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 116.538 161.985 150.234 1.00 19.45 ? 372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 117.165 160.694 151.892 1.00 17.29 ? 372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 117.542 161.702 151.128 1.00 23.41 ? 372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 116.298 158.959 148.483 1.00 17.44 ? 373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 117.362 158.653 147.535 1.00 17.98 ? 373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.954 157.486 146.648 1.00 18.99 ? 373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 117.079 157.540 145.419 1.00 30.91 ? 373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 118.677 158.363 148.280 1.00 22.75 ? 373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 119.065 159.555 149.158 1.00 17.32 ? 373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 119.785 158.024 147.297 1.00 19.50 ? 373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 120.194 159.269 150.119 1.00 13.19 ? 373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 116.457 156.416 147.257 1.00 13.52 ? 374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.963 155.255 146.535 1.00 8.78  ? 374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 115.468 154.242 147.554 1.00 12.49 ? 374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.834 154.290 148.731 1.00 21.31 ? 374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 117.044 154.631 145.647 1.00 16.31 ? 374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 116.506 153.612 144.826 1.00 27.62 ? 374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 114.619 153.334 147.088 1.00 23.34 ? 375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 114.296 152.154 147.867 1.00 13.63 ? 375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 115.476 151.189 147.859 1.00 12.91 ? 375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 116.334 151.220 146.973 1.00 27.18 ? 375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 113.053 151.462 147.308 1.00 12.06 ? 375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.834 151.556 148.200 1.00 14.61 ? 375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 111.267 152.958 148.220 1.00 17.92 ? 375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.778 152.938 148.510 1.00 22.12 ? 375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 109.481 152.338 149.839 1.00 28.79 ? 375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 115.522 150.330 148.870 1.00 13.66 ? 376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 116.500 149.250 148.894 1.00 13.56 ? 376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.957 148.110 148.043 1.00 13.56 ? 376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.868 147.589 148.307 1.00 25.71 ? 376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.791 148.788 150.329 1.00 10.05 ? 376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.798 147.651 150.322 1.00 0.39  ? 376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 117.299 149.951 151.166 1.00 2.78  ? 376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.712 147.725 147.014 1.00 16.68 ? 377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 116.251 146.739 146.048 1.00 14.19 ? 377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.893 145.371 146.204 1.00 11.30 ? 377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 116.293 144.378 145.788 1.00 28.67 ? 377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 116.503 147.238 144.618 1.00 14.73 ? 377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.826 148.555 144.296 1.00 11.34 ? 377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 116.725 149.422 143.440 1.00 20.92 ? 377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 116.469 150.895 143.687 1.00 23.81 ? 377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 117.536 151.740 143.086 1.00 28.54 ? 377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 118.085 145.293 146.782 1.00 13.04 ? 378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.786 144.026 146.932 1.00 7.75  ? 378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.807 144.177 148.051 1.00 10.04 ? 378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.976 145.257 148.623 1.00 18.19 ? 378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 119.436 143.588 145.615 1.00 7.54  ? 378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.574 144.465 145.166 1.00 12.21 ? 378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 120.398 145.828 145.003 1.00 13.29 ? 378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.816 143.919 144.891 1.00 4.62  ? 378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 121.438 146.630 144.586 1.00 9.48  ? 378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.859 144.718 144.471 1.00 4.67  ? 378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.669 146.075 144.318 1.00 11.63 ? 378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.482 143.080 148.361 1.00 12.18 ? 379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.473 143.033 149.423 1.00 0.75  ? 379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.822 142.625 148.836 1.00 5.11  ? 379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.983 142.498 147.620 1.00 11.28 ? 379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 121.021 142.082 150.533 1.00 8.13  ? 379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.625 142.419 151.766 1.00 10.48 ? 379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.793 142.417 149.716 1.00 14.67 ? 380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 125.151 142.088 149.320 1.00 4.52  ? 380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 125.344 140.572 149.331 1.00 9.49  ? 380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 124.391 139.800 149.456 1.00 12.78 ? 380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 126.147 142.798 150.234 1.00 11.89 ? 380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 126.125 142.262 151.648 1.00 3.04  ? 380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 125.062 142.058 152.229 1.00 15.30 ? 380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 127.301 142.038 152.213 1.00 6.55  ? 380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.594 140.132 149.188 1.00 21.75 ? 381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.900 138.708 149.189 1.00 7.54  ? 381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.720 138.075 150.562 1.00 8.19  ? 381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.667 136.845 150.661 1.00 19.16 ? 381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 128.329 138.488 148.689 1.00 14.25 ? 381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.864 137.056 148.641 1.00 19.33 ? 381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 128.044 136.197 147.695 1.00 15.12 ? 381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.325 137.058 148.235 1.00 18.96 ? 381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.623 138.878 151.620 1.00 13.33 ? 382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.400 138.371 152.966 1.00 7.71  ? 382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 125.022 138.722 153.511 1.00 10.21 ? 382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.679 138.286 154.614 1.00 12.39 ? 382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.486 138.894 153.913 1.00 17.51 ? 382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 129.158 138.357 153.482 1.00 32.30 ? 382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 124.229 139.498 152.771 1.00 9.99  ? 383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.825 139.751 153.089 1.00 5.40  ? 383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.645 140.634 154.322 1.00 10.84 ? 383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.623 140.549 155.005 1.00 18.85 ? 383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 122.054 138.438 153.263 1.00 8.46  ? 383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 122.540 137.696 154.369 1.00 24.20 ? 383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.617 141.494 154.627 1.00 11.06 ? 384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 123.471 142.439 155.726 1.00 12.38 ? 384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 123.617 143.892 155.295 1.00 16.15 ? 384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 123.551 144.784 156.147 1.00 30.46 ? 384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 124.472 142.125 156.851 1.00 7.12  ? 384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.700 143.026 156.919 1.00 10.43 ? 384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.629 142.868 155.733 1.00 18.68 ? 384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 127.533 143.714 155.571 1.00 27.16 ? 384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 126.473 141.888 154.980 1.00 10.28 ? 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.792 144.159 154.005 1.00 12.79 ? 385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.929 145.517 153.490 1.00 7.03  ? 385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.605 145.916 152.854 1.00 18.03 ? 385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 122.133 145.258 151.920 1.00 20.96 ? 385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 125.083 145.622 152.482 1.00 9.76  ? 385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 125.099 146.998 151.838 1.00 12.20 ? 385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 126.404 145.330 153.164 1.00 6.52  ? 385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 122.007 146.999 153.356 1.00 10.80 ? 386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.691 147.461 152.905 1.00 0.00  ? 386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.755 148.980 152.765 1.00 4.87  ? 386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 120.508 149.715 153.724 1.00 17.00 ? 386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.599 147.026 153.872 1.00 7.07  ? 386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 119.450 145.517 154.067 1.00 5.58  ? 386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 118.510 145.220 155.219 1.00 2.95  ? 386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.961 144.862 152.784 1.00 4.78  ? 386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 121.083 149.444 151.562 1.00 12.76 ? 387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 121.253 150.864 151.301 1.00 11.01 ? 387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 120.573 151.227 149.991 1.00 6.75  ? 387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 120.360 150.381 149.120 1.00 16.76 ? 387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.735 151.253 151.247 1.00 7.73  ? 387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 123.535 150.795 152.446 1.00 4.11  ? 387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.990 151.181 152.350 1.00 9.97  ? 387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 125.370 152.014 151.531 1.00 21.43 ? 387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.817 150.575 153.191 1.00 13.44 ? 387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 120.226 152.503 149.868 1.00 13.69 ? 388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.668 153.010 148.624 1.00 11.11 ? 388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.727 153.002 147.530 1.00 9.99  ? 388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.878 153.383 147.754 1.00 24.76 ? 388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 119.125 154.424 148.820 1.00 6.20  ? 388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 120.335 152.554 146.343 1.00 11.05 ? 389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 121.214 152.548 145.187 1.00 9.13  ? 389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 120.488 153.156 143.998 1.00 13.57 ? 389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 119.258 153.115 143.912 1.00 24.86 ? 389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 121.688 151.129 144.841 1.00 11.83 ? 389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 120.593 150.244 144.691 1.00 23.90 ? 389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 121.263 153.726 143.081 1.00 15.83 ? 390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.737 154.277 141.842 1.00 10.19 ? 390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 121.516 153.675 140.684 1.00 9.92  ? 390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.750 153.678 140.695 1.00 23.55 ? 390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.831 155.805 141.829 1.00 12.79 ? 390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.854 156.482 142.777 1.00 14.02 ? 390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 120.126 157.961 142.944 1.00 20.40 ? 390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 121.144 158.473 142.480 1.00 26.95 ? 390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 119.216 158.658 143.612 1.00 18.70 ? 390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.794 153.154 139.693 1.00 19.03 ? 391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 121.442 152.461 138.589 1.00 14.40 ? 391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 122.170 153.463 137.701 1.00 18.47 ? 391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.698 154.582 137.461 1.00 19.62 ? 391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 120.415 151.646 137.781 1.00 16.18 ? 391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 119.567 152.564 136.918 1.00 15.48 ? 391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 121.118 150.601 136.934 1.00 17.29 ? 391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 123.337 153.058 137.214 1.00 26.57 ? 392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 124.111 153.864 136.286 1.00 16.30 ? 392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.708 153.549 134.852 1.00 25.60 ? 392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 123.255 152.445 134.540 1.00 29.96 ? 392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 125.610 153.619 136.469 1.00 21.45 ? 392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 126.020 153.914 137.791 1.00 28.69 ? 392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.873 154.536 133.982 1.00 30.13 ? 393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 123.608 154.386 132.555 1.00 27.72 ? 393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.942 154.486 131.826 1.00 27.50 ? 393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 125.463 155.584 131.612 1.00 30.98 ? 393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 122.620 155.440 132.066 1.00 32.70 ? 393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 122.586 155.485 130.651 1.00 37.26 ? 393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 125.492 153.338 131.448 1.00 32.60 ? 394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.740 153.276 130.700 1.00 29.49 ? 394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 126.407 153.249 129.215 1.00 26.91 ? 394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.711 152.343 128.746 1.00 32.29 ? 394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 127.556 152.050 131.106 1.00 26.95 ? 394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.977 152.073 132.557 1.00 30.11 ? 394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.967 152.939 132.999 1.00 27.75 ? 394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 127.375 151.238 133.487 1.00 24.55 ? 394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 129.351 152.967 134.323 1.00 28.05 ? 394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.752 151.259 134.814 1.00 25.11 ? 394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.740 152.125 135.227 1.00 34.09 ? 394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 129.119 152.149 136.550 1.00 36.44 ? 394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.897 154.242 128.486 1.00 34.03 ? 395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 126.537 154.451 127.096 1.00 35.09 ? 395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 127.645 153.936 126.179 1.00 34.98 ? 395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 128.608 153.301 126.619 1.00 35.22 ? 395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 126.242 155.932 126.860 1.00 33.48 ? 395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 127.389 156.711 127.217 1.00 37.99 ? 395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 125.062 156.373 127.708 1.00 31.09 ? 395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 127.506 154.206 124.884 1.00 36.25 ? 396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 128.496 153.772 123.915 1.00 36.37 ? 396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.810 154.521 124.114 1.00 36.41 ? 396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.859 155.606 124.698 1.00 40.32 ? 396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.989 153.985 122.488 1.00 36.41 ? 396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.607 153.408 122.267 1.00 42.76 ? 396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.357 152.272 122.718 1.00 39.73 ? 396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.773 154.089 121.635 1.00 45.48 ? 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.887 153.918 123.618 1.00 37.62 ? 397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 132.193 154.558 123.667 1.00 38.54 ? 397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 132.130 155.941 123.032 1.00 40.30 ? 397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 131.474 156.144 122.008 1.00 45.98 ? 397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 133.232 153.698 122.946 1.00 34.78 ? 397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.648 153.948 123.404 1.00 35.71 ? 397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 135.202 153.214 124.443 1.00 36.78 ? 397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 135.426 154.929 122.805 1.00 35.36 ? 397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 136.495 153.443 124.863 1.00 36.03 ? 397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.717 155.166 123.221 1.00 32.68 ? 397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 137.247 154.420 124.250 1.00 35.18 ? 397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 138.536 154.655 124.666 1.00 39.83 ? 397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 132.820 156.894 123.652 1.00 39.08 ? 398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 132.883 158.297 123.255 1.00 46.27 ? 398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 131.642 159.064 123.696 1.00 45.80 ? 398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 131.577 160.280 123.474 1.00 45.61 ? 398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 133.073 158.481 121.741 1.00 46.45 ? 398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 134.431 158.005 121.264 1.00 50.07 ? 398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 135.403 158.098 122.044 1.00 51.09 ? 398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 134.527 157.537 120.110 1.00 49.31 ? 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 130.660 158.409 124.305 1.00 45.21 ? 399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 129.530 159.084 124.919 1.00 41.95 ? 399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 129.771 159.226 126.415 1.00 45.19 ? 399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 130.615 158.538 126.994 1.00 44.07 ? 399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 128.227 158.322 124.670 1.00 40.26 ? 399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 127.726 158.400 123.239 1.00 43.18 ? 399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 126.299 157.907 123.092 1.00 48.76 ? 399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 125.903 156.987 123.838 1.00 46.02 ? 399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.572 158.439 122.226 1.00 49.74 ? 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 129.019 160.128 127.039 1.00 47.68 ? 400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 129.145 160.350 128.471 1.00 41.98 ? 400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 128.274 159.360 129.233 1.00 43.52 ? 400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 127.093 159.185 128.916 1.00 41.72 ? 400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.756 161.783 128.829 1.00 42.12 ? 400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.875 162.794 128.644 1.00 46.17 ? 400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 131.222 162.274 129.111 1.00 50.67 ? 400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 131.253 161.422 130.024 1.00 49.35 ? 400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 132.252 162.716 128.561 1.00 49.26 ? 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.861 158.712 130.234 1.00 39.92 ? 401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 128.130 157.765 131.061 1.00 35.02 ? 401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 127.370 158.493 132.160 1.00 34.68 ? 401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.870 159.454 132.751 1.00 38.67 ? 401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 129.085 156.746 131.683 1.00 31.67 ? 401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 129.621 155.756 130.673 1.00 41.34 ? 401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.872 155.387 129.743 1.00 46.91 ? 401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.791 155.343 130.810 1.00 39.70 ? 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 126.154 158.029 132.431 1.00 32.62 ? 402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 125.365 158.529 133.553 1.00 30.27 ? 402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 125.698 157.663 134.759 1.00 24.13 ? 402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 125.164 156.563 134.916 1.00 29.03 ? 402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.875 158.501 133.229 1.00 31.98 ? 402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 123.006 159.259 134.223 1.00 35.22 ? 402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.724 158.465 135.487 1.00 40.72 ? 402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 122.600 157.225 135.400 1.00 38.59 ? 402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 122.629 159.082 136.570 1.00 37.10 ? 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 126.590 158.155 135.611 1.00 24.67 ? 403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 127.053 157.387 136.761 1.00 27.94 ? 403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 126.033 157.520 137.883 1.00 29.67 ? 403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 125.681 158.632 138.290 1.00 24.12 ? 403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 128.442 157.855 137.217 1.00 21.11 ? 403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 129.453 157.709 136.077 1.00 24.43 ? 403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 128.890 157.075 138.441 1.00 17.50 ? 403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 129.432 156.355 135.414 1.00 24.81 ? 403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 125.556 156.388 138.380 1.00 21.73 ? 404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 124.610 156.337 139.471 1.00 8.01  ? 404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 125.288 156.134 140.808 1.00 18.00 ? 404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 126.416 156.585 141.037 1.00 29.33 ? 404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 124.597 155.440 141.706 1.00 22.59 ? 405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 125.101 155.170 143.045 1.00 6.11  ? 405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 125.129 153.669 143.277 1.00 6.10  ? 405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 124.078 153.021 143.304 1.00 16.38 ? 405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 124.240 155.859 144.105 1.00 17.98 ? 405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 124.246 157.387 144.103 1.00 17.32 ? 405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 123.237 157.926 145.101 1.00 17.90 ? 405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 125.638 157.916 144.398 1.00 16.09 ? 405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 126.327 153.121 143.443 1.00 18.07 ? 406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 126.502 151.748 143.879 1.00 8.78  ? 406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.572 151.719 145.403 1.00 18.39 ? 406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 126.465 152.745 146.076 1.00 25.39 ? 406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 127.749 151.135 143.241 1.00 14.27 ? 406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 127.464 150.514 141.887 1.00 24.80 ? 406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 126.277 150.290 141.568 1.00 25.98 ? 406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 128.427 150.254 141.138 1.00 33.29 ? 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 126.740 150.526 145.960 1.00 23.34 ? 407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.749 150.345 147.405 1.00 14.16 ? 407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 128.064 149.705 147.821 1.00 16.84 ? 407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 128.538 148.757 147.185 1.00 21.85 ? 407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 125.552 149.499 147.884 1.00 15.36 ? 407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 124.238 150.229 147.604 1.00 5.71  ? 407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.680 149.197 149.362 1.00 12.45 ? 407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 123.111 149.312 147.192 1.00 16.82 ? 407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.658 150.245 148.881 1.00 21.78 ? 408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.814 149.647 149.529 1.00 18.49 ? 408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.927 150.232 150.927 1.00 20.79 ? 408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 129.760 151.440 151.115 1.00 35.49 ? 408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 131.105 149.895 148.741 1.00 21.13 ? 408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.478 151.262 148.782 1.00 27.24 ? 408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 130.201 149.374 151.903 1.00 20.14 ? 409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 130.446 149.823 153.263 1.00 30.23 ? 409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 131.616 149.044 153.839 1.00 25.45 ? 409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.763 147.844 153.597 1.00 32.43 ? 409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 129.202 149.663 154.155 1.00 22.01 ? 409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.756 147.958 154.546 1.00 42.52 ? 409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 132.452 149.743 154.596 1.00 19.03 ? 410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 133.550 149.121 155.318 1.00 22.91 ? 410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 133.063 148.721 156.703 1.00 21.62 ? 410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 132.366 149.488 157.373 1.00 22.49 ? 410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 134.751 150.063 155.416 1.00 22.82 ? 410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 134.364 151.456 155.862 1.00 27.28 ? 410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 133.597 152.145 155.190 1.00 30.33 ? 410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 134.900 151.881 156.996 1.00 30.30 ? 410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 133.430 147.517 157.125 1.00 19.04 ? 411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.838 146.895 158.296 1.00 14.14 ? 411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.778 146.943 159.492 1.00 14.23 ? 411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 135.004 146.964 159.352 1.00 22.28 ? 411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.458 145.439 158.012 1.00 20.10 ? 411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.929 145.131 156.614 1.00 16.74 ? 411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.616 143.653 156.479 1.00 18.86 ? 411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.704 145.973 156.316 1.00 18.00 ? 411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 133.170 146.971 160.671 1.00 18.22 ? 412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.877 146.749 161.915 1.00 9.78  ? 412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.891 146.170 162.904 1.00 13.76 ? 412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 131.684 146.418 162.823 1.00 22.99 ? 412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 133.413 145.388 163.840 1.00 13.81 ? 413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 132.582 144.667 164.793 1.00 11.40 ? 413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.946 145.067 166.212 1.00 15.77 ? 413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 134.126 145.080 166.577 1.00 26.69 ? 413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.730 143.154 164.620 1.00 12.62 ? 413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.955 142.689 163.531 1.00 26.47 ? 413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.933 145.398 167.003 1.00 18.51 ? 414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 132.110 145.528 168.438 1.00 13.26 ? 414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 132.160 144.145 169.068 1.00 17.39 ? 414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 131.375 143.260 168.718 1.00 21.11 ? 414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.971 146.337 169.057 1.00 18.94 ? 414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 130.694 147.728 168.492 1.00 15.44 ? 414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 129.500 148.344 169.194 1.00 17.84 ? 414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.918 148.614 168.631 1.00 20.50 ? 414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 133.095 143.957 169.991 1.00 25.62 ? 415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 133.146 142.739 170.793 1.00 22.83 ? 415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 132.235 142.969 171.991 1.00 23.39 ? 415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 132.599 143.668 172.938 1.00 33.12 ? 415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 134.575 142.417 171.211 1.00 24.78 ? 415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 134.731 140.993 171.703 1.00 25.03 ? 415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.877 140.475 172.417 1.00 31.25 ? 415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 135.825 140.352 171.316 1.00 25.30 ? 415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 131.040 142.379 171.944 1.00 15.73 ? 416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 130.013 142.700 172.931 1.00 17.81 ? 416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 130.490 142.355 174.335 1.00 22.98 ? 416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 130.297 143.131 175.278 1.00 27.39 ? 416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.696 141.981 172.583 1.00 23.52 ? 416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 128.075 142.596 171.329 1.00 19.24 ? 416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.727 142.060 173.747 1.00 10.93 ? 416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.944 141.787 170.741 1.00 16.26 ? 416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 131.119 141.191 174.500 1.00 24.44 ? 417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.595 140.794 175.820 1.00 26.77 ? 417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.629 141.779 176.351 1.00 28.41 ? 417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 132.562 142.203 177.511 1.00 34.53 ? 417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 132.175 139.380 175.763 1.00 31.25 ? 417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 132.950 138.923 176.999 1.00 28.44 ? 417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 132.026 138.836 178.203 1.00 30.62 ? 417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 133.629 137.591 176.748 1.00 31.30 ? 417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.590 142.163 175.510 1.00 26.51 ? 418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.643 143.071 175.956 1.00 27.75 ? 418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 134.108 144.481 176.165 1.00 27.45 ? 418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 134.518 145.172 177.104 1.00 30.46 ? 418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.792 143.073 174.949 1.00 29.75 ? 418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.651 141.830 175.044 1.00 27.10 ? 418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 137.044 141.254 174.032 1.00 26.94 ? 418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 136.947 141.409 176.266 1.00 31.68 ? 418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 133.196 144.927 175.300 1.00 27.92 ? 419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 132.606 146.253 175.463 1.00 28.70 ? 419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.812 146.325 176.759 1.00 30.74 ? 419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 131.861 147.329 177.481 1.00 32.93 ? 419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.736 146.605 174.243 1.00 27.36 ? 419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.839 147.788 174.556 1.00 27.55 ? 419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 132.611 146.899 173.037 1.00 22.80 ? 419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 131.062 145.267 177.073 1.00 34.06 ? 420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 130.262 145.264 178.292 1.00 30.03 ? 420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 131.137 145.131 179.532 1.00 28.59 ? 420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 130.847 145.737 180.570 1.00 32.07 ? 420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 129.228 144.141 178.234 1.00 29.07 ? 420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 128.088 144.412 177.269 1.00 22.73 ? 420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 126.966 145.690 177.863 1.00 42.68 ? 420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 126.678 145.133 179.539 1.00 28.85 ? 420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 132.209 144.340 179.448 1.00 37.15 ? 421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 133.117 144.210 180.583 1.00 34.95 ? 421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.816 145.530 180.885 1.00 34.49 ? 421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 134.013 145.881 182.054 1.00 38.90 ? 421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 134.138 143.104 180.315 1.00 30.94 ? 421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 135.499 143.602 179.860 1.00 37.61 ? 421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 136.548 142.507 179.849 1.00 43.51 ? 421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 136.993 142.098 180.941 1.00 42.80 ? 421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 136.927 142.056 178.747 1.00 39.06 ? 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 134.199 146.274 179.847 1.00 33.92 ? 422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 134.853 147.563 180.030 1.00 32.48 ? 422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 133.870 148.710 180.217 1.00 37.92 ? 422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 134.303 149.829 180.511 1.00 39.30 ? 422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 135.763 147.868 178.837 1.00 31.39 ? 422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.981 147.001 178.766 1.00 37.42 ? 422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 137.002 145.801 178.090 1.00 36.69 ? 422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 138.222 147.164 179.282 1.00 37.38 ? 422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 138.202 145.260 178.195 1.00 38.64 ? 422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 138.961 146.067 178.914 1.00 38.15 ? 422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 132.570 148.464 180.061 1.00 41.75 ? 423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 131.555 149.504 180.205 1.00 38.97 ? 423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 131.869 150.693 179.300 1.00 40.81 ? 423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 131.840 151.853 179.716 1.00 42.37 ? 423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 131.430 149.944 181.664 1.00 39.08 ? 423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 130.789 148.913 182.573 1.00 40.16 ? 423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 130.865 149.339 184.029 1.00 43.62 ? 423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 131.150 148.154 184.939 1.00 44.11 ? 423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 130.030 147.174 184.945 1.00 44.86 ? 423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 132.169 150.392 178.040 1.00 34.79 ? 424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 132.656 151.378 177.082 1.00 30.35 ? 424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 131.879 151.294 175.776 1.00 30.17 ? 424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 132.450 151.263 174.684 1.00 38.81 ? 424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 134.148 151.190 176.831 1.00 33.76 ? 424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 134.407 149.929 176.240 1.00 32.33 ? 424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 130.550 151.257 175.869 1.00 30.70 ? 425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 129.732 151.248 174.660 1.00 25.53 ? 425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.896 152.557 173.899 1.00 30.94 ? 425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 130.128 152.563 172.685 1.00 33.11 ? 425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 128.257 150.980 175.005 1.00 28.64 ? 425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 128.071 149.545 175.498 1.00 31.40 ? 425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 127.373 151.247 173.797 1.00 27.41 ? 425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 126.644 149.212 175.864 1.00 32.31 ? 425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 129.794 153.686 174.602 1.00 31.97 ? 426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.885 154.983 173.938 1.00 29.03 ? 426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 131.256 155.189 173.307 1.00 29.47 ? 426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 131.366 155.502 172.115 1.00 36.02 ? 426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 129.580 156.100 174.935 1.00 27.18 ? 426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.918 157.489 174.430 1.00 32.04 ? 426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 129.661 158.563 175.466 1.00 39.22 ? 426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 129.278 158.217 176.602 1.00 39.49 ? 426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 129.841 159.756 175.143 1.00 39.36 ? 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 132.318 155.013 174.096 1.00 31.23 ? 427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 133.666 155.255 173.594 1.00 30.44 ? 427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 134.013 154.292 172.467 1.00 33.86 ? 427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 134.559 154.696 171.434 1.00 34.92 ? 427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 134.677 155.136 174.736 1.00 31.07 ? 427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 136.122 155.328 174.310 1.00 35.81 ? 427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 137.084 154.985 175.436 1.00 37.25 ? 427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 137.001 153.513 175.808 1.00 37.06 ? 427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 136.939 152.636 174.607 1.00 37.56 ? 427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 133.705 153.007 172.651 1.00 29.29 ? 428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 134.005 152.024 171.617 1.00 24.88 ? 428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 133.244 152.327 170.334 1.00 24.36 ? 428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 133.815 152.275 169.240 1.00 29.13 ? 428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 133.674 150.615 172.112 1.00 23.23 ? 428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 134.494 150.300 173.244 1.00 29.92 ? 428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.921 149.593 171.016 1.00 19.13 ? 428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.956 152.657 170.449 1.00 20.59 ? 429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 131.154 152.935 169.263 1.00 24.86 ? 429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 131.690 154.158 168.533 1.00 22.70 ? 429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 131.813 154.158 167.303 1.00 25.40 ? 429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 129.672 153.106 169.647 1.00 22.28 ? 429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 128.895 153.720 168.498 1.00 19.02 ? 429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 129.071 151.769 170.045 1.00 20.46 ? 429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 132.021 155.217 169.272 1.00 24.60 ? 430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 132.510 156.431 168.627 1.00 18.25 ? 430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 133.865 156.208 167.965 1.00 21.53 ? 430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 134.098 156.679 166.845 1.00 27.81 ? 430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 132.571 157.569 169.644 1.00 22.02 ? 430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 131.210 157.910 170.227 1.00 22.89 ? 430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 131.194 159.278 170.874 1.00 30.33 ? 430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 129.780 159.683 171.249 1.00 29.82 ? 430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 129.734 161.022 171.897 1.00 32.31 ? 430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 134.770 155.484 168.630 1.00 25.33 ? 431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 136.068 155.202 168.024 1.00 21.07 ? 431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 135.925 154.325 166.786 1.00 25.84 ? 431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 136.613 154.543 165.780 1.00 31.65 ? 431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.991 154.545 169.047 1.00 29.95 ? 431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 137.991 155.479 169.727 1.00 31.49 ? 431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 138.946 154.691 170.603 1.00 28.39 ? 431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 138.750 156.293 168.692 1.00 31.55 ? 431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 135.046 153.322 166.841 1.00 23.66 ? 432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 134.808 152.485 165.672 1.00 15.83 ? 432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 134.220 153.300 164.529 1.00 20.11 ? 432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 134.580 153.097 163.365 1.00 24.25 ? 432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.885 151.323 166.038 1.00 20.56 ? 432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 133.305 154.219 164.841 1.00 25.32 ? 433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 132.753 155.092 163.811 1.00 21.27 ? 433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 133.842 155.948 163.182 1.00 20.87 ? 433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 133.877 156.121 161.960 1.00 28.18 ? 433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 131.652 155.972 164.403 1.00 19.09 ? 433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 130.604 155.146 164.924 1.00 25.14 ? 433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 131.078 156.896 163.341 1.00 19.05 ? 433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 134.743 156.492 164.002 1.00 24.19 ? 434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 135.844 157.285 163.464 1.00 19.08 ? 434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 136.730 156.451 162.547 1.00 19.62 ? 434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 137.111 156.900 161.459 1.00 28.11 ? 434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 136.670 157.883 164.602 1.00 22.44 ? 434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 135.895 158.896 165.415 1.00 32.03 ? 434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 134.996 159.551 164.849 1.00 35.18 ? 434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 136.186 159.041 166.620 1.00 37.12 ? 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 137.068 155.231 162.969 1.00 18.53 ? 435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 137.936 154.388 162.152 1.00 17.05 ? 435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 137.258 153.995 160.845 1.00 17.99 ? 435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 137.897 153.977 159.786 1.00 25.67 ? 435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 138.355 153.146 162.939 1.00 19.74 ? 435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 137.264 152.265 163.129 1.00 21.93 ? 435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.961 153.684 160.896 1.00 22.63 ? 436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 135.236 153.328 159.681 1.00 11.68 ? 436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 135.114 154.522 158.746 1.00 18.40 ? 436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 135.207 154.373 157.522 1.00 22.34 ? 436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 133.858 152.775 160.038 1.00 19.84 ? 436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 133.841 151.405 160.718 1.00 19.63 ? 436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 132.542 151.203 161.478 1.00 15.43 ? 436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 134.050 150.296 159.704 1.00 18.72 ? 436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 134.908 155.717 159.303 1.00 22.43 ? 437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 134.886 156.922 158.484 1.00 19.37 ? 437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 136.231 157.150 157.812 1.00 24.19 ? 437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 136.290 157.514 156.634 1.00 27.35 ? 437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 134.503 158.130 159.337 1.00 21.85 ? 437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 133.347 157.814 160.122 1.00 21.50 ? 437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 134.196 159.327 158.454 1.00 22.83 ? 437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 137.326 156.944 158.547 1.00 21.96 ? 438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 138.647 157.084 157.943 1.00 21.04 ? 438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 138.851 156.072 156.823 1.00 22.02 ? 438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 139.386 156.410 155.759 1.00 29.69 ? 438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 139.737 156.930 159.003 1.00 24.00 ? 438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 141.125 156.984 158.447 1.00 28.07 ? 438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 141.762 158.170 158.150 1.00 27.95 ? 438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 141.995 155.999 158.123 1.00 28.47 ? 438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 142.965 157.912 157.671 1.00 31.12 ? 438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 143.132 156.603 157.644 1.00 34.12 ? 438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 138.434 154.825 157.043 1.00 22.41 ? 439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 138.586 153.805 156.009 1.00 22.78 ? 439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 137.790 154.186 154.769 1.00 30.90 ? 439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 138.271 154.051 153.638 1.00 33.18 ? 439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 138.169 152.425 156.548 1.00 21.05 ? 439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 138.174 151.396 155.427 1.00 20.49 ? 439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 139.090 151.998 157.672 1.00 20.13 ? 439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 136.560 154.665 154.960 1.00 31.55 ? 440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 135.749 155.094 153.826 1.00 19.31 ? 440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 136.392 156.272 153.101 1.00 26.01 ? 440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 136.394 156.324 151.866 1.00 34.00 ? 440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 134.341 155.453 154.302 1.00 24.86 ? 440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 133.514 155.835 153.219 1.00 32.69 ? 440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 136.943 157.227 153.852 1.00 30.60 ? 441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 137.543 158.408 153.240 1.00 26.11 ? 441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 138.785 158.050 152.435 1.00 32.14 ? 441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 139.018 158.616 151.361 1.00 39.73 ? 441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 137.882 159.437 154.316 1.00 24.91 ? 441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 136.701 160.283 154.751 1.00 31.91 ? 441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 136.831 160.774 156.177 1.00 36.89 ? 441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 137.839 160.440 156.835 1.00 37.93 ? 441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 135.923 161.493 156.641 1.00 35.63 ? 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 139.597 157.121 152.935 1.00 28.82 ? 442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 140.824 156.740 152.249 1.00 29.22 ? 442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 140.594 155.718 151.144 1.00 30.71 ? 442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 141.555 155.329 150.473 1.00 35.88 ? 442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 141.846 156.187 153.247 1.00 33.26 ? 442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 141.337 154.989 153.847 1.00 32.55 ? 442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 142.132 157.209 154.334 1.00 32.77 ? 442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 139.358 155.277 150.938 1.00 30.98 ? 443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 139.048 154.311 149.896 1.00 34.44 ? 443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 138.693 155.027 148.600 1.00 37.02 ? 443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 137.928 155.995 148.599 1.00 38.02 ? 443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.891 153.405 150.322 1.00 35.69 ? 443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 138.304 152.588 151.424 1.00 41.22 ? 443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 137.463 152.514 149.170 1.00 27.44 ? 443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 139.262 154.547 147.498 1.00 43.97 ? 444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.979 155.111 146.181 1.00 44.95 ? 444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 139.164 154.013 145.145 1.00 44.31 ? 444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 140.297 153.615 144.858 1.00 46.24 ? 444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.882 156.304 145.883 1.00 43.68 ? 444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 139.547 156.972 144.563 1.00 47.91 ? 444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 138.599 156.518 143.888 1.00 42.91 ? 444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 140.230 157.952 144.201 1.00 48.55 ? 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 138.059 153.525 144.593 1.00 37.83 ? 445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 138.081 152.532 143.527 1.00 39.79 ? 445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 138.001 153.287 142.208 1.00 40.05 ? 445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 137.014 153.977 141.934 1.00 42.83 ? 445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.937 151.518 143.665 1.00 35.85 ? 445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 137.179 150.593 144.860 1.00 32.95 ? 445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.795 150.702 142.391 1.00 38.72 ? 445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 136.939 151.241 146.201 1.00 38.05 ? 445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 139.039 153.156 141.387 1.00 42.92 ? 446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 139.152 153.905 140.144 1.00 46.69 ? 446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 138.645 153.129 138.935 1.00 43.27 ? 446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 138.844 153.575 137.800 1.00 41.76 ? 446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.604 154.335 139.924 1.00 45.08 ? 446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.623 153.243 140.192 1.00 43.24 ? 446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 142.962 153.831 140.608 1.00 47.81 ? 446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 142.886 154.509 141.897 1.00 48.84 ? 446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 142.696 155.813 142.051 1.00 51.38 ? 446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 142.553 156.618 141.011 1.00 48.10 ? 446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 142.647 156.321 143.279 1.00 51.16 ? 446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.996 151.986 139.150 1.00 34.72 ? 447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 137.409 151.211 138.069 1.00 29.19 ? 447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.937 150.904 138.298 1.00 31.91 ? 447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 135.344 150.158 137.511 1.00 38.57 ? 447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 138.184 149.902 137.871 1.00 33.24 ? 447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 139.227 150.008 136.781 1.00 32.27 ? 447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 139.051 150.741 135.809 1.00 31.06 ? 447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 140.326 149.286 136.943 1.00 34.04 ? 447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 135.335 151.452 139.351 1.00 33.90 ? 448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.907 151.310 139.630 1.00 29.51 ? 448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 133.355 152.705 139.885 1.00 28.58 ? 448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 133.226 153.134 141.039 1.00 29.20 ? 448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.660 150.377 140.815 1.00 23.92 ? 448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 133.028 153.449 138.823 1.00 31.23 ? 449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 132.640 154.857 139.018 1.00 23.20 ? 449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 131.458 155.034 139.951 1.00 21.51 ? 449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 131.461 155.955 140.777 1.00 23.97 ? 449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 132.312 155.331 137.594 1.00 18.40 ? 449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 132.903 154.313 136.688 1.00 27.06 ? 449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.892 153.023 137.423 1.00 24.14 ? 449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 130.445 154.173 139.848 1.00 25.02 ? 450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 129.297 154.280 140.740 1.00 19.74 ? 450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 129.696 153.995 142.181 1.00 22.25 ? 450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 129.229 154.669 143.103 1.00 23.39 ? 450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 128.187 153.334 140.286 1.00 15.61 ? 450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 130.568 153.009 142.393 1.00 20.96 ? 451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 131.012 152.687 143.747 1.00 18.19 ? 451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 131.776 153.859 144.347 1.00 17.76 ? 451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 131.541 154.255 145.493 1.00 20.30 ? 451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.861 151.402 143.742 1.00 24.52 ? 451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 132.603 151.250 145.058 1.00 21.03 ? 451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.985 150.192 143.476 1.00 15.83 ? 451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 132.706 154.432 143.582 1.00 23.95 ? 452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 133.481 155.562 144.084 1.00 21.77 ? 452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 132.586 156.762 144.366 1.00 21.03 ? 452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 132.712 157.413 145.412 1.00 31.17 ? 452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 134.576 155.921 143.080 1.00 18.84 ? 452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 135.132 157.323 143.223 1.00 27.98 ? 452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 135.907 157.727 141.983 1.00 29.08 ? 452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 137.314 157.359 142.068 1.00 35.21 ? 452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 138.167 157.416 141.054 1.00 37.50 ? 452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 137.789 157.830 139.855 1.00 33.79 ? 452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 139.430 157.049 141.247 1.00 37.02 ? 452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 131.662 157.059 143.450 1.00 18.02 ? 453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 130.766 158.192 143.641 1.00 19.82 ? 453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 129.879 157.995 144.863 1.00 25.39 ? 453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 129.674 158.929 145.645 1.00 31.17 ? 453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 129.915 158.404 142.389 1.00 23.22 ? 453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 129.038 159.637 142.449 1.00 27.77 ? 453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.741 159.445 141.691 1.00 21.77 ? 453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 126.776 160.486 142.024 1.00 26.82 ? 453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 125.490 160.448 141.705 1.00 27.02 ? 453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 124.974 159.431 141.035 1.00 26.72 ? 453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 124.702 161.455 142.069 1.00 28.04 ? 453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 129.346 156.785 145.048 1.00 27.72 ? 454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 128.477 156.526 146.188 1.00 14.33 ? 454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 129.256 156.550 147.494 1.00 18.86 ? 454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.740 157.000 148.519 1.00 28.10 ? 454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 127.763 155.189 146.011 1.00 18.22 ? 454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 130.498 156.065 147.484 1.00 17.98 ? 455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 131.320 156.154 148.684 1.00 15.20 ? 455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 131.587 157.606 149.051 1.00 23.03 ? 455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 131.560 157.973 150.231 1.00 32.89 ? 455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 132.631 155.396 148.481 1.00 20.30 ? 455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 133.590 155.574 149.638 1.00 25.78 ? 455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 133.320 155.138 150.755 1.00 31.11 ? 455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 134.717 156.223 149.378 1.00 27.15 ? 455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.849 158.449 148.051 1.00 24.15 ? 456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 132.102 159.857 148.330 1.00 22.80 ? 456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.838 160.590 148.770 1.00 24.96 ? 456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.912 161.498 149.606 1.00 31.43 ? 456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 132.711 160.528 147.099 1.00 24.57 ? 456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.804 162.039 147.190 1.00 27.03 ? 456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.935 162.660 145.809 1.00 31.73 ? 456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 132.088 161.924 144.776 1.00 34.13 ? 456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 130.645 161.872 145.144 1.00 28.46 ? 456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 129.677 160.215 148.233 1.00 23.93 ? 457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 128.442 160.952 148.479 1.00 19.98 ? 457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.713 160.498 149.742 1.00 26.52 ? 457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 127.246 161.333 150.522 1.00 30.93 ? 457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 127.513 160.825 147.267 1.00 21.07 ? 457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 127.600 159.188 149.956 1.00 25.53 ? 458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 126.797 158.657 151.051 1.00 19.36 ? 458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 127.603 158.410 152.317 1.00 24.85 ? 458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 127.039 158.460 153.415 1.00 28.07 ? 458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 126.114 157.354 150.624 1.00 22.28 ? 458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 125.491 157.396 149.239 1.00 18.67 ? 458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 123.775 157.948 149.259 1.00 37.41 ? 458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.997 156.638 150.201 1.00 23.56 ? 458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 128.904 158.149 152.194 1.00 21.35 ? 459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 129.762 157.930 153.358 1.00 22.35 ? 459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 129.206 156.820 154.244 1.00 21.24 ? 459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 129.083 156.966 155.462 1.00 30.68 ? 459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.941 159.222 154.152 1.00 21.89 ? 459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.958 160.470 153.292 1.00 25.61 ? 459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 129.843 161.725 154.132 1.00 28.28 ? 459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 130.049 162.963 153.283 1.00 29.22 ? 459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 131.158 162.776 152.308 1.00 29.30 ? 459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 128.862 155.696 153.624 1.00 20.43 ? 460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 128.231 154.599 154.340 1.00 15.23 ? 460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 129.274 153.734 155.035 1.00 24.20 ? 460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 130.314 153.401 154.461 1.00 29.27 ? 460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 127.402 153.747 153.381 1.00 14.47 ? 460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.123 154.319 153.178 1.00 32.84 ? 460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.985 153.374 156.284 1.00 18.20 ? 461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 129.836 152.494 157.069 1.00 18.97 ? 461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.965 151.404 157.672 1.00 18.31 ? 461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 127.754 151.563 157.835 1.00 21.72 ? 461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 130.597 153.247 158.183 1.00 16.04 ? 461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 129.608 153.908 159.146 1.00 12.65 ? 461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 131.535 154.279 157.580 1.00 15.38 ? 461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 130.242 154.452 160.400 1.00 11.35 ? 461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 129.594 150.280 157.991 1.00 13.17 ? 462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.893 149.236 158.707 1.00 6.67  ? 462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 129.573 148.878 160.009 1.00 9.90  ? 462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 130.652 148.281 160.010 1.00 23.48 ? 462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.943 149.223 161.125 1.00 8.79  ? 463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 129.454 148.891 162.448 1.00 8.52  ? 463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 128.664 147.698 162.969 1.00 15.81 ? 463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 127.490 147.830 163.326 1.00 25.08 ? 463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 129.349 150.084 163.394 1.00 16.15 ? 463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.809 149.826 164.830 1.00 12.91 ? 463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 131.198 149.210 164.839 1.00 2.01  ? 463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 129.783 151.108 165.643 1.00 17.29 ? 463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 129.310 146.534 163.008 1.00 10.55 ? 464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 128.681 145.316 163.461 1.00 9.06  ? 464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 129.014 144.993 164.904 1.00 10.00 ? 464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 129.690 145.743 165.610 1.00 18.09 ? 464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 128.521 143.840 165.343 1.00 13.87 ? 465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.773 143.346 166.685 1.00 7.97  ? 465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.984 141.842 166.627 1.00 12.94 ? 465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 128.477 141.162 165.733 1.00 25.28 ? 465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 127.626 143.687 167.641 1.00 14.86 ? 465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.744 141.331 167.590 1.00 18.95 ? 466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 130.003 139.906 167.700 1.00 18.06 ? 466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 130.055 139.528 169.172 1.00 14.24 ? 466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 130.117 140.387 170.055 1.00 20.30 ? 466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 131.303 139.510 166.989 1.00 19.86 ? 466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 132.566 140.007 167.671 1.00 23.32 ? 466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.992 140.014 166.572 1.00 37.88 ? 466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.897 141.420 167.210 1.00 28.84 ? 466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 130.022 138.222 169.432 1.00 17.11 ? 467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 130.105 137.683 170.785 1.00 17.90 ? 467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 128.825 137.920 171.581 1.00 21.64 ? 467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 128.865 138.043 172.806 1.00 26.22 ? 467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 131.306 138.262 171.539 1.00 21.91 ? 467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 132.044 137.218 172.347 1.00 23.82 ? 467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 131.837 136.019 172.172 1.00 27.00 ? 467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 132.918 137.670 173.236 1.00 21.84 ? 467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 127.681 137.995 170.901 1.00 17.03 ? 468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.414 138.109 171.615 1.00 15.95 ? 468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 126.099 136.824 172.370 1.00 23.12 ? 468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 125.829 136.849 173.577 1.00 23.55 ? 468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 125.290 138.452 170.638 1.00 22.00 ? 468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 123.864 138.369 171.188 1.00 16.70 ? 468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 123.684 139.317 172.362 1.00 14.92 ? 468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 122.844 138.654 170.100 1.00 14.32 ? 468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 126.149 135.685 171.676 1.00 22.46 ? 469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.922 134.410 172.344 1.00 16.17 ? 469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 127.016 134.122 173.359 1.00 24.07 ? 469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.739 133.613 174.448 1.00 35.85 ? 469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.833 133.276 171.327 1.00 20.11 ? 469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 125.268 132.010 171.892 1.00 25.67 ? 469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.228 130.829 171.184 1.00 29.59 ? 469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.721 131.741 173.101 1.00 25.29 ? 469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.682 129.888 171.931 1.00 25.47 ? 469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.365 130.415 173.100 1.00 25.34 ? 469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.268 134.428 173.019 1.00 25.67 ? 470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.342 134.232 173.977 1.00 21.66 ? 470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 129.140 135.051 175.235 1.00 19.03 ? 470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 129.236 134.536 176.352 1.00 30.54 ? 470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 128.829 136.338 175.069 1.00 22.10 ? 471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 128.631 137.200 176.228 1.00 24.98 ? 471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 127.446 136.734 177.063 1.00 23.95 ? 471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 127.505 136.747 178.298 1.00 28.10 ? 471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 128.430 138.649 175.784 1.00 24.16 ? 471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 127.968 139.553 176.903 1.00 23.97 ? 471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.862 140.011 177.860 1.00 24.42 ? 471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 126.637 139.926 177.019 1.00 20.01 ? 471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 128.448 140.827 178.889 1.00 23.07 ? 471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 126.214 140.738 178.048 1.00 20.19 ? 471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 127.124 141.187 178.979 1.00 24.85 ? 471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 126.708 142.000 180.005 1.00 34.60 ? 471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 126.356 136.328 176.409 1.00 26.58 ? 472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 125.180 135.885 177.150 1.00 27.71 ? 472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 125.449 134.582 177.895 1.00 26.91 ? 472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 125.078 134.444 179.066 1.00 33.10 ? 472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 123.990 135.728 176.204 1.00 29.46 ? 472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 123.446 137.012 175.573 1.00 28.19 ? 472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.460 136.686 174.464 1.00 26.17 ? 472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 122.802 137.904 176.623 1.00 21.83 ? 472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 126.089 133.615 177.234 1.00 27.82 ? 473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.376 132.336 177.874 1.00 24.62 ? 473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 127.342 132.502 179.038 1.00 30.11 ? 473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 127.179 131.859 180.081 1.00 37.40 ? 473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.931 131.351 176.847 1.00 25.88 ? 473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 128.356 133.355 178.883 1.00 30.67 ? 474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 129.287 133.599 179.977 1.00 29.65 ? 474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.654 134.378 181.120 1.00 31.10 ? 474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 129.275 134.502 182.180 1.00 36.95 ? 474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 130.524 134.337 179.463 1.00 28.86 ? 474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 131.113 133.736 178.201 1.00 32.52 ? 474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 132.613 133.906 178.113 1.00 35.60 ? 474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.294 134.050 179.127 1.00 41.40 ? 474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 133.137 133.892 176.894 1.00 36.26 ? 474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 127.445 134.903 180.934 1.00 29.95 ? 475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 126.721 135.603 181.986 1.00 31.17 ? 475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 125.498 134.830 182.462 1.00 31.20 ? 475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 124.643 135.401 183.146 1.00 32.29 ? 475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 126.314 136.997 181.509 1.00 32.60 ? 475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 127.467 137.977 181.531 1.00 28.65 ? 475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 127.715 138.640 182.537 1.00 35.73 ? 475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 128.186 138.067 180.421 1.00 26.39 ? 475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 125.395 133.550 182.119 1.00 32.89 ? 476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 124.285 132.729 182.569 1.00 33.00 ? 476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.936 133.121 182.009 1.00 35.02 ? 476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.931 133.068 182.730 1.00 40.12 ? 476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.884 133.512 180.738 1.00 28.29 ? 477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.647 133.912 180.080 1.00 31.19 ? 477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.451 133.037 178.852 1.00 35.05 ? 477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 122.366 132.895 178.032 1.00 38.62 ? 477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 121.662 135.401 179.693 1.00 29.43 ? 477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.806 136.276 180.939 1.00 32.14 ? 477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 120.400 135.764 178.931 1.00 28.25 ? 477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 122.236 137.693 180.641 1.00 34.18 ? 477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 120.265 132.448 178.731 1.00 31.43 ? 478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.953 131.630 177.568 1.00 28.17 ? 478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.716 132.509 176.348 1.00 30.07 ? 478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 119.057 133.549 176.429 1.00 34.68 ? 478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.726 130.762 177.840 1.00 31.53 ? 478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.261 132.082 175.208 1.00 28.16 ? 479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 120.119 132.863 173.984 1.00 21.99 ? 479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.652 133.078 173.632 1.00 28.70 ? 479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 118.272 134.151 173.149 1.00 35.70 ? 479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.853 132.174 172.834 1.00 21.99 ? 479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.948 133.005 171.576 1.00 27.97 ? 479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.928 132.998 170.635 1.00 27.56 ? 479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 122.062 133.796 171.328 1.00 25.04 ? 479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 120.012 133.757 169.486 1.00 27.63 ? 479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 122.156 134.557 170.182 1.00 23.31 ? 479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 121.129 134.534 169.264 1.00 30.75 ? 479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 121.219 135.291 168.120 1.00 31.97 ? 479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.813 132.072 173.867 1.00 32.01 ? 480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.397 132.141 173.533 1.00 33.40 ? 480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.548 132.752 174.639 1.00 35.70 ? 480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.329 132.862 174.474 1.00 38.45 ? 480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.865 130.745 173.201 1.00 33.39 ? 480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.508 130.099 171.988 1.00 33.82 ? 480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.518 128.588 172.082 1.00 41.67 ? 480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 117.458 128.035 172.690 1.00 42.71 ? 480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 115.583 127.951 171.553 1.00 40.94 ? 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 116.149 133.146 175.752 1.00 33.91 ? 481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.379 133.669 176.867 1.00 30.22 ? 481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.926 135.103 176.598 1.00 33.51 ? 481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 115.552 135.826 175.819 1.00 35.88 ? 481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 116.203 133.623 178.148 1.00 30.82 ? 481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.900 134.838 178.350 1.00 37.89 ? 481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.827 135.531 177.223 1.00 37.40 ? 482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.437 136.945 177.117 1.00 32.29 ? 482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 114.480 137.891 177.681 1.00 32.66 ? 482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.566 139.041 177.233 1.00 37.68 ? 482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 112.125 137.007 177.912 1.00 33.04 ? 482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 111.624 135.606 177.936 1.00 33.92 ? 482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.844 134.742 177.982 1.00 36.39 ? 482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 115.273 137.444 178.657 1.00 35.55 ? 483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 116.328 138.291 179.205 1.00 31.13 ? 483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 117.404 138.575 178.164 1.00 31.58 ? 483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 117.936 139.689 178.101 1.00 36.22 ? 483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 116.934 137.636 180.445 1.00 32.09 ? 483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.989 137.568 181.633 1.00 38.17 ? 483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 115.023 136.400 181.546 1.00 42.81 ? 483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 114.816 135.879 180.431 1.00 42.10 ? 483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.469 136.004 182.592 1.00 39.91 ? 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 117.745 137.577 177.347 1.00 26.67 ? 484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 118.713 137.801 176.280 1.00 28.69 ? 484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 118.201 138.835 175.286 1.00 28.99 ? 484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 118.954 139.711 174.844 1.00 28.87 ? 484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 119.030 136.485 175.574 1.00 25.26 ? 484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 116.921 138.749 174.922 1.00 32.02 ? 485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 116.348 139.737 174.016 1.00 25.69 ? 485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 116.307 141.117 174.659 1.00 24.10 ? 485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 116.515 142.126 173.980 1.00 29.83 ? 485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 114.952 139.300 173.576 1.00 27.04 ? 485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 114.961 138.208 172.523 1.00 22.16 ? 485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.572 137.963 171.966 1.00 26.40 ? 485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 112.642 137.511 172.993 1.00 31.54 ? 485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.541 136.257 173.412 1.00 30.91 ? 485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 113.303 135.299 172.913 1.00 29.90 ? 485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 111.651 135.958 174.352 1.00 30.42 ? 485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 116.039 141.183 175.963 1.00 27.54 ? 486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 116.061 142.465 176.660 1.00 28.12 ? 486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 117.452 143.085 176.618 1.00 30.60 ? 486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 117.611 144.283 176.338 1.00 34.22 ? 486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.595 142.276 178.104 1.00 31.64 ? 486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 115.329 143.587 178.808 1.00 40.39 ? 486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.458 144.348 178.338 1.00 41.83 ? 486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 115.988 143.856 179.833 1.00 40.69 ? 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 118.478 142.275 176.887 1.00 27.28 ? 487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 119.841 142.787 176.815 1.00 24.33 ? 487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 120.182 143.241 175.406 1.00 25.48 ? 487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.814 144.284 175.223 1.00 30.45 ? 487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 120.854 141.741 177.270 1.00 29.11 ? 487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 122.241 142.011 176.762 1.00 29.48 ? 487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 123.062 142.922 177.406 1.00 26.23 ? 487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 122.710 141.388 175.618 1.00 23.81 ? 487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 124.329 143.189 176.929 1.00 27.58 ? 487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 123.976 141.654 175.137 1.00 23.27 ? 487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.786 142.555 175.794 1.00 27.42 ? 487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.810 142.451 174.397 1.00 24.59 ? 488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 120.112 142.839 173.025 1.00 17.74 ? 488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 119.424 144.148 172.672 1.00 23.48 ? 488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 120.030 145.035 172.061 1.00 31.84 ? 488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.695 141.731 172.059 1.00 21.84 ? 488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 118.160 144.292 173.071 1.00 22.02 ? 489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 117.438 145.535 172.846 1.00 23.04 ? 489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 118.188 146.716 173.446 1.00 23.63 ? 489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 118.472 147.700 172.756 1.00 28.23 ? 489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 116.033 145.425 173.439 1.00 24.09 ? 489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 115.134 146.569 173.032 1.00 29.67 ? 489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 115.047 146.919 171.856 1.00 35.37 ? 489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 114.455 147.158 174.006 1.00 31.41 ? 489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 118.543 146.623 174.729 1.00 19.49 ? 490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 119.200 147.750 175.387 1.00 22.26 ? 490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 120.560 148.042 174.761 1.00 21.80 ? 490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.891 149.199 174.468 1.00 22.37 ? 490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 119.346 147.474 176.884 1.00 31.63 ? 490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 118.066 147.143 177.436 1.00 36.88 ? 490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 119.899 148.695 177.600 1.00 24.29 ? 490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 121.360 146.997 174.539 1.00 20.04 ? 491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 122.715 147.182 174.037 1.00 18.35 ? 491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 122.708 147.796 172.646 1.00 20.84 ? 491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 123.472 148.724 172.360 1.00 21.23 ? 491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 123.453 145.843 174.030 1.00 22.35 ? 491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.844 145.917 173.468 1.00 18.15 ? 491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.069 145.751 172.112 1.00 15.74 ? 491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 125.928 146.145 174.297 1.00 17.90 ? 491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.344 145.821 171.595 1.00 18.09 ? 491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 127.206 146.213 173.783 1.00 15.78 ? 491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 127.415 146.052 172.432 1.00 20.51 ? 491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.850 147.293 171.758 1.00 20.20 ? 492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.850 147.811 170.400 1.00 11.01 ? 492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 121.142 149.153 170.301 1.00 13.80 ? 492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 121.490 149.959 169.435 1.00 23.62 ? 492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 121.247 146.779 169.451 1.00 14.78 ? 492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 122.169 145.630 169.172 1.00 18.57 ? 492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 123.223 145.772 168.285 1.00 16.18 ? 492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 122.004 144.417 169.818 1.00 14.80 ? 492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 124.081 144.722 168.034 1.00 12.60 ? 492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.859 143.365 169.574 1.00 14.11 ? 492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.899 143.516 168.679 1.00 13.84 ? 492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 120.192 149.443 171.194 1.00 13.16 ? 493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 119.690 150.807 171.288 1.00 15.58 ? 493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 120.808 151.768 171.663 1.00 17.23 ? 493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.933 152.846 171.074 1.00 24.60 ? 493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 118.559 150.890 172.310 1.00 17.88 ? 493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.907 152.257 172.384 1.00 19.02 ? 493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 118.554 153.259 173.736 1.00 37.09 ? 493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 118.553 152.072 175.073 1.00 26.08 ? 493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 121.634 151.392 172.643 1.00 16.96 ? 494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 122.754 152.247 173.024 1.00 17.12 ? 494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 123.745 152.399 171.877 1.00 21.67 ? 494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 124.264 153.496 171.631 1.00 26.32 ? 494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 123.450 151.678 174.259 1.00 17.99 ? 494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 122.634 151.772 175.534 1.00 22.17 ? 494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 123.567 151.255 176.984 1.00 40.07 ? 494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 125.015 152.296 176.840 1.00 26.77 ? 494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 124.025 151.304 171.170 1.00 17.30 ? 495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.958 151.355 170.048 1.00 10.11 ? 495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 124.438 152.296 168.971 1.00 19.83 ? 495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 125.182 153.125 168.436 1.00 27.47 ? 495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 125.204 149.943 169.489 1.00 17.76 ? 495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.948 150.021 168.165 1.00 9.69  ? 495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.972 149.101 170.492 1.00 14.71 ? 495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 123.152 152.179 168.635 1.00 19.62 ? 496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 122.559 153.063 167.639 1.00 14.17 ? 496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 122.592 154.512 168.101 1.00 16.20 ? 496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.908 155.415 167.318 1.00 21.58 ? 496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 121.124 152.624 167.348 1.00 14.61 ? 496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 120.557 153.273 166.107 1.00 15.84 ? 496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 121.258 153.459 165.116 1.00 19.80 ? 496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 119.279 153.621 166.155 1.00 18.30 ? 496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 122.268 154.755 169.372 1.00 17.62 ? 497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 122.285 156.113 169.899 1.00 14.40 ? 497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 123.666 156.733 169.760 1.00 20.22 ? 497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.810 157.860 169.273 1.00 22.36 ? 497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.839 156.103 171.362 1.00 18.20 ? 497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.913 157.444 172.034 1.00 24.43 ? 497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 120.831 158.307 172.009 1.00 23.90 ? 497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 123.060 157.835 172.705 1.00 21.05 ? 497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 120.896 159.537 172.630 1.00 19.70 ? 497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 123.130 159.065 173.325 1.00 20.99 ? 497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 122.046 159.916 173.288 1.00 19.80 ? 497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 124.701 155.998 170.162 1.00 28.07 ? 498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 126.042 156.566 170.137 1.00 21.75 ? 498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 126.606 156.652 168.726 1.00 23.40 ? 498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 127.368 157.576 168.433 1.00 29.16 ? 498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.965 155.766 171.056 1.00 17.94 ? 498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 126.667 156.023 172.512 1.00 24.35 ? 498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 126.820 157.292 173.053 1.00 22.55 ? 498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 126.203 155.011 173.339 1.00 27.23 ? 498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 126.540 157.541 174.378 1.00 24.84 ? 498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.917 155.251 174.667 1.00 23.86 ? 498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 126.089 156.518 175.181 1.00 28.61 ? 498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 125.807 156.764 176.504 1.00 35.01 ? 498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 126.220 155.744 167.828 1.00 16.85 ? 499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 126.650 155.876 166.441 1.00 10.53 ? 499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.991 157.078 165.777 1.00 16.71 ? 499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 126.642 157.808 165.022 1.00 24.20 ? 499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 126.352 154.592 165.665 1.00 12.73 ? 499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.965 154.424 165.446 1.00 24.19 ? 499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 124.707 157.314 166.060 1.00 15.58 ? 500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 124.040 158.503 165.538 1.00 21.40 ? 500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 124.682 159.762 166.102 1.00 18.40 ? 500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 124.893 160.747 165.384 1.00 26.15 ? 500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 122.533 158.453 165.847 1.00 21.98 ? 500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.853 157.352 165.036 1.00 19.04 ? 500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 121.887 159.799 165.562 1.00 14.37 ? 500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 120.440 157.066 165.473 1.00 18.77 ? 500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.987 159.758 167.401 1.00 20.08 ? 501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 125.622 160.920 168.009 1.00 22.88 ? 501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.989 161.186 167.392 1.00 24.65 ? 501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 127.338 162.338 167.116 1.00 30.79 ? 501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 125.741 160.721 169.519 1.00 25.69 ? 501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 125.730 162.014 170.310 1.00 23.11 ? 501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 125.840 161.786 171.801 1.00 28.63 ? 501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 126.754 161.111 172.272 1.00 33.60 ? 501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 124.903 162.346 172.556 1.00 30.29 ? 501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 127.775 160.132 167.161 1.00 24.27 ? 502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 129.081 160.311 166.537 1.00 19.87 ? 502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 128.949 160.801 165.101 1.00 20.10 ? 502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 129.747 161.628 164.650 1.00 26.81 ? 502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.876 159.008 166.587 1.00 21.06 ? 502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 131.349 159.189 166.272 1.00 20.31 ? 502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.944 160.337 167.066 1.00 22.83 ? 502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 133.271 160.699 166.586 1.00 27.20 ? 502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 133.709 161.944 166.463 1.00 26.41 ? 502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 132.953 162.979 166.788 1.00 26.45 ? 502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 134.939 162.156 166.003 1.00 27.21 ? 502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.962 160.293 164.361 1.00 17.99 ? 503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 127.750 160.769 162.998 1.00 20.29 ? 503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 127.385 162.248 162.987 1.00 22.62 ? 503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 127.895 163.017 162.164 1.00 26.70 ? 503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 126.663 159.936 162.320 1.00 18.12 ? 503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 126.603 160.203 160.932 1.00 20.14 ? 503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 126.511 162.667 163.904 1.00 25.26 ? 504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 126.158 164.080 163.998 1.00 24.91 ? 504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 127.362 164.925 164.397 1.00 28.92 ? 504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 127.554 166.030 163.878 1.00 34.95 ? 504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 125.012 164.268 164.991 1.00 27.76 ? 504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 128.183 164.425 165.322 1.00 27.15 ? 505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 129.374 165.160 165.730 1.00 27.66 ? 505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 130.356 165.302 164.575 1.00 28.31 ? 505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 130.973 166.357 164.403 1.00 33.46 ? 505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 130.040 164.464 166.916 1.00 26.68 ? 505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 129.252 164.543 168.210 1.00 26.34 ? 505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 129.723 163.535 169.238 1.00 36.22 ? 505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 130.644 162.752 168.926 1.00 38.16 ? 505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 129.176 163.526 170.360 1.00 35.37 ? 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 130.521 164.245 163.779 1.00 27.77 ? 506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 131.399 164.317 162.617 1.00 24.77 ? 506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 130.850 165.305 161.597 1.00 27.53 ? 506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 131.602 166.076 160.992 1.00 33.89 ? 506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 131.592 162.919 162.003 1.00 26.78 ? 506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 132.300 161.995 162.994 1.00 25.97 ? 506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 132.370 163.010 160.700 1.00 22.78 ? 506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 132.239 160.534 162.614 1.00 22.06 ? 506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 129.532 165.298 161.388 1.00 28.01 ? 507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 128.931 166.249 160.460 1.00 27.59 ? 507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 129.148 167.682 160.929 1.00 30.50 ? 507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 129.426 168.574 160.120 1.00 35.15 ? 507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 127.441 165.953 160.296 1.00 24.03 ? 507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 129.019 167.921 162.235 1.00 32.99 ? 508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 129.257 169.257 162.772 1.00 32.99 ? 508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 130.723 169.657 162.640 1.00 38.20 ? 508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 131.030 170.794 162.264 1.00 41.38 ? 508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 128.813 169.318 164.233 1.00 37.16 ? 508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 129.062 170.656 164.906 1.00 36.90 ? 508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 128.774 170.583 166.395 1.00 36.48 ? 508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 128.914 171.944 167.054 1.00 38.41 ? 508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 128.002 172.096 168.220 1.00 41.12 ? 508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 131.641 168.738 162.948 1.00 36.41 ? 509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 133.064 169.053 162.870 1.00 35.24 ? 509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 133.483 169.358 161.439 1.00 39.96 ? 509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 134.215 170.322 161.189 1.00 46.39 ? 509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 133.889 167.895 163.430 1.00 36.97 ? 509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 133.767 167.703 164.930 1.00 42.20 ? 509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 134.184 166.314 165.373 1.00 45.11 ? 509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 134.814 165.597 164.567 1.00 40.82 ? 509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 133.884 165.941 166.526 1.00 45.03 ? 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 133.031 168.546 160.487 1.00 36.39 ? 510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 133.358 168.742 159.084 1.00 30.78 ? 510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 132.399 169.688 158.379 1.00 35.81 ? 510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 132.659 170.064 157.231 1.00 40.55 ? 510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 133.373 167.395 158.355 1.00 31.36 ? 510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 134.293 166.370 158.986 1.00 30.66 ? 510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 134.442 165.144 158.107 1.00 34.56 ? 510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 135.460 164.179 158.689 1.00 36.99 ? 510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 136.154 163.394 157.635 1.00 36.65 ? 510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 131.309 170.079 159.029 1.00 37.01 ? 511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 130.346 170.963 158.395 1.00 31.61 ? 511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 129.790 170.406 157.105 1.00 39.14 ? 511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 129.623 171.148 156.129 1.00 42.68 ? 511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 129.502 169.108 157.075 1.00 34.42 ? 512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 128.999 168.474 155.867 1.00 32.01 ? 512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 128.293 167.180 156.238 1.00 30.67 ? 512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 128.799 166.400 157.048 1.00 34.30 ? 512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 130.131 168.206 154.868 1.00 32.78 ? 512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.685 166.794 154.911 1.00 33.98 ? 512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 131.932 166.634 154.067 1.00 41.23 ? 512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 132.909 167.376 154.301 1.00 36.93 ? 512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 131.937 165.765 153.169 1.00 40.07 ? 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 127.123 166.971 155.650 1.00 31.80 ? 513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 126.341 165.755 155.800 1.00 25.56 ? 513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 126.517 164.886 154.560 1.00 25.94 ? 513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 127.329 165.176 153.677 1.00 33.67 ? 513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 124.867 166.088 156.035 1.00 26.31 ? 513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 124.382 166.898 154.958 1.00 31.98 ? 513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 124.693 166.839 157.344 1.00 24.74 ? 513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 125.748 163.805 154.496 1.00 20.95 ? 514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.790 162.961 153.316 1.00 20.76 ? 514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.809 163.473 152.266 1.00 22.22 ? 514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.843 164.179 152.567 1.00 28.30 ? 514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 125.490 161.504 153.676 1.00 19.94 ? 514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 124.097 161.269 154.183 1.00 17.63 ? 514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 123.072 160.941 153.312 1.00 19.14 ? 514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 123.815 161.353 155.535 1.00 18.27 ? 514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.793 160.715 153.778 1.00 17.45 ? 514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 122.539 161.126 156.006 1.00 17.57 ? 514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 121.528 160.807 155.126 1.00 16.43 ? 514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 125.079 163.114 151.014 1.00 23.74 ? 515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 124.287 163.623 149.903 1.00 25.34 ? 515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.815 163.281 150.086 1.00 29.27 ? 515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 122.457 162.126 150.332 1.00 35.69 ? 515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.804 163.051 148.585 1.00 30.93 ? 515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.845 163.939 147.936 1.00 34.35 ? 515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 126.654 164.543 148.670 1.00 32.53 ? 515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.852 164.034 146.691 1.00 36.50 ? 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.961 164.295 149.953 1.00 29.97 ? 516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 120.518 164.142 150.096 1.00 28.79 ? 516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 120.118 163.783 151.523 1.00 25.94 ? 516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 119.150 163.052 151.739 1.00 33.29 ? 516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.969 163.106 149.112 1.00 24.51 ? 516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 120.186 163.470 147.653 1.00 25.76 ? 516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.701 162.394 146.706 1.00 31.96 ? 516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.502 162.260 146.465 1.00 34.39 ? 516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.631 161.619 146.161 1.00 30.64 ? 516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.859 164.292 152.508 1.00 24.99 ? 517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 120.485 164.069 153.900 1.00 23.11 ? 517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 119.184 164.783 154.243 1.00 29.20 ? 517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 118.387 164.280 155.043 1.00 34.83 ? 517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 121.603 164.534 154.833 1.00 21.35 ? 517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 121.099 164.909 156.206 1.00 27.43 ? 517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 120.887 163.940 157.177 1.00 20.15 ? 517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 120.816 166.231 156.526 1.00 30.35 ? 517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 120.418 164.277 158.427 1.00 23.61 ? 517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 120.346 166.576 157.774 1.00 22.65 ? 517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 120.147 165.595 158.720 1.00 25.88 ? 517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 119.679 165.935 159.967 1.00 37.57 ? 517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 118.955 165.958 153.652 1.00 30.47 ? 518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 117.803 166.770 154.030 1.00 28.56 ? 518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 116.492 166.028 153.815 1.00 34.91 ? 518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 115.519 166.268 154.539 1.00 38.31 ? 518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 117.808 168.081 153.244 1.00 29.56 ? 518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.944 169.022 153.609 1.00 36.20 ? 518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 120.269 168.611 152.994 1.00 42.46 ? 518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 120.275 167.689 152.152 1.00 38.18 ? 518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 121.304 169.210 153.354 1.00 41.86 ? 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 116.440 165.135 152.833 1.00 26.37 ? 519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 115.256 164.345 152.583 1.00 21.66 ? 519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 115.134 163.081 153.398 1.00 19.89 ? 519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 114.118 162.389 153.299 1.00 27.64 ? 519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 116.135 162.758 154.211 1.00 19.98 ? 520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 116.132 161.524 154.978 1.00 23.41 ? 520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 115.227 161.645 156.200 1.00 24.67 ? 520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 114.817 162.737 156.601 1.00 24.89 ? 520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 117.553 161.160 155.410 1.00 19.58 ? 520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 118.080 162.128 156.298 1.00 20.83 ? 520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 114.909 160.491 156.790 1.00 21.34 ? 521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 114.107 160.475 158.007 1.00 22.05 ? 521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 114.853 161.066 159.195 1.00 26.63 ? 521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 114.213 161.514 160.151 1.00 28.63 ? 521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 113.660 159.048 158.326 1.00 24.85 ? 521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 114.808 158.199 158.437 1.00 29.00 ? 521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.749 158.521 157.231 1.00 18.47 ? 521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 116.188 161.068 159.163 1.00 28.02 ? 522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 116.945 161.774 160.190 1.00 20.40 ? 522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 116.667 163.270 160.141 1.00 27.20 ? 522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 116.478 163.910 161.182 1.00 27.72 ? 522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 118.442 161.513 160.020 1.00 16.19 ? 522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 118.834 160.055 160.006 1.00 17.59 ? 522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 118.833 159.305 161.173 1.00 24.12 ? 522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 119.222 159.434 158.828 1.00 19.66 ? 522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 119.201 157.976 161.165 1.00 20.26 ? 522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 119.587 158.107 158.810 1.00 20.09 ? 522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 119.575 157.382 159.981 1.00 21.38 ? 522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.939 156.059 159.962 1.00 28.32 ? 522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 116.639 163.845 158.937 1.00 28.62 ? 523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 116.430 165.282 158.803 1.00 26.64 ? 523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 115.031 165.683 159.247 1.00 29.69 ? 523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 114.859 166.690 159.943 1.00 34.53 ? 523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 116.680 165.713 157.359 1.00 23.24 ? 523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 114.019 164.909 158.857 1.00 30.33 ? 524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 112.643 165.215 159.220 1.00 28.21 ? 524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 112.296 164.796 160.641 1.00 33.32 ? 524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 111.249 165.210 161.151 1.00 41.68 ? 524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 111.677 164.542 158.241 1.00 31.39 ? 524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 111.559 163.151 158.560 1.00 33.45 ? 524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 112.185 164.687 156.816 1.00 31.26 ? 524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 113.139 163.995 161.288 1.00 25.82 ? 525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 112.890 163.548 162.640 1.00 23.97 ? 525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 112.027 162.313 162.762 1.00 31.06 ? 525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 111.854 161.808 163.878 1.00 33.46 ? 525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 111.481 161.807 161.656 1.00 34.44 ? 526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 110.661 160.604 161.710 1.00 32.81 ? 526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 111.456 159.386 162.161 1.00 33.62 ? 526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 110.860 158.412 162.633 1.00 38.82 ? 526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 110.028 160.345 160.342 1.00 31.26 ? 526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 109.317 159.010 160.221 1.00 34.63 ? 526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 109.257 158.510 158.791 1.00 40.41 ? 526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 109.195 159.349 157.868 1.00 40.78 ? 526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 109.274 157.278 158.588 1.00 38.91 ? 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 112.783 159.420 162.027 1.00 30.89 ? 527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 113.602 158.293 162.457 1.00 25.77 ? 527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 113.510 158.081 163.963 1.00 25.82 ? 527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 113.478 156.939 164.436 1.00 34.11 ? 527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 115.055 158.516 162.036 1.00 21.19 ? 527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.988 157.397 162.430 1.00 24.55 ? 527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 116.660 157.424 163.644 1.00 26.74 ? 527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 116.197 156.313 161.589 1.00 22.26 ? 527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 117.512 156.405 164.010 1.00 21.36 ? 527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 117.047 155.290 161.948 1.00 22.47 ? 527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 117.702 155.341 163.158 1.00 21.56 ? 527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 118.551 154.322 163.519 1.00 30.62 ? 527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 113.463 159.166 164.729 1.00 27.85 ? 528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 113.557 159.114 166.181 1.00 24.84 ? 528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 112.209 158.922 166.863 1.00 32.72 ? 528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 112.141 158.995 168.093 1.00 39.46 ? 528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 114.218 160.390 166.707 1.00 27.02 ? 528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 115.577 160.652 166.130 1.00 29.85 ? 528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 115.718 161.365 164.952 1.00 25.93 ? 528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 116.716 160.194 166.769 1.00 28.56 ? 528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 116.968 161.609 164.421 1.00 31.23 ? 528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 117.968 160.437 166.243 1.00 25.26 ? 528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 118.094 161.144 165.067 1.00 31.64 ? 528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 111.140 158.685 166.101 1.00 35.68 ? 529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.808 158.607 166.695 1.00 32.02 ? 529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 109.742 157.531 167.773 1.00 35.56 ? 529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 109.317 157.794 168.905 1.00 40.17 ? 529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 108.768 158.344 165.606 1.00 31.36 ? 529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 108.406 159.595 164.833 1.00 39.26 ? 529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.782 160.698 165.279 1.00 41.28 ? 529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.746 159.475 163.780 1.00 43.00 ? 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 110.168 156.310 167.442 1.00 36.05 ? 530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 110.090 155.219 168.407 1.00 35.90 ? 530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 111.052 155.423 169.568 1.00 34.72 ? 530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.786 154.959 170.681 1.00 35.86 ? 530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 110.366 153.884 167.717 1.00 37.23 ? 530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 111.834 153.499 167.658 1.00 32.20 ? 530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 112.039 152.277 166.781 1.00 33.95 ? 530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 113.461 151.764 166.871 1.00 28.68 ? 530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.950 151.279 165.554 1.00 39.97 ? 530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 112.170 156.109 169.333 1.00 34.71 ? 531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 113.136 156.334 170.400 1.00 27.57 ? 531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 112.672 157.426 171.355 1.00 30.02 ? 531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.929 157.349 172.561 1.00 35.02 ? 531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 114.497 156.679 169.803 1.00 24.68 ? 531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 115.201 155.493 169.193 1.00 26.42 ? 531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 115.520 154.383 169.962 1.00 22.60 ? 531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 115.542 155.478 167.848 1.00 22.88 ? 531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 116.164 153.297 169.413 1.00 28.30 ? 531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 116.186 154.395 167.290 1.00 21.17 ? 531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 116.495 153.307 168.077 1.00 27.96 ? 531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 117.136 152.224 167.527 1.00 33.71 ? 531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.991 158.448 170.835 1.00 35.80 ? 532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 111.469 159.503 171.694 1.00 35.17 ? 532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 110.162 159.103 172.363 1.00 36.03 ? 532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 109.802 159.681 173.395 1.00 41.18 ? 532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 111.271 160.807 170.904 1.00 36.50 ? 532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 112.608 161.344 170.421 1.00 32.12 ? 532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 110.329 160.580 169.735 1.00 33.58 ? 532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 109.441 158.127 171.809 1.00 40.40 ? 533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 108.174 157.697 172.383 1.00 39.17 ? 533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 108.283 156.434 173.226 1.00 42.01 ? 533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 107.391 156.179 174.043 1.00 47.43 ? 533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 107.141 157.466 171.273 1.00 43.03 ? 533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 107.368 156.233 170.614 1.00 45.93 ? 533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 109.339 155.645 173.056 1.00 40.08 ? 534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 109.483 154.369 173.739 1.00 38.23 ? 534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 110.780 154.341 174.536 1.00 40.92 ? 534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 111.744 155.040 174.213 1.00 46.26 ? 534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 109.463 153.200 172.745 1.00 40.66 ? 534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 108.346 153.341 171.859 1.00 43.43 ? 534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 109.355 151.873 173.480 1.00 38.02 ? 534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 110.791 153.522 175.584 1.00 40.17 ? 535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.959 153.327 176.429 1.00 35.63 ? 535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 112.568 151.961 176.148 1.00 38.73 ? 535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 111.847 150.976 175.959 1.00 43.90 ? 535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 111.594 153.444 177.910 1.00 37.79 ? 535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 112.764 153.143 178.824 1.00 44.82 ? 535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 113.702 153.966 178.882 1.00 43.22 ? 535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.746 152.083 179.484 1.00 46.02 ? 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 113.900 151.905 176.120 1.00 30.54 ? 536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 114.616 150.675 175.807 1.00 30.22 ? 536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 115.556 150.252 176.930 1.00 36.58 ? 536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 116.454 149.434 176.707 1.00 40.33 ? 536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 115.381 150.827 174.492 1.00 29.35 ? 536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 114.491 150.966 173.291 1.00 29.86 ? 536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 114.045 149.848 172.612 1.00 28.90 ? 536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 114.093 152.214 172.846 1.00 27.78 ? 536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 113.225 149.971 171.510 1.00 28.87 ? 536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 113.272 152.342 171.745 1.00 32.52 ? 536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 112.838 151.219 171.076 1.00 29.13 ? 536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 115.370 150.792 178.130 1.00 35.00 ? 537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 116.134 150.325 179.273 1.00 33.99 ? 537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 115.710 148.903 179.634 1.00 36.38 ? 537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 114.573 148.500 179.374 1.00 38.06 ? 537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 115.934 151.252 180.468 1.00 34.55 ? 537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 114.590 151.229 180.914 1.00 38.01 ? 537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 116.606 148.119 180.229 1.00 37.20 ? 538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 116.283 146.713 180.496 1.00 35.98 ? 538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 115.051 146.582 181.379 1.00 40.09 ? 538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 114.884 147.308 182.361 1.00 39.19 ? 538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 117.540 146.185 181.199 1.00 39.36 ? 538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 118.617 147.169 180.871 1.00 35.26 ? 538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 117.933 148.489 180.745 1.00 36.12 ? 538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 114.183 145.639 181.017 1.00 41.89 ? 539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.993 145.341 181.802 1.00 41.12 ? 539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 113.242 144.288 182.872 1.00 45.49 ? 539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 112.372 144.074 183.723 1.00 47.07 ? 539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.855 144.877 180.886 1.00 42.61 ? 539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.403 145.918 179.876 1.00 42.38 ? 539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 111.348 147.305 180.496 1.00 47.31 ? 539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 111.419 148.392 179.433 1.00 46.28 ? 539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 112.500 148.137 178.441 1.00 46.35 ? 539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 114.400 143.636 182.851 1.00 46.15 ? 540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 114.768 142.630 183.836 1.00 41.44 ? 540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 115.874 143.181 184.721 1.00 43.48 ? 540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 116.830 143.784 184.222 1.00 45.99 ? 540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 115.228 141.339 183.155 1.00 41.48 ? 540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 114.148 140.653 182.355 1.00 43.98 ? 540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.257 139.780 182.962 1.00 45.96 ? 540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 114.018 140.879 180.992 1.00 42.31 ? 540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.268 139.150 182.235 1.00 43.72 ? 540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 113.032 140.255 180.257 1.00 44.37 ? 540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 112.159 139.391 180.883 1.00 45.46 ? 540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 111.175 138.766 180.155 1.00 43.31 ? 540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 115.741 142.976 186.032 1.00 48.82 ? 541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 116.760 143.461 186.956 1.00 48.21 ? 541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 118.118 142.845 186.647 1.00 46.27 ? 541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 119.152 143.514 186.759 1.00 44.50 ? 541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 116.349 143.162 188.397 1.00 47.31 ? 541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 117.517 143.042 189.361 1.00 48.41 ? 541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 117.723 144.300 190.181 1.00 52.24 ? 541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.045 145.310 189.900 1.00 50.96 ? 541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 118.562 144.279 191.106 1.00 51.97 ? 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 118.136 141.569 186.257 1.00 45.82 ? 542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 119.399 140.917 185.930 1.00 45.19 ? 542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 120.086 141.602 184.755 1.00 46.86 ? 542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 121.298 141.843 184.790 1.00 45.85 ? 542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 119.160 139.438 185.629 1.00 43.78 ? 542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.349 138.729 185.005 1.00 45.43 ? 542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 120.087 137.240 184.863 1.00 43.49 ? 542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.280 136.525 184.252 1.00 44.77 ? 542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 122.543 136.838 184.975 1.00 44.10 ? 542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 119.329 141.922 183.703 1.00 40.46 ? 543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 119.909 142.623 182.562 1.00 38.64 ? 543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 120.284 144.048 182.946 1.00 39.44 ? 543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 121.341 144.555 182.550 1.00 39.86 ? 543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 118.942 142.595 181.364 1.00 41.51 ? 543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 118.543 141.156 181.030 1.00 40.39 ? 543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 119.574 143.267 180.154 1.00 37.78 ? 543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 119.714 140.211 180.903 1.00 36.40 ? 543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 119.428 144.718 183.722 1.00 42.33 ? 544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 119.730 146.080 184.149 1.00 41.15 ? 544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 121.025 146.142 184.946 1.00 44.37 ? 544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.750 147.141 184.874 1.00 48.94 ? 544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 118.570 146.642 184.971 1.00 42.19 ? 544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 121.332 145.093 185.712 1.00 44.48 ? 545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 122.591 145.060 186.446 1.00 46.86 ? 545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.784 144.951 185.506 1.00 46.16 ? 545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.851 145.503 185.795 1.00 45.80 ? 545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 122.591 143.899 187.440 1.00 46.95 ? 545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 121.624 144.114 188.586 1.00 48.81 ? 545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 121.150 145.228 188.813 1.00 47.23 ? 545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 121.326 143.047 189.316 1.00 47.44 ? 545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 123.626 144.243 184.385 1.00 44.26 ? 546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 124.721 144.113 183.429 1.00 40.06 ? 546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 125.199 145.470 182.933 1.00 40.00 ? 546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 126.364 145.613 182.547 1.00 46.59 ? 546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 124.287 143.244 182.249 1.00 40.36 ? 546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 124.032 141.763 182.529 1.00 41.74 ? 546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 123.535 141.065 181.274 1.00 39.22 ? 546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 125.288 141.091 183.055 1.00 39.32 ? 546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 124.323 146.472 182.932 1.00 39.64 ? 547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 124.653 147.805 182.452 1.00 39.96 ? 547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 125.054 148.753 183.574 1.00 41.09 ? 547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 125.170 149.959 183.339 1.00 43.01 ? 547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 123.475 148.392 181.672 1.00 36.97 ? 547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 123.239 147.731 180.344 1.00 39.61 ? 547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 123.879 148.186 179.205 1.00 37.89 ? 547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 122.374 146.656 180.236 1.00 35.61 ? 547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 123.663 147.580 177.984 1.00 35.86 ? 547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 122.154 146.048 179.018 1.00 34.78 ? 547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.799 146.510 177.890 1.00 37.61 ? 547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 125.260 148.240 184.785 1.00 46.99 ? 548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 125.692 149.088 185.887 1.00 47.86 ? 548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 127.012 149.767 185.546 1.00 49.17 ? 548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.920 149.152 184.981 1.00 49.27 ? 548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.836 148.265 187.168 1.00 45.92 ? 548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 125.149 148.878 188.376 1.00 49.22 ? 548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 123.692 149.202 188.115 1.00 52.10 ? 548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 122.872 148.262 188.070 1.00 51.58 ? 548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 123.365 150.397 187.955 1.00 50.86 ? 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 127.116 151.046 185.897 1.00 47.05 ? 549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 128.264 151.843 185.527 1.00 45.36 ? 549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 128.222 152.397 184.122 1.00 48.67 ? 549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 129.187 153.048 183.701 1.00 50.81 ? 549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 127.140 152.163 183.385 1.00 43.00 ? 550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.984 152.646 182.020 1.00 41.17 ? 550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 125.664 153.392 181.918 1.00 42.60 ? 550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 124.633 152.900 182.388 1.00 46.77 ? 550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 127.019 151.489 181.018 1.00 42.48 ? 550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.986 151.685 179.868 1.00 44.18 ? 550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.983 150.286 178.732 1.00 54.77 ? 550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.766 148.922 179.870 1.00 42.26 ? 550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 125.696 154.574 181.311 1.00 39.41 ? 551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 124.489 155.375 181.152 1.00 39.36 ? 551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 123.671 154.839 179.984 1.00 40.81 ? 551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 124.164 154.767 178.853 1.00 38.65 ? 551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 124.846 156.842 180.930 1.00 41.90 ? 551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 123.669 157.701 180.590 1.00 44.64 ? 551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 122.617 157.897 181.458 1.00 43.07 ? 551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 123.374 158.411 179.476 1.00 44.02 ? 551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 121.726 158.693 180.894 1.00 44.18 ? 551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 122.162 159.020 179.691 1.00 45.73 ? 551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 122.426 154.466 180.256 1.00 38.73 ? 552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 121.510 153.978 179.231 1.00 38.50 ? 552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 120.699 155.167 178.724 1.00 35.56 ? 552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.963 155.777 179.515 1.00 40.60 ? 552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 120.590 152.879 179.774 1.00 38.77 ? 552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 121.417 151.722 180.337 1.00 34.67 ? 552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 119.649 152.386 178.685 1.00 37.31 ? 552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 120.584 150.594 180.897 1.00 35.87 ? 552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.804 155.530 177.447 1.00 38.72 ? 553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 120.063 156.695 176.954 1.00 36.71 ? 553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 118.567 156.541 177.176 1.00 36.88 ? 553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.989 155.477 176.948 1.00 43.43 ? 553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 120.412 156.728 175.462 1.00 34.32 ? 553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 121.723 156.025 175.371 1.00 30.49 ? 553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 121.678 154.950 176.414 1.00 32.56 ? 553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.941 157.626 177.619 1.00 37.89 ? 554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 116.514 157.661 177.886 1.00 37.00 ? 554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 115.786 158.352 176.737 1.00 37.88 ? 554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 116.371 158.695 175.708 1.00 34.90 ? 554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 116.237 158.368 179.215 1.00 35.52 ? 554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 116.089 159.774 178.986 1.00 41.88 ? 554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 117.381 158.140 180.187 1.00 36.34 ? 554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 114.479 158.555 176.918 1.00 39.27 ? 555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 113.710 159.297 175.925 1.00 35.50 ? 555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 114.190 160.739 175.831 1.00 38.65 ? 555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 114.219 161.321 174.741 1.00 40.90 ? 555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 112.220 159.249 176.261 1.00 39.08 ? 555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 112.041 159.389 177.676 1.00 46.63 ? 555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 111.614 157.931 175.804 1.00 36.88 ? 555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 114.559 161.338 176.965 1.00 36.28 ? 556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 115.111 162.689 176.941 1.00 37.65 ? 556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 116.423 162.731 176.168 1.00 38.58 ? 556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 116.667 163.662 175.390 1.00 41.85 ? 556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 115.312 163.199 178.368 1.00 40.88 ? 556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 114.041 163.691 179.035 1.00 40.96 ? 556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 113.007 164.172 178.036 1.00 45.78 ? 556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 113.163 165.294 177.512 1.00 45.57 ? 556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 112.038 163.428 177.777 1.00 44.51 ? 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 117.285 161.734 176.375 1.00 38.22 ? 557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 118.532 161.672 175.621 1.00 34.24 ? 557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 118.262 161.548 174.129 1.00 35.60 ? 557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.938 162.183 173.312 1.00 38.51 ? 557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 119.385 160.502 176.111 1.00 34.88 ? 557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 119.782 160.640 177.565 1.00 41.94 ? 557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 120.274 161.721 177.948 1.00 42.98 ? 557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 119.603 159.666 178.326 1.00 42.56 ? 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 117.273 160.737 173.754 1.00 29.20 ? 558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.948 160.579 172.341 1.00 24.56 ? 558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 116.358 161.856 171.757 1.00 31.45 ? 558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 116.619 162.187 170.598 1.00 36.12 ? 558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.996 159.402 172.154 1.00 29.12 ? 558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 116.708 158.095 172.051 1.00 23.94 ? 558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.778 157.124 173.003 1.00 26.64 ? 558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 117.461 157.617 170.932 1.00 26.13 ? 558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 117.525 156.068 172.546 1.00 28.23 ? 558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.955 156.345 171.275 1.00 24.27 ? 558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 117.761 158.139 169.670 1.00 29.00 ? 558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 118.732 155.587 170.405 1.00 22.98 ? 558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 118.535 157.385 168.808 1.00 21.22 ? 558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 119.011 156.124 169.179 1.00 17.09 ? 558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 115.561 162.588 172.537 1.00 36.13 ? 559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 115.056 163.875 172.066 1.00 34.21 ? 559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 116.194 164.866 171.858 1.00 36.21 ? 559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 116.213 165.610 170.869 1.00 37.20 ? 559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 114.036 164.437 173.055 1.00 34.94 ? 559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 112.749 163.641 173.152 1.00 38.21 ? 559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 111.872 164.169 174.273 1.00 36.54 ? 559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 110.895 163.114 174.759 1.00 37.80 ? 559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 110.391 163.421 176.126 1.00 39.75 ? 559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 117.150 164.894 172.788 1.00 33.95 ? 560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 118.303 165.773 172.629 1.00 31.38 ? 560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 119.118 165.391 171.400 1.00 34.63 ? 560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 119.577 166.263 170.656 1.00 37.58 ? 560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 119.170 165.737 173.886 1.00 33.86 ? 560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 118.634 166.583 175.026 1.00 34.94 ? 560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 119.575 166.565 176.217 1.00 39.27 ? 560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 118.927 167.185 177.443 1.00 38.99 ? 560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 117.614 166.556 177.759 1.00 40.71 ? 560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 119.308 164.090 171.172 1.00 32.21 ? 561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 120.027 163.644 169.982 1.00 27.38 ? 561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 119.271 164.007 168.711 1.00 29.09 ? 561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 119.882 164.382 167.706 1.00 34.43 ? 561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 120.275 162.137 170.048 1.00 28.19 ? 561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 120.988 161.526 168.839 1.00 27.51 ? 561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 122.352 162.167 168.638 1.00 24.75 ? 561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 121.119 160.020 168.993 1.00 25.79 ? 561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 117.944 163.887 168.732 1.00 28.65 ? 562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 117.137 164.275 167.581 1.00 32.32 ? 562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 117.300 165.759 167.279 1.00 30.88 ? 562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 117.475 166.155 166.120 1.00 35.23 ? 562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 115.672 163.927 167.845 1.00 27.08 ? 562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 114.689 164.463 166.824 1.00 32.00 ? 562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 113.264 164.269 167.311 1.00 30.74 ? 562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 112.254 164.824 166.326 1.00 32.43 ? 562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 110.885 164.305 166.592 1.00 32.80 ? 562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 117.256 166.596 168.317 1.00 27.19 ? 563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 117.463 168.027 168.119 1.00 32.52 ? 563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 118.865 168.312 167.592 1.00 31.99 ? 563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 119.046 169.149 166.700 1.00 36.24 ? 563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 117.215 168.778 169.426 1.00 33.39 ? 563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 119.869 167.619 168.131 1.00 33.62 ? 564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 121.241 167.815 167.679 1.00 27.88 ? 564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 121.396 167.437 166.211 1.00 31.91 ? 564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 122.071 168.138 165.449 1.00 36.35 ? 564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 122.190 166.997 168.554 1.00 28.98 ? 564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 123.641 167.296 168.326 1.00 32.85 ? 564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 124.249 168.367 168.957 1.00 32.39 ? 564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 124.401 166.500 167.487 1.00 34.80 ? 564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 125.586 168.641 168.750 1.00 33.94 ? 564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 125.737 166.770 167.277 1.00 32.00 ? 564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 126.331 167.842 167.908 1.00 34.70 ? 564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 120.780 166.329 165.798 1.00 33.07 ? 565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 120.853 165.909 164.403 1.00 29.10 ? 565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 120.133 166.906 163.508 1.00 32.80 ? 565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 120.623 167.257 162.428 1.00 39.06 ? 565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 120.285 164.488 164.243 1.00 30.01 ? 565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 119.962 164.207 162.786 1.00 28.45 ? 565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 121.268 163.466 164.779 1.00 31.49 ? 565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 118.960 167.380 163.935 1.00 33.21 ? 566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 118.249 168.383 163.153 1.00 32.18 ? 566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 119.070 169.655 163.004 1.00 37.45 ? 566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 119.005 170.318 161.963 1.00 43.18 ? 566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 116.898 168.694 163.797 1.00 31.25 ? 566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 119.839 170.015 164.031 1.00 37.46 ? 567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 120.673 171.210 163.955 1.00 33.68 ? 567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 121.896 171.000 163.069 1.00 37.71 ? 567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 122.268 171.895 162.303 1.00 43.31 ? 567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 121.103 171.636 165.359 1.00 36.04 ? 567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 122.326 172.537 165.389 1.00 40.69 ? 567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 121.970 174.010 165.372 1.00 46.45 ? 567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 121.077 174.417 166.144 1.00 45.30 ? 567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.587 174.762 164.588 1.00 45.51 ? 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 122.535 169.832 163.155 1.00 37.50 ? 568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 123.812 169.607 162.494 1.00 33.92 ? 568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 123.767 168.576 161.377 1.00 32.05 ? 568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 124.662 168.578 160.527 1.00 38.68 ? 568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 124.869 169.173 163.520 1.00 34.66 ? 568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 125.063 170.153 164.632 1.00 36.90 ? 568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 125.717 171.354 164.460 1.00 34.79 ? 568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.683 170.115 165.931 1.00 37.62 ? 568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 125.734 172.011 165.606 1.00 36.68 ? 568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 125.113 171.281 166.514 1.00 38.18 ? 568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 122.765 167.710 161.350 1.00 27.67 ? 569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 122.689 166.689 160.328 1.00 28.71 ? 569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 123.486 165.450 160.673 1.00 26.28 ? 569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 123.993 165.272 161.784 1.00 34.99 ? 569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 123.592 164.569 159.683 1.00 22.57 ? 570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 124.277 163.294 159.837 1.00 21.03 ? 570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 125.342 163.150 158.763 1.00 21.30 ? 570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 125.124 163.519 157.606 1.00 27.49 ? 570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 123.295 162.119 159.757 1.00 25.90 ? 570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 122.237 162.116 160.844 1.00 23.56 ? 570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 122.680 161.071 162.240 1.00 37.03 ? 570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.640 159.453 161.475 1.00 20.38 ? 570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 126.496 162.609 159.154 1.00 14.87 ? 571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 127.582 162.400 158.206 1.00 16.84 ? 571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 127.411 161.119 157.400 1.00 18.26 ? 571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 127.795 161.076 156.227 1.00 19.79 ? 571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 128.921 162.377 158.944 1.00 20.56 ? 571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 130.124 162.449 158.034 1.00 22.30 ? 571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 130.512 163.649 157.455 1.00 23.13 ? 571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 130.870 161.314 157.750 1.00 18.21 ? 571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 131.611 163.717 156.623 1.00 25.01 ? 571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 131.968 161.372 156.918 1.00 19.87 ? 571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 132.335 162.576 156.358 1.00 26.44 ? 571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 133.430 162.639 155.529 1.00 27.94 ? 571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 126.840 160.077 157.997 1.00 19.64 ? 572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 126.728 158.769 157.367 1.00 8.22  ? 572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 125.279 158.498 156.992 1.00 17.00 ? 572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 124.381 158.630 157.831 1.00 30.89 ? 572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 127.241 157.666 158.297 1.00 15.06 ? 572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 128.580 157.956 158.898 1.00 15.57 ? 572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 128.731 158.671 160.066 1.00 14.05 ? 572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 129.830 157.625 158.496 1.00 11.66 ? 572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 130.015 158.769 160.357 1.00 17.53 ? 572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 130.704 158.143 159.419 1.00 19.08 ? 572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 125.054 158.125 155.731 1.00 11.24 ? 573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 123.724 157.690 155.318 1.00 7.01  ? 573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 123.337 156.393 156.015 1.00 11.95 ? 573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 122.176 156.205 156.393 1.00 23.89 ? 573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 123.670 157.523 153.800 1.00 17.01 ? 573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 124.679 156.641 153.347 1.00 21.17 ? 573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 124.299 155.490 156.186 1.00 16.52 ? 574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 124.099 154.225 156.873 1.00 2.93  ? 574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 125.281 153.993 157.798 1.00 5.83  ? 574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 126.419 154.318 157.451 1.00 14.66 ? 574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.954 153.071 155.876 1.00 11.53 ? 574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.891 153.319 154.834 1.00 5.70  ? 574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.571 152.966 155.067 1.00 8.35  ? 574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 123.203 153.928 153.628 1.00 4.45  ? 574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.596 153.200 154.123 1.00 9.82  ? 574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 122.233 154.167 152.679 1.00 11.25 ? 574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.931 153.798 152.931 1.00 9.02  ? 574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.959 154.031 151.989 1.00 20.05 ? 574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 125.010 153.442 158.976 1.00 11.93 ? 575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 126.037 153.304 160.001 1.00 5.22  ? 575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 126.243 151.877 160.481 1.00 12.80 ? 575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 127.387 151.460 160.671 1.00 17.98 ? 575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 125.696 154.188 161.207 1.00 10.84 ? 575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 125.698 155.676 160.918 1.00 7.13  ? 575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 124.855 156.419 161.939 1.00 11.90 ? 575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 123.437 156.115 161.793 1.00 18.34 ? 575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 122.745 155.346 162.620 1.00 10.55 ? 575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 123.311 154.777 163.671 1.00 14.31 ? 575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 121.454 155.137 162.386 1.00 13.09 ? 575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 125.173 151.114 160.681 1.00 21.19 ? 576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 125.239 149.840 161.383 1.00 8.21  ? 576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.790 148.709 160.472 1.00 8.63  ? 576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.739 148.800 159.831 1.00 15.77 ? 576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 124.374 149.871 162.646 1.00 7.14  ? 576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 124.647 151.016 163.624 1.00 13.98 ? 576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 123.656 150.993 164.773 1.00 11.13 ? 576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 126.072 150.953 164.146 1.00 10.10 ? 576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.590 147.646 160.422 1.00 7.75  ? 577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 125.213 146.416 159.738 1.00 4.24  ? 577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 126.009 145.278 160.357 1.00 18.34 ? 577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 127.230 145.384 160.502 1.00 21.00 ? 577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 125.464 146.510 158.227 1.00 8.23  ? 577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 127.169 146.219 157.695 1.00 27.90 ? 577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 125.320 144.206 160.730 1.00 13.66 ? 578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.932 143.080 161.426 1.00 6.85  ? 578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 126.295 142.035 160.378 1.00 7.36  ? 578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.466 141.211 159.986 1.00 19.17 ? 578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 125.008 142.511 162.506 1.00 11.03 ? 578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 124.652 143.599 163.521 1.00 2.78  ? 578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.668 141.329 163.202 1.00 8.01  ? 578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.715 143.138 164.607 1.00 11.67 ? 578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.543 142.070 159.923 1.00 14.16 ? 579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 128.051 141.104 158.965 1.00 8.68  ? 579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.429 139.800 159.661 1.00 19.94 ? 579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.602 139.761 160.882 1.00 22.30 ? 579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 129.255 141.679 158.229 1.00 9.26  ? 579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.562 138.711 158.901 1.00 28.70 ? 580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 128.830 137.408 159.533 1.00 22.76 ? 580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 130.091 137.379 160.381 1.00 23.37 ? 580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 130.111 136.688 161.407 1.00 33.54 ? 580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 128.924 136.446 158.338 1.00 21.40 ? 580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 129.044 137.307 157.126 1.00 21.75 ? 580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.380 138.599 157.446 1.00 20.65 ? 580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 131.144 138.093 159.988 1.00 20.16 ? 581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.354 138.237 160.800 1.00 30.93 ? 581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 132.905 136.870 161.222 1.00 34.10 ? 581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 133.013 136.534 162.402 1.00 36.38 ? 581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 132.094 139.157 162.004 1.00 36.09 ? 581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 133.321 139.771 162.420 1.00 43.91 ? 581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 131.448 138.423 163.175 1.00 21.24 ? 581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.279 136.084 160.218 1.00 32.54 ? 582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.666 134.709 160.462 1.00 34.45 ? 582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 135.110 134.487 160.866 1.00 36.13 ? 582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 135.377 133.894 161.915 1.00 38.25 ? 582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 136.052 134.956 160.047 1.00 36.88 ? 583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.452 134.594 160.252 1.00 37.59 ? 583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 138.032 135.252 161.499 1.00 38.38 ? 583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 138.751 134.604 162.268 1.00 37.49 ? 583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.275 134.966 159.019 1.00 43.19 ? 583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.084 134.026 157.975 1.00 44.44 ? 583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.733 136.535 161.721 1.00 33.74 ? 584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 138.337 137.260 162.838 1.00 31.28 ? 584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.688 136.950 164.176 1.00 32.00 ? 584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 138.142 137.468 165.203 1.00 34.92 ? 584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 138.292 138.783 162.610 1.00 33.45 ? 584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 136.848 139.261 162.452 1.00 33.13 ? 584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 139.139 139.171 161.409 1.00 29.97 ? 584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 136.723 140.599 161.756 1.00 35.27 ? 584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.638 136.127 164.199 1.00 31.66 ? 585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 136.034 135.755 165.473 1.00 30.44 ? 585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 136.977 134.900 166.309 1.00 29.39 ? 585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 136.948 134.974 167.542 1.00 29.89 ? 585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.714 135.022 165.237 1.00 29.93 ? 585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 134.915 133.814 164.527 1.00 39.68 ? 585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 137.809 134.081 165.663 1.00 35.14 ? 586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 138.793 133.291 166.395 1.00 36.08 ? 586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 139.824 134.187 167.067 1.00 34.29 ? 586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 140.158 133.995 168.242 1.00 34.58 ? 586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 139.474 132.301 165.452 1.00 34.42 ? 586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.544 131.249 164.896 1.00 36.44 ? 586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 138.011 130.264 165.714 1.00 36.35 ? 586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 138.192 131.248 163.554 1.00 36.65 ? 586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 137.160 129.304 165.211 1.00 38.78 ? 586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 137.341 130.291 163.042 1.00 36.52 ? 586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.828 129.322 163.874 1.00 37.31 ? 586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.979 128.367 163.368 1.00 38.93 ? 586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 140.337 135.178 166.335 1.00 30.68 ? 587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 141.314 136.098 166.909 1.00 28.31 ? 587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 140.714 136.834 168.097 1.00 33.41 ? 587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.354 136.984 169.145 1.00 37.74 ? 587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 141.819 137.079 165.834 1.00 32.65 ? 587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 142.922 137.960 166.396 1.00 32.87 ? 587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 142.303 136.320 164.611 1.00 34.75 ? 587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.475 137.304 167.955 1.00 32.81 ? 588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 138.799 137.994 169.042 1.00 24.95 ? 588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 138.343 137.052 170.145 1.00 29.83 ? 588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 137.958 137.527 171.218 1.00 36.11 ? 588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 137.601 138.771 168.500 1.00 27.27 ? 588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 137.980 140.026 167.741 1.00 27.65 ? 588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 138.296 141.182 168.664 1.00 29.46 ? 588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 137.671 141.343 169.710 1.00 34.73 ? 588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 139.276 141.990 168.286 1.00 30.69 ? 588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.378 135.741 169.912 1.00 32.78 ? 589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 137.950 134.760 170.906 1.00 27.91 ? 589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.470 134.942 171.233 1.00 28.60 ? 589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 136.056 134.936 172.393 1.00 32.54 ? 589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 138.812 134.851 172.166 1.00 29.83 ? 589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.740 133.655 172.920 1.00 41.59 ? 589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 135.667 135.105 170.185 1.00 27.27 ? 590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 134.269 135.476 170.320 1.00 24.39 ? 590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.405 134.602 169.424 1.00 25.29 ? 590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.882 133.989 168.468 1.00 29.76 ? 590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 134.055 136.956 169.970 1.00 21.87 ? 590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 133.870 137.126 168.577 1.00 25.08 ? 590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 132.119 134.544 169.758 1.00 26.07 ? 591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 131.152 133.891 168.889 1.00 20.99 ? 591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 130.872 134.767 167.673 1.00 24.62 ? 591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 130.816 135.995 167.771 1.00 22.99 ? 591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.856 133.603 169.646 1.00 23.57 ? 591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 129.174 134.833 169.922 1.00 35.10 ? 591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.151 132.887 170.954 1.00 22.04 ? 591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 130.701 134.128 166.521 1.00 23.83 ? 592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.566 134.865 165.273 1.00 24.16 ? 592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 129.280 135.682 165.262 1.00 26.99 ? 592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 128.196 135.159 165.540 1.00 28.88 ? 592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.592 133.903 164.087 1.00 24.66 ? 592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 129.407 136.962 164.940 1.00 25.38 ? 593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 128.274 137.868 164.744 1.00 11.61 ? 593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 127.360 137.807 165.969 1.00 14.91 ? 593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 127.822 137.634 167.101 1.00 25.38 ? 593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.594 137.533 163.430 1.00 25.21 ? 593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.657 138.529 163.068 1.00 29.60 ? 593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 126.054 137.956 165.753 1.00 20.69 ? 594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 125.063 137.829 166.813 1.00 19.49 ? 594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 124.365 136.475 166.773 1.00 16.38 ? 594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 123.411 136.250 167.521 1.00 19.31 ? 594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 124.038 138.973 166.751 1.00 22.91 ? 594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.688 140.289 167.146 1.00 13.82 ? 594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 123.435 139.067 165.361 1.00 22.91 ? 594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 124.820 135.569 165.913 1.00 25.11 ? 595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 124.179 134.275 165.775 1.00 21.12 ? 595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.552 133.364 166.944 1.00 25.32 ? 595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 125.610 133.527 167.557 1.00 30.70 ? 595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.588 133.616 164.462 1.00 21.78 ? 595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.273 134.441 163.227 1.00 25.79 ? 595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 122.670 134.054 162.505 1.00 35.97 ? 595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.607 135.072 163.520 1.00 15.95 ? 595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.697 132.402 167.276 1.00 32.84 ? 596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 124.075 131.392 168.267 1.00 23.07 ? 596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 125.132 130.449 167.711 1.00 26.02 ? 596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.270 130.261 166.501 1.00 31.41 ? 596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.761 130.660 168.549 1.00 24.93 ? 596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.957 130.845 167.311 1.00 29.89 ? 596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.340 132.184 166.745 1.00 28.33 ? 596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.891 129.851 168.629 1.00 27.93 ? 597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.998 128.989 168.241 1.00 30.87 ? 597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.468 127.749 167.536 1.00 32.24 ? 597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.427 127.192 167.909 1.00 34.85 ? 597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.840 128.607 169.470 1.00 30.75 ? 597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 127.007 127.776 170.448 1.00 31.41 ? 597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.388 129.850 170.147 1.00 29.59 ? 597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.830 126.997 171.442 1.00 30.86 ? 597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.186 127.313 166.500 1.00 43.18 ? 598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.810 126.094 165.795 1.00 41.72 ? 598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.194 124.849 166.585 1.00 41.97 ? 598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.454 123.859 166.584 1.00 47.60 ? 598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.461 126.066 164.412 1.00 41.24 ? 598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.706 126.849 163.354 1.00 40.38 ? 598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.623 126.987 161.809 1.00 59.59 ? 598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.782 128.290 162.214 1.00 43.59 ? 598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.339 124.879 167.263 1.00 43.28 ? 599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 128.823 123.731 168.015 1.00 43.32 ? 599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.641 124.218 169.200 1.00 40.08 ? 599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.385 125.194 169.088 1.00 46.95 ? 599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 129.664 122.800 167.134 1.00 44.95 ? 599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 130.690 123.518 166.276 1.00 43.40 ? 599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 130.820 122.908 164.896 1.00 48.73 ? 599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 129.779 122.703 164.236 1.00 52.84 ? 599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.960 122.631 164.469 1.00 47.86 ? 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.500 123.525 170.332 1.00 39.89 ? 600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 130.209 123.930 171.541 1.00 37.05 ? 600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.717 123.849 171.350 1.00 38.03 ? 600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 132.456 124.734 171.797 1.00 44.05 ? 600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.771 123.063 172.720 1.00 37.40 ? 600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 128.451 123.486 173.331 1.00 37.89 ? 600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 128.139 122.677 174.573 1.00 38.17 ? 600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.803 122.958 175.084 1.00 37.44 ? 600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.704 122.340 174.676 1.00 41.28 ? 600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.744 121.404 173.742 1.00 41.31 ? 600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.535 122.669 175.217 1.00 39.74 ? 600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 132.193 122.794 170.697 1.00 42.59 ? 601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.607 122.620 170.391 1.00 42.97 ? 601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.728 122.419 168.889 1.00 44.04 ? 601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 133.061 121.548 168.318 1.00 45.36 ? 601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 134.221 121.439 171.158 1.00 42.45 ? 601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 133.945 121.580 172.656 1.00 42.85 ? 601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.714 121.358 170.897 1.00 39.80 ? 601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 134.327 120.365 173.465 1.00 41.67 ? 601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.576 123.221 168.254 1.00 51.23 ? 602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.730 123.197 166.806 1.00 49.11 ? 602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 135.890 122.282 166.436 1.00 51.58 ? 602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 137.017 122.480 166.902 1.00 54.51 ? 602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.963 124.609 166.270 1.00 48.75 ? 602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.267 124.901 164.955 1.00 52.63 ? 602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 133.816 126.345 164.844 1.00 57.30 ? 602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 134.662 127.248 165.013 1.00 56.56 ? 602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 132.616 126.577 164.585 1.00 53.97 ? 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.612 121.285 165.602 1.00 58.91 ? 603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.626 120.361 165.114 1.00 58.18 ? 603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 137.051 120.792 163.717 1.00 56.93 ? 603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 136.239 120.781 162.786 1.00 58.99 ? 603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 136.097 118.928 165.097 1.00 59.66 ? 603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 137.172 117.872 165.280 1.00 61.99 ? 603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 136.829 116.566 164.593 1.00 62.91 ? 603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 136.744 116.552 163.348 1.00 62.22 ? 603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 136.646 115.552 165.300 1.00 59.89 ? 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.316 121.170 163.576 1.00 60.45 ? 604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.863 121.624 162.309 1.00 60.95 ? 604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 140.042 120.746 161.919 1.00 62.05 ? 604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.707 120.155 162.776 1.00 61.95 ? 604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 139.320 123.086 162.385 1.00 61.78 ? 604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 138.249 124.074 162.821 1.00 62.24 ? 604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 137.130 124.201 161.800 1.00 62.05 ? 604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 136.003 123.331 162.113 1.00 63.95 ? 604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.739 123.614 161.829 1.00 60.40 ? 604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.403 124.739 161.222 1.00 60.18 ? 604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.789 122.748 162.167 1.00 60.78 ? 604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.293 120.662 160.617 1.00 66.27 ? 605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.452 119.960 160.082 1.00 67.23 ? 605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.365 120.976 159.406 1.00 67.54 ? 605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.933 121.708 158.508 1.00 67.15 ? 605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.031 118.854 159.110 1.00 67.78 ? 605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 142.036 117.833 159.082 1.00 69.23 ? 605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 140.824 119.398 157.702 1.00 66.03 ? 605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.612 121.044 159.864 1.00 67.96 ? 606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.629 121.922 159.290 1.00 67.94 ? 606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.809 121.040 158.899 1.00 68.56 ? 606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.566 120.583 159.762 1.00 67.62 ? 606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 145.031 123.016 160.275 1.00 66.19 ? 606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.926 124.013 160.546 1.00 66.72 ? 606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.627 125.015 159.632 1.00 65.48 ? 606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.173 123.944 161.709 1.00 66.10 ? 606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 142.614 125.923 159.874 1.00 66.55 ? 606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 142.159 124.846 161.960 1.00 65.31 ? 606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.884 125.833 161.040 1.00 67.77 ? 606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.873 126.733 161.289 1.00 68.60 ? 606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 145.965 120.802 157.601 1.00 74.62 ? 607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 146.920 119.799 157.162 1.00 73.81 ? 607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.406 118.421 157.526 1.00 74.20 ? 607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.240 118.087 157.289 1.00 74.61 ? 607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.278 117.602 158.109 1.00 76.14 ? 608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 146.897 116.293 158.619 1.00 77.98 ? 608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 146.614 116.313 160.115 1.00 78.57 ? 608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.373 115.255 160.705 1.00 78.12 ? 608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 147.983 115.264 158.302 1.00 78.21 ? 608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.022 114.894 156.832 1.00 78.30 ? 608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 147.077 115.159 156.089 1.00 77.12 ? 608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 149.118 114.278 156.406 1.00 78.65 ? 608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 146.634 117.487 160.737 1.00 75.09 ? 609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.401 117.636 162.166 1.00 74.37 ? 609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.018 118.228 162.396 1.00 72.38 ? 609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 144.666 119.248 161.794 1.00 71.38 ? 609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.469 118.526 162.802 1.00 72.78 ? 609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.427 119.833 162.257 1.00 72.95 ? 609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.243 117.588 163.265 1.00 65.50 ? 610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 142.905 118.045 163.613 1.00 65.25 ? 610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 142.971 118.870 164.891 1.00 64.63 ? 610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 143.561 118.438 165.886 1.00 62.87 ? 610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 141.955 116.859 163.783 1.00 64.82 ? 610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 142.209 116.031 165.029 1.00 63.67 ? 610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 140.932 115.388 165.537 1.00 65.66 ? 610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 140.385 114.391 164.527 1.00 66.01 ? 610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 138.898 114.330 164.543 1.00 65.07 ? 610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.369 120.055 164.858 1.00 64.13 ? 611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.398 120.989 165.974 1.00 61.57 ? 611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 141.016 121.088 166.603 1.00 57.97 ? 611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 139.999 121.017 165.906 1.00 58.79 ? 611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.862 122.376 165.523 1.00 62.28 ? 611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 142.356 122.645 164.210 1.00 60.67 ? 611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 144.379 122.445 165.496 1.00 60.09 ? 611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 140.987 121.252 167.920 1.00 54.96 ? 612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.748 121.328 168.681 1.00 53.11 ? 612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.591 122.733 169.243 1.00 55.32 ? 612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.476 123.223 169.953 1.00 58.02 ? 612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.745 120.299 169.812 1.00 56.10 ? 612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.530 118.882 169.337 1.00 57.49 ? 612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.368 118.521 168.671 1.00 57.63 ? 612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 140.495 117.907 169.547 1.00 58.61 ? 612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.171 117.227 168.233 1.00 58.58 ? 612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.307 116.611 169.111 1.00 59.11 ? 612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.144 116.276 168.455 1.00 59.68 ? 612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 138.950 114.985 168.019 1.00 60.10 ? 612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.471 123.375 168.928 1.00 48.81 ? 613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.198 124.736 169.388 1.00 42.77 ? 613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 136.921 124.773 170.212 1.00 40.43 ? 613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 135.813 124.788 169.647 1.00 42.33 ? 613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.094 125.700 168.208 1.00 40.04 ? 613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.878 127.136 168.621 1.00 41.62 ? 613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.810 127.800 169.406 1.00 43.04 ? 613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.744 127.830 168.224 1.00 42.55 ? 613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.618 129.113 169.785 1.00 43.84 ? 613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.543 129.142 168.599 1.00 43.15 ? 613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 137.483 129.780 169.379 1.00 44.16 ? 613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 137.286 131.089 169.753 1.00 43.98 ? 613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 137.014 124.785 171.538 1.00 38.60 ? 614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 135.818 125.010 172.352 1.00 39.14 ? 614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.304 126.427 172.166 1.00 40.77 ? 614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.057 127.350 171.846 1.00 40.12 ? 614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.309 124.779 173.787 1.00 40.52 ? 614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.652 124.121 173.651 1.00 41.36 ? 614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.217 124.617 172.366 1.00 39.12 ? 614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.004 126.593 172.367 1.00 41.25 ? 615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.421 127.920 172.261 1.00 36.95 ? 615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 134.056 128.839 173.301 1.00 36.93 ? 615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.241 128.434 174.455 1.00 38.64 ? 615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.906 127.863 172.457 1.00 35.74 ? 615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.123 127.752 171.161 1.00 36.58 ? 615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 131.838 128.719 169.819 1.00 53.27 ? 615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 132.833 127.477 168.998 1.00 38.98 ? 615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.409 130.067 172.931 1.00 42.14 ? 616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 135.135 130.938 173.863 1.00 36.76 ? 616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 134.406 131.074 175.190 1.00 35.68 ? 616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 133.222 131.410 175.240 1.00 41.07 ? 616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 135.203 132.271 173.114 1.00 35.33 ? 616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 135.115 131.892 171.676 1.00 37.92 ? 616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 134.200 130.707 171.622 1.00 39.13 ? 616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 135.133 130.820 176.275 1.00 35.20 ? 617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.557 130.828 177.600 1.00 37.36 ? 617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.844 129.556 177.995 1.00 40.77 ? 617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 133.296 129.493 179.102 1.00 41.32 ? 617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.833 128.542 177.132 1.00 41.06 ? 618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 133.127 127.307 177.438 1.00 38.42 ? 618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.730 126.634 178.664 1.00 40.27 ? 618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 134.950 126.609 178.846 1.00 45.75 ? 618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 133.175 126.361 176.238 1.00 38.42 ? 618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 132.451 125.021 176.380 1.00 41.92 ? 618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 130.960 125.231 176.574 1.00 39.41 ? 618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.719 124.142 175.170 1.00 40.34 ? 618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 132.862 126.089 179.509 1.00 45.10 ? 619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.282 125.414 180.729 1.00 46.02 ? 619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.138 124.525 181.196 1.00 48.01 ? 619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.061 124.498 180.595 1.00 52.82 ? 619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 133.694 126.420 181.806 1.00 42.56 ? 619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.383 123.790 182.281 1.00 54.00 ? 620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 131.353 122.908 182.821 1.00 52.81 ? 620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 130.158 123.701 183.336 1.00 53.26 ? 620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 129.006 123.301 183.136 1.00 56.76 ? 620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 131.939 122.039 183.933 1.00 57.04 ? 620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 133.113 121.377 183.498 1.00 60.56 ? 620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 130.412 124.830 184.002 1.00 51.23 ? 621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.332 125.579 184.633 1.00 51.61 ? 621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.481 126.350 183.631 1.00 52.06 ? 621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 127.336 126.688 183.947 1.00 52.13 ? 621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 129.900 126.537 185.682 1.00 52.24 ? 621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.637 127.709 185.065 1.00 54.17 ? 621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.058 127.657 183.910 1.00 55.70 ? 621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 130.796 128.777 185.837 1.00 52.17 ? 621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 129.005 126.638 182.439 1.00 44.50 ? 622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.248 127.335 181.407 1.00 45.09 ? 622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 127.984 126.455 180.190 1.00 47.58 ? 622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 127.669 126.968 179.112 1.00 51.27 ? 622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 128.962 128.625 180.995 1.00 46.48 ? 622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.300 128.373 180.320 1.00 47.00 ? 622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.599 127.261 179.890 1.00 49.62 ? 622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 131.114 129.417 180.227 1.00 43.26 ? 622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.109 125.135 180.342 1.00 41.05 ? 623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 127.860 124.231 179.225 1.00 41.27 ? 623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 126.419 124.334 178.742 1.00 42.36 ? 623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.160 124.349 177.533 1.00 37.88 ? 623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.188 122.796 179.637 1.00 41.92 ? 623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 128.006 121.788 178.548 1.00 40.24 ? 623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 126.855 121.137 178.217 1.00 39.53 ? 623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 129.011 121.306 177.649 1.00 43.01 ? 623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 127.078 120.284 177.166 1.00 37.62 ? 623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.395 120.368 176.799 1.00 39.39 ? 623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.372 121.578 177.479 1.00 41.30 ? 623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 129.092 119.701 175.794 1.00 40.26 ? 623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 131.061 120.915 176.481 1.00 42.18 ? 623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.421 119.988 175.652 1.00 41.89 ? 623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 125.466 124.403 179.673 1.00 47.83 ? 624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 124.058 124.436 179.293 1.00 45.81 ? 624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 123.703 125.719 178.554 1.00 44.60 ? 624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 122.885 125.692 177.628 1.00 46.49 ? 624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.184 124.262 180.537 1.00 45.65 ? 624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 121.825 124.894 180.426 1.00 48.58 ? 624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 120.767 124.193 179.872 1.00 49.31 ? 624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 121.599 126.176 180.896 1.00 48.63 ? 624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 119.513 124.765 179.775 1.00 47.90 ? 624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 120.347 126.754 180.800 1.00 47.43 ? 624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 119.304 126.047 180.239 1.00 46.39 ? 624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.303 126.847 178.940 1.00 38.94 ? 625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 124.029 128.110 178.268 1.00 38.69 ? 625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.673 128.199 176.892 1.00 35.29 ? 625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.240 129.018 176.074 1.00 38.56 ? 625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.494 129.282 179.134 1.00 35.61 ? 625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 123.750 129.408 180.430 1.00 37.86 ? 625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.419 129.784 180.444 1.00 38.23 ? 625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.379 129.146 181.634 1.00 37.04 ? 625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.729 129.899 181.635 1.00 37.30 ? 625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.695 129.260 182.828 1.00 36.47 ? 625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 122.368 129.638 182.828 1.00 37.50 ? 625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.687 127.387 176.614 1.00 33.35 ? 626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.274 127.327 175.277 1.00 32.87 ? 626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.501 126.366 174.382 1.00 33.99 ? 626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.060 125.478 173.742 1.00 39.93 ? 626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.743 126.935 175.369 1.00 33.32 ? 626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.680 128.119 175.402 1.00 34.82 ? 626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.878 128.900 174.272 1.00 36.36 ? 626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.360 128.460 176.562 1.00 33.61 ? 626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.730 129.983 174.295 1.00 34.23 ? 626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 130.215 129.542 176.594 1.00 34.41 ? 626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 130.396 130.299 175.458 1.00 34.99 ? 626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 131.244 131.380 175.481 1.00 38.39 ? 626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 124.189 126.562 174.329 1.00 35.65 ? 627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.327 125.703 173.534 1.00 34.10 ? 627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.616 125.890 172.051 1.00 35.17 ? 627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.800 127.013 171.575 1.00 38.30 ? 627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 121.862 126.010 173.840 1.00 35.18 ? 627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 120.861 125.123 173.131 1.00 33.73 ? 627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.465 125.356 173.678 1.00 34.68 ? 627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.430 124.533 172.937 1.00 41.48 ? 627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 117.056 124.813 173.433 1.00 40.15 ? 627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.669 124.781 171.321 1.00 40.55 ? 628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 123.961 124.845 169.898 1.00 38.37 ? 628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 122.767 125.398 169.127 1.00 39.30 ? 628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.610 125.237 169.524 1.00 37.34 ? 628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.346 123.465 169.369 1.00 36.19 ? 628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.841 123.198 169.408 1.00 40.59 ? 628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 126.176 121.721 169.446 1.00 47.63 ? 628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.823 121.006 168.484 1.00 42.69 ? 628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 126.795 121.275 170.434 1.00 44.14 ? 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 123.064 126.060 168.006 1.00 37.06 ? 629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.020 126.731 167.240 1.00 32.34 ? 629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.007 125.739 166.684 1.00 34.71 ? 629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 119.803 126.017 166.661 1.00 40.09 ? 629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.644 127.551 166.111 1.00 31.60 ? 629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.475 124.578 166.224 1.00 43.03 ? 630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.567 123.599 165.637 1.00 36.11 ? 630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.554 123.073 166.643 1.00 39.06 ? 630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.491 122.590 166.239 1.00 44.21 ? 630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.363 122.443 165.036 1.00 37.22 ? 630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.288 122.870 163.922 1.00 38.40 ? 630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 121.792 123.193 162.669 1.00 37.47 ? 630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.658 122.958 164.127 1.00 40.17 ? 630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.632 123.587 161.649 1.00 39.22 ? 630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.506 123.351 163.113 1.00 41.29 ? 630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 123.988 123.663 161.877 1.00 43.58 ? 630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 124.831 124.054 160.864 1.00 49.19 ? 630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 119.855 123.152 167.937 1.00 40.43 ? 631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 118.925 122.720 168.969 1.00 38.00 ? 631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 117.990 123.827 169.438 1.00 40.61 ? 631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 117.047 123.543 170.183 1.00 43.57 ? 631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 119.695 122.162 170.171 1.00 40.27 ? 631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.412 120.867 169.850 1.00 47.12 ? 631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 119.839 120.037 169.113 1.00 46.94 ? 631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 121.549 120.679 170.331 1.00 48.16 ? 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.220 125.070 169.024 1.00 38.93 ? 632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.358 126.165 169.432 1.00 37.33 ? 632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.107 126.231 168.564 1.00 37.51 ? 632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.057 125.705 167.449 1.00 37.13 ? 632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.089 127.507 169.358 1.00 35.31 ? 632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 119.548 127.481 169.751 1.00 38.12 ? 632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 119.958 128.962 170.693 1.00 43.25 ? 632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 121.724 128.778 170.880 1.00 35.56 ? 632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.087 126.896 169.098 1.00 31.55 ? 633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 113.885 127.206 168.338 1.00 30.10 ? 633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.178 128.372 167.403 1.00 33.88 ? 633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.471 129.482 167.860 1.00 34.42 ? 633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.735 127.546 169.284 1.00 25.12 ? 633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.419 127.740 168.559 1.00 34.63 ? 633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.392 127.612 167.318 1.00 39.73 ? 633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.409 128.023 169.235 1.00 36.61 ? 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.104 128.124 166.094 1.00 28.04 ? 634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.362 129.188 165.133 1.00 24.62 ? 634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.408 130.361 165.303 1.00 26.36 ? 634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.743 131.478 164.897 1.00 27.24 ? 634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.282 128.647 163.706 1.00 28.12 ? 634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.491 127.831 163.278 1.00 30.97 ? 634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 117.047 128.720 163.507 1.00 47.17 ? 634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.481 128.246 165.178 1.00 32.98 ? 634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.231 130.140 165.889 1.00 26.72 ? 635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.345 131.259 166.190 1.00 25.15 ? 635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.959 132.176 167.240 1.00 26.26 ? 635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.858 133.403 167.137 1.00 29.51 ? 635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.982 130.744 166.651 1.00 24.83 ? 635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 109.044 130.428 165.524 1.00 30.69 ? 635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.487 129.743 164.406 1.00 29.13 ? 635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.717 130.814 165.581 1.00 29.09 ? 635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.627 129.450 163.368 1.00 26.04 ? 635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.852 130.524 164.545 1.00 27.26 ? 635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.308 129.840 163.438 1.00 23.89 ? 635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.610 131.602 168.253 1.00 27.28 ? 636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 113.285 132.423 169.252 1.00 27.64 ? 636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.494 133.142 168.666 1.00 22.14 ? 636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.776 134.287 169.038 1.00 30.50 ? 636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.696 131.561 170.444 1.00 28.82 ? 636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 112.530 130.868 171.123 1.00 28.85 ? 636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.575 131.881 171.729 1.00 31.55 ? 636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.678 131.240 172.772 1.00 31.36 ? 636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.337 131.885 172.816 1.00 32.27 ? 636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 115.218 132.495 167.751 1.00 20.90 ? 637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 116.323 133.167 167.075 1.00 18.67 ? 637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.801 134.320 166.230 1.00 25.02 ? 637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.419 135.389 166.157 1.00 29.21 ? 637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 117.125 132.158 166.232 1.00 23.17 ? 637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 118.316 132.840 165.579 1.00 23.85 ? 637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.573 130.989 167.093 1.00 23.94 ? 637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 114.654 134.122 165.576 1.00 25.79 ? 638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 114.032 135.198 164.813 1.00 22.29 ? 638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.624 136.334 165.739 1.00 17.41 ? 638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 113.772 137.512 165.400 1.00 27.40 ? 638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.830 134.664 164.012 1.00 22.52 ? 638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.976 135.814 163.510 1.00 15.31 ? 638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 113.303 133.801 162.856 1.00 22.52 ? 638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 113.096 136.001 166.916 1.00 17.93 ? 639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 112.738 137.033 167.885 1.00 20.95 ? 639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 113.962 137.835 168.308 1.00 26.09 ? 639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 113.911 139.067 168.395 1.00 30.13 ? 639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 112.070 136.396 169.103 1.00 20.34 ? 639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.628 136.021 168.845 1.00 29.42 ? 639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 109.945 136.761 168.107 1.00 31.81 ? 639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 110.178 134.985 169.376 1.00 34.59 ? 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 115.076 137.149 168.565 1.00 22.94 ? 640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 116.311 137.838 168.927 1.00 20.96 ? 640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 116.778 138.757 167.805 1.00 22.74 ? 640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 117.109 139.927 168.036 1.00 30.55 ? 640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 117.391 136.812 169.267 1.00 22.71 ? 640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 118.730 137.416 169.643 1.00 27.19 ? 640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 118.586 138.732 170.861 1.00 34.39 ? 640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 119.571 138.044 172.185 1.00 25.24 ? 640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 116.812 138.240 166.575 1.00 17.21 ? 641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 117.301 139.033 165.453 1.00 17.72 ? 641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 116.384 140.219 165.187 1.00 21.72 ? 641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.850 141.296 164.798 1.00 28.09 ? 641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.462 138.148 164.204 1.00 24.79 ? 641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.437 137.003 164.488 1.00 21.23 ? 641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 117.935 138.976 163.024 1.00 10.32 ? 641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 119.667 137.427 165.255 1.00 16.62 ? 641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 115.076 140.050 165.387 1.00 18.90 ? 642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 114.150 141.160 165.205 1.00 19.67 ? 642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 114.327 142.203 166.298 1.00 17.81 ? 642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 114.222 143.407 166.037 1.00 26.10 ? 642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.712 140.645 165.179 1.00 15.09 ? 642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.595 141.762 167.529 1.00 16.79 ? 643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.908 142.710 168.591 1.00 18.30 ? 643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 116.160 143.508 168.252 1.00 21.13 ? 643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 116.206 144.726 168.461 1.00 21.57 ? 643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 115.082 141.975 169.920 1.00 17.52 ? 643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 113.837 141.383 170.308 1.00 28.55 ? 643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 115.534 142.937 171.002 1.00 16.71 ? 643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 117.185 142.838 167.724 1.00 15.63 ? 644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 118.400 143.543 167.330 1.00 14.44 ? 644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 118.145 144.414 166.107 1.00 14.28 ? 644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 118.595 145.563 166.042 1.00 16.38 ? 644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 119.542 142.541 167.080 1.00 19.50 ? 644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.835 141.736 168.347 1.00 14.69 ? 644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.788 143.263 166.592 1.00 8.25  ? 644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.701 140.527 168.106 1.00 16.97 ? 644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 117.414 143.887 165.122 1.00 14.63 ? 645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 117.239 144.587 163.856 1.00 12.96 ? 645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 116.505 145.912 164.006 1.00 19.07 ? 645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.658 146.788 163.149 1.00 20.99 ? 645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 116.496 143.696 162.860 1.00 10.51 ? 645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 116.275 144.345 161.506 1.00 4.60  ? 645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 117.530 144.362 160.659 1.00 10.57 ? 645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 117.925 143.344 160.095 1.00 16.66 ? 645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 118.167 145.522 160.568 1.00 10.79 ? 645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.716 146.086 165.065 1.00 21.32 ? 646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 115.001 147.342 165.244 1.00 17.28 ? 646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.929 148.505 165.565 1.00 12.89 ? 646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 115.481 149.655 165.539 1.00 20.93 ? 646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.946 147.192 166.340 1.00 19.06 ? 646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 114.502 147.189 167.747 1.00 20.29 ? 646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 113.424 146.990 168.790 1.00 29.54 ? 646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.550 147.837 168.965 1.00 32.67 ? 646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 113.481 145.865 169.492 1.00 23.57 ? 646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 117.200 148.239 165.863 1.00 22.06 ? 647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 118.175 149.286 166.131 1.00 14.27 ? 647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 119.287 149.341 165.096 1.00 10.77 ? 647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 120.214 150.143 165.248 1.00 26.29 ? 647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.785 149.102 167.527 1.00 12.82 ? 647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 117.768 148.931 168.611 1.00 13.80 ? 647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.842 149.903 168.921 1.00 18.26 ? 647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 117.529 147.901 169.456 1.00 11.62 ? 647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 116.077 149.479 169.911 1.00 17.47 ? 647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 116.474 148.267 170.254 1.00 17.45 ? 647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 119.225 148.517 164.055 1.00 10.38 ? 648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 120.208 148.504 162.979 1.00 14.01 ? 648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 119.569 149.139 161.753 1.00 13.88 ? 648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 118.487 148.721 161.325 1.00 25.64 ? 648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.687 147.074 162.674 1.00 14.38 ? 648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 121.157 146.378 163.954 1.00 12.21 ? 648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.791 147.085 161.626 1.00 1.05  ? 648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 122.328 147.053 164.625 1.00 4.99  ? 648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 120.229 150.155 161.193 1.00 11.72 ? 649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.684 150.803 160.005 1.00 4.81  ? 649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.841 149.929 158.769 1.00 12.21 ? 649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.986 149.957 157.878 1.00 32.78 ? 649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 120.349 152.164 159.790 1.00 19.29 ? 649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.849 152.121 159.995 1.00 16.57 ? 649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 122.319 151.244 160.746 1.00 23.29 ? 649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 122.556 152.960 159.405 1.00 17.59 ? 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.924 149.165 158.693 1.00 12.81 ? 650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 121.109 148.166 157.654 1.00 6.04  ? 650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 120.602 146.815 158.156 1.00 11.69 ? 650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.900 146.725 159.166 1.00 21.12 ? 650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 122.569 148.118 157.219 1.00 8.18  ? 650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.995 149.313 156.390 1.00 6.23  ? 650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 124.429 149.215 155.931 1.00 12.62 ? 650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 124.737 148.504 154.977 1.00 20.40 ? 650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 125.318 149.933 156.606 1.00 2.98  ? 650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.935 145.747 157.440 1.00 3.14  ? 651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 120.453 144.432 157.798 1.00 7.19  ? 651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 121.378 143.672 158.735 1.00 12.88 ? 651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 122.480 144.103 159.066 1.00 9.14  ? 651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.887 142.518 159.175 1.00 19.38 ? 652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.635 141.581 160.002 1.00 8.24  ? 652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.756 140.277 159.231 1.00 9.72  ? 652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 120.749 139.733 158.764 1.00 25.81 ? 652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 120.954 141.346 161.363 1.00 6.05  ? 652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.708 142.675 162.080 1.00 2.68  ? 652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 121.782 140.400 162.217 1.00 11.56 ? 652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 119.919 142.538 163.357 1.00 11.61 ? 652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 122.980 139.780 159.092 1.00 7.44  ? 653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 123.216 138.540 158.359 1.00 14.49 ? 653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.670 137.384 159.188 1.00 15.71 ? 653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 123.292 136.946 160.157 1.00 24.68 ? 653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.702 138.374 158.064 1.00 14.21 ? 653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 124.975 137.104 157.508 1.00 24.33 ? 653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.499 136.886 158.803 1.00 23.37 ? 654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.720 135.950 159.606 1.00 14.71 ? 654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 120.765 134.577 158.947 1.00 16.20 ? 654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 120.156 134.366 157.893 1.00 20.84 ? 654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 119.284 136.449 159.754 1.00 16.57 ? 654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.432 135.612 160.664 1.00 19.78 ? 654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.998 134.657 161.489 1.00 18.26 ? 654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 117.061 135.792 160.700 1.00 21.61 ? 654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 118.214 133.892 162.325 1.00 16.99 ? 654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 116.272 135.031 161.537 1.00 21.82 ? 654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.849 134.079 162.351 1.00 17.92 ? 654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.485 133.649 159.569 1.00 19.89 ? 655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.551 132.266 159.119 1.00 25.70 ? 655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.524 131.434 159.875 1.00 25.03 ? 655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.381 131.574 161.093 1.00 27.08 ? 655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.950 131.686 159.330 1.00 28.46 ? 655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.872 132.315 158.432 1.00 35.08 ? 655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.950 130.187 159.080 1.00 26.29 ? 655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.809 130.579 159.151 1.00 31.89 ? 656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.874 129.636 159.748 1.00 33.03 ? 656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.560 128.288 159.918 1.00 30.07 ? 656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.167 127.769 158.976 1.00 27.19 ? 656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.615 129.486 158.892 1.00 28.69 ? 656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.948 130.775 158.413 1.00 31.82 ? 656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.764 130.460 157.516 1.00 31.07 ? 656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.515 131.624 159.597 1.00 29.14 ? 656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.462 127.728 161.118 1.00 30.53 ? 657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.082 126.452 161.455 1.00 32.61 ? 657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 118.979 125.409 161.571 1.00 37.30 ? 657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.195 125.429 162.526 1.00 39.71 ? 657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.887 126.570 162.747 1.00 31.21 ? 657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.870 127.703 162.737 1.00 36.49 ? 657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.122 127.546 162.170 1.00 35.34 ? 657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.536 128.931 163.282 1.00 35.48 ? 657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 124.024 128.589 162.153 1.00 36.47 ? 657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.435 129.977 163.270 1.00 31.97 ? 657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.681 129.806 162.704 1.00 35.90 ? 657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 118.924 124.500 160.604 1.00 39.59 ? 658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 117.828 123.552 160.471 1.00 40.20 ? 658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.305 122.136 160.757 1.00 41.79 ? 658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.417 121.755 160.380 1.00 42.26 ? 658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.226 123.614 159.066 1.00 40.83 ? 658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.055 125.008 158.466 1.00 37.69 ? 658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 116.738 124.913 156.985 1.00 40.23 ? 658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.970 125.770 159.202 1.00 37.22 ? 658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.459 121.364 161.431 1.00 51.50 ? 659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.689 119.937 161.578 1.00 50.52 ? 659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.229 119.204 160.324 1.00 51.93 ? 659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.336 119.660 159.605 1.00 53.11 ? 659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 116.955 119.397 162.805 1.00 51.46 ? 659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.505 119.908 164.126 1.00 51.93 ? 659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 116.942 119.128 165.302 1.00 52.36 ? 659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 117.584 119.562 166.610 1.00 51.66 ? 659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 117.311 118.599 167.712 1.00 53.66 ? 659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 117.856 118.057 160.060 1.00 58.94 ? 660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.521 117.293 158.864 1.00 58.85 ? 660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.088 116.780 158.884 1.00 56.88 ? 660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.524 116.514 157.818 1.00 55.28 ? 660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.491 116.123 158.694 1.00 58.84 ? 660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.364 115.094 159.800 1.00 60.24 ? 660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 118.221 115.494 160.974 1.00 60.14 ? 660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.406 113.884 159.493 1.00 59.40 ? 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.487 116.634 160.067 1.00 53.33 ? 661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 114.111 116.164 160.150 1.00 55.16 ? 661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 113.106 117.227 159.728 1.00 56.84 ? 661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 111.972 116.884 159.378 1.00 58.24 ? 661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 113.796 115.698 161.572 1.00 57.48 ? 661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 114.131 116.736 162.501 1.00 56.19 ? 661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 114.592 114.447 161.910 1.00 58.13 ? 661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.490 118.499 159.753 1.00 55.54 ? 662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.566 119.566 159.399 1.00 52.24 ? 662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.186 119.484 157.926 1.00 53.85 ? 662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 113.040 119.294 157.056 1.00 54.64 ? 662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.186 120.928 159.707 1.00 51.99 ? 662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 113.448 121.172 161.183 1.00 52.79 ? 662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 113.445 122.925 161.597 1.00 58.42 ? 662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 113.442 123.653 159.961 1.00 53.45 ? 662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 110.893 119.629 157.652 1.00 47.28 ? 663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.387 119.608 156.290 1.00 43.39 ? 663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.511 120.995 155.662 1.00 43.35 ? 663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 110.935 121.962 156.300 1.00 46.72 ? 663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 108.937 119.130 156.270 1.00 39.57 ? 663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.100 120.114 156.888 1.00 43.13 ? 663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 108.800 117.817 157.025 1.00 45.54 ? 663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 110.140 121.096 154.384 1.00 38.91 ? 664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 110.102 122.404 153.740 1.00 41.37 ? 664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.036 123.294 154.363 1.00 39.62 ? 664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.155 124.524 154.325 1.00 44.36 ? 664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 109.853 122.256 152.239 1.00 41.23 ? 664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 108.656 121.500 152.024 1.00 43.25 ? 664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 111.022 121.547 151.573 1.00 38.84 ? 664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 107.992 122.693 154.937 1.00 36.49 ? 665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 106.956 123.478 155.596 1.00 36.86 ? 665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.512 124.218 156.805 1.00 39.76 ? 665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.142 125.368 157.059 1.00 41.27 ? 665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 105.793 122.577 156.005 1.00 38.10 ? 665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.467 123.305 156.135 1.00 36.53 ? 665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 104.119 123.553 157.590 1.00 38.49 ? 665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 102.679 123.530 157.818 1.00 42.07 ? 665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.110 123.555 159.015 1.00 45.10 ? 665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 102.832 123.599 160.123 1.00 42.39 ? 665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 100.784 123.539 159.103 1.00 43.33 ? 665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.393 123.573 157.571 1.00 36.65 ? 666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 108.999 124.240 158.719 1.00 34.59 ? 666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 109.866 125.414 158.282 1.00 40.74 ? 666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 109.844 126.481 158.907 1.00 43.95 ? 666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 109.817 123.239 159.533 1.00 40.89 ? 666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 108.992 122.061 160.004 1.00 47.71 ? 666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 107.908 122.286 160.581 1.00 46.44 ? 666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.425 120.908 159.795 1.00 50.11 ? 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.639 125.235 157.210 1.00 34.79 ? 667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.443 126.334 156.687 1.00 27.67 ? 667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.558 127.480 156.211 1.00 30.07 ? 667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.860 128.654 156.456 1.00 36.06 ? 667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.334 125.831 155.551 1.00 34.82 ? 667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.727 126.450 155.424 1.00 35.69 ? 667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.496 125.788 154.296 1.00 32.35 ? 667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.639 127.952 155.209 1.00 36.05 ? 667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.459 127.157 155.525 1.00 29.55 ? 668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.534 128.194 155.083 1.00 27.67 ? 668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.916 128.922 156.269 1.00 26.38 ? 668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.736 130.142 156.231 1.00 30.16 ? 668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.445 127.588 154.200 1.00 27.01 ? 668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.913 127.346 152.782 1.00 31.94 ? 668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 108.596 128.181 152.191 1.00 33.09 ? 668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 107.546 126.198 152.227 1.00 34.99 ? 668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.564 128.186 157.324 1.00 29.63 ? 669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.002 128.817 158.512 1.00 33.48 ? 669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.013 129.746 159.167 1.00 25.82 ? 669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.659 130.839 159.620 1.00 23.67 ? 669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.531 127.753 159.503 1.00 28.94 ? 669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.435 126.852 158.973 1.00 27.53 ? 669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.260 126.797 159.931 1.00 33.60 ? 669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.689 126.723 161.321 1.00 35.05 ? 669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 104.279 127.547 162.276 1.00 34.11 ? 669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.420 128.521 162.027 1.00 27.69 ? 669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 104.741 127.387 163.513 1.00 32.94 ? 669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.276 129.324 159.235 1.00 23.92 ? 670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.313 130.190 159.788 1.00 25.25 ? 670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.452 131.453 158.948 1.00 24.69 ? 670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.559 132.564 159.482 1.00 24.23 ? 670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.647 129.431 159.895 1.00 28.75 ? 670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.521 128.271 160.882 1.00 28.38 ? 670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.762 130.371 160.324 1.00 29.69 ? 670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.563 127.195 160.694 1.00 28.15 ? 670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.452 131.305 157.622 1.00 26.09 ? 671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.551 132.470 156.747 1.00 20.91 ? 671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.370 133.412 156.946 1.00 22.37 ? 671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.541 134.635 157.004 1.00 30.15 ? 671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.634 132.023 155.287 1.00 22.69 ? 671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.950 131.352 154.955 1.00 33.81 ? 671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 113.004 131.844 155.407 1.00 35.02 ? 671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.932 130.329 154.237 1.00 34.28 ? 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.161 132.858 157.051 1.00 14.50 ? 672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.971 133.689 157.199 1.00 16.65 ? 672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.948 134.385 158.551 1.00 19.98 ? 672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.493 135.527 158.657 1.00 20.47 ? 672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.713 132.842 157.008 1.00 25.91 ? 672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.512 132.226 155.623 1.00 21.16 ? 672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.376 131.217 155.643 1.00 20.27 ? 672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.260 133.306 154.586 1.00 21.64 ? 672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.420 133.708 159.599 1.00 21.86 ? 673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.515 134.344 160.908 1.00 17.60 ? 673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.556 135.456 160.902 1.00 18.92 ? 673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.338 136.520 161.492 1.00 20.89 ? 673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.839 133.300 161.974 1.00 13.97 ? 673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.910 133.856 163.376 1.00 20.24 ? 673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.774 134.337 164.010 1.00 20.26 ? 673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 109.112 133.894 164.069 1.00 19.23 ? 673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.833 134.846 165.290 1.00 21.48 ? 673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 109.181 134.401 165.348 1.00 20.05 ? 673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 108.039 134.875 165.955 1.00 23.89 ? 673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 108.103 135.379 167.232 1.00 23.91 ? 673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 109.693 135.230 160.240 1.00 18.45 ? 674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 110.698 136.280 160.122 1.00 12.94 ? 674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 110.144 137.487 159.377 1.00 15.69 ? 674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.378 138.633 159.775 1.00 20.66 ? 674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 111.944 135.741 159.421 1.00 12.35 ? 674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.405 137.250 158.292 1.00 19.67 ? 675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.765 138.353 157.584 1.00 17.65 ? 675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.752 139.059 158.477 1.00 19.95 ? 675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.641 140.289 158.455 1.00 21.60 ? 675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 108.096 137.844 156.308 1.00 17.03 ? 675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 107.234 138.863 155.632 1.00 20.94 ? 675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 105.879 138.963 155.863 1.00 22.19 ? 675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.534 139.832 154.735 1.00 15.69 ? 675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.382 139.948 155.138 1.00 22.65 ? 675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.365 140.490 154.443 1.00 27.17 ? 675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 107.000 138.289 159.265 1.00 23.41 ? 676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 106.042 138.869 160.200 1.00 17.85 ? 676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.744 139.673 161.286 1.00 26.76 ? 676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 106.256 140.731 161.700 1.00 25.74 ? 676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 105.191 137.757 160.815 1.00 23.55 ? 676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 104.299 138.216 161.924 1.00 28.61 ? 676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 103.176 138.985 161.708 1.00 29.08 ? 676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 104.360 138.008 163.261 1.00 25.73 ? 676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.586 139.234 162.863 1.00 29.78 ? 676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 103.285 138.653 163.821 1.00 29.10 ? 676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 107.890 139.190 161.757 1.00 21.28 ? 677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.606 139.812 162.862 1.00 17.45 ? 677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 109.503 140.960 162.423 1.00 20.71 ? 677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 110.263 141.480 163.246 1.00 27.99 ? 677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.438 138.763 163.602 1.00 20.81 ? 677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.649 137.941 164.603 1.00 20.08 ? 677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 108.043 138.810 165.689 1.00 20.24 ? 677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 108.926 138.933 166.843 1.00 26.81 ? 677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.570 140.042 167.180 1.00 34.13 ? 677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 109.435 141.158 166.483 1.00 27.67 ? 677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 110.366 140.032 168.245 1.00 25.83 ? 677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.439 141.365 161.159 1.00 20.97 ? 678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 110.233 142.472 160.674 1.00 15.51 ? 678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.634 142.126 160.229 1.00 13.12 ? 678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 112.438 143.041 160.014 1.00 23.68 ? 678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.959 140.840 160.086 1.00 7.70  ? 679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 113.269 140.464 159.573 1.00 12.73 ? 679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.432 141.016 158.165 1.00 12.39 ? 679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.485 141.038 157.369 1.00 23.72 ? 679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.441 138.936 159.603 1.00 12.96 ? 679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.430 138.426 161.046 1.00 10.32 ? 679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.722 138.526 158.896 1.00 9.27  ? 679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.531 138.995 161.902 1.00 13.78 ? 679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.641 141.479 157.853 1.00 12.39 ? 680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.903 142.093 156.558 1.00 5.56  ? 680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.481 141.099 155.558 1.00 11.19 ? 680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 115.028 141.036 154.411 1.00 19.20 ? 680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.849 143.284 156.725 1.00 8.90  ? 680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 115.227 144.472 157.426 1.00 0.00  ? 680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 116.218 145.611 157.547 1.00 6.04  ? 680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.676 146.726 158.419 1.00 8.83  ? 680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.620 147.871 158.483 1.00 12.65 ? 680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.479 140.323 155.970 1.00 7.31  ? 681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 117.109 139.348 155.095 1.00 5.82  ? 681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 117.360 138.064 155.869 1.00 13.90 ? 681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.549 138.081 157.088 1.00 22.74 ? 681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.431 139.873 154.510 1.00 15.14 ? 681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 119.284 140.320 155.571 1.00 24.15 ? 681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 118.175 141.030 153.556 1.00 10.68 ? 681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.345 136.947 155.150 1.00 13.87 ? 682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.727 135.649 155.692 1.00 8.57  ? 682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 118.917 135.159 154.882 1.00 12.89 ? 682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 118.840 135.066 153.651 1.00 20.77 ? 682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.567 134.644 155.651 1.00 16.24 ? 682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.325 135.251 156.305 1.00 18.29 ? 682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.952 133.372 156.375 1.00 20.74 ? 682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 114.122 134.348 156.288 1.00 20.86 ? 682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 120.019 134.855 155.569 1.00 21.02 ? 683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 121.277 134.613 154.871 1.00 15.81 ? 683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.366 133.188 154.337 1.00 21.89 ? 683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.415 132.970 153.123 1.00 36.09 ? 683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.451 134.906 155.809 1.00 19.49 ? 683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 123.804 134.850 155.142 1.00 16.47 ? 683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 123.924 134.951 153.763 1.00 14.04 ? 683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 124.964 134.703 155.890 1.00 10.09 ? 683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 125.154 134.904 153.151 1.00 14.84 ? 683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 126.202 134.658 155.284 1.00 17.39 ? 683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.291 134.759 153.914 1.00 21.24 ? 683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.522 134.713 153.302 1.00 27.63 ? 683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.372 132.204 155.226 1.00 32.48 ? 684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.618 130.830 154.824 1.00 26.42 ? 684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.662 129.906 155.555 1.00 33.42 ? 684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 120.234 130.188 156.678 1.00 34.45 ? 684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 123.065 130.406 155.107 1.00 27.97 ? 684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.987 130.528 153.918 1.00 26.02 ? 684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.698 129.891 152.720 1.00 32.79 ? 684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.151 131.280 153.995 1.00 29.91 ? 684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.542 130.001 151.630 1.00 34.28 ? 684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.999 131.397 152.914 1.00 26.35 ? 684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.691 130.757 151.733 1.00 34.79 ? 684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.534 130.870 150.653 1.00 38.30 ? 684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.330 128.802 154.901 1.00 35.80 ? 685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.585 127.711 155.513 1.00 32.35 ? 685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.586 126.580 155.730 1.00 36.52 ? 685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 120.853 125.784 154.828 1.00 43.17 ? 685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.415 127.281 154.639 1.00 30.46 ? 685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.147 126.520 156.934 1.00 33.83 ? 686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.103 125.482 157.291 1.00 35.87 ? 686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.369 124.318 157.940 1.00 40.57 ? 686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 120.592 124.511 158.880 1.00 40.64 ? 686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.170 126.027 158.241 1.00 39.59 ? 686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.327 126.721 157.552 1.00 40.79 ? 686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.417 127.076 158.548 1.00 40.96 ? 686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.728 126.607 158.117 1.00 43.95 ? 686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.301 125.490 158.544 1.00 45.05 ? 686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 126.706 124.699 159.421 1.00 42.85 ? 686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.502 125.159 158.078 1.00 45.28 ? 686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.617 123.114 157.437 1.00 46.65 ? 687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 120.988 121.906 157.945 1.00 46.49 ? 687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 122.028 121.020 158.615 1.00 43.91 ? 687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.178 120.940 158.175 1.00 44.81 ? 687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.287 121.132 156.823 1.00 43.74 ? 687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.317 121.975 156.190 1.00 46.02 ? 687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.589 119.904 157.381 1.00 44.19 ? 687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.613 120.359 159.689 1.00 49.71 ? 688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.510 119.499 160.448 1.00 51.70 ? 688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.265 118.030 160.119 1.00 53.44 ? 688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.123 117.604 159.954 1.00 55.31 ? 688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.339 119.742 161.948 1.00 49.78 ? 688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.252 118.904 162.824 1.00 49.27 ? 688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.110 119.288 164.286 1.00 50.46 ? 688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 123.983 118.419 165.173 1.00 53.02 ? 688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 123.827 118.767 166.611 1.00 54.24 ? 688 LYS B NZ    1 
ATOM   11109 N  N     . THR C 2 332 ? 144.280 107.774 111.616 1.00 29.75 ? 311 THR C N     1 
ATOM   11110 C  CA    . THR C 2 332 ? 145.409 107.171 112.313 1.00 33.42 ? 311 THR C CA    1 
ATOM   11111 C  C     . THR C 2 332 ? 146.504 108.201 112.568 1.00 31.78 ? 311 THR C C     1 
ATOM   11112 O  O     . THR C 2 332 ? 146.480 109.295 112.008 1.00 34.05 ? 311 THR C O     1 
ATOM   11113 C  CB    . THR C 2 332 ? 145.998 105.990 111.520 1.00 34.98 ? 311 THR C CB    1 
ATOM   11114 O  OG1   . THR C 2 332 ? 146.959 105.299 112.327 1.00 33.22 ? 311 THR C OG1   1 
ATOM   11115 C  CG2   . THR C 2 332 ? 146.670 106.484 110.249 1.00 32.63 ? 311 THR C CG2   1 
ATOM   11116 N  N     . VAL C 2 333 ? 147.463 107.843 113.418 1.00 31.80 ? 312 VAL C N     1 
ATOM   11117 C  CA    . VAL C 2 333 ? 148.554 108.732 113.799 1.00 32.03 ? 312 VAL C CA    1 
ATOM   11118 C  C     . VAL C 2 333 ? 149.871 108.055 113.447 1.00 31.05 ? 312 VAL C C     1 
ATOM   11119 O  O     . VAL C 2 333 ? 150.156 106.954 113.933 1.00 37.64 ? 312 VAL C O     1 
ATOM   11120 C  CB    . VAL C 2 333 ? 148.515 109.082 115.296 1.00 31.94 ? 312 VAL C CB    1 
ATOM   11121 C  CG1   . VAL C 2 333 ? 149.650 110.030 115.649 1.00 35.19 ? 312 VAL C CG1   1 
ATOM   11122 C  CG2   . VAL C 2 333 ? 147.172 109.690 115.664 1.00 31.89 ? 312 VAL C CG2   1 
ATOM   11123 N  N     . GLU C 2 334 ? 150.667 108.707 112.607 1.00 30.63 ? 313 GLU C N     1 
ATOM   11124 C  CA    . GLU C 2 334 ? 152.020 108.264 112.321 1.00 36.82 ? 313 GLU C CA    1 
ATOM   11125 C  C     . GLU C 2 334 ? 152.977 109.438 112.441 1.00 38.18 ? 313 GLU C C     1 
ATOM   11126 O  O     . GLU C 2 334 ? 152.600 110.584 112.175 1.00 39.00 ? 313 GLU C O     1 
ATOM   11127 C  CB    . GLU C 2 334 ? 152.134 107.645 110.920 1.00 35.32 ? 313 GLU C CB    1 
ATOM   11128 C  CG    . GLU C 2 334 ? 151.187 108.225 109.889 1.00 37.19 ? 313 GLU C CG    1 
ATOM   11129 C  CD    . GLU C 2 334 ? 151.586 107.860 108.471 1.00 41.54 ? 313 GLU C CD    1 
ATOM   11130 O  OE1   . GLU C 2 334 ? 152.647 107.224 108.298 1.00 35.42 ? 313 GLU C OE1   1 
ATOM   11131 O  OE2   . GLU C 2 334 ? 150.840 108.205 107.531 1.00 41.02 ? 313 GLU C OE2   1 
ATOM   11132 N  N     . PRO C 2 335 ? 154.220 109.185 112.837 1.00 33.28 ? 314 PRO C N     1 
ATOM   11133 C  CA    . PRO C 2 335 ? 155.162 110.281 113.069 1.00 35.79 ? 314 PRO C CA    1 
ATOM   11134 C  C     . PRO C 2 335 ? 155.656 110.899 111.769 1.00 35.44 ? 314 PRO C C     1 
ATOM   11135 O  O     . PRO C 2 335 ? 155.581 110.309 110.690 1.00 35.41 ? 314 PRO C O     1 
ATOM   11136 C  CB    . PRO C 2 335 ? 156.309 109.602 113.824 1.00 36.88 ? 314 PRO C CB    1 
ATOM   11137 C  CG    . PRO C 2 335 ? 156.283 108.196 113.335 1.00 35.05 ? 314 PRO C CG    1 
ATOM   11138 C  CD    . PRO C 2 335 ? 154.841 107.864 113.038 1.00 33.26 ? 314 PRO C CD    1 
ATOM   11139 N  N     . LEU C 2 336 ? 156.168 112.119 111.898 1.00 32.52 ? 315 LEU C N     1 
ATOM   11140 C  CA    . LEU C 2 336 ? 156.761 112.840 110.780 1.00 31.09 ? 315 LEU C CA    1 
ATOM   11141 C  C     . LEU C 2 336 ? 158.237 112.475 110.681 1.00 32.85 ? 315 LEU C C     1 
ATOM   11142 O  O     . LEU C 2 336 ? 158.985 112.627 111.652 1.00 34.34 ? 315 LEU C O     1 
ATOM   11143 C  CB    . LEU C 2 336 ? 156.596 114.348 110.961 1.00 25.46 ? 315 LEU C CB    1 
ATOM   11144 C  CG    . LEU C 2 336 ? 155.318 114.990 110.420 1.00 31.53 ? 315 LEU C CG    1 
ATOM   11145 C  CD1   . LEU C 2 336 ? 155.173 116.400 110.962 1.00 29.56 ? 315 LEU C CD1   1 
ATOM   11146 C  CD2   . LEU C 2 336 ? 155.322 114.997 108.900 1.00 25.47 ? 315 LEU C CD2   1 
ATOM   11147 N  N     . LYS C 2 337 ? 158.651 111.995 109.514 1.00 30.29 ? 316 LYS C N     1 
ATOM   11148 C  CA    . LYS C 2 337 ? 160.054 111.705 109.271 1.00 29.27 ? 316 LYS C CA    1 
ATOM   11149 C  C     . LYS C 2 337 ? 160.754 112.928 108.684 1.00 24.34 ? 316 LYS C C     1 
ATOM   11150 O  O     . LYS C 2 337 ? 160.123 113.902 108.270 1.00 31.89 ? 316 LYS C O     1 
ATOM   11151 C  CB    . LYS C 2 337 ? 160.201 110.496 108.347 1.00 27.34 ? 316 LYS C CB    1 
ATOM   11152 C  CG    . LYS C 2 337 ? 159.102 110.358 107.311 1.00 30.14 ? 316 LYS C CG    1 
ATOM   11153 C  CD    . LYS C 2 337 ? 158.898 108.900 106.932 1.00 33.94 ? 316 LYS C CD    1 
ATOM   11154 C  CE    . LYS C 2 337 ? 158.345 108.098 108.100 1.00 30.61 ? 316 LYS C CE    1 
ATOM   11155 N  NZ    . LYS C 2 337 ? 156.936 108.459 108.417 1.00 36.38 ? 316 LYS C NZ    1 
ATOM   11156 N  N     . ASP C 2 338 ? 162.086 112.868 108.656 1.00 30.40 ? 317 ASP C N     1 
ATOM   11157 C  CA    . ASP C 2 338 ? 162.864 114.013 108.196 1.00 32.51 ? 317 ASP C CA    1 
ATOM   11158 C  C     . ASP C 2 338 ? 162.521 114.374 106.757 1.00 28.90 ? 317 ASP C C     1 
ATOM   11159 O  O     . ASP C 2 338 ? 162.444 115.557 106.408 1.00 22.50 ? 317 ASP C O     1 
ATOM   11160 C  CB    . ASP C 2 338 ? 164.358 113.723 108.337 1.00 27.18 ? 317 ASP C CB    1 
ATOM   11161 C  CG    . ASP C 2 338 ? 164.764 113.443 109.770 1.00 32.70 ? 317 ASP C CG    1 
ATOM   11162 O  OD1   . ASP C 2 338 ? 163.868 113.231 110.614 1.00 34.97 ? 317 ASP C OD1   1 
ATOM   11163 O  OD2   . ASP C 2 338 ? 165.981 113.439 110.054 1.00 35.21 ? 317 ASP C OD2   1 
ATOM   11164 N  N     . ASP C 2 339 ? 162.314 113.369 105.905 1.00 31.41 ? 318 ASP C N     1 
ATOM   11165 C  CA    . ASP C 2 339 ? 161.993 113.624 104.506 1.00 32.31 ? 318 ASP C CA    1 
ATOM   11166 C  C     . ASP C 2 339 ? 160.637 114.289 104.319 1.00 28.21 ? 318 ASP C C     1 
ATOM   11167 O  O     . ASP C 2 339 ? 160.374 114.818 103.234 1.00 28.94 ? 318 ASP C O     1 
ATOM   11168 C  CB    . ASP C 2 339 ? 162.043 112.319 103.711 1.00 27.80 ? 318 ASP C CB    1 
ATOM   11169 C  CG    . ASP C 2 339 ? 163.431 112.005 103.197 1.00 37.08 ? 318 ASP C CG    1 
ATOM   11170 O  OD1   . ASP C 2 339 ? 164.247 112.945 103.078 1.00 36.40 ? 318 ASP C OD1   1 
ATOM   11171 O  OD2   . ASP C 2 339 ? 163.709 110.821 102.911 1.00 36.58 ? 318 ASP C OD2   1 
ATOM   11172 N  N     . ASP C 2 340 ? 159.775 114.277 105.337 1.00 28.83 ? 319 ASP C N     1 
ATOM   11173 C  CA    . ASP C 2 340 ? 158.477 114.930 105.229 1.00 20.00 ? 319 ASP C CA    1 
ATOM   11174 C  C     . ASP C 2 340 ? 158.580 116.448 105.212 1.00 14.54 ? 319 ASP C C     1 
ATOM   11175 O  O     . ASP C 2 340 ? 157.582 117.116 104.923 1.00 28.61 ? 319 ASP C O     1 
ATOM   11176 C  CB    . ASP C 2 340 ? 157.571 114.492 106.380 1.00 23.12 ? 319 ASP C CB    1 
ATOM   11177 C  CG    . ASP C 2 340 ? 157.133 113.048 106.259 1.00 31.13 ? 319 ASP C CG    1 
ATOM   11178 O  OD1   . ASP C 2 340 ? 157.369 112.442 105.193 1.00 30.52 ? 319 ASP C OD1   1 
ATOM   11179 O  OD2   . ASP C 2 340 ? 156.553 112.518 107.229 1.00 37.33 ? 319 ASP C OD2   1 
ATOM   11180 N  N     . PHE C 2 341 ? 159.751 117.006 105.513 1.00 20.85 ? 320 PHE C N     1 
ATOM   11181 C  CA    . PHE C 2 341 ? 159.955 118.446 105.537 1.00 15.27 ? 320 PHE C CA    1 
ATOM   11182 C  C     . PHE C 2 341 ? 160.640 118.962 104.280 1.00 13.98 ? 320 PHE C C     1 
ATOM   11183 O  O     . PHE C 2 341 ? 161.018 120.136 104.229 1.00 17.66 ? 320 PHE C O     1 
ATOM   11184 C  CB    . PHE C 2 341 ? 160.767 118.840 106.772 1.00 14.81 ? 320 PHE C CB    1 
ATOM   11185 C  CG    . PHE C 2 341 ? 160.055 118.589 108.067 1.00 17.09 ? 320 PHE C CG    1 
ATOM   11186 C  CD1   . PHE C 2 341 ? 160.086 117.337 108.656 1.00 10.37 ? 320 PHE C CD1   1 
ATOM   11187 C  CD2   . PHE C 2 341 ? 159.349 119.601 108.693 1.00 10.45 ? 320 PHE C CD2   1 
ATOM   11188 C  CE1   . PHE C 2 341 ? 159.429 117.100 109.845 1.00 7.03  ? 320 PHE C CE1   1 
ATOM   11189 C  CE2   . PHE C 2 341 ? 158.690 119.369 109.883 1.00 13.32 ? 320 PHE C CE2   1 
ATOM   11190 C  CZ    . PHE C 2 341 ? 158.730 118.116 110.460 1.00 3.64  ? 320 PHE C CZ    1 
ATOM   11191 N  N     . TYR C 2 342 ? 160.810 118.115 103.270 1.00 16.46 ? 321 TYR C N     1 
ATOM   11192 C  CA    . TYR C 2 342 ? 161.468 118.495 102.031 1.00 16.25 ? 321 TYR C CA    1 
ATOM   11193 C  C     . TYR C 2 342 ? 160.620 118.046 100.852 1.00 21.99 ? 321 TYR C C     1 
ATOM   11194 O  O     . TYR C 2 342 ? 159.971 116.997 100.896 1.00 17.96 ? 321 TYR C O     1 
ATOM   11195 C  CB    . TYR C 2 342 ? 162.873 117.890 101.934 1.00 19.82 ? 321 TYR C CB    1 
ATOM   11196 C  CG    . TYR C 2 342 ? 163.766 118.253 103.098 1.00 16.70 ? 321 TYR C CG    1 
ATOM   11197 C  CD1   . TYR C 2 342 ? 163.804 117.466 104.240 1.00 20.67 ? 321 TYR C CD1   1 
ATOM   11198 C  CD2   . TYR C 2 342 ? 164.565 119.387 103.057 1.00 16.00 ? 321 TYR C CD2   1 
ATOM   11199 C  CE1   . TYR C 2 342 ? 164.616 117.794 105.307 1.00 14.93 ? 321 TYR C CE1   1 
ATOM   11200 C  CE2   . TYR C 2 342 ? 165.380 119.724 104.118 1.00 19.30 ? 321 TYR C CE2   1 
ATOM   11201 C  CZ    . TYR C 2 342 ? 165.402 118.925 105.241 1.00 24.01 ? 321 TYR C CZ    1 
ATOM   11202 O  OH    . TYR C 2 342 ? 166.214 119.259 106.300 1.00 25.58 ? 321 TYR C OH    1 
ATOM   11203 N  N     . PHE C 2 343 ? 160.629 118.854 99.797  1.00 18.10 ? 322 PHE C N     1 
ATOM   11204 C  CA    . PHE C 2 343 ? 159.802 118.590 98.628  1.00 25.12 ? 322 PHE C CA    1 
ATOM   11205 C  C     . PHE C 2 343 ? 160.569 118.868 97.340  1.00 30.04 ? 322 PHE C C     1 
ATOM   11206 O  O     . PHE C 2 343 ? 161.357 119.810 97.259  1.00 30.76 ? 322 PHE C O     1 
ATOM   11207 C  CB    . PHE C 2 343 ? 158.526 119.436 98.677  1.00 19.42 ? 322 PHE C CB    1 
ATOM   11208 C  CG    . PHE C 2 343 ? 157.882 119.485 100.033 1.00 15.10 ? 322 PHE C CG    1 
ATOM   11209 C  CD1   . PHE C 2 343 ? 158.240 120.457 100.951 1.00 13.48 ? 322 PHE C CD1   1 
ATOM   11210 C  CD2   . PHE C 2 343 ? 156.921 118.556 100.391 1.00 18.02 ? 322 PHE C CD2   1 
ATOM   11211 C  CE1   . PHE C 2 343 ? 157.652 120.503 102.198 1.00 13.10 ? 322 PHE C CE1   1 
ATOM   11212 C  CE2   . PHE C 2 343 ? 156.330 118.596 101.637 1.00 14.11 ? 322 PHE C CE2   1 
ATOM   11213 C  CZ    . PHE C 2 343 ? 156.696 119.571 102.541 1.00 10.84 ? 322 PHE C CZ    1 
ATOM   11214 N  N     . THR D 2 332 ? 112.402 116.940 152.686 1.00 32.64 ? 311 THR D N     1 
ATOM   11215 C  CA    . THR D 2 332 ? 111.026 116.534 152.950 1.00 31.78 ? 311 THR D CA    1 
ATOM   11216 C  C     . THR D 2 332 ? 110.050 117.639 152.565 1.00 32.37 ? 311 THR D C     1 
ATOM   11217 O  O     . THR D 2 332 ? 109.795 118.555 153.345 1.00 35.72 ? 311 THR D O     1 
ATOM   11218 C  CB    . THR D 2 332 ? 110.818 116.171 154.430 1.00 33.94 ? 311 THR D CB    1 
ATOM   11219 O  OG1   . THR D 2 332 ? 111.942 115.419 154.903 1.00 36.69 ? 311 THR D OG1   1 
ATOM   11220 C  CG2   . THR D 2 332 ? 109.554 115.345 154.600 1.00 32.38 ? 311 THR D CG2   1 
ATOM   11221 N  N     . VAL D 2 333 ? 109.503 117.546 151.357 1.00 30.43 ? 312 VAL D N     1 
ATOM   11222 C  CA    . VAL D 2 333 ? 108.584 118.559 150.850 1.00 25.25 ? 312 VAL D CA    1 
ATOM   11223 C  C     . VAL D 2 333 ? 107.217 118.356 151.493 1.00 34.67 ? 312 VAL D C     1 
ATOM   11224 O  O     . VAL D 2 333 ? 106.637 117.268 151.415 1.00 39.77 ? 312 VAL D O     1 
ATOM   11225 C  CB    . VAL D 2 333 ? 108.486 118.500 149.320 1.00 28.81 ? 312 VAL D CB    1 
ATOM   11226 C  CG1   . VAL D 2 333 ? 107.578 119.604 148.805 1.00 33.67 ? 312 VAL D CG1   1 
ATOM   11227 C  CG2   . VAL D 2 333 ? 109.868 118.608 148.700 1.00 31.46 ? 312 VAL D CG2   1 
ATOM   11228 N  N     . GLU D 2 334 ? 106.702 119.406 152.130 1.00 38.13 ? 313 GLU D N     1 
ATOM   11229 C  CA    . GLU D 2 334 ? 105.359 119.404 152.681 1.00 32.68 ? 313 GLU D CA    1 
ATOM   11230 C  C     . GLU D 2 334 ? 104.689 120.734 152.361 1.00 42.07 ? 313 GLU D C     1 
ATOM   11231 O  O     . GLU D 2 334 ? 105.357 121.775 152.335 1.00 44.37 ? 313 GLU D O     1 
ATOM   11232 C  CB    . GLU D 2 334 ? 105.383 119.167 154.198 1.00 35.51 ? 313 GLU D CB    1 
ATOM   11233 C  CG    . GLU D 2 334 ? 104.157 119.669 154.938 1.00 40.09 ? 313 GLU D CG    1 
ATOM   11234 C  CD    . GLU D 2 334 ? 104.159 119.272 156.401 1.00 41.38 ? 313 GLU D CD    1 
ATOM   11235 O  OE1   . GLU D 2 334 ? 105.121 118.603 156.836 1.00 38.01 ? 313 GLU D OE1   1 
ATOM   11236 O  OE2   . GLU D 2 334 ? 103.199 119.625 157.117 1.00 41.10 ? 313 GLU D OE2   1 
ATOM   11237 N  N     . PRO D 2 335 ? 103.383 120.736 152.113 1.00 34.04 ? 314 PRO D N     1 
ATOM   11238 C  CA    . PRO D 2 335 ? 102.724 121.956 151.644 1.00 37.54 ? 314 PRO D CA    1 
ATOM   11239 C  C     . PRO D 2 335 ? 102.291 122.869 152.780 1.00 39.25 ? 314 PRO D C     1 
ATOM   11240 O  O     . PRO D 2 335 ? 101.988 122.430 153.892 1.00 37.42 ? 314 PRO D O     1 
ATOM   11241 C  CB    . PRO D 2 335 ? 101.505 121.427 150.874 1.00 35.55 ? 314 PRO D CB    1 
ATOM   11242 C  CG    . PRO D 2 335 ? 101.363 119.968 151.260 1.00 34.61 ? 314 PRO D CG    1 
ATOM   11243 C  CD    . PRO D 2 335 ? 102.442 119.614 152.238 1.00 38.99 ? 314 PRO D CD    1 
ATOM   11244 N  N     . LEU D 2 336 ? 102.267 124.164 152.475 1.00 37.68 ? 315 LEU D N     1 
ATOM   11245 C  CA    . LEU D 2 336 ? 101.747 125.154 153.405 1.00 31.18 ? 315 LEU D CA    1 
ATOM   11246 C  C     . LEU D 2 336 ? 100.240 124.973 153.563 1.00 34.09 ? 315 LEU D C     1 
ATOM   11247 O  O     . LEU D 2 336 ? 99.528  124.661 152.605 1.00 40.33 ? 315 LEU D O     1 
ATOM   11248 C  CB    . LEU D 2 336 ? 102.069 126.562 152.907 1.00 30.11 ? 315 LEU D CB    1 
ATOM   11249 C  CG    . LEU D 2 336 ? 103.525 127.016 153.058 1.00 28.46 ? 315 LEU D CG    1 
ATOM   11250 C  CD1   . LEU D 2 336 ? 103.783 128.268 152.236 1.00 27.43 ? 315 LEU D CD1   1 
ATOM   11251 C  CD2   . LEU D 2 336 ? 103.887 127.249 154.515 1.00 31.93 ? 315 LEU D CD2   1 
ATOM   11252 N  N     . LYS D 2 337 ? 99.750  125.176 154.787 1.00 34.15 ? 316 LYS D N     1 
ATOM   11253 C  CA    . LYS D 2 337 ? 98.393  124.775 155.147 1.00 38.53 ? 316 LYS D CA    1 
ATOM   11254 C  C     . LYS D 2 337 ? 97.535  125.980 155.545 1.00 43.06 ? 316 LYS D C     1 
ATOM   11255 O  O     . LYS D 2 337 ? 96.590  125.879 156.322 1.00 52.48 ? 316 LYS D O     1 
ATOM   11256 C  CB    . LYS D 2 337 ? 98.430  123.737 156.267 1.00 43.23 ? 316 LYS D CB    1 
ATOM   11257 C  CG    . LYS D 2 337 ? 98.678  122.318 155.783 1.00 44.18 ? 316 LYS D CG    1 
ATOM   11258 C  CD    . LYS D 2 337 ? 99.595  121.564 156.730 1.00 42.17 ? 316 LYS D CD    1 
ATOM   11259 C  CE    . LYS D 2 337 ? 98.820  120.979 157.900 1.00 45.82 ? 316 LYS D CE    1 
ATOM   11260 N  NZ    . LYS D 2 337 ? 98.272  122.035 158.794 1.00 42.77 ? 316 LYS D NZ    1 
ATOM   11261 N  N     . ASP D 2 338 ? 97.872  127.151 155.006 1.00 30.41 ? 317 ASP D N     1 
ATOM   11262 C  CA    . ASP D 2 338 ? 97.032  128.337 155.148 1.00 36.21 ? 317 ASP D CA    1 
ATOM   11263 C  C     . ASP D 2 338 ? 97.016  128.873 156.575 1.00 38.96 ? 317 ASP D C     1 
ATOM   11264 O  O     . ASP D 2 338 ? 96.424  129.924 156.839 1.00 45.43 ? 317 ASP D O     1 
ATOM   11265 C  CB    . ASP D 2 338 ? 95.603  128.030 154.695 1.00 38.67 ? 317 ASP D CB    1 
ATOM   11266 C  CG    . ASP D 2 338 ? 95.034  129.107 153.794 1.00 42.65 ? 317 ASP D CG    1 
ATOM   11267 O  OD1   . ASP D 2 338 ? 94.396  128.759 152.779 1.00 43.60 ? 317 ASP D OD1   1 
ATOM   11268 O  OD2   . ASP D 2 338 ? 95.221  130.302 154.103 1.00 40.06 ? 317 ASP D OD2   1 
ATOM   11269 N  N     . ASP D 2 339 ? 97.665  128.168 157.498 1.00 37.70 ? 318 ASP D N     1 
ATOM   11270 C  CA    . ASP D 2 339 ? 97.842  128.671 158.853 1.00 37.72 ? 318 ASP D CA    1 
ATOM   11271 C  C     . ASP D 2 339 ? 99.280  129.068 159.137 1.00 36.27 ? 318 ASP D C     1 
ATOM   11272 O  O     . ASP D 2 339 ? 99.534  129.761 160.127 1.00 44.43 ? 318 ASP D O     1 
ATOM   11273 C  CB    . ASP D 2 339 ? 97.383  127.628 159.875 1.00 33.05 ? 318 ASP D CB    1 
ATOM   11274 C  CG    . ASP D 2 339 ? 95.909  127.746 160.206 1.00 43.22 ? 318 ASP D CG    1 
ATOM   11275 O  OD1   . ASP D 2 339 ? 95.094  127.864 159.267 1.00 43.86 ? 318 ASP D OD1   1 
ATOM   11276 O  OD2   . ASP D 2 339 ? 95.565  127.724 161.406 1.00 42.14 ? 318 ASP D OD2   1 
ATOM   11277 N  N     . ASP D 2 340 ? 100.219 128.643 158.292 1.00 28.22 ? 319 ASP D N     1 
ATOM   11278 C  CA    . ASP D 2 340 ? 101.610 129.042 158.438 1.00 24.24 ? 319 ASP D CA    1 
ATOM   11279 C  C     . ASP D 2 340 ? 101.800 130.528 158.173 1.00 29.87 ? 319 ASP D C     1 
ATOM   11280 O  O     . ASP D 2 340 ? 102.862 131.078 158.481 1.00 42.86 ? 319 ASP D O     1 
ATOM   11281 C  CB    . ASP D 2 340 ? 102.482 128.214 157.494 1.00 29.20 ? 319 ASP D CB    1 
ATOM   11282 C  CG    . ASP D 2 340 ? 102.164 126.734 157.566 1.00 35.23 ? 319 ASP D CG    1 
ATOM   11283 O  OD1   . ASP D 2 340 ? 101.475 126.325 158.523 1.00 33.87 ? 319 ASP D OD1   1 
ATOM   11284 O  OD2   . ASP D 2 340 ? 102.595 125.980 156.670 1.00 46.31 ? 319 ASP D OD2   1 
ATOM   11285 N  N     . PHE D 2 341 ? 100.791 131.185 157.605 1.00 24.46 ? 320 PHE D N     1 
ATOM   11286 C  CA    . PHE D 2 341 ? 100.845 132.603 157.286 1.00 16.71 ? 320 PHE D CA    1 
ATOM   11287 C  C     . PHE D 2 341 ? 100.287 133.479 158.402 1.00 20.53 ? 320 PHE D C     1 
ATOM   11288 O  O     . PHE D 2 341 ? 100.197 134.700 158.233 1.00 23.45 ? 320 PHE D O     1 
ATOM   11289 C  CB    . PHE D 2 341 ? 100.090 132.874 155.983 1.00 22.18 ? 320 PHE D CB    1 
ATOM   11290 C  CG    . PHE D 2 341 ? 100.697 132.210 154.782 1.00 18.10 ? 320 PHE D CG    1 
ATOM   11291 C  CD1   . PHE D 2 341 ? 101.642 132.867 154.016 1.00 16.07 ? 320 PHE D CD1   1 
ATOM   11292 C  CD2   . PHE D 2 341 ? 100.320 130.928 154.418 1.00 18.98 ? 320 PHE D CD2   1 
ATOM   11293 C  CE1   . PHE D 2 341 ? 102.202 132.259 152.911 1.00 11.21 ? 320 PHE D CE1   1 
ATOM   11294 C  CE2   . PHE D 2 341 ? 100.877 130.314 153.314 1.00 18.90 ? 320 PHE D CE2   1 
ATOM   11295 C  CZ    . PHE D 2 341 ? 101.818 130.981 152.560 1.00 14.14 ? 320 PHE D CZ    1 
ATOM   11296 N  N     . TYR D 2 342 ? 99.909  132.888 159.532 1.00 16.25 ? 321 TYR D N     1 
ATOM   11297 C  CA    . TYR D 2 342 ? 99.312  133.635 160.631 1.00 23.89 ? 321 TYR D CA    1 
ATOM   11298 C  C     . TYR D 2 342 ? 100.017 133.270 161.926 1.00 27.68 ? 321 TYR D C     1 
ATOM   11299 O  O     . TYR D 2 342 ? 100.330 132.099 162.158 1.00 27.93 ? 321 TYR D O     1 
ATOM   11300 C  CB    . TYR D 2 342 ? 97.811  133.350 160.739 1.00 18.45 ? 321 TYR D CB    1 
ATOM   11301 C  CG    . TYR D 2 342 ? 97.033  133.797 159.525 1.00 20.05 ? 321 TYR D CG    1 
ATOM   11302 C  CD1   . TYR D 2 342 ? 96.608  135.111 159.392 1.00 23.35 ? 321 TYR D CD1   1 
ATOM   11303 C  CD2   . TYR D 2 342 ? 96.733  132.905 158.504 1.00 22.69 ? 321 TYR D CD2   1 
ATOM   11304 C  CE1   . TYR D 2 342 ? 95.901  135.523 158.281 1.00 23.94 ? 321 TYR D CE1   1 
ATOM   11305 C  CE2   . TYR D 2 342 ? 96.026  133.307 157.390 1.00 21.84 ? 321 TYR D CE2   1 
ATOM   11306 C  CZ    . TYR D 2 342 ? 95.613  134.617 157.284 1.00 26.78 ? 321 TYR D CZ    1 
ATOM   11307 O  OH    . TYR D 2 342 ? 94.907  135.023 156.174 1.00 35.28 ? 321 TYR D OH    1 
ATOM   11308 N  N     . PHE D 2 343 ? 100.259 134.272 162.765 1.00 26.29 ? 322 PHE D N     1 
ATOM   11309 C  CA    . PHE D 2 343 ? 101.015 134.076 163.994 1.00 30.81 ? 322 PHE D CA    1 
ATOM   11310 C  C     . PHE D 2 343 ? 100.382 134.834 165.156 1.00 35.47 ? 322 PHE D C     1 
ATOM   11311 O  O     . PHE D 2 343 ? 100.027 136.006 165.030 1.00 34.40 ? 322 PHE D O     1 
ATOM   11312 C  CB    . PHE D 2 343 ? 102.463 134.524 163.794 1.00 21.57 ? 322 PHE D CB    1 
ATOM   11313 C  CG    . PHE D 2 343 ? 103.157 133.826 162.661 1.00 24.72 ? 322 PHE D CG    1 
ATOM   11314 C  CD1   . PHE D 2 343 ? 103.683 132.558 162.830 1.00 30.83 ? 322 PHE D CD1   1 
ATOM   11315 C  CD2   . PHE D 2 343 ? 103.265 134.431 161.422 1.00 17.69 ? 322 PHE D CD2   1 
ATOM   11316 C  CE1   . PHE D 2 343 ? 104.316 131.914 161.788 1.00 28.36 ? 322 PHE D CE1   1 
ATOM   11317 C  CE2   . PHE D 2 343 ? 103.895 133.791 160.377 1.00 15.64 ? 322 PHE D CE2   1 
ATOM   11318 C  CZ    . PHE D 2 343 ? 104.421 132.530 160.560 1.00 17.88 ? 322 PHE D CZ    1 
HETATM 11319 P  PA    . TTP E 3 .   ? 146.590 143.231 134.950 1.00 12.29 ? 801 TTP A PA    1 
HETATM 11320 O  O1A   . TTP E 3 .   ? 145.162 143.707 134.903 1.00 17.62 ? 801 TTP A O1A   1 
HETATM 11321 O  O2A   . TTP E 3 .   ? 147.427 143.957 133.927 1.00 21.44 ? 801 TTP A O2A   1 
HETATM 11322 O  O3A   . TTP E 3 .   ? 147.189 143.377 136.435 1.00 27.08 ? 801 TTP A O3A   1 
HETATM 11323 P  PB    . TTP E 3 .   ? 148.268 144.514 136.794 1.00 24.47 ? 801 TTP A PB    1 
HETATM 11324 O  O1B   . TTP E 3 .   ? 148.645 145.340 135.590 1.00 36.93 ? 801 TTP A O1B   1 
HETATM 11325 O  O2B   . TTP E 3 .   ? 147.752 145.394 137.903 1.00 28.79 ? 801 TTP A O2B   1 
HETATM 11326 O  O3B   . TTP E 3 .   ? 149.513 143.630 137.295 1.00 22.70 ? 801 TTP A O3B   1 
HETATM 11327 P  PG    . TTP E 3 .   ? 150.827 143.484 136.379 1.00 25.17 ? 801 TTP A PG    1 
HETATM 11328 O  O1G   . TTP E 3 .   ? 151.380 144.845 136.041 1.00 27.94 ? 801 TTP A O1G   1 
HETATM 11329 O  O2G   . TTP E 3 .   ? 151.870 142.677 137.109 1.00 34.66 ? 801 TTP A O2G   1 
HETATM 11330 O  O3G   . TTP E 3 .   ? 150.460 142.766 135.106 1.00 32.64 ? 801 TTP A O3G   1 
HETATM 11331 O  "O5'" . TTP E 3 .   ? 146.664 141.643 134.725 1.00 20.09 ? 801 TTP A "O5'" 1 
HETATM 11332 C  "C5'" . TTP E 3 .   ? 147.651 141.091 133.861 1.00 18.36 ? 801 TTP A "C5'" 1 
HETATM 11333 C  "C4'" . TTP E 3 .   ? 147.194 139.726 133.376 1.00 19.42 ? 801 TTP A "C4'" 1 
HETATM 11334 O  "O4'" . TTP E 3 .   ? 146.761 138.942 134.486 1.00 27.75 ? 801 TTP A "O4'" 1 
HETATM 11335 C  "C3'" . TTP E 3 .   ? 146.025 139.839 132.415 1.00 24.14 ? 801 TTP A "C3'" 1 
HETATM 11336 O  "O3'" . TTP E 3 .   ? 146.428 139.475 131.091 1.00 27.74 ? 801 TTP A "O3'" 1 
HETATM 11337 C  "C2'" . TTP E 3 .   ? 144.968 138.885 132.933 1.00 26.46 ? 801 TTP A "C2'" 1 
HETATM 11338 C  "C1'" . TTP E 3 .   ? 145.584 138.208 134.150 1.00 23.44 ? 801 TTP A "C1'" 1 
HETATM 11339 N  N1    . TTP E 3 .   ? 144.675 138.202 135.299 1.00 24.28 ? 801 TTP A N1    1 
HETATM 11340 C  C2    . TTP E 3 .   ? 144.119 136.985 135.754 1.00 23.58 ? 801 TTP A C2    1 
HETATM 11341 O  O2    . TTP E 3 .   ? 144.400 135.921 135.166 1.00 22.85 ? 801 TTP A O2    1 
HETATM 11342 N  N3    . TTP E 3 .   ? 143.290 136.945 136.804 1.00 24.45 ? 801 TTP A N3    1 
HETATM 11343 C  C4    . TTP E 3 .   ? 142.968 138.063 137.456 1.00 27.61 ? 801 TTP A C4    1 
HETATM 11344 O  O4    . TTP E 3 .   ? 142.195 138.018 138.435 1.00 32.39 ? 801 TTP A O4    1 
HETATM 11345 C  C5    . TTP E 3 .   ? 143.538 139.355 137.005 1.00 23.22 ? 801 TTP A C5    1 
HETATM 11346 C  C5M   . TTP E 3 .   ? 143.205 140.643 137.709 1.00 25.93 ? 801 TTP A C5M   1 
HETATM 11347 C  C6    . TTP E 3 .   ? 144.392 139.355 135.915 1.00 25.04 ? 801 TTP A C6    1 
HETATM 11348 MG MG    . MG  F 4 .   ? 149.212 145.398 133.758 1.00 28.90 ? 802 MG  A MG    1 
HETATM 11349 P  PG    . ATP G 5 .   ? 108.657 135.836 80.564  1.00 69.04 ? 803 ATP A PG    1 
HETATM 11350 O  O1G   . ATP G 5 .   ? 109.072 136.940 79.651  1.00 55.92 ? 803 ATP A O1G   1 
HETATM 11351 O  O2G   . ATP G 5 .   ? 109.678 134.697 80.657  1.00 57.63 ? 803 ATP A O2G   1 
HETATM 11352 O  O3G   . ATP G 5 .   ? 108.304 136.309 81.978  1.00 56.73 ? 803 ATP A O3G   1 
HETATM 11353 P  PB    . ATP G 5 .   ? 106.268 134.030 80.474  1.00 63.99 ? 803 ATP A PB    1 
HETATM 11354 O  O1B   . ATP G 5 .   ? 104.882 134.539 80.429  1.00 56.62 ? 803 ATP A O1B   1 
HETATM 11355 O  O2B   . ATP G 5 .   ? 106.544 132.780 79.637  1.00 55.81 ? 803 ATP A O2B   1 
HETATM 11356 O  O3B   . ATP G 5 .   ? 107.322 135.136 80.030  1.00 55.92 ? 803 ATP A O3B   1 
HETATM 11357 P  PA    . ATP G 5 .   ? 106.870 132.427 82.887  1.00 63.15 ? 803 ATP A PA    1 
HETATM 11358 O  O1A   . ATP G 5 .   ? 107.962 131.543 82.434  1.00 58.46 ? 803 ATP A O1A   1 
HETATM 11359 O  O2A   . ATP G 5 .   ? 105.490 131.772 82.947  1.00 53.96 ? 803 ATP A O2A   1 
HETATM 11360 O  O3A   . ATP G 5 .   ? 106.736 133.714 81.962  1.00 54.74 ? 803 ATP A O3A   1 
HETATM 11361 O  "O5'" . ATP G 5 .   ? 107.185 133.047 84.304  1.00 52.95 ? 803 ATP A "O5'" 1 
HETATM 11362 C  "C5'" . ATP G 5 .   ? 106.330 134.052 84.888  1.00 52.93 ? 803 ATP A "C5'" 1 
HETATM 11363 C  "C4'" . ATP G 5 .   ? 107.172 135.063 85.621  1.00 53.43 ? 803 ATP A "C4'" 1 
HETATM 11364 O  "O4'" . ATP G 5 .   ? 107.794 134.369 86.721  1.00 52.51 ? 803 ATP A "O4'" 1 
HETATM 11365 C  "C3'" . ATP G 5 .   ? 108.368 135.491 84.787  1.00 53.48 ? 803 ATP A "C3'" 1 
HETATM 11366 O  "O3'" . ATP G 5 .   ? 107.966 136.677 84.114  1.00 57.07 ? 803 ATP A "O3'" 1 
HETATM 11367 C  "C2'" . ATP G 5 .   ? 109.344 135.931 85.872  1.00 52.44 ? 803 ATP A "C2'" 1 
HETATM 11368 O  "O2'" . ATP G 5 .   ? 108.790 137.106 86.448  1.00 53.71 ? 803 ATP A "O2'" 1 
HETATM 11369 C  "C1'" . ATP G 5 .   ? 109.117 134.840 86.922  1.00 52.98 ? 803 ATP A "C1'" 1 
HETATM 11370 N  N9    . ATP G 5 .   ? 110.002 133.702 86.706  1.00 54.37 ? 803 ATP A N9    1 
HETATM 11371 C  C8    . ATP G 5 .   ? 109.695 132.514 86.096  1.00 53.38 ? 803 ATP A C8    1 
HETATM 11372 N  N7    . ATP G 5 .   ? 110.692 131.665 86.042  1.00 53.37 ? 803 ATP A N7    1 
HETATM 11373 C  C5    . ATP G 5 .   ? 111.732 132.342 86.662  1.00 54.75 ? 803 ATP A C5    1 
HETATM 11374 C  C6    . ATP G 5 .   ? 113.069 131.992 86.930  1.00 49.48 ? 803 ATP A C6    1 
HETATM 11375 N  N6    . ATP G 5 .   ? 113.613 130.818 86.593  1.00 49.97 ? 803 ATP A N6    1 
HETATM 11376 N  N1    . ATP G 5 .   ? 113.841 132.899 87.567  1.00 51.18 ? 803 ATP A N1    1 
HETATM 11377 C  C2    . ATP G 5 .   ? 113.306 134.075 87.904  1.00 50.78 ? 803 ATP A C2    1 
HETATM 11378 N  N3    . ATP G 5 .   ? 112.062 134.515 87.706  1.00 51.81 ? 803 ATP A N3    1 
HETATM 11379 C  C4    . ATP G 5 .   ? 111.321 133.599 87.076  1.00 53.82 ? 803 ATP A C4    1 
HETATM 11380 P  PA    . TTP H 3 .   ? 120.333 146.578 124.573 1.00 10.25 ? 801 TTP B PA    1 
HETATM 11381 O  O1A   . TTP H 3 .   ? 121.834 146.642 124.684 1.00 21.91 ? 801 TTP B O1A   1 
HETATM 11382 O  O2A   . TTP H 3 .   ? 119.685 147.676 125.379 1.00 20.55 ? 801 TTP B O2A   1 
HETATM 11383 O  O3A   . TTP H 3 .   ? 119.879 146.632 123.032 1.00 30.28 ? 801 TTP B O3A   1 
HETATM 11384 P  PB    . TTP H 3 .   ? 119.188 147.949 122.423 1.00 25.31 ? 801 TTP B PB    1 
HETATM 11385 O  O1B   . TTP H 3 .   ? 119.227 149.109 123.386 1.00 34.69 ? 801 TTP B O1B   1 
HETATM 11386 O  O2B   . TTP H 3 .   ? 119.832 148.324 121.114 1.00 29.70 ? 801 TTP B O2B   1 
HETATM 11387 O  O3B   . TTP H 3 .   ? 117.688 147.422 122.188 1.00 18.55 ? 801 TTP B O3B   1 
HETATM 11388 P  PG    . TTP H 3 .   ? 116.440 148.109 122.933 1.00 20.18 ? 801 TTP B PG    1 
HETATM 11389 O  O1G   . TTP H 3 .   ? 116.065 149.398 122.247 1.00 28.67 ? 801 TTP B O1G   1 
HETATM 11390 O  O2G   . TTP H 3 .   ? 115.268 147.162 122.895 1.00 23.97 ? 801 TTP B O2G   1 
HETATM 11391 O  O3G   . TTP H 3 .   ? 116.800 148.393 124.369 1.00 31.12 ? 801 TTP B O3G   1 
HETATM 11392 O  "O5'" . TTP H 3 .   ? 119.792 145.138 125.035 1.00 18.75 ? 801 TTP B "O5'" 1 
HETATM 11393 C  "C5'" . TTP H 3 .   ? 118.639 145.048 125.867 1.00 15.35 ? 801 TTP B "C5'" 1 
HETATM 11394 C  "C4'" . TTP H 3 .   ? 118.621 143.705 126.581 1.00 17.50 ? 801 TTP B "C4'" 1 
HETATM 11395 O  "O4'" . TTP H 3 .   ? 118.740 142.643 125.636 1.00 27.35 ? 801 TTP B "O4'" 1 
HETATM 11396 C  "C3'" . TTP H 3 .   ? 119.778 143.571 127.556 1.00 18.41 ? 801 TTP B "C3'" 1 
HETATM 11397 O  "O3'" . TTP H 3 .   ? 119.316 143.674 128.906 1.00 29.17 ? 801 TTP B "O3'" 1 
HETATM 11398 C  "C2'" . TTP H 3 .   ? 120.380 142.204 127.296 1.00 24.62 ? 801 TTP B "C2'" 1 
HETATM 11399 C  "C1'" . TTP H 3 .   ? 119.570 141.603 126.155 1.00 24.54 ? 801 TTP B "C1'" 1 
HETATM 11400 N  N1    . TTP H 3 .   ? 120.441 141.096 125.092 1.00 22.26 ? 801 TTP B N1    1 
HETATM 11401 C  C2    . TTP H 3 .   ? 120.625 139.704 124.931 1.00 23.20 ? 801 TTP B C2    1 
HETATM 11402 O  O2    . TTP H 3 .   ? 120.043 138.912 125.700 1.00 25.71 ? 801 TTP B O2    1 
HETATM 11403 N  N3    . TTP H 3 .   ? 121.413 139.213 123.968 1.00 25.31 ? 801 TTP B N3    1 
HETATM 11404 C  C4    . TTP H 3 .   ? 122.049 140.032 123.127 1.00 28.09 ? 801 TTP B C4    1 
HETATM 11405 O  O4    . TTP H 3 .   ? 122.781 139.567 122.230 1.00 34.85 ? 801 TTP B O4    1 
HETATM 11406 C  C5    . TTP H 3 .   ? 121.873 141.496 123.271 1.00 24.84 ? 801 TTP B C5    1 
HETATM 11407 C  C5M   . TTP H 3 .   ? 122.571 142.459 122.348 1.00 23.82 ? 801 TTP B C5M   1 
HETATM 11408 C  C6    . TTP H 3 .   ? 121.051 141.965 124.280 1.00 25.14 ? 801 TTP B C6    1 
HETATM 11409 MG MG    . MG  I 4 .   ? 118.562 149.213 125.687 1.00 30.79 ? 802 MG  B MG    1 
HETATM 11410 P  PG    . ATP J 5 .   ? 156.079 137.699 180.111 1.00 72.82 ? 803 ATP B PG    1 
HETATM 11411 O  O1G   . ATP J 5 .   ? 155.624 138.798 181.011 1.00 63.31 ? 803 ATP B O1G   1 
HETATM 11412 O  O2G   . ATP J 5 .   ? 154.948 136.766 179.664 1.00 63.47 ? 803 ATP B O2G   1 
HETATM 11413 O  O3G   . ATP J 5 .   ? 156.843 138.192 178.878 1.00 63.49 ? 803 ATP B O3G   1 
HETATM 11414 P  PB    . ATP J 5 .   ? 157.525 135.207 180.933 1.00 73.44 ? 803 ATP B PB    1 
HETATM 11415 O  O1B   . ATP J 5 .   ? 158.990 135.031 181.010 1.00 63.09 ? 803 ATP B O1B   1 
HETATM 11416 O  O2B   . ATP J 5 .   ? 156.716 134.570 182.063 1.00 62.66 ? 803 ATP B O2B   1 
HETATM 11417 O  O3B   . ATP J 5 .   ? 157.112 136.743 180.869 1.00 63.04 ? 803 ATP B O3B   1 
HETATM 11418 P  PA    . ATP J 5 .   ? 156.496 133.244 178.972 1.00 71.06 ? 803 ATP B PA    1 
HETATM 11419 O  O1A   . ATP J 5 .   ? 155.285 132.731 179.643 1.00 63.87 ? 803 ATP B O1A   1 
HETATM 11420 O  O2A   . ATP J 5 .   ? 157.716 132.326 179.050 1.00 62.40 ? 803 ATP B O2A   1 
HETATM 11421 O  O3A   . ATP J 5 .   ? 156.936 134.654 179.562 1.00 63.62 ? 803 ATP B O3A   1 
HETATM 11422 O  "O5'" . ATP J 5 .   ? 156.220 133.573 177.453 1.00 58.80 ? 803 ATP B "O5'" 1 
HETATM 11423 C  "C5'" . ATP J 5 .   ? 157.264 134.079 176.596 1.00 60.43 ? 803 ATP B "C5'" 1 
HETATM 11424 C  "C4'" . ATP J 5 .   ? 156.663 134.987 175.557 1.00 61.61 ? 803 ATP B "C4'" 1 
HETATM 11425 O  "O4'" . ATP J 5 .   ? 155.780 134.178 174.757 1.00 63.32 ? 803 ATP B "O4'" 1 
HETATM 11426 C  "C3'" . ATP J 5 .   ? 155.698 135.979 176.182 1.00 61.44 ? 803 ATP B "C3'" 1 
HETATM 11427 O  "O3'" . ATP J 5 .   ? 156.462 137.148 176.448 1.00 63.49 ? 803 ATP B "O3'" 1 
HETATM 11428 C  "C2'" . ATP J 5 .   ? 154.807 136.320 174.991 1.00 59.36 ? 803 ATP B "C2'" 1 
HETATM 11429 O  "O2'" . ATP J 5 .   ? 155.607 137.093 174.107 1.00 59.29 ? 803 ATP B "O2'" 1 
HETATM 11430 C  "C1'" . ATP J 5 .   ? 154.682 134.954 174.306 1.00 61.36 ? 803 ATP B "C1'" 1 
HETATM 11431 N  N9    . ATP J 5 .   ? 153.475 134.256 174.727 1.00 60.50 ? 803 ATP B N9    1 
HETATM 11432 C  C8    . ATP J 5 .   ? 153.385 133.194 175.589 1.00 59.47 ? 803 ATP B C8    1 
HETATM 11433 N  N7    . ATP J 5 .   ? 152.163 132.763 175.784 1.00 60.62 ? 803 ATP B N7    1 
HETATM 11434 C  C5    . ATP J 5 .   ? 151.391 133.600 174.991 1.00 61.83 ? 803 ATP B C5    1 
HETATM 11435 C  C6    . ATP J 5 .   ? 150.006 133.671 174.751 1.00 57.82 ? 803 ATP B C6    1 
HETATM 11436 N  N6    . ATP J 5 .   ? 149.110 132.850 175.309 1.00 58.95 ? 803 ATP B N6    1 
HETATM 11437 N  N1    . ATP J 5 .   ? 149.562 134.625 173.904 1.00 58.92 ? 803 ATP B N1    1 
HETATM 11438 C  C2    . ATP J 5 .   ? 150.450 135.450 173.343 1.00 57.54 ? 803 ATP B C2    1 
HETATM 11439 N  N3    . ATP J 5 .   ? 151.775 135.479 173.493 1.00 59.67 ? 803 ATP B N3    1 
HETATM 11440 C  C4    . ATP J 5 .   ? 152.186 134.524 174.334 1.00 61.73 ? 803 ATP B C4    1 
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